CNRS Nantes University US2B US2B
home |  start a new run |  job status |  references&downloads |  examples |  help  

Should you encounter any unexpected behaviour,
please let us know.


***  PROTEIN BINDING 19-JUL-24 9G6Z  ***

elNémo ID: 2412090304591789805

Job options:

ID        	=	 2412090304591789805
JOBID     	=	 PROTEIN BINDING 19-JUL-24 9G6Z
USERID    	=	 unknown
PRIVAT    	=	 0

NMODES    	=	 5
DQMIN     	=	 -100
DQMAX     	=	 100
DQSTEP    	=	 20
DOGRAPHS  	=	 on

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


HEADER    PROTEIN BINDING                         19-JUL-24   9G6Z              
TITLE     C. ELEGANS TOFU-6 ETUDOR TOFU-1 PEPTIDE COMPLEX                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: EMBRYONIC DEVELOPMENTAL PROTEIN TOFU-6;                    
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: 21U-RNA BIOGENESIS FOULED UP PROTEIN 6,MATERNAL EFFECT      
COMPND   5 LETHAL PROTEIN 47;                                                   
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: PROTEIN TOFU-1;                                            
COMPND   9 CHAIN: B;                                                            
COMPND  10 SYNONYM: 21U-RNA BIOGENESIS FOULED UP PROTEIN 1;                     
COMPND  11 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: CAENORHABDITIS ELEGANS;                         
SOURCE   3 ORGANISM_TAXID: 6239;                                                
SOURCE   4 GENE: TOFU-6, MEL-47, EEED8.1;                                       
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 MOL_ID: 2;                                                           
SOURCE   8 ORGANISM_SCIENTIFIC: CAENORHABDITIS ELEGANS;                         
SOURCE   9 ORGANISM_TAXID: 6239;                                                
SOURCE  10 GENE: TOFU-1, C27H6.3;                                               
SOURCE  11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  12 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    PIRNA BIOGENESIS, TUDOR DOMAIN, RNA BINDING PROTEIN, PROTEIN BINDING  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.KETTING,S.FALK                                                      
REVDAT   1   04-DEC-24 9G6Z    0                                                
SPRSDE     04-DEC-24 9G6Z      8BY5                                             
JRNL        AUTH   N.PODVALNAYA,A.W.BRONKHORST,R.LICHTENBERGER,S.HELLMANN,      
JRNL        AUTH 2 E.NISCHWITZ,T.FALK,E.KARAULANOV,F.BUTTER,S.FALK,R.F.KETTING  
JRNL        TITL   PIRNA PROCESSING BY A TRIMERIC SCHLAFEN-DOMAIN NUCLEASE.     
JRNL        REF    NATURE                        V. 622   402 2023              
JRNL        REFN                   ESSN 1476-4687                               
JRNL        PMID   37758951                                                     
JRNL        DOI    10.1093/NAR/GKAB1038                                         
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.22 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.21_5207                                     
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : GEOSTD + MONOMER LIBRARY + CDL V1.2           
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.22                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 36.52                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 12053                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.181                           
REMARK   3   R VALUE            (WORKING SET) : 0.176                           
REMARK   3   FREE R VALUE                     : 0.230                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.060                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 1212                            
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 36.5200 -  4.6200    1.00     1242   139  0.1542 0.2046        
REMARK   3     2  4.6200 -  3.6700    0.97     1186   135  0.1368 0.1751        
REMARK   3     3  3.6700 -  3.2100    0.98     1193   129  0.1686 0.2137        
REMARK   3     4  3.2100 -  2.9100    0.99     1207   138  0.1889 0.2526        
REMARK   3     5  2.9100 -  2.7100    1.00     1195   131  0.2248 0.2942        
REMARK   3     6  2.7100 -  2.5500    1.00     1208   133  0.2083 0.2866        
REMARK   3     7  2.5500 -  2.4200    0.99     1201   145  0.2005 0.2970        
REMARK   3     8  2.4200 -  2.3100    1.00     1204   129  0.2204 0.2786        
REMARK   3     9  2.3100 -  2.2200    0.99     1205   133  0.2565 0.3185        
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   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.317            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.050           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 35.81                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 44.09                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.005           1722                                  
REMARK   3   ANGLE     :  0.671           2323                                  
REMARK   3   CHIRALITY :  0.042            261                                  
REMARK   3   PLANARITY :  0.005            294                                  
REMARK   3   DIHEDRAL  : 18.871            653                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 11                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 115 THROUGH 124 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   7.8904   3.4920  11.3644              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4372 T22:   0.3402                                     
REMARK   3      T33:   0.4317 T12:  -0.0725                                     
REMARK   3      T13:  -0.1390 T23:  -0.0720                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6840 L22:   6.8447                                     
REMARK   3      L33:   5.6770 L12:  -0.7155                                     
REMARK   3      L13:   0.5237 L23:  -4.5721                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0962 S12:  -0.1088 S13:   0.3723                       
REMARK   3      S21:  -1.0099 S22:   0.2838 S23:   0.4719                       
REMARK   3      S31:   0.4027 S32:  -0.3173 S33:  -0.2191                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 125 THROUGH 136 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  15.9666 -12.0328  28.0619              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2620 T22:   0.2873                                     
REMARK   3      T33:   0.3547 T12:  -0.0147                                     
REMARK   3      T13:  -0.0235 T23:  -0.0402                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2586 L22:   1.8322                                     
REMARK   3      L33:   2.5230 L12:   0.1359                                     
REMARK   3      L13:   0.9518 L23:   0.3367                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0716 S12:  -0.0972 S13:  -0.0917                       
REMARK   3      S21:   0.0554 S22:   0.1340 S23:  -0.0953                       
REMARK   3      S31:   0.1722 S32:   0.0467 S33:  -0.0104                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 137 THROUGH 159 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  12.2377  -1.1379  28.5891              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2468 T22:   0.2945                                     
REMARK   3      T33:   0.3791 T12:  -0.0264                                     
REMARK   3      T13:  -0.0249 T23:  -0.0025                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8314 L22:   0.8571                                     
REMARK   3      L33:   2.2345 L12:  -0.3904                                     
REMARK   3      L13:   0.2975 L23:  -0.3860                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0638 S12:   0.2227 S13:  -0.2534                       
REMARK   3      S21:  -0.0577 S22:  -0.0212 S23:   0.0440                       
REMARK   3      S31:   0.0290 S32:  -0.2554 S33:   0.1188                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 160 THROUGH 175 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  24.0075  -6.1165  11.0834              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4808 T22:   0.4708                                     
REMARK   3      T33:   0.5295 T12:  -0.0039                                     
REMARK   3      T13:   0.1167 T23:  -0.1657                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.6804 L22:   2.3010                                     
REMARK   3      L33:   3.6571 L12:  -0.2769                                     
REMARK   3      L13:  -0.1798 L23:  -0.5277                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2552 S12:   0.7822 S13:  -0.6582                       
REMARK   3      S21:  -0.2005 S22:   0.0254 S23:   0.0171                       
REMARK   3      S31:   0.1822 S32:  -0.1535 S33:  -0.1074                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 176 THROUGH 190 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  12.6797  11.0228   7.1441              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6035 T22:   0.4728                                     
REMARK   3      T33:   0.3720 T12:   0.0330                                     
REMARK   3      T13:   0.0246 T23:   0.0191                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7517 L22:   1.9257                                     
REMARK   3      L33:   2.2548 L12:  -0.5017                                     
REMARK   3      L13:  -0.9042 L23:   0.0972                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0374 S12:   0.6008 S13:  -0.2489                       
REMARK   3      S21:  -0.9274 S22:  -0.2280 S23:   0.1401                       
REMARK   3      S31:  -0.2521 S32:  -0.1655 S33:   0.1732                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 191 THROUGH 208 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  20.0837   8.0124  12.6869              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3993 T22:   0.3973                                     
REMARK   3      T33:   0.4173 T12:  -0.0538                                     
REMARK   3      T13:   0.0681 T23:   0.0116                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1614 L22:   1.9692                                     
REMARK   3      L33:   2.0712 L12:   0.1039                                     
REMARK   3      L13:   0.0463 L23:  -0.0463                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1637 S12:   0.4956 S13:   0.3028                       
REMARK   3      S21:  -0.5440 S22:   0.2291 S23:  -0.5095                       
REMARK   3      S31:  -0.1979 S32:   0.2544 S33:  -0.0916                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 209 THROUGH 222 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  18.7370   8.0707  20.8956              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3023 T22:   0.2970                                     
REMARK   3      T33:   0.4572 T12:  -0.0539                                     
REMARK   3      T13:   0.0352 T23:  -0.0186                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7063 L22:   5.9367                                     
REMARK   3      L33:   1.6322 L12:  -1.4731                                     
REMARK   3      L13:  -1.1024 L23:   0.6539                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1308 S12:   0.1831 S13:   0.3208                       
REMARK   3      S21:  -0.1741 S22:  -0.1758 S23:  -0.8284                       
REMARK   3      S31:  -0.1113 S32:   0.3315 S33:   0.0355                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 223 THROUGH 253 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  13.2298   2.0768  19.0259              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2772 T22:   0.3267                                     
REMARK   3      T33:   0.2601 T12:   0.0120                                     
REMARK   3      T13:  -0.0082 T23:  -0.0216                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7461 L22:   2.5281                                     
REMARK   3      L33:   1.6843 L12:   0.1841                                     
REMARK   3      L13:   0.2357 L23:   0.1232                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0367 S12:   0.3231 S13:  -0.0036                       
REMARK   3      S21:  -0.4829 S22:   0.1605 S23:  -0.0829                       
REMARK   3      S31:   0.1399 S32:  -0.2590 S33:  -0.0878                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 254 THROUGH 295 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  14.7384  -3.0439  35.9779              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2681 T22:   0.2745                                     
REMARK   3      T33:   0.3665 T12:   0.0038                                     
REMARK   3      T13:  -0.0077 T23:  -0.0466                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7502 L22:   1.7991                                     
REMARK   3      L33:   2.2087 L12:  -0.2885                                     
REMARK   3      L13:  -0.0719 L23:  -0.1013                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0905 S12:  -0.2006 S13:   0.2263                       
REMARK   3      S21:   0.2066 S22:   0.0820 S23:   0.0744                       
REMARK   3      S31:  -0.1384 S32:  -0.0750 S33:   0.0096                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 296 THROUGH 314 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  11.4223  -6.8894  45.9118              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4414 T22:   0.4048                                     
REMARK   3      T33:   0.3568 T12:   0.0581                                     
REMARK   3      T13:  -0.0400 T23:  -0.0495                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.2955 L22:   3.4678                                     
REMARK   3      L33:   2.1153 L12:  -1.4710                                     
REMARK   3      L13:  -0.2531 L23:  -0.0159                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4093 S12:  -0.5989 S13:  -0.3767                       
REMARK   3      S21:   0.7217 S22:   0.2804 S23:  -0.0310                       
REMARK   3      S31:  -0.1755 S32:  -0.0319 S33:   0.0990                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 85 THROUGH 96 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  19.0462   0.7899  47.6369              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6455 T22:   0.9287                                     
REMARK   3      T33:   0.5353 T12:   0.0083                                     
REMARK   3      T13:  -0.0309 T23:  -0.2323                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.5854 L22:   4.3231                                     
REMARK   3      L33:   6.0171 L12:  -0.8620                                     
REMARK   3      L13:   1.2615 L23:  -1.4537                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2089 S12:  -0.0757 S13:   0.5064                       
REMARK   3      S21:   0.7124 S22:  -0.1526 S23:  -0.1992                       
REMARK   3      S31:  -1.4391 S32:   1.6405 S33:   0.1849                       
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 9G6Z COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-JUL-24.                  
REMARK 100 THE DEPOSITION ID IS D_1292140463.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 26-SEP-21                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : MASSIF-3                           
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9677                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER R 4M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AUTOPROC                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 12063                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.220                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 60.930                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY                : 5.100                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 10.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.22                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.26                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 39.34                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.03                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M NA BROMIDE, 0.1 M BIS TRIS         
REMARK 280  PROPANE PH 7.5, 20% (W/V) PEG 3350, VAPOR DIFFUSION, SITTING        
REMARK 280  DROP, TEMPERATURE 295.15K                                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       29.57500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       34.60100            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       29.57500            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       34.60100            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
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 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1560 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 10810 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A   114                                                      
REMARK 465     GLY B    77                                                      
REMARK 465     PRO B    78                                                      
REMARK 465     ASP B    79                                                      
REMARK 465     SER B    80                                                      
REMARK 465     MET B    81                                                      
REMARK 465     GLU B    82                                                      
REMARK 465     VAL B    83                                                      
REMARK 465     GLU B    84                                                      
REMARK 465     ALA B    97                                                      
REMARK 465     GLY B    98                                                      
REMARK 465     ASP B    99                                                      
REMARK 465     GLN B   100                                                      
REMARK 465     MET B   101                                                      
REMARK 465     ASN B   102                                                      
REMARK 465     SER B   103                                                      
REMARK 465     ARG B   104                                                      
REMARK 465     ILE B   105                                                      
REMARK 465     GLU B   106                                                      
REMARK 465     GLY B   107                                                      
REMARK 465     LEU B   108                                                      
REMARK 465     PHE B   109                                                      
REMARK 465     GLU B   110                                                      
REMARK 465     ASP B   111                                                      
REMARK 465     LEU B   112                                                      
REMARK 465     ASP B   113                                                      
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    VAL A 137     -169.99   -112.91                                   
REMARK 500    GLN A 178       59.96   -100.94                                   
REMARK 500    SER A 184      -95.75   -107.56                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  9G6Z A  119   314  UNP    Q09293   TOFU6_CAEEL    119    314             
DBREF  9G6Z B   82   113  UNP    O17608   TOFU1_CAEEL     82    113             
SEQADV 9G6Z GLY A  114  UNP  Q09293              EXPRESSION TAG                 
SEQADV 9G6Z PRO A  115  UNP  Q09293              EXPRESSION TAG                 
SEQADV 9G6Z ASP A  116  UNP  Q09293              EXPRESSION TAG                 
SEQADV 9G6Z SER A  117  UNP  Q09293              EXPRESSION TAG                 
SEQADV 9G6Z MET A  118  UNP  Q09293              EXPRESSION TAG                 
SEQADV 9G6Z GLY B   77  UNP  O17608              EXPRESSION TAG                 
SEQADV 9G6Z PRO B   78  UNP  O17608              EXPRESSION TAG                 
SEQADV 9G6Z ASP B   79  UNP  O17608              EXPRESSION TAG                 
SEQADV 9G6Z SER B   80  UNP  O17608              EXPRESSION TAG                 
SEQADV 9G6Z MET B   81  UNP  O17608              EXPRESSION TAG                 
SEQRES   1 A  201  GLY PRO ASP SER MET VAL LEU LEU SER SER SER TRP LEU          
SEQRES   2 A  201  PRO LEU ASN LYS ASP ILE GLU VAL GLU VAL VAL ASP TYR          
SEQRES   3 A  201  LEU PRO SER SER SER VAL ALA PRO ASP LEU PHE ALA LEU          
SEQRES   4 A  201  THR LEU LEU ARG ILE ASN ASP SER SER MET LYS GLU LYS          
SEQRES   5 A  201  TYR ASP SER MET HIS GLU LYS MET ASN ALA TYR ALA GLN          
SEQRES   6 A  201  ILE VAL PRO PHE ASP SER GLU LEU GLU ILE GLY TYR ASP          
SEQRES   7 A  201  GLY VAL PHE ARG ASP ALA PRO ARG SER VAL ARG ARG VAL          
SEQRES   8 A  201  ARG ARG ILE SER ALA THR LYS LEU TYR LEU VAL ASP PHE          
SEQRES   9 A  201  GLY LYS ILE ILE ASN TYR GLU LYS ALA LYS CYS PHE GLN          
SEQRES  10 A  201  LEU PRO LYS VAL PHE GLN SER MET PRO THR ARG VAL SER          
SEQRES  11 A  201  LEU CYS GLY LEU ASP GLY LEU THR TRP SER PRO VAL ALA          
SEQRES  12 A  201  ILE PRO SER PHE ASP ASN ILE ARG GLU VAL VAL LYS LYS          
SEQRES  13 A  201  TRP GLY GLN MET GLU ASN SER THR LEU HIS ALA MET ALA          
SEQRES  14 A  201  CYS GLY PHE GLN GLY SER ILE ASN MET ILE ASN LEU PHE          
SEQRES  15 A  201  CYS GLY LYS SER ILE LEU ALA ASP ARG LEU GLN ARG LYS          
SEQRES  16 A  201  GLY VAL CYS GLU TYR LEU                                      
SEQRES   1 B   37  GLY PRO ASP SER MET GLU VAL GLU GLU SER LEU LEU ASP          
SEQRES   2 B   37  ALA LEU LEU GLY LYS ALA LEU ALA GLY ASP GLN MET ASN          
SEQRES   3 B   37  SER ARG ILE GLU GLY LEU PHE GLU ASP LEU ASP                  
HET    GOL  A 401      14                                                       
HET    GOL  A 402      14                                                       
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  GOL    2(C3 H8 O3)                                                  
FORMUL   5  HOH   *77(H2 O)                                                     
HELIX    1 AA1 ASP A  159  TYR A  176  1                                  18    
HELIX    2 AA2 GLU A  224  ALA A  226  5                                   3    
HELIX    3 AA3 PRO A  232  GLN A  236  5                                   5    
HELIX    4 AA4 ALA A  256  PRO A  258  5                                   3    
HELIX    5 AA5 SER A  259  ASN A  275  1                                  17    
HELIX    6 AA6 LEU A  301  LYS A  308  1                                   8    
HELIX    7 AA7 SER B   86  LEU B   96  1                                  11    
SHEET    1 AA1 7 SER A 299  ILE A 300  0                                        
SHEET    2 AA1 7 ILE A 289  CYS A 296 -1  N  CYS A 296   O  SER A 299           
SHEET    3 AA1 7 LEU A 278  GLN A 286 -1  N  CYS A 283   O  MET A 291           
SHEET    4 AA1 7 ASP A 131  VAL A 136 -1  N  ILE A 132   O  ALA A 280           
SHEET    5 AA1 7 ALA A 151  ARG A 156 -1  O  LEU A 155   N  GLU A 135           
SHEET    6 AA1 7 SER A 243  LEU A 247 -1  O  SER A 243   N  LEU A 154           
SHEET    7 AA1 7 ILE A 289  CYS A 296  1  O  ASN A 290   N  LEU A 244           
SHEET    1 AA2 5 ILE A 220  ASN A 222  0                                        
SHEET    2 AA2 5 LYS A 211  LEU A 214 -1  N  LEU A 212   O  ILE A 221           
SHEET    3 AA2 5 SER A 200  SER A 208 -1  N  ARG A 205   O  TYR A 213           
SHEET    4 AA2 5 ASP A 191  ALA A 197 -1  N  PHE A 194   O  ARG A 202           
SHEET    5 AA2 5 CYS A 228  PHE A 229 -1  O  PHE A 229   N  VAL A 193           
SHEET    1 AA3 2 LEU A 250  TRP A 252  0                                        
SHEET    2 AA3 2 CYS A 311  TYR A 313 -1  O  GLU A 312   N  THR A 251           
CRYST1   59.150   69.202   60.946  90.00  91.47  90.00 C 1 2 1       4          
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      0.016906  0.000000  0.000435        0.00000                         
SCALE2      0.000000  0.014450  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016413        0.00000                         
ATOM      1  N   PRO A 115       3.452  12.092   0.618  1.00 93.90           N  
ANISOU    1  N   PRO A 115    13583   9785  12308  -1174  -3300    764       N  
ATOM      2  CA  PRO A 115       3.992  12.451   1.938  1.00 90.01           C  
ANISOU    2  CA  PRO A 115    12691   9444  12067   -977  -2934    552       C  
ATOM      3  C   PRO A 115       5.005  11.432   2.445  1.00 84.70           C  
ANISOU    3  C   PRO A 115    12154   8830  11198   -982  -2670    332       C  
ATOM      4  O   PRO A 115       5.091  10.333   1.895  1.00 81.62           O  
ANISOU    4  O   PRO A 115    12136   8376  10501  -1117  -2774    349       O  
ATOM      5  CB  PRO A 115       2.750  12.474   2.838  1.00 92.72           C  
ANISOU    5  CB  PRO A 115    12528   9972  12730   -930  -3088    678       C  
ATOM      6  CG  PRO A 115       1.605  12.725   1.903  1.00106.56           C  
ANISOU    6  CG  PRO A 115    14290  11665  14534  -1052  -3507   1013       C  
ATOM      7  CD  PRO A 115       1.976  12.060   0.601  1.00101.32           C  
ANISOU    7  CD  PRO A 115    14240  10806  13452  -1285  -3720   1044       C  
ATOM      8  HA  PRO A 115       4.394  13.333   1.920  1.00108.02           H  
ATOM      9  HB2 PRO A 115       2.651  11.621   3.288  1.00111.27           H  
ATOM     10  HB3 PRO A 115       2.828  13.187   3.492  1.00111.27           H  
ATOM     11  HG2 PRO A 115       0.794  12.337   2.268  1.00127.88           H  
ATOM     12  HG3 PRO A 115       1.488  13.680   1.779  1.00127.88           H  
ATOM     13  HD2 PRO A 115       1.650  11.146   0.574  1.00121.59           H  
ATOM     14  HD3 PRO A 115       1.627  12.559  -0.154  1.00121.59           H  
ATOM     15  N   ASP A 116       5.761  11.789   3.481  1.00 76.81           N  
ANISOU   15  N   ASP A 116    10895   7928  10363   -836  -2353    144       N  
ATOM     16  CA  ASP A 116       6.726  10.854   4.044  1.00 72.03           C  
ANISOU   16  CA  ASP A 116    10351   7404   9615   -825  -2108    -25       C  
ATOM     17  C   ASP A 116       6.006   9.686   4.706  1.00 73.85           C  
ANISOU   17  C   ASP A 116    10459   7778   9824   -898  -2242    -35       C  
ATOM     18  O   ASP A 116       4.965   9.860   5.349  1.00 72.39           O  
ANISOU   18  O   ASP A 116     9924   7713   9870   -882  -2388     38       O  
ATOM     19  CB  ASP A 116       7.628  11.547   5.066  1.00 68.07           C  
ANISOU   19  CB  ASP A 116     9578   6973   9314   -696  -1824   -188       C  
ATOM     20  CG  ASP A 116       8.380  12.728   4.477  1.00 69.75           C  
ANISOU   20  CG  ASP A 116     9882   7032   9587   -666  -1714   -144       C  
ATOM     21  OD1 ASP A 116       8.615  13.716   5.212  1.00 65.43           O  
ANISOU   21  OD1 ASP A 116     9116   6472   9273   -600  -1646   -223       O  
ATOM     22  OD2 ASP A 116       8.723  12.672   3.275  1.00 66.15           O  
ANISOU   22  OD2 ASP A 116     9760   6445   8927   -709  -1702    -20       O  
ATOM     23  H   ASP A 116       5.732  12.555   3.870  1.00 92.18           H  
ATOM     24  HA  ASP A 116       7.289  10.515   3.331  1.00 86.44           H  
ATOM     25  HB2 ASP A 116       7.084  11.873   5.799  1.00 81.69           H  
ATOM     26  HB3 ASP A 116       8.281  10.910   5.395  1.00 81.69           H  
ATOM     27  N   SER A 117       6.563   8.487   4.542  1.00 78.35           N  
ANISOU   27  N   SER A 117    11324   8327  10117   -959  -2168    -93       N  
ATOM     28  CA  SER A 117       6.027   7.304   5.200  1.00 74.59           C  
ANISOU   28  CA  SER A 117    10770   7964   9607  -1046  -2278   -106       C  
ATOM     29  C   SER A 117       6.407   7.330   6.676  1.00 74.32           C  
ANISOU   29  C   SER A 117    10320   8139   9779   -907  -2026   -268       C  
ATOM     30  O   SER A 117       7.578   7.528   7.021  1.00 73.75           O  
ANISOU   30  O   SER A 117    10243   8086   9694   -796  -1737   -402       O  
ATOM     31  CB  SER A 117       6.559   6.038   4.535  1.00 78.23           C  
ANISOU   31  CB  SER A 117    11772   8281   9673  -1125  -2261   -126       C  
ATOM     32  OG  SER A 117       6.054   4.878   5.171  1.00 80.21           O  
ANISOU   32  OG  SER A 117    11976   8610   9890  -1233  -2387   -131       O  
ATOM     33  H   SER A 117       7.254   8.335   4.053  1.00 94.02           H  
ATOM     34  HA  SER A 117       5.060   7.296   5.127  1.00 89.51           H  
ATOM     35  HB2 SER A 117       6.284   6.032   3.605  1.00 93.88           H  
ATOM     36  HB3 SER A 117       7.527   6.034   4.595  1.00 93.88           H  
ATOM     37  HG  SER A 117       6.360   4.190   4.798  1.00 96.25           H  
ATOM     38  N   MET A 118       5.420   7.133   7.545  1.00 63.51           N  
ANISOU   38  N   MET A 118     8600   6928   8601   -917  -2144   -216       N  
ATOM     39  CA  MET A 118       5.633   7.174   8.991  1.00 60.12           C  
ANISOU   39  CA  MET A 118     7825   6687   8332   -770  -1923   -359       C  
ATOM     40  C   MET A 118       5.975   5.766   9.458  1.00 56.59           C  
ANISOU   40  C   MET A 118     7472   6315   7715   -835  -1862   -423       C  
ATOM     41  O   MET A 118       5.130   4.869   9.419  1.00 55.96           O  
ANISOU   41  O   MET A 118     7398   6264   7600   -977  -2071   -291       O  
ATOM     42  CB  MET A 118       4.396   7.706   9.703  1.00 63.36           C  
ANISOU   42  CB  MET A 118     7830   7228   9017   -679  -2004   -235       C  
ATOM     43  CG  MET A 118       3.870   8.993   9.100  1.00 73.69           C  
ANISOU   43  CG  MET A 118     9077   8434  10487   -606  -2100   -113       C  
ATOM     44  SD  MET A 118       4.125  10.395  10.182  1.00 78.00           S  
ANISOU   44  SD  MET A 118     9417   8984  11234   -309  -1830   -277       S  
ATOM     45  CE  MET A 118       2.601  10.377  11.139  1.00 66.04           C  
ANISOU   45  CE  MET A 118     7468   7666   9957   -120  -1821    -64       C  
ATOM     46  H   MET A 118       4.605   6.973   7.320  1.00 76.21           H  
ATOM     47  HA  MET A 118       6.370   7.771   9.192  1.00 72.15           H  
ATOM     48  HB2 MET A 118       3.692   7.041   9.649  1.00 76.04           H  
ATOM     49  HB3 MET A 118       4.618   7.879  10.631  1.00 76.04           H  
ATOM     50  HG2 MET A 118       4.333   9.167   8.265  1.00 88.43           H  
ATOM     51  HG3 MET A 118       2.918   8.904   8.939  1.00 88.43           H  
ATOM     52  HE1 MET A 118       2.603  11.130  11.750  1.00 79.24           H  
ATOM     53  HE2 MET A 118       1.847  10.444  10.533  1.00 79.24           H  
ATOM     54  HE3 MET A 118       2.552   9.547  11.638  1.00 79.24           H  
ATOM     55  N   VAL A 119       7.211   5.572   9.902  1.00 50.77           N  
ANISOU   55  N   VAL A 119     6796   5603   6891   -744  -1598   -591       N  
ATOM     56  CA  VAL A 119       7.751   4.254  10.202  1.00 42.29           C  
ANISOU   56  CA  VAL A 119     5874   4566   5628   -769  -1499   -643       C  
ATOM     57  C   VAL A 119       7.840   4.086  11.708  1.00 37.18           C  
ANISOU   57  C   VAL A 119     4888   4128   5111   -672  -1361   -751       C  
ATOM     58  O   VAL A 119       8.295   4.987  12.421  1.00 37.20           O  
ANISOU   58  O   VAL A 119     4686   4195   5253   -556  -1232   -856       O  
ATOM     59  CB  VAL A 119       9.136   4.067   9.550  1.00 46.40           C  
ANISOU   59  CB  VAL A 119     6704   4974   5951   -702  -1271   -682       C  
ATOM     60  CG1 VAL A 119       9.682   2.682   9.846  1.00 45.16           C  
ANISOU   60  CG1 VAL A 119     6728   4836   5594   -675  -1139   -711       C  
ATOM     61  CG2 VAL A 119       9.057   4.315   8.049  1.00 49.77           C  
ANISOU   61  CG2 VAL A 119     7528   5177   6206   -761  -1372   -573       C  
ATOM     62  H   VAL A 119       7.772   6.209  10.040  1.00 60.92           H  
ATOM     63  HA  VAL A 119       7.147   3.576   9.861  1.00 50.75           H  
ATOM     64  HB  VAL A 119       9.753   4.714   9.926  1.00 55.68           H  
ATOM     65 HG11 VAL A 119      10.457   2.521   9.285  1.00 54.19           H  
ATOM     66 HG12 VAL A 119       9.936   2.636  10.782  1.00 54.19           H  
ATOM     67 HG13 VAL A 119       8.994   2.024   9.658  1.00 54.19           H  
ATOM     68 HG21 VAL A 119       9.917   4.114   7.650  1.00 59.73           H  
ATOM     69 HG22 VAL A 119       8.374   3.739   7.670  1.00 59.73           H  
ATOM     70 HG23 VAL A 119       8.828   5.245   7.895  1.00 59.73           H  
ATOM     71  N   LEU A 120       7.421   2.925  12.192  1.00 40.38           N  
ANISOU   71  N   LEU A 120     5285   4612   5446   -733  -1408   -718       N  
ATOM     72  CA  LEU A 120       7.514   2.596  13.616  1.00 40.54           C  
ANISOU   72  CA  LEU A 120     5036   4829   5540   -638  -1269   -804       C  
ATOM     73  C   LEU A 120       7.965   1.141  13.727  1.00 36.37           C  
ANISOU   73  C   LEU A 120     4711   4296   4811   -690  -1217   -807       C  
ATOM     74  O   LEU A 120       7.165   0.215  13.564  1.00 39.00           O  
ANISOU   74  O   LEU A 120     5138   4600   5082   -832  -1390   -690       O  
ATOM     75  CB  LEU A 120       6.194   2.838  14.323  1.00 38.32           C  
ANISOU   75  CB  LEU A 120     4427   4683   5449   -618  -1363   -698       C  
ATOM     76  CG  LEU A 120       6.207   2.762  15.844  1.00 41.47           C  
ANISOU   76  CG  LEU A 120     4573   5276   5908   -465  -1183   -784       C  
ATOM     77  CD1 LEU A 120       7.337   3.548  16.447  1.00 37.66           C  
ANISOU   77  CD1 LEU A 120     4107   4791   5410   -328  -1009   -997       C  
ATOM     78  CD2 LEU A 120       4.871   3.266  16.401  1.00 45.67           C  
ANISOU   78  CD2 LEU A 120     4788   5925   6639   -363  -1201   -628       C  
ATOM     79  H   LEU A 120       7.074   2.301  11.713  1.00 48.46           H  
ATOM     80  HA  LEU A 120       8.188   3.153  14.037  1.00 48.65           H  
ATOM     81  HB2 LEU A 120       5.885   3.726  14.086  1.00 45.98           H  
ATOM     82  HB3 LEU A 120       5.561   2.172  14.011  1.00 45.98           H  
ATOM     83  HG  LEU A 120       6.340   1.835  16.096  1.00 49.77           H  
ATOM     84 HD11 LEU A 120       7.276   3.497  17.414  1.00 45.19           H  
ATOM     85 HD12 LEU A 120       8.179   3.171  16.148  1.00 45.19           H  
ATOM     86 HD13 LEU A 120       7.267   4.472  16.160  1.00 45.19           H  
ATOM     87 HD21 LEU A 120       4.890   3.207  17.369  1.00 54.80           H  
ATOM     88 HD22 LEU A 120       4.743   4.188  16.128  1.00 54.80           H  
ATOM     89 HD23 LEU A 120       4.155   2.714  16.050  1.00 54.80           H  
ATOM     90  N   LEU A 121       9.251   0.951  13.991  1.00 33.56           N  
ANISOU   90  N   LEU A 121     4424   3958   4370   -582   -996   -908       N  
ATOM     91  CA  LEU A 121       9.797  -0.385  14.167  1.00 31.62           C  
ANISOU   91  CA  LEU A 121     4370   3703   3940   -567   -893   -902       C  
ATOM     92  C   LEU A 121       9.202  -1.062  15.402  1.00 30.12           C  
ANISOU   92  C   LEU A 121     3954   3686   3804   -582   -919   -907       C  
ATOM     93  O   LEU A 121       9.051  -0.447  16.461  1.00 30.87           O  
ANISOU   93  O   LEU A 121     3728   3952   4049   -503   -869   -970       O  
ATOM     94  CB  LEU A 121      11.320  -0.303  14.313  1.00 31.35           C  
ANISOU   94  CB  LEU A 121     4336   3702   3873   -414   -631   -943       C  
ATOM     95  CG  LEU A 121      12.083   0.298  13.129  1.00 35.57           C  
ANISOU   95  CG  LEU A 121     5069   4087   4358   -364   -528   -883       C  
ATOM     96  CD1 LEU A 121      13.579   0.375  13.414  1.00 34.52           C  
ANISOU   96  CD1 LEU A 121     4811   4039   4268   -219   -266   -832       C  
ATOM     97  CD2 LEU A 121      11.821  -0.509  11.866  1.00 34.23           C  
ANISOU   97  CD2 LEU A 121     5414   3678   3916   -396   -562   -804       C  
ATOM     98  H   LEU A 121       9.830   1.581  14.074  1.00 40.27           H  
ATOM     99  HA  LEU A 121       9.578  -0.926  13.392  1.00 37.94           H  
ATOM    100  HB2 LEU A 121      11.519   0.244  15.089  1.00 37.62           H  
ATOM    101  HB3 LEU A 121      11.658  -1.203  14.446  1.00 37.62           H  
ATOM    102  HG  LEU A 121      11.767   1.204  12.987  1.00 42.68           H  
ATOM    103 HD11 LEU A 121      14.032   0.720  12.628  1.00 41.43           H  
ATOM    104 HD12 LEU A 121      13.726   0.968  14.167  1.00 41.43           H  
ATOM    105 HD13 LEU A 121      13.907  -0.513  13.622  1.00 41.43           H  
ATOM    106 HD21 LEU A 121      12.407  -0.191  11.162  1.00 41.08           H  
ATOM    107 HD22 LEU A 121      11.999  -1.445  12.047  1.00 41.08           H  
ATOM    108 HD23 LEU A 121      10.895  -0.393  11.604  1.00 41.08           H  
ATOM    109  N   SER A 122       8.880  -2.343  15.271  1.00 34.16           N  
ANISOU  109  N   SER A 122     4688   4125   4167   -677   -991   -832       N  
ATOM    110  CA  SER A 122       8.615  -3.140  16.458  1.00 36.22           C  
ANISOU  110  CA  SER A 122     4767   4544   4450   -670   -955   -820       C  
ATOM    111  C   SER A 122       9.929  -3.382  17.203  1.00 34.59           C  
ANISOU  111  C   SER A 122     4520   4436   4186   -489   -700   -921       C  
ATOM    112  O   SER A 122      11.015  -3.089  16.709  1.00 32.26           O  
ANISOU  112  O   SER A 122     4336   4080   3842   -387   -558   -952       O  
ATOM    113  CB  SER A 122       7.937  -4.458  16.094  1.00 36.29           C  
ANISOU  113  CB  SER A 122     5056   4413   4321   -856  -1137   -688       C  
ATOM    114  OG  SER A 122       8.813  -5.324  15.404  1.00 40.27           O  
ANISOU  114  OG  SER A 122     6040   4700   4561   -813  -1046   -718       O  
ATOM    115  H   SER A 122       8.811  -2.764  14.524  1.00 41.00           H  
ATOM    116  HA  SER A 122       8.005  -2.667  17.046  1.00 43.46           H  
ATOM    117  HB2 SER A 122       7.645  -4.894  16.910  1.00 43.55           H  
ATOM    118  HB3 SER A 122       7.174  -4.270  15.526  1.00 43.55           H  
ATOM    119  HG  SER A 122       9.068  -4.965  14.689  1.00 48.32           H  
ATOM    120  N   SER A 123       9.821  -3.907  18.416  1.00 29.55           N  
ANISOU  120  N   SER A 123     3692   3968   3569   -449   -645   -929       N  
ATOM    121  CA  SER A 123      10.970  -4.102  19.281  1.00 30.71           C  
ANISOU  121  CA  SER A 123     3747   4238   3684   -299   -459   -993       C  
ATOM    122  C   SER A 123      11.217  -5.588  19.526  1.00 33.60           C  
ANISOU  122  C   SER A 123     4303   4571   3892   -282   -391   -925       C  
ATOM    123  O   SER A 123      10.336  -6.437  19.348  1.00 28.24           O  
ANISOU  123  O   SER A 123     3779   3802   3148   -413   -513   -843       O  
ATOM    124  CB  SER A 123      10.773  -3.373  20.610  1.00 30.52           C  
ANISOU  124  CB  SER A 123     3400   4424   3772   -234   -446  -1076       C  
ATOM    125  OG  SER A 123      10.867  -1.967  20.431  1.00 31.61           O  
ANISOU  125  OG  SER A 123     3436   4548   4026   -212   -481  -1158       O  
ATOM    126  H   SER A 123       9.077  -4.162  18.764  1.00 35.46           H  
ATOM    127  HA  SER A 123      11.762  -3.748  18.847  1.00 36.86           H  
ATOM    128  HB2 SER A 123       9.895  -3.588  20.962  1.00 36.62           H  
ATOM    129  HB3 SER A 123      11.460  -3.659  21.232  1.00 36.62           H  
ATOM    130  HG  SER A 123      11.609  -1.770  20.089  1.00 37.93           H  
ATOM    131  N   SER A 124      12.441  -5.891  19.950  1.00 31.08           N  
ANISOU  131  N   SER A 124     3963   4318   3528   -129   -215   -926       N  
ATOM    132  CA  SER A 124      12.863  -7.274  20.100  1.00 32.04           C  
ANISOU  132  CA  SER A 124     4299   4381   3493    -56   -105   -846       C  
ATOM    133  C   SER A 124      12.153  -7.936  21.272  1.00 30.41           C  
ANISOU  133  C   SER A 124     3958   4310   3287   -114   -168   -833       C  
ATOM    134  O   SER A 124      12.053  -7.365  22.371  1.00 27.31           O  
ANISOU  134  O   SER A 124     3254   4134   2990    -87   -176   -889       O  
ATOM    135  CB  SER A 124      14.380  -7.353  20.312  1.00 30.05           C  
ANISOU  135  CB  SER A 124     3971   4205   3242    152    112   -784       C  
ATOM    136  OG  SER A 124      15.062  -6.935  19.162  1.00 33.84           O  
ANISOU  136  OG  SER A 124     4597   4552   3710    236    230   -726       O  
ATOM    137  H   SER A 124      13.044  -5.313  20.156  1.00 37.30           H  
ATOM    138  HA  SER A 124      12.636  -7.758  19.291  1.00 38.45           H  
ATOM    139  HB2 SER A 124      14.627  -6.778  21.053  1.00 36.06           H  
ATOM    140  HB3 SER A 124      14.625  -8.271  20.509  1.00 36.06           H  
ATOM    141  HG  SER A 124      14.766  -6.192  18.907  1.00 40.61           H  
ATOM    142  N   TRP A 125      11.684  -9.163  21.034  1.00 27.67           N  
ANISOU  142  N   TRP A 125     3181   3361   3972   -505   -294   -320       N  
ATOM    143  CA  TRP A 125      11.045  -9.964  22.060  1.00 29.65           C  
ANISOU  143  CA  TRP A 125     3401   3614   4252   -470   -283   -321       C  
ATOM    144  C   TRP A 125      12.090 -10.721  22.863  1.00 34.24           C  
ANISOU  144  C   TRP A 125     3984   4184   4842   -432   -238   -350       C  
ATOM    145  O   TRP A 125      13.115 -11.157  22.329  1.00 32.80           O  
ANISOU  145  O   TRP A 125     3824   3994   4645   -438   -211   -385       O  
ATOM    146  CB  TRP A 125      10.069 -10.964  21.430  1.00 29.14           C  
ANISOU  146  CB  TRP A 125     3349   3548   4177   -521   -300   -313       C  
ATOM    147  CG  TRP A 125       8.919 -10.317  20.743  1.00 36.41           C  
ANISOU  147  CG  TRP A 125     4251   4490   5094   -548   -361   -285       C  
ATOM    148  CD1 TRP A 125       8.689 -10.262  19.400  1.00 38.64           C  
ANISOU  148  CD1 TRP A 125     4576   4774   5332   -603   -403   -281       C  
ATOM    149  CD2 TRP A 125       7.841  -9.609  21.367  1.00 33.19           C  
ANISOU  149  CD2 TRP A 125     3773   4114   4724   -510   -396   -262       C  
ATOM    150  NE1 TRP A 125       7.522  -9.564  19.148  1.00 37.82           N  
ANISOU  150  NE1 TRP A 125     4434   4692   5244   -600   -477   -248       N  
ATOM    151  CE2 TRP A 125       6.986  -9.156  20.339  1.00 36.60           C  
ANISOU  151  CE2 TRP A 125     4203   4556   5148   -537   -471   -243       C  
ATOM    152  CE3 TRP A 125       7.514  -9.319  22.695  1.00 31.86           C  
ANISOU  152  CE3 TRP A 125     3540   3977   4587   -447   -372   -265       C  
ATOM    153  CZ2 TRP A 125       5.821  -8.448  20.598  1.00 39.84           C  
ANISOU  153  CZ2 TRP A 125     4536   5002   5599   -492   -526   -230       C  
ATOM    154  CZ3 TRP A 125       6.353  -8.612  22.950  1.00 37.73           C  
ANISOU  154  CZ3 TRP A 125     4207   4768   5361   -406   -411   -262       C  
ATOM    155  CH2 TRP A 125       5.522  -8.183  21.907  1.00 39.41           C  
ANISOU  155  CH2 TRP A 125     4406   4983   5583   -423   -490   -246       C  
ATOM    156  H   TRP A 125      11.729  -9.554  20.270  1.00 33.21           H  
ATOM    157  HA  TRP A 125      10.549  -9.385  22.661  1.00 35.58           H  
ATOM    158  HB2 TRP A 125      10.546 -11.496  20.774  1.00 34.97           H  
ATOM    159  HB3 TRP A 125       9.714 -11.538  22.127  1.00 34.97           H  
ATOM    160  HD1 TRP A 125       9.237 -10.638  18.749  1.00 46.37           H  
ATOM    161  HE1 TRP A 125       7.187  -9.412  18.370  1.00 45.39           H  
ATOM    162  HE3 TRP A 125       8.065  -9.595  23.391  1.00 38.23           H  
ATOM    163  HZ2 TRP A 125       5.264  -8.166  19.909  1.00 47.81           H  
ATOM    164  HZ3 TRP A 125       6.120  -8.418  23.829  1.00 45.28           H  
ATOM    165  HH2 TRP A 125       4.749  -7.706  22.109  1.00 47.29           H  
ATOM    166  N   LEU A 126      11.822 -10.883  24.133  1.00 33.73           N  
ANISOU  166  N   LEU A 126     3893   4128   4794   -388   -232   -336       N  
ATOM    167  CA  LEU A 126      12.670 -11.730  24.963  1.00 32.62           C  
ANISOU  167  CA  LEU A 126     3765   3972   4657   -348   -210   -347       C  
ATOM    168  C   LEU A 126      12.078 -13.135  25.069  1.00 34.94           C  
ANISOU  168  C   LEU A 126     4092   4230   4953   -377   -208   -319       C  
ATOM    169  O   LEU A 126      10.854 -13.298  25.055  1.00 30.69           O  
ANISOU  169  O   LEU A 126     3539   3708   4415   -425   -215   -281       O  
ATOM    170  CB  LEU A 126      12.818 -11.120  26.352  1.00 33.00           C  
ANISOU  170  CB  LEU A 126     3783   4054   4702   -289   -213   -342       C  
ATOM    171  CG  LEU A 126      13.394  -9.700  26.346  1.00 35.82           C  
ANISOU  171  CG  LEU A 126     4117   4423   5070   -267   -233   -376       C  
ATOM    172  CD1 LEU A 126      13.588  -9.191  27.762  1.00 36.76           C  
ANISOU  172  CD1 LEU A 126     4216   4573   5178   -202   -246   -393       C  
ATOM    173  CD2 LEU A 126      14.709  -9.642  25.571  1.00 35.56           C  
ANISOU  173  CD2 LEU A 126     4088   4374   5048   -287   -224   -408       C  
ATOM    174  H   LEU A 126      11.160 -10.521  24.546  1.00 40.47           H  
ATOM    175  HA  LEU A 126      13.555 -11.806  24.574  1.00 39.15           H  
ATOM    176  HB2 LEU A 126      11.944 -11.084  26.771  1.00 39.60           H  
ATOM    177  HB3 LEU A 126      13.414 -11.680  26.875  1.00 39.60           H  
ATOM    178  HG  LEU A 126      12.761  -9.115  25.901  1.00 42.98           H  
ATOM    179 HD11 LEU A 126      13.992  -8.310  27.728  1.00 44.11           H  
ATOM    180 HD12 LEU A 126      12.725  -9.143  28.201  1.00 44.11           H  
ATOM    181 HD13 LEU A 126      14.169  -9.803  28.240  1.00 44.11           H  
ATOM    182 HD21 LEU A 126      15.204  -8.855  25.847  1.00 42.67           H  
ATOM    183 HD22 LEU A 126      15.224 -10.441  25.763  1.00 42.67           H  
ATOM    184 HD23 LEU A 126      14.514  -9.595  24.622  1.00 42.67           H  
ATOM    185  N   PRO A 127      12.922 -14.167  25.184  1.00 33.06           N  
ANISOU  185  N   PRO A 127     3896   3939   4727   -351   -207   -337       N  
ATOM    186  CA  PRO A 127      12.414 -15.555  25.143  1.00 34.43           C  
ANISOU  186  CA  PRO A 127     4126   4040   4916   -389   -223   -310       C  
ATOM    187  C   PRO A 127      11.746 -15.930  26.456  1.00 33.59           C  
ANISOU  187  C   PRO A 127     4019   3943   4799   -402   -223   -228       C  
ATOM    188  O   PRO A 127      12.289 -15.698  27.542  1.00 33.89           O  
ANISOU  188  O   PRO A 127     4050   4009   4818   -343   -220   -209       O  
ATOM    189  CB  PRO A 127      13.675 -16.397  24.896  1.00 33.02           C  
ANISOU  189  CB  PRO A 127     3992   3793   4760   -327   -232   -369       C  
ATOM    190  CG  PRO A 127      14.777 -15.570  25.522  1.00 33.35           C  
ANISOU  190  CG  PRO A 127     3983   3891   4797   -251   -220   -392       C  
ATOM    191  CD  PRO A 127      14.387 -14.111  25.349  1.00 32.10           C  
ANISOU  191  CD  PRO A 127     3768   3813   4615   -282   -202   -386       C  
ATOM    192  HA  PRO A 127      11.789 -15.673  24.411  1.00 41.32           H  
ATOM    193  HB2 PRO A 127      13.594 -17.261  25.329  1.00 39.62           H  
ATOM    194  HB3 PRO A 127      13.820 -16.515  23.944  1.00 39.62           H  
ATOM    195  HG2 PRO A 127      14.853 -15.792  26.463  1.00 40.02           H  
ATOM    196  HG3 PRO A 127      15.615 -15.754  25.069  1.00 40.02           H  
ATOM    197  HD2 PRO A 127      14.627 -13.595  26.134  1.00 38.52           H  
ATOM    198  HD3 PRO A 127      14.809 -13.732  24.562  1.00 38.52           H  
ATOM    199  N   LEU A 128      10.565 -16.528  26.349  1.00 34.83           N  
ANISOU  199  N   LEU A 128     4182   4087   4963   -490   -229   -177       N  
ATOM    200  CA  LEU A 128       9.770 -16.823  27.533  1.00 35.45           C  
ANISOU  200  CA  LEU A 128     4245   4207   5017   -531   -212    -86       C  
ATOM    201  C   LEU A 128      10.500 -17.808  28.437  1.00 29.35           C  
ANISOU  201  C   LEU A 128     3554   3358   4239   -502   -233    -36       C  
ATOM    202  O   LEU A 128      10.969 -18.857  27.990  1.00 31.79           O  
ANISOU  202  O   LEU A 128     3947   3541   4592   -505   -276    -46       O  
ATOM    203  CB  LEU A 128       8.412 -17.376  27.115  1.00 31.28           C  
ANISOU  203  CB  LEU A 128     3696   3681   4508   -653   -216    -41       C  
ATOM    204  CG  LEU A 128       7.428 -17.725  28.226  1.00 38.98           C  
ANISOU  204  CG  LEU A 128     4634   4726   5452   -729   -182     62       C  
ATOM    205  CD1 LEU A 128       7.124 -16.491  29.066  1.00 38.65           C  
ANISOU  205  CD1 LEU A 128     4492   4840   5353   -666   -128     54       C  
ATOM    206  CD2 LEU A 128       6.148 -18.318  27.641  1.00 38.55           C  
ANISOU  206  CD2 LEU A 128     4543   4671   5434   -868   -196     98       C  
ATOM    207  H   LEU A 128      10.204 -16.771  25.608  1.00 41.79           H  
ATOM    208  HA  LEU A 128       9.624 -16.009  28.040  1.00 42.54           H  
ATOM    209  HB2 LEU A 128       7.980 -16.712  26.555  1.00 37.54           H  
ATOM    210  HB3 LEU A 128       8.565 -18.189  26.609  1.00 37.54           H  
ATOM    211  HG  LEU A 128       7.823 -18.393  28.807  1.00 46.78           H  
ATOM    212 HD11 LEU A 128       6.397 -16.695  29.675  1.00 46.38           H  
ATOM    213 HD12 LEU A 128       7.918 -16.248  29.568  1.00 46.38           H  
ATOM    214 HD13 LEU A 128       6.869 -15.763  28.478  1.00 46.38           H  
ATOM    215 HD21 LEU A 128       5.540 -18.533  28.366  1.00 46.26           H  
ATOM    216 HD22 LEU A 128       5.740 -17.666  27.050  1.00 46.26           H  
ATOM    217 HD23 LEU A 128       6.370 -19.121  27.145  1.00 46.26           H  
ATOM    218  N   ASN A 129      10.598 -17.456  29.717  1.00 33.63           N  
ANISOU  218  N   ASN A 129     4080   3976   4723   -465   -211     14       N  
ATOM    219  CA  ASN A 129      11.139 -18.316  30.766  1.00 35.69           C  
ANISOU  219  CA  ASN A 129     4420   4183   4956   -443   -240     89       C  
ATOM    220  C   ASN A 129      12.571 -18.746  30.499  1.00 37.18           C  
ANISOU  220  C   ASN A 129     4671   4265   5192   -340   -300     31       C  
ATOM    221  O   ASN A 129      13.015 -19.773  31.012  1.00 36.84           O  
ANISOU  221  O   ASN A 129     4717   4122   5158   -321   -354     88       O  
ATOM    222  CB  ASN A 129      10.252 -19.549  30.968  1.00 38.68           C  
ANISOU  222  CB  ASN A 129     4863   4493   5342   -567   -252    202       C  
ATOM    223  CG  ASN A 129       8.891 -19.188  31.501  1.00 37.20           C  
ANISOU  223  CG  ASN A 129     4592   4447   5096   -668   -183    272       C  
ATOM    224  OD1 ASN A 129       8.767 -18.334  32.385  1.00 39.68           O  
ANISOU  224  OD1 ASN A 129     4842   4905   5329   -624   -133    274       O  
ATOM    225  ND2 ASN A 129       7.862 -19.807  30.953  1.00 43.82           N  
ANISOU  225  ND2 ASN A 129     5419   5256   5975   -800   -181    314       N  
ATOM    226  H   ASN A 129      10.347 -16.689  30.015  1.00 40.36           H  
ATOM    227  HA  ASN A 129      11.151 -17.806  31.591  1.00 42.82           H  
ATOM    228  HB2 ASN A 129      10.134 -20.000  30.117  1.00 46.42           H  
ATOM    229  HB3 ASN A 129      10.676 -20.147  31.603  1.00 46.42           H  
ATOM    230 HD21 ASN A 129       7.064 -19.636  31.223  1.00 52.58           H  
ATOM    231 HD22 ASN A 129       7.990 -20.382  30.326  1.00 52.58           H  
ATOM    232  N   LYS A 130      13.310 -17.975  29.716  1.00 34.87           N  
ANISOU  232  N   LYS A 130     4326   3995   4929   -275   -293    -79       N  
ATOM    233  CA  LYS A 130      14.694 -18.275  29.380  1.00 38.84           C  
ANISOU  233  CA  LYS A 130     4848   4433   5476   -174   -333   -154       C  
ATOM    234  C   LYS A 130      15.574 -17.177  29.954  1.00 34.23           C  
ANISOU  234  C   LYS A 130     4194   3947   4866    -95   -329   -199       C  
ATOM    235  O   LYS A 130      15.310 -15.987  29.749  1.00 31.69           O  
ANISOU  235  O   LYS A 130     3804   3714   4524   -116   -289   -233       O  
ATOM    236  CB  LYS A 130      14.854 -18.388  27.861  1.00 42.31           C  
ANISOU  236  CB  LYS A 130     5279   4830   5966   -186   -321   -249       C  
ATOM    237  CG  LYS A 130      16.285 -18.535  27.376  1.00 53.13           C  
ANISOU  237  CG  LYS A 130     6633   6177   7376    -81   -338   -350       C  
ATOM    238  CD  LYS A 130      16.800 -19.957  27.500  1.00 64.24           C  
ANISOU  238  CD  LYS A 130     8128   7445   8837    -14   -405   -356       C  
ATOM    239  CE  LYS A 130      18.263 -20.039  27.079  1.00 68.99           C  
ANISOU  239  CE  LYS A 130     8679   8052   9480    114   -417   -475       C  
ATOM    240  NZ  LYS A 130      19.141 -19.251  27.997  1.00 57.36           N  
ANISOU  240  NZ  LYS A 130     7127   6676   7992    182   -426   -470       N  
ATOM    241  H   LYS A 130      13.022 -17.249  29.355  1.00 41.85           H  
ATOM    242  HA  LYS A 130      14.976 -19.116  29.772  1.00 46.61           H  
ATOM    243  HB2 LYS A 130      14.363 -19.168  27.558  1.00 50.77           H  
ATOM    244  HB3 LYS A 130      14.490 -17.587  27.453  1.00 50.77           H  
ATOM    245  HG2 LYS A 130      16.331 -18.280  26.442  1.00 63.75           H  
ATOM    246  HG3 LYS A 130      16.860 -17.961  27.906  1.00 63.75           H  
ATOM    247  HD2 LYS A 130      16.728 -20.249  28.422  1.00 77.09           H  
ATOM    248  HD3 LYS A 130      16.281 -20.541  26.926  1.00 77.09           H  
ATOM    249  HE2 LYS A 130      18.553 -20.965  27.101  1.00 82.78           H  
ATOM    250  HE3 LYS A 130      18.360 -19.682  26.183  1.00 82.78           H  
ATOM    251  HZ1 LYS A 130      19.993 -19.348  27.762  1.00 68.84           H  
ATOM    252  HZ2 LYS A 130      18.926 -18.388  27.957  1.00 68.84           H  
ATOM    253  HZ3 LYS A 130      19.038 -19.535  28.835  1.00 68.84           H  
ATOM    254  N   ASP A 131      16.598 -17.579  30.693  1.00 36.84           N  
ANISOU  254  N   ASP A 131     4547   4252   5200     -5   -384   -197       N  
ATOM    255  CA  ASP A 131      17.562 -16.637  31.247  1.00 33.59           C  
ANISOU  255  CA  ASP A 131     4065   3925   4771     68   -399   -249       C  
ATOM    256  C   ASP A 131      18.392 -16.022  30.130  1.00 38.42           C  
ANISOU  256  C   ASP A 131     4596   4562   5439     86   -374   -360       C  
ATOM    257  O   ASP A 131      18.917 -16.734  29.269  1.00 34.04           O  
ANISOU  257  O   ASP A 131     4046   3949   4939    117   -376   -413       O  
ATOM    258  CB  ASP A 131      18.467 -17.341  32.258  1.00 36.99           C  
ANISOU  258  CB  ASP A 131     4537   4321   5196    163   -483   -218       C  
ATOM    259  CG  ASP A 131      19.557 -16.433  32.797  1.00 41.05           C  
ANISOU  259  CG  ASP A 131     4970   4924   5703    236   -517   -284       C  
ATOM    260  OD1 ASP A 131      20.448 -16.027  32.009  1.00 37.34           O  
ANISOU  260  OD1 ASP A 131     4414   4475   5297    266   -507   -382       O  
ATOM    261  OD2 ASP A 131      19.526 -16.123  34.005  1.00 40.22           O  
ANISOU  261  OD2 ASP A 131     4883   4877   5521    255   -553   -239       O  
ATOM    262  H   ASP A 131      16.761 -18.400  30.892  1.00 44.21           H  
ATOM    263  HA  ASP A 131      17.092 -15.924  31.707  1.00 40.31           H  
ATOM    264  HB2 ASP A 131      17.930 -17.644  33.007  1.00 44.39           H  
ATOM    265  HB3 ASP A 131      18.892 -18.099  31.827  1.00 44.39           H  
ATOM    266  N   ILE A 132      18.517 -14.696  30.152  1.00 37.36           N  
ANISOU  266  N   ILE A 132     4392   4516   5289     66   -349   -397       N  
ATOM    267  CA  ILE A 132      19.335 -13.972  29.193  1.00 33.57           C  
ANISOU  267  CA  ILE A 132     3832   4073   4849     58   -323   -480       C  
ATOM    268  C   ILE A 132      20.179 -12.949  29.940  1.00 36.51           C  
ANISOU  268  C   ILE A 132     4137   4516   5220     86   -356   -515       C  
ATOM    269  O   ILE A 132      19.849 -12.530  31.051  1.00 34.01           O  
ANISOU  269  O   ILE A 132     3839   4225   4856    100   -389   -485       O  
ATOM    270  CB  ILE A 132      18.484 -13.274  28.107  1.00 37.61           C  
ANISOU  270  CB  ILE A 132     4340   4596   5352    -36   -266   -482       C  
ATOM    271  CG1 ILE A 132      17.486 -12.313  28.747  1.00 36.08           C  
ANISOU  271  CG1 ILE A 132     4153   4436   5120    -71   -267   -440       C  
ATOM    272  CG2 ILE A 132      17.762 -14.307  27.256  1.00 41.16           C  
ANISOU  272  CG2 ILE A 132     4850   4983   5807    -68   -245   -466       C  
ATOM    273  CD1 ILE A 132      16.760 -11.434  27.760  1.00 38.04           C  
ANISOU  273  CD1 ILE A 132     4391   4692   5370   -143   -238   -442       C  
ATOM    274  H   ILE A 132      18.128 -14.187  30.726  1.00 44.84           H  
ATOM    275  HA  ILE A 132      19.934 -14.596  28.754  1.00 40.28           H  
ATOM    276  HB  ILE A 132      19.077 -12.762  27.534  1.00 45.13           H  
ATOM    277 HG12 ILE A 132      16.821 -12.831  29.227  1.00 43.30           H  
ATOM    278 HG13 ILE A 132      17.963 -11.735  29.362  1.00 43.30           H  
ATOM    279 HG21 ILE A 132      17.311 -13.855  26.526  1.00 49.40           H  
ATOM    280 HG22 ILE A 132      18.411 -14.936  26.905  1.00 49.40           H  
ATOM    281 HG23 ILE A 132      17.114 -14.773  27.807  1.00 49.40           H  
ATOM    282 HD11 ILE A 132      16.255 -10.764  28.247  1.00 45.65           H  
ATOM    283 HD12 ILE A 132      17.409 -11.005  27.182  1.00 45.65           H  
ATOM    284 HD13 ILE A 132      16.158 -11.982  27.232  1.00 45.65           H  
ATOM    285  N   GLU A 133      21.289 -12.559  29.315  1.00 33.08           N  
ANISOU  285  N   GLU A 133     3617   4121   4832     88   -347   -586       N  
ATOM    286  CA  GLU A 133      22.114 -11.464  29.803  1.00 34.03           C  
ANISOU  286  CA  GLU A 133     3659   4304   4966     81   -381   -626       C  
ATOM    287  C   GLU A 133      21.630 -10.174  29.160  1.00 29.79           C  
ANISOU  287  C   GLU A 133     3114   3777   4426    -22   -344   -624       C  
ATOM    288  O   GLU A 133      21.335 -10.134  27.966  1.00 27.20           O  
ANISOU  288  O   GLU A 133     2791   3441   4102    -84   -285   -619       O  
ATOM    289  CB  GLU A 133      23.592 -11.700  29.477  1.00 31.99           C  
ANISOU  289  CB  GLU A 133     3291   4097   4766    122   -390   -698       C  
ATOM    290  CG  GLU A 133      24.203 -12.885  30.232  1.00 34.48           C  
ANISOU  290  CG  GLU A 133     3610   4392   5099    250   -459   -705       C  
ATOM    291  CD  GLU A 133      25.651 -13.113  29.891  1.00 41.94           C  
ANISOU  291  CD  GLU A 133     4420   5402   6112    310   -471   -792       C  
ATOM    292  OE1 GLU A 133      26.018 -12.969  28.709  1.00 43.90           O  
ANISOU  292  OE1 GLU A 133     4596   5698   6387    263   -390   -845       O  
ATOM    293  OE2 GLU A 133      26.438 -13.431  30.811  1.00 53.25           O  
ANISOU  293  OE2 GLU A 133     5811   6854   7567    406   -562   -810       O  
ATOM    294  H   GLU A 133      21.588 -12.922  28.595  1.00 39.70           H  
ATOM    295  HA  GLU A 133      22.043 -11.391  30.768  1.00 40.83           H  
ATOM    296  HB2 GLU A 133      23.679 -11.877  28.527  1.00 38.39           H  
ATOM    297  HB3 GLU A 133      24.095 -10.905  29.714  1.00 38.39           H  
ATOM    298  HG2 GLU A 133      24.143 -12.716  31.186  1.00 41.38           H  
ATOM    299  HG3 GLU A 133      23.711 -13.690  30.007  1.00 41.38           H  
ATOM    300  N   VAL A 134      21.548  -9.115  29.954  1.00 28.10           N  
ANISOU  300  N   VAL A 134     2899   3575   4202    -35   -389   -631       N  
ATOM    301  CA  VAL A 134      20.984  -7.863  29.485  1.00 31.13           C  
ANISOU  301  CA  VAL A 134     3298   3938   4593   -116   -380   -625       C  
ATOM    302  C   VAL A 134      21.758  -6.693  30.070  1.00 28.75           C  
ANISOU  302  C   VAL A 134     2953   3649   4322   -141   -444   -673       C  
ATOM    303  O   VAL A 134      22.288  -6.760  31.181  1.00 29.74           O  
ANISOU  303  O   VAL A 134     3058   3803   4437    -80   -506   -708       O  
ATOM    304  CB  VAL A 134      19.485  -7.740  29.864  1.00 26.99           C  
ANISOU  304  CB  VAL A 134     2851   3383   4021   -100   -376   -586       C  
ATOM    305  CG1 VAL A 134      18.700  -8.874  29.271  1.00 31.78           C  
ANISOU  305  CG1 VAL A 134     3496   3973   4606   -100   -323   -538       C  
ATOM    306  CG2 VAL A 134      19.325  -7.699  31.370  1.00 30.34           C  
ANISOU  306  CG2 VAL A 134     3295   3834   4396    -26   -425   -601       C  
ATOM    307  H   VAL A 134      21.813  -9.100  30.772  1.00 33.72           H  
ATOM    308  HA  VAL A 134      21.079  -7.829  28.521  1.00 37.36           H  
ATOM    309  HB  VAL A 134      19.131  -6.913  29.502  1.00 32.39           H  
ATOM    310 HG11 VAL A 134      17.755  -8.715  29.417  1.00 38.14           H  
ATOM    311 HG12 VAL A 134      18.885  -8.923  28.320  1.00 38.14           H  
ATOM    312 HG13 VAL A 134      18.967  -9.701  29.702  1.00 38.14           H  
ATOM    313 HG21 VAL A 134      18.387  -7.807  31.591  1.00 36.40           H  
ATOM    314 HG22 VAL A 134      19.843  -8.419  31.762  1.00 36.40           H  
ATOM    315 HG23 VAL A 134      19.646  -6.844  31.698  1.00 36.40           H  
ATOM    316  N   GLU A 135      21.806  -5.610  29.309  1.00 28.13           N  
ANISOU  316  N   GLU A 135     2867   3541   4279   -237   -440   -670       N  
ATOM    317  CA  GLU A 135      22.212  -4.306  29.808  1.00 33.30           C  
ANISOU  317  CA  GLU A 135     3513   4168   4972   -281   -515   -708       C  
ATOM    318  C   GLU A 135      20.964  -3.446  29.932  1.00 29.71           C  
ANISOU  318  C   GLU A 135     3149   3636   4505   -275   -543   -697       C  
ATOM    319  O   GLU A 135      20.128  -3.425  29.022  1.00 26.77           O  
ANISOU  319  O   GLU A 135     2817   3228   4125   -305   -501   -645       O  
ATOM    320  CB  GLU A 135      23.242  -3.657  28.882  1.00 37.46           C  
ANISOU  320  CB  GLU A 135     3970   4705   5558   -410   -503   -703       C  
ATOM    321  CG  GLU A 135      23.263  -2.143  28.973  1.00 53.86           C  
ANISOU  321  CG  GLU A 135     6081   6700   7684   -498   -579   -710       C  
ATOM    322  CD  GLU A 135      24.529  -1.533  28.372  1.00 76.60           C  
ANISOU  322  CD  GLU A 135     8871   9607  10625   -643   -580   -705       C  
ATOM    323  OE1 GLU A 135      24.996  -0.496  28.901  1.00 77.81           O  
ANISOU  323  OE1 GLU A 135     9021   9708  10834   -704   -671   -739       O  
ATOM    324  OE2 GLU A 135      25.049  -2.087  27.380  1.00 80.32           O  
ANISOU  324  OE2 GLU A 135     9273  10159  11085   -700   -489   -672       O  
ATOM    325  H   GLU A 135      21.602  -5.606  28.474  1.00 33.75           H  
ATOM    326  HA  GLU A 135      22.626  -4.385  30.681  1.00 39.96           H  
ATOM    327  HB2 GLU A 135      24.125  -3.981  29.119  1.00 44.95           H  
ATOM    328  HB3 GLU A 135      23.036  -3.897  27.966  1.00 44.95           H  
ATOM    329  HG2 GLU A 135      22.500  -1.787  28.491  1.00 64.63           H  
ATOM    330  HG3 GLU A 135      23.217  -1.881  29.906  1.00 64.63           H  
ATOM    331  N   VAL A 136      20.817  -2.779  31.069  1.00 31.24           N  
ANISOU  331  N   VAL A 136     3369   3808   4691   -222   -618   -757       N  
ATOM    332  CA  VAL A 136      19.790  -1.754  31.224  1.00 31.88           C  
ANISOU  332  CA  VAL A 136     3521   3811   4779   -202   -660   -777       C  
ATOM    333  C   VAL A 136      20.256  -0.489  30.511  1.00 33.58           C  
ANISOU  333  C   VAL A 136     3753   3928   5079   -314   -718   -771       C  
ATOM    334  O   VAL A 136      21.299   0.076  30.856  1.00 33.57           O  
ANISOU  334  O   VAL A 136     3719   3913   5123   -371   -780   -814       O  
ATOM    335  CB  VAL A 136      19.503  -1.479  32.703  1.00 33.42           C  
ANISOU  335  CB  VAL A 136     3743   4030   4925    -97   -719   -863       C  
ATOM    336  CG1 VAL A 136      18.338  -0.494  32.829  1.00 30.46           C  
ANISOU  336  CG1 VAL A 136     3431   3583   4557    -47   -753   -903       C  
ATOM    337  CG2 VAL A 136      19.202  -2.782  33.439  1.00 38.40           C  
ANISOU  337  CG2 VAL A 136     4363   4766   5460    -12   -664   -843       C  
ATOM    338  H   VAL A 136      21.302  -2.900  31.770  1.00 37.48           H  
ATOM    339  HA  VAL A 136      18.970  -2.057  30.805  1.00 38.25           H  
ATOM    340  HB  VAL A 136      20.284  -1.082  33.117  1.00 40.10           H  
ATOM    341 HG11 VAL A 136      18.139  -0.360  33.769  1.00 36.55           H  
ATOM    342 HG12 VAL A 136      18.592   0.349  32.421  1.00 36.55           H  
ATOM    343 HG13 VAL A 136      17.563  -0.861  32.376  1.00 36.55           H  
ATOM    344 HG21 VAL A 136      19.038  -2.586  34.374  1.00 46.08           H  
ATOM    345 HG22 VAL A 136      18.418  -3.194  33.044  1.00 46.08           H  
ATOM    346 HG23 VAL A 136      19.965  -3.375  33.354  1.00 46.08           H  
ATOM    347  N   VAL A 137      19.478  -0.042  29.522  1.00 26.50           N  
ANISOU  347  N   VAL A 137     2883   3008   4177   -231   -227    248       N  
ATOM    348  CA  VAL A 137      19.861   1.101  28.702  1.00 28.48           C  
ANISOU  348  CA  VAL A 137     3144   3316   4362   -241   -257    289       C  
ATOM    349  C   VAL A 137      18.931   2.284  28.942  1.00 32.29           C  
ANISOU  349  C   VAL A 137     3681   3794   4794   -232   -313    311       C  
ATOM    350  O   VAL A 137      18.135   2.284  29.886  1.00 27.68           O  
ANISOU  350  O   VAL A 137     3123   3172   4223   -212   -328    300       O  
ATOM    351  CB  VAL A 137      19.878   0.716  27.209  1.00 29.43           C  
ANISOU  351  CB  VAL A 137     3223   3521   4438   -237   -220    236       C  
ATOM    352  CG1 VAL A 137      20.952  -0.344  26.956  1.00 29.05           C  
ANISOU  352  CG1 VAL A 137     3128   3479   4432   -225   -164    214       C  
ATOM    353  CG2 VAL A 137      18.499   0.217  26.748  1.00 29.47           C  
ANISOU  353  CG2 VAL A 137     3223   3552   4423   -228   -214    143       C  
ATOM    354  H   VAL A 137      18.721  -0.388  29.309  1.00 31.80           H  
ATOM    355  HA  VAL A 137      20.749   1.380  28.973  1.00 34.18           H  
ATOM    356  HB  VAL A 137      20.090   1.504  26.684  1.00 35.32           H  
ATOM    357 HG11 VAL A 137      20.977  -0.548  26.008  1.00 34.87           H  
ATOM    358 HG12 VAL A 137      21.812   0.003  27.242  1.00 34.87           H  
ATOM    359 HG13 VAL A 137      20.733  -1.142  27.461  1.00 34.87           H  
ATOM    360 HG21 VAL A 137      18.550  -0.030  25.811  1.00 35.37           H  
ATOM    361 HG22 VAL A 137      18.248  -0.554  27.280  1.00 35.37           H  
ATOM    362 HG23 VAL A 137      17.850   0.928  26.867  1.00 35.37           H  
ATOM    363  N   ASP A 138      19.050   3.310  28.107  1.00 31.65           N  
ANISOU  363  N   ASP A 138     3619   3754   4653   -239   -342    350       N  
ATOM    364  CA  ASP A 138      18.203   4.483  28.243  1.00 33.84           C  
ANISOU  364  CA  ASP A 138     3959   4017   4881   -213   -398    374       C  
ATOM    365  C   ASP A 138      16.739   4.106  28.021  1.00 32.18           C  
ANISOU  365  C   ASP A 138     3730   3854   4643   -171   -387    302       C  
ATOM    366  O   ASP A 138      16.409   3.203  27.247  1.00 23.49           O  
ANISOU  366  O   ASP A 138     2571   2816   3537   -179   -347    237       O  
ATOM    367  CB  ASP A 138      18.633   5.558  27.247  1.00 29.70           C  
ANISOU  367  CB  ASP A 138     3458   3524   4301   -230   -427    441       C  
ATOM    368  CG  ASP A 138      19.960   6.200  27.621  1.00 35.00           C  
ANISOU  368  CG  ASP A 138     4153   4143   5002   -287   -457    530       C  
ATOM    369  OD1 ASP A 138      20.494   5.862  28.700  1.00 32.11           O  
ANISOU  369  OD1 ASP A 138     3788   3720   4691   -303   -462    532       O  
ATOM    370  OD2 ASP A 138      20.465   7.029  26.832  1.00 32.45           O  
ANISOU  370  OD2 ASP A 138     3841   3844   4643   -321   -476    605       O  
ATOM    371  H   ASP A 138      19.612   3.350  27.456  1.00 37.98           H  
ATOM    372  HA  ASP A 138      18.288   4.851  29.136  1.00 40.61           H  
ATOM    373  HB2 ASP A 138      18.730   5.157  26.369  1.00 35.64           H  
ATOM    374  HB3 ASP A 138      17.958   6.254  27.221  1.00 35.64           H  
ATOM    375  N   TYR A 139      15.853   4.819  28.701  1.00 28.79           N  
ANISOU  375  N   TYR A 139     3347   3400   4190   -126   -426    309       N  
ATOM    376  CA  TYR A 139      14.440   4.481  28.660  1.00 30.03           C  
ANISOU  376  CA  TYR A 139     3469   3619   4322    -86   -416    252       C  
ATOM    377  C   TYR A 139      13.838   4.912  27.327  1.00 28.82           C  
ANISOU  377  C   TYR A 139     3297   3559   4094    -64   -430    240       C  
ATOM    378  O   TYR A 139      13.892   6.090  26.963  1.00 25.20           O  
ANISOU  378  O   TYR A 139     2895   3095   3586    -31   -473    297       O  
ATOM    379  CB  TYR A 139      13.693   5.118  29.826  1.00 31.84           C  
ANISOU  379  CB  TYR A 139     3745   3815   4537    -24   -447    265       C  
ATOM    380  CG  TYR A 139      12.211   4.781  29.801  1.00 30.94           C  
ANISOU  380  CG  TYR A 139     3572   3790   4392     18   -434    218       C  
ATOM    381  CD1 TYR A 139      11.786   3.468  29.851  1.00 32.11           C  
ANISOU  381  CD1 TYR A 139     3638   3978   4584    -29   -386    168       C  
ATOM    382  CD2 TYR A 139      11.252   5.780  29.684  1.00 31.98           C  
ANISOU  382  CD2 TYR A 139     3729   3968   4453    104   -472    228       C  
ATOM    383  CE1 TYR A 139      10.444   3.142  29.809  1.00 34.37           C  
ANISOU  383  CE1 TYR A 139     3855   4358   4846    -12   -377    132       C  
ATOM    384  CE2 TYR A 139       9.896   5.470  29.641  1.00 34.82           C  
ANISOU  384  CE2 TYR A 139     4014   4437   4780    143   -459    191       C  
ATOM    385  CZ  TYR A 139       9.501   4.143  29.706  1.00 33.55           C  
ANISOU  385  CZ  TYR A 139     3758   4324   4666     75   -412    145       C  
ATOM    386  OH  TYR A 139       8.179   3.805  29.669  1.00 39.32           O  
ANISOU  386  OH  TYR A 139     4400   5171   5370     92   -403    116       O  
ATOM    387  H   TYR A 139      16.045   5.499  29.192  1.00 34.55           H  
ATOM    388  HA  TYR A 139      14.346   3.518  28.736  1.00 36.04           H  
ATOM    389  HB2 TYR A 139      14.066   4.792  30.660  1.00 38.21           H  
ATOM    390  HB3 TYR A 139      13.787   6.083  29.776  1.00 38.21           H  
ATOM    391  HD1 TYR A 139      12.417   2.787  29.914  1.00 38.53           H  
ATOM    392  HD2 TYR A 139      11.520   6.669  29.635  1.00 38.37           H  
ATOM    393  HE1 TYR A 139      10.177   2.252  29.850  1.00 41.25           H  
ATOM    394  HE2 TYR A 139       9.261   6.146  29.569  1.00 41.79           H  
ATOM    395  HH  TYR A 139       7.708   4.497  29.598  1.00 47.19           H  
ATOM    396  N   LEU A 140      13.275   3.949  26.600  1.00 26.18           N  
ANISOU  396  N   LEU A 140     2888   3308   3753    -84   -398    169       N  
ATOM    397  CA  LEU A 140      12.534   4.202  25.376  1.00 27.06           C  
ANISOU  397  CA  LEU A 140     2965   3533   3782    -61   -414    144       C  
ATOM    398  C   LEU A 140      11.050   4.207  25.702  1.00 32.22           C  
ANISOU  398  C   LEU A 140     3579   4252   4411    -18   -431    111       C  
ATOM    399  O   LEU A 140      10.504   3.148  26.041  1.00 28.83           O  
ANISOU  399  O   LEU A 140     3087   3841   4026    -57   -404     49       O  
ATOM    400  CB  LEU A 140      12.847   3.120  24.346  1.00 28.01           C  
ANISOU  400  CB  LEU A 140     3027   3716   3901   -112   -377     70       C  
ATOM    401  CG  LEU A 140      12.015   3.099  23.063  1.00 32.79           C  
ANISOU  401  CG  LEU A 140     3582   4461   4416    -97   -394     19       C  
ATOM    402  CD1 LEU A 140      12.053   4.448  22.386  1.00 32.26           C  
ANISOU  402  CD1 LEU A 140     3555   4443   4258    -42   -432    105       C  
ATOM    403  CD2 LEU A 140      12.539   1.997  22.140  1.00 32.28           C  
ANISOU  403  CD2 LEU A 140     3477   4438   4349   -143   -358    -67       C  
ATOM    404  H   LEU A 140      13.311   3.115  26.805  1.00 31.42           H  
ATOM    405  HA  LEU A 140      12.778   5.066  25.008  1.00 32.47           H  
ATOM    406  HB2 LEU A 140      13.773   3.227  24.077  1.00 33.62           H  
ATOM    407  HB3 LEU A 140      12.723   2.259  24.774  1.00 33.62           H  
ATOM    408  HG  LEU A 140      11.086   2.909  23.269  1.00 39.35           H  
ATOM    409 HD11 LEU A 140      11.625   4.378  21.518  1.00 38.71           H  
ATOM    410 HD12 LEU A 140      11.580   5.091  22.937  1.00 38.71           H  
ATOM    411 HD13 LEU A 140      12.978   4.721  22.278  1.00 38.71           H  
ATOM    412 HD21 LEU A 140      12.017   1.995  21.323  1.00 38.73           H  
ATOM    413 HD22 LEU A 140      13.471   2.173  21.936  1.00 38.73           H  
ATOM    414 HD23 LEU A 140      12.454   1.142  22.590  1.00 38.73           H  
ATOM    415  N   PRO A 141      10.364   5.351  25.637  1.00 39.49           N  
ANISOU  415  N   PRO A 141     4531   5208   5265     63   -475    155       N  
ATOM    416  CA  PRO A 141       8.944   5.376  26.020  1.00 35.28           C  
ANISOU  416  CA  PRO A 141     3944   4757   4702    120   -486    130       C  
ATOM    417  C   PRO A 141       8.064   4.660  25.012  1.00 35.23           C  
ANISOU  417  C   PRO A 141     3834   4896   4656     91   -485     61       C  
ATOM    418  O   PRO A 141       8.329   4.653  23.807  1.00 35.03           O  
ANISOU  418  O   PRO A 141     3797   4931   4580     73   -495     46       O  
ATOM    419  CB  PRO A 141       8.604   6.876  26.072  1.00 41.60           C  
ANISOU  419  CB  PRO A 141     4820   5548   5437    233   -537    198       C  
ATOM    420  CG  PRO A 141       9.931   7.594  26.133  1.00 40.34           C  
ANISOU  420  CG  PRO A 141     4770   5257   5302    214   -552    264       C  
ATOM    421  CD  PRO A 141      10.893   6.707  25.375  1.00 36.88           C  
ANISOU  421  CD  PRO A 141     4292   4828   4892    112   -516    240       C  
ATOM    422  HA  PRO A 141       8.830   4.978  26.896  1.00 42.33           H  
ATOM    423  HB2 PRO A 141       8.112   7.129  25.275  1.00 49.92           H  
ATOM    424  HB3 PRO A 141       8.074   7.065  26.862  1.00 49.92           H  
ATOM    425  HG2 PRO A 141       9.856   8.464  25.710  1.00 48.41           H  
ATOM    426  HG3 PRO A 141      10.209   7.696  27.056  1.00 48.41           H  
ATOM    427  HD2 PRO A 141      10.877   6.909  24.426  1.00 44.25           H  
ATOM    428  HD3 PRO A 141      11.795   6.800  25.719  1.00 44.25           H  
ATOM    429  N   SER A 142       6.988   4.067  25.525  1.00 40.77           N  
ANISOU  429  N   SER A 142     4452   5665   5372     83   -476     22       N  
ATOM    430  CA  SER A 142       6.037   3.322  24.709  1.00 35.71           C  
ANISOU  430  CA  SER A 142     3700   5166   4702     37   -485    -50       C  
ATOM    431  C   SER A 142       4.619   3.670  25.132  1.00 37.10           C  
ANISOU  431  C   SER A 142     3796   5465   4834    104   -504    -36       C  
ATOM    432  O   SER A 142       4.322   3.770  26.325  1.00 35.82           O  
ANISOU  432  O   SER A 142     3635   5269   4704    138   -483     -2       O  
ATOM    433  CB  SER A 142       6.258   1.815  24.840  1.00 37.34           C  
ANISOU  433  CB  SER A 142     3861   5328   4999    -90   -447   -126       C  
ATOM    434  OG  SER A 142       5.167   1.071  24.315  1.00 39.47           O  
ANISOU  434  OG  SER A 142     4019   5723   5253   -149   -464   -198       O  
ATOM    435  H   SER A 142       6.784   4.083  26.360  1.00 48.92           H  
ATOM    436  HA  SER A 142       6.145   3.573  23.779  1.00 42.85           H  
ATOM    437  HB2 SER A 142       7.062   1.575  24.354  1.00 44.81           H  
ATOM    438  HB3 SER A 142       6.360   1.596  25.780  1.00 44.81           H  
ATOM    439  HG  SER A 142       5.292   0.250  24.441  1.00 47.36           H  
ATOM    440  N   SER A 143       3.738   3.829  24.150  1.00 32.25           N  
ANISOU  440  N   SER A 143     3105   5010   4138    128   -543    -61       N  
ATOM    441  CA  SER A 143       2.328   4.023  24.454  1.00 38.44           C  
ANISOU  441  CA  SER A 143     3782   5946   4877    186   -560    -52       C  
ATOM    442  C   SER A 143       1.688   2.788  25.087  1.00 34.58           C  
ANISOU  442  C   SER A 143     3181   5494   4461     72   -530    -97       C  
ATOM    443  O   SER A 143       0.515   2.851  25.448  1.00 32.28           O  
ANISOU  443  O   SER A 143     2781   5344   4140    107   -536    -81       O  
ATOM    444  CB  SER A 143       1.567   4.395  23.176  1.00 37.20           C  
ANISOU  444  CB  SER A 143     3555   5970   4612    230   -615    -69       C  
ATOM    445  OG  SER A 143       1.621   3.328  22.228  1.00 36.72           O  
ANISOU  445  OG  SER A 143     3432   5963   4558    100   -626   -162       O  
ATOM    446  H   SER A 143       3.931   3.828  23.312  1.00 38.70           H  
ATOM    447  HA  SER A 143       2.244   4.759  25.080  1.00 46.13           H  
ATOM    448  HB2 SER A 143       0.640   4.572  23.400  1.00 44.65           H  
ATOM    449  HB3 SER A 143       1.972   5.185  22.786  1.00 44.65           H  
ATOM    450  HG  SER A 143       1.208   3.544  21.529  1.00 44.07           H  
ATOM    451  N   SER A 144       2.424   1.683  25.229  1.00 33.49           N  
ANISOU  451  N   SER A 144     3067   5238   4421    -58   -496   -144       N  
ATOM    452  CA  SER A 144       1.875   0.432  25.730  1.00 38.90           C  
ANISOU  452  CA  SER A 144     3659   5935   5188   -186   -471   -182       C  
ATOM    453  C   SER A 144       2.160   0.204  27.209  1.00 34.12           C  
ANISOU  453  C   SER A 144     3086   5217   4660   -189   -416   -120       C  
ATOM    454  O   SER A 144       1.911  -0.893  27.712  1.00 34.64           O  
ANISOU  454  O   SER A 144     3095   5257   4810   -304   -387   -132       O  
ATOM    455  CB  SER A 144       2.425  -0.749  24.921  1.00 42.69           C  
ANISOU  455  CB  SER A 144     4148   6347   5727   -325   -474   -279       C  
ATOM    456  OG  SER A 144       2.091  -0.633  23.545  1.00 44.59           O  
ANISOU  456  OG  SER A 144     4348   6712   5881   -327   -528   -347       O  
ATOM    457  H   SER A 144       3.261   1.638  25.036  1.00 40.19           H  
ATOM    458  HA  SER A 144       0.912   0.463  25.614  1.00 46.68           H  
ATOM    459  HB2 SER A 144       3.391  -0.767  25.009  1.00 51.23           H  
ATOM    460  HB3 SER A 144       2.045  -1.571  25.268  1.00 51.23           H  
ATOM    461  HG  SER A 144       2.424  -1.271  23.114  1.00 53.50           H  
ATOM    462  N   VAL A 145       2.647   1.213  27.917  1.00 28.71           N  
ANISOU  462  N   VAL A 145     2493   4469   3948    -68   -405    -53       N  
ATOM    463  CA  VAL A 145       2.958   1.116  29.334  1.00 29.30           C  
ANISOU  463  CA  VAL A 145     2607   4452   4074    -52   -359      4       C  
ATOM    464  C   VAL A 145       1.896   1.877  30.119  1.00 33.30           C  
ANISOU  464  C   VAL A 145     3056   5088   4509     68   -356     58       C  
ATOM    465  O   VAL A 145       1.644   3.058  29.856  1.00 32.11           O  
ANISOU  465  O   VAL A 145     2939   4990   4270    204   -390     75       O  
ATOM    466  CB  VAL A 145       4.365   1.673  29.629  1.00 32.24           C  
ANISOU  466  CB  VAL A 145     3130   4656   4464     -6   -357     30       C  
ATOM    467  CG1 VAL A 145       4.667   1.590  31.107  1.00 37.59           C  
ANISOU  467  CG1 VAL A 145     3845   5256   5180     15   -318     85       C  
ATOM    468  CG2 VAL A 145       5.420   0.902  28.823  1.00 37.09           C  
ANISOU  468  CG2 VAL A 145     3786   5167   5140   -109   -353    -21       C  
ATOM    469  H   VAL A 145       2.812   1.989  27.586  1.00 34.45           H  
ATOM    470  HA  VAL A 145       2.926   0.186  29.607  1.00 35.16           H  
ATOM    471  HB  VAL A 145       4.396   2.606  29.365  1.00 38.69           H  
ATOM    472 HG11 VAL A 145       5.519   2.020  31.279  1.00 45.10           H  
ATOM    473 HG12 VAL A 145       3.963   2.042  31.599  1.00 45.10           H  
ATOM    474 HG13 VAL A 145       4.708   0.657  31.369  1.00 45.10           H  
ATOM    475 HG21 VAL A 145       6.302   1.222  29.070  1.00 44.51           H  
ATOM    476 HG22 VAL A 145       5.343  -0.044  29.027  1.00 44.51           H  
ATOM    477 HG23 VAL A 145       5.266   1.050  27.877  1.00 44.51           H  
ATOM    478  N   ALA A 146       1.300   1.211  31.102  1.00 35.00           N  
ANISOU  478  N   ALA A 146     3188   5351   4760     24   -311     92       N  
ATOM    479  CA  ALA A 146       0.362   1.883  31.987  1.00 37.28           C  
ANISOU  479  CA  ALA A 146     3419   5771   4974    151   -294    146       C  
ATOM    480  C   ALA A 146       1.106   2.850  32.915  1.00 35.83           C  
ANISOU  480  C   ALA A 146     3380   5477   4757    286   -289    181       C  
ATOM    481  O   ALA A 146       2.267   2.624  33.258  1.00 34.07           O  
ANISOU  481  O   ALA A 146     3264   5087   4594    240   -279    183       O  
ATOM    482  CB  ALA A 146      -0.425   0.871  32.818  1.00 35.55           C  
ANISOU  482  CB  ALA A 146     3066   5643   4798     58   -240    187       C  
ATOM    483  H   ALA A 146       1.421   0.377  31.276  1.00 42.00           H  
ATOM    484  HA  ALA A 146      -0.272   2.391  31.457  1.00 44.73           H  
ATOM    485  HB1 ALA A 146      -1.041   1.347  33.396  1.00 42.66           H  
ATOM    486  HB2 ALA A 146      -0.916   0.285  32.221  1.00 42.66           H  
ATOM    487  HB3 ALA A 146       0.196   0.351  33.353  1.00 42.66           H  
ATOM    488  N   PRO A 147       0.457   3.938  33.327  1.00 35.17           N  
ANISOU  488  N   PRO A 147     3301   5487   4575    459   -299    204       N  
ATOM    489  CA  PRO A 147       1.090   4.852  34.288  1.00 34.90           C  
ANISOU  489  CA  PRO A 147     3409   5345   4505    588   -302    224       C  
ATOM    490  C   PRO A 147       1.670   4.163  35.505  1.00 34.72           C  
ANISOU  490  C   PRO A 147     3413   5244   4534    528   -253    254       C  
ATOM    491  O   PRO A 147       2.676   4.634  36.042  1.00 31.03           O  
ANISOU  491  O   PRO A 147     3085   4632   4073    565   -268    254       O  
ATOM    492  CB  PRO A 147      -0.066   5.787  34.694  1.00 37.52           C  
ANISOU  492  CB  PRO A 147     3695   5838   4724    779   -303    240       C  
ATOM    493  CG  PRO A 147      -0.974   5.809  33.518  1.00 32.73           C  
ANISOU  493  CG  PRO A 147     2970   5380   4085    777   -331    226       C  
ATOM    494  CD  PRO A 147      -0.824   4.467  32.804  1.00 33.71           C  
ANISOU  494  CD  PRO A 147     3004   5503   4303    557   -321    205       C  
ATOM    495  HA  PRO A 147       1.786   5.355  33.838  1.00 41.88           H  
ATOM    496  HB2 PRO A 147      -0.519   5.432  35.475  1.00 45.03           H  
ATOM    497  HB3 PRO A 147       0.278   6.674  34.884  1.00 45.03           H  
ATOM    498  HG2 PRO A 147      -1.888   5.931  33.820  1.00 39.27           H  
ATOM    499  HG3 PRO A 147      -0.720   6.536  32.929  1.00 39.27           H  
ATOM    500  HD2 PRO A 147      -1.558   3.874  33.027  1.00 40.46           H  
ATOM    501  HD3 PRO A 147      -0.778   4.592  31.843  1.00 40.46           H  
ATOM    502  N   ASP A 148       1.065   3.076  35.985  1.00 36.51           N  
ANISOU  502  N   ASP A 148     3509   5566   4798    433   -196    287       N  
ATOM    503  CA  ASP A 148       1.508   2.436  37.217  1.00 36.58           C  
ANISOU  503  CA  ASP A 148     3535   5521   4843    392   -145    335       C  
ATOM    504  C   ASP A 148       2.347   1.188  36.970  1.00 34.09           C  
ANISOU  504  C   ASP A 148     3229   5070   4655    207   -129    336       C  
ATOM    505  O   ASP A 148       2.630   0.448  37.915  1.00 35.13           O  
ANISOU  505  O   ASP A 148     3355   5164   4828    154    -84    390       O  
ATOM    506  CB  ASP A 148       0.311   2.082  38.101  1.00 32.45           C  
ANISOU  506  CB  ASP A 148     2867   5192   4272    420    -84    396       C  
ATOM    507  CG  ASP A 148      -0.622   1.065  37.452  1.00 42.18           C  
ANISOU  507  CG  ASP A 148     3924   6545   5557    273    -65    409       C  
ATOM    508  OD1 ASP A 148      -0.273   0.483  36.404  1.00 40.90           O  
ANISOU  508  OD1 ASP A 148     3764   6298   5477    140    -96    363       O  
ATOM    509  OD2 ASP A 148      -1.726   0.858  37.999  1.00 39.49           O  
ANISOU  509  OD2 ASP A 148     3438   6395   5171    291    -20    465       O  
ATOM    510  H   ASP A 148       0.394   2.691  35.611  1.00 43.81           H  
ATOM    511  HA  ASP A 148       2.056   3.074  37.700  1.00 43.90           H  
ATOM    512  HB2 ASP A 148       0.633   1.704  38.933  1.00 38.95           H  
ATOM    513  HB3 ASP A 148      -0.200   2.887  38.278  1.00 38.95           H  
ATOM    514  N   LEU A 149       2.737   0.928  35.727  1.00 29.46           N  
ANISOU  514  N   LEU A 149     2656   4414   4122    121   -165    281       N  
ATOM    515  CA  LEU A 149       3.689  -0.133  35.419  1.00 34.86           C  
ANISOU  515  CA  LEU A 149     3376   4950   4920    -23   -155    267       C  
ATOM    516  C   LEU A 149       5.097   0.457  35.416  1.00 33.04           C  
ANISOU  516  C   LEU A 149     3296   4563   4696     22   -185    253       C  
ATOM    517  O   LEU A 149       5.358   1.437  34.716  1.00 29.42           O  
ANISOU  517  O   LEU A 149     2899   4090   4188     91   -232    220       O  
ATOM    518  CB  LEU A 149       3.371  -0.766  34.070  1.00 33.80           C  
ANISOU  518  CB  LEU A 149     3175   4837   4829   -134   -178    203       C  
ATOM    519  CG  LEU A 149       4.327  -1.865  33.603  1.00 37.07           C  
ANISOU  519  CG  LEU A 149     3633   5096   5355   -265   -171    168       C  
ATOM    520  CD1 LEU A 149       4.226  -3.090  34.506  1.00 38.89           C  
ANISOU  520  CD1 LEU A 149     3822   5280   5676   -367   -118    222       C  
ATOM    521  CD2 LEU A 149       4.053  -2.255  32.156  1.00 34.44           C  
ANISOU  521  CD2 LEU A 149     3257   4794   5036   -345   -206     81       C  
ATOM    522  H   LEU A 149       2.460   1.358  35.036  1.00 35.35           H  
ATOM    523  HA  LEU A 149       3.642  -0.831  36.091  1.00 41.84           H  
ATOM    524  HB2 LEU A 149       2.486  -1.158  34.121  1.00 40.56           H  
ATOM    525  HB3 LEU A 149       3.386  -0.067  33.397  1.00 40.56           H  
ATOM    526  HG  LEU A 149       5.232  -1.521  33.654  1.00 44.48           H  
ATOM    527 HD11 LEU A 149       4.869  -3.753  34.210  1.00 46.67           H  
ATOM    528 HD12 LEU A 149       4.420  -2.826  35.419  1.00 46.67           H  
ATOM    529 HD13 LEU A 149       3.328  -3.451  34.449  1.00 46.67           H  
ATOM    530 HD21 LEU A 149       4.724  -2.894  31.868  1.00 41.33           H  
ATOM    531 HD22 LEU A 149       3.170  -2.653  32.098  1.00 41.33           H  
ATOM    532 HD23 LEU A 149       4.094  -1.460  31.601  1.00 41.33           H  
ATOM    533  N   PHE A 150       5.988  -0.117  36.216  1.00 33.85           N  
ANISOU  533  N   PHE A 150     3449   4554   4857    -18   -158    289       N  
ATOM    534  CA  PHE A 150       7.392   0.294  36.184  1.00 30.04           C  
ANISOU  534  CA  PHE A 150     3089   3933   4393      1   -187    281       C  
ATOM    535  C   PHE A 150       8.005  -0.305  34.924  1.00 28.45           C  
ANISOU  535  C   PHE A 150     2890   3660   4260    -93   -198    229       C  
ATOM    536  O   PHE A 150       8.259  -1.508  34.857  1.00 30.92           O  
ANISOU  536  O   PHE A 150     3174   3915   4661   -190   -165    226       O  
ATOM    537  CB  PHE A 150       8.146  -0.148  37.425  1.00 31.36           C  
ANISOU  537  CB  PHE A 150     3298   4024   4592     -4   -160    338       C  
ATOM    538  CG  PHE A 150       9.614   0.191  37.375  1.00 36.06           C  
ANISOU  538  CG  PHE A 150     3996   4493   5211      1   -194    334       C  
ATOM    539  CD1 PHE A 150      10.039   1.507  37.414  1.00 33.98           C  
ANISOU  539  CD1 PHE A 150     3822   4210   4881     85   -249    320       C  
ATOM    540  CD2 PHE A 150      10.569  -0.809  37.269  1.00 34.39           C  
ANISOU  540  CD2 PHE A 150     3792   4182   5092    -80   -173    345       C  
ATOM    541  CE1 PHE A 150      11.397   1.814  37.361  1.00 39.53           C  
ANISOU  541  CE1 PHE A 150     4604   4807   5609     69   -283    325       C  
ATOM    542  CE2 PHE A 150      11.907  -0.509  37.217  1.00 35.55           C  
ANISOU  542  CE2 PHE A 150     4012   4240   5257    -75   -202    348       C  
ATOM    543  CZ  PHE A 150      12.326   0.807  37.260  1.00 34.99           C  
ANISOU  543  CZ  PHE A 150     4015   4161   5119    -10   -258    341       C  
ATOM    544  H   PHE A 150       5.808  -0.740  36.782  1.00 40.62           H  
ATOM    545  HA  PHE A 150       7.441   1.262  36.151  1.00 36.05           H  
ATOM    546  HB2 PHE A 150       7.764   0.292  38.199  1.00 37.63           H  
ATOM    547  HB3 PHE A 150       8.065  -1.111  37.516  1.00 37.63           H  
ATOM    548  HD1 PHE A 150       9.414   2.192  37.476  1.00 40.78           H  
ATOM    549  HD2 PHE A 150      10.298  -1.698  37.233  1.00 41.26           H  
ATOM    550  HE1 PHE A 150      11.674   2.701  37.394  1.00 47.44           H  
ATOM    551  HE2 PHE A 150      12.533  -1.193  37.153  1.00 42.67           H  
ATOM    552  HZ  PHE A 150      13.233   1.010  37.221  1.00 41.99           H  
ATOM    553  N   ALA A 151       8.208   0.528  33.912  1.00 26.08           N  
ANISOU  553  N   ALA A 151     2627   3367   3917    -58   -241    189       N  
ATOM    554  CA  ALA A 151       8.784   0.110  32.647  1.00 31.99           C  
ANISOU  554  CA  ALA A 151     3378   4074   4702   -126   -251    137       C  
ATOM    555  C   ALA A 151      10.281   0.388  32.629  1.00 31.26           C  
ANISOU  555  C   ALA A 151     3376   3868   4633   -121   -263    153       C  
ATOM    556  O   ALA A 151      10.790   1.248  33.345  1.00 27.95           O  
ANISOU  556  O   ALA A 151     3026   3410   4184    -61   -286    195       O  
ATOM    557  CB  ALA A 151       8.109   0.838  31.478  1.00 29.69           C  
ANISOU  557  CB  ALA A 151     3062   3882   4336    -90   -289     98       C  
ATOM    558  H   ALA A 151       8.013   1.365  33.937  1.00 31.30           H  
ATOM    559  HA  ALA A 151       8.647  -0.843  32.532  1.00 38.39           H  
ATOM    560  HB1 ALA A 151       8.562   0.601  30.654  1.00 35.63           H  
ATOM    561  HB2 ALA A 151       7.178   0.568  31.433  1.00 35.63           H  
ATOM    562  HB3 ALA A 151       8.169   1.795  31.625  1.00 35.63           H  
ATOM    563  N   LEU A 152      10.985  -0.365  31.797  1.00 30.64           N  
ANISOU  563  N   LEU A 152     3292   3742   4606   -186   -249    115       N  
ATOM    564  CA  LEU A 152      12.410  -0.134  31.588  1.00 32.67           C  
ANISOU  564  CA  LEU A 152     3611   3922   4882   -184   -256    132       C  
ATOM    565  C   LEU A 152      12.779  -0.750  30.252  1.00 34.75           C  
ANISOU  565  C   LEU A 152     3851   4193   5161   -230   -244     69       C  
ATOM    566  O   LEU A 152      12.043  -1.585  29.707  1.00 29.08           O  
ANISOU  566  O   LEU A 152     3079   3508   4460   -276   -230      6       O  
ATOM    567  CB  LEU A 152      13.247  -0.703  32.719  1.00 29.47           C  
ANISOU  567  CB  LEU A 152     3230   3428   4541   -194   -232    180       C  
ATOM    568  CG  LEU A 152      13.379  -2.201  32.844  1.00 33.63           C  
ANISOU  568  CG  LEU A 152     3721   3897   5158   -254   -184    163       C  
ATOM    569  CD1 LEU A 152      14.248  -2.559  34.042  1.00 40.52           C  
ANISOU  569  CD1 LEU A 152     4623   4693   6078   -242   -168    230       C  
ATOM    570  CD2 LEU A 152      12.029  -2.885  32.955  1.00 45.30           C  
ANISOU  570  CD2 LEU A 152     5138   5419   6654   -296   -164    140       C  
ATOM    571  H   LEU A 152      10.662  -1.018  31.340  1.00 36.76           H  
ATOM    572  HA  LEU A 152      12.595   0.818  31.552  1.00 39.21           H  
ATOM    573  HB2 LEU A 152      14.147  -0.355  32.618  1.00 35.37           H  
ATOM    574  HB3 LEU A 152      12.862  -0.390  33.552  1.00 35.37           H  
ATOM    575  HG  LEU A 152      13.804  -2.531  32.036  1.00 40.35           H  
ATOM    576 HD11 LEU A 152      14.318  -3.525  34.104  1.00 48.62           H  
ATOM    577 HD12 LEU A 152      15.128  -2.170  33.922  1.00 48.62           H  
ATOM    578 HD13 LEU A 152      13.837  -2.205  34.847  1.00 48.62           H  
ATOM    579 HD21 LEU A 152      12.163  -3.808  33.221  1.00 54.36           H  
ATOM    580 HD22 LEU A 152      11.495  -2.423  33.620  1.00 54.36           H  
ATOM    581 HD23 LEU A 152      11.586  -2.851  32.093  1.00 54.36           H  
ATOM    582  N   THR A 153      13.910  -0.304  29.715  1.00 27.37           N  
ANISOU  582  N   THR A 153     2952   3235   4210   -219   -254     85       N  
ATOM    583  CA  THR A 153      14.412  -0.773  28.432  1.00 29.84           C  
ANISOU  583  CA  THR A 153     3246   3574   4518   -243   -238     29       C  
ATOM    584  C   THR A 153      15.657  -1.622  28.651  1.00 29.39           C  
ANISOU  584  C   THR A 153     3197   3438   4533   -256   -200     34       C  
ATOM    585  O   THR A 153      16.614  -1.183  29.296  1.00 28.43           O  
ANISOU  585  O   THR A 153     3103   3274   4424   -240   -206    104       O  
ATOM    586  CB  THR A 153      14.721   0.406  27.514  1.00 26.12           C  
ANISOU  586  CB  THR A 153     2796   3166   3961   -213   -270     56       C  
ATOM    587  OG1 THR A 153      13.647   1.332  27.584  1.00 25.12           O  
ANISOU  587  OG1 THR A 153     2677   3094   3773   -177   -310     73       O  
ATOM    588  CG2 THR A 153      14.903  -0.047  26.071  1.00 28.21           C  
ANISOU  588  CG2 THR A 153     3028   3501   4188   -227   -254    -11       C  
ATOM    589  H   THR A 153      14.415   0.285  30.086  1.00 32.84           H  
ATOM    590  HA  THR A 153      13.745  -1.330  28.001  1.00 35.81           H  
ATOM    591  HB  THR A 153      15.549   0.827  27.795  1.00 31.34           H  
ATOM    592  HG1 THR A 153      12.932   0.961  27.347  1.00 30.14           H  
ATOM    593 HG21 THR A 153      15.075   0.720  25.502  1.00 33.85           H  
ATOM    594 HG22 THR A 153      15.651  -0.660  26.007  1.00 33.85           H  
ATOM    595 HG23 THR A 153      14.101  -0.496  25.760  1.00 33.85           H  
ATOM    596  N   LEU A 154      15.638  -2.834  28.119  1.00 30.17           N  
ANISOU  596  N   LEU A 154     3272   3515   4676   -284   -167    -43       N  
ATOM    597  CA  LEU A 154      16.768  -3.745  28.206  1.00 31.17           C  
ANISOU  597  CA  LEU A 154     3406   3569   4870   -276   -128    -50       C  
ATOM    598  C   LEU A 154      17.352  -3.971  26.816  1.00 31.68           C  
ANISOU  598  C   LEU A 154     3456   3688   4891   -260   -110   -119       C  
ATOM    599  O   LEU A 154      16.634  -3.967  25.807  1.00 29.42           O  
ANISOU  599  O   LEU A 154     3155   3475   4548   -273   -123   -195       O  
ATOM    600  CB  LEU A 154      16.354  -5.099  28.811  1.00 33.97           C  
ANISOU  600  CB  LEU A 154     3760   3825   5322   -309    -99    -84       C  
ATOM    601  CG  LEU A 154      15.721  -5.060  30.203  1.00 33.99           C  
ANISOU  601  CG  LEU A 154     3765   3788   5362   -325   -105    -11       C  
ATOM    602  CD1 LEU A 154      15.339  -6.446  30.651  1.00 33.94           C  
ANISOU  602  CD1 LEU A 154     3757   3685   5455   -370    -74    -33       C  
ATOM    603  CD2 LEU A 154      16.674  -4.405  31.199  1.00 36.88           C  
ANISOU  603  CD2 LEU A 154     4156   4134   5725   -282   -112     89       C  
ATOM    604  H   LEU A 154      14.966  -3.159  27.693  1.00 36.20           H  
ATOM    605  HA  LEU A 154      17.451  -3.357  28.776  1.00 37.41           H  
ATOM    606  HB2 LEU A 154      15.708  -5.509  28.216  1.00 40.77           H  
ATOM    607  HB3 LEU A 154      17.147  -5.655  28.874  1.00 40.77           H  
ATOM    608  HG  LEU A 154      14.911  -4.529  30.172  1.00 40.79           H  
ATOM    609 HD11 LEU A 154      14.941  -6.394  31.534  1.00 40.73           H  
ATOM    610 HD12 LEU A 154      14.701  -6.816  30.021  1.00 40.73           H  
ATOM    611 HD13 LEU A 154      16.135  -6.999  30.679  1.00 40.73           H  
ATOM    612 HD21 LEU A 154      16.311  -4.502  32.093  1.00 44.26           H  
ATOM    613 HD22 LEU A 154      17.538  -4.841  31.143  1.00 44.26           H  
ATOM    614 HD23 LEU A 154      16.763  -3.464  30.978  1.00 44.26           H  
ATOM    615  N   LEU A 155      18.663  -4.172  26.774  1.00 30.66           N  
ANISOU  615  N   LEU A 155     3327   3541   4781   -225    -81    -90       N  
ATOM    616  CA  LEU A 155      19.376  -4.575  25.559  1.00 30.36           C  
ANISOU  616  CA  LEU A 155     3272   3560   4705   -191    -49   -155       C  
ATOM    617  C   LEU A 155      20.040  -5.914  25.846  1.00 30.52           C  
ANISOU  617  C   LEU A 155     3301   3480   4814   -158     -4   -198       C  
ATOM    618  O   LEU A 155      21.020  -5.979  26.600  1.00 29.69           O  
ANISOU  618  O   LEU A 155     3190   3335   4756   -126     13   -120       O  
ATOM    619  CB  LEU A 155      20.398  -3.521  25.152  1.00 36.21           C  
ANISOU  619  CB  LEU A 155     3989   4393   5375   -167    -50    -70       C  
ATOM    620  CG  LEU A 155      21.257  -3.808  23.920  1.00 35.59           C  
ANISOU  620  CG  LEU A 155     3878   4409   5237   -121     -8   -114       C  
ATOM    621  CD1 LEU A 155      20.451  -4.037  22.664  1.00 35.49           C  
ANISOU  621  CD1 LEU A 155     3864   4474   5145   -119    -10   -228       C  
ATOM    622  CD2 LEU A 155      22.218  -2.641  23.729  1.00 38.87           C  
ANISOU  622  CD2 LEU A 155     4261   4916   5593   -122    -13      7       C  
ATOM    623  H   LEU A 155      19.180  -4.080  27.455  1.00 36.79           H  
ATOM    624  HA  LEU A 155      18.753  -4.684  24.824  1.00 36.44           H  
ATOM    625  HB2 LEU A 155      19.918  -2.696  24.974  1.00 43.45           H  
ATOM    626  HB3 LEU A 155      21.007  -3.396  25.897  1.00 43.45           H  
ATOM    627  HG  LEU A 155      21.742  -4.635  24.067  1.00 42.71           H  
ATOM    628 HD11 LEU A 155      21.057  -4.201  21.925  1.00 42.58           H  
ATOM    629 HD12 LEU A 155      19.874  -4.806  22.795  1.00 42.58           H  
ATOM    630 HD13 LEU A 155      19.915  -3.249  22.484  1.00 42.58           H  
ATOM    631 HD21 LEU A 155      22.770  -2.811  22.950  1.00 46.65           H  
ATOM    632 HD22 LEU A 155      21.705  -1.828  23.601  1.00 46.65           H  
ATOM    633 HD23 LEU A 155      22.776  -2.559  24.519  1.00 46.65           H  
ATOM    634  N   ARG A 156      19.490  -6.982  25.276  1.00 27.60           N  
ANISOU  634  N   ARG A 156     2949   3067   4472   -165      9   -321       N  
ATOM    635  CA  ARG A 156      20.100  -8.295  25.423  1.00 30.73           C  
ANISOU  635  CA  ARG A 156     3371   3350   4955   -122     50   -373       C  
ATOM    636  C   ARG A 156      21.492  -8.289  24.792  1.00 32.95           C  
ANISOU  636  C   ARG A 156     3626   3702   5193    -30     92   -369       C  
ATOM    637  O   ARG A 156      21.682  -7.786  23.680  1.00 31.45           O  
ANISOU  637  O   ARG A 156     3408   3643   4897     -9     97   -405       O  
ATOM    638  CB  ARG A 156      19.218  -9.357  24.777  1.00 29.10           C  
ANISOU  638  CB  ARG A 156     3200   3080   4779   -156     44   -522       C  
ATOM    639  CG  ARG A 156      19.785 -10.766  24.888  1.00 37.55           C  
ANISOU  639  CG  ARG A 156     4318   4001   5947   -106     80   -588       C  
ATOM    640  CD  ARG A 156      18.834 -11.787  24.276  1.00 36.37           C  
ANISOU  640  CD  ARG A 156     4215   3767   5835   -162     60   -743       C  
ATOM    641  NE  ARG A 156      19.374 -13.136  24.369  1.00 36.18           N  
ANISOU  641  NE  ARG A 156     4258   3576   5914   -108     91   -810       N  
ATOM    642  CZ  ARG A 156      18.799 -14.209  23.849  1.00 40.66           C  
ANISOU  642  CZ  ARG A 156     4888   4027   6533   -145     74   -957       C  
ATOM    643  NH1 ARG A 156      17.644 -14.132  23.201  1.00 34.48           N  
ANISOU  643  NH1 ARG A 156     4098   3295   5709   -245     24  -1054       N  
ATOM    644  NH2 ARG A 156      19.399 -15.384  23.974  1.00 39.24           N  
ANISOU  644  NH2 ARG A 156     4783   3678   6450    -79    102  -1010       N  
ATOM    645  H   ARG A 156      18.771  -6.973  24.804  1.00 33.12           H  
ATOM    646  HA  ARG A 156      20.189  -8.516  26.363  1.00 36.88           H  
ATOM    647  HB2 ARG A 156      18.352  -9.351  25.213  1.00 34.92           H  
ATOM    648  HB3 ARG A 156      19.118  -9.150  23.835  1.00 34.92           H  
ATOM    649  HG2 ARG A 156      20.631 -10.813  24.414  1.00 45.06           H  
ATOM    650  HG3 ARG A 156      19.916 -10.990  25.822  1.00 45.06           H  
ATOM    651  HD2 ARG A 156      17.988 -11.763  24.750  1.00 43.64           H  
ATOM    652  HD3 ARG A 156      18.696 -11.577  23.339  1.00 43.64           H  
ATOM    653  HE  ARG A 156      20.117 -13.243  24.790  1.00 43.42           H  
ATOM    654 HH11 ARG A 156      17.252 -13.372  23.111  1.00 41.38           H  
ATOM    655 HH12 ARG A 156      17.288 -14.842  22.871  1.00 41.38           H  
ATOM    656 HH21 ARG A 156      20.151 -15.442  24.388  1.00 47.09           H  
ATOM    657 HH22 ARG A 156      19.037 -16.090  23.641  1.00 47.09           H  
ATOM    658  N   ILE A 157      22.465  -8.843  25.510  1.00 32.01           N  
ANISOU  658  N   ILE A 157     3507   3508   5147     28    123   -315       N  
ATOM    659  CA  ILE A 157      23.842  -8.857  25.048  1.00 32.75           C  
ANISOU  659  CA  ILE A 157     3557   3683   5204    122    167   -293       C  
ATOM    660  C   ILE A 157      24.301 -10.301  24.910  1.00 38.26           C  
ANISOU  660  C   ILE A 157     4292   4273   5973    213    212   -385       C  
ATOM    661  O   ILE A 157      23.682 -11.233  25.432  1.00 31.75           O  
ANISOU  661  O   ILE A 157     3531   3285   5247    190    204   -431       O  
ATOM    662  CB  ILE A 157      24.785  -8.073  25.984  1.00 38.70           C  
ANISOU  662  CB  ILE A 157     4260   4479   5966    126    160   -133       C  
ATOM    663  CG1 ILE A 157      24.820  -8.693  27.377  1.00 36.13           C  
ANISOU  663  CG1 ILE A 157     3963   4011   5752    129    154    -72       C  
ATOM    664  CG2 ILE A 157      24.335  -6.609  26.081  1.00 30.64           C  
ANISOU  664  CG2 ILE A 157     3222   3543   4876     41    109    -53       C  
ATOM    665  CD1 ILE A 157      25.951  -8.137  28.264  1.00 36.20           C  
ANISOU  665  CD1 ILE A 157     3917   4068   5768    152    146     69       C  
ATOM    666  H   ILE A 157      22.348  -9.219  26.275  1.00 38.41           H  
ATOM    667  HA  ILE A 157      23.880  -8.445  24.170  1.00 39.30           H  
ATOM    668  HB  ILE A 157      25.678  -8.115  25.607  1.00 46.44           H  
ATOM    669 HG12 ILE A 157      23.977  -8.514  27.821  1.00 43.35           H  
ATOM    670 HG13 ILE A 157      24.952  -9.651  27.291  1.00 43.35           H  
ATOM    671 HG21 ILE A 157      24.987  -6.112  26.598  1.00 36.77           H  
ATOM    672 HG22 ILE A 157      24.270  -6.239  25.187  1.00 36.77           H  
ATOM    673 HG23 ILE A 157      23.469  -6.574  26.517  1.00 36.77           H  
ATOM    674 HD11 ILE A 157      25.954  -8.615  29.108  1.00 43.44           H  
ATOM    675 HD12 ILE A 157      26.799  -8.263  27.810  1.00 43.44           H  
ATOM    676 HD13 ILE A 157      25.795  -7.193  28.419  1.00 43.44           H  
ATOM    677  N   ASN A 158      25.413 -10.475  24.193  1.00 38.54           N  
ANISOU  677  N   ASN A 158     4286   4400   5956    320    260   -406       N  
ATOM    678  CA  ASN A 158      26.005 -11.794  23.988  1.00 41.76           C  
ANISOU  678  CA  ASN A 158     4730   4716   6420    439    308   -496       C  
ATOM    679  C   ASN A 158      25.031 -12.757  23.318  1.00 42.18           C  
ANISOU  679  C   ASN A 158     4876   4653   6498    424    297   -677       C  
ATOM    680  O   ASN A 158      25.046 -13.959  23.584  1.00 41.20           O  
ANISOU  680  O   ASN A 158     4825   4355   6474    474    310   -745       O  
ATOM    681  CB  ASN A 158      26.511 -12.358  25.319  1.00 35.21           C  
ANISOU  681  CB  ASN A 158     3913   3752   5712    475    313   -396       C  
ATOM    682  CG  ASN A 158      27.646 -11.521  25.903  1.00 39.76           C  
ANISOU  682  CG  ASN A 158     4391   4456   6259    503    320   -234       C  
ATOM    683  OD1 ASN A 158      28.521 -11.060  25.171  1.00 37.04           O  
ANISOU  683  OD1 ASN A 158     3968   4279   5826    561    352   -218       O  
ATOM    684  ND2 ASN A 158      27.622 -11.302  27.214  1.00 37.61           N  
ANISOU  684  ND2 ASN A 158     4117   4117   6054    455    288   -112       N  
ATOM    685  H   ASN A 158      25.846  -9.837  23.812  1.00 46.25           H  
ATOM    686  HA  ASN A 158      26.762 -11.710  23.387  1.00 50.11           H  
ATOM    687  HB2 ASN A 158      25.782 -12.368  25.958  1.00 42.25           H  
ATOM    688  HB3 ASN A 158      26.841 -13.259  25.178  1.00 42.25           H  
ATOM    689 HD21 ASN A 158      28.243 -10.835  27.584  1.00 45.13           H  
ATOM    690 HD22 ASN A 158      26.987 -11.628  27.693  1.00 45.13           H  
ATOM    691  N   ASP A 159      24.184 -12.234  22.437  1.00 48.44           N  
ANISOU  691  N   ASP A 159     5668   5539   7199    352    267   -753       N  
ATOM    692  CA  ASP A 159      23.269 -13.045  21.641  1.00 51.67           C  
ANISOU  692  CA  ASP A 159     6151   5874   7608    326    246   -937       C  
ATOM    693  C   ASP A 159      23.844 -13.163  20.231  1.00 56.13           C  
ANISOU  693  C   ASP A 159     6702   6582   8043    435    283  -1061       C  
ATOM    694  O   ASP A 159      23.647 -12.284  19.388  1.00 52.62           O  
ANISOU  694  O   ASP A 159     6206   6322   7464    412    274  -1064       O  
ATOM    695  CB  ASP A 159      21.871 -12.434  21.623  1.00 55.74           C  
ANISOU  695  CB  ASP A 159     6665   6413   8100    178    182   -942       C  
ATOM    696  CG  ASP A 159      20.923 -13.194  20.717  1.00 60.05           C  
ANISOU  696  CG  ASP A 159     7271   6913   8631    137    148  -1136       C  
ATOM    697  OD1 ASP A 159      20.306 -12.568  19.827  1.00 65.62           O  
ANISOU  697  OD1 ASP A 159     7946   7766   9218     95    117  -1189       O  
ATOM    698  OD2 ASP A 159      20.830 -14.433  20.875  1.00 56.14           O  
ANISOU  698  OD2 ASP A 159     6857   6232   8242    149    149  -1234       O  
ATOM    699  H   ASP A 159      24.119 -11.391  22.279  1.00 58.13           H  
ATOM    700  HA  ASP A 159      23.210 -13.932  22.027  1.00 62.01           H  
ATOM    701  HB2 ASP A 159      21.507 -12.449  22.522  1.00 66.88           H  
ATOM    702  HB3 ASP A 159      21.927 -11.520  21.303  1.00 66.88           H  
ATOM    703  N   SER A 160      24.545 -14.269  19.976  1.00 58.14           N  
ANISOU  703  N   SER A 160     7524   4904   9662   -450    521   -966       N  
ATOM    704  CA  SER A 160      25.227 -14.434  18.699  1.00 64.44           C  
ANISOU  704  CA  SER A 160     8278   5740  10468   -347    497  -1273       C  
ATOM    705  C   SER A 160      24.261 -14.576  17.531  1.00 62.58           C  
ANISOU  705  C   SER A 160     7986   5580  10213   -430    481  -1474       C  
ATOM    706  O   SER A 160      24.572 -14.119  16.423  1.00 66.17           O  
ANISOU  706  O   SER A 160     8397   6223  10520   -357    511  -1687       O  
ATOM    707  CB  SER A 160      26.141 -15.660  18.770  1.00 65.10           C  
ANISOU  707  CB  SER A 160     8385   5541  10808   -245    401  -1364       C  
ATOM    708  OG  SER A 160      25.437 -16.770  19.304  1.00 72.16           O  
ANISOU  708  OG  SER A 160     9325   6138  11953   -353    323  -1260       O  
ATOM    709  H   SER A 160      24.638 -14.929  20.519  1.00 69.77           H  
ATOM    710  HA  SER A 160      25.765 -13.644  18.534  1.00 77.33           H  
ATOM    711  HB2 SER A 160      26.448 -15.879  17.876  1.00 78.12           H  
ATOM    712  HB3 SER A 160      26.898 -15.459  19.342  1.00 78.12           H  
ATOM    713  HG  SER A 160      25.949 -17.433  19.363  1.00 86.59           H  
ATOM    714  N   SER A 161      23.093 -15.174  17.754  1.00 58.96           N  
ANISOU  714  N   SER A 161     7514   5002   9886   -590    433  -1399       N  
ATOM    715  CA  SER A 161      22.158 -15.397  16.659  1.00 65.36           C  
ANISOU  715  CA  SER A 161     8252   5893  10689   -690    386  -1600       C  
ATOM    716  C   SER A 161      21.836 -14.097  15.934  1.00 66.86           C  
ANISOU  716  C   SER A 161     8378   6456  10569   -652    472  -1633       C  
ATOM    717  O   SER A 161      21.887 -14.029  14.701  1.00 72.03           O  
ANISOU  717  O   SER A 161     8990   7257  11122   -612    448  -1883       O  
ATOM    718  CB  SER A 161      20.881 -16.048  17.185  1.00 66.06           C  
ANISOU  718  CB  SER A 161     8306   5843  10950   -900    336  -1451       C  
ATOM    719  OG  SER A 161      20.205 -15.202  18.098  1.00 65.68           O  
ANISOU  719  OG  SER A 161     8232   5957  10768   -950    435  -1148       O  
ATOM    720  H   SER A 161      22.822 -15.455  18.520  1.00 70.75           H  
ATOM    721  HA  SER A 161      22.566 -16.004  16.021  1.00 78.43           H  
ATOM    722  HB2 SER A 161      20.293 -16.234  16.437  1.00 79.27           H  
ATOM    723  HB3 SER A 161      21.115 -16.874  17.637  1.00 79.27           H  
ATOM    724  HG  SER A 161      20.693 -15.050  18.765  1.00 78.82           H  
ATOM    725  N   MET A 162      21.510 -13.050  16.685  1.00 60.79           N  
ANISOU  725  N   MET A 162     7613   5844   9640   -652    577  -1379       N  
ATOM    726  CA  MET A 162      21.158 -11.771  16.092  1.00 59.50           C  
ANISOU  726  CA  MET A 162     7407   5998   9202   -602    669  -1368       C  
ATOM    727  C   MET A 162      22.364 -10.873  15.841  1.00 58.82           C  
ANISOU  727  C   MET A 162     7375   6032   8943   -453    752  -1412       C  
ATOM    728  O   MET A 162      22.234  -9.888  15.107  1.00 55.33           O  
ANISOU  728  O   MET A 162     6908   5831   8283   -399    824  -1438       O  
ATOM    729  CB  MET A 162      20.159 -11.017  16.983  1.00 58.23           C  
ANISOU  729  CB  MET A 162     7231   5939   8954   -658    758  -1086       C  
ATOM    730  CG  MET A 162      18.729 -11.537  16.923  1.00 64.69           C  
ANISOU  730  CG  MET A 162     7933   6779   9869   -810    705  -1035       C  
ATOM    731  SD  MET A 162      18.042 -11.641  15.253  1.00 65.57           S  
ANISOU  731  SD  MET A 162     7908   7105   9899   -844    611  -1296       S  
ATOM    732  CE  MET A 162      18.209 -13.397  14.936  1.00 66.38           C  
ANISOU  732  CE  MET A 162     8016   6893  10313   -980    436  -1535       C  
ATOM    733  H   MET A 162      21.486 -13.057  17.545  1.00 72.95           H  
ATOM    734  HA  MET A 162      20.721 -11.951  15.245  1.00 71.40           H  
ATOM    735  HB2 MET A 162      20.455 -11.086  17.904  1.00 69.87           H  
ATOM    736  HB3 MET A 162      20.142 -10.087  16.708  1.00 69.87           H  
ATOM    737  HG2 MET A 162      18.707 -12.428  17.305  1.00 77.63           H  
ATOM    738  HG3 MET A 162      18.161 -10.942  17.437  1.00 77.63           H  
ATOM    739  HE1 MET A 162      17.820 -13.600  14.070  1.00 79.66           H  
ATOM    740  HE2 MET A 162      19.151 -13.630  14.938  1.00 79.66           H  
ATOM    741  HE3 MET A 162      17.745 -13.889  15.631  1.00 79.66           H  
ATOM    742  N   LYS A 163      23.521 -11.176  16.435  1.00 56.82           N  
ANISOU  742  N   LYS A 163     7183   5622   8782   -389    744  -1403       N  
ATOM    743  CA  LYS A 163      24.669 -10.284  16.309  1.00 54.45           C  
ANISOU  743  CA  LYS A 163     6911   5449   8330   -279    824  -1418       C  
ATOM    744  C   LYS A 163      25.059 -10.091  14.847  1.00 48.76           C  
ANISOU  744  C   LYS A 163     6132   4906   7487   -203    843  -1655       C  
ATOM    745  O   LYS A 163      25.185  -8.958  14.371  1.00 46.90           O  
ANISOU  745  O   LYS A 163     5895   4888   7035   -164    942  -1625       O  
ATOM    746  CB  LYS A 163      25.848 -10.833  17.111  1.00 54.02           C  
ANISOU  746  CB  LYS A 163     6891   5215   8420   -224    780  -1388       C  
ATOM    747  CG  LYS A 163      27.143 -10.077  16.893  1.00 49.75           C  
ANISOU  747  CG  LYS A 163     6338   4808   7757   -128    844  -1433       C  
ATOM    748  CD  LYS A 163      28.187 -10.433  17.949  1.00 50.86           C  
ANISOU  748  CD  LYS A 163     6496   4815   8014    -86    793  -1335       C  
ATOM    749  CE  LYS A 163      29.557  -9.865  17.582  1.00 48.64           C  
ANISOU  749  CE  LYS A 163     6153   4679   7648     -1    838  -1415       C  
ATOM    750  NZ  LYS A 163      29.477  -8.434  17.186  1.00 43.36           N  
ANISOU  750  NZ  LYS A 163     5501   4233   6740    -45    961  -1379       N  
ATOM    751  H   LYS A 163      23.663 -11.881  16.907  1.00 68.18           H  
ATOM    752  HA  LYS A 163      24.432  -9.418  16.675  1.00 65.34           H  
ATOM    753  HB2 LYS A 163      25.632 -10.784  18.055  1.00 64.83           H  
ATOM    754  HB3 LYS A 163      25.997 -11.756  16.852  1.00 64.83           H  
ATOM    755  HG2 LYS A 163      27.503 -10.303  16.021  1.00 59.70           H  
ATOM    756  HG3 LYS A 163      26.971  -9.124  16.944  1.00 59.70           H  
ATOM    757  HD2 LYS A 163      27.920 -10.062  18.804  1.00 61.04           H  
ATOM    758  HD3 LYS A 163      28.263 -11.398  18.015  1.00 61.04           H  
ATOM    759  HE2 LYS A 163      30.147  -9.935  18.349  1.00 58.36           H  
ATOM    760  HE3 LYS A 163      29.922 -10.366  16.836  1.00 58.36           H  
ATOM    761  HZ1 LYS A 163      30.295  -8.106  17.063  1.00 52.03           H  
ATOM    762  HZ2 LYS A 163      29.016  -8.353  16.429  1.00 52.03           H  
ATOM    763  HZ3 LYS A 163      29.071  -7.964  17.824  1.00 52.03           H  
ATOM    764  N   GLU A 164      25.244 -11.190  14.116  1.00 47.17           N  
ANISOU  764  N   GLU A 164     5894   4612   7416   -177    755  -1892       N  
ATOM    765  CA  GLU A 164      25.639 -11.073  12.717  1.00 52.93           C  
ANISOU  765  CA  GLU A 164     6573   5535   8002    -93    780  -2136       C  
ATOM    766  C   GLU A 164      24.578 -10.353  11.898  1.00 52.79           C  
ANISOU  766  C   GLU A 164     6518   5771   7768   -139    806  -2132       C  
ATOM    767  O   GLU A 164      24.910  -9.653  10.935  1.00 50.39           O  
ANISOU  767  O   GLU A 164     6188   5712   7246    -64    880  -2208       O  
ATOM    768  CB  GLU A 164      25.922 -12.457  12.125  1.00 59.53           C  
ANISOU  768  CB  GLU A 164     7398   6201   9021    -53    677  -2421       C  
ATOM    769  CG  GLU A 164      24.688 -13.308  11.870  1.00 72.39           C  
ANISOU  769  CG  GLU A 164     9020   7717  10766   -184    558  -2519       C  
ATOM    770  CD  GLU A 164      24.249 -13.287  10.407  1.00 78.90           C  
ANISOU  770  CD  GLU A 164     9795   8777  11406   -179    530  -2780       C  
ATOM    771  OE1 GLU A 164      23.198 -13.898  10.094  1.00 80.50           O  
ANISOU  771  OE1 GLU A 164     9973   8935  11676   -308    419  -2880       O  
ATOM    772  OE2 GLU A 164      24.948 -12.662   9.575  1.00 74.98           O  
ANISOU  772  OE2 GLU A 164     9275   8523  10689    -57    618  -2879       O  
ATOM    773  H   GLU A 164      25.151 -11.996  14.401  1.00 56.60           H  
ATOM    774  HA  GLU A 164      26.459 -10.559  12.668  1.00 63.51           H  
ATOM    775  HB2 GLU A 164      26.377 -12.341  11.276  1.00 71.44           H  
ATOM    776  HB3 GLU A 164      26.490 -12.944  12.742  1.00 71.44           H  
ATOM    777  HG2 GLU A 164      24.882 -14.227  12.112  1.00 86.86           H  
ATOM    778  HG3 GLU A 164      23.955 -12.972  12.409  1.00 86.86           H  
ATOM    779  N   LYS A 165      23.305 -10.497  12.269  1.00 50.37           N  
ANISOU  779  N   LYS A 165     6197   5428   7515   -255    752  -2024       N  
ATOM    780  CA  LYS A 165      22.248  -9.822  11.528  1.00 51.74           C  
ANISOU  780  CA  LYS A 165     6307   5862   7489   -283    764  -1998       C  
ATOM    781  C   LYS A 165      22.304  -8.315  11.751  1.00 47.04           C  
ANISOU  781  C   LYS A 165     5746   5445   6683   -218    909  -1770       C  
ATOM    782  O   LYS A 165      22.227  -7.535  10.797  1.00 46.10           O  
ANISOU  782  O   LYS A 165     5601   5577   6339   -151    964  -1790       O  
ATOM    783  CB  LYS A 165      20.884 -10.377  11.934  1.00 54.48           C  
ANISOU  783  CB  LYS A 165     6596   6137   7967   -428    672  -1923       C  
ATOM    784  CG  LYS A 165      20.660 -11.845  11.572  1.00 61.17           C  
ANISOU  784  CG  LYS A 165     7415   6798   9028   -528    516  -2164       C  
ATOM    785  CD  LYS A 165      19.163 -12.143  11.445  1.00 64.31           C  
ANISOU  785  CD  LYS A 165     7702   7267   9466   -690    422  -2132       C  
ATOM    786  CE  LYS A 165      18.847 -13.624  11.634  1.00 71.40           C  
ANISOU  786  CE  LYS A 165     8597   7864  10668   -851    278  -2273       C  
ATOM    787  NZ  LYS A 165      18.935 -14.420  10.372  1.00 75.77           N  
ANISOU  787  NZ  LYS A 165     9139   8432  11220   -872    150  -2653       N  
ATOM    788  H   LYS A 165      23.035 -10.971  12.933  1.00 60.45           H  
ATOM    789  HA  LYS A 165      22.369  -9.995  10.582  1.00 62.08           H  
ATOM    790  HB2 LYS A 165      20.791 -10.295  12.896  1.00 65.38           H  
ATOM    791  HB3 LYS A 165      20.195  -9.858  11.489  1.00 65.38           H  
ATOM    792  HG2 LYS A 165      21.087 -12.040  10.723  1.00 73.40           H  
ATOM    793  HG3 LYS A 165      21.030 -12.411  12.267  1.00 73.40           H  
ATOM    794  HD2 LYS A 165      18.681 -11.644  12.123  1.00 77.17           H  
ATOM    795  HD3 LYS A 165      18.860 -11.881  10.562  1.00 77.17           H  
ATOM    796  HE2 LYS A 165      19.479 -14.001  12.267  1.00 85.68           H  
ATOM    797  HE3 LYS A 165      17.944 -13.711  11.977  1.00 85.68           H  
ATOM    798  HZ1 LYS A 165      18.752 -15.275  10.538  1.00 90.93           H  
ATOM    799  HZ2 LYS A 165      18.351 -14.111   9.776  1.00 90.93           H  
ATOM    800  HZ3 LYS A 165      19.755 -14.361  10.031  1.00 90.93           H  
ATOM    801  N   TYR A 166      22.440  -7.884  13.008  1.00 40.49           N  
ANISOU  801  N   TYR A 166     4986   4482   5917   -235    973  -1551       N  
ATOM    802  CA  TYR A 166      22.524  -6.453  13.278  1.00 43.55           C  
ANISOU  802  CA  TYR A 166     5435   4989   6125   -179   1112  -1358       C  
ATOM    803  C   TYR A 166      23.819  -5.864  12.733  1.00 38.82           C  
ANISOU  803  C   TYR A 166     4869   4469   5410   -102   1190  -1428       C  
ATOM    804  O   TYR A 166      23.806  -4.790  12.124  1.00 39.89           O  
ANISOU  804  O   TYR A 166     5022   4786   5350    -48   1288  -1361       O  
ATOM    805  CB  TYR A 166      22.395  -6.180  14.778  1.00 37.67           C  
ANISOU  805  CB  TYR A 166     4770   4083   5459   -220   1157  -1144       C  
ATOM    806  CG  TYR A 166      20.967  -6.243  15.256  1.00 38.19           C  
ANISOU  806  CG  TYR A 166     4792   4163   5554   -276   1150  -1002       C  
ATOM    807  CD1 TYR A 166      20.100  -5.183  15.039  1.00 37.03           C  
ANISOU  807  CD1 TYR A 166     4632   4194   5243   -220   1240   -869       C  
ATOM    808  CD2 TYR A 166      20.480  -7.364  15.916  1.00 39.02           C  
ANISOU  808  CD2 TYR A 166     4858   4106   5861   -377   1059   -985       C  
ATOM    809  CE1 TYR A 166      18.792  -5.230  15.468  1.00 37.83           C  
ANISOU  809  CE1 TYR A 166     4659   4342   5372   -255   1245   -732       C  
ATOM    810  CE2 TYR A 166      19.171  -7.427  16.353  1.00 38.44           C  
ANISOU  810  CE2 TYR A 166     4715   4072   5819   -442   1066   -840       C  
ATOM    811  CZ  TYR A 166      18.329  -6.356  16.124  1.00 38.38           C  
ANISOU  811  CZ  TYR A 166     4671   4274   5638   -375   1160   -719       C  
ATOM    812  OH  TYR A 166      17.025  -6.414  16.544  1.00 39.03           O  
ANISOU  812  OH  TYR A 166     4650   4427   5751   -424   1176   -570       O  
ATOM    813  H   TYR A 166      22.486  -8.389  13.703  1.00 48.59           H  
ATOM    814  HA  TYR A 166      21.782  -6.012  12.836  1.00 52.27           H  
ATOM    815  HB2 TYR A 166      22.905  -6.845  15.265  1.00 45.20           H  
ATOM    816  HB3 TYR A 166      22.737  -5.293  14.968  1.00 45.20           H  
ATOM    817  HD1 TYR A 166      20.407  -4.426  14.594  1.00 44.43           H  
ATOM    818  HD2 TYR A 166      21.047  -8.086  16.066  1.00 46.82           H  
ATOM    819  HE1 TYR A 166      18.224  -4.509  15.318  1.00 45.39           H  
ATOM    820  HE2 TYR A 166      18.860  -8.183  16.796  1.00 46.13           H  
ATOM    821  HH  TYR A 166      16.615  -5.722  16.303  1.00 46.83           H  
ATOM    822  N   ASP A 167      24.947  -6.547  12.941  1.00 41.96           N  
ANISOU  822  N   ASP A 167     5269   4740   5935    -90   1154  -1544       N  
ATOM    823  CA  ASP A 167      26.206  -6.065  12.375  1.00 44.29           C  
ANISOU  823  CA  ASP A 167     5555   5141   6132    -24   1232  -1615       C  
ATOM    824  C   ASP A 167      26.119  -5.963  10.852  1.00 46.80           C  
ANISOU  824  C   ASP A 167     5809   5701   6272     39   1257  -1768       C  
ATOM    825  O   ASP A 167      26.594  -4.992  10.253  1.00 43.07           O  
ANISOU  825  O   ASP A 167     5341   5406   5617     79   1372  -1716       O  
ATOM    826  CB  ASP A 167      27.357  -6.981  12.781  1.00 44.69           C  
ANISOU  826  CB  ASP A 167     5577   5038   6365      2   1174  -1728       C  
ATOM    827  CG  ASP A 167      27.706  -6.860  14.253  1.00 42.18           C  
ANISOU  827  CG  ASP A 167     5323   4542   6161    -47   1160  -1552       C  
ATOM    828  OD1 ASP A 167      27.091  -6.035  14.951  1.00 42.01           O  
ANISOU  828  OD1 ASP A 167     5380   4515   6066   -104   1209  -1365       O  
ATOM    829  OD2 ASP A 167      28.600  -7.610  14.715  1.00 48.75           O  
ANISOU  829  OD2 ASP A 167     6126   5249   7149    -15   1098  -1605       O  
ATOM    830  H   ASP A 167      25.009  -7.274  13.396  1.00 50.36           H  
ATOM    831  HA  ASP A 167      26.388  -5.182  12.731  1.00 53.15           H  
ATOM    832  HB2 ASP A 167      27.107  -7.901  12.606  1.00 53.63           H  
ATOM    833  HB3 ASP A 167      28.145  -6.747  12.265  1.00 53.63           H  
ATOM    834  N   SER A 168      25.501  -6.950  10.204  1.00 45.42           N  
ANISOU  834  N   SER A 168     5578   5540   6139     38   1149  -1955       N  
ATOM    835  CA  SER A 168      25.347  -6.873   8.755  1.00 53.29           C  
ANISOU  835  CA  SER A 168     6520   6800   6928     96   1158  -2113       C  
ATOM    836  C   SER A 168      24.473  -5.686   8.358  1.00 53.74           C  
ANISOU  836  C   SER A 168     6584   7074   6759    103   1225  -1922       C  
ATOM    837  O   SER A 168      24.775  -4.975   7.391  1.00 53.04           O  
ANISOU  837  O   SER A 168     6485   7226   6443    173   1312  -1917       O  
ATOM    838  CB  SER A 168      24.764  -8.175   8.219  1.00 52.44           C  
ANISOU  838  CB  SER A 168     6364   6647   6914     69   1007  -2370       C  
ATOM    839  OG  SER A 168      24.575  -8.100   6.822  1.00 57.48           O  
ANISOU  839  OG  SER A 168     6955   7570   7316    124   1002  -2540       O  
ATOM    840  H   SER A 168      25.172  -7.655  10.570  1.00 54.50           H  
ATOM    841  HA  SER A 168      26.221  -6.750   8.353  1.00 63.95           H  
ATOM    842  HB2 SER A 168      25.377  -8.901   8.417  1.00 62.93           H  
ATOM    843  HB3 SER A 168      23.909  -8.338   8.646  1.00 62.93           H  
ATOM    844  HG  SER A 168      24.259  -8.823   6.535  1.00 68.98           H  
ATOM    845  N   MET A 169      23.384  -5.455   9.095  1.00 46.76           N  
ANISOU  845  N   MET A 169     5715   6116   5935     45   1194  -1748       N  
ATOM    846  CA  MET A 169      22.516  -4.316   8.803  1.00 47.57           C  
ANISOU  846  CA  MET A 169     5822   6407   5847     84   1262  -1546       C  
ATOM    847  C   MET A 169      23.297  -3.007   8.846  1.00 48.13           C  
ANISOU  847  C   MET A 169     5983   6516   5788    141   1429  -1373       C  
ATOM    848  O   MET A 169      23.178  -2.170   7.944  1.00 49.38           O  
ANISOU  848  O   MET A 169     6142   6893   5729    214   1503  -1296       O  
ATOM    849  CB  MET A 169      21.352  -4.287   9.798  1.00 48.06           C  
ANISOU  849  CB  MET A 169     5878   6357   6024     28   1229  -1376       C  
ATOM    850  CG  MET A 169      20.361  -3.148   9.615  1.00 45.06           C  
ANISOU  850  CG  MET A 169     5491   6152   5478    100   1300  -1154       C  
ATOM    851  SD  MET A 169      19.372  -2.881  11.114  1.00 47.40           S  
ANISOU  851  SD  MET A 169     5812   6282   5917     66   1338   -923       S  
ATOM    852  CE  MET A 169      20.659  -2.225  12.201  1.00 47.98           C  
ANISOU  852  CE  MET A 169     6071   6114   6044     64   1468   -839       C  
ATOM    853  H   MET A 169      23.130  -5.936   9.761  1.00 56.11           H  
ATOM    854  HA  MET A 169      22.145  -4.425   7.914  1.00 57.09           H  
ATOM    855  HB2 MET A 169      20.858  -5.117   9.713  1.00 57.67           H  
ATOM    856  HB3 MET A 169      21.718  -4.210  10.693  1.00 57.67           H  
ATOM    857  HG2 MET A 169      20.844  -2.331   9.418  1.00 54.07           H  
ATOM    858  HG3 MET A 169      19.758  -3.362   8.886  1.00 54.07           H  
ATOM    859  HE1 MET A 169      20.260  -1.978  13.049  1.00 57.58           H  
ATOM    860  HE2 MET A 169      21.334  -2.908  12.339  1.00 57.58           H  
ATOM    861  HE3 MET A 169      21.058  -1.446  11.783  1.00 57.58           H  
ATOM    862  N   HIS A 170      24.106  -2.813   9.890  1.00 42.64           N  
ANISOU  862  N   HIS A 170     5367   5611   5224    100   1485  -1305       N  
ATOM    863  CA  HIS A 170      24.846  -1.564  10.021  1.00 47.49           C  
ANISOU  863  CA  HIS A 170     6073   6229   5744    115   1634  -1149       C  
ATOM    864  C   HIS A 170      25.886  -1.409   8.918  1.00 46.91           C  
ANISOU  864  C   HIS A 170     5954   6332   5536    151   1701  -1245       C  
ATOM    865  O   HIS A 170      26.151  -0.290   8.464  1.00 45.54           O  
ANISOU  865  O   HIS A 170     5830   6262   5209    174   1829  -1101       O  
ATOM    866  CB  HIS A 170      25.514  -1.494  11.390  1.00 41.40           C  
ANISOU  866  CB  HIS A 170     5381   5215   5135     41   1648  -1088       C  
ATOM    867  CG  HIS A 170      24.553  -1.274  12.518  1.00 44.34           C  
ANISOU  867  CG  HIS A 170     5827   5443   5577     18   1640   -940       C  
ATOM    868  ND1 HIS A 170      24.265  -2.246  13.451  1.00 43.45           N  
ANISOU  868  ND1 HIS A 170     5695   5175   5637    -35   1539   -974       N  
ATOM    869  CD2 HIS A 170      23.817  -0.191  12.862  1.00 35.34           C  
ANISOU  869  CD2 HIS A 170     4781   4295   4353     52   1734   -751       C  
ATOM    870  CE1 HIS A 170      23.398  -1.766  14.326  1.00 43.36           C  
ANISOU  870  CE1 HIS A 170     5753   5094   5628    -38   1578   -813       C  
ATOM    871  NE2 HIS A 170      23.115  -0.519  13.993  1.00 37.23           N  
ANISOU  871  NE2 HIS A 170     5047   4400   4700     24   1697   -688       N  
ATOM    872  H   HIS A 170      24.239  -3.379  10.523  1.00 51.17           H  
ATOM    873  HA  HIS A 170      24.219  -0.827   9.947  1.00 56.99           H  
ATOM    874  HB2 HIS A 170      25.977  -2.330  11.554  1.00 49.68           H  
ATOM    875  HB3 HIS A 170      26.146  -0.758  11.391  1.00 49.68           H  
ATOM    876  HD1 HIS A 170      24.596  -3.039  13.463  1.00 52.14           H  
ATOM    877  HD2 HIS A 170      23.792   0.624  12.415  1.00 42.41           H  
ATOM    878  HE1 HIS A 170      23.047  -2.228  15.052  1.00 52.03           H  
ATOM    879  N   GLU A 171      26.498  -2.511   8.480  1.00 52.71           N  
ANISOU  879  N   GLU A 171     6598   7098   6331    162   1629  -1482       N  
ATOM    880  CA  GLU A 171      27.435  -2.434   7.363  1.00 51.92           C  
ANISOU  880  CA  GLU A 171     6436   7210   6082    217   1708  -1589       C  
ATOM    881  C   GLU A 171      26.734  -1.925   6.109  1.00 51.91           C  
ANISOU  881  C   GLU A 171     6419   7493   5811    286   1743  -1551       C  
ATOM    882  O   GLU A 171      27.223  -1.013   5.430  1.00 52.84           O  
ANISOU  882  O   GLU A 171     6550   7782   5744    316   1879  -1436       O  
ATOM    883  CB  GLU A 171      28.064  -3.803   7.110  1.00 58.64           C  
ANISOU  883  CB  GLU A 171     7198   8036   7048    251   1622  -1877       C  
ATOM    884  CG  GLU A 171      28.876  -4.345   8.279  1.00 70.00           C  
ANISOU  884  CG  GLU A 171     8634   9218   8743    211   1582  -1897       C  
ATOM    885  CD  GLU A 171      29.221  -5.819   8.117  1.00 80.35           C  
ANISOU  885  CD  GLU A 171     9876  10443  10209    269   1475  -2170       C  
ATOM    886  OE1 GLU A 171      29.298  -6.533   9.143  1.00 85.26           O  
ANISOU  886  OE1 GLU A 171    10516  10811  11068    240   1382  -2174       O  
ATOM    887  OE2 GLU A 171      29.405  -6.262   6.962  1.00 81.37           O  
ANISOU  887  OE2 GLU A 171     9946  10754  10218    352   1486  -2380       O  
ATOM    888  H   GLU A 171      26.390  -3.299   8.807  1.00 63.25           H  
ATOM    889  HA  GLU A 171      28.148  -1.815   7.589  1.00 62.31           H  
ATOM    890  HB2 GLU A 171      27.356  -4.439   6.923  1.00 70.37           H  
ATOM    891  HB3 GLU A 171      28.658  -3.734   6.346  1.00 70.37           H  
ATOM    892  HG2 GLU A 171      29.706  -3.847   8.347  1.00 84.00           H  
ATOM    893  HG3 GLU A 171      28.361  -4.244   9.096  1.00 84.00           H  
ATOM    894  N   LYS A 172      25.565  -2.496   5.795  1.00 49.50           N  
ANISOU  894  N   LYS A 172     6080   7251   5478    304   1616  -1632       N  
ATOM    895  CA  LYS A 172      24.838  -2.077   4.601  1.00 49.82           C  
ANISOU  895  CA  LYS A 172     6088   7597   5246    377   1617  -1598       C  
ATOM    896  C   LYS A 172      24.307  -0.656   4.746  1.00 48.82           C  
ANISOU  896  C   LYS A 172     6038   7503   5007    408   1725  -1267       C  
ATOM    897  O   LYS A 172      24.288   0.106   3.775  1.00 53.93           O  
ANISOU  897  O   LYS A 172     6691   8393   5408    483   1808  -1152       O  
ATOM    898  CB  LYS A 172      23.691  -3.044   4.317  1.00 49.35           C  
ANISOU  898  CB  LYS A 172     5952   7596   5202    362   1432  -1766       C  
ATOM    899  CG  LYS A 172      24.115  -4.459   3.957  1.00 55.50           C  
ANISOU  899  CG  LYS A 172     6676   8342   6070    343   1321  -2122       C  
ATOM    900  CD  LYS A 172      24.484  -4.575   2.486  1.00 64.98           C  
ANISOU  900  CD  LYS A 172     7831   9874   6985    430   1342  -2308       C  
ATOM    901  CE  LYS A 172      24.433  -6.027   2.018  1.00 76.32           C  
ANISOU  901  CE  LYS A 172     9222  11291   8485    416   1190  -2697       C  
ATOM    902  NZ  LYS A 172      25.765  -6.531   1.565  1.00 70.71           N  
ANISOU  902  NZ  LYS A 172     8507  10601   7758    497   1276  -2926       N  
ATOM    903  H   LYS A 172      25.182  -3.117   6.250  1.00 59.41           H  
ATOM    904  HA  LYS A 172      25.446  -2.098   3.846  1.00 59.79           H  
ATOM    905  HB2 LYS A 172      23.133  -3.100   5.109  1.00 59.22           H  
ATOM    906  HB3 LYS A 172      23.175  -2.697   3.572  1.00 59.22           H  
ATOM    907  HG2 LYS A 172      24.890  -4.705   4.486  1.00 66.60           H  
ATOM    908  HG3 LYS A 172      23.383  -5.069   4.137  1.00 66.60           H  
ATOM    909  HD2 LYS A 172      23.858  -4.060   1.954  1.00 77.98           H  
ATOM    910  HD3 LYS A 172      25.385  -4.242   2.352  1.00 77.98           H  
ATOM    911  HE2 LYS A 172      24.134  -6.586   2.752  1.00 91.58           H  
ATOM    912  HE3 LYS A 172      23.815  -6.098   1.274  1.00 91.58           H  
ATOM    913  HZ1 LYS A 172      25.696  -7.377   1.299  1.00 84.85           H  
ATOM    914  HZ2 LYS A 172      26.062  -6.038   0.886  1.00 84.85           H  
ATOM    915  HZ3 LYS A 172      26.351  -6.485   2.233  1.00 84.85           H  
ATOM    916  N   MET A 173      23.863  -0.283   5.946  1.00 47.39           N  
ANISOU  916  N   MET A 173     5928   7080   5000    366   1732  -1108       N  
ATOM    917  CA  MET A 173      23.338   1.065   6.142  1.00 54.39           C  
ANISOU  917  CA  MET A 173     6909   7956   5802    418   1843   -810       C  
ATOM    918  C   MET A 173      24.421   2.113   5.916  1.00 51.43           C  
ANISOU  918  C   MET A 173     6626   7571   5342    413   2018   -673       C  
ATOM    919  O   MET A 173      24.172   3.143   5.281  1.00 54.37           O  
ANISOU  919  O   MET A 173     7052   8068   5538    489   2117   -466       O  
ATOM    920  CB  MET A 173      22.743   1.206   7.543  1.00 46.88           C  
ANISOU  920  CB  MET A 173     6025   6738   5049    380   1831   -702       C  
ATOM    921  CG  MET A 173      21.274   0.825   7.628  1.00 49.31           C  
ANISOU  921  CG  MET A 173     6246   7119   5370    418   1721   -677       C  
ATOM    922  SD  MET A 173      20.575   0.907   9.293  1.00 44.88           S  
ANISOU  922  SD  MET A 173     5746   6283   5024    380   1731   -553       S  
ATOM    923  CE  MET A 173      20.825   2.619   9.705  1.00 45.48           C  
ANISOU  923  CE  MET A 173     6016   6236   5028    460   1934   -290       C  
ATOM    924  H   MET A 173      23.854  -0.781   6.647  1.00 56.87           H  
ATOM    925  HA  MET A 173      22.621   1.209   5.504  1.00 65.27           H  
ATOM    926  HB2 MET A 173      23.233   0.630   8.150  1.00 56.26           H  
ATOM    927  HB3 MET A 173      22.825   2.131   7.825  1.00 56.26           H  
ATOM    928  HG2 MET A 173      20.764   1.430   7.066  1.00 59.17           H  
ATOM    929  HG3 MET A 173      21.172  -0.086   7.312  1.00 59.17           H  
ATOM    930  HE1 MET A 173      20.404   2.803  10.560  1.00 54.57           H  
ATOM    931  HE2 MET A 173      21.777   2.794   9.761  1.00 54.57           H  
ATOM    932  HE3 MET A 173      20.426   3.172   9.015  1.00 54.57           H  
ATOM    933  N   ASN A 174      25.629   1.867   6.428  1.00 51.83           N  
ANISOU  933  N   ASN A 174     6689   7476   5526    320   2054   -769       N  
ATOM    934  CA  ASN A 174      26.729   2.798   6.213  1.00 55.27           C  
ANISOU  934  CA  ASN A 174     7183   7914   5903    276   2215   -649       C  
ATOM    935  C   ASN A 174      27.090   2.900   4.739  1.00 57.54           C  
ANISOU  935  C   ASN A 174     7396   8524   5942    342   2284   -662       C  
ATOM    936  O   ASN A 174      27.490   3.971   4.271  1.00 61.52           O  
ANISOU  936  O   ASN A 174     7962   9091   6322    339   2435   -458       O  
ATOM    937  CB  ASN A 174      27.952   2.368   7.027  1.00 51.93           C  
ANISOU  937  CB  ASN A 174     6736   7322   5672    162   2213   -770       C  
ATOM    938  CG  ASN A 174      27.689   2.380   8.525  1.00 51.57           C  
ANISOU  938  CG  ASN A 174     6782   6978   5832     92   2156   -732       C  
ATOM    939  OD1 ASN A 174      26.666   2.884   8.984  1.00 49.52           O  
ANISOU  939  OD1 ASN A 174     6619   6624   5572    127   2156   -597       O  
ATOM    940  ND2 ASN A 174      28.619   1.827   9.294  1.00 47.72           N  
ANISOU  940  ND2 ASN A 174     6258   6363   5510      8   2111   -844       N  
ATOM    941  H   ASN A 174      25.832   1.177   6.898  1.00 62.19           H  
ATOM    942  HA  ASN A 174      26.457   3.676   6.522  1.00 66.32           H  
ATOM    943  HB2 ASN A 174      28.202   1.466   6.772  1.00 62.31           H  
ATOM    944  HB3 ASN A 174      28.684   2.978   6.845  1.00 62.31           H  
ATOM    945 HD21 ASN A 174      28.515   1.810  10.148  1.00 57.27           H  
ATOM    946 HD22 ASN A 174      29.324   1.487   8.939  1.00 57.27           H  
ATOM    947  N   ALA A 175      26.953   1.807   3.995  1.00 54.54           N  
ANISOU  947  N   ALA A 175     6894   8345   5483    398   2180   -899       N  
ATOM    948  CA  ALA A 175      27.289   1.784   2.578  1.00 61.58           C  
ANISOU  948  CA  ALA A 175     7713   9581   6105    472   2240   -951       C  
ATOM    949  C   ALA A 175      26.123   2.180   1.683  1.00 62.77           C  
ANISOU  949  C   ALA A 175     7870   9976   6005    581   2203   -829       C  
ATOM    950  O   ALA A 175      26.303   2.270   0.464  1.00 56.67           O  
ANISOU  950  O   ALA A 175     7050   9526   4956    653   2253   -838       O  
ATOM    951  CB  ALA A 175      27.779   0.386   2.176  1.00 56.19           C  
ANISOU  951  CB  ALA A 175     6909   8999   5443    492   2148  -1307       C  
ATOM    952  H   ALA A 175      26.663   1.054   4.294  1.00 65.44           H  
ATOM    953  HA  ALA A 175      28.010   2.414   2.424  1.00 73.90           H  
ATOM    954  HB1 ALA A 175      28.001   0.388   1.232  1.00 67.43           H  
ATOM    955  HB2 ALA A 175      28.564   0.164   2.701  1.00 67.43           H  
ATOM    956  HB3 ALA A 175      27.074  -0.258   2.348  1.00 67.43           H  
ATOM    957  N   TYR A 176      24.945   2.427   2.255  1.00 53.31           N  
ANISOU  957  N   TYR A 176     8175   6567   5513    396   2801     87       N  
ATOM    958  CA  TYR A 176      23.750   2.645   1.448  1.00 57.39           C  
ANISOU  958  CA  TYR A 176     8903   7068   5834    401   2585    -65       C  
ATOM    959  C   TYR A 176      23.851   3.951   0.667  1.00 61.21           C  
ANISOU  959  C   TYR A 176     9577   7629   6051    393   2553     31       C  
ATOM    960  O   TYR A 176      24.203   4.998   1.219  1.00 62.47           O  
ANISOU  960  O   TYR A 176     9660   7832   6244    335   2552    210       O  
ATOM    961  CB  TYR A 176      22.510   2.653   2.341  1.00 55.63           C  
ANISOU  961  CB  TYR A 176     8559   6808   5769    354   2327   -121       C  
ATOM    962  CG  TYR A 176      21.223   2.403   1.590  1.00 55.00           C  
ANISOU  962  CG  TYR A 176     8639   6706   5553    369   2111   -331       C  
ATOM    963  CD1 TYR A 176      20.956   1.161   1.034  1.00 53.17           C  
ANISOU  963  CD1 TYR A 176     8477   6403   5324    401   2148   -543       C  
ATOM    964  CD2 TYR A 176      20.272   3.405   1.442  1.00 61.06           C  
ANISOU  964  CD2 TYR A 176     9483   7525   6191    354   1869   -324       C  
ATOM    965  CE1 TYR A 176      19.782   0.923   0.348  1.00 54.17           C  
ANISOU  965  CE1 TYR A 176     8732   6525   5326    400   1937   -754       C  
ATOM    966  CE2 TYR A 176      19.089   3.174   0.761  1.00 61.70           C  
ANISOU  966  CE2 TYR A 176     9685   7613   6146    374   1655   -519       C  
ATOM    967  CZ  TYR A 176      18.854   1.929   0.214  1.00 57.20           C  
ANISOU  967  CZ  TYR A 176     9169   6986   5580    389   1684   -740       C  
ATOM    968  OH  TYR A 176      17.685   1.689  -0.469  1.00 62.77           O  
ANISOU  968  OH  TYR A 176     9978   7711   6159    395   1460   -952       O  
ATOM    969  H   TYR A 176      24.813   2.473   3.103  1.00 63.97           H  
ATOM    970  HA  TYR A 176      23.664   1.923   0.807  1.00 68.87           H  
ATOM    971  HB2 TYR A 176      22.602   1.958   3.011  1.00 66.75           H  
ATOM    972  HB3 TYR A 176      22.439   3.520   2.770  1.00 66.75           H  
ATOM    973  HD1 TYR A 176      21.580   0.477   1.124  1.00 63.81           H  
ATOM    974  HD2 TYR A 176      20.433   4.246   1.806  1.00 73.27           H  
ATOM    975  HE1 TYR A 176      19.619   0.085  -0.021  1.00 65.01           H  
ATOM    976  HE2 TYR A 176      18.459   3.852   0.673  1.00 74.04           H  
ATOM    977  HH  TYR A 176      17.196   2.373  -0.451  1.00 75.32           H  
ATOM    978  N   ALA A 177      23.526   3.886  -0.626  1.00 65.42           N  
ANISOU  978  N   ALA A 177    10371   8174   6312    453   2529    -91       N  
ATOM    979  CA  ALA A 177      23.666   5.053  -1.485  1.00 68.95           C  
ANISOU  979  CA  ALA A 177    11033   8686   6478    468   2529      8       C  
ATOM    980  C   ALA A 177      22.460   5.979  -1.391  1.00 70.57           C  
ANISOU  980  C   ALA A 177    11304   8912   6599    456   2234     12       C  
ATOM    981  O   ALA A 177      22.618   7.206  -1.373  1.00 69.64           O  
ANISOU  981  O   ALA A 177    11246   8823   6390    434   2224    178       O  
ATOM    982  CB  ALA A 177      23.878   4.613  -2.937  1.00 65.73           C  
ANISOU  982  CB  ALA A 177    10894   8297   5785    556   2638   -112       C  
ATOM    983  H   ALA A 177      23.226   3.185  -1.023  1.00 78.51           H  
ATOM    984  HA  ALA A 177      24.448   5.551  -1.198  1.00 82.74           H  
ATOM    985  HB1 ALA A 177      23.973   5.401  -3.495  1.00 78.88           H  
ATOM    986  HB2 ALA A 177      24.681   4.072  -2.989  1.00 78.88           H  
ATOM    987  HB3 ALA A 177      23.110   4.094  -3.225  1.00 78.88           H  
ATOM    988  N   GLN A 178      21.258   5.416  -1.318  1.00 70.06           N  
ANISOU  988  N   GLN A 178    11220   8827   6572    470   2003   -169       N  
ATOM    989  CA  GLN A 178      20.034   6.192  -1.508  1.00 72.56           C  
ANISOU  989  CA  GLN A 178    11630   9183   6758    492   1717   -198       C  
ATOM    990  C   GLN A 178      19.376   6.534  -0.171  1.00 72.89           C  
ANISOU  990  C   GLN A 178    11439   9197   7059    428   1554   -139       C  
ATOM    991  O   GLN A 178      18.226   6.177   0.104  1.00 72.80           O  
ANISOU  991  O   GLN A 178    11353   9179   7128    427   1335   -275       O  
ATOM    992  CB  GLN A 178      19.071   5.431  -2.414  1.00 66.76           C  
ANISOU  992  CB  GLN A 178    11031   8470   5866    550   1548   -449       C  
ATOM    993  CG  GLN A 178      19.625   5.134  -3.799  1.00 72.57           C  
ANISOU  993  CG  GLN A 178    12029   9241   6303    625   1690   -524       C  
ATOM    994  CD  GLN A 178      19.922   6.395  -4.587  1.00 80.32           C  
ANISOU  994  CD  GLN A 178    13243  10292   6983    687   1719   -357       C  
ATOM    995  OE1 GLN A 178      19.588   7.503  -4.155  1.00 80.32           O  
ANISOU  995  OE1 GLN A 178    13222  10307   6989    677   1606   -204       O  
ATOM    996  NE2 GLN A 178      20.554   6.236  -5.750  1.00 76.26           N  
ANISOU  996  NE2 GLN A 178    12964   9811   6202    755   1886   -384       N  
ATOM    997  H   GLN A 178      21.123   4.581  -1.159  1.00 84.07           H  
ATOM    998  HA  GLN A 178      20.272   7.029  -1.937  1.00 87.08           H  
ATOM    999  HB2 GLN A 178      18.855   4.584  -1.995  1.00 80.12           H  
ATOM   1000  HB3 GLN A 178      18.267   5.961  -2.526  1.00 80.12           H  
ATOM   1001  HG2 GLN A 178      20.450   4.632  -3.710  1.00 87.08           H  
ATOM   1002  HG3 GLN A 178      18.973   4.615  -4.296  1.00 87.08           H  
ATOM   1003 HE21 GLN A 178      20.771   5.448  -6.017  1.00 91.52           H  
ATOM   1004 HE22 GLN A 178      20.745   6.921  -6.233  1.00 91.52           H  
ATOM   1005  N   ILE A 179      20.117   7.252   0.668  1.00 65.99           N  
ANISOU 1005  N   ILE A 179    10445   8312   6315    369   1668     62       N  
ATOM   1006  CA  ILE A 179      19.540   7.840   1.874  1.00 66.85           C  
ANISOU 1006  CA  ILE A 179    10378   8404   6619    316   1520    142       C  
ATOM   1007  C   ILE A 179      18.830   9.119   1.442  1.00 63.50           C  
ANISOU 1007  C   ILE A 179    10124   8011   5992    358   1348    210       C  
ATOM   1008  O   ILE A 179      19.470  10.072   0.990  1.00 60.10           O  
ANISOU 1008  O   ILE A 179     9844   7591   5402    362   1456    357       O  
ATOM   1009  CB  ILE A 179      20.599   8.116   2.944  1.00 71.82           C  
ANISOU 1009  CB  ILE A 179    10818   9018   7453    234   1695    313       C  
ATOM   1010  CG1 ILE A 179      21.064   6.790   3.556  1.00 71.23           C  
ANISOU 1010  CG1 ILE A 179    10544   8912   7608    217   1820    246       C  
ATOM   1011  CG2 ILE A 179      20.045   9.040   4.018  1.00 65.85           C  
ANISOU 1011  CG2 ILE A 179     9947   8250   6821    185   1546    412       C  
ATOM   1012  CD1 ILE A 179      22.173   6.932   4.569  1.00 83.24           C  
ANISOU 1012  CD1 ILE A 179    11863  10447   9318    154   1990    406       C  
ATOM   1013  H   ILE A 179      20.955   7.413   0.561  1.00 79.19           H  
ATOM   1014  HA  ILE A 179      18.893   7.230   2.260  1.00 80.22           H  
ATOM   1015  HB  ILE A 179      21.358   8.558   2.532  1.00 86.18           H  
ATOM   1016 HG12 ILE A 179      20.310   6.372   4.001  1.00 85.48           H  
ATOM   1017 HG13 ILE A 179      21.388   6.216   2.844  1.00 85.48           H  
ATOM   1018 HG21 ILE A 179      20.725   9.180   4.695  1.00 79.01           H  
ATOM   1019 HG22 ILE A 179      19.802   9.886   3.612  1.00 79.01           H  
ATOM   1020 HG23 ILE A 179      19.262   8.627   4.416  1.00 79.01           H  
ATOM   1021 HD11 ILE A 179      22.419   6.052   4.894  1.00 99.89           H  
ATOM   1022 HD12 ILE A 179      22.936   7.353   4.145  1.00 99.89           H  
ATOM   1023 HD13 ILE A 179      21.859   7.481   5.305  1.00 99.89           H  
ATOM   1024  N   VAL A 180      17.507   9.138   1.568  1.00 62.13           N  
ANISOU 1024  N   VAL A 180     9928   7850   5829    394   1090    107       N  
ATOM   1025  CA  VAL A 180      16.710  10.269   1.101  1.00 57.69           C  
ANISOU 1025  CA  VAL A 180     9529   7324   5067    468    907    161       C  
ATOM   1026  C   VAL A 180      16.271  11.082   2.312  1.00 55.83           C  
ANISOU 1026  C   VAL A 180     9143   7053   5017    427    810    274       C  
ATOM   1027  O   VAL A 180      15.984  10.508   3.375  1.00 54.60           O  
ANISOU 1027  O   VAL A 180     8754   6870   5124    368    772    225       O  
ATOM   1028  CB  VAL A 180      15.501   9.796   0.276  1.00 58.25           C  
ANISOU 1028  CB  VAL A 180     9686   7459   4987    555    671    -38       C  
ATOM   1029  CG1 VAL A 180      15.915   8.695  -0.694  1.00 65.73           C  
ANISOU 1029  CG1 VAL A 180    10735   8426   5812    571    774   -198       C  
ATOM   1030  CG2 VAL A 180      14.376   9.325   1.178  1.00 56.77           C  
ANISOU 1030  CG2 VAL A 180     9268   7264   5038    526    471   -153       C  
ATOM   1031  H   VAL A 180      17.045   8.505   1.922  1.00 74.56           H  
ATOM   1032  HA  VAL A 180      17.256  10.834   0.534  1.00 69.23           H  
ATOM   1033  HB  VAL A 180      15.167  10.546  -0.241  1.00 69.90           H  
ATOM   1034 HG11 VAL A 180      15.141   8.421  -1.210  1.00 78.87           H  
ATOM   1035 HG12 VAL A 180      16.602   9.039  -1.287  1.00 78.87           H  
ATOM   1036 HG13 VAL A 180      16.260   7.943  -0.189  1.00 78.87           H  
ATOM   1037 HG21 VAL A 180      13.643   9.006   0.629  1.00 68.13           H  
ATOM   1038 HG22 VAL A 180      14.704   8.607   1.743  1.00 68.13           H  
ATOM   1039 HG23 VAL A 180      14.079  10.068   1.727  1.00 68.13           H  
ATOM   1040  N   PRO A 181      16.200  12.402   2.203  1.00 54.20           N  
ANISOU 1040  N   PRO A 181     9072   6837   4682    461    777    424       N  
ATOM   1041  CA  PRO A 181      15.731  13.215   3.331  1.00 51.88           C  
ANISOU 1041  CA  PRO A 181     8657   6501   4553    431    684    520       C  
ATOM   1042  C   PRO A 181      14.211  13.224   3.420  1.00 49.83           C  
ANISOU 1042  C   PRO A 181     8353   6279   4303    517    404    415       C  
ATOM   1043  O   PRO A 181      13.499  12.819   2.502  1.00 49.73           O  
ANISOU 1043  O   PRO A 181     8431   6335   4132    605    261    284       O  
ATOM   1044  CB  PRO A 181      16.276  14.613   3.010  1.00 53.23           C  
ANISOU 1044  CB  PRO A 181     9032   6632   4563    441    780    714       C  
ATOM   1045  CG  PRO A 181      16.320  14.643   1.497  1.00 53.83           C  
ANISOU 1045  CG  PRO A 181     9376   6756   4321    544    792    692       C  
ATOM   1046  CD  PRO A 181      16.644  13.228   1.058  1.00 53.76           C  
ANISOU 1046  CD  PRO A 181     9305   6796   4327    527    858    528       C  
ATOM   1047  HA  PRO A 181      16.106  12.898   4.167  1.00 62.25           H  
ATOM   1048  HB2 PRO A 181      15.678  15.293   3.358  1.00 63.88           H  
ATOM   1049  HB3 PRO A 181      17.161  14.723   3.391  1.00 63.88           H  
ATOM   1050  HG2 PRO A 181      15.458  14.921   1.151  1.00 64.60           H  
ATOM   1051  HG3 PRO A 181      17.009  15.259   1.204  1.00 64.60           H  
ATOM   1052  HD2 PRO A 181      16.153  12.995   0.255  1.00 64.52           H  
ATOM   1053  HD3 PRO A 181      17.597  13.123   0.907  1.00 64.52           H  
ATOM   1054  N   PHE A 182      13.725  13.699   4.564  1.00 47.75           N  
ANISOU 1054  N   PHE A 182     7937   5976   4229    490    327    469       N  
ATOM   1055  CA  PHE A 182      12.299  13.932   4.728  1.00 49.35           C  
ANISOU 1055  CA  PHE A 182     8089   6213   4448    578     76    403       C  
ATOM   1056  C   PHE A 182      11.869  15.163   3.934  1.00 54.58           C  
ANISOU 1056  C   PHE A 182     8993   6891   4854    710    -23    503       C  
ATOM   1057  O   PHE A 182      12.549  16.192   3.941  1.00 51.17           O  
ANISOU 1057  O   PHE A 182     8707   6391   4345    699    104    674       O  
ATOM   1058  CB  PHE A 182      11.952  14.139   6.202  1.00 47.70           C  
ANISOU 1058  CB  PHE A 182     7662   5954   4507    520     48    445       C  
ATOM   1059  CG  PHE A 182      12.057  12.894   7.035  1.00 46.21           C  
ANISOU 1059  CG  PHE A 182     7227   5758   4574    425    101    342       C  
ATOM   1060  CD1 PHE A 182      10.989  12.015   7.131  1.00 44.34           C  
ANISOU 1060  CD1 PHE A 182     6844   5560   4445    445    -53    175       C  
ATOM   1061  CD2 PHE A 182      13.222  12.606   7.730  1.00 42.20           C  
ANISOU 1061  CD2 PHE A 182     6629   5205   4200    317    309    415       C  
ATOM   1062  CE1 PHE A 182      11.085  10.871   7.893  1.00 42.69           C  
ANISOU 1062  CE1 PHE A 182     6427   5321   4471    360     17     92       C  
ATOM   1063  CE2 PHE A 182      13.320  11.466   8.495  1.00 41.95           C  
ANISOU 1063  CE2 PHE A 182     6386   5163   4392    251    365    338       C  
ATOM   1064  CZ  PHE A 182      12.249  10.593   8.573  1.00 42.47           C  
ANISOU 1064  CZ  PHE A 182     6330   5244   4563    273    228    180       C  
ATOM   1065  H   PHE A 182      14.199  13.892   5.255  1.00 57.30           H  
ATOM   1066  HA  PHE A 182      11.813  13.158   4.404  1.00 59.22           H  
ATOM   1067  HB2 PHE A 182      12.560  14.796   6.576  1.00 57.24           H  
ATOM   1068  HB3 PHE A 182      11.039  14.460   6.265  1.00 57.24           H  
ATOM   1069  HD1 PHE A 182      10.200  12.199   6.675  1.00 53.21           H  
ATOM   1070  HD2 PHE A 182      13.945  13.189   7.678  1.00 50.64           H  
ATOM   1071  HE1 PHE A 182      10.363  10.287   7.948  1.00 51.23           H  
ATOM   1072  HE2 PHE A 182      14.105  11.283   8.960  1.00 50.35           H  
ATOM   1073  HZ  PHE A 182      12.316   9.818   9.084  1.00 50.96           H  
ATOM   1074  N   ASP A 183      10.734  15.048   3.237  1.00 58.46           N  
ANISOU 1074  N   ASP A 183     9526   7472   5213    835   -251    394       N  
ATOM   1075  CA  ASP A 183      10.080  16.232   2.694  1.00 59.87           C  
ANISOU 1075  CA  ASP A 183     9894   7672   5182    991   -385    496       C  
ATOM   1076  C   ASP A 183       9.904  17.282   3.783  1.00 58.72           C  
ANISOU 1076  C   ASP A 183     9694   7431   5186    986   -373    642       C  
ATOM   1077  O   ASP A 183      10.242  18.457   3.601  1.00 56.30           O  
ANISOU 1077  O   ASP A 183     9589   7051   4752   1034   -298    814       O  
ATOM   1078  CB  ASP A 183       8.721  15.872   2.092  1.00 66.63           C  
ANISOU 1078  CB  ASP A 183    10714   8661   5942   1122   -669    340       C  
ATOM   1079  CG  ASP A 183       8.835  15.272   0.708  1.00 82.09           C  
ANISOU 1079  CG  ASP A 183    12837  10721   7634   1178   -706    225       C  
ATOM   1080  OD1 ASP A 183       7.900  14.552   0.295  1.00 86.76           O  
ANISOU 1080  OD1 ASP A 183    13338  11429   8197   1223   -916     33       O  
ATOM   1081  OD2 ASP A 183       9.859  15.508   0.035  1.00 97.76           O  
ANISOU 1081  OD2 ASP A 183    15037  12670   9437   1171   -522    319       O  
ATOM   1082  H   ASP A 183      10.331  14.307   3.070  1.00 70.15           H  
ATOM   1083  HA  ASP A 183      10.631  16.594   1.983  1.00 71.84           H  
ATOM   1084  HB2 ASP A 183       8.283  15.224   2.665  1.00 79.96           H  
ATOM   1085  HB3 ASP A 183       8.181  16.676   2.027  1.00 79.96           H  
ATOM   1086  N   SER A 184       9.376  16.854   4.938  1.00 64.94           N  
ANISOU 1086  N   SER A 184    10218   8209   6248    923   -434    573       N  
ATOM   1087  CA  SER A 184       9.134  17.731   6.067  1.00 61.25           C  
ANISOU 1087  CA  SER A 184     9678   7657   5936    916   -428    683       C  
ATOM   1088  C   SER A 184      10.170  17.398   7.131  1.00 61.04           C  
ANISOU 1088  C   SER A 184     9512   7552   6127    735   -224    719       C  
ATOM   1089  O   SER A 184      11.299  17.915   7.069  1.00 59.67           O  
ANISOU 1089  O   SER A 184     9465   7310   5898    660    -36    838       O  
ATOM   1090  CB  SER A 184       7.686  17.569   6.555  1.00 61.98           C  
ANISOU 1090  CB  SER A 184     9583   7812   6154   1002   -655    586       C  
ATOM   1091  OG  SER A 184       7.583  17.808   7.946  1.00 64.35           O  
ANISOU 1091  OG  SER A 184     9714   8039   6698    935   -609    630       O  
ATOM   1092  H   SER A 184       9.147  16.039   5.086  1.00 77.93           H  
ATOM   1093  HA  SER A 184       9.267  18.648   5.781  1.00 73.50           H  
ATOM   1094  HB2 SER A 184       7.123  18.203   6.084  1.00 74.37           H  
ATOM   1095  HB3 SER A 184       7.392  16.663   6.370  1.00 74.37           H  
ATOM   1096  HG  SER A 184       6.791  17.688   8.200  1.00 77.22           H  
ATOM   1097  N   GLU A 185       9.858  16.557   8.110  1.00 59.19           N  
ANISOU 1097  N   GLU A 185     9020   7332   6138    662   -248    624       N  
ATOM   1098  CA  GLU A 185      10.850  16.126   9.084  1.00 55.76           C  
ANISOU 1098  CA  GLU A 185     8447   6847   5893    509    -65    654       C  
ATOM   1099  C   GLU A 185      10.320  14.892   9.795  1.00 49.63           C  
ANISOU 1099  C   GLU A 185     7411   6106   5340    466   -115    518       C  
ATOM   1100  O   GLU A 185       9.135  14.564   9.716  1.00 52.08           O  
ANISOU 1100  O   GLU A 185     7634   6466   5689    537   -289    412       O  
ATOM   1101  CB  GLU A 185      11.180  17.232  10.094  1.00 56.42           C  
ANISOU 1101  CB  GLU A 185     8541   6843   6054    464     11    795       C  
ATOM   1102  CG  GLU A 185       9.978  17.781  10.846  1.00 55.68           C  
ANISOU 1102  CG  GLU A 185     8368   6733   6053    547   -141    793       C  
ATOM   1103  CD  GLU A 185      10.347  18.919  11.775  1.00 55.90           C  
ANISOU 1103  CD  GLU A 185     8441   6662   6135    501    -56    921       C  
ATOM   1104  OE1 GLU A 185      11.270  18.742  12.603  1.00 55.42           O  
ANISOU 1104  OE1 GLU A 185     8287   6576   6196    364     86    951       O  
ATOM   1105  OE2 GLU A 185       9.721  19.995  11.671  1.00 56.38           O  
ANISOU 1105  OE2 GLU A 185     8636   6673   6113    607   -132    987       O  
ATOM   1106  H   GLU A 185       9.075  16.222   8.232  1.00 71.03           H  
ATOM   1107  HA  GLU A 185      11.669  15.889   8.622  1.00 66.91           H  
ATOM   1108  HB2 GLU A 185      11.798  16.876  10.751  1.00 67.71           H  
ATOM   1109  HB3 GLU A 185      11.591  17.972   9.619  1.00 67.71           H  
ATOM   1110  HG2 GLU A 185       9.329  18.113  10.206  1.00 66.81           H  
ATOM   1111  HG3 GLU A 185       9.586  17.072  11.378  1.00 66.81           H  
ATOM   1112  N   LEU A 186      11.223  14.207  10.484  1.00 42.93           N  
ANISOU 1112  N   LEU A 186     6437   5233   4641    349     45    527       N  
ATOM   1113  CA  LEU A 186      10.849  13.044  11.273  1.00 35.24           C  
ANISOU 1113  CA  LEU A 186     5228   4269   3893    304     38    425       C  
ATOM   1114  C   LEU A 186       9.815  13.429  12.321  1.00 36.43           C  
ANISOU 1114  C   LEU A 186     5242   4408   4191    335    -74    432       C  
ATOM   1115  O   LEU A 186      10.070  14.285  13.170  1.00 37.34           O  
ANISOU 1115  O   LEU A 186     5359   4482   4348    315    -27    545       O  
ATOM   1116  CB  LEU A 186      12.096  12.465  11.932  1.00 34.92           C  
ANISOU 1116  CB  LEU A 186     5094   4204   3971    196    241    478       C  
ATOM   1117  CG  LEU A 186      11.949  11.210  12.768  1.00 32.10           C  
ANISOU 1117  CG  LEU A 186     4515   3839   3842    152    283    403       C  
ATOM   1118  CD1 LEU A 186      11.226  10.114  12.005  1.00 34.97           C  
ANISOU 1118  CD1 LEU A 186     4853   4219   4216    179    205    231       C  
ATOM   1119  CD2 LEU A 186      13.340  10.751  13.196  1.00 33.03           C  
ANISOU 1119  CD2 LEU A 186     4577   3950   4022     75    487    477       C  
ATOM   1120  H   LEU A 186      12.061  14.396  10.512  1.00 51.52           H  
ATOM   1121  HA  LEU A 186      10.458  12.366  10.700  1.00 42.29           H  
ATOM   1122  HB2 LEU A 186      12.730  12.256  11.228  1.00 41.91           H  
ATOM   1123  HB3 LEU A 186      12.462  13.146  12.517  1.00 41.91           H  
ATOM   1124  HG  LEU A 186      11.412  11.396  13.554  1.00 38.52           H  
ATOM   1125 HD11 LEU A 186      11.226   9.304  12.539  1.00 41.97           H  
ATOM   1126 HD12 LEU A 186      10.315  10.397  11.833  1.00 41.97           H  
ATOM   1127 HD13 LEU A 186      11.687   9.957  11.166  1.00 41.97           H  
ATOM   1128 HD21 LEU A 186      13.256   9.950  13.737  1.00 39.63           H  
ATOM   1129 HD22 LEU A 186      13.867  10.562  12.404  1.00 39.63           H  
ATOM   1130 HD23 LEU A 186      13.760  11.457  13.712  1.00 39.63           H  
ATOM   1131  N   GLU A 187       8.644  12.799  12.260  1.00 41.66           N  
ANISOU 1131  N   GLU A 187     5786   5107   4935    380   -216    303       N  
ATOM   1132  CA AGLU A 187       7.597  13.097  13.228  0.55 42.55           C  
ANISOU 1132  CA AGLU A 187     5754   5217   5197    416   -313    303       C  
ATOM   1133  CA BGLU A 187       7.592  13.087  13.224  0.45 45.48           C  
ANISOU 1133  CA BGLU A 187     6124   5588   5569    416   -313    302       C  
ATOM   1134  C   GLU A 187       7.929  12.473  14.579  1.00 38.78           C  
ANISOU 1134  C   GLU A 187     5088   4698   4949    328   -186    328       C  
ATOM   1135  O   GLU A 187       8.594  11.434  14.669  1.00 37.97           O  
ANISOU 1135  O   GLU A 187     4916   4582   4927    253    -67    293       O  
ATOM   1136  CB AGLU A 187       6.247  12.585  12.740  0.55 45.28           C  
ANISOU 1136  CB AGLU A 187     6004   5627   5572    481   -499    152       C  
ATOM   1137  CB BGLU A 187       6.253  12.556  12.723  0.45 48.49           C  
ANISOU 1137  CB BGLU A 187     6411   6035   5979    479   -498    149       C  
ATOM   1138  CG AGLU A 187       5.094  12.910  13.687  0.55 45.95           C  
ANISOU 1138  CG AGLU A 187     5925   5718   5814    530   -595    152       C  
ATOM   1139  CG BGLU A 187       5.843  13.076  11.346  0.45 45.48           C  
ANISOU 1139  CG BGLU A 187     6206   5722   5353    586   -650    112       C  
ATOM   1140  CD AGLU A 187       4.993  14.396  14.003  0.55 45.63           C  
ANISOU 1140  CD AGLU A 187     6002   5651   5682    618   -623    292       C  
ATOM   1141  CD BGLU A 187       5.578  14.576  11.331  0.45 45.53           C  
ANISOU 1141  CD BGLU A 187     6355   5718   5227    701   -717    248       C  
ATOM   1142  OE1AGLU A 187       4.659  15.177  13.087  0.55 49.49           O  
ANISOU 1142  OE1AGLU A 187     6650   6175   5981    728   -739    313       O  
ATOM   1143  OE1BGLU A 187       4.994  15.092  12.303  0.45 48.27           O  
ANISOU 1143  OE1BGLU A 187     6600   6039   5701    732   -744    298       O  
ATOM   1144  OE2AGLU A 187       5.262  14.784  15.162  0.55 40.55           O  
ANISOU 1144  OE2AGLU A 187     5308   4949   5150    582   -526    383       O  
ATOM   1145  OE2BGLU A 187       5.963  15.239  10.345  0.45 48.51           O  
ANISOU 1145  OE2BGLU A 187     6957   6104   5369    765   -730    307       O  
ATOM   1146  H  AGLU A 187       8.435  12.203  11.676  0.55 49.99           H  
ATOM   1147  H  BGLU A 187       8.437  12.205  11.674  0.45 49.99           H  
ATOM   1148  HA AGLU A 187       7.529  14.058  13.339  0.55 51.06           H  
ATOM   1149  HA BGLU A 187       7.509  14.047  13.339  0.45 54.58           H  
ATOM   1150  HB2AGLU A 187       6.050  12.991  11.881  0.55 54.34           H  
ATOM   1151  HB2BGLU A 187       6.304  11.589  12.667  0.45 58.19           H  
ATOM   1152  HB3AGLU A 187       6.293  11.620  12.648  0.55 54.34           H  
ATOM   1153  HB3BGLU A 187       5.562  12.816  13.352  0.45 58.19           H  
ATOM   1154  HG2AGLU A 187       4.260  12.633  13.277  0.55 55.13           H  
ATOM   1155  HG2BGLU A 187       6.556  12.892  10.714  0.45 54.58           H  
ATOM   1156  HG3AGLU A 187       5.227  12.435  14.522  0.55 55.13           H  
ATOM   1157  HG3BGLU A 187       5.030  12.626  11.068  0.45 54.58           H  
ATOM   1158  N   ILE A 188       7.461  13.132  15.642  1.00 39.55           N  
ANISOU 1158  N   ILE A 188     5112   4774   5141    350   -206    395       N  
ATOM   1159  CA  ILE A 188       7.708  12.652  16.996  1.00 38.41           C  
ANISOU 1159  CA  ILE A 188     4802   4601   5191    284    -94    431       C  
ATOM   1160  C   ILE A 188       7.038  11.302  17.191  1.00 40.21           C  
ANISOU 1160  C   ILE A 188     4842   4836   5598    261   -101    312       C  
ATOM   1161  O   ILE A 188       5.866  11.106  16.835  1.00 37.52           O  
ANISOU 1161  O   ILE A 188     4436   4525   5297    308   -236    208       O  
ATOM   1162  CB  ILE A 188       7.210  13.684  18.018  1.00 40.03           C  
ANISOU 1162  CB  ILE A 188     4986   4784   5437    327   -125    511       C  
ATOM   1163  CG1 ILE A 188       8.244  14.799  18.170  1.00 39.56           C  
ANISOU 1163  CG1 ILE A 188     5088   4690   5253    295    -46    635       C  
ATOM   1164  CG2 ILE A 188       6.919  13.025  19.357  1.00 38.44           C  
ANISOU 1164  CG2 ILE A 188     4584   4574   5447    294    -58    510       C  
ATOM   1165  CD1 ILE A 188       7.649  16.180  18.280  1.00 46.67           C  
ANISOU 1165  CD1 ILE A 188     6104   5554   6073    377   -128    692       C  
ATOM   1166  H   ILE A 188       6.999  13.857  15.604  1.00 47.46           H  
ATOM   1167  HA  ILE A 188       8.663  12.533  17.120  1.00 46.09           H  
ATOM   1168  HB  ILE A 188       6.380  14.068  17.693  1.00 48.03           H  
ATOM   1169 HG12 ILE A 188       8.761  14.636  18.974  1.00 47.47           H  
ATOM   1170 HG13 ILE A 188       8.826  14.791  17.394  1.00 47.47           H  
ATOM   1171 HG21 ILE A 188       6.654  13.707  19.994  1.00 46.13           H  
ATOM   1172 HG22 ILE A 188       6.202  12.382  19.243  1.00 46.13           H  
ATOM   1173 HG23 ILE A 188       7.720  12.575  19.668  1.00 46.13           H  
ATOM   1174 HD11 ILE A 188       8.366  16.827  18.373  1.00 56.00           H  
ATOM   1175 HD12 ILE A 188       7.136  16.368  17.478  1.00 56.00           H  
ATOM   1176 HD13 ILE A 188       7.070  16.213  19.058  1.00 56.00           H  
ATOM   1177  N   GLY A 189       7.774  10.372  17.785  1.00 31.38           N  
ANISOU 1177  N   GLY A 189     3633   3691   4599    188     48    328       N  
ATOM   1178  CA  GLY A 189       7.292   9.026  18.013  1.00 37.18           C  
ANISOU 1178  CA  GLY A 189     4209   4402   5517    155     84    228       C  
ATOM   1179  C   GLY A 189       7.599   8.029  16.922  1.00 36.63           C  
ANISOU 1179  C   GLY A 189     4183   4322   5412    121    108    114       C  
ATOM   1180  O   GLY A 189       7.251   6.848  17.072  1.00 35.00           O  
ANISOU 1180  O   GLY A 189     3859   4074   5366     81    156     21       O  
ATOM   1181  H   GLY A 189       8.575  10.503  18.070  1.00 37.66           H  
ATOM   1182  HA2 GLY A 189       7.688   8.693  18.834  1.00 44.62           H  
ATOM   1183  HA3 GLY A 189       6.328   9.059  18.118  1.00 44.62           H  
ATOM   1184  N   TYR A 190       8.258   8.451  15.842  1.00 35.78           N  
ANISOU 1184  N   TYR A 190     4252   4242   5101    135     93    118       N  
ATOM   1185  CA  TYR A 190       8.461   7.623  14.661  1.00 36.88           C  
ANISOU 1185  CA  TYR A 190     4465   4381   5168    118     99     -7       C  
ATOM   1186  C   TYR A 190       9.936   7.580  14.282  1.00 36.76           C  
ANISOU 1186  C   TYR A 190     4568   4357   5042     95    256     73       C  
ATOM   1187  O   TYR A 190      10.777   8.264  14.870  1.00 30.06           O  
ANISOU 1187  O   TYR A 190     3741   3515   4166     85    342    219       O  
ATOM   1188  CB  TYR A 190       7.597   8.139  13.516  1.00 40.79           C  
ANISOU 1188  CB  TYR A 190     5062   4939   5498    177    -99   -106       C  
ATOM   1189  CG  TYR A 190       6.126   8.020  13.828  1.00 44.44           C  
ANISOU 1189  CG  TYR A 190     5371   5425   6090    197   -253   -205       C  
ATOM   1190  CD1 TYR A 190       5.456   6.821  13.625  1.00 50.31           C  
ANISOU 1190  CD1 TYR A 190     5992   6151   6972    143   -279   -378       C  
ATOM   1191  CD2 TYR A 190       5.413   9.085  14.352  1.00 45.77           C  
ANISOU 1191  CD2 TYR A 190     5508   5626   6255    265   -359   -129       C  
ATOM   1192  CE1 TYR A 190       4.110   6.694  13.918  1.00 46.46           C  
ANISOU 1192  CE1 TYR A 190     5338   5694   6621    147   -412   -473       C  
ATOM   1193  CE2 TYR A 190       4.066   8.966  14.651  1.00 45.19           C  
ANISOU 1193  CE2 TYR A 190     5272   5585   6312    289   -490   -217       C  
ATOM   1194  CZ  TYR A 190       3.425   7.762  14.431  1.00 48.31           C  
ANISOU 1194  CZ  TYR A 190     5529   5976   6849    224   -517   -389       C  
ATOM   1195  OH  TYR A 190       2.086   7.626  14.719  1.00 49.60           O  
ANISOU 1195  OH  TYR A 190     5509   6180   7157    234   -640   -482       O  
ATOM   1196  H   TYR A 190       8.604   9.234  15.772  1.00 42.94           H  
ATOM   1197  HA  TYR A 190       8.213   6.705  14.852  1.00 44.26           H  
ATOM   1198  HB2 TYR A 190       7.800   9.075  13.359  1.00 48.95           H  
ATOM   1199  HB3 TYR A 190       7.782   7.621  12.717  1.00 48.95           H  
ATOM   1200  HD1 TYR A 190       5.920   6.090  13.287  1.00 60.37           H  
ATOM   1201  HD2 TYR A 190       5.846   9.893  14.506  1.00 54.92           H  
ATOM   1202  HE1 TYR A 190       3.672   5.888  13.766  1.00 55.75           H  
ATOM   1203  HE2 TYR A 190       3.597   9.691  14.997  1.00 54.23           H  
ATOM   1204  HH  TYR A 190       1.785   8.345  15.033  1.00 59.52           H  
ATOM   1205  N   ASP A 191      10.245   6.745  13.286  1.00 32.71           N  
ANISOU 1205  N   ASP A 191     4516   4323   3589   -179   -252    501       N  
ATOM   1206  CA  ASP A 191      11.600   6.271  13.057  1.00 31.31           C  
ANISOU 1206  CA  ASP A 191     4332   4121   3442   -235   -111    399       C  
ATOM   1207  C   ASP A 191      12.206   6.766  11.742  1.00 33.51           C  
ANISOU 1207  C   ASP A 191     4694   4426   3613   -339     -7    464       C  
ATOM   1208  O   ASP A 191      11.511   6.986  10.745  1.00 31.12           O  
ANISOU 1208  O   ASP A 191     4479   4200   3143   -388    -43    568       O  
ATOM   1209  CB  ASP A 191      11.620   4.740  13.085  1.00 30.89           C  
ANISOU 1209  CB  ASP A 191     4271   4118   3348   -248    -88    272       C  
ATOM   1210  CG  ASP A 191      11.192   4.172  14.431  1.00 30.84           C  
ANISOU 1210  CG  ASP A 191     4179   4086   3453   -156   -168    224       C  
ATOM   1211  OD1 ASP A 191      11.131   4.955  15.399  1.00 34.28           O  
ANISOU 1211  OD1 ASP A 191     4552   4476   3995    -80   -220    256       O  
ATOM   1212  OD2 ASP A 191      10.920   2.953  14.520  1.00 28.67           O  
ANISOU 1212  OD2 ASP A 191     3902   3836   3157   -164   -178    155       O  
ATOM   1213  H   ASP A 191       9.672   6.438  12.723  1.00 39.25           H  
ATOM   1214  HA  ASP A 191      12.167   6.632  13.756  1.00 37.57           H  
ATOM   1215  HB2 ASP A 191      11.010   4.403  12.410  1.00 37.07           H  
ATOM   1216  HB3 ASP A 191      12.521   4.431  12.902  1.00 37.07           H  
ATOM   1217  N   GLY A 192      13.518   6.932  11.770  1.00 30.65           N  
ANISOU 1217  N   GLY A 192     4292   4013   3342   -372    121    408       N  
ATOM   1218  CA  GLY A 192      14.289   7.238  10.585  1.00 33.02           C  
ANISOU 1218  CA  GLY A 192     4649   4352   3544   -479    258    452       C  
ATOM   1219  C   GLY A 192      15.727   6.791  10.845  1.00 36.11           C  
ANISOU 1219  C   GLY A 192     4950   4715   4054   -495    404    316       C  
ATOM   1220  O   GLY A 192      15.979   5.866  11.624  1.00 33.03           O  
ANISOU 1220  O   GLY A 192     4484   4309   3757   -430    395    180       O  
ATOM   1221  H   GLY A 192      13.995   6.871  12.483  1.00 36.78           H  
ATOM   1222  HA2 GLY A 192      13.935   6.764   9.816  1.00 39.62           H  
ATOM   1223  HA3 GLY A 192      14.272   8.191  10.404  1.00 39.62           H  
ATOM   1224  N   VAL A 193      16.680   7.471  10.198  1.00 39.68           N  
ANISOU 1224  N   VAL A 193     5400   5163   4513   -582    538    367       N  
ATOM   1225  CA  VAL A 193      18.095   7.227  10.442  1.00 34.34           C  
ANISOU 1225  CA  VAL A 193     4609   4466   3974   -600    679    254       C  
ATOM   1226  C   VAL A 193      18.778   8.523  10.847  1.00 35.14           C  
ANISOU 1226  C   VAL A 193     4642   4460   4250   -639    697    334       C  
ATOM   1227  O   VAL A 193      18.334   9.623  10.494  1.00 36.56           O  
ANISOU 1227  O   VAL A 193     4894   4590   4406   -684    658    496       O  
ATOM   1228  CB  VAL A 193      18.824   6.615   9.213  1.00 40.35           C  
ANISOU 1228  CB  VAL A 193     5400   5345   4586   -686    869    198       C  
ATOM   1229  CG1 VAL A 193      18.353   5.193   8.961  1.00 43.72           C  
ANISOU 1229  CG1 VAL A 193     5874   5846   4890   -643    859     60       C  
ATOM   1230  CG2 VAL A 193      18.613   7.488   7.987  1.00 43.47           C  
ANISOU 1230  CG2 VAL A 193     5912   5807   4798   -799    928    374       C  
ATOM   1231  H   VAL A 193      16.525   8.080   9.612  1.00 47.62           H  
ATOM   1232  HA  VAL A 193      18.156   6.600  11.180  1.00 41.21           H  
ATOM   1233  HB  VAL A 193      19.776   6.580   9.395  1.00 48.42           H  
ATOM   1234 HG11 VAL A 193      18.832   4.833   8.199  1.00 52.46           H  
ATOM   1235 HG12 VAL A 193      18.534   4.657   9.749  1.00 52.46           H  
ATOM   1236 HG13 VAL A 193      17.401   5.204   8.780  1.00 52.46           H  
ATOM   1237 HG21 VAL A 193      19.051   7.075   7.226  1.00 52.17           H  
ATOM   1238 HG22 VAL A 193      17.662   7.569   7.817  1.00 52.17           H  
ATOM   1239 HG23 VAL A 193      18.995   8.364   8.154  1.00 52.17           H  
ATOM   1240  N   PHE A 194      19.883   8.384  11.576  1.00 41.21           N  
ANISOU 1240  N   PHE A 194     5266   5187   5206   -624    753    221       N  
ATOM   1241  CA  PHE A 194      20.727   9.497  11.987  1.00 39.74           C  
ANISOU 1241  CA  PHE A 194     4988   4901   5210   -681    781    258       C  
ATOM   1242  C   PHE A 194      22.110   9.288  11.393  1.00 42.50           C  
ANISOU 1242  C   PHE A 194     5239   5311   5598   -770    981    207       C  
ATOM   1243  O   PHE A 194      22.724   8.237  11.597  1.00 40.81           O  
ANISOU 1243  O   PHE A 194     4931   5160   5416   -718   1042     60       O  
ATOM   1244  CB  PHE A 194      20.803   9.597  13.510  1.00 40.36           C  
ANISOU 1244  CB  PHE A 194     4956   4894   5485   -584    645    160       C  
ATOM   1245  CG  PHE A 194      21.632  10.745  14.004  1.00 39.35           C  
ANISOU 1245  CG  PHE A 194     4733   4656   5563   -650    651    170       C  
ATOM   1246  CD1 PHE A 194      21.111  12.025  14.042  1.00 44.51           C  
ANISOU 1246  CD1 PHE A 194     5458   5184   6269   -685    580    287       C  
ATOM   1247  CD2 PHE A 194      22.930  10.541  14.438  1.00 45.72           C  
ANISOU 1247  CD2 PHE A 194     5369   5476   6526   -675    722     57       C  
ATOM   1248  CE1 PHE A 194      21.878  13.087  14.495  1.00 49.22           C  
ANISOU 1248  CE1 PHE A 194     5970   5655   7075   -759    582    282       C  
ATOM   1249  CE2 PHE A 194      23.703  11.596  14.890  1.00 44.44           C  
ANISOU 1249  CE2 PHE A 194     5108   5213   6562   -755    718     54       C  
ATOM   1250  CZ  PHE A 194      23.173  12.871  14.922  1.00 47.03           C  
ANISOU 1250  CZ  PHE A 194     5521   5402   6946   -803    649    160       C  
ATOM   1251  H   PHE A 194      20.174   7.624  11.853  1.00 49.46           H  
ATOM   1252  HA  PHE A 194      20.367  10.335  11.656  1.00 47.68           H  
ATOM   1253  HB2 PHE A 194      19.906   9.708  13.861  1.00 48.43           H  
ATOM   1254  HB3 PHE A 194      21.195   8.780  13.856  1.00 48.43           H  
ATOM   1255  HD1 PHE A 194      20.238  12.175  13.761  1.00 53.41           H  
ATOM   1256  HD2 PHE A 194      23.287   9.682  14.426  1.00 54.86           H  
ATOM   1257  HE1 PHE A 194      21.520  13.945  14.511  1.00 59.06           H  
ATOM   1258  HE2 PHE A 194      24.577  11.447  15.171  1.00 53.32           H  
ATOM   1259  HZ  PHE A 194      23.687  13.582  15.231  1.00 56.44           H  
ATOM   1260  N   ARG A 195      22.593  10.281  10.659  1.00 44.32           N  
ANISOU 1260  N   ARG A 195     5484   5520   5835   -902   1088    335       N  
ATOM   1261  CA  ARG A 195      23.892  10.215   9.996  1.00 44.97           C  
ANISOU 1261  CA  ARG A 195     5464   5676   5947  -1007   1302    310       C  
ATOM   1262  C   ARG A 195      24.808  11.261  10.632  1.00 45.23           C  
ANISOU 1262  C   ARG A 195     5356   5590   6240  -1084   1309    329       C  
ATOM   1263  O   ARG A 195      24.712  12.455  10.327  1.00 44.91           O  
ANISOU 1263  O   ARG A 195     5372   5452   6240  -1188   1310    490       O  
ATOM   1264  CB  ARG A 195      23.751  10.441   8.492  1.00 46.91           C  
ANISOU 1264  CB  ARG A 195     5841   6026   5957  -1121   1448    456       C  
ATOM   1265  CG  ARG A 195      25.093  10.526   7.770  1.00 57.00           C  
ANISOU 1265  CG  ARG A 195     7007   7391   7258  -1245   1692    452       C  
ATOM   1266  CD  ARG A 195      24.967  10.123   6.312  1.00 63.93           C  
ANISOU 1266  CD  ARG A 195     8007   8449   7833  -1313   1856    509       C  
ATOM   1267  NE  ARG A 195      24.424  11.187   5.478  1.00 72.31           N  
ANISOU 1267  NE  ARG A 195     9220   9503   8751  -1426   1857    764       N  
ATOM   1268  CZ  ARG A 195      23.924  11.003   4.263  1.00 81.17           C  
ANISOU 1268  CZ  ARG A 195    10498  10780   9563  -1475   1926    858       C  
ATOM   1269  NH1 ARG A 195      23.835   9.797   3.729  1.00 89.06           N  
ANISOU 1269  NH1 ARG A 195    11534  11946  10359  -1426   1998    697       N  
ATOM   1270  NH2 ARG A 195      23.500  12.056   3.569  1.00 87.11           N  
ANISOU 1270  NH2 ARG A 195    11376  11517  10207  -1575   1918   1121       N  
ATOM   1271  H   ARG A 195      22.177  11.022  10.526  1.00 53.18           H  
ATOM   1272  HA  ARG A 195      24.279   9.338  10.141  1.00 53.97           H  
ATOM   1273  HB2 ARG A 195      23.252   9.703   8.109  1.00 56.30           H  
ATOM   1274  HB3 ARG A 195      23.278  11.274   8.342  1.00 56.30           H  
ATOM   1275  HG2 ARG A 195      25.420  11.438   7.807  1.00 68.40           H  
ATOM   1276  HG3 ARG A 195      25.726   9.928   8.197  1.00 68.40           H  
ATOM   1277  HD2 ARG A 195      25.845   9.893   5.970  1.00 76.71           H  
ATOM   1278  HD3 ARG A 195      24.374   9.358   6.245  1.00 76.71           H  
ATOM   1279  HE  ARG A 195      24.428  11.986   5.794  1.00 86.77           H  
ATOM   1280 HH11 ARG A 195      24.104   9.110   4.171  1.00106.87           H  
ATOM   1281 HH12 ARG A 195      23.507   9.699   2.940  1.00106.87           H  
ATOM   1282 HH21 ARG A 195      23.553  12.845   3.909  1.00104.54           H  
ATOM   1283 HH22 ARG A 195      23.174  11.949   2.781  1.00104.54           H  
ATOM   1284  N   ASP A 196      25.695  10.798  11.521  1.00 49.22           N  
ANISOU 1284  N   ASP A 196     5674   6098   6930  -1034   1304    166       N  
ATOM   1285  CA  ASP A 196      26.625  11.697  12.191  1.00 58.59           C  
ANISOU 1285  CA  ASP A 196     6703   7186   8372  -1114   1296    151       C  
ATOM   1286  C   ASP A 196      27.874  11.961  11.359  1.00 59.80           C  
ANISOU 1286  C   ASP A 196     6734   7406   8579  -1268   1525    187       C  
ATOM   1287  O   ASP A 196      28.644  12.864  11.700  1.00 54.94           O  
ANISOU 1287  O   ASP A 196     5996   6705   8175  -1379   1538    207       O  
ATOM   1288  CB  ASP A 196      27.029  11.127  13.549  1.00 56.64           C  
ANISOU 1288  CB  ASP A 196     6296   6935   8291   -994   1171    -31       C  
ATOM   1289  CG  ASP A 196      28.015   9.987  13.431  1.00 61.53           C  
ANISOU 1289  CG  ASP A 196     6755   7687   8935   -948   1296   -162       C  
ATOM   1290  OD1 ASP A 196      27.584   8.838  13.199  1.00 61.51           O  
ANISOU 1290  OD1 ASP A 196     6816   7763   8791   -838   1310   -219       O  
ATOM   1291  OD2 ASP A 196      29.233  10.247  13.551  1.00 73.41           O  
ANISOU 1291  OD2 ASP A 196     8063   9212  10616  -1024   1384   -208       O  
ATOM   1292  H   ASP A 196      25.774   9.972  11.749  1.00 59.07           H  
ATOM   1293  HA  ASP A 196      26.180  12.544  12.350  1.00 70.31           H  
ATOM   1294  HB2 ASP A 196      27.443  11.829  14.076  1.00 67.97           H  
ATOM   1295  HB3 ASP A 196      26.238  10.795  14.001  1.00 67.97           H  
ATOM   1296  N   ALA A 197      28.090  11.198  10.296  1.00 53.71           N  
ANISOU 1296  N   ALA A 197     5991   6789   7627  -1281   1706    186       N  
ATOM   1297  CA  ALA A 197      29.222  11.378   9.399  1.00 53.45           C  
ANISOU 1297  CA  ALA A 197     5846   6855   7607  -1424   1954    224       C  
ATOM   1298  C   ALA A 197      28.987  10.512   8.169  1.00 54.38           C  
ANISOU 1298  C   ALA A 197     6078   7148   7437  -1409   2119    224       C  
ATOM   1299  O   ALA A 197      28.164   9.595   8.207  1.00 52.20           O  
ANISOU 1299  O   ALA A 197     5914   6907   7012  -1278   2032    142       O  
ATOM   1300  CB  ALA A 197      30.546  10.997  10.079  1.00 55.25           C  
ANISOU 1300  CB  ALA A 197     5795   7122   8077  -1407   2011     60       C  
ATOM   1301  H   ALA A 197      27.577  10.548  10.065  1.00 64.45           H  
ATOM   1302  HA  ALA A 197      29.280  12.305   9.121  1.00 64.14           H  
ATOM   1303  HB1 ALA A 197      31.274  11.133   9.452  1.00 66.30           H  
ATOM   1304  HB2 ALA A 197      30.673  11.559  10.860  1.00 66.30           H  
ATOM   1305  HB3 ALA A 197      30.508  10.065  10.345  1.00 66.30           H  
ATOM   1306  N   PRO A 198      29.681  10.790   7.068  1.00 56.99           N  
ANISOU 1306  N   PRO A 198     6381   7593   7678  -1551   2358    310       N  
ATOM   1307  CA  PRO A 198      29.570   9.908   5.899  1.00 58.24           C  
ANISOU 1307  CA  PRO A 198     6634   7945   7549  -1536   2532    270       C  
ATOM   1308  C   PRO A 198      29.819   8.460   6.296  1.00 56.55           C  
ANISOU 1308  C   PRO A 198     6327   7796   7363  -1365   2538     14       C  
ATOM   1309  O   PRO A 198      30.747   8.151   7.047  1.00 57.95           O  
ANISOU 1309  O   PRO A 198     6282   7953   7782  -1310   2553   -118       O  
ATOM   1310  CB  PRO A 198      30.652  10.434   4.946  1.00 60.47           C  
ANISOU 1310  CB  PRO A 198     6816   8349   7812  -1713   2812    365       C  
ATOM   1311  CG  PRO A 198      30.796  11.886   5.316  1.00 60.40           C  
ANISOU 1311  CG  PRO A 198     6778   8174   7999  -1858   2744    562       C  
ATOM   1312  CD  PRO A 198      30.559  11.952   6.814  1.00 59.74           C  
ANISOU 1312  CD  PRO A 198     6620   7902   8175  -1744   2484    453       C  
ATOM   1313  HA  PRO A 198      28.702   9.994   5.476  1.00 69.89           H  
ATOM   1314  HB2 PRO A 198      31.482   9.953   5.086  1.00 72.57           H  
ATOM   1315  HB3 PRO A 198      30.362  10.335   4.025  1.00 72.57           H  
ATOM   1316  HG2 PRO A 198      31.689  12.194   5.094  1.00 72.48           H  
ATOM   1317  HG3 PRO A 198      30.135  12.413   4.839  1.00 72.48           H  
ATOM   1318  HD2 PRO A 198      31.395  11.867   7.300  1.00 71.69           H  
ATOM   1319  HD3 PRO A 198      30.117  12.780   7.058  1.00 71.69           H  
ATOM   1320  N   ARG A 199      28.973   7.566   5.790  1.00 54.73           N  
ANISOU 1320  N   ARG A 199     6267   7636   6892  -1279   2515    -54       N  
ATOM   1321  CA  ARG A 199      29.089   6.138   6.060  1.00 61.46           C  
ANISOU 1321  CA  ARG A 199     7066   8525   7762  -1118   2521   -288       C  
ATOM   1322  C   ARG A 199      29.061   5.836   7.556  1.00 58.94           C  
ANISOU 1322  C   ARG A 199     6632   8057   7705   -980   2309   -376       C  
ATOM   1323  O   ARG A 199      29.732   4.909   8.029  1.00 56.32           O  
ANISOU 1323  O   ARG A 199     6147   7733   7520   -863   2342   -547       O  
ATOM   1324  CB  ARG A 199      30.351   5.565   5.407  1.00 61.41           C  
ANISOU 1324  CB  ARG A 199     6894   8667   7773  -1129   2802   -423       C  
ATOM   1325  CG  ARG A 199      30.277   5.526   3.879  1.00 66.57           C  
ANISOU 1325  CG  ARG A 199     7684   9510   8102  -1233   3023   -386       C  
ATOM   1326  CD  ARG A 199      31.505   4.873   3.296  1.00 72.01           C  
ANISOU 1326  CD  ARG A 199     8198  10353   8811  -1220   3311   -551       C  
ATOM   1327  NE  ARG A 199      31.201   3.942   2.216  1.00 78.24           N  
ANISOU 1327  NE  ARG A 199     9129  11294   9304  -1186   3453   -690       N  
ATOM   1328  CZ  ARG A 199      31.149   4.271   0.931  1.00 79.44           C  
ANISOU 1328  CZ  ARG A 199     9402  11635   9146  -1318   3639   -608       C  
ATOM   1329  NH1 ARG A 199      31.307   5.521   0.531  1.00 77.69           N  
ANISOU 1329  NH1 ARG A 199     9193  11458   8868  -1495   3701   -355       N  
ATOM   1330  NH2 ARG A 199      30.930   3.323   0.027  1.00 82.22           N  
ANISOU 1330  NH2 ARG A 199     9872  12132   9237  -1275   3764   -784       N  
ATOM   1331  H   ARG A 199      28.311   7.767   5.278  1.00 65.68           H  
ATOM   1332  HA  ARG A 199      28.322   5.688   5.673  1.00 73.76           H  
ATOM   1333  HB2 ARG A 199      31.110   6.116   5.654  1.00 73.69           H  
ATOM   1334  HB3 ARG A 199      30.483   4.658   5.722  1.00 73.69           H  
ATOM   1335  HG2 ARG A 199      29.499   5.015   3.606  1.00 79.89           H  
ATOM   1336  HG3 ARG A 199      30.218   6.430   3.534  1.00 79.89           H  
ATOM   1337  HD2 ARG A 199      32.089   5.561   2.942  1.00 86.42           H  
ATOM   1338  HD3 ARG A 199      31.960   4.379   3.996  1.00 86.42           H  
ATOM   1339  HE  ARG A 199      31.044   3.122   2.426  1.00 93.89           H  
ATOM   1340 HH11 ARG A 199      31.447   6.143   1.108  1.00 93.23           H  
ATOM   1341 HH12 ARG A 199      31.269   5.712  -0.307  1.00 93.23           H  
ATOM   1342 HH21 ARG A 199      30.823   2.507   0.276  1.00 98.67           H  
ATOM   1343 HH22 ARG A 199      30.894   3.526  -0.809  1.00 98.67           H  
ATOM   1344  N   SER A 200      28.285   6.612   8.309  1.00 53.76           N  
ANISOU 1344  N   SER A 200     6050   7271   7106   -987   2092   -258       N  
ATOM   1345  CA  SER A 200      27.983   6.329   9.711  1.00 49.04           C  
ANISOU 1345  CA  SER A 200     5392   6552   6687   -855   1869   -327       C  
ATOM   1346  C   SER A 200      26.488   6.587   9.867  1.00 47.48           C  
ANISOU 1346  C   SER A 200     5407   6285   6348   -831   1675   -227       C  
ATOM   1347  O   SER A 200      26.067   7.738  10.013  1.00 44.64           O  
ANISOU 1347  O   SER A 200     5108   5848   6007   -906   1588    -81       O  
ATOM   1348  CB  SER A 200      28.805   7.189  10.653  1.00 48.81           C  
ANISOU 1348  CB  SER A 200     5174   6446   6926   -896   1812   -308       C  
ATOM   1349  OG  SER A 200      28.509   6.878  12.000  1.00 53.25           O  
ANISOU 1349  OG  SER A 200     5686   6923   7625   -765   1598   -380       O  
ATOM   1350  H   SER A 200      27.910   7.331   8.022  1.00 64.52           H  
ATOM   1351  HA  SER A 200      28.184   5.403   9.922  1.00 58.84           H  
ATOM   1352  HB2 SER A 200      29.748   7.025  10.491  1.00 58.57           H  
ATOM   1353  HB3 SER A 200      28.598   8.123  10.491  1.00 58.57           H  
ATOM   1354  HG  SER A 200      27.693   7.005  12.151  1.00 63.91           H  
ATOM   1355  N   VAL A 201      25.693   5.519   9.826  1.00 47.13           N  
ANISOU 1355  N   VAL A 201     5468   6261   6178   -728   1610   -308       N  
ATOM   1356  CA  VAL A 201      24.240   5.604   9.755  1.00 41.52           C  
ANISOU 1356  CA  VAL A 201     4952   5522   5302   -713   1454   -222       C  
ATOM   1357  C   VAL A 201      23.649   4.617  10.753  1.00 42.51           C  
ANISOU 1357  C   VAL A 201     5070   5589   5490   -566   1293   -324       C  
ATOM   1358  O   VAL A 201      23.982   3.428  10.733  1.00 44.80           O  
ANISOU 1358  O   VAL A 201     5318   5905   5800   -489   1352   -467       O  
ATOM   1359  CB  VAL A 201      23.733   5.306   8.330  1.00 44.48           C  
ANISOU 1359  CB  VAL A 201     5494   6018   5389   -783   1561   -194       C  
ATOM   1360  CG1 VAL A 201      22.218   5.371   8.259  1.00 44.03           C  
ANISOU 1360  CG1 VAL A 201     5614   5946   5169   -766   1383   -104       C  
ATOM   1361  CG2 VAL A 201      24.362   6.270   7.335  1.00 45.12           C  
ANISOU 1361  CG2 VAL A 201     5580   6174   5391   -933   1734    -67       C  
ATOM   1362  H   VAL A 201      25.983   4.710   9.839  1.00 56.56           H  
ATOM   1363  HA  VAL A 201      23.952   6.495  10.008  1.00 49.83           H  
ATOM   1364  HB  VAL A 201      23.995   4.404   8.090  1.00 53.38           H  
ATOM   1365 HG11 VAL A 201      21.920   4.916   7.456  1.00 52.83           H  
ATOM   1366 HG12 VAL A 201      21.847   4.935   9.042  1.00 52.83           H  
ATOM   1367 HG13 VAL A 201      21.943   6.300   8.235  1.00 52.83           H  
ATOM   1368 HG21 VAL A 201      24.039   6.061   6.445  1.00 54.15           H  
ATOM   1369 HG22 VAL A 201      24.113   7.177   7.573  1.00 54.15           H  
ATOM   1370 HG23 VAL A 201      25.326   6.173   7.368  1.00 54.15           H  
ATOM   1371  N   ARG A 202      22.754   5.106  11.608  1.00 43.54           N  
ANISOU 1371  N   ARG A 202     5246   5641   5657   -526   1099   -247       N  
ATOM   1372  CA  ARG A 202      22.116   4.296  12.636  1.00 40.91           C  
ANISOU 1372  CA  ARG A 202     4906   5260   5376   -399    942   -310       C  
ATOM   1373  C   ARG A 202      20.633   4.624  12.683  1.00 38.39           C  
ANISOU 1373  C   ARG A 202     4734   4926   4928   -395    790   -206       C  
ATOM   1374  O   ARG A 202      20.215   5.720  12.296  1.00 38.09           O  
ANISOU 1374  O   ARG A 202     4768   4878   4829   -466    768    -77       O  
ATOM   1375  CB  ARG A 202      22.777   4.532  14.002  1.00 39.07           C  
ANISOU 1375  CB  ARG A 202     4509   4966   5371   -329    856   -348       C  
ATOM   1376  CG  ARG A 202      24.262   4.142  14.045  1.00 42.30           C  
ANISOU 1376  CG  ARG A 202     4738   5401   5932   -318    988   -453       C  
ATOM   1377  CD  ARG A 202      24.999   4.805  15.211  1.00 44.47           C  
ANISOU 1377  CD  ARG A 202     4846   5635   6414   -298    902   -464       C  
ATOM   1378  NE  ARG A 202      24.976   6.262  15.105  1.00 55.76           N  
ANISOU 1378  NE  ARG A 202     6297   7023   7867   -414    889   -368       N  
ATOM   1379  CZ  ARG A 202      25.401   7.094  16.047  1.00 55.49           C  
ANISOU 1379  CZ  ARG A 202     6155   6937   7994   -426    795   -376       C  
ATOM   1380  NH1 ARG A 202      25.882   6.649  17.198  1.00 56.25           N  
ANISOU 1380  NH1 ARG A 202     6110   7043   8220   -330    696   -467       N  
ATOM   1381  NH2 ARG A 202      25.342   8.404  15.831  1.00 58.48           N  
ANISOU 1381  NH2 ARG A 202     6570   7247   8402   -540    795   -289       N  
ATOM   1382  H   ARG A 202      22.494   5.926  11.610  1.00 52.25           H  
ATOM   1383  HA  ARG A 202      22.195   3.353  12.424  1.00 49.09           H  
ATOM   1384  HB2 ARG A 202      22.711   5.474  14.223  1.00 46.89           H  
ATOM   1385  HB3 ARG A 202      22.312   4.002  14.669  1.00 46.89           H  
ATOM   1386  HG2 ARG A 202      24.337   3.180  14.148  1.00 50.76           H  
ATOM   1387  HG3 ARG A 202      24.689   4.421  13.220  1.00 50.76           H  
ATOM   1388  HD2 ARG A 202      24.571   4.554  16.045  1.00 53.36           H  
ATOM   1389  HD3 ARG A 202      25.924   4.514  15.213  1.00 53.36           H  
ATOM   1390  HE  ARG A 202      24.664   6.605  14.380  1.00 66.91           H  
ATOM   1391 HH11 ARG A 202      25.924   5.803  17.348  1.00 67.50           H  
ATOM   1392 HH12 ARG A 202      26.153   7.206  17.795  1.00 67.50           H  
ATOM   1393 HH21 ARG A 202      25.031   8.703  15.087  1.00 70.17           H  
ATOM   1394 HH22 ARG A 202      25.616   8.952  16.434  1.00 70.17           H  
ATOM   1395  N   ARG A 203      19.843   3.664  13.146  1.00 35.51           N  
ANISOU 1395  N   ARG A 203     4405   4554   4532   -312    689   -253       N  
ATOM   1396  CA  ARG A 203      18.392   3.809  13.181  1.00 35.22           C  
ANISOU 1396  CA  ARG A 203     4486   4522   4375   -304    550   -166       C  
ATOM   1397  C   ARG A 203      17.964   4.526  14.456  1.00 33.56           C  
ANISOU 1397  C   ARG A 203     4222   4250   4278   -237    400   -110       C  
ATOM   1398  O   ARG A 203      18.451   4.223  15.548  1.00 34.74           O  
ANISOU 1398  O   ARG A 203     4263   4368   4570   -160    358   -175       O  
ATOM   1399  CB  ARG A 203      17.718   2.437  13.093  1.00 33.00           C  
ANISOU 1399  CB  ARG A 203     4258   4260   4018   -264    515   -242       C  
ATOM   1400  CG  ARG A 203      18.137   1.624  11.861  1.00 35.65           C  
ANISOU 1400  CG  ARG A 203     4652   4653   4239   -322    664   -341       C  
ATOM   1401  CD  ARG A 203      17.225   0.424  11.636  1.00 40.79           C  
ANISOU 1401  CD  ARG A 203     5388   5309   4800   -311    607   -410       C  
ATOM   1402  NE  ARG A 203      17.186  -0.487  12.780  1.00 34.54           N  
ANISOU 1402  NE  ARG A 203     4523   4431   4169   -210    531   -463       N  
ATOM   1403  CZ  ARG A 203      16.393  -1.549  12.869  1.00 39.74           C  
ANISOU 1403  CZ  ARG A 203     5234   5059   4805   -196    464   -508       C  
ATOM   1404  NH1 ARG A 203      15.553  -1.873  11.894  1.00 34.46           N  
ANISOU 1404  NH1 ARG A 203     4687   4446   3962   -279    452   -529       N  
ATOM   1405  NH2 ARG A 203      16.448  -2.314  13.959  1.00 36.39           N  
ANISOU 1405  NH2 ARG A 203     4738   4551   4538   -106    403   -526       N  
ATOM   1406  H   ARG A 203      20.126   2.911  13.450  1.00 42.61           H  
ATOM   1407  HA  ARG A 203      18.099   4.340  12.424  1.00 42.27           H  
ATOM   1408  HB2 ARG A 203      17.952   1.923  13.881  1.00 39.60           H  
ATOM   1409  HB3 ARG A 203      16.757   2.563  13.052  1.00 39.60           H  
ATOM   1410  HG2 ARG A 203      18.094   2.190  11.074  1.00 42.78           H  
ATOM   1411  HG3 ARG A 203      19.042   1.298  11.986  1.00 42.78           H  
ATOM   1412  HD2 ARG A 203      16.322   0.740  11.476  1.00 48.95           H  
ATOM   1413  HD3 ARG A 203      17.543  -0.075  10.868  1.00 48.95           H  
ATOM   1414  HE  ARG A 203      17.713  -0.324  13.441  1.00 41.45           H  
ATOM   1415 HH11 ARG A 203      15.513  -1.390  11.183  1.00 41.36           H  
ATOM   1416 HH12 ARG A 203      15.048  -2.565  11.973  1.00 41.36           H  
ATOM   1417 HH21 ARG A 203      16.993  -2.118  14.594  1.00 43.67           H  
ATOM   1418 HH22 ARG A 203      15.939  -3.004  14.026  1.00 43.67           H  
ATOM   1419  N   VAL A 204      17.040   5.478  14.312  1.00 31.05           N  
ANISOU 1419  N   VAL A 204     3981   3923   3892   -258    317      8       N  
ATOM   1420  CA  VAL A 204      16.617   6.297  15.435  1.00 31.58           C  
ANISOU 1420  CA  VAL A 204     4005   3930   4062   -193    191     46       C  
ATOM   1421  C   VAL A 204      15.100   6.416  15.475  1.00 30.54           C  
ANISOU 1421  C   VAL A 204     3955   3823   3826   -155     68    130       C  
ATOM   1422  O   VAL A 204      14.395   6.270  14.476  1.00 27.47           O  
ANISOU 1422  O   VAL A 204     3663   3488   3287   -204     70    196       O  
ATOM   1423  CB  VAL A 204      17.241   7.715  15.407  1.00 30.56           C  
ANISOU 1423  CB  VAL A 204     3852   3725   4036   -247    220     99       C  
ATOM   1424  CG1 VAL A 204      18.720   7.657  15.762  1.00 34.17           C  
ANISOU 1424  CG1 VAL A 204     4180   4162   4643   -270    309      2       C  
ATOM   1425  CG2 VAL A 204      17.036   8.355  14.026  1.00 34.95           C  
ANISOU 1425  CG2 VAL A 204     4518   4291   4469   -350    291    227       C  
ATOM   1426  H   VAL A 204      16.647   5.665  13.570  1.00 37.26           H  
ATOM   1427  HA  VAL A 204      16.897   5.839  16.243  1.00 37.89           H  
ATOM   1428  HB  VAL A 204      16.800   8.270  16.069  1.00 36.68           H  
ATOM   1429 HG11 VAL A 204      19.090   8.553  15.720  1.00 41.01           H  
ATOM   1430 HG12 VAL A 204      18.816   7.301  16.659  1.00 41.01           H  
ATOM   1431 HG13 VAL A 204      19.175   7.081  15.127  1.00 41.01           H  
ATOM   1432 HG21 VAL A 204      17.364   9.268  14.049  1.00 41.94           H  
ATOM   1433 HG22 VAL A 204      17.527   7.844  13.365  1.00 41.94           H  
ATOM   1434 HG23 VAL A 204      16.089   8.350  13.813  1.00 41.94           H  
ATOM   1435  N   ARG A 205      14.613   6.686  16.685  1.00 30.83           N  
ANISOU 1435  N   ARG A 205     3938   3834   3942    -65    -43    121       N  
ATOM   1436  CA  ARG A 205      13.245   7.113  16.938  1.00 30.81           C  
ANISOU 1436  CA  ARG A 205     3976   3846   3885    -12   -159    200       C  
ATOM   1437  C   ARG A 205      13.284   8.512  17.535  1.00 31.27           C  
ANISOU 1437  C   ARG A 205     4009   3816   4057     26   -205    225       C  
ATOM   1438  O   ARG A 205      14.068   8.771  18.455  1.00 30.94           O  
ANISOU 1438  O   ARG A 205     3886   3730   4140     55   -206    137       O  
ATOM   1439  CB  ARG A 205      12.529   6.156  17.898  1.00 30.69           C  
ANISOU 1439  CB  ARG A 205     3914   3890   3857     70   -237    159       C  
ATOM   1440  CG  ARG A 205      11.092   6.550  18.216  1.00 32.67           C  
ANISOU 1440  CG  ARG A 205     4178   4178   4058    130   -346    235       C  
ATOM   1441  CD  ARG A 205      10.309   5.348  18.728  1.00 33.50           C  
ANISOU 1441  CD  ARG A 205     4254   4363   4111    162   -394    222       C  
ATOM   1442  NE  ARG A 205      10.387   4.234  17.787  1.00 34.28           N  
ANISOU 1442  NE  ARG A 205     4406   4489   4129     79   -345    206       N  
ATOM   1443  CZ  ARG A 205      10.065   2.984  18.076  1.00 34.34           C  
ANISOU 1443  CZ  ARG A 205     4398   4528   4122     77   -358    176       C  
ATOM   1444  NH1 ARG A 205       9.620   2.644  19.278  1.00 30.50           N  
ANISOU 1444  NH1 ARG A 205     3840   4068   3680    150   -416    183       N  
ATOM   1445  NH2 ARG A 205      10.187   2.054  17.137  1.00 36.50           N  
ANISOU 1445  NH2 ARG A 205     4731   4804   4334     -2   -310    138       N  
ATOM   1446  H   ARG A 205      15.079   6.626  17.405  1.00 36.99           H  
ATOM   1447  HA  ARG A 205      12.748   7.132  16.105  1.00 36.98           H  
ATOM   1448  HB2 ARG A 205      12.510   5.272  17.498  1.00 36.83           H  
ATOM   1449  HB3 ARG A 205      13.019   6.131  18.734  1.00 36.83           H  
ATOM   1450  HG2 ARG A 205      11.088   7.237  18.901  1.00 39.21           H  
ATOM   1451  HG3 ARG A 205      10.660   6.880  17.413  1.00 39.21           H  
ATOM   1452  HD2 ARG A 205      10.679   5.059  19.577  1.00 40.20           H  
ATOM   1453  HD3 ARG A 205       9.377   5.592  18.839  1.00 40.20           H  
ATOM   1454  HE  ARG A 205      10.660   4.402  16.989  1.00 41.13           H  
ATOM   1455 HH11 ARG A 205       9.535   3.242  19.890  1.00 36.60           H  
ATOM   1456 HH12 ARG A 205       9.416   1.825  19.446  1.00 36.60           H  
ATOM   1457 HH21 ARG A 205      10.472   2.268  16.354  1.00 43.80           H  
ATOM   1458 HH22 ARG A 205       9.982   1.237  17.311  1.00 43.80           H  
ATOM   1459  N   ARG A 206      12.452   9.408  17.012  1.00 31.27           N  
ANISOU 1459  N   ARG A 206     4076   3785   4020     27   -251    338       N  
ATOM   1460  CA  ARG A 206      12.285  10.724  17.623  1.00 32.07           C  
ANISOU 1460  CA  ARG A 206     4162   3778   4244     82   -308    355       C  
ATOM   1461  C   ARG A 206      11.320  10.568  18.788  1.00 30.00           C  
ANISOU 1461  C   ARG A 206     3846   3563   3988    209   -410    306       C  
ATOM   1462  O   ARG A 206      10.108  10.583  18.603  1.00 36.55           O  
ANISOU 1462  O   ARG A 206     4700   4442   4744    259   -475    384       O  
ATOM   1463  CB  ARG A 206      11.792  11.739  16.610  1.00 32.60           C  
ANISOU 1463  CB  ARG A 206     4319   3778   4287     48   -317    512       C  
ATOM   1464  CG  ARG A 206      11.842  13.164  17.152  1.00 33.96           C  
ANISOU 1464  CG  ARG A 206     4484   3788   4631     94   -357    520       C  
ATOM   1465  CD  ARG A 206      11.457  14.193  16.110  1.00 34.72           C  
ANISOU 1465  CD  ARG A 206     4673   3791   4726     60   -363    703       C  
ATOM   1466  NE  ARG A 206      11.716  15.542  16.600  1.00 35.55           N  
ANISOU 1466  NE  ARG A 206     4776   3699   5034     86   -384    697       N  
ATOM   1467  CZ  ARG A 206      11.401  16.651  15.946  1.00 35.23           C  
ANISOU 1467  CZ  ARG A 206     4810   3520   5056     79   -403    857       C  
ATOM   1468  NH1 ARG A 206      10.830  16.608  14.754  1.00 39.00           N  
ANISOU 1468  NH1 ARG A 206     5369   4058   5389     47   -408   1050       N  
ATOM   1469  NH2 ARG A 206      11.666  17.830  16.499  1.00 36.13           N  
ANISOU 1469  NH2 ARG A 206     4918   3426   5384    105   -423    824       N  
ATOM   1470  H   ARG A 206      11.974   9.278  16.309  1.00 37.53           H  
ATOM   1471  HA  ARG A 206      13.137  11.043  17.960  1.00 38.48           H  
ATOM   1472  HB2 ARG A 206      12.352  11.696  15.819  1.00 39.12           H  
ATOM   1473  HB3 ARG A 206      10.873  11.535  16.377  1.00 39.12           H  
ATOM   1474  HG2 ARG A 206      11.223  13.243  17.895  1.00 40.75           H  
ATOM   1475  HG3 ARG A 206      12.744  13.360  17.449  1.00 40.75           H  
ATOM   1476  HD2 ARG A 206      11.979  14.051  15.305  1.00 41.66           H  
ATOM   1477  HD3 ARG A 206      10.511  14.114  15.910  1.00 41.66           H  
ATOM   1478  HE  ARG A 206      12.099  15.623  17.366  1.00 42.66           H  
ATOM   1479 HH11 ARG A 206      10.656  15.850  14.388  1.00 46.80           H  
ATOM   1480 HH12 ARG A 206      10.633  17.338  14.345  1.00 46.80           H  
ATOM   1481 HH21 ARG A 206      12.037  17.867  17.274  1.00 43.36           H  
ATOM   1482 HH22 ARG A 206      11.465  18.555  16.083  1.00 43.36           H  
ATOM   1483  N   ILE A 207      11.859  10.381  19.994  1.00 29.27           N  
ANISOU 1483  N   ILE A 207     3671   3477   3974    259   -422    178       N  
ATOM   1484  CA  ILE A 207      11.008  10.158  21.154  1.00 31.33           C  
ANISOU 1484  CA  ILE A 207     3876   3812   4215    374   -502    130       C  
ATOM   1485  C   ILE A 207      10.442  11.460  21.708  1.00 32.57           C  
ANISOU 1485  C   ILE A 207     4029   3890   4455    461   -561    114       C  
ATOM   1486  O   ILE A 207       9.465  11.436  22.465  1.00 30.78           O  
ANISOU 1486  O   ILE A 207     3766   3735   4194    566   -619     97       O  
ATOM   1487  CB  ILE A 207      11.773   9.402  22.250  1.00 27.87           C  
ANISOU 1487  CB  ILE A 207     3355   3436   3799    400   -500     13       C  
ATOM   1488  CG1 ILE A 207      13.060  10.129  22.636  1.00 31.31           C  
ANISOU 1488  CG1 ILE A 207     3749   3782   4366    368   -480    -86       C  
ATOM   1489  CG2 ILE A 207      12.098   7.987  21.774  1.00 27.58           C  
ANISOU 1489  CG2 ILE A 207     3320   3468   3691    345   -450     32       C  
ATOM   1490  CD1 ILE A 207      13.731   9.565  23.891  1.00 28.98           C  
ANISOU 1490  CD1 ILE A 207     3357   3565   4090    416   -512   -201       C  
ATOM   1491  H   ILE A 207      12.703  10.378  20.161  1.00 35.13           H  
ATOM   1492  HA  ILE A 207      10.259   9.608  20.878  1.00 37.60           H  
ATOM   1493  HB  ILE A 207      11.205   9.361  23.035  1.00 33.44           H  
ATOM   1494 HG12 ILE A 207      13.691  10.057  21.904  1.00 37.58           H  
ATOM   1495 HG13 ILE A 207      12.853  11.062  22.805  1.00 37.58           H  
ATOM   1496 HG21 ILE A 207      12.504   7.493  22.504  1.00 33.09           H  
ATOM   1497 HG22 ILE A 207      11.277   7.551  21.497  1.00 33.09           H  
ATOM   1498 HG23 ILE A 207      12.713   8.038  21.026  1.00 33.09           H  
ATOM   1499 HD11 ILE A 207      14.494  10.119  24.117  1.00 34.78           H  
ATOM   1500 HD12 ILE A 207      13.091   9.568  24.620  1.00 34.78           H  
ATOM   1501 HD13 ILE A 207      14.023   8.657  23.711  1.00 34.78           H  
ATOM   1502  N   SER A 208      11.032  12.599  21.355  1.00 37.49           N  
ANISOU 1502  N   SER A 208     4687   4360   5196    420   -542    118       N  
ATOM   1503  CA  SER A 208      10.524  13.901  21.767  1.00 32.56           C  
ANISOU 1503  CA  SER A 208     4073   3616   4681    502   -594    100       C  
ATOM   1504  C   SER A 208      11.044  14.937  20.782  1.00 37.63           C  
ANISOU 1504  C   SER A 208     4788   4079   5431    414   -557    192       C  
ATOM   1505  O   SER A 208      11.796  14.619  19.853  1.00 31.90           O  
ANISOU 1505  O   SER A 208     4095   3351   4674    290   -484    262       O  
ATOM   1506  CB  SER A 208      10.942  14.227  23.199  1.00 32.70           C  
ANISOU 1506  CB  SER A 208     4018   3628   4780    569   -629    -88       C  
ATOM   1507  OG  SER A 208      12.359  14.335  23.295  1.00 33.54           O  
ANISOU 1507  OG  SER A 208     4097   3670   4976    469   -590   -171       O  
ATOM   1508  H   SER A 208      11.740  12.643  20.869  1.00 44.99           H  
ATOM   1509  HA  SER A 208       9.554  13.895  21.728  1.00 39.07           H  
ATOM   1510  HB2 SER A 208      10.541  15.071  23.461  1.00 39.24           H  
ATOM   1511  HB3 SER A 208      10.637  13.518  23.787  1.00 39.24           H  
ATOM   1512  HG  SER A 208      12.578  14.545  24.078  1.00 40.25           H  
ATOM   1513  N   ALA A 209      10.653  16.194  21.005  1.00 33.78           N  
ANISOU 1513  N   ALA A 209     4574   3264   4997   -536    315   -154       N  
ATOM   1514  CA  ALA A 209      11.004  17.249  20.061  1.00 34.75           C  
ANISOU 1514  CA  ALA A 209     4757   3337   5111   -480    434    -13       C  
ATOM   1515  C   ALA A 209      12.514  17.426  19.945  1.00 32.65           C  
ANISOU 1515  C   ALA A 209     4422   3039   4944   -573    552     65       C  
ATOM   1516  O   ALA A 209      13.030  17.678  18.850  1.00 31.94           O  
ANISOU 1516  O   ALA A 209     4375   2944   4816   -494    696    185       O  
ATOM   1517  CB  ALA A 209      10.353  18.566  20.482  1.00 36.12           C  
ANISOU 1517  CB  ALA A 209     4998   3373   5351   -501    466     12       C  
ATOM   1518  H   ALA A 209      10.192  16.455  21.682  1.00 40.54           H  
ATOM   1519  HA  ALA A 209      10.665  16.999  19.187  1.00 41.70           H  
ATOM   1520  HB1 ALA A 209      10.596  19.256  19.845  1.00 43.34           H  
ATOM   1521  HB2 ALA A 209       9.389  18.452  20.494  1.00 43.34           H  
ATOM   1522  HB3 ALA A 209      10.669  18.806  21.367  1.00 43.34           H  
ATOM   1523  N   THR A 210      13.240  17.301  21.056  1.00 31.32           N  
ANISOU 1523  N   THR A 210     4154   2832   4914   -729    494     -5       N  
ATOM   1524  CA  THR A 210      14.673  17.553  21.059  1.00 35.75           C  
ANISOU 1524  CA  THR A 210     4594   3338   5651   -832    577     43       C  
ATOM   1525  C   THR A 210      15.539  16.302  21.195  1.00 30.04           C  
ANISOU 1525  C   THR A 210     3742   2714   4959   -848    516     -3       C  
ATOM   1526  O   THR A 210      16.763  16.434  21.284  1.00 32.94           O  
ANISOU 1526  O   THR A 210     3961   3031   5523   -934    562     18       O  
ATOM   1527  CB  THR A 210      15.046  18.524  22.198  1.00 38.74           C  
ANISOU 1527  CB  THR A 210     4937   3571   6211   -997    524    -13       C  
ATOM   1528  OG1 THR A 210      14.814  17.899  23.474  1.00 35.73           O  
ANISOU 1528  OG1 THR A 210     4568   3214   5793  -1053    324   -154       O  
ATOM   1529  CG2 THR A 210      14.240  19.815  22.114  1.00 36.97           C  
ANISOU 1529  CG2 THR A 210     4843   3225   5978   -986    608     36       C  
ATOM   1530  H   THR A 210      12.920  17.069  21.820  1.00 37.58           H  
ATOM   1531  HA  THR A 210      14.883  17.964  20.206  1.00 42.90           H  
ATOM   1532  HB  THR A 210      15.985  18.752  22.115  1.00 46.49           H  
ATOM   1533  HG1 THR A 210      14.001  17.700  23.553  1.00 42.87           H  
ATOM   1534 HG21 THR A 210      14.535  20.436  22.798  1.00 44.36           H  
ATOM   1535 HG22 THR A 210      14.360  20.226  21.243  1.00 44.36           H  
ATOM   1536 HG23 THR A 210      13.297  19.627  22.245  1.00 44.36           H  
ATOM   1537  N   LYS A 211      14.957  15.100  21.189  1.00 32.16           N  
ANISOU 1537  N   LYS A 211     4044   3104   5070   -764    424    -68       N  
ATOM   1538  CA  LYS A 211      15.734  13.890  21.436  1.00 33.96           C  
ANISOU 1538  CA  LYS A 211     4166   3412   5326   -771    364   -114       C  
ATOM   1539  C   LYS A 211      15.452  12.794  20.421  1.00 32.43           C  
ANISOU 1539  C   LYS A 211     4011   3337   4974   -634    418    -99       C  
ATOM   1540  O   LYS A 211      14.298  12.519  20.083  1.00 31.51           O  
ANISOU 1540  O   LYS A 211     4003   3267   4702   -546    379   -139       O  
ATOM   1541  CB  LYS A 211      15.456  13.313  22.843  1.00 26.75           C  
ANISOU 1541  CB  LYS A 211     3273   2496   4394   -827    177   -242       C  
ATOM   1542  CG  LYS A 211      15.808  14.240  23.989  1.00 29.37           C  
ANISOU 1542  CG  LYS A 211     3603   2707   4849   -954     78   -289       C  
ATOM   1543  CD  LYS A 211      17.287  14.629  23.997  1.00 31.48           C  
ANISOU 1543  CD  LYS A 211     3685   2923   5353  -1043     73   -263       C  
ATOM   1544  CE  LYS A 211      17.581  15.504  25.216  1.00 32.27           C  
ANISOU 1544  CE  LYS A 211     3798   2894   5569  -1169    -82   -353       C  
ATOM   1545  NZ  LYS A 211      18.902  16.180  25.168  1.00 39.40           N  
ANISOU 1545  NZ  LYS A 211     4488   3706   6774  -1279    -84   -347       N  
ATOM   1546  H   LYS A 211      14.120  14.964  21.045  1.00 38.59           H  
ATOM   1547  HA  LYS A 211      16.667  14.140  21.347  1.00 40.75           H  
ATOM   1548  HB2 LYS A 211      14.510  13.109  22.912  1.00 32.09           H  
ATOM   1549  HB3 LYS A 211      15.979  12.503  22.953  1.00 32.09           H  
ATOM   1550  HG2 LYS A 211      15.284  15.053  23.911  1.00 35.24           H  
ATOM   1551  HG3 LYS A 211      15.609  13.797  24.828  1.00 35.24           H  
ATOM   1552  HD2 LYS A 211      17.836  13.831  24.046  1.00 37.78           H  
ATOM   1553  HD3 LYS A 211      17.500  15.129  23.194  1.00 37.78           H  
ATOM   1554  HE2 LYS A 211      16.900  16.192  25.277  1.00 38.73           H  
ATOM   1555  HE3 LYS A 211      17.563  14.948  26.011  1.00 38.73           H  
ATOM   1556  HZ1 LYS A 211      18.945  16.715  24.458  1.00 47.28           H  
ATOM   1557  HZ2 LYS A 211      19.022  16.666  25.904  1.00 47.28           H  
ATOM   1558  HZ3 LYS A 211      19.552  15.574  25.113  1.00 47.28           H  
ATOM   1559  N   LEU A 212      16.520  12.156  19.957  1.00 31.67           N  
ANISOU 1559  N   LEU A 212     3814   3277   4944   -616    499    -57       N  
ATOM   1560  CA  LEU A 212      16.445  10.917  19.201  1.00 34.52           C  
ANISOU 1560  CA  LEU A 212     4209   3741   5168   -499    536    -69       C  
ATOM   1561  C   LEU A 212      16.890   9.758  20.084  1.00 31.02           C  
ANISOU 1561  C   LEU A 212     3670   3339   4776   -531    421   -153       C  
ATOM   1562  O   LEU A 212      17.679   9.934  21.017  1.00 30.78           O  
ANISOU 1562  O   LEU A 212     3522   3262   4913   -623    339   -170       O  
ATOM   1563  CB  LEU A 212      17.329  10.969  17.960  1.00 34.33           C  
ANISOU 1563  CB  LEU A 212     4175   3707   5162   -426    761     53       C  
ATOM   1564  CG  LEU A 212      17.020  12.082  16.962  1.00 41.69           C  
ANISOU 1564  CG  LEU A 212     5253   4575   6012   -357    918    166       C  
ATOM   1565  CD1 LEU A 212      18.166  12.196  15.967  1.00 43.34           C  
ANISOU 1565  CD1 LEU A 212     5445   4723   6300   -308   1202    301       C  
ATOM   1566  CD2 LEU A 212      15.684  11.810  16.270  1.00 37.64           C  
ANISOU 1566  CD2 LEU A 212     4947   4136   5219   -209    830    122       C  
ATOM   1567  H   LEU A 212      17.326  12.433  20.072  1.00 38.01           H  
ATOM   1568  HA  LEU A 212      15.531  10.767  18.915  1.00 41.43           H  
ATOM   1569  HB2 LEU A 212      18.247  11.088  18.248  1.00 41.20           H  
ATOM   1570  HB3 LEU A 212      17.236  10.126  17.488  1.00 41.20           H  
ATOM   1571  HG  LEU A 212      16.935  12.935  17.416  1.00 50.03           H  
ATOM   1572 HD11 LEU A 212      18.029  12.983  15.417  1.00 52.01           H  
ATOM   1573 HD12 LEU A 212      19.001  12.274  16.455  1.00 52.01           H  
ATOM   1574 HD13 LEU A 212      18.181  11.402  15.410  1.00 52.01           H  
ATOM   1575 HD21 LEU A 212      15.581  12.428  15.529  1.00 45.17           H  
ATOM   1576 HD22 LEU A 212      15.677  10.897  15.943  1.00 45.17           H  
ATOM   1577 HD23 LEU A 212      14.965  11.938  16.909  1.00 45.17           H  
ATOM   1578  N   TYR A 213      16.393   8.566  19.770  1.00 29.14           N  
ANISOU 1578  N   TYR A 213     3495   3180   4398   -443    404   -213       N  
ATOM   1579  CA  TYR A 213      16.753   7.346  20.481  1.00 30.61           C  
ANISOU 1579  CA  TYR A 213     3628   3396   4607   -442    329   -280       C  
ATOM   1580  C   TYR A 213      17.362   6.366  19.492  1.00 29.42           C  
ANISOU 1580  C   TYR A 213     3452   3302   4423   -345    456   -247       C  
ATOM   1581  O   TYR A 213      16.698   5.965  18.530  1.00 29.40           O  
ANISOU 1581  O   TYR A 213     3566   3345   4261   -254    514   -269       O  
ATOM   1582  CB  TYR A 213      15.526   6.720  21.159  1.00 29.11           C  
ANISOU 1582  CB  TYR A 213     3546   3208   4308   -434    228   -397       C  
ATOM   1583  CG  TYR A 213      15.863   5.598  22.108  1.00 24.26           C  
ANISOU 1583  CG  TYR A 213     2922   2585   3709   -430    164   -452       C  
ATOM   1584  CD1 TYR A 213      16.226   4.345  21.637  1.00 25.66           C  
ANISOU 1584  CD1 TYR A 213     3082   2812   3857   -352    224   -464       C  
ATOM   1585  CD2 TYR A 213      15.805   5.793  23.480  1.00 24.43           C  
ANISOU 1585  CD2 TYR A 213     2991   2535   3755   -487     49   -491       C  
ATOM   1586  CE1 TYR A 213      16.526   3.309  22.512  1.00 27.60           C  
ANISOU 1586  CE1 TYR A 213     3341   3035   4111   -328    176   -503       C  
ATOM   1587  CE2 TYR A 213      16.102   4.769  24.360  1.00 26.02           C  
ANISOU 1587  CE2 TYR A 213     3236   2714   3935   -451     -8   -529       C  
ATOM   1588  CZ  TYR A 213      16.462   3.527  23.869  1.00 25.16           C  
ANISOU 1588  CZ  TYR A 213     3094   2655   3811   -370     58   -529       C  
ATOM   1589  OH  TYR A 213      16.774   2.513  24.745  1.00 26.47           O  
ANISOU 1589  OH  TYR A 213     3322   2784   3952   -316     10   -554       O  
ATOM   1590  H   TYR A 213      15.830   8.436  19.133  1.00 34.97           H  
ATOM   1591  HA  TYR A 213      17.413   7.554  21.162  1.00 36.73           H  
ATOM   1592  HB2 TYR A 213      15.064   7.407  21.664  1.00 34.94           H  
ATOM   1593  HB3 TYR A 213      14.941   6.362  20.473  1.00 34.94           H  
ATOM   1594  HD1 TYR A 213      16.270   4.196  20.720  1.00 30.80           H  
ATOM   1595  HD2 TYR A 213      15.563   6.627  23.814  1.00 29.31           H  
ATOM   1596  HE1 TYR A 213      16.768   2.474  22.183  1.00 33.12           H  
ATOM   1597  HE2 TYR A 213      16.061   4.915  25.277  1.00 31.22           H  
ATOM   1598  HH  TYR A 213      16.709   2.786  25.537  1.00 31.76           H  
ATOM   1599  N   LEU A 214      18.611   5.968  19.736  1.00 36.31           N  
ANISOU 1599  N   LEU A 214     4176   4165   5454   -356    486   -207       N  
ATOM   1600  CA  LEU A 214      19.300   4.982  18.890  1.00 33.01           C  
ANISOU 1600  CA  LEU A 214     3725   3783   5034   -260    634   -172       C  
ATOM   1601  C   LEU A 214      18.756   3.602  19.250  1.00 33.59           C  
ANISOU 1601  C   LEU A 214     3876   3898   4988   -204    558   -273       C  
ATOM   1602  O   LEU A 214      19.226   2.950  20.195  1.00 29.60           O  
ANISOU 1602  O   LEU A 214     3299   3380   4566   -212    464   -300       O  
ATOM   1603  CB  LEU A 214      20.811   5.072  19.084  1.00 31.27           C  
ANISOU 1603  CB  LEU A 214     3279   3519   5085   -288    693    -99       C  
ATOM   1604  CG  LEU A 214      21.447   6.368  18.576  1.00 39.04           C  
ANISOU 1604  CG  LEU A 214     4165   4425   6243   -347    841      3       C  
ATOM   1605  CD1 LEU A 214      22.823   6.588  19.215  1.00 38.86           C  
ANISOU 1605  CD1 LEU A 214     3852   4334   6579   -421    805     24       C  
ATOM   1606  CD2 LEU A 214      21.571   6.382  17.061  1.00 37.13           C  
ANISOU 1606  CD2 LEU A 214     4031   4172   5906   -244   1135    100       C  
ATOM   1607  H   LEU A 214      19.088   6.255  20.391  1.00 43.57           H  
ATOM   1608  HA  LEU A 214      19.114   5.152  17.953  1.00 39.61           H  
ATOM   1609  HB2 LEU A 214      21.004   5.004  20.032  1.00 37.53           H  
ATOM   1610  HB3 LEU A 214      21.227   4.336  18.607  1.00 37.53           H  
ATOM   1611  HG  LEU A 214      20.864   7.100  18.831  1.00 46.85           H  
ATOM   1612 HD11 LEU A 214      23.203   7.411  18.870  1.00 46.63           H  
ATOM   1613 HD12 LEU A 214      22.718   6.650  20.177  1.00 46.63           H  
ATOM   1614 HD13 LEU A 214      23.398   5.839  18.992  1.00 46.63           H  
ATOM   1615 HD21 LEU A 214      21.753   7.288  16.767  1.00 44.56           H  
ATOM   1616 HD22 LEU A 214      22.298   5.797  16.798  1.00 44.56           H  
ATOM   1617 HD23 LEU A 214      20.738   6.070  16.673  1.00 44.56           H  
ATOM   1618  N   VAL A 215      17.772   3.143  18.474  1.00 31.76           N  
ANISOU 1618  N   VAL A 215     3798   3703   4567   -138    594   -335       N  
ATOM   1619  CA  VAL A 215      16.968   2.001  18.864  1.00 32.09           C  
ANISOU 1619  CA  VAL A 215     3917   3754   4523   -113    526   -457       C  
ATOM   1620  C   VAL A 215      17.744   0.691  18.891  1.00 32.84           C  
ANISOU 1620  C   VAL A 215     3972   3851   4654    -49    596   -460       C  
ATOM   1621  O   VAL A 215      17.292  -0.282  19.510  1.00 29.87           O  
ANISOU 1621  O   VAL A 215     3644   3451   4254    -39    553   -544       O  
ATOM   1622  CB  VAL A 215      15.753   1.889  17.917  1.00 31.53           C  
ANISOU 1622  CB  VAL A 215     3984   3708   4286    -60    521   -547       C  
ATOM   1623  CG1 VAL A 215      14.803   3.064  18.131  1.00 31.12           C  
ANISOU 1623  CG1 VAL A 215     3964   3641   4220   -113    422   -560       C  
ATOM   1624  CG2 VAL A 215      16.205   1.835  16.465  1.00 31.58           C  
ANISOU 1624  CG2 VAL A 215     4069   3750   4182     48    657   -494       C  
ATOM   1625  H   VAL A 215      17.554   3.481  17.714  1.00 38.11           H  
ATOM   1626  HA  VAL A 215      16.664   2.154  19.773  1.00 38.51           H  
ATOM   1627  HB  VAL A 215      15.279   1.067  18.117  1.00 37.83           H  
ATOM   1628 HG11 VAL A 215      14.043   2.968  17.536  1.00 37.35           H  
ATOM   1629 HG12 VAL A 215      14.503   3.063  19.054  1.00 37.35           H  
ATOM   1630 HG13 VAL A 215      15.273   3.890  17.937  1.00 37.35           H  
ATOM   1631 HG21 VAL A 215      15.462   1.544  15.913  1.00 37.90           H  
ATOM   1632 HG22 VAL A 215      16.494   2.719  16.190  1.00 37.90           H  
ATOM   1633 HG23 VAL A 215      16.941   1.208  16.386  1.00 37.90           H  
ATOM   1634  N   ASP A 216      18.899   0.630  18.253  1.00 29.56           N  
ANISOU 1634  N   ASP A 216     3471   3445   4317      1    730   -366       N  
ATOM   1635  CA  ASP A 216      19.726  -0.569  18.270  1.00 33.97           C  
ANISOU 1635  CA  ASP A 216     3973   3996   4940     75    811   -356       C  
ATOM   1636  C   ASP A 216      20.905  -0.463  19.226  1.00 32.12           C  
ANISOU 1636  C   ASP A 216     3539   3732   4932     52    741   -286       C  
ATOM   1637  O   ASP A 216      21.705  -1.392  19.305  1.00 33.68           O  
ANISOU 1637  O   ASP A 216     3660   3917   5221    127    793   -265       O  
ATOM   1638  CB  ASP A 216      20.216  -0.862  16.849  1.00 36.27           C  
ANISOU 1638  CB  ASP A 216     4311   4296   5176    172   1036   -308       C  
ATOM   1639  CG  ASP A 216      19.066  -1.015  15.868  1.00 34.98           C  
ANISOU 1639  CG  ASP A 216     4369   4158   4762    222   1049   -402       C  
ATOM   1640  OD1 ASP A 216      18.039  -1.612  16.258  1.00 32.61           O  
ANISOU 1640  OD1 ASP A 216     4145   3862   4383    202    924   -534       O  
ATOM   1641  OD2 ASP A 216      19.175  -0.524  14.719  1.00 34.90           O  
ANISOU 1641  OD2 ASP A 216     4464   4151   4644    287   1181   -349       O  
ATOM   1642  H   ASP A 216      19.232   1.277  17.796  1.00 35.48           H  
ATOM   1643  HA  ASP A 216      19.192  -1.323  18.565  1.00 40.77           H  
ATOM   1644  HB2 ASP A 216      20.776  -0.129  16.548  1.00 43.53           H  
ATOM   1645  HB3 ASP A 216      20.725  -1.688  16.852  1.00 43.53           H  
ATOM   1646  N   PHE A 217      21.007   0.622  19.978  1.00 31.22           N  
ANISOU 1646  N   PHE A 217     3346   3600   4917    -42    602   -264       N  
ATOM   1647  CA  PHE A 217      22.084   0.813  20.941  1.00 33.90           C  
ANISOU 1647  CA  PHE A 217     3496   3905   5480    -64    466   -231       C  
ATOM   1648  C   PHE A 217      21.609   1.204  22.330  1.00 39.82           C  
ANISOU 1648  C   PHE A 217     4317   4627   6188   -125    218   -292       C  
ATOM   1649  O   PHE A 217      22.381   1.053  23.283  1.00 33.64           O  
ANISOU 1649  O   PHE A 217     3441   3814   5528   -105     45   -296       O  
ATOM   1650  CB  PHE A 217      23.045   1.892  20.436  1.00 31.56           C  
ANISOU 1650  CB  PHE A 217     2993   3578   5422   -120    555   -145       C  
ATOM   1651  CG  PHE A 217      23.743   1.514  19.168  1.00 36.20           C  
ANISOU 1651  CG  PHE A 217     3512   4158   6084    -43    840    -65       C  
ATOM   1652  CD1 PHE A 217      23.179   1.810  17.939  1.00 34.22           C  
ANISOU 1652  CD1 PHE A 217     3429   3918   5657    -15   1051    -32       C  
ATOM   1653  CD2 PHE A 217      24.963   0.849  19.202  1.00 37.61           C  
ANISOU 1653  CD2 PHE A 217     3479   4306   6503     23    899    -24       C  
ATOM   1654  CE1 PHE A 217      23.829   1.458  16.758  1.00 41.96           C  
ANISOU 1654  CE1 PHE A 217     4406   4870   6668     77   1344     45       C  
ATOM   1655  CE2 PHE A 217      25.617   0.503  18.019  1.00 36.26           C  
ANISOU 1655  CE2 PHE A 217     3261   4105   6410    103   1212     55       C  
ATOM   1656  CZ  PHE A 217      25.051   0.807  16.803  1.00 36.00           C  
ANISOU 1656  CZ  PHE A 217     3436   4074   6168    130   1446     91       C  
ATOM   1657  H   PHE A 217      20.453   1.279  19.950  1.00 37.46           H  
ATOM   1658  HA  PHE A 217      22.577  -0.018  21.025  1.00 40.68           H  
ATOM   1659  HB2 PHE A 217      22.545   2.706  20.270  1.00 37.87           H  
ATOM   1660  HB3 PHE A 217      23.722   2.051  21.113  1.00 37.87           H  
ATOM   1661  HD1 PHE A 217      22.360   2.249  17.902  1.00 41.07           H  
ATOM   1662  HD2 PHE A 217      25.347   0.633  20.021  1.00 45.13           H  
ATOM   1663  HE1 PHE A 217      23.441   1.660  15.937  1.00 50.36           H  
ATOM   1664  HE2 PHE A 217      26.437   0.067  18.053  1.00 43.51           H  
ATOM   1665  HZ  PHE A 217      25.486   0.576  16.014  1.00 43.20           H  
ATOM   1666  N   GLY A 218      20.380   1.704  22.480  1.00 31.80           N  
ANISOU 1666  N   GLY A 218     3471   3607   5004   -184    191   -344       N  
ATOM   1667  CA  GLY A 218      19.887   2.109  23.776  1.00 29.09           C  
ANISOU 1667  CA  GLY A 218     3234   3213   4607   -234      4   -398       C  
ATOM   1668  C   GLY A 218      20.392   3.435  24.268  1.00 32.53           C  
ANISOU 1668  C   GLY A 218     3568   3611   5179   -330   -129   -382       C  
ATOM   1669  O   GLY A 218      20.532   3.608  25.485  1.00 31.12           O  
ANISOU 1669  O   GLY A 218     3447   3380   4996   -341   -330   -426       O  
ATOM   1670  H   GLY A 218      19.818   1.816  21.838  1.00 38.16           H  
ATOM   1671  HA2 GLY A 218      18.919   2.159  23.737  1.00 34.91           H  
ATOM   1672  HA3 GLY A 218      20.142   1.437  24.428  1.00 34.91           H  
ATOM   1673  N   LYS A 219      20.667   4.381  23.361  1.00 33.25           N  
ANISOU 1673  N   LYS A 219     3538   3711   5385   -392    -15   -325       N  
ATOM   1674  CA  LYS A 219      21.238   5.672  23.724  1.00 37.41           C  
ANISOU 1674  CA  LYS A 219     3938   4178   6096   -497   -107   -313       C  
ATOM   1675  C   LYS A 219      20.385   6.809  23.190  1.00 31.43           C  
ANISOU 1675  C   LYS A 219     3272   3403   5269   -569     -3   -291       C  
ATOM   1676  O   LYS A 219      20.031   6.822  22.005  1.00 30.35           O  
ANISOU 1676  O   LYS A 219     3171   3301   5059   -530    194   -235       O  
ATOM   1677  CB  LYS A 219      22.675   5.850  23.172  1.00 39.12           C  
ANISOU 1677  CB  LYS A 219     3868   4376   6621   -507    -31   -248       C  
ATOM   1678  CG  LYS A 219      23.765   5.552  24.166  1.00 50.21           C  
ANISOU 1678  CG  LYS A 219     5097   5747   8233   -494   -270   -294       C  
ATOM   1679  CD  LYS A 219      23.835   4.061  24.442  1.00 50.87           C  
ANISOU 1679  CD  LYS A 219     5248   5881   8200   -354   -316   -306       C  
ATOM   1680  CE  LYS A 219      24.500   3.777  25.782  1.00 59.42           C  
ANISOU 1680  CE  LYS A 219     6291   6928   9357   -307   -646   -375       C  
ATOM   1681  NZ  LYS A 219      24.284   2.356  26.179  1.00 63.77           N  
ANISOU 1681  NZ  LYS A 219     7007   7508   9717   -156   -677   -380       N  
ATOM   1682  H   LYS A 219      20.528   4.292  22.517  1.00 39.90           H  
ATOM   1683  HA  LYS A 219      21.251   5.714  24.693  1.00 44.89           H  
ATOM   1684  HB2 LYS A 219      22.793   5.250  22.419  1.00 46.95           H  
ATOM   1685  HB3 LYS A 219      22.784   6.770  22.884  1.00 46.95           H  
ATOM   1686  HG2 LYS A 219      24.619   5.841  23.809  1.00 60.25           H  
ATOM   1687  HG3 LYS A 219      23.580   6.013  25.000  1.00 60.25           H  
ATOM   1688  HD2 LYS A 219      22.937   3.695  24.463  1.00 61.04           H  
ATOM   1689  HD3 LYS A 219      24.354   3.629  23.746  1.00 61.04           H  
ATOM   1690  HE2 LYS A 219      25.454   3.937  25.711  1.00 71.30           H  
ATOM   1691  HE3 LYS A 219      24.117   4.351  26.463  1.00 71.30           H  
ATOM   1692  HZ1 LYS A 219      24.677   2.195  26.961  1.00 76.53           H  
ATOM   1693  HZ2 LYS A 219      23.412   2.190  26.254  1.00 76.53           H  
ATOM   1694  HZ3 LYS A 219      24.629   1.812  25.565  1.00 76.53           H  
ATOM   1695  N   ILE A 220      20.106   7.780  24.049  1.00 28.92           N  
ANISOU 1695  N   ILE A 220     3004   3017   4966   -659   -141   -336       N  
ATOM   1696  CA  ILE A 220      19.415   8.999  23.650  1.00 29.41           C  
ANISOU 1696  CA  ILE A 220     3135   3038   5002   -727    -53   -309       C  
ATOM   1697  C   ILE A 220      20.447  10.035  23.222  1.00 33.41           C  
ANISOU 1697  C   ILE A 220     3443   3474   5776   -810     24   -246       C  
ATOM   1698  O   ILE A 220      21.463  10.240  23.901  1.00 31.93           O  
ANISOU 1698  O   ILE A 220     3086   3232   5816   -872   -117   -285       O  
ATOM   1699  CB  ILE A 220      18.532   9.526  24.799  1.00 29.93           C  
ANISOU 1699  CB  ILE A 220     3376   3041   4955   -778   -201   -390       C  
ATOM   1700  CG1 ILE A 220      17.319   8.589  24.989  1.00 31.89           C  
ANISOU 1700  CG1 ILE A 220     3814   3326   4975   -700   -180   -439       C  
ATOM   1701  CG2 ILE A 220      18.073  10.948  24.525  1.00 31.13           C  
ANISOU 1701  CG2 ILE A 220     3560   3123   5144   -858   -129   -360       C  
ATOM   1702  CD1 ILE A 220      16.582   8.773  26.291  1.00 26.38           C  
ANISOU 1702  CD1 ILE A 220     3308   2544   4173   -724   -291   -520       C  
ATOM   1703  H   ILE A 220      20.311   7.756  24.884  1.00 34.70           H  
ATOM   1704  HA  ILE A 220      18.845   8.813  22.888  1.00 35.29           H  
ATOM   1705  HB  ILE A 220      19.057   9.537  25.614  1.00 35.92           H  
ATOM   1706 HG12 ILE A 220      16.688   8.751  24.270  1.00 38.26           H  
ATOM   1707 HG13 ILE A 220      17.631   7.671  24.956  1.00 38.26           H  
ATOM   1708 HG21 ILE A 220      17.354  11.171  25.137  1.00 37.35           H  
ATOM   1709 HG22 ILE A 220      18.820  11.552  24.659  1.00 37.35           H  
ATOM   1710 HG23 ILE A 220      17.759  11.007  23.609  1.00 37.35           H  
ATOM   1711 HD11 ILE A 220      15.919   8.070  26.381  1.00 31.66           H  
ATOM   1712 HD12 ILE A 220      17.216   8.725  27.023  1.00 31.66           H  
ATOM   1713 HD13 ILE A 220      16.146   9.640  26.288  1.00 31.66           H  
ATOM   1714  N   ILE A 221      20.193  10.684  22.087  1.00 38.76           N  
ANISOU 1714  N   ILE A 221     4146   4138   6441   -801    248   -154       N  
ATOM   1715  CA  ILE A 221      21.048  11.744  21.574  1.00 32.89           C  
ANISOU 1715  CA  ILE A 221     3250   3293   5954   -878    402    -76       C  
ATOM   1716  C   ILE A 221      20.158  12.906  21.151  1.00 35.46           C  
ANISOU 1716  C   ILE A 221     3738   3561   6175   -897    511    -26       C  
ATOM   1717  O   ILE A 221      18.938  12.777  21.034  1.00 32.56           O  
ANISOU 1717  O   ILE A 221     3572   3252   5549   -829    482    -42       O  
ATOM   1718  CB  ILE A 221      21.932  11.277  20.400  1.00 36.59           C  
ANISOU 1718  CB  ILE A 221     3595   3768   6541   -807    659     28       C  
ATOM   1719  CG1 ILE A 221      21.079  10.821  19.218  1.00 38.14           C  
ANISOU 1719  CG1 ILE A 221     4018   4042   6433   -665    837     96       C  
ATOM   1720  CG2 ILE A 221      22.854  10.148  20.854  1.00 37.36           C  
ANISOU 1720  CG2 ILE A 221     3507   3910   6780   -779    549    -20       C  
ATOM   1721  CD1 ILE A 221      21.873  10.580  17.945  1.00 36.62           C  
ANISOU 1721  CD1 ILE A 221     3785   3821   6309   -580   1149    215       C  
ATOM   1722  H   ILE A 221      19.513  10.521  21.587  1.00 46.51           H  
ATOM   1723  HA  ILE A 221      21.637  12.049  22.282  1.00 39.47           H  
ATOM   1724  HB  ILE A 221      22.469  12.031  20.110  1.00 43.91           H  
ATOM   1725 HG12 ILE A 221      20.639   9.989  19.453  1.00 45.77           H  
ATOM   1726 HG13 ILE A 221      20.417  11.504  19.028  1.00 45.77           H  
ATOM   1727 HG21 ILE A 221      23.473   9.939  20.137  1.00 44.84           H  
ATOM   1728 HG22 ILE A 221      23.343  10.437  21.640  1.00 44.84           H  
ATOM   1729 HG23 ILE A 221      22.318   9.368  21.066  1.00 44.84           H  
ATOM   1730 HD11 ILE A 221      21.258  10.388  17.221  1.00 43.95           H  
ATOM   1731 HD12 ILE A 221      22.389  11.375  17.740  1.00 43.95           H  
ATOM   1732 HD13 ILE A 221      22.469   9.826  18.083  1.00 43.95           H  
ATOM   1733  N   ASN A 222      20.791  14.048  20.912  1.00 35.19           N  
ANISOU 1733  N   ASN A 222     3600   3396   6376   -986    645     33       N  
ATOM   1734  CA  ASN A 222      20.055  15.251  20.545  1.00 37.79           C  
ANISOU 1734  CA  ASN A 222     4084   3643   6634  -1000    762     94       C  
ATOM   1735  C   ASN A 222      19.521  15.144  19.123  1.00 39.56           C  
ANISOU 1735  C   ASN A 222     4485   3908   6636   -842    998    222       C  
ATOM   1736  O   ASN A 222      20.191  14.617  18.224  1.00 38.41           O  
ANISOU 1736  O   ASN A 222     4298   3777   6519   -767   1192    302       O  
ATOM   1737  CB  ASN A 222      20.960  16.480  20.677  1.00 36.23           C  
ANISOU 1737  CB  ASN A 222     3723   3263   6782  -1144    869    120       C  
ATOM   1738  CG  ASN A 222      21.272  16.806  22.126  1.00 39.90           C  
ANISOU 1738  CG  ASN A 222     4075   3668   7418  -1292    578    -35       C  
ATOM   1739  OD1 ASN A 222      20.503  16.469  23.032  1.00 39.71           O  
ANISOU 1739  OD1 ASN A 222     4190   3711   7188  -1279    340   -135       O  
ATOM   1740  ND2 ASN A 222      22.389  17.469  22.354  1.00 39.84           N  
ANISOU 1740  ND2 ASN A 222     3827   3516   7793  -1428    600    -63       N  
ATOM   1741  H   ASN A 222      21.643  14.154  20.956  1.00 42.23           H  
ATOM   1742  HA  ASN A 222      19.299  15.361  21.141  1.00 45.35           H  
ATOM   1743  HB2 ASN A 222      21.797  16.311  20.218  1.00 43.48           H  
ATOM   1744  HB3 ASN A 222      20.515  17.247  20.284  1.00 43.48           H  
ATOM   1745 HD21 ASN A 222      22.898  17.692  21.698  1.00 47.81           H  
ATOM   1746 HD22 ASN A 222      22.610  17.677  23.159  1.00 47.81           H  
ATOM   1747  N   TYR A 223      18.302  15.643  18.929  1.00 37.71           N  
ANISOU 1747  N   TYR A 223     4749   4630   4948    500    450    340       N  
ATOM   1748  CA  TYR A 223      17.724  15.715  17.593  1.00 39.93           C  
ANISOU 1748  CA  TYR A 223     5157   4965   5048    465    453    407       C  
ATOM   1749  C   TYR A 223      18.470  16.758  16.770  1.00 37.48           C  
ANISOU 1749  C   TYR A 223     4962   4574   4706    409    562    464       C  
ATOM   1750  O   TYR A 223      18.574  17.920  17.178  1.00 43.73           O  
ANISOU 1750  O   TYR A 223     5772   5287   5557    442    547    522       O  
ATOM   1751  CB  TYR A 223      16.237  16.051  17.671  1.00 31.97           C  
ANISOU 1751  CB  TYR A 223     4167   4024   3956    547    300    490       C  
ATOM   1752  CG  TYR A 223      15.620  16.331  16.323  1.00 35.64           C  
ANISOU 1752  CG  TYR A 223     4776   4528   4236    521    270    574       C  
ATOM   1753  CD1 TYR A 223      15.508  15.333  15.368  1.00 41.21           C  
ANISOU 1753  CD1 TYR A 223     5542   5303   4815    449    286    542       C  
ATOM   1754  CD2 TYR A 223      15.143  17.598  16.005  1.00 41.12           C  
ANISOU 1754  CD2 TYR A 223     5563   5182   4878    572    215    686       C  
ATOM   1755  CE1 TYR A 223      14.943  15.584  14.127  1.00 42.04           C  
ANISOU 1755  CE1 TYR A 223     5799   5437   4735    421    244    619       C  
ATOM   1756  CE2 TYR A 223      14.571  17.859  14.767  1.00 44.30           C  
ANISOU 1756  CE2 TYR A 223     6115   5613   5104    551    168    769       C  
ATOM   1757  CZ  TYR A 223      14.475  16.845  13.833  1.00 43.50           C  
ANISOU 1757  CZ  TYR A 223     6075   5584   4870    473    180    735       C  
ATOM   1758  OH  TYR A 223      13.918  17.089  12.599  1.00 47.27           O  
ANISOU 1758  OH  TYR A 223     6720   6083   5157    448    119    817       O  
ATOM   1759  H   TYR A 223      17.793  15.945  19.552  1.00 45.25           H  
ATOM   1760  HA  TYR A 223      17.812  14.852  17.158  1.00 47.92           H  
ATOM   1761  HB2 TYR A 223      15.766  15.300  18.065  1.00 38.36           H  
ATOM   1762  HB3 TYR A 223      16.122  16.841  18.222  1.00 38.36           H  
ATOM   1763  HD1 TYR A 223      15.819  14.478  15.563  1.00 49.46           H  
ATOM   1764  HD2 TYR A 223      15.208  18.281  16.632  1.00 49.34           H  
ATOM   1765  HE1 TYR A 223      14.880  14.904  13.496  1.00 50.44           H  
ATOM   1766  HE2 TYR A 223      14.254  18.711  14.568  1.00 53.16           H  
ATOM   1767  HH  TYR A 223      13.663  17.888  12.552  1.00 56.72           H  
ATOM   1768  N   GLU A 224      19.003  16.346  15.620  1.00 38.29           N  
ANISOU 1768  N   GLU A 224     5152   4688   4710    318    679    446       N  
ATOM   1769  CA  GLU A 224      19.642  17.258  14.669  1.00 43.93           C  
ANISOU 1769  CA  GLU A 224     6002   5333   5358    245    801    509       C  
ATOM   1770  C   GLU A 224      18.916  17.138  13.335  1.00 42.79           C  
ANISOU 1770  C   GLU A 224     6036   5244   4978    213    779    574       C  
ATOM   1771  O   GLU A 224      19.078  16.143  12.619  1.00 47.08           O  
ANISOU 1771  O   GLU A 224     6619   5839   5429    155    844    513       O  
ATOM   1772  CB  GLU A 224      21.130  16.959  14.517  1.00 43.96           C  
ANISOU 1772  CB  GLU A 224     5952   5283   5466    155    997    422       C  
ATOM   1773  CG  GLU A 224      21.940  17.384  15.729  1.00 44.63           C  
ANISOU 1773  CG  GLU A 224     5886   5289   5783    174   1007    379       C  
ATOM   1774  CD  GLU A 224      23.420  17.105  15.575  1.00 51.03           C  
ANISOU 1774  CD  GLU A 224     6615   6052   6724     87   1192    293       C  
ATOM   1775  OE1 GLU A 224      24.089  17.838  14.812  1.00 51.60           O  
ANISOU 1775  OE1 GLU A 224     6768   6066   6770      0   1335    336       O  
ATOM   1776  OE2 GLU A 224      23.909  16.141  16.214  1.00 49.80           O  
ANISOU 1776  OE2 GLU A 224     6311   5912   6698    106   1196    184       O  
ATOM   1777  H   GLU A 224      19.006  15.526  15.363  1.00 45.95           H  
ATOM   1778  HA  GLU A 224      19.553  18.169  14.991  1.00 52.72           H  
ATOM   1779  HB2 GLU A 224      21.249  16.004  14.395  1.00 52.75           H  
ATOM   1780  HB3 GLU A 224      21.471  17.437  13.745  1.00 52.75           H  
ATOM   1781  HG2 GLU A 224      21.828  18.338  15.865  1.00 53.56           H  
ATOM   1782  HG3 GLU A 224      21.623  16.899  16.507  1.00 53.56           H  
ATOM   1783  N   LYS A 225      18.113  18.151  13.018  1.00 42.44           N  
ANISOU 1783  N   LYS A 225     6107   5181   4836    256    676    695       N  
ATOM   1784  CA  LYS A 225      17.270  18.121  11.830  1.00 47.34           C  
ANISOU 1784  CA  LYS A 225     6903   5852   5231    241    605    771       C  
ATOM   1785  C   LYS A 225      18.062  17.774  10.581  1.00 46.90           C  
ANISOU 1785  C   LYS A 225     7002   5784   5036    118    777    749       C  
ATOM   1786  O   LYS A 225      17.599  16.996   9.739  1.00 44.76           O  
ANISOU 1786  O   LYS A 225     6828   5581   4597     84    747    735       O  
ATOM   1787  CB  LYS A 225      16.589  19.485  11.688  1.00 52.84           C  
ANISOU 1787  CB  LYS A 225     7710   6493   5873    306    494    909       C  
ATOM   1788  CG  LYS A 225      15.605  19.634  10.546  1.00 60.20           C  
ANISOU 1788  CG  LYS A 225     8826   7466   6580    312    373   1006       C  
ATOM   1789  CD  LYS A 225      14.902  20.997  10.648  1.00 64.52           C  
ANISOU 1789  CD  LYS A 225     9449   7948   7118    407    241   1137       C  
ATOM   1790  CE  LYS A 225      14.050  21.293   9.428  1.00 76.49           C  
ANISOU 1790  CE  LYS A 225    11174   9480   8407    411    116   1247       C  
ATOM   1791  NZ  LYS A 225      12.980  20.278   9.229  1.00 66.36           N  
ANISOU 1791  NZ  LYS A 225     9830   8332   7052    442    -43   1220       N  
ATOM   1792  H   LYS A 225      18.038  18.874  13.479  1.00 50.93           H  
ATOM   1793  HA  LYS A 225      16.590  17.436  11.928  1.00 56.80           H  
ATOM   1794  HB2 LYS A 225      16.103  19.666  12.508  1.00 63.41           H  
ATOM   1795  HB3 LYS A 225      17.279  20.154  11.557  1.00 63.41           H  
ATOM   1796  HG2 LYS A 225      16.075  19.586   9.699  1.00 72.24           H  
ATOM   1797  HG3 LYS A 225      14.936  18.933  10.595  1.00 72.24           H  
ATOM   1798  HD2 LYS A 225      14.325  21.001  11.428  1.00 77.42           H  
ATOM   1799  HD3 LYS A 225      15.571  21.695  10.726  1.00 77.42           H  
ATOM   1800  HE2 LYS A 225      13.628  22.159   9.537  1.00 91.78           H  
ATOM   1801  HE3 LYS A 225      14.614  21.296   8.639  1.00 91.78           H  
ATOM   1802  HZ1 LYS A 225      13.342  19.473   9.109  1.00 79.63           H  
ATOM   1803  HZ2 LYS A 225      12.449  20.252   9.942  1.00 79.63           H  
ATOM   1804  HZ3 LYS A 225      12.493  20.485   8.513  1.00 79.63           H  
ATOM   1805  N   ALA A 226      19.264  18.330  10.446  1.00 46.96           N  
ANISOU 1805  N   ALA A 226     7034   5701   5109     43    965    741       N  
ATOM   1806  CA  ALA A 226      20.030  18.154   9.218  1.00 46.70           C  
ANISOU 1806  CA  ALA A 226     7162   5647   4935    -77   1158    730       C  
ATOM   1807  C   ALA A 226      20.647  16.768   9.105  1.00 43.61           C  
ANISOU 1807  C   ALA A 226     6685   5311   4572   -122   1281    586       C  
ATOM   1808  O   ALA A 226      20.991  16.348   8.000  1.00 46.53           O  
ANISOU 1808  O   ALA A 226     7205   5690   4782   -206   1414    564       O  
ATOM   1809  CB  ALA A 226      21.127  19.218   9.131  1.00 41.07           C  
ANISOU 1809  CB  ALA A 226     6486   4819   4299   -153   1334    768       C  
ATOM   1810  H   ALA A 226      19.654  18.809  11.045  1.00 56.36           H  
ATOM   1811  HA  ALA A 226      19.432  18.271   8.464  1.00 56.04           H  
ATOM   1812  HB1 ALA A 226      21.631  19.086   8.313  1.00 49.28           H  
ATOM   1813  HB2 ALA A 226      20.716  20.096   9.129  1.00 49.28           H  
ATOM   1814  HB3 ALA A 226      21.714  19.130   9.899  1.00 49.28           H  
ATOM   1815  N   LYS A 227      20.791  16.050  10.212  1.00 48.52           N  
ANISOU 1815  N   LYS A 227     7086   5962   5386    -66   1238    489       N  
ATOM   1816  CA  LYS A 227      21.409  14.735  10.216  1.00 49.73           C  
ANISOU 1816  CA  LYS A 227     7151   6153   5593    -93   1343    349       C  
ATOM   1817  C   LYS A 227      20.393  13.602  10.217  1.00 45.68           C  
ANISOU 1817  C   LYS A 227     6638   5732   4987    -50   1189    309       C  
ATOM   1818  O   LYS A 227      20.783  12.439  10.344  1.00 41.77           O  
ANISOU 1818  O   LYS A 227     6068   5262   4542    -58   1244    191       O  
ATOM   1819  CB  LYS A 227      22.342  14.610  11.421  1.00 51.44           C  
ANISOU 1819  CB  LYS A 227     7133   6327   6085    -65   1397    263       C  
ATOM   1820  CG  LYS A 227      23.458  15.642  11.413  1.00 52.86           C  
ANISOU 1820  CG  LYS A 227     7292   6413   6379   -126   1558    288       C  
ATOM   1821  CD  LYS A 227      24.480  15.406  12.516  1.00 56.23           C  
ANISOU 1821  CD  LYS A 227     7484   6798   7083   -109   1607    190       C  
ATOM   1822  CE  LYS A 227      25.612  16.429  12.423  1.00 59.82           C  
ANISOU 1822  CE  LYS A 227     7912   7160   7655   -191   1770    215       C  
ATOM   1823  NZ  LYS A 227      26.656  16.199  13.455  1.00 68.96           N  
ANISOU 1823  NZ  LYS A 227     8834   8276   9091   -180   1805    116       N  
ATOM   1824  H   LYS A 227      20.531  16.310  10.990  1.00 58.22           H  
ATOM   1825  HA  LYS A 227      21.941  14.641   9.410  1.00 59.68           H  
ATOM   1826  HB2 LYS A 227      21.826  14.732  12.233  1.00 61.73           H  
ATOM   1827  HB3 LYS A 227      22.748  13.729  11.416  1.00 61.73           H  
ATOM   1828  HG2 LYS A 227      23.920  15.603  10.561  1.00 63.43           H  
ATOM   1829  HG3 LYS A 227      23.075  16.524  11.542  1.00 63.43           H  
ATOM   1830  HD2 LYS A 227      24.052  15.496  13.381  1.00 67.48           H  
ATOM   1831  HD3 LYS A 227      24.859  14.517  12.423  1.00 67.48           H  
ATOM   1832  HE2 LYS A 227      26.029  16.365  11.550  1.00 71.78           H  
ATOM   1833  HE3 LYS A 227      25.249  17.319  12.553  1.00 71.78           H  
ATOM   1834  HZ1 LYS A 227      27.301  16.807  13.376  1.00 82.75           H  
ATOM   1835  HZ2 LYS A 227      26.299  16.259  14.268  1.00 82.75           H  
ATOM   1836  HZ3 LYS A 227      27.010  15.388  13.355  1.00 82.75           H  
ATOM   1837  N   CYS A 228      19.109  13.911  10.059  1.00 48.45           N  
ANISOU 1837  N   CYS A 228     7070   6130   5209     -8    995    403       N  
ATOM   1838  CA  CYS A 228      18.043  12.919  10.089  1.00 43.75           C  
ANISOU 1838  CA  CYS A 228     6463   5625   4536     22    830    376       C  
ATOM   1839  C   CYS A 228      17.516  12.684   8.681  1.00 45.50           C  
ANISOU 1839  C   CYS A 228     6915   5882   4492    -40    806    414       C  
ATOM   1840  O   CYS A 228      17.232  13.642   7.949  1.00 43.78           O  
ANISOU 1840  O   CYS A 228     6860   5638   4136    -55    782    524       O  
ATOM   1841  CB  CYS A 228      16.906  13.362  11.003  1.00 43.06           C  
ANISOU 1841  CB  CYS A 228     6267   5575   4517    119    616    447       C  
ATOM   1842  SG  CYS A 228      17.236  13.117  12.747  1.00 45.38           S  
ANISOU 1842  SG  CYS A 228     6304   5854   5086    193    598    373       S  
ATOM   1843  H   CYS A 228      18.824  14.712   9.930  1.00 58.14           H  
ATOM   1844  HA  CYS A 228      18.399  12.081  10.423  1.00 52.50           H  
ATOM   1845  HB2 CYS A 228      16.745  14.308  10.863  1.00 51.67           H  
ATOM   1846  HB3 CYS A 228      16.111  12.854  10.779  1.00 51.67           H  
ATOM   1847  HG  CYS A 228      16.240  13.360  13.371  1.00 54.46           H  
ATOM   1848  N   PHE A 229      17.385  11.409   8.309  1.00 37.52           N  
ANISOU 1848  N   PHE A 229     5934   4919   3402    -77    804    321       N  
ATOM   1849  CA  PHE A 229      16.895  11.021   6.995  1.00 40.36           C  
ANISOU 1849  CA  PHE A 229     6525   5310   3500   -143    771    338       C  
ATOM   1850  C   PHE A 229      15.907   9.877   7.168  1.00 39.34           C  
ANISOU 1850  C   PHE A 229     6352   5262   3336   -134    590    289       C  
ATOM   1851  O   PHE A 229      15.765   9.308   8.253  1.00 37.20           O  
ANISOU 1851  O   PHE A 229     5881   5014   3238    -87    533    232       O  
ATOM   1852  CB  PHE A 229      18.049  10.627   6.069  1.00 41.84           C  
ANISOU 1852  CB  PHE A 229     6855   5448   3594   -230   1023    257       C  
ATOM   1853  CG  PHE A 229      19.093  11.699   5.921  1.00 45.52           C  
ANISOU 1853  CG  PHE A 229     7346   5835   4113   -258   1224    299       C  
ATOM   1854  CD1 PHE A 229      20.089  11.847   6.871  1.00 47.07           C  
ANISOU 1854  CD1 PHE A 229     7333   5988   4564   -232   1352    241       C  
ATOM   1855  CD2 PHE A 229      19.072  12.562   4.838  1.00 46.33           C  
ANISOU 1855  CD2 PHE A 229     7688   5902   4012   -316   1274    400       C  
ATOM   1856  CE1 PHE A 229      21.052  12.833   6.743  1.00 51.31           C  
ANISOU 1856  CE1 PHE A 229     7881   6450   5163   -272   1533    279       C  
ATOM   1857  CE2 PHE A 229      20.027  13.549   4.702  1.00 47.54           C  
ANISOU 1857  CE2 PHE A 229     7870   5976   4216   -358   1465    443       C  
ATOM   1858  CZ  PHE A 229      21.022  13.688   5.658  1.00 49.87           C  
ANISOU 1858  CZ  PHE A 229     7937   6232   4779   -339   1597    381       C  
ATOM   1859  H   PHE A 229      17.580  10.741   8.814  1.00 45.02           H  
ATOM   1860  HA  PHE A 229      16.425  11.763   6.582  1.00 48.43           H  
ATOM   1861  HB2 PHE A 229      18.483   9.838   6.429  1.00 50.21           H  
ATOM   1862  HB3 PHE A 229      17.692  10.436   5.188  1.00 50.21           H  
ATOM   1863  HD1 PHE A 229      20.111  11.276   7.605  1.00 56.48           H  
ATOM   1864  HD2 PHE A 229      18.406  12.476   4.195  1.00 55.59           H  
ATOM   1865  HE1 PHE A 229      21.719  12.920   7.386  1.00 61.57           H  
ATOM   1866  HE2 PHE A 229      20.004  14.121   3.969  1.00 57.05           H  
ATOM   1867  HZ  PHE A 229      21.665  14.353   5.570  1.00 59.85           H  
ATOM   1868  N   GLN A 230      15.220   9.543   6.084  1.00 37.10           N  
ANISOU 1868  N   GLN A 230     6265   5012   2817   -188    496    313       N  
ATOM   1869  CA  GLN A 230      14.238   8.473   6.135  1.00 39.72           C  
ANISOU 1869  CA  GLN A 230     6572   5419   3103   -200    314    271       C  
ATOM   1870  C   GLN A 230      14.925   7.115   6.266  1.00 41.86           C  
ANISOU 1870  C   GLN A 230     6813   5673   3418   -239    437    115       C  
ATOM   1871  O   GLN A 230      16.047   6.905   5.797  1.00 43.79           O  
ANISOU 1871  O   GLN A 230     7143   5858   3637   -276    660     40       O  
ATOM   1872  CB  GLN A 230      13.355   8.498   4.888  1.00 39.80           C  
ANISOU 1872  CB  GLN A 230     6815   5462   2844   -255    164    337       C  
ATOM   1873  CG  GLN A 230      12.689   9.837   4.637  1.00 43.97           C  
ANISOU 1873  CG  GLN A 230     7400   5994   3314   -209     31    495       C  
ATOM   1874  CD  GLN A 230      11.489   9.731   3.723  1.00 48.04           C  
ANISOU 1874  CD  GLN A 230     8074   6564   3616   -240   -209    563       C  
ATOM   1875  OE1 GLN A 230      10.645   8.846   3.884  1.00 50.73           O  
ANISOU 1875  OE1 GLN A 230     8340   6976   3961   -256   -376    525       O  
ATOM   1876  NE2 GLN A 230      11.407  10.633   2.753  1.00 47.82           N  
ANISOU 1876  NE2 GLN A 230     8271   6498   3401   -255   -235    668       N  
ATOM   1877  H   GLN A 230      15.304   9.917   5.314  1.00 44.52           H  
ATOM   1878  HA  GLN A 230      13.668   8.598   6.910  1.00 47.67           H  
ATOM   1879  HB2 GLN A 230      13.901   8.289   4.114  1.00 47.76           H  
ATOM   1880  HB3 GLN A 230      12.655   7.834   4.988  1.00 47.76           H  
ATOM   1881  HG2 GLN A 230      12.390  10.206   5.483  1.00 52.77           H  
ATOM   1882  HG3 GLN A 230      13.330  10.436   4.223  1.00 52.77           H  
ATOM   1883 HE21 GLN A 230      12.017  11.234   2.673  1.00 57.38           H  
ATOM   1884 HE22 GLN A 230      10.744  10.617   2.206  1.00 57.38           H  
ATOM   1885  N   LEU A 231      14.237   6.188   6.920  1.00 43.34           N  
ANISOU 1885  N   LEU A 231     6877   5910   3679   -230    296     68       N  
ATOM   1886  CA  LEU A 231      14.724   4.819   7.050  1.00 44.45           C  
ANISOU 1886  CA  LEU A 231     7008   6029   3853   -263    374    -76       C  
ATOM   1887  C   LEU A 231      14.286   4.016   5.836  1.00 48.69           C  
ANISOU 1887  C   LEU A 231     7778   6579   4143   -352    318   -116       C  
ATOM   1888  O   LEU A 231      13.077   3.821   5.643  1.00 49.80           O  
ANISOU 1888  O   LEU A 231     7946   6785   4192   -380     94    -64       O  
ATOM   1889  CB  LEU A 231      14.190   4.186   8.320  1.00 43.74           C  
ANISOU 1889  CB  LEU A 231     6701   5973   3946   -224    250   -104       C  
ATOM   1890  CG  LEU A 231      14.536   2.719   8.567  1.00 49.57           C  
ANISOU 1890  CG  LEU A 231     7429   6681   4726   -254    291   -243       C  
ATOM   1891  CD1 LEU A 231      16.035   2.527   8.719  1.00 48.87           C  
ANISOU 1891  CD1 LEU A 231     7317   6506   4748   -226    531   -344       C  
ATOM   1892  CD2 LEU A 231      13.795   2.205   9.802  1.00 46.67           C  
ANISOU 1892  CD2 LEU A 231     6869   6351   4511   -228    140   -242       C  
ATOM   1893  H   LEU A 231      13.479   6.326   7.302  1.00 52.01           H  
ATOM   1894  HA  LEU A 231      15.693   4.811   7.091  1.00 53.34           H  
ATOM   1895  HB2 LEU A 231      14.538   4.689   9.073  1.00 52.49           H  
ATOM   1896  HB3 LEU A 231      13.222   4.248   8.300  1.00 52.49           H  
ATOM   1897  HG  LEU A 231      14.255   2.196   7.800  1.00 59.49           H  
ATOM   1898 HD11 LEU A 231      16.216   1.592   8.906  1.00 58.65           H  
ATOM   1899 HD12 LEU A 231      16.473   2.791   7.895  1.00 58.65           H  
ATOM   1900 HD13 LEU A 231      16.351   3.077   9.453  1.00 58.65           H  
ATOM   1901 HD21 LEU A 231      14.009   1.268   9.932  1.00 56.00           H  
ATOM   1902 HD22 LEU A 231      14.077   2.719  10.576  1.00 56.00           H  
ATOM   1903 HD23 LEU A 231      12.841   2.311   9.665  1.00 56.00           H  
ATOM   1904  N   PRO A 232      15.212   3.535   5.000  1.00 42.35           N  
ANISOU 1904  N   PRO A 232     7147   5717   3228   -398    512   -209       N  
ATOM   1905  CA  PRO A 232      14.793   2.784   3.807  1.00 45.16           C  
ANISOU 1905  CA  PRO A 232     7758   6076   3324   -485    458   -252       C  
ATOM   1906  C   PRO A 232      14.073   1.496   4.185  1.00 48.98           C  
ANISOU 1906  C   PRO A 232     8193   6586   3832   -516    296   -327       C  
ATOM   1907  O   PRO A 232      14.357   0.874   5.216  1.00 47.79           O  
ANISOU 1907  O   PRO A 232     7856   6419   3883   -476    322   -396       O  
ATOM   1908  CB  PRO A 232      16.112   2.498   3.075  1.00 47.69           C  
ANISOU 1908  CB  PRO A 232     8231   6318   3572   -510    749   -358       C  
ATOM   1909  CG  PRO A 232      17.096   3.481   3.622  1.00 50.78           C  
ANISOU 1909  CG  PRO A 232     8474   6677   4144   -451    935   -324       C  
ATOM   1910  CD  PRO A 232      16.673   3.721   5.058  1.00 44.32           C  
ANISOU 1910  CD  PRO A 232     7368   5893   3577   -375    793   -278       C  
ATOM   1911  HA  PRO A 232      14.220   3.327   3.244  1.00 54.19           H  
ATOM   1912  HB2 PRO A 232      16.396   1.588   3.255  1.00 57.23           H  
ATOM   1913  HB3 PRO A 232      15.991   2.624   2.121  1.00 57.23           H  
ATOM   1914  HG2 PRO A 232      17.990   3.107   3.584  1.00 60.94           H  
ATOM   1915  HG3 PRO A 232      17.058   4.303   3.109  1.00 60.94           H  
ATOM   1916  HD2 PRO A 232      17.082   3.075   5.654  1.00 53.18           H  
ATOM   1917  HD3 PRO A 232      16.898   4.622   5.340  1.00 53.18           H  
ATOM   1918  N   LYS A 233      13.146   1.087   3.315  1.00 48.21           N  
ANISOU 1918  N   LYS A 233     8278   6521   3517   -594    121   -312       N  
ATOM   1919  CA  LYS A 233      12.320  -0.081   3.600  1.00 53.39           C  
ANISOU 1919  CA  LYS A 233     8900   7205   4183   -645    -60   -368       C  
ATOM   1920  C   LYS A 233      13.168  -1.310   3.908  1.00 49.36           C  
ANISOU 1920  C   LYS A 233     8387   6616   3750   -647     93   -529       C  
ATOM   1921  O   LYS A 233      12.824  -2.103   4.788  1.00 50.07           O  
ANISOU 1921  O   LYS A 233     8331   6711   3982   -646      3   -571       O  
ATOM   1922  CB  LYS A 233      11.397  -0.359   2.410  1.00 54.46           C  
ANISOU 1922  CB  LYS A 233     9279   7369   4046   -744   -248   -345       C  
ATOM   1923  CG  LYS A 233      10.216  -1.281   2.717  1.00 63.30           C  
ANISOU 1923  CG  LYS A 233    10330   8539   5182   -809   -503   -359       C  
ATOM   1924  CD  LYS A 233       8.952  -0.476   3.033  1.00 68.05           C  
ANISOU 1924  CD  LYS A 233    10776   9246   5835   -794   -755   -211       C  
ATOM   1925  CE  LYS A 233       7.694  -1.336   2.939  1.00 86.88           C  
ANISOU 1925  CE  LYS A 233    13150  11687   8174   -892  -1024   -216       C  
ATOM   1926  NZ  LYS A 233       7.483  -2.204   4.136  1.00 91.69           N  
ANISOU 1926  NZ  LYS A 233    13534  12306   8998   -898  -1043   -273       N  
ATOM   1927  H   LYS A 233      12.979   1.466   2.561  1.00 57.85           H  
ATOM   1928  HA  LYS A 233      11.774   0.106   4.379  1.00 64.07           H  
ATOM   1929  HB2 LYS A 233      11.034   0.485   2.098  1.00 65.36           H  
ATOM   1930  HB3 LYS A 233      11.918  -0.776   1.707  1.00 65.36           H  
ATOM   1931  HG2 LYS A 233      10.037  -1.842   1.947  1.00 75.96           H  
ATOM   1932  HG3 LYS A 233      10.429  -1.831   3.487  1.00 75.96           H  
ATOM   1933  HD2 LYS A 233       9.013  -0.125   3.935  1.00 81.66           H  
ATOM   1934  HD3 LYS A 233       8.869   0.253   2.398  1.00 81.66           H  
ATOM   1935  HE2 LYS A 233       6.922  -0.756   2.852  1.00104.26           H  
ATOM   1936  HE3 LYS A 233       7.765  -1.913   2.163  1.00104.26           H  
ATOM   1937  HZ1 LYS A 233       6.745  -2.690   4.033  1.00110.03           H  
ATOM   1938  HZ2 LYS A 233       8.177  -2.750   4.243  1.00110.03           H  
ATOM   1939  HZ3 LYS A 233       7.397  -1.700   4.865  1.00110.03           H  
ATOM   1940  N   VAL A 234      14.285  -1.482   3.195  1.00 54.19           N  
ANISOU 1940  N   VAL A 234     9163   7152   4273   -647    332   -619       N  
ATOM   1941  CA  VAL A 234      15.101  -2.679   3.357  1.00 53.23           C  
ANISOU 1941  CA  VAL A 234     9062   6949   4214   -638    478   -780       C  
ATOM   1942  C   VAL A 234      15.656  -2.800   4.770  1.00 52.10           C  
ANISOU 1942  C   VAL A 234     8636   6785   4377   -548    538   -808       C  
ATOM   1943  O   VAL A 234      16.053  -3.894   5.188  1.00 48.55           O  
ANISOU 1943  O   VAL A 234     8158   6271   4017   -533    581   -926       O  
ATOM   1944  CB  VAL A 234      16.242  -2.681   2.310  1.00 57.36           C  
ANISOU 1944  CB  VAL A 234     9797   7400   4598   -641    752   -866       C  
ATOM   1945  CG1 VAL A 234      17.314  -1.658   2.668  1.00 55.48           C  
ANISOU 1945  CG1 VAL A 234     9414   7149   4517   -565    975   -832       C  
ATOM   1946  CG2 VAL A 234      16.845  -4.077   2.177  1.00 58.73           C  
ANISOU 1946  CG2 VAL A 234    10061   7486   4770   -643    865  -1043       C  
ATOM   1947  H   VAL A 234      14.586  -0.922   2.616  1.00 65.02           H  
ATOM   1948  HA  VAL A 234      14.542  -3.455   3.199  1.00 63.88           H  
ATOM   1949  HB  VAL A 234      15.872  -2.429   1.449  1.00 68.84           H  
ATOM   1950 HG11 VAL A 234      18.008  -1.677   1.991  1.00 66.58           H  
ATOM   1951 HG12 VAL A 234      16.910  -0.776   2.702  1.00 66.58           H  
ATOM   1952 HG13 VAL A 234      17.689  -1.883   3.533  1.00 66.58           H  
ATOM   1953 HG21 VAL A 234      17.558  -4.052   1.519  1.00 70.48           H  
ATOM   1954 HG22 VAL A 234      17.199  -4.352   3.037  1.00 70.48           H  
ATOM   1955 HG23 VAL A 234      16.154  -4.694   1.891  1.00 70.48           H  
ATOM   1956  N   PHE A 235      15.678  -1.698   5.527  1.00 48.22           N  
ANISOU 1956  N   PHE A 235     7945   6336   4040   -486    532   -702       N  
ATOM   1957  CA  PHE A 235      16.196  -1.697   6.887  1.00 47.21           C  
ANISOU 1957  CA  PHE A 235     7562   6186   4190   -401    575   -719       C  
ATOM   1958  C   PHE A 235      15.088  -1.608   7.929  1.00 45.89           C  
ANISOU 1958  C   PHE A 235     7218   6087   4133   -395    348   -633       C  
ATOM   1959  O   PHE A 235      15.358  -1.304   9.091  1.00 43.47           O  
ANISOU 1959  O   PHE A 235     6706   5774   4036   -324    360   -613       O  
ATOM   1960  CB  PHE A 235      17.184  -0.552   7.070  1.00 43.83           C  
ANISOU 1960  CB  PHE A 235     7037   5740   3875   -335    757   -679       C  
ATOM   1961  CG  PHE A 235      18.334  -0.589   6.111  1.00 43.58           C  
ANISOU 1961  CG  PHE A 235     7151   5646   3760   -344   1011   -762       C  
ATOM   1962  CD1 PHE A 235      19.102  -1.733   5.979  1.00 44.29           C  
ANISOU 1962  CD1 PHE A 235     7286   5662   3880   -331   1143   -915       C  
ATOM   1963  CD2 PHE A 235      18.635   0.511   5.326  1.00 45.72           C  
ANISOU 1963  CD2 PHE A 235     7522   5928   3921   -364   1125   -688       C  
ATOM   1964  CE1 PHE A 235      20.159  -1.779   5.095  1.00 47.87           C  
ANISOU 1964  CE1 PHE A 235     7863   6062   4263   -334   1398   -999       C  
ATOM   1965  CE2 PHE A 235      19.696   0.470   4.428  1.00 51.56           C  
ANISOU 1965  CE2 PHE A 235     8397   6613   4579   -382   1384   -766       C  
ATOM   1966  CZ  PHE A 235      20.458  -0.676   4.314  1.00 48.67           C  
ANISOU 1966  CZ  PHE A 235     8058   6182   4252   -364   1527   -924       C  
ATOM   1967  H   PHE A 235      15.393  -0.930   5.265  1.00 57.86           H  
ATOM   1968  HA  PHE A 235      16.669  -2.531   7.035  1.00 56.65           H  
ATOM   1969  HB2 PHE A 235      16.716   0.288   6.939  1.00 52.59           H  
ATOM   1970  HB3 PHE A 235      17.547  -0.593   7.968  1.00 52.59           H  
ATOM   1971  HD1 PHE A 235      18.902  -2.481   6.494  1.00 53.15           H  
ATOM   1972  HD2 PHE A 235      18.123   1.284   5.400  1.00 54.86           H  
ATOM   1973  HE1 PHE A 235      20.671  -2.552   5.023  1.00 57.44           H  
ATOM   1974  HE2 PHE A 235      19.891   1.213   3.904  1.00 61.87           H  
ATOM   1975  HZ  PHE A 235      21.170  -0.707   3.716  1.00 58.40           H  
ATOM   1976  N   GLN A 236      13.844  -1.871   7.527  1.00 48.69           N  
ANISOU 1976  N   GLN A 236     7650   6504   4347   -470    144   -585       N  
ATOM   1977  CA  GLN A 236      12.712  -1.890   8.443  1.00 49.45           C  
ANISOU 1977  CA  GLN A 236     7577   6671   4541   -477    -62   -511       C  
ATOM   1978  C   GLN A 236      12.324  -3.296   8.879  1.00 47.60           C  
ANISOU 1978  C   GLN A 236     7337   6410   4340   -534   -152   -596       C  
ATOM   1979  O   GLN A 236      11.324  -3.460   9.584  1.00 43.69           O  
ANISOU 1979  O   GLN A 236     6713   5974   3912   -561   -317   -542       O  
ATOM   1980  CB  GLN A 236      11.498  -1.211   7.796  1.00 50.40           C  
ANISOU 1980  CB  GLN A 236     7746   6886   4518   -523   -250   -392       C  
ATOM   1981  CG  GLN A 236      11.753   0.216   7.348  1.00 52.56           C  
ANISOU 1981  CG  GLN A 236     8046   7178   4745   -470   -188   -293       C  
ATOM   1982  CD  GLN A 236      10.514   0.876   6.775  1.00 49.37           C  
ANISOU 1982  CD  GLN A 236     7683   6860   4215   -500   -400   -172       C  
ATOM   1983  OE1 GLN A 236       9.408   0.352   6.893  1.00 48.87           O  
ANISOU 1983  OE1 GLN A 236     7570   6859   4139   -552   -600   -153       O  
ATOM   1984  NE2 GLN A 236      10.698   2.027   6.147  1.00 51.95           N  
ANISOU 1984  NE2 GLN A 236     8098   7188   4453   -468   -360    -86       N  
ATOM   1985  H   GLN A 236      13.630  -2.045   6.712  1.00 58.43           H  
ATOM   1986  HA  GLN A 236      12.953  -1.386   9.236  1.00 59.34           H  
ATOM   1987  HB2 GLN A 236      11.236  -1.723   7.014  1.00 60.48           H  
ATOM   1988  HB3 GLN A 236      10.772  -1.193   8.439  1.00 60.48           H  
ATOM   1989  HG2 GLN A 236      12.047   0.739   8.110  1.00 63.07           H  
ATOM   1990  HG3 GLN A 236      12.438   0.215   6.662  1.00 63.07           H  
ATOM   1991 HE21 GLN A 236      11.489   2.359   6.083  1.00 62.34           H  
ATOM   1992 HE22 GLN A 236      10.028   2.441   5.804  1.00 62.34           H  
ATOM   1993  N   SER A 237      13.080  -4.312   8.466  1.00 52.12           N  
ANISOU 1993  N   SER A 237     8050   6891   4864   -554    -42   -727       N  
ATOM   1994  CA  SER A 237      12.737  -5.697   8.763  1.00 48.07           C  
ANISOU 1994  CA  SER A 237     7572   6331   4360   -616   -129   -812       C  
ATOM   1995  C   SER A 237      13.254  -6.164  10.113  1.00 43.75           C  
ANISOU 1995  C   SER A 237     6856   5725   4041   -549    -82   -854       C  
ATOM   1996  O   SER A 237      12.621  -7.017  10.741  1.00 44.51           O  
ANISOU 1996  O   SER A 237     6915   5813   4185   -602   -205   -868       O  
ATOM   1997  CB  SER A 237      13.274  -6.614   7.659  1.00 51.24           C  
ANISOU 1997  CB  SER A 237     8229   6648   4593   -662    -41   -940       C  
ATOM   1998  OG  SER A 237      14.636  -6.346   7.383  1.00 52.59           O  
ANISOU 1998  OG  SER A 237     8436   6750   4797   -578    203  -1009       O  
ATOM   1999  H   SER A 237      13.802  -4.223   8.008  1.00 62.55           H  
ATOM   2000  HA  SER A 237      11.771  -5.781   8.780  1.00 57.68           H  
ATOM   2001  HB2 SER A 237      13.187  -7.536   7.948  1.00 61.49           H  
ATOM   2002  HB3 SER A 237      12.756  -6.469   6.852  1.00 61.49           H  
ATOM   2003  HG  SER A 237      14.916  -6.867   6.786  1.00 63.11           H  
ATOM   2004  N   MET A 238      14.370  -5.631  10.577  1.00 40.83           N  
ANISOU 2004  N   MET A 238     6391   5313   3811   -443     84   -872       N  
ATOM   2005  CA  MET A 238      14.883  -6.002  11.895  1.00 41.06           C  
ANISOU 2005  CA  MET A 238     6265   5282   4056   -373    109   -906       C  
ATOM   2006  C   MET A 238      14.157  -5.203  12.973  1.00 38.56           C  
ANISOU 2006  C   MET A 238     5751   5044   3854   -351      0   -784       C  
ATOM   2007  O   MET A 238      14.023  -3.985  12.843  1.00 32.72           O  
ANISOU 2007  O   MET A 238     4949   4374   3109   -319     13   -692       O  
ATOM   2008  CB  MET A 238      16.388  -5.742  11.986  1.00 41.15           C  
ANISOU 2008  CB  MET A 238     6235   5212   4186   -268    316   -977       C  
ATOM   2009  CG  MET A 238      17.241  -6.662  11.122  1.00 45.03           C  
ANISOU 2009  CG  MET A 238     6895   5609   4607   -266    453  -1118       C  
ATOM   2010  SD  MET A 238      17.230  -8.352  11.732  1.00 53.94           S  
ANISOU 2010  SD  MET A 238     8073   6625   5798   -276    376  -1232       S  
ATOM   2011  CE  MET A 238      18.354  -8.231  13.116  1.00 50.55           C  
ANISOU 2011  CE  MET A 238     7431   6119   5656   -140    450  -1258       C  
ATOM   2012  H   MET A 238      14.851  -5.056  10.156  1.00 49.00           H  
ATOM   2013  HA  MET A 238      14.735  -6.950  12.037  1.00 49.28           H  
ATOM   2014  HB2 MET A 238      16.562  -4.830  11.704  1.00 49.38           H  
ATOM   2015  HB3 MET A 238      16.667  -5.862  12.908  1.00 49.38           H  
ATOM   2016  HG2 MET A 238      16.893  -6.664  10.217  1.00 54.04           H  
ATOM   2017  HG3 MET A 238      18.158  -6.345  11.125  1.00 54.04           H  
ATOM   2018  HE1 MET A 238      18.439  -9.104  13.531  1.00 60.66           H  
ATOM   2019  HE2 MET A 238      19.219  -7.932  12.795  1.00 60.66           H  
ATOM   2020  HE3 MET A 238      18.000  -7.594  13.756  1.00 60.66           H  
ATOM   2021  N   PRO A 239      13.676  -5.846  14.038  1.00 40.34           N  
ANISOU 2021  N   PRO A 239     5891   5257   4179   -367   -100   -781       N  
ATOM   2022  CA  PRO A 239      13.138  -5.085  15.169  1.00 40.77           C  
ANISOU 2022  CA  PRO A 239     5760   5375   4354   -330   -167   -679       C  
ATOM   2023  C   PRO A 239      14.231  -4.236  15.798  1.00 38.52           C  
ANISOU 2023  C   PRO A 239     5368   5049   4217   -212    -41   -676       C  
ATOM   2024  O   PRO A 239      15.424  -4.454  15.571  1.00 34.00           O  
ANISOU 2024  O   PRO A 239     4836   4390   3691   -160     89   -762       O  
ATOM   2025  CB  PRO A 239      12.644  -6.166  16.137  1.00 39.18           C  
ANISOU 2025  CB  PRO A 239     5530   5138   4220   -378   -262   -703       C  
ATOM   2026  CG  PRO A 239      12.492  -7.406  15.300  1.00 45.48           C  
ANISOU 2026  CG  PRO A 239     6504   5884   4891   -472   -298   -790       C  
ATOM   2027  CD  PRO A 239      13.548  -7.306  14.231  1.00 47.14           C  
ANISOU 2027  CD  PRO A 239     6839   6040   5032   -427   -156   -869       C  
ATOM   2028  HA  PRO A 239      12.387  -4.531  14.901  1.00 48.92           H  
ATOM   2029  HB2 PRO A 239      13.297  -6.302  16.841  1.00 47.02           H  
ATOM   2030  HB3 PRO A 239      11.793  -5.901  16.521  1.00 47.02           H  
ATOM   2031  HG2 PRO A 239      12.632  -8.192  15.850  1.00 54.57           H  
ATOM   2032  HG3 PRO A 239      11.605  -7.430  14.908  1.00 54.57           H  
ATOM   2033  HD2 PRO A 239      14.385  -7.691  14.532  1.00 56.57           H  
ATOM   2034  HD3 PRO A 239      13.257  -7.740  13.414  1.00 56.57           H  
ATOM   2035  N   THR A 240      13.815  -3.247  16.591  1.00 31.36           N  
ANISOU 2035  N   THR A 240     4321   4203   3392   -168    -82   -579       N  
ATOM   2036  CA  THR A 240      14.777  -2.530  17.416  1.00 30.21           C  
ANISOU 2036  CA  THR A 240     4069   4008   3403    -66      7   -577       C  
ATOM   2037  C   THR A 240      15.550  -3.551  18.248  1.00 31.28           C  
ANISOU 2037  C   THR A 240     4196   4031   3657    -35     28   -671       C  
ATOM   2038  O   THR A 240      14.972  -4.497  18.790  1.00 31.06           O  
ANISOU 2038  O   THR A 240     4187   3986   3627    -83    -63   -686       O  
ATOM   2039  CB  THR A 240      14.108  -1.505  18.346  1.00 27.74           C  
ANISOU 2039  CB  THR A 240     3620   3761   3160    -26    -57   -470       C  
ATOM   2040  OG1 THR A 240      13.399  -2.176  19.398  1.00 28.32           O  
ANISOU 2040  OG1 THR A 240     3640   3839   3281    -52   -152   -460       O  
ATOM   2041  CG2 THR A 240      13.170  -0.599  17.569  1.00 31.79           C  
ANISOU 2041  CG2 THR A 240     4138   4381   3558    -51   -110   -373       C  
ATOM   2042  H   THR A 240      13.000  -2.981  16.666  1.00 37.64           H  
ATOM   2043  HA  THR A 240      15.373  -2.024  16.842  1.00 36.26           H  
ATOM   2044  HB  THR A 240      14.792  -0.946  18.746  1.00 33.29           H  
ATOM   2045  HG1 THR A 240      13.943  -2.494  19.954  1.00 33.98           H  
ATOM   2046 HG21 THR A 240      12.866   0.128  18.135  1.00 38.14           H  
ATOM   2047 HG22 THR A 240      13.629  -0.227  16.800  1.00 38.14           H  
ATOM   2048 HG23 THR A 240      12.400  -1.102  17.263  1.00 38.14           H  
ATOM   2049  N   ARG A 241      16.863  -3.362  18.353  1.00 29.91           N  
ANISOU 2049  N   ARG A 241     3993   3777   3594     43    144   -732       N  
ATOM   2050  CA  ARG A 241      17.652  -4.270  19.171  1.00 33.70           C  
ANISOU 2050  CA  ARG A 241     4458   4143   4203     90    147   -818       C  
ATOM   2051  C   ARG A 241      17.213  -4.191  20.632  1.00 28.51           C  
ANISOU 2051  C   ARG A 241     3713   3481   3640    112     43   -763       C  
ATOM   2052  O   ARG A 241      17.182  -5.202  21.339  1.00 30.26           O  
ANISOU 2052  O   ARG A 241     3966   3632   3900    104    -22   -804       O  
ATOM   2053  CB  ARG A 241      19.137  -3.965  19.032  1.00 35.57           C  
ANISOU 2053  CB  ARG A 241     4647   4305   4564    175    284   -888       C  
ATOM   2054  CG  ARG A 241      20.009  -5.178  19.313  1.00 35.35           C  
ANISOU 2054  CG  ARG A 241     4647   4152   4631    220    303  -1008       C  
ATOM   2055  CD  ARG A 241      21.457  -4.952  18.913  1.00 38.00           C  
ANISOU 2055  CD  ARG A 241     4927   4425   5086    297    457  -1089       C  
ATOM   2056  NE  ARG A 241      22.223  -6.194  18.963  1.00 37.20           N  
ANISOU 2056  NE  ARG A 241     4866   4207   5062    346    479  -1213       N  
ATOM   2057  CZ  ARG A 241      23.462  -6.324  18.513  1.00 40.98           C  
ANISOU 2057  CZ  ARG A 241     5305   4621   5646    415    620  -1311       C  
ATOM   2058  NH1 ARG A 241      24.109  -5.304  17.975  1.00 35.99           N  
ANISOU 2058  NH1 ARG A 241     4594   4030   5052    429    761  -1298       N  
ATOM   2059  NH2 ARG A 241      24.066  -7.509  18.601  1.00 44.68           N  
ANISOU 2059  NH2 ARG A 241     5813   4976   6187    471    625  -1424       N  
ATOM   2060  H   ARG A 241      17.307  -2.733  17.970  1.00 35.89           H  
ATOM   2061  HA  ARG A 241      17.518  -5.178  18.858  1.00 40.44           H  
ATOM   2062  HB2 ARG A 241      19.316  -3.669  18.126  1.00 42.69           H  
ATOM   2063  HB3 ARG A 241      19.378  -3.268  19.663  1.00 42.69           H  
ATOM   2064  HG2 ARG A 241      19.985  -5.374  20.263  1.00 42.42           H  
ATOM   2065  HG3 ARG A 241      19.672  -5.936  18.810  1.00 42.42           H  
ATOM   2066  HD2 ARG A 241      21.490  -4.609  18.006  1.00 45.60           H  
ATOM   2067  HD3 ARG A 241      21.863  -4.317  19.523  1.00 45.60           H  
ATOM   2068  HE  ARG A 241      21.845  -6.886  19.308  1.00 44.64           H  
ATOM   2069 HH11 ARG A 241      23.726  -4.536  17.912  1.00 43.19           H  
ATOM   2070 HH12 ARG A 241      24.913  -5.408  17.688  1.00 43.19           H  
ATOM   2071 HH21 ARG A 241      23.652  -8.179  18.947  1.00 53.62           H  
ATOM   2072 HH22 ARG A 241      24.870  -7.604  18.311  1.00 53.62           H  
ATOM   2073  N   VAL A 242      16.854  -2.990  21.102  1.00 23.77           N  
ANISOU 2073  N   VAL A 242     3017   2947   3067    138     27   -670       N  
ATOM   2074  CA  VAL A 242      16.365  -2.856  22.471  1.00 27.61           C  
ANISOU 2074  CA  VAL A 242     3437   3433   3622    157    -58   -617       C  
ATOM   2075  C   VAL A 242      14.995  -3.518  22.594  1.00 28.61           C  
ANISOU 2075  C   VAL A 242     3600   3624   3648     65   -156   -576       C  
ATOM   2076  O   VAL A 242      14.253  -3.692  21.610  1.00 23.77           O  
ANISOU 2076  O   VAL A 242     3036   3085   2912    -10   -176   -559       O  
ATOM   2077  CB  VAL A 242      16.304  -1.384  22.919  1.00 24.64           C  
ANISOU 2077  CB  VAL A 242     2962   3105   3295    214    -44   -535       C  
ATOM   2078  CG1 VAL A 242      17.700  -0.759  22.912  1.00 29.35           C  
ANISOU 2078  CG1 VAL A 242     3512   3628   4011    290     45   -577       C  
ATOM   2079  CG2 VAL A 242      15.352  -0.598  22.039  1.00 26.28           C  
ANISOU 2079  CG2 VAL A 242     3169   3432   3385    176    -48   -454       C  
ATOM   2080  H   VAL A 242      16.886  -2.255  20.656  1.00 28.52           H  
ATOM   2081  HA  VAL A 242      16.986  -3.313  23.061  1.00 33.14           H  
ATOM   2082  HB  VAL A 242      15.967  -1.347  23.828  1.00 29.57           H  
ATOM   2083 HG11 VAL A 242      17.635   0.164  23.203  1.00 35.22           H  
ATOM   2084 HG12 VAL A 242      18.272  -1.257  23.516  1.00 35.22           H  
ATOM   2085 HG13 VAL A 242      18.059  -0.797  22.011  1.00 35.22           H  
ATOM   2086 HG21 VAL A 242      15.452   0.347  22.232  1.00 31.54           H  
ATOM   2087 HG22 VAL A 242      15.567  -0.770  21.109  1.00 31.54           H  
ATOM   2088 HG23 VAL A 242      14.443  -0.880  22.226  1.00 31.54           H  
ATOM   2089  N   SER A 243      14.654  -3.875  23.832  1.00 31.33           N  
ANISOU 2089  N   SER A 243     3922   3938   4043     64   -219   -557       N  
ATOM   2090  CA  SER A 243      13.407  -4.553  24.166  1.00 30.63           C  
ANISOU 2090  CA  SER A 243     3853   3900   3885    -31   -300   -518       C  
ATOM   2091  C   SER A 243      12.601  -3.686  25.124  1.00 31.20           C  
ANISOU 2091  C   SER A 243     3826   4046   3982    -12   -323   -426       C  
ATOM   2092  O   SER A 243      13.138  -3.201  26.127  1.00 29.84           O  
ANISOU 2092  O   SER A 243     3621   3819   3896     66   -308   -419       O  
ATOM   2093  CB  SER A 243      13.690  -5.916  24.801  1.00 28.17           C  
ANISOU 2093  CB  SER A 243     3633   3472   3600    -63   -342   -582       C  
ATOM   2094  OG  SER A 243      14.371  -6.746  23.895  1.00 31.56           O  
ANISOU 2094  OG  SER A 243     4158   3829   4004    -73   -317   -674       O  
ATOM   2095  H   SER A 243      15.150  -3.729  24.519  1.00 37.59           H  
ATOM   2096  HA  SER A 243      12.879  -4.686  23.363  1.00 36.75           H  
ATOM   2097  HB2 SER A 243      14.240  -5.790  25.590  1.00 33.81           H  
ATOM   2098  HB3 SER A 243      12.850  -6.334  25.044  1.00 33.81           H  
ATOM   2099  HG  SER A 243      13.905  -6.862  23.205  1.00 37.87           H  
ATOM   2100  N   LEU A 244      11.332  -3.459  24.790  1.00 27.05           N  
ANISOU 2100  N   LEU A 244     3252   3643   3383    -77   -361   -357       N  
ATOM   2101  CA  LEU A 244      10.419  -2.768  25.683  1.00 28.01           C  
ANISOU 2101  CA  LEU A 244     3274   3841   3526    -63   -375   -276       C  
ATOM   2102  C   LEU A 244      10.003  -3.709  26.806  1.00 29.36           C  
ANISOU 2102  C   LEU A 244     3475   3969   3710   -124   -403   -279       C  
ATOM   2103  O   LEU A 244       9.537  -4.822  26.552  1.00 29.01           O  
ANISOU 2103  O   LEU A 244     3488   3920   3616   -233   -447   -301       O  
ATOM   2104  CB  LEU A 244       9.188  -2.302  24.906  1.00 28.25           C  
ANISOU 2104  CB  LEU A 244     3228   4016   3488   -111   -413   -207       C  
ATOM   2105  CG  LEU A 244       9.427  -1.467  23.645  1.00 30.52           C  
ANISOU 2105  CG  LEU A 244     3518   4349   3730    -73   -401   -192       C  
ATOM   2106  CD1 LEU A 244       8.129  -1.325  22.867  1.00 35.63           C  
ANISOU 2106  CD1 LEU A 244     4109   5126   4300   -140   -478   -131       C  
ATOM   2107  CD2 LEU A 244       9.992  -0.107  23.991  1.00 35.26           C  
ANISOU 2107  CD2 LEU A 244     4066   4935   4395     50   -343   -158       C  
ATOM   2108  H   LEU A 244      10.976  -3.699  24.045  1.00 32.46           H  
ATOM   2109  HA  LEU A 244      10.853  -1.992  26.070  1.00 33.61           H  
ATOM   2110  HB2 LEU A 244       8.695  -3.091  24.631  1.00 33.90           H  
ATOM   2111  HB3 LEU A 244       8.647  -1.763  25.502  1.00 33.90           H  
ATOM   2112  HG  LEU A 244      10.078  -1.918  23.086  1.00 36.63           H  
ATOM   2113 HD11 LEU A 244       8.292  -0.788  22.076  1.00 42.75           H  
ATOM   2114 HD12 LEU A 244       7.817  -2.207  22.609  1.00 42.75           H  
ATOM   2115 HD13 LEU A 244       7.468  -0.892  23.430  1.00 42.75           H  
ATOM   2116 HD21 LEU A 244      10.116   0.401  23.174  1.00 42.31           H  
ATOM   2117 HD22 LEU A 244       9.369   0.355  24.575  1.00 42.31           H  
ATOM   2118 HD23 LEU A 244      10.843  -0.223  24.441  1.00 42.31           H  
ATOM   2119  N   CYS A 245      10.195  -3.277  28.047  1.00 26.87           N  
ANISOU 2119  N   CYS A 245     3141   3614   3456    -59   -380   -259       N  
ATOM   2120  CA  CYS A 245      10.020  -4.180  29.173  1.00 27.09           C  
ANISOU 2120  CA  CYS A 245     3234   3573   3487   -110   -400   -266       C  
ATOM   2121  C   CYS A 245       9.242  -3.513  30.291  1.00 32.48           C  
ANISOU 2121  C   CYS A 245     3850   4311   4180    -90   -369   -198       C  
ATOM   2122  O   CYS A 245       9.142  -2.283  30.367  1.00 29.85           O  
ANISOU 2122  O   CYS A 245     3432   4036   3874     -2   -334   -159       O  
ATOM   2123  CB  CYS A 245      11.365  -4.668  29.723  1.00 31.42           C  
ANISOU 2123  CB  CYS A 245     3888   3957   4092    -50   -411   -336       C  
ATOM   2124  SG  CYS A 245      12.257  -5.664  28.559  1.00 30.85           S  
ANISOU 2124  SG  CYS A 245     3904   3803   4015    -71   -430   -430       S  
ATOM   2125  H   CYS A 245      10.424  -2.475  28.258  1.00 32.25           H  
ATOM   2126  HA  CYS A 245       9.501  -4.939  28.864  1.00 32.51           H  
ATOM   2127  HB2 CYS A 245      11.914  -3.899  29.944  1.00 37.70           H  
ATOM   2128  HB3 CYS A 245      11.207  -5.202  30.518  1.00 37.70           H  
ATOM   2129  HG  CYS A 245      12.393  -5.046  27.539  1.00 37.02           H  
ATOM   2130  N   GLY A 246       8.682  -4.353  31.155  1.00 26.86           N  
ANISOU 2130  N   GLY A 246     3189   3575   3442   -173   -376   -186       N  
ATOM   2131  CA  GLY A 246       8.024  -3.875  32.353  1.00 30.70           C  
ANISOU 2131  CA  GLY A 246     3641   4094   3928   -159   -328   -131       C  
ATOM   2132  C   GLY A 246       8.258  -4.856  33.479  1.00 27.01           C  
ANISOU 2132  C   GLY A 246     3318   3505   3440   -210   -340   -148       C  
ATOM   2133  O   GLY A 246       8.340  -6.060  33.265  1.00 28.90           O  
ANISOU 2133  O   GLY A 246     3649   3679   3651   -304   -385   -179       O  
ATOM   2134  H   GLY A 246       8.672  -5.208  31.065  1.00 32.23           H  
ATOM   2135  HA2 GLY A 246       8.380  -3.010  32.606  1.00 36.84           H  
ATOM   2136  HA3 GLY A 246       7.070  -3.791  32.198  1.00 36.84           H  
ATOM   2137  N   LEU A 247       8.371  -4.325  34.689  1.00 29.72           N  
ANISOU 2137  N   LEU A 247     3697   3807   3786   -146   -303   -127       N  
ATOM   2138  CA  LEU A 247       8.666  -5.142  35.859  1.00 31.01           C  
ANISOU 2138  CA  LEU A 247     4025   3840   3917   -182   -321   -137       C  
ATOM   2139  C   LEU A 247       7.395  -5.886  36.268  1.00 33.94           C  
ANISOU 2139  C   LEU A 247     4399   4272   4223   -330   -274    -88       C  
ATOM   2140  O   LEU A 247       6.400  -5.272  36.665  1.00 34.91           O  
ANISOU 2140  O   LEU A 247     4423   4510   4333   -342   -189    -35       O  
ATOM   2141  CB  LEU A 247       9.195  -4.287  37.002  1.00 33.91           C  
ANISOU 2141  CB  LEU A 247     4449   4141   4295    -69   -304   -132       C  
ATOM   2142  CG  LEU A 247       9.979  -5.055  38.061  1.00 35.24           C  
ANISOU 2142  CG  LEU A 247     4817   4133   4439    -69   -367   -158       C  
ATOM   2143  CD1 LEU A 247      11.162  -5.812  37.456  1.00 41.88           C  
ANISOU 2143  CD1 LEU A 247     5723   4853   5336    -45   -469   -227       C  
ATOM   2144  CD2 LEU A 247      10.467  -4.097  39.146  1.00 35.23           C  
ANISOU 2144  CD2 LEU A 247     4874   4073   4441     42   -362   -154       C  
ATOM   2145  H   LEU A 247       8.280  -3.487  34.862  1.00 35.66           H  
ATOM   2146  HA  LEU A 247       9.354  -5.790  35.641  1.00 37.21           H  
ATOM   2147  HB2 LEU A 247       9.785  -3.612  36.633  1.00 40.69           H  
ATOM   2148  HB3 LEU A 247       8.442  -3.865  37.444  1.00 40.69           H  
ATOM   2149  HG  LEU A 247       9.389  -5.713  38.459  1.00 42.28           H  
ATOM   2150 HD11 LEU A 247      11.648  -6.258  38.167  1.00 50.26           H  
ATOM   2151 HD12 LEU A 247      10.827  -6.466  36.823  1.00 50.26           H  
ATOM   2152 HD13 LEU A 247      11.743  -5.180  37.003  1.00 50.26           H  
ATOM   2153 HD21 LEU A 247      10.956  -4.601  39.816  1.00 42.28           H  
ATOM   2154 HD22 LEU A 247      11.047  -3.432  38.744  1.00 42.28           H  
ATOM   2155 HD23 LEU A 247       9.700  -3.664  39.553  1.00 42.28           H  
ATOM   2156  N   ASP A 248       7.459  -7.208  36.196  1.00 32.96           N  
ANISOU 2156  N   ASP A 248     4392   4064   4066   -441   -326   -110       N  
ATOM   2157  CA  ASP A 248       6.302  -8.067  36.320  1.00 42.83           C  
ANISOU 2157  CA  ASP A 248     5641   5368   5264   -611   -293    -69       C  
ATOM   2158  C   ASP A 248       5.927  -8.306  37.774  1.00 43.45           C  
ANISOU 2158  C   ASP A 248     5834   5392   5283   -659   -230    -27       C  
ATOM   2159  O   ASP A 248       6.775  -8.298  38.668  1.00 38.39           O  
ANISOU 2159  O   ASP A 248     5350   4614   4623   -584   -258    -44       O  
ATOM   2160  CB  ASP A 248       6.596  -9.407  35.634  1.00 37.25           C  
ANISOU 2160  CB  ASP A 248     5042   4570   4541   -713   -380   -114       C  
ATOM   2161  CG  ASP A 248       5.417 -10.343  35.661  1.00 46.31           C  
ANISOU 2161  CG  ASP A 248     6190   5765   5640   -909   -359    -75       C  
ATOM   2162  OD1 ASP A 248       4.358  -9.945  35.133  1.00 41.23           O  
ANISOU 2162  OD1 ASP A 248     5366   5289   5011   -971   -317    -36       O  
ATOM   2163  OD2 ASP A 248       5.559 -11.468  36.201  1.00 50.57           O  
ANISOU 2163  OD2 ASP A 248     6911   6170   6134  -1003   -391    -81       O  
ATOM   2164  H   ASP A 248       8.190  -7.644  36.072  1.00 39.55           H  
ATOM   2165  HA  ASP A 248       5.539  -7.644  35.895  1.00 51.40           H  
ATOM   2166  HB2 ASP A 248       6.830  -9.245  34.707  1.00 44.70           H  
ATOM   2167  HB3 ASP A 248       7.334  -9.841  36.091  1.00 44.70           H  
ATOM   2168  N   GLY A 249       4.630  -8.505  38.000  1.00 38.91           N  
ANISOU 2168  N   GLY A 249     5178   4927   4677   -789   -144     28       N  
ATOM   2169  CA  GLY A 249       4.132  -9.037  39.253  1.00 39.18           C  
ANISOU 2169  CA  GLY A 249     5339   4909   4637   -887    -70     71       C  
ATOM   2170  C   GLY A 249       3.900  -8.053  40.372  1.00 45.72           C  
ANISOU 2170  C   GLY A 249     6163   5769   5438   -801     43    104       C  
ATOM   2171  O   GLY A 249       3.828  -8.478  41.532  1.00 44.21           O  
ANISOU 2171  O   GLY A 249     6144   5488   5165   -855     93    129       O  
ATOM   2172  H   GLY A 249       4.010  -8.335  37.429  1.00 46.69           H  
ATOM   2173  HA2 GLY A 249       3.286  -9.478  39.079  1.00 47.01           H  
ATOM   2174  HA3 GLY A 249       4.769  -9.693  39.577  1.00 47.01           H  
ATOM   2175  N   LEU A 250       3.727  -6.764  40.071  1.00 41.62           N  
ANISOU 2175  N   LEU A 250     5468   5370   4976   -675     90    107       N  
ATOM   2176  CA  LEU A 250       3.734  -5.744  41.105  1.00 40.91           C  
ANISOU 2176  CA  LEU A 250     5403   5281   4860   -562    181    122       C  
ATOM   2177  C   LEU A 250       2.548  -4.799  41.014  1.00 40.26           C  
ANISOU 2177  C   LEU A 250     5094   5388   4817   -539    313    162       C  
ATOM   2178  O   LEU A 250       2.098  -4.452  39.922  1.00 38.10           O  
ANISOU 2178  O   LEU A 250     4614   5242   4619   -530    290    167       O  
ATOM   2179  CB  LEU A 250       5.017  -4.900  41.021  1.00 36.74           C  
ANISOU 2179  CB  LEU A 250     4926   4665   4368   -382     93     75       C  
ATOM   2180  CG  LEU A 250       6.331  -5.615  41.317  1.00 37.23           C  
ANISOU 2180  CG  LEU A 250     5207   4529   4410   -360    -37     30       C  
ATOM   2181  CD1 LEU A 250       7.486  -4.639  41.159  1.00 30.09           C  
ANISOU 2181  CD1 LEU A 250     4297   3568   3569   -189   -111    -14       C  
ATOM   2182  CD2 LEU A 250       6.303  -6.214  42.705  1.00 39.97           C  
ANISOU 2182  CD2 LEU A 250     5781   4757   4650   -420     -9     53       C  
ATOM   2183  H   LEU A 250       3.605  -6.463  39.275  1.00 49.94           H  
ATOM   2184  HA  LEU A 250       3.667  -6.202  41.957  1.00 49.09           H  
ATOM   2185  HB2 LEU A 250       5.084  -4.544  40.121  1.00 44.09           H  
ATOM   2186  HB3 LEU A 250       4.939  -4.173  41.660  1.00 44.09           H  
ATOM   2187  HG  LEU A 250       6.463  -6.344  40.691  1.00 44.68           H  
ATOM   2188 HD11 LEU A 250       8.252  -4.974  41.651  1.00 36.11           H  
ATOM   2189 HD12 LEU A 250       7.706  -4.561  40.218  1.00 36.11           H  
ATOM   2190 HD13 LEU A 250       7.220  -3.775  41.510  1.00 36.11           H  
ATOM   2191 HD21 LEU A 250       7.197  -6.509  42.940  1.00 47.97           H  
ATOM   2192 HD22 LEU A 250       6.001  -5.540  43.334  1.00 47.97           H  
ATOM   2193 HD23 LEU A 250       5.693  -6.968  42.711  1.00 47.97           H  
ATOM   2194  N   THR A 251       2.066  -4.373  42.181  1.00 41.12           N  
ANISOU 2194  N   THR A 251     5249   5506   4870   -521    448    188       N  
ATOM   2195  CA  THR A 251       1.106  -3.281  42.319  1.00 40.04           C  
ANISOU 2195  CA  THR A 251     4919   5521   4773   -449    586    215       C  
ATOM   2196  C   THR A 251       1.801  -2.173  43.098  1.00 34.78           C  
ANISOU 2196  C   THR A 251     4362   4776   4076   -273    608    191       C  
ATOM   2197  O   THR A 251       2.118  -2.348  44.279  1.00 36.47           O  
ANISOU 2197  O   THR A 251     4792   4876   4191   -277    652    187       O  
ATOM   2198  CB  THR A 251      -0.159  -3.739  43.031  1.00 40.60           C  
ANISOU 2198  CB  THR A 251     4942   5678   4807   -587    756    261       C  
ATOM   2199  OG1 THR A 251      -0.690  -4.885  42.364  1.00 42.67           O  
ANISOU 2199  OG1 THR A 251     5135   5984   5092   -772    714    281       O  
ATOM   2200  CG2 THR A 251      -1.198  -2.623  43.026  1.00 37.38           C  
ANISOU 2200  CG2 THR A 251     4292   5442   4469   -500    896    283       C  
ATOM   2201  H   THR A 251       2.291  -4.716  42.937  1.00 49.35           H  
ATOM   2202  HA  THR A 251       0.850  -2.952  41.444  1.00 48.05           H  
ATOM   2203  HB  THR A 251       0.045  -3.966  43.952  1.00 48.72           H  
ATOM   2204  HG1 THR A 251      -1.368  -5.166  42.771  1.00 51.20           H  
ATOM   2205 HG21 THR A 251      -2.030  -2.944  43.407  1.00 44.85           H  
ATOM   2206 HG22 THR A 251      -0.880  -1.872  43.551  1.00 44.85           H  
ATOM   2207 HG23 THR A 251      -1.362  -2.326  42.118  1.00 44.85           H  
ATOM   2208  N   TRP A 252       2.052  -1.048  42.436  1.00 38.70           N  
ANISOU 2208  N   TRP A 252     4728   5324   4651   -125    570    175       N  
ATOM   2209  CA  TRP A 252       2.858   0.007  43.040  1.00 41.35           C  
ANISOU 2209  CA  TRP A 252     5175   5567   4968     37    560    145       C  
ATOM   2210  C   TRP A 252       2.014   0.921  43.920  1.00 42.87           C  
ANISOU 2210  C   TRP A 252     5330   5826   5133    112    733    162       C  
ATOM   2211  O   TRP A 252       0.861   1.232  43.598  1.00 41.03           O  
ANISOU 2211  O   TRP A 252     4883   5751   4955    105    839    192       O  
ATOM   2212  CB  TRP A 252       3.525   0.839  41.945  1.00 39.46           C  
ANISOU 2212  CB  TRP A 252     4829   5342   4822    156    450    123       C  
ATOM   2213  CG  TRP A 252       4.706   0.187  41.325  1.00 37.68           C  
ANISOU 2213  CG  TRP A 252     4693   5008   4615    131    292     88       C  
ATOM   2214  CD1 TRP A 252       4.712  -0.673  40.261  1.00 36.00           C  
ANISOU 2214  CD1 TRP A 252     4412   4829   4437     36    215     86       C  
ATOM   2215  CD2 TRP A 252       6.068   0.333  41.734  1.00 33.48           C  
ANISOU 2215  CD2 TRP A 252     4335   4312   4073    206    192     44       C  
ATOM   2216  NE1 TRP A 252       6.003  -1.069  39.983  1.00 37.13           N  
ANISOU 2216  NE1 TRP A 252     4674   4839   4593     56     89     40       N  
ATOM   2217  CE2 TRP A 252       6.853  -0.459  40.869  1.00 36.09           C  
ANISOU 2217  CE2 TRP A 252     4678   4589   4445    159     69     15       C  
ATOM   2218  CE3 TRP A 252       6.703   1.061  42.745  1.00 33.82           C  
ANISOU 2218  CE3 TRP A 252     4523   4246   4080    306    190     22       C  
ATOM   2219  CZ2 TRP A 252       8.239  -0.537  40.987  1.00 32.35           C  
ANISOU 2219  CZ2 TRP A 252     4331   3965   3994    216    -48    -33       C  
ATOM   2220  CZ3 TRP A 252       8.079   0.975  42.861  1.00 36.57           C  
ANISOU 2220  CZ3 TRP A 252     5003   4443   4448    352     54    -22       C  
ATOM   2221  CH2 TRP A 252       8.828   0.181  41.993  1.00 34.32           C  
ANISOU 2221  CH2 TRP A 252     4704   4116   4221    310    -59    -49       C  
ATOM   2222  H   TRP A 252       1.770  -0.873  41.643  1.00 46.44           H  
ATOM   2223  HA  TRP A 252       3.539  -0.399  43.598  1.00 49.62           H  
ATOM   2224  HB2 TRP A 252       2.877   1.005  41.242  1.00 47.35           H  
ATOM   2225  HB3 TRP A 252       3.820   1.680  42.329  1.00 47.35           H  
ATOM   2226  HD1 TRP A 252       3.957  -0.949  39.795  1.00 43.20           H  
ATOM   2227  HE1 TRP A 252       6.237  -1.610  39.357  1.00 44.55           H  
ATOM   2228  HE3 TRP A 252       6.210   1.593  43.327  1.00 40.58           H  
ATOM   2229  HZ2 TRP A 252       8.744  -1.057  40.405  1.00 38.81           H  
ATOM   2230  HZ3 TRP A 252       8.512   1.454  43.530  1.00 43.88           H  
ATOM   2231  HH2 TRP A 252       9.751   0.139  42.099  1.00 41.19           H  
ATOM   2232  N   SER A 253       2.599   1.354  45.039  1.00 45.26           N  
ANISOU 2232  N   SER A 253     5843   6003   5350    187    756    138       N  
ATOM   2233  CA  SER A 253       1.974   2.392  45.851  1.00 49.00           C  
ANISOU 2233  CA  SER A 253     6308   6517   5793    290    914    138       C  
ATOM   2234  C   SER A 253       1.888   3.676  45.036  1.00 50.83           C  
ANISOU 2234  C   SER A 253     6349   6828   6135    444    896    132       C  
ATOM   2235  O   SER A 253       2.881   4.067  44.405  1.00 48.10           O  
ANISOU 2235  O   SER A 253     6022   6414   5839    513    749    109       O  
ATOM   2236  CB  SER A 253       2.773   2.639  47.124  1.00 48.90           C  
ANISOU 2236  CB  SER A 253     6589   6333   5658    346    908    106       C  
ATOM   2237  OG  SER A 253       2.712   1.520  47.991  1.00 60.13           O  
ANISOU 2237  OG  SER A 253     8207   7680   6959    209    943    121       O  
ATOM   2238  H   SER A 253       3.349   1.064  45.345  1.00 54.31           H  
ATOM   2239  HA  SER A 253       1.082   2.112  46.108  1.00 58.80           H  
ATOM   2240  HB2 SER A 253       3.699   2.804  46.887  1.00 58.68           H  
ATOM   2241  HB3 SER A 253       2.406   3.412  47.581  1.00 58.68           H  
ATOM   2242  HG  SER A 253       3.121   1.688  48.706  1.00 72.15           H  
ATOM   2243  N   PRO A 254       0.735   4.350  45.008  1.00 61.36           N  
ANISOU 2243  N   PRO A 254     7055   7952   8306   1537   1096  -1064       N  
ATOM   2244  CA  PRO A 254       0.642   5.585  44.202  1.00 64.73           C  
ANISOU 2244  CA  PRO A 254     7496   8226   8874   1637   1016  -1101       C  
ATOM   2245  C   PRO A 254       1.673   6.637  44.582  1.00 57.15           C  
ANISOU 2245  C   PRO A 254     6755   7081   7879   1671    941  -1242       C  
ATOM   2246  O   PRO A 254       2.127   7.389  43.712  1.00 55.98           O  
ANISOU 2246  O   PRO A 254     6659   6769   7843   1662    826  -1242       O  
ATOM   2247  CB  PRO A 254      -0.792   6.076  44.466  1.00 62.78           C  
ANISOU 2247  CB  PRO A 254     7109   8067   8677   1828   1152  -1113       C  
ATOM   2248  CG  PRO A 254      -1.549   4.839  44.851  1.00 65.76           C  
ANISOU 2248  CG  PRO A 254     7324   8662   8998   1764   1273  -1020       C  
ATOM   2249  CD  PRO A 254      -0.563   3.964  45.594  1.00 66.99           C  
ANISOU 2249  CD  PRO A 254     7614   8844   8994   1622   1270  -1029       C  
ATOM   2250  HA  PRO A 254       0.736   5.368  43.261  1.00 77.68           H  
ATOM   2251  HB2 PRO A 254      -0.793   6.725  45.188  1.00 75.34           H  
ATOM   2252  HB3 PRO A 254      -1.160   6.475  43.662  1.00 75.34           H  
ATOM   2253  HG2 PRO A 254      -2.296   5.077  45.423  1.00 78.91           H  
ATOM   2254  HG3 PRO A 254      -1.872   4.392  44.053  1.00 78.91           H  
ATOM   2255  HD2 PRO A 254      -0.583   4.151  46.546  1.00 80.38           H  
ATOM   2256  HD3 PRO A 254      -0.748   3.025  45.437  1.00 80.38           H  
ATOM   2257  N   VAL A 255       2.063   6.712  45.856  1.00 53.74           N  
ANISOU 2257  N   VAL A 255     6457   6672   7292   1704   1000  -1362       N  
ATOM   2258  CA  VAL A 255       3.049   7.701  46.265  1.00 55.38           C  
ANISOU 2258  CA  VAL A 255     6872   6707   7465   1721    918  -1513       C  
ATOM   2259  C   VAL A 255       4.419   7.410  45.661  1.00 52.05           C  
ANISOU 2259  C   VAL A 255     6524   6193   7062   1532    756  -1478       C  
ATOM   2260  O   VAL A 255       5.245   8.319  45.547  1.00 51.26           O  
ANISOU 2260  O   VAL A 255     6558   5918   7001   1514    657  -1569       O  
ATOM   2261  CB  VAL A 255       3.134   7.760  47.806  1.00 55.69           C  
ANISOU 2261  CB  VAL A 255     7036   6817   7308   1796   1013  -1655       C  
ATOM   2262  CG1 VAL A 255       3.987   6.613  48.345  1.00 56.68           C  
ANISOU 2262  CG1 VAL A 255     7205   7052   7280   1644    981  -1616       C  
ATOM   2263  CG2 VAL A 255       3.673   9.111  48.262  1.00 60.82           C  
ANISOU 2263  CG2 VAL A 255     7883   7278   7949   1880    959  -1844       C  
ATOM   2264  H   VAL A 255       1.774   6.208  46.490  1.00 64.49           H  
ATOM   2265  HA  VAL A 255       2.764   8.570  45.943  1.00 66.46           H  
ATOM   2266  HB  VAL A 255       2.242   7.660  48.174  1.00 66.83           H  
ATOM   2267 HG11 VAL A 255       3.991   6.650  49.314  1.00 68.02           H  
ATOM   2268 HG12 VAL A 255       3.608   5.771  48.047  1.00 68.02           H  
ATOM   2269 HG13 VAL A 255       4.892   6.707  48.007  1.00 68.02           H  
ATOM   2270 HG21 VAL A 255       3.720   9.122  49.231  1.00 72.99           H  
ATOM   2271 HG22 VAL A 255       4.558   9.240  47.887  1.00 72.99           H  
ATOM   2272 HG23 VAL A 255       3.077   9.810  47.952  1.00 72.99           H  
ATOM   2273  N   ALA A 256       4.681   6.161  45.270  1.00 46.03           N  
ANISOU 2273  N   ALA A 256     5673   5540   6277   1390    732  -1349       N  
ATOM   2274  CA  ALA A 256       5.979   5.778  44.737  1.00 48.09           C  
ANISOU 2274  CA  ALA A 256     5989   5738   6547   1222    594  -1313       C  
ATOM   2275  C   ALA A 256       6.112   6.022  43.240  1.00 44.45           C  
ANISOU 2275  C   ALA A 256     5465   5172   6252   1161    500  -1216       C  
ATOM   2276  O   ALA A 256       7.230   6.234  42.750  1.00 45.79           O  
ANISOU 2276  O   ALA A 256     5706   5236   6457   1055    385  -1220       O  
ATOM   2277  CB  ALA A 256       6.248   4.297  45.028  1.00 47.00           C  
ANISOU 2277  CB  ALA A 256     5805   5752   6302   1112    614  -1223       C  
ATOM   2278  H   ALA A 256       4.114   5.515  45.304  1.00 55.24           H  
ATOM   2279  HA  ALA A 256       6.659   6.307  45.183  1.00 57.71           H  
ATOM   2280  HB1 ALA A 256       7.115   4.057  44.667  1.00 56.40           H  
ATOM   2281  HB2 ALA A 256       6.240   4.158  45.988  1.00 56.40           H  
ATOM   2282  HB3 ALA A 256       5.556   3.762  44.610  1.00 56.40           H  
ATOM   2283  N   ILE A 257       5.007   6.004  42.508  1.00 44.09           N  
ANISOU 2283  N   ILE A 257     5283   5166   6305   1224    544  -1127       N  
ATOM   2284  CA  ILE A 257       5.025   6.095  41.051  1.00 44.30           C  
ANISOU 2284  CA  ILE A 257     5242   5126   6466   1170    456  -1017       C  
ATOM   2285  C   ILE A 257       5.837   7.296  40.581  1.00 40.24           C  
ANISOU 2285  C   ILE A 257     4854   4404   6031   1167    360  -1069       C  
ATOM   2286  O   ILE A 257       6.538   7.190  39.563  1.00 37.08           O  
ANISOU 2286  O   ILE A 257     4456   3943   5690   1054    266   -992       O  
ATOM   2287  CB  ILE A 257       3.585   6.136  40.500  1.00 41.63           C  
ANISOU 2287  CB  ILE A 257     4741   4862   6216   1277    516   -939       C  
ATOM   2288  CG1 ILE A 257       2.905   4.779  40.754  1.00 46.21           C  
ANISOU 2288  CG1 ILE A 257     5178   5643   6736   1222    596   -863       C  
ATOM   2289  CG2 ILE A 257       3.573   6.487  39.024  1.00 38.71           C  
ANISOU 2289  CG2 ILE A 257     4327   4409   5973   1252    414   -840       C  
ATOM   2290  CD1 ILE A 257       1.453   4.694  40.289  1.00 45.41           C  
ANISOU 2290  CD1 ILE A 257     4884   5649   6719   1308    654   -788       C  
ATOM   2291  H   ILE A 257       4.216   5.939  42.837  1.00 52.91           H  
ATOM   2292  HA  ILE A 257       5.483   5.312  40.706  1.00 53.16           H  
ATOM   2293  HB  ILE A 257       3.090   6.830  40.964  1.00 49.96           H  
ATOM   2294 HG12 ILE A 257       3.403   4.092  40.284  1.00 55.45           H  
ATOM   2295 HG13 ILE A 257       2.917   4.603  41.708  1.00 55.45           H  
ATOM   2296 HG21 ILE A 257       2.682   6.338  38.671  1.00 46.46           H  
ATOM   2297 HG22 ILE A 257       3.819   7.420  38.919  1.00 46.46           H  
ATOM   2298 HG23 ILE A 257       4.211   5.923  38.560  1.00 46.46           H  
ATOM   2299 HD11 ILE A 257       1.041   3.907  40.681  1.00 54.49           H  
ATOM   2300 HD12 ILE A 257       0.982   5.491  40.576  1.00 54.49           H  
ATOM   2301 HD13 ILE A 257       1.434   4.629  39.322  1.00 54.49           H  
ATOM   2302  N   PRO A 258       5.786   8.448  41.258  1.00 38.78           N  
ANISOU 2302  N   PRO A 258     4782   4102   5853   1281    382  -1197       N  
ATOM   2303  CA  PRO A 258       6.652   9.566  40.838  1.00 38.48           C  
ANISOU 2303  CA  PRO A 258     4878   3845   5897   1250    288  -1246       C  
ATOM   2304  C   PRO A 258       8.140   9.239  40.897  1.00 41.51           C  
ANISOU 2304  C   PRO A 258     5341   4196   6233   1069    196  -1268       C  
ATOM   2305  O   PRO A 258       8.935   9.924  40.241  1.00 39.10           O  
ANISOU 2305  O   PRO A 258     5107   3734   6015    994    111  -1260       O  
ATOM   2306  CB  PRO A 258       6.287  10.691  41.819  1.00 40.66           C  
ANISOU 2306  CB  PRO A 258     5272   4016   6162   1406    344  -1406       C  
ATOM   2307  CG  PRO A 258       4.907  10.361  42.273  1.00 41.51           C  
ANISOU 2307  CG  PRO A 258     5261   4277   6235   1562    473  -1395       C  
ATOM   2308  CD  PRO A 258       4.831   8.854  42.312  1.00 44.41           C  
ANISOU 2308  CD  PRO A 258     5499   4862   6514   1454    502  -1296       C  
ATOM   2309  HA  PRO A 258       6.420   9.843  39.938  1.00 46.17           H  
ATOM   2310  HB2 PRO A 258       6.908  10.695  42.565  1.00 48.79           H  
ATOM   2311  HB3 PRO A 258       6.309  11.547  41.365  1.00 48.79           H  
ATOM   2312  HG2 PRO A 258       4.756  10.734  43.155  1.00 49.81           H  
ATOM   2313  HG3 PRO A 258       4.262  10.721  41.645  1.00 49.81           H  
ATOM   2314  HD2 PRO A 258       5.106   8.515  43.178  1.00 53.30           H  
ATOM   2315  HD3 PRO A 258       3.935   8.547  42.105  1.00 53.30           H  
ATOM   2316  N   SER A 259       8.540   8.208  41.642  1.00 38.44           N  
ANISOU 2316  N   SER A 259     4937   3955   5714    999    212  -1286       N  
ATOM   2317  CA  SER A 259       9.952   7.846  41.748  1.00 44.71           C  
ANISOU 2317  CA  SER A 259     5788   4739   6460    844    121  -1306       C  
ATOM   2318  C   SER A 259      10.449   6.953  40.615  1.00 38.94           C  
ANISOU 2318  C   SER A 259     4965   4059   5771    715     69  -1159       C  
ATOM   2319  O   SER A 259      11.627   6.579  40.623  1.00 38.80           O  
ANISOU 2319  O   SER A 259     4973   4048   5722    594     -1  -1163       O  
ATOM   2320  CB  SER A 259      10.211   7.137  43.085  1.00 40.87           C  
ANISOU 2320  CB  SER A 259     5338   4387   5803    843    152  -1386       C  
ATOM   2321  OG  SER A 259      10.122   8.033  44.174  1.00 45.34           O  
ANISOU 2321  OG  SER A 259     6026   4893   6309    936    175  -1552       O  
ATOM   2322  H   SER A 259       8.012   7.703  42.096  1.00 46.13           H  
ATOM   2323  HA  SER A 259      10.467   8.667  41.723  1.00 53.65           H  
ATOM   2324  HB2 SER A 259       9.550   6.437  43.202  1.00 49.04           H  
ATOM   2325  HB3 SER A 259      11.102   6.753  43.068  1.00 49.04           H  
ATOM   2326  HG  SER A 259      10.272   7.626  44.894  1.00 54.41           H  
ATOM   2327  N   PHE A 260       9.596   6.613  39.646  1.00 39.21           N  
ANISOU 2327  N   PHE A 260     4892   4134   5873    743     97  -1036       N  
ATOM   2328  CA  PHE A 260       9.987   5.635  38.631  1.00 37.82           C  
ANISOU 2328  CA  PHE A 260     4636   4023   5711    628     57   -910       C  
ATOM   2329  C   PHE A 260      11.267   6.055  37.899  1.00 37.76           C  
ANISOU 2329  C   PHE A 260     4682   3903   5760    512    -35   -893       C  
ATOM   2330  O   PHE A 260      12.147   5.222  37.638  1.00 31.36           O  
ANISOU 2330  O   PHE A 260     3849   3152   4914    403    -72   -851       O  
ATOM   2331  CB  PHE A 260       8.852   5.433  37.632  1.00 37.18           C  
ANISOU 2331  CB  PHE A 260     4443   3984   5698    679     83   -797       C  
ATOM   2332  CG  PHE A 260       7.770   4.464  38.102  1.00 38.02           C  
ANISOU 2332  CG  PHE A 260     4446   4254   5748    725    168   -769       C  
ATOM   2333  CD1 PHE A 260       7.793   3.925  39.382  1.00 32.37           C  
ANISOU 2333  CD1 PHE A 260     3753   3626   4918    737    232   -836       C  
ATOM   2334  CD2 PHE A 260       6.755   4.085  37.244  1.00 37.06           C  
ANISOU 2334  CD2 PHE A 260     4199   4201   5681    747    180   -670       C  
ATOM   2335  CE1 PHE A 260       6.818   3.045  39.789  1.00 38.03           C  
ANISOU 2335  CE1 PHE A 260     4374   4486   5589    765    321   -796       C  
ATOM   2336  CE2 PHE A 260       5.768   3.202  37.646  1.00 36.37           C  
ANISOU 2336  CE2 PHE A 260     4002   4261   5556    768    259   -641       C  
ATOM   2337  CZ  PHE A 260       5.800   2.682  38.919  1.00 39.14           C  
ANISOU 2337  CZ  PHE A 260     4380   4689   5804    773    337   -699       C  
ATOM   2338  H   PHE A 260       8.801   6.927  39.556  1.00 47.06           H  
ATOM   2339  HA  PHE A 260      10.160   4.790  39.075  1.00 45.38           H  
ATOM   2340  HB2 PHE A 260       8.428   6.290  37.466  1.00 44.61           H  
ATOM   2341  HB3 PHE A 260       9.223   5.082  36.807  1.00 44.61           H  
ATOM   2342  HD1 PHE A 260       8.473   4.163  39.970  1.00 38.84           H  
ATOM   2343  HD2 PHE A 260       6.735   4.429  36.380  1.00 44.47           H  
ATOM   2344  HE1 PHE A 260       6.842   2.692  40.649  1.00 45.63           H  
ATOM   2345  HE2 PHE A 260       5.087   2.962  37.060  1.00 43.65           H  
ATOM   2346  HZ  PHE A 260       5.140   2.088  39.196  1.00 46.97           H  
ATOM   2347  N   ASP A 261      11.386   7.340  37.542  1.00 33.59           N  
ANISOU 2347  N   ASP A 261     4226   3209   5328    536    -66   -920       N  
ATOM   2348  CA  ASP A 261      12.597   7.804  36.862  1.00 37.97           C  
ANISOU 2348  CA  ASP A 261     4828   3654   5945    413   -141   -896       C  
ATOM   2349  C   ASP A 261      13.831   7.592  37.735  1.00 37.60           C  
ANISOU 2349  C   ASP A 261     4826   3628   5834    316   -185   -992       C  
ATOM   2350  O   ASP A 261      14.839   7.040  37.284  1.00 37.19           O  
ANISOU 2350  O   ASP A 261     4738   3617   5777    198   -228   -943       O  
ATOM   2351  CB  ASP A 261      12.471   9.276  36.479  1.00 41.62           C  
ANISOU 2351  CB  ASP A 261     5378   3914   6524    456   -159   -913       C  
ATOM   2352  CG  ASP A 261      11.466   9.507  35.360  1.00 43.70           C  
ANISOU 2352  CG  ASP A 261     5591   4153   6858    540   -141   -788       C  
ATOM   2353  OD1 ASP A 261      11.017   8.521  34.735  1.00 40.31           O  
ANISOU 2353  OD1 ASP A 261     5056   3865   6395    534   -129   -688       O  
ATOM   2354  OD2 ASP A 261      11.119  10.688  35.120  1.00 50.39           O  
ANISOU 2354  OD2 ASP A 261     6513   4837   7797    616   -145   -792       O  
ATOM   2355  H   ASP A 261      10.793   7.948  37.680  1.00 40.31           H  
ATOM   2356  HA  ASP A 261      12.700   7.290  36.046  1.00 45.56           H  
ATOM   2357  HB2 ASP A 261      12.179   9.780  37.254  1.00 49.95           H  
ATOM   2358  HB3 ASP A 261      13.335   9.599  36.179  1.00 49.95           H  
ATOM   2359  N   ASN A 262      13.770   8.032  38.995  1.00 38.87           N  
ANISOU 2359  N   ASN A 262     5063   3768   5938    370   -177  -1134       N  
ATOM   2360  CA  ASN A 262      14.894   7.810  39.903  1.00 40.94           C  
ANISOU 2360  CA  ASN A 262     5364   4070   6121    287   -234  -1231       C  
ATOM   2361  C   ASN A 262      15.219   6.327  40.031  1.00 40.86           C  
ANISOU 2361  C   ASN A 262     5270   4246   6009    246   -230  -1166       C  
ATOM   2362  O   ASN A 262      16.397   5.938  40.077  1.00 41.53           O  
ANISOU 2362  O   ASN A 262     5338   4369   6072    143   -295  -1169       O  
ATOM   2363  CB  ASN A 262      14.593   8.400  41.283  1.00 46.09           C  
ANISOU 2363  CB  ASN A 262     6118   4698   6696    374   -220  -1397       C  
ATOM   2364  CG  ASN A 262      14.467   9.908  41.258  1.00 47.77           C  
ANISOU 2364  CG  ASN A 262     6440   4699   7012    406   -237  -1487       C  
ATOM   2365  OD1 ASN A 262      14.816  10.556  40.273  1.00 46.47           O  
ANISOU 2365  OD1 ASN A 262     6283   4395   6978    339   -272  -1425       O  
ATOM   2366  ND2 ASN A 262      13.973  10.475  42.352  1.00 47.28           N  
ANISOU 2366  ND2 ASN A 262     6474   4604   6886    513   -206  -1634       N  
ATOM   2367  H   ASN A 262      13.105   8.453  39.340  1.00 46.64           H  
ATOM   2368  HA  ASN A 262      15.670   8.265  39.541  1.00 49.13           H  
ATOM   2369  HB2 ASN A 262      13.755   8.034  41.607  1.00 55.31           H  
ATOM   2370  HB3 ASN A 262      15.313   8.168  41.890  1.00 55.31           H  
ATOM   2371 HD21 ASN A 262      13.881  11.329  42.390  1.00 56.73           H  
ATOM   2372 HD22 ASN A 262      13.745   9.988  43.024  1.00 56.73           H  
ATOM   2373  N   ILE A 263      14.189   5.481  40.104  1.00 35.61           N  
ANISOU 2373  N   ILE A 263     4549   3694   5288    326   -152  -1105       N  
ATOM   2374  CA  ILE A 263      14.439   4.048  40.236  1.00 39.80           C  
ANISOU 2374  CA  ILE A 263     5018   4378   5728    290   -141  -1038       C  
ATOM   2375  C   ILE A 263      15.118   3.507  38.984  1.00 34.78           C  
ANISOU 2375  C   ILE A 263     4315   3745   5156    191   -180   -926       C  
ATOM   2376  O   ILE A 263      16.012   2.654  39.067  1.00 32.77           O  
ANISOU 2376  O   ILE A 263     4036   3566   4851    129   -213   -902       O  
ATOM   2377  CB  ILE A 263      13.134   3.297  40.528  1.00 39.35           C  
ANISOU 2377  CB  ILE A 263     4913   4426   5614    379    -43   -992       C  
ATOM   2378  CG1 ILE A 263      12.561   3.749  41.874  1.00 44.29           C  
ANISOU 2378  CG1 ILE A 263     5606   5072   6149    482     11  -1107       C  
ATOM   2379  CG2 ILE A 263      13.372   1.795  40.543  1.00 38.40           C  
ANISOU 2379  CG2 ILE A 263     4741   4432   5417    331    -30   -909       C  
ATOM   2380  CD1 ILE A 263      11.055   3.616  41.967  1.00 45.29           C  
ANISOU 2380  CD1 ILE A 263     5677   5256   6276    589    122  -1072       C  
ATOM   2381  H   ILE A 263      13.360   5.706  40.079  1.00 42.74           H  
ATOM   2382  HA  ILE A 263      15.036   3.914  40.989  1.00 47.76           H  
ATOM   2383  HB  ILE A 263      12.499   3.503  39.825  1.00 47.22           H  
ATOM   2384 HG12 ILE A 263      12.950   3.207  42.578  1.00 53.15           H  
ATOM   2385 HG13 ILE A 263      12.785   4.683  42.012  1.00 53.15           H  
ATOM   2386 HG21 ILE A 263      12.590   1.355  40.912  1.00 46.08           H  
ATOM   2387 HG22 ILE A 263      13.526   1.491  39.635  1.00 46.08           H  
ATOM   2388 HG23 ILE A 263      14.148   1.604  41.092  1.00 46.08           H  
ATOM   2389 HD11 ILE A 263      10.764   3.914  42.843  1.00 54.35           H  
ATOM   2390 HD12 ILE A 263      10.646   4.164  41.278  1.00 54.35           H  
ATOM   2391 HD13 ILE A 263      10.811   2.686  41.836  1.00 54.35           H  
ATOM   2392  N   ARG A 264      14.725   4.013  37.810  1.00 32.25           N  
ANISOU 2392  N   ARG A 264     3968   3344   4940    186   -175   -854       N  
ATOM   2393  CA  ARG A 264      15.367   3.578  36.574  1.00 39.68           C  
ANISOU 2393  CA  ARG A 264     4858   4290   5929     98   -203   -752       C  
ATOM   2394  C   ARG A 264      16.845   3.951  36.555  1.00 36.31           C  
ANISOU 2394  C   ARG A 264     4450   3818   5529     -4   -270   -785       C  
ATOM   2395  O   ARG A 264      17.680   3.168  36.093  1.00 36.66           O  
ANISOU 2395  O   ARG A 264     4444   3928   5558    -72   -288   -732       O  
ATOM   2396  CB  ARG A 264      14.650   4.170  35.359  1.00 30.13           C  
ANISOU 2396  CB  ARG A 264     3633   3004   4811    121   -191   -669       C  
ATOM   2397  CG  ARG A 264      13.595   3.224  34.769  1.00 39.14           C  
ANISOU 2397  CG  ARG A 264     4700   4242   5928    162   -150   -582       C  
ATOM   2398  CD  ARG A 264      13.027   3.718  33.433  1.00 35.28           C  
ANISOU 2398  CD  ARG A 264     4190   3700   5515    177   -160   -489       C  
ATOM   2399  NE  ARG A 264      12.191   4.908  33.602  1.00 34.19           N  
ANISOU 2399  NE  ARG A 264     4084   3467   5441    275   -150   -516       N  
ATOM   2400  CZ  ARG A 264      10.921   4.888  33.987  1.00 39.41           C  
ANISOU 2400  CZ  ARG A 264     4702   4173   6098    382   -107   -528       C  
ATOM   2401  NH1 ARG A 264      10.282   3.746  34.235  1.00 33.11           N  
ANISOU 2401  NH1 ARG A 264     3825   3514   5240    388    -69   -509       N  
ATOM   2402  NH2 ARG A 264      10.270   6.043  34.135  1.00 45.54           N  
ANISOU 2402  NH2 ARG A 264     5514   4851   6939    486    -96   -557       N  
ATOM   2403  H   ARG A 264      14.101   4.596  37.707  1.00 38.70           H  
ATOM   2404  HA  ARG A 264      15.298   2.612  36.517  1.00 47.62           H  
ATOM   2405  HB2 ARG A 264      14.203   4.989  35.626  1.00 36.15           H  
ATOM   2406  HB3 ARG A 264      15.304   4.359  34.668  1.00 36.15           H  
ATOM   2407  HG2 ARG A 264      13.999   2.355  34.619  1.00 46.96           H  
ATOM   2408  HG3 ARG A 264      12.858   3.143  35.395  1.00 46.96           H  
ATOM   2409  HD2 ARG A 264      13.759   3.943  32.838  1.00 42.34           H  
ATOM   2410  HD3 ARG A 264      12.482   3.018  33.039  1.00 42.34           H  
ATOM   2411  HE  ARG A 264      12.548   5.674  33.440  1.00 41.03           H  
ATOM   2412 HH11 ARG A 264       9.459   3.758  34.484  1.00 39.73           H  
ATOM   2413 HH12 ARG A 264      10.693   2.995  34.147  1.00 39.73           H  
ATOM   2414 HH21 ARG A 264      10.673   6.787  33.980  1.00 54.65           H  
ATOM   2415 HH22 ARG A 264       9.447   6.044  34.384  1.00 54.65           H  
ATOM   2416  N   GLU A 265      17.187   5.146  37.046  1.00 35.49           N  
ANISOU 2416  N   GLU A 265     4414   3600   5471    -19   -306   -878       N  
ATOM   2417  CA  GLU A 265      18.594   5.532  37.096  1.00 39.81           C  
ANISOU 2417  CA  GLU A 265     4963   4110   6053   -134   -376   -918       C  
ATOM   2418  C   GLU A 265      19.395   4.562  37.965  1.00 37.69           C  
ANISOU 2418  C   GLU A 265     4660   3980   5681   -156   -413   -960       C  
ATOM   2419  O   GLU A 265      20.481   4.111  37.585  1.00 38.45           O  
ANISOU 2419  O   GLU A 265     4691   4129   5789   -239   -449   -922       O  
ATOM   2420  CB  GLU A 265      18.751   6.957  37.626  1.00 41.18           C  
ANISOU 2420  CB  GLU A 265     5229   4129   6290   -152   -414  -1030       C  
ATOM   2421  CG  GLU A 265      18.104   8.059  36.792  1.00 49.69           C  
ANISOU 2421  CG  GLU A 265     6359   5039   7483   -128   -387   -986       C  
ATOM   2422  CD  GLU A 265      17.876   7.660  35.339  1.00 65.30           C  
ANISOU 2422  CD  GLU A 265     8272   7036   9503   -141   -352   -822       C  
ATOM   2423  OE1 GLU A 265      16.705   7.743  34.879  1.00 65.66           O  
ANISOU 2423  OE1 GLU A 265     8322   7065   9562    -40   -307   -764       O  
ATOM   2424  OE2 GLU A 265      18.858   7.271  34.656  1.00 62.89           O  
ANISOU 2424  OE2 GLU A 265     7909   6773   9215   -246   -369   -755       O  
ATOM   2425  H   GLU A 265      16.637   5.734  37.349  1.00 42.59           H  
ATOM   2426  HA  GLU A 265      18.945   5.510  36.192  1.00 47.77           H  
ATOM   2427  HB2 GLU A 265      18.352   6.996  38.510  1.00 49.42           H  
ATOM   2428  HB3 GLU A 265      19.698   7.157  37.680  1.00 49.42           H  
ATOM   2429  HG2 GLU A 265      17.243   8.281  37.178  1.00 59.63           H  
ATOM   2430  HG3 GLU A 265      18.682   8.838  36.799  1.00 59.63           H  
ATOM   2431  N   VAL A 266      18.869   4.251  39.151  1.00 36.23           N  
ANISOU 2431  N   VAL A 266     4516   3859   5390    -74   -400  -1036       N  
ATOM   2432  CA  VAL A 266      19.506   3.279  40.035  1.00 37.94           C  
ANISOU 2432  CA  VAL A 266     4713   4212   5489    -73   -434  -1062       C  
ATOM   2433  C   VAL A 266      19.688   1.941  39.322  1.00 38.00           C  
ANISOU 2433  C   VAL A 266     4641   4320   5479    -81   -406   -938       C  
ATOM   2434  O   VAL A 266      20.771   1.342  39.356  1.00 33.92           O  
ANISOU 2434  O   VAL A 266     4074   3874   4939   -127   -455   -922       O  
ATOM   2435  CB  VAL A 266      18.679   3.135  41.327  1.00 44.13           C  
ANISOU 2435  CB  VAL A 266     5567   5050   6149     32   -400  -1140       C  
ATOM   2436  CG1 VAL A 266      18.779   1.737  41.902  1.00 50.92           C  
ANISOU 2436  CG1 VAL A 266     6404   6062   6883     68   -385  -1091       C  
ATOM   2437  CG2 VAL A 266      19.121   4.176  42.347  1.00 50.37           C  
ANISOU 2437  CG2 VAL A 266     6442   5785   6911     22   -469  -1298       C  
ATOM   2438  H   VAL A 266      18.144   4.589  39.467  1.00 43.47           H  
ATOM   2439  HA  VAL A 266      20.391   3.599  40.272  1.00 45.52           H  
ATOM   2440  HB  VAL A 266      17.745   3.286  41.114  1.00 52.95           H  
ATOM   2441 HG11 VAL A 266      18.454   1.747  42.816  1.00 61.11           H  
ATOM   2442 HG12 VAL A 266      18.239   1.135  41.365  1.00 61.11           H  
ATOM   2443 HG13 VAL A 266      19.706   1.453  41.884  1.00 61.11           H  
ATOM   2444 HG21 VAL A 266      18.568   4.095  43.140  1.00 60.45           H  
ATOM   2445 HG22 VAL A 266      20.051   4.020  42.575  1.00 60.45           H  
ATOM   2446 HG23 VAL A 266      19.018   5.060  41.961  1.00 60.45           H  
ATOM   2447  N   VAL A 267      18.635   1.463  38.657  1.00 29.24           N  
ANISOU 2447  N   VAL A 267     3515   3215   4381    -35   -329   -853       N  
ATOM   2448  CA  VAL A 267      18.689   0.164  38.001  1.00 33.27           C  
ANISOU 2448  CA  VAL A 267     3968   3804   4868    -41   -300   -749       C  
ATOM   2449  C   VAL A 267      19.716   0.182  36.875  1.00 33.42           C  
ANISOU 2449  C   VAL A 267     3931   3803   4963   -123   -330   -694       C  
ATOM   2450  O   VAL A 267      20.401  -0.818  36.627  1.00 29.80           O  
ANISOU 2450  O   VAL A 267     3429   3418   4474   -136   -335   -646       O  
ATOM   2451  CB  VAL A 267      17.293  -0.233  37.485  1.00 26.65           C  
ANISOU 2451  CB  VAL A 267     3121   2968   4037     10   -223   -682       C  
ATOM   2452  CG1 VAL A 267      17.370  -1.552  36.723  1.00 31.69           C  
ANISOU 2452  CG1 VAL A 267     3715   3667   4660    -11   -200   -588       C  
ATOM   2453  CG2 VAL A 267      16.317  -0.366  38.637  1.00 32.08           C  
ANISOU 2453  CG2 VAL A 267     3846   3698   4646     89   -174   -727       C  
ATOM   2454  H   VAL A 267      17.883   1.871  38.572  1.00 35.09           H  
ATOM   2455  HA  VAL A 267      18.969  -0.499  38.652  1.00 39.92           H  
ATOM   2456  HB  VAL A 267      16.973   0.461  36.887  1.00 31.98           H  
ATOM   2457 HG11 VAL A 267      16.475  -1.915  36.630  1.00 38.03           H  
ATOM   2458 HG12 VAL A 267      17.753  -1.389  35.847  1.00 38.03           H  
ATOM   2459 HG13 VAL A 267      17.928  -2.171  37.219  1.00 38.03           H  
ATOM   2460 HG21 VAL A 267      15.412  -0.326  38.290  1.00 38.50           H  
ATOM   2461 HG22 VAL A 267      16.465  -1.217  39.079  1.00 38.50           H  
ATOM   2462 HG23 VAL A 267      16.465   0.361  39.261  1.00 38.50           H  
ATOM   2463  N   LYS A 268      19.847   1.329  36.187  1.00 35.19           N  
ANISOU 2463  N   LYS A 268     4160   3925   5285   -173   -343   -696       N  
ATOM   2464  CA  LYS A 268      20.832   1.443  35.109  1.00 42.27           C  
ANISOU 2464  CA  LYS A 268     5004   4807   6251   -258   -357   -636       C  
ATOM   2465  C   LYS A 268      22.261   1.264  35.618  1.00 38.75           C  
ANISOU 2465  C   LYS A 268     4508   4422   5795   -315   -417   -678       C  
ATOM   2466  O   LYS A 268      23.157   0.887  34.856  1.00 33.29           O  
ANISOU 2466  O   LYS A 268     3745   3772   5132   -366   -414   -621       O  
ATOM   2467  CB  LYS A 268      20.701   2.799  34.412  1.00 41.91           C  
ANISOU 2467  CB  LYS A 268     4988   4627   6309   -304   -357   -625       C  
ATOM   2468  CG  LYS A 268      20.078   2.727  33.025  1.00 47.89           C  
ANISOU 2468  CG  LYS A 268     5737   5358   7099   -296   -308   -513       C  
ATOM   2469  CD  LYS A 268      19.774   4.108  32.437  1.00 45.47           C  
ANISOU 2469  CD  LYS A 268     5482   4908   6887   -317   -308   -491       C  
ATOM   2470  CE  LYS A 268      21.024   4.943  32.289  1.00 52.13           C  
ANISOU 2470  CE  LYS A 268     6318   5681   7808   -433   -338   -502       C  
ATOM   2471  NZ  LYS A 268      22.021   4.303  31.387  1.00 50.64           N  
ANISOU 2471  NZ  LYS A 268     6050   5575   7616   -504   -318   -422       N  
ATOM   2472  H   LYS A 268      19.386   2.041  36.325  1.00 42.23           H  
ATOM   2473  HA  LYS A 268      20.650   0.744  34.461  1.00 50.73           H  
ATOM   2474  HB2 LYS A 268      20.142   3.375  34.957  1.00 50.30           H  
ATOM   2475  HB3 LYS A 268      21.585   3.186  34.319  1.00 50.30           H  
ATOM   2476  HG2 LYS A 268      20.692   2.275  32.425  1.00 57.46           H  
ATOM   2477  HG3 LYS A 268      19.244   2.235  33.078  1.00 57.46           H  
ATOM   2478  HD2 LYS A 268      19.375   4.002  31.559  1.00 54.57           H  
ATOM   2479  HD3 LYS A 268      19.162   4.579  33.024  1.00 54.57           H  
ATOM   2480  HE2 LYS A 268      20.788   5.807  31.916  1.00 62.56           H  
ATOM   2481  HE3 LYS A 268      21.435   5.059  33.160  1.00 62.56           H  
ATOM   2482  HZ1 LYS A 268      22.750   4.810  31.331  1.00 60.77           H  
ATOM   2483  HZ2 LYS A 268      22.248   3.503  31.703  1.00 60.77           H  
ATOM   2484  HZ3 LYS A 268      21.675   4.204  30.573  1.00 60.77           H  
ATOM   2485  N   LYS A 269      22.510   1.573  36.892  1.00 38.14           N  
ANISOU 2485  N   LYS A 269     4460   4358   5674   -306   -474   -782       N  
ATOM   2486  CA  LYS A 269      23.855   1.460  37.453  1.00 42.08           C  
ANISOU 2486  CA  LYS A 269     4900   4928   6161   -359   -552   -830       C  
ATOM   2487  C   LYS A 269      24.037   0.202  38.306  1.00 38.18           C  
ANISOU 2487  C   LYS A 269     4394   4568   5546   -281   -570   -830       C  
ATOM   2488  O   LYS A 269      25.130  -0.033  38.831  1.00 35.13           O  
ANISOU 2488  O   LYS A 269     3950   4262   5134   -303   -644   -863       O  
ATOM   2489  CB  LYS A 269      24.208   2.686  38.311  1.00 42.52           C  
ANISOU 2489  CB  LYS A 269     4998   4914   6245   -416   -630   -955       C  
ATOM   2490  CG  LYS A 269      23.687   4.054  37.835  1.00 51.49           C  
ANISOU 2490  CG  LYS A 269     6198   5879   7486   -462   -609   -977       C  
ATOM   2491  CD  LYS A 269      23.687   4.264  36.308  1.00 60.62           C  
ANISOU 2491  CD  LYS A 269     7316   6971   8745   -514   -548   -855       C  
ATOM   2492  CE  LYS A 269      24.991   3.857  35.615  1.00 59.93           C  
ANISOU 2492  CE  LYS A 269     7110   6960   8700   -605   -559   -792       C  
ATOM   2493  NZ  LYS A 269      24.936   4.225  34.151  1.00 63.02           N  
ANISOU 2493  NZ  LYS A 269     7487   7280   9177   -656   -491   -676       N  
ATOM   2494  H   LYS A 269      21.916   1.849  37.449  1.00 45.77           H  
ATOM   2495  HA  LYS A 269      24.476   1.431  36.709  1.00 50.50           H  
ATOM   2496  HB2 LYS A 269      23.847   2.542  39.200  1.00 51.03           H  
ATOM   2497  HB3 LYS A 269      25.175   2.753  38.353  1.00 51.03           H  
ATOM   2498  HG2 LYS A 269      22.772   4.157  38.140  1.00 61.79           H  
ATOM   2499  HG3 LYS A 269      24.246   4.746  38.221  1.00 61.79           H  
ATOM   2500  HD2 LYS A 269      22.972   3.734  35.921  1.00 72.74           H  
ATOM   2501  HD3 LYS A 269      23.539   5.205  36.124  1.00 72.74           H  
ATOM   2502  HE2 LYS A 269      25.738   4.321  36.025  1.00 71.91           H  
ATOM   2503  HE3 LYS A 269      25.116   2.898  35.690  1.00 71.91           H  
ATOM   2504  HZ1 LYS A 269      25.663   3.925  33.734  1.00 75.62           H  
ATOM   2505  HZ2 LYS A 269      24.216   3.862  33.774  1.00 75.62           H  
ATOM   2506  HZ3 LYS A 269      24.895   5.109  34.061  1.00 75.62           H  
ATOM   2507  N   TRP A 270      22.986  -0.596  38.459  1.00 34.52           N  
ANISOU 2507  N   TRP A 270     3981   4127   5009   -193   -507   -790       N  
ATOM   2508  CA  TRP A 270      23.021  -1.744  39.361  1.00 35.50           C  
ANISOU 2508  CA  TRP A 270     4120   4355   5012   -116   -514   -781       C  
ATOM   2509  C   TRP A 270      24.076  -2.758  38.940  1.00 34.46           C  
ANISOU 2509  C   TRP A 270     3910   4305   4880   -114   -533   -716       C  
ATOM   2510  O   TRP A 270      24.838  -3.255  39.777  1.00 32.79           O  
ANISOU 2510  O   TRP A 270     3680   4182   4597    -79   -597   -736       O  
ATOM   2511  CB  TRP A 270      21.625  -2.377  39.396  1.00 30.37           C  
ANISOU 2511  CB  TRP A 270     3531   3698   4311    -46   -425   -732       C  
ATOM   2512  CG  TRP A 270      21.494  -3.639  40.164  1.00 35.89           C  
ANISOU 2512  CG  TRP A 270     4259   4481   4895     27   -407   -694       C  
ATOM   2513  CD1 TRP A 270      22.330  -4.116  41.131  1.00 35.72           C  
ANISOU 2513  CD1 TRP A 270     4244   4546   4783     62   -472   -715       C  
ATOM   2514  CD2 TRP A 270      20.446  -4.602  40.026  1.00 32.90           C  
ANISOU 2514  CD2 TRP A 270     3912   4108   4481     70   -321   -619       C  
ATOM   2515  NE1 TRP A 270      21.866  -5.317  41.603  1.00 33.29           N  
ANISOU 2515  NE1 TRP A 270     3982   4285   4382    132   -424   -648       N  
ATOM   2516  CE2 TRP A 270      20.709  -5.638  40.943  1.00 34.56           C  
ANISOU 2516  CE2 TRP A 270     4158   4392   4580    128   -328   -591       C  
ATOM   2517  CE3 TRP A 270      19.309  -4.680  39.225  1.00 32.47           C  
ANISOU 2517  CE3 TRP A 270     3856   4003   4479     60   -245   -572       C  
ATOM   2518  CZ2 TRP A 270      19.878  -6.740  41.081  1.00 31.45           C  
ANISOU 2518  CZ2 TRP A 270     3806   4008   4136    165   -250   -514       C  
ATOM   2519  CZ3 TRP A 270      18.472  -5.781  39.363  1.00 34.90           C  
ANISOU 2519  CZ3 TRP A 270     4189   4333   4738     90   -177   -507       C  
ATOM   2520  CH2 TRP A 270      18.768  -6.798  40.286  1.00 34.43           C  
ANISOU 2520  CH2 TRP A 270     4173   4333   4577    137   -175   -477       C  
ATOM   2521  H   TRP A 270      22.235  -0.496  38.051  1.00 41.43           H  
ATOM   2522  HA  TRP A 270      23.256  -1.450  40.254  1.00 42.60           H  
ATOM   2523  HB2 TRP A 270      21.013  -1.738  39.794  1.00 36.45           H  
ATOM   2524  HB3 TRP A 270      21.357  -2.570  38.484  1.00 36.45           H  
ATOM   2525  HD1 TRP A 270      23.101  -3.688  41.428  1.00 42.87           H  
ATOM   2526  HE1 TRP A 270      22.241  -5.792  42.214  1.00 39.95           H  
ATOM   2527  HE3 TRP A 270      19.113  -4.009  38.612  1.00 38.97           H  
ATOM   2528  HZ2 TRP A 270      20.070  -7.415  41.691  1.00 37.74           H  
ATOM   2529  HZ3 TRP A 270      17.708  -5.846  38.837  1.00 41.88           H  
ATOM   2530  HH2 TRP A 270      18.195  -7.527  40.359  1.00 41.32           H  
ATOM   2531  N   GLY A 271      24.125  -3.087  37.647  1.00 34.70           N  
ANISOU 2531  N   GLY A 271     3895   4310   4980   -139   -479   -637       N  
ATOM   2532  CA  GLY A 271      25.102  -4.051  37.177  1.00 32.57           C  
ANISOU 2532  CA  GLY A 271     3553   4113   4711   -122   -481   -580       C  
ATOM   2533  C   GLY A 271      26.524  -3.585  37.419  1.00 38.85           C  
ANISOU 2533  C   GLY A 271     4250   4968   5545   -171   -564   -622       C  
ATOM   2534  O   GLY A 271      27.382  -4.367  37.828  1.00 30.93           O  
ANISOU 2534  O   GLY A 271     3192   4059   4500   -121   -606   -610       O  
ATOM   2535  H   GLY A 271      23.610  -2.770  37.036  1.00 41.64           H  
ATOM   2536  HA2 GLY A 271      24.972  -4.894  37.639  1.00 39.09           H  
ATOM   2537  HA3 GLY A 271      24.983  -4.192  36.224  1.00 39.09           H  
ATOM   2538  N   GLN A 272      26.785  -2.299  37.168  1.00 37.50           N  
ANISOU 2538  N   GLN A 272     4050   4738   5459   -272   -591   -668       N  
ATOM   2539  CA  GLN A 272      28.095  -1.726  37.444  1.00 38.16           C  
ANISOU 2539  CA  GLN A 272     4031   4874   5595   -347   -676   -718       C  
ATOM   2540  C   GLN A 272      28.442  -1.847  38.919  1.00 37.19           C  
ANISOU 2540  C   GLN A 272     3922   4830   5380   -305   -782   -800       C  
ATOM   2541  O   GLN A 272      29.564  -2.235  39.269  1.00 38.69           O  
ANISOU 2541  O   GLN A 272     4010   5132   5560   -298   -856   -806       O  
ATOM   2542  CB  GLN A 272      28.112  -0.265  36.995  1.00 44.03           C  
ANISOU 2542  CB  GLN A 272     4774   5506   6449   -472   -681   -755       C  
ATOM   2543  CG  GLN A 272      29.454   0.432  37.096  1.00 56.99           C  
ANISOU 2543  CG  GLN A 272     6296   7184   8174   -588   -760   -800       C  
ATOM   2544  CD  GLN A 272      29.362   1.913  36.760  1.00 62.21           C  
ANISOU 2544  CD  GLN A 272     6987   7703   8946   -719   -763   -839       C  
ATOM   2545  OE1 GLN A 272      29.902   2.755  37.476  1.00 72.03           O  
ANISOU 2545  OE1 GLN A 272     8217   8925  10226   -806   -856   -938       O  
ATOM   2546  NE2 GLN A 272      28.672   2.233  35.670  1.00 63.66           N  
ANISOU 2546  NE2 GLN A 272     7222   7784   9182   -732   -666   -761       N  
ATOM   2547  H   GLN A 272      26.220  -1.741  36.839  1.00 45.00           H  
ATOM   2548  HA  GLN A 272      28.773  -2.205  36.942  1.00 45.79           H  
ATOM   2549  HB2 GLN A 272      27.837  -0.228  36.066  1.00 52.84           H  
ATOM   2550  HB3 GLN A 272      27.487   0.231  37.546  1.00 52.84           H  
ATOM   2551  HG2 GLN A 272      29.788   0.348  38.003  1.00 68.39           H  
ATOM   2552  HG3 GLN A 272      30.074   0.020  36.475  1.00 68.39           H  
ATOM   2553 HE21 GLN A 272      28.307   1.616  35.195  1.00 76.39           H  
ATOM   2554 HE22 GLN A 272      28.592   3.058  35.438  1.00 76.39           H  
ATOM   2555  N   MET A 273      27.488  -1.529  39.806  1.00 35.09           N  
ANISOU 2555  N   MET A 273     3777   4519   5037   -269   -791   -862       N  
ATOM   2556  CA  MET A 273      27.766  -1.633  41.237  1.00 40.84           C  
ANISOU 2556  CA  MET A 273     4537   5330   5649   -222   -890   -942       C  
ATOM   2557  C   MET A 273      27.929  -3.087  41.682  1.00 38.49           C  
ANISOU 2557  C   MET A 273     4238   5146   5241   -101   -890   -870       C  
ATOM   2558  O   MET A 273      28.644  -3.358  42.648  1.00 35.28           O  
ANISOU 2558  O   MET A 273     3809   4845   4750    -61   -991   -907       O  
ATOM   2559  CB  MET A 273      26.656  -0.973  42.061  1.00 41.33           C  
ANISOU 2559  CB  MET A 273     4738   5322   5642   -199   -878  -1024       C  
ATOM   2560  CG  MET A 273      26.682   0.554  42.113  1.00 49.80           C  
ANISOU 2560  CG  MET A 273     5838   6287   6798   -303   -922  -1135       C  
ATOM   2561  SD  MET A 273      28.295   1.365  42.147  1.00 56.05           S  
ANISOU 2561  SD  MET A 273     6504   7106   7685   -447  -1058  -1213       S  
ATOM   2562  CE  MET A 273      28.516   1.694  40.392  1.00 57.35           C  
ANISOU 2562  CE  MET A 273     6577   7179   8034   -546   -965  -1104       C  
ATOM   2563  H   MET A 273      26.696  -1.260  39.607  1.00 42.11           H  
ATOM   2564  HA  MET A 273      28.590  -1.148  41.406  1.00 49.01           H  
ATOM   2565  HB2 MET A 273      25.802  -1.234  41.683  1.00 49.60           H  
ATOM   2566  HB3 MET A 273      26.726  -1.292  42.975  1.00 49.60           H  
ATOM   2567  HG2 MET A 273      26.220   0.885  41.327  1.00 59.77           H  
ATOM   2568  HG3 MET A 273      26.213   0.832  42.915  1.00 59.77           H  
ATOM   2569  HE1 MET A 273      29.381   2.110  40.255  1.00 68.82           H  
ATOM   2570  HE2 MET A 273      28.471   0.856  39.906  1.00 68.82           H  
ATOM   2571  HE3 MET A 273      27.811   2.290  40.091  1.00 68.82           H  
ATOM   2572  N   GLU A 274      27.251  -4.030  41.021  1.00 34.05           N  
ANISOU 2572  N   GLU A 274     3709   4556   4672    -39   -783   -769       N  
ATOM   2573  CA  GLU A 274      27.462  -5.440  41.305  1.00 35.90           C  
ANISOU 2573  CA  GLU A 274     3950   4868   4823     71   -775   -691       C  
ATOM   2574  C   GLU A 274      28.728  -5.979  40.645  1.00 36.88           C  
ANISOU 2574  C   GLU A 274     3940   5062   5011     80   -801   -642       C  
ATOM   2575  O   GLU A 274      29.155  -7.089  40.985  1.00 32.90           O  
ANISOU 2575  O   GLU A 274     3429   4629   4442    184   -818   -586       O  
ATOM   2576  CB  GLU A 274      26.275  -6.281  40.830  1.00 34.98           C  
ANISOU 2576  CB  GLU A 274     3920   4684   4685    121   -653   -609       C  
ATOM   2577  CG  GLU A 274      24.949  -5.960  41.496  1.00 40.11           C  
ANISOU 2577  CG  GLU A 274     4686   5286   5267    132   -607   -638       C  
ATOM   2578  CD  GLU A 274      24.731  -6.729  42.789  1.00 41.84           C  
ANISOU 2578  CD  GLU A 274     4989   5574   5334    226   -622   -622       C  
ATOM   2579  OE1 GLU A 274      25.657  -7.430  43.241  1.00 38.48           O  
ANISOU 2579  OE1 GLU A 274     4538   5231   4852    286   -688   -592       O  
ATOM   2580  OE2 GLU A 274      23.616  -6.630  43.353  1.00 46.44           O  
ANISOU 2580  OE2 GLU A 274     5663   6133   5850    246   -562   -631       O  
ATOM   2581  H   GLU A 274      26.667  -3.873  40.409  1.00 40.86           H  
ATOM   2582  HA  GLU A 274      27.533  -5.544  42.266  1.00 43.08           H  
ATOM   2583  HB2 GLU A 274      26.162  -6.142  39.876  1.00 41.97           H  
ATOM   2584  HB3 GLU A 274      26.470  -7.215  41.007  1.00 41.97           H  
ATOM   2585  HG2 GLU A 274      24.923  -5.013  41.704  1.00 48.13           H  
ATOM   2586  HG3 GLU A 274      24.228  -6.186  40.888  1.00 48.13           H  
ATOM   2587  N   ASN A 275      29.328  -5.222  39.720  1.00 34.19           N  
ANISOU 2587  N   ASN A 275     3494   4701   4795    -20   -798   -657       N  
ATOM   2588  CA  ASN A 275      30.467  -5.697  38.924  1.00 35.47           C  
ANISOU 2588  CA  ASN A 275     3517   4932   5028    -13   -793   -605       C  
ATOM   2589  C   ASN A 275      30.130  -7.028  38.257  1.00 33.72           C  
ANISOU 2589  C   ASN A 275     3338   4694   4781     91   -695   -510       C  
ATOM   2590  O   ASN A 275      30.966  -7.927  38.118  1.00 34.19           O  
ANISOU 2590  O   ASN A 275     3326   4828   4836    175   -701   -464       O  
ATOM   2591  CB  ASN A 275      31.727  -5.828  39.772  1.00 32.98           C  
ANISOU 2591  CB  ASN A 275     3088   4756   4686     18   -920   -637       C  
ATOM   2592  CG  ASN A 275      32.992  -5.858  38.920  1.00 38.96           C  
ANISOU 2592  CG  ASN A 275     3659   5591   5553    -13   -918   -607       C  
ATOM   2593  OD1 ASN A 275      33.177  -5.011  38.039  1.00 35.79           O  
ANISOU 2593  OD1 ASN A 275     3192   5144   5261   -135   -874   -614       O  
ATOM   2594  ND2 ASN A 275      33.866  -6.821  39.179  1.00 37.83           N  
ANISOU 2594  ND2 ASN A 275     3429   5566   5379    101   -959   -566       N  
ATOM   2595  H   ASN A 275      29.091  -4.417  39.531  1.00 41.03           H  
ATOM   2596  HA  ASN A 275      30.648  -5.044  38.230  1.00 42.56           H  
ATOM   2597  HB2 ASN A 275      31.786  -5.070  40.375  1.00 39.57           H  
ATOM   2598  HB3 ASN A 275      31.685  -6.653  40.281  1.00 39.57           H  
ATOM   2599 HD21 ASN A 275      34.593  -6.876  38.723  1.00 45.40           H  
ATOM   2600 HD22 ASN A 275      33.706  -7.391  39.803  1.00 45.40           H  
ATOM   2601  N   SER A 276      28.872  -7.150  37.839  1.00 31.35           N  
ANISOU 2601  N   SER A 276     3155   4289   4466     86   -607   -485       N  
ATOM   2602  CA  SER A 276      28.341  -8.377  37.258  1.00 38.48           C  
ANISOU 2602  CA  SER A 276     4125   5153   5341    163   -519   -411       C  
ATOM   2603  C   SER A 276      27.391  -8.011  36.127  1.00 34.62           C  
ANISOU 2603  C   SER A 276     3682   4566   4906     94   -430   -395       C  
ATOM   2604  O   SER A 276      26.789  -6.935  36.130  1.00 31.67           O  
ANISOU 2604  O   SER A 276     3330   4142   4562     15   -434   -434       O  
ATOM   2605  CB  SER A 276      27.581  -9.234  38.288  1.00 32.77           C  
ANISOU 2605  CB  SER A 276     3524   4418   4508    249   -520   -387       C  
ATOM   2606  OG  SER A 276      28.370  -9.492  39.439  1.00 38.37           O  
ANISOU 2606  OG  SER A 276     4210   5224   5146    320   -615   -398       O  
ATOM   2607  H   SER A 276      28.291  -6.518  37.883  1.00 37.62           H  
ATOM   2608  HA  SER A 276      29.076  -8.905  36.909  1.00 46.17           H  
ATOM   2609  HB2 SER A 276      26.779  -8.759  38.559  1.00 39.32           H  
ATOM   2610  HB3 SER A 276      27.342 -10.079  37.877  1.00 39.32           H  
ATOM   2611  HG  SER A 276      28.558  -8.771  39.825  1.00 46.05           H  
ATOM   2612  N   THR A 277      27.255  -8.912  35.167  1.00 31.21           N  
ANISOU 2612  N   THR A 277     3270   4106   4482    131   -356   -341       N  
ATOM   2613  CA  THR A 277      26.244  -8.750  34.136  1.00 38.54           C  
ANISOU 2613  CA  THR A 277     4254   4952   5436     78   -283   -323       C  
ATOM   2614  C   THR A 277      24.867  -9.066  34.719  1.00 29.98           C  
ANISOU 2614  C   THR A 277     3282   3810   4300     90   -264   -320       C  
ATOM   2615  O   THR A 277      24.673 -10.107  35.350  1.00 33.66           O  
ANISOU 2615  O   THR A 277     3807   4276   4704    160   -258   -294       O  
ATOM   2616  CB  THR A 277      26.544  -9.669  32.955  1.00 34.75           C  
ANISOU 2616  CB  THR A 277     3771   4465   4966    116   -216   -282       C  
ATOM   2617  OG1 THR A 277      27.894  -9.473  32.544  1.00 39.32           O  
ANISOU 2617  OG1 THR A 277     4232   5120   5588    121   -222   -280       O  
ATOM   2618  CG2 THR A 277      25.595  -9.361  31.801  1.00 33.01           C  
ANISOU 2618  CG2 THR A 277     3600   4178   4766     52   -158   -269       C  
ATOM   2619  H   THR A 277      27.733  -9.622  35.089  1.00 37.45           H  
ATOM   2620  HA  THR A 277      26.245  -7.835  33.812  1.00 46.25           H  
ATOM   2621  HB  THR A 277      26.421 -10.597  33.208  1.00 41.70           H  
ATOM   2622  HG1 THR A 277      28.079  -9.990  31.909  1.00 47.18           H  
ATOM   2623 HG21 THR A 277      25.824  -9.902  31.030  1.00 39.62           H  
ATOM   2624 HG22 THR A 277      24.681  -9.557  32.062  1.00 39.62           H  
ATOM   2625 HG23 THR A 277      25.659  -8.424  31.560  1.00 39.62           H  
ATOM   2626  N   LEU A 278      23.918  -8.162  34.524  1.00 35.75           N  
ANISOU 2626  N   LEU A 278     4036   4490   5056     26   -252   -339       N  
ATOM   2627  CA  LEU A 278      22.558  -8.430  34.956  1.00 31.07           C  
ANISOU 2627  CA  LEU A 278     3525   3855   4425     33   -221   -332       C  
ATOM   2628  C   LEU A 278      21.926  -9.490  34.059  1.00 31.67           C  
ANISOU 2628  C   LEU A 278     3645   3889   4498     38   -162   -285       C  
ATOM   2629  O   LEU A 278      22.244  -9.602  32.874  1.00 31.05           O  
ANISOU 2629  O   LEU A 278     3545   3800   4453     19   -140   -270       O  
ATOM   2630  CB  LEU A 278      21.717  -7.156  34.930  1.00 29.60           C  
ANISOU 2630  CB  LEU A 278     3340   3630   4276    -21   -222   -366       C  
ATOM   2631  CG  LEU A 278      22.066  -6.028  35.906  1.00 35.08           C  
ANISOU 2631  CG  LEU A 278     4021   4338   4971    -33   -279   -432       C  
ATOM   2632  CD1 LEU A 278      20.944  -4.985  35.904  1.00 33.90           C  
ANISOU 2632  CD1 LEU A 278     3899   4128   4852    -59   -261   -461       C  
ATOM   2633  CD2 LEU A 278      22.321  -6.516  37.316  1.00 38.32           C  
ANISOU 2633  CD2 LEU A 278     4463   4806   5292     26   -314   -455       C  
ATOM   2634  H   LEU A 278      24.034  -7.397  34.150  1.00 42.90           H  
ATOM   2635  HA  LEU A 278      22.565  -8.756  35.870  1.00 37.28           H  
ATOM   2636  HB2 LEU A 278      21.785  -6.780  34.038  1.00 35.52           H  
ATOM   2637  HB3 LEU A 278      20.799  -7.407  35.115  1.00 35.52           H  
ATOM   2638  HG  LEU A 278      22.896  -5.626  35.607  1.00 42.10           H  
ATOM   2639 HD11 LEU A 278      21.176  -4.270  36.517  1.00 40.68           H  
ATOM   2640 HD12 LEU A 278      20.844  -4.631  35.006  1.00 40.68           H  
ATOM   2641 HD13 LEU A 278      20.118  -5.408  36.186  1.00 40.68           H  
ATOM   2642 HD21 LEU A 278      22.426  -5.749  37.901  1.00 45.99           H  
ATOM   2643 HD22 LEU A 278      21.568  -7.053  37.606  1.00 45.99           H  
ATOM   2644 HD23 LEU A 278      23.131  -7.050  37.323  1.00 45.99           H  
ATOM   2645  N   HIS A 279      21.016 -10.264  34.632  1.00 31.98           N  
ANISOU 2645  N   HIS A 279     3751   3906   4494     58   -133   -263       N  
ATOM   2646  CA  HIS A 279      20.254 -11.262  33.896  1.00 33.71           C  
ANISOU 2646  CA  HIS A 279     4019   4073   4715     43    -84   -229       C  
ATOM   2647  C   HIS A 279      18.764 -10.946  34.000  1.00 35.60           C  
ANISOU 2647  C   HIS A 279     4271   4290   4965     -6    -58   -228       C  
ATOM   2648  O   HIS A 279      18.303 -10.321  34.963  1.00 29.88           O  
ANISOU 2648  O   HIS A 279     3542   3589   4223      1    -60   -244       O  
ATOM   2649  CB  HIS A 279      20.520 -12.670  34.427  1.00 32.22           C  
ANISOU 2649  CB  HIS A 279     3897   3866   4481    101    -66   -191       C  
ATOM   2650  CG  HIS A 279      21.922 -13.153  34.201  1.00 33.77           C  
ANISOU 2650  CG  HIS A 279     4074   4084   4673    170    -85   -187       C  
ATOM   2651  ND1 HIS A 279      22.227 -14.182  33.334  1.00 39.09           N  
ANISOU 2651  ND1 HIS A 279     4786   4712   5355    198    -53   -172       N  
ATOM   2652  CD2 HIS A 279      23.100 -12.753  34.739  1.00 38.80           C  
ANISOU 2652  CD2 HIS A 279     4650   4790   5301    219   -135   -200       C  
ATOM   2653  CE1 HIS A 279      23.532 -14.394  33.349  1.00 40.24           C  
ANISOU 2653  CE1 HIS A 279     4889   4900   5498    276    -72   -171       C  
ATOM   2654  NE2 HIS A 279      24.086 -13.541  34.194  1.00 36.26           N  
ANISOU 2654  NE2 HIS A 279     4317   4474   4988    285   -126   -185       N  
ATOM   2655  H   HIS A 279      20.817 -10.229  35.467  1.00 38.38           H  
ATOM   2656  HA  HIS A 279      20.509 -11.240  32.961  1.00 40.45           H  
ATOM   2657  HB2 HIS A 279      20.356 -12.678  35.383  1.00 38.67           H  
ATOM   2658  HB3 HIS A 279      19.920 -13.288  33.981  1.00 38.67           H  
ATOM   2659  HD1 HIS A 279      21.657 -14.617  32.858  1.00 46.91           H  
ATOM   2660  HD2 HIS A 279      23.219 -12.073  35.362  1.00 46.56           H  
ATOM   2661  HE1 HIS A 279      23.984 -15.034  32.849  1.00 48.28           H  
ATOM   2662  N   ALA A 280      18.013 -11.396  33.000  1.00 33.93           N  
ANISOU 2662  N   ALA A 280     4072   4041   4778    -51    -34   -213       N  
ATOM   2663  CA  ALA A 280      16.578 -11.183  32.955  1.00 30.98           C  
ANISOU 2663  CA  ALA A 280     3687   3660   4425    -99    -14   -207       C  
ATOM   2664  C   ALA A 280      15.904 -12.462  32.489  1.00 35.77           C  
ANISOU 2664  C   ALA A 280     4338   4222   5031   -140     15   -182       C  
ATOM   2665  O   ALA A 280      16.537 -13.354  31.911  1.00 33.31           O  
ANISOU 2665  O   ALA A 280     4074   3872   4708   -131     16   -180       O  
ATOM   2666  CB  ALA A 280      16.207 -10.022  32.025  1.00 28.17           C  
ANISOU 2666  CB  ALA A 280     3277   3312   4116   -130    -39   -224       C  
ATOM   2667  H   ALA A 280      18.319 -11.835  32.326  1.00 40.72           H  
ATOM   2668  HA  ALA A 280      16.255 -10.973  33.845  1.00 37.18           H  
ATOM   2669  HB1 ALA A 280      15.243  -9.916  32.021  1.00 33.81           H  
ATOM   2670  HB2 ALA A 280      16.627  -9.210  32.349  1.00 33.81           H  
ATOM   2671  HB3 ALA A 280      16.521 -10.222  31.129  1.00 33.81           H  
ATOM   2672  N   MET A 281      14.605 -12.544  32.762  1.00 30.35           N  
ANISOU 2672  N   MET A 281     3632   3538   4360   -187     40   -168       N  
ATOM   2673  CA  MET A 281      13.781 -13.651  32.293  1.00 31.43           C  
ANISOU 2673  CA  MET A 281     3798   3631   4514   -255     61   -150       C  
ATOM   2674  C   MET A 281      12.388 -13.110  32.025  1.00 32.30           C  
ANISOU 2674  C   MET A 281     3826   3778   4667   -313     60   -151       C  
ATOM   2675  O   MET A 281      11.744 -12.575  32.936  1.00 31.48           O  
ANISOU 2675  O   MET A 281     3675   3718   4567   -299     92   -140       O  
ATOM   2676  CB  MET A 281      13.725 -14.797  33.314  1.00 32.66           C  
ANISOU 2676  CB  MET A 281     4024   3745   4640   -254    112   -108       C  
ATOM   2677  CG  MET A 281      12.878 -15.975  32.841  1.00 30.52           C  
ANISOU 2677  CG  MET A 281     3790   3407   4400   -345    134    -91       C  
ATOM   2678  SD  MET A 281      12.836 -17.369  33.973  1.00 36.94           S  
ANISOU 2678  SD  MET A 281     4707   4144   5187   -352    204    -22       S  
ATOM   2679  CE  MET A 281      14.537 -17.869  34.006  1.00 37.53           C  
ANISOU 2679  CE  MET A 281     4878   4170   5213   -234    180    -24       C  
ATOM   2680  H   MET A 281      14.172 -11.961  33.223  1.00 36.42           H  
ATOM   2681  HA  MET A 281      14.165 -14.008  31.477  1.00 37.72           H  
ATOM   2682  HB2 MET A 281      14.625 -15.120  33.475  1.00 39.19           H  
ATOM   2683  HB3 MET A 281      13.340 -14.464  34.140  1.00 39.19           H  
ATOM   2684  HG2 MET A 281      11.966 -15.671  32.718  1.00 36.63           H  
ATOM   2685  HG3 MET A 281      13.238 -16.294  31.998  1.00 36.63           H  
ATOM   2686  HE1 MET A 281      14.634 -18.619  34.613  1.00 45.04           H  
ATOM   2687  HE2 MET A 281      14.806 -18.131  33.111  1.00 45.04           H  
ATOM   2688  HE3 MET A 281      15.079 -17.125  34.310  1.00 45.04           H  
ATOM   2689  N   ALA A 282      11.937 -13.241  30.783  1.00 29.98           N  
ANISOU 2689  N   ALA A 282     3514   3477   4400   -369     20   -167       N  
ATOM   2690  CA  ALA A 282      10.573 -12.873  30.440  1.00 32.38           C  
ANISOU 2690  CA  ALA A 282     3729   3826   4749   -425      6   -164       C  
ATOM   2691  C   ALA A 282       9.587 -13.841  31.086  1.00 35.41           C  
ANISOU 2691  C   ALA A 282     4100   4199   5156   -499     56   -137       C  
ATOM   2692  O   ALA A 282       9.706 -15.058  30.928  1.00 36.30           O  
ANISOU 2692  O   ALA A 282     4287   4242   5263   -556     67   -133       O  
ATOM   2693  CB  ALA A 282      10.405 -12.866  28.925  1.00 32.09           C  
ANISOU 2693  CB  ALA A 282     3685   3791   4716   -466    -63   -188       C  
ATOM   2694  H   ALA A 282      12.401 -13.539  30.123  1.00 35.98           H  
ATOM   2695  HA  ALA A 282      10.380 -11.982  30.771  1.00 38.86           H  
ATOM   2696  HB1 ALA A 282       9.491 -12.621  28.710  1.00 38.51           H  
ATOM   2697  HB2 ALA A 282      11.019 -12.220  28.542  1.00 38.51           H  
ATOM   2698  HB3 ALA A 282      10.599 -13.752  28.581  1.00 38.51           H  
ATOM   2699  N   CYS A 283       8.620 -13.292  31.820  1.00 37.83           N  
ANISOU 2699  N   CYS A 283     4314   4569   5490   -498     94   -116       N  
ATOM   2700  CA  CYS A 283       7.548 -14.076  32.430  1.00 42.20           C  
ANISOU 2700  CA  CYS A 283     4828   5134   6075   -579    155    -80       C  
ATOM   2701  C   CYS A 283       6.297 -14.105  31.563  1.00 42.18           C  
ANISOU 2701  C   CYS A 283     4710   5178   6139   -669    112    -88       C  
ATOM   2702  O   CYS A 283       5.495 -15.040  31.663  1.00 39.76           O  
ANISOU 2702  O   CYS A 283     4376   4860   5871   -779    141    -66       O  
ATOM   2703  CB  CYS A 283       7.165 -13.500  33.797  1.00 41.74           C  
ANISOU 2703  CB  CYS A 283     4723   5137   6000   -521    238    -53       C  
ATOM   2704  SG  CYS A 283       8.568 -13.116  34.855  1.00 50.00           S  
ANISOU 2704  SG  CYS A 283     5879   6163   6957   -401    260    -58       S  
ATOM   2705  H   CYS A 283       8.561 -12.449  31.984  1.00 45.40           H  
ATOM   2706  HA  CYS A 283       7.871 -14.981  32.561  1.00 50.65           H  
ATOM   2707  HB2 CYS A 283       6.667 -12.679  33.659  1.00 50.09           H  
ATOM   2708  HB3 CYS A 283       6.614 -14.148  34.263  1.00 50.09           H  
ATOM   2709  HG  CYS A 283       8.164 -12.671  35.893  1.00 60.01           H  
ATOM   2710  N   GLY A 284       6.100 -13.080  30.746  1.00 40.10           N  
ANISOU 2710  N   GLY A 284     4376   4969   5891   -627     42   -113       N  
ATOM   2711  CA  GLY A 284       4.968 -13.044  29.848  1.00 37.86           C  
ANISOU 2711  CA  GLY A 284     3978   4745   5662   -698    -22   -120       C  
ATOM   2712  C   GLY A 284       5.061 -11.834  28.952  1.00 37.83           C  
ANISOU 2712  C   GLY A 284     3935   4786   5653   -619   -103   -136       C  
ATOM   2713  O   GLY A 284       6.089 -11.159  28.896  1.00 35.01           O  
ANISOU 2713  O   GLY A 284     3654   4394   5254   -532   -110   -144       O  
ATOM   2714  H   GLY A 284       6.611 -12.390  30.695  1.00 48.12           H  
ATOM   2715  HA2 GLY A 284       4.956 -13.843  29.299  1.00 45.43           H  
ATOM   2716  HA3 GLY A 284       4.143 -12.997  30.357  1.00 45.43           H  
ATOM   2717  N   PHE A 285       3.957 -11.538  28.276  1.00 37.59           N  
ANISOU 2717  N   PHE A 285     3779   4835   5669   -649   -166   -132       N  
ATOM   2718  CA  PHE A 285       3.914 -10.423  27.343  1.00 34.93           C  
ANISOU 2718  CA  PHE A 285     3406   4540   5326   -572   -252   -131       C  
ATOM   2719  C   PHE A 285       2.575  -9.727  27.442  1.00 41.95           C  
ANISOU 2719  C   PHE A 285     4119   5536   6285   -540   -268   -107       C  
ATOM   2720  O   PHE A 285       1.527 -10.380  27.450  1.00 39.48           O  
ANISOU 2720  O   PHE A 285     3691   5285   6022   -633   -275   -103       O  
ATOM   2721  CB  PHE A 285       4.175 -10.910  25.918  1.00 38.40           C  
ANISOU 2721  CB  PHE A 285     3907   4966   5717   -633   -355   -157       C  
ATOM   2722  CG  PHE A 285       5.382 -11.819  25.810  1.00 40.64           C  
ANISOU 2722  CG  PHE A 285     4354   5149   5939   -668   -328   -188       C  
ATOM   2723  CD1 PHE A 285       6.651 -11.293  25.678  1.00 33.37           C  
ANISOU 2723  CD1 PHE A 285     3535   4181   4965   -585   -313   -188       C  
ATOM   2724  CD2 PHE A 285       5.233 -13.191  25.859  1.00 35.70           C  
ANISOU 2724  CD2 PHE A 285     3773   4475   5318   -781   -315   -215       C  
ATOM   2725  CE1 PHE A 285       7.763 -12.127  25.589  1.00 38.70           C  
ANISOU 2725  CE1 PHE A 285     4339   4776   5588   -600   -285   -214       C  
ATOM   2726  CE2 PHE A 285       6.335 -14.027  25.767  1.00 39.65           C  
ANISOU 2726  CE2 PHE A 285     4424   4875   5765   -791   -288   -242       C  
ATOM   2727  CZ  PHE A 285       7.603 -13.491  25.632  1.00 36.30           C  
ANISOU 2727  CZ  PHE A 285     4086   4420   5284   -692   -272   -242       C  
ATOM   2728  H   PHE A 285       3.218 -11.973  28.341  1.00 45.11           H  
ATOM   2729  HA  PHE A 285       4.591  -9.769  27.575  1.00 41.92           H  
ATOM   2730  HB2 PHE A 285       3.400 -11.405  25.609  1.00 46.08           H  
ATOM   2731  HB3 PHE A 285       4.328 -10.142  25.346  1.00 46.08           H  
ATOM   2732  HD1 PHE A 285       6.765 -10.371  25.649  1.00 40.05           H  
ATOM   2733  HD2 PHE A 285       4.384 -13.558  25.954  1.00 42.85           H  
ATOM   2734  HE1 PHE A 285       8.613 -11.761  25.500  1.00 46.44           H  
ATOM   2735  HE2 PHE A 285       6.222 -14.950  25.797  1.00 47.58           H  
ATOM   2736  HZ  PHE A 285       8.344 -14.051  25.570  1.00 43.55           H  
ATOM   2737  N   GLN A 286       2.618  -8.403  27.535  1.00 37.78           N  
ANISOU 2737  N   GLN A 286     3565   5024   5768   -410   -271    -90       N  
ATOM   2738  CA  GLN A 286       1.416  -7.564  27.598  1.00 38.52           C  
ANISOU 2738  CA  GLN A 286     3493   5213   5930   -338   -286    -65       C  
ATOM   2739  C   GLN A 286       1.517  -6.579  26.443  1.00 37.68           C  
ANISOU 2739  C   GLN A 286     3398   5111   5808   -257   -395    -43       C  
ATOM   2740  O   GLN A 286       2.252  -5.588  26.525  1.00 34.10           O  
ANISOU 2740  O   GLN A 286     3029   4591   5337   -156   -382    -34       O  
ATOM   2741  CB  GLN A 286       1.304  -6.861  28.940  1.00 33.12           C  
ANISOU 2741  CB  GLN A 286     2780   4528   5274   -236   -172    -64       C  
ATOM   2742  CG  GLN A 286       1.032  -7.830  30.075  1.00 40.12           C  
ANISOU 2742  CG  GLN A 286     3644   5432   6166   -314    -60    -68       C  
ATOM   2743  CD  GLN A 286       0.891  -7.144  31.409  1.00 39.80           C  
ANISOU 2743  CD  GLN A 286     3583   5407   6131   -206     57    -73       C  
ATOM   2744  OE1 GLN A 286       0.966  -5.915  31.498  1.00 38.09           O  
ANISOU 2744  OE1 GLN A 286     3370   5179   5925    -72     52    -85       O  
ATOM   2745  NE2 GLN A 286       0.689  -7.935  32.462  1.00 40.09           N  
ANISOU 2745  NE2 GLN A 286     3613   5464   6155   -263    167    -65       N  
ATOM   2746  H   GLN A 286       3.350  -7.952  27.565  1.00 45.34           H  
ATOM   2747  HA  GLN A 286       0.619  -8.105  27.486  1.00 46.23           H  
ATOM   2748  HB2 GLN A 286       2.137  -6.401  29.128  1.00 39.74           H  
ATOM   2749  HB3 GLN A 286       0.574  -6.224  28.905  1.00 39.74           H  
ATOM   2750  HG2 GLN A 286       0.206  -8.304  29.894  1.00 48.14           H  
ATOM   2751  HG3 GLN A 286       1.769  -8.458  30.138  1.00 48.14           H  
ATOM   2752 HE21 GLN A 286       0.646  -8.787  32.358  1.00 48.11           H  
ATOM   2753 HE22 GLN A 286       0.602  -7.592  33.246  1.00 48.11           H  
ATOM   2754  N   GLY A 287       0.801  -6.871  25.370  1.00 35.19           N  
ANISOU 2754  N   GLY A 287     3004   4871   5494   -310   -505    -33       N  
ATOM   2755  CA  GLY A 287       0.930  -6.087  24.158  1.00 35.93           C  
ANISOU 2755  CA  GLY A 287     3130   4975   5549   -243   -617     -1       C  
ATOM   2756  C   GLY A 287       2.366  -6.168  23.665  1.00 36.74           C  
ANISOU 2756  C   GLY A 287     3424   4973   5560   -257   -615    -12       C  
ATOM   2757  O   GLY A 287       2.910  -7.257  23.425  1.00 35.81           O  
ANISOU 2757  O   GLY A 287     3390   4824   5390   -364   -612    -52       O  
ATOM   2758  H   GLY A 287       0.234  -7.515  25.318  1.00 42.22           H  
ATOM   2759  HA2 GLY A 287       0.337  -6.432  23.472  1.00 43.12           H  
ATOM   2760  HA3 GLY A 287       0.704  -5.160  24.333  1.00 43.12           H  
ATOM   2761  N   SER A 288       3.001  -5.009  23.517  1.00 38.43           N  
ANISOU 2761  N   SER A 288     3711   5129   5761   -149   -611     24       N  
ATOM   2762  CA  SER A 288       4.370  -4.943  23.021  1.00 41.60           C  
ANISOU 2762  CA  SER A 288     4274   5446   6086   -159   -602     25       C  
ATOM   2763  C   SER A 288       5.408  -4.993  24.136  1.00 35.60           C  
ANISOU 2763  C   SER A 288     3595   4595   5336   -157   -491     -8       C  
ATOM   2764  O   SER A 288       6.602  -4.845  23.856  1.00 38.94           O  
ANISOU 2764  O   SER A 288     4132   4952   5711   -159   -473     -6       O  
ATOM   2765  CB  SER A 288       4.556  -3.668  22.201  1.00 40.61           C  
ANISOU 2765  CB  SER A 288     4188   5300   5943    -60   -656     92       C  
ATOM   2766  OG  SER A 288       4.330  -2.528  23.007  1.00 43.39           O  
ANISOU 2766  OG  SER A 288     4504   5607   6375     49   -611    113       O  
ATOM   2767  H   SER A 288       2.657  -4.243  23.698  1.00 46.11           H  
ATOM   2768  HA  SER A 288       4.528  -5.704  22.441  1.00 49.92           H  
ATOM   2769  HB2 SER A 288       5.463  -3.640  21.858  1.00 48.74           H  
ATOM   2770  HB3 SER A 288       3.924  -3.668  21.465  1.00 48.74           H  
ATOM   2771  HG  SER A 288       4.444  -1.829  22.555  1.00 52.07           H  
ATOM   2772  N   ILE A 289       4.984  -5.220  25.377  1.00 32.93           N  
ANISOU 2772  N   ILE A 289     3196   4264   5052   -155   -418    -35       N  
ATOM   2773  CA  ILE A 289       5.856  -5.129  26.538  1.00 31.58           C  
ANISOU 2773  CA  ILE A 289     3093   4022   4882   -136   -325    -65       C  
ATOM   2774  C   ILE A 289       6.252  -6.526  26.987  1.00 31.29           C  
ANISOU 2774  C   ILE A 289     3100   3977   4812   -232   -280    -99       C  
ATOM   2775  O   ILE A 289       5.389  -7.379  27.221  1.00 28.83           O  
ANISOU 2775  O   ILE A 289     2718   3716   4522   -296   -269   -105       O  
ATOM   2776  CB  ILE A 289       5.170  -4.370  27.688  1.00 29.65           C  
ANISOU 2776  CB  ILE A 289     2774   3791   4701    -50   -264    -72       C  
ATOM   2777  CG1 ILE A 289       4.633  -3.032  27.184  1.00 34.68           C  
ANISOU 2777  CG1 ILE A 289     3366   4426   5382     58   -314    -36       C  
ATOM   2778  CG2 ILE A 289       6.127  -4.163  28.849  1.00 31.98           C  
ANISOU 2778  CG2 ILE A 289     3154   4017   4979    -24   -186   -111       C  
ATOM   2779  CD1 ILE A 289       5.674  -2.185  26.478  1.00 39.16           C  
ANISOU 2779  CD1 ILE A 289     4049   4905   5925     89   -350    -10       C  
ATOM   2780  H   ILE A 289       4.175  -5.434  25.573  1.00 39.52           H  
ATOM   2781  HA  ILE A 289       6.662  -4.655  26.281  1.00 37.89           H  
ATOM   2782  HB  ILE A 289       4.426  -4.904  28.006  1.00 35.58           H  
ATOM   2783 HG12 ILE A 289       3.912  -3.201  26.557  1.00 41.61           H  
ATOM   2784 HG13 ILE A 289       4.301  -2.525  27.941  1.00 41.61           H  
ATOM   2785 HG21 ILE A 289       5.730  -3.541  29.479  1.00 38.38           H  
ATOM   2786 HG22 ILE A 289       6.286  -5.017  29.282  1.00 38.38           H  
ATOM   2787 HG23 ILE A 289       6.962  -3.804  28.510  1.00 38.38           H  
ATOM   2788 HD11 ILE A 289       5.323  -1.289  26.356  1.00 46.99           H  
ATOM   2789 HD12 ILE A 289       6.478  -2.154  27.020  1.00 46.99           H  
ATOM   2790 HD13 ILE A 289       5.873  -2.582  25.615  1.00 46.99           H  
ATOM   2791  N   ASN A 290       7.560  -6.757  27.114  1.00 25.74           N  
ANISOU 2791  N   ASN A 290     2509   3208   4063   -242   -252   -115       N  
ATOM   2792  CA  ASN A 290       8.071  -7.949  27.781  1.00 28.45           C  
ANISOU 2792  CA  ASN A 290     2907   3525   4379   -299   -198   -141       C  
ATOM   2793  C   ASN A 290       7.914  -7.766  29.294  1.00 30.36           C  
ANISOU 2793  C   ASN A 290     3126   3768   4641   -259   -119   -150       C  
ATOM   2794  O   ASN A 290       8.456  -6.814  29.866  1.00 31.19           O  
ANISOU 2794  O   ASN A 290     3257   3846   4747   -187    -99   -162       O  
ATOM   2795  CB  ASN A 290       9.542  -8.185  27.432  1.00 28.57           C  
ANISOU 2795  CB  ASN A 290     3033   3484   4340   -300   -196   -153       C  
ATOM   2796  CG  ASN A 290       9.767  -8.420  25.953  1.00 32.09           C  
ANISOU 2796  CG  ASN A 290     3514   3934   4743   -333   -257   -148       C  
ATOM   2797  OD1 ASN A 290       9.675  -9.540  25.474  1.00 30.92           O  
ANISOU 2797  OD1 ASN A 290     3399   3785   4565   -397   -271   -169       O  
ATOM   2798  ND2 ASN A 290      10.079  -7.356  25.225  1.00 31.13           N  
ANISOU 2798  ND2 ASN A 290     3400   3814   4614   -289   -291   -120       N  
ATOM   2799  H   ASN A 290       8.174  -6.232  26.820  1.00 30.89           H  
ATOM   2800  HA  ASN A 290       7.567  -8.724  27.489  1.00 34.15           H  
ATOM   2801  HB2 ASN A 290      10.057  -7.406  27.693  1.00 34.29           H  
ATOM   2802  HB3 ASN A 290       9.858  -8.967  27.911  1.00 34.29           H  
ATOM   2803 HD21 ASN A 290      10.216  -7.437  24.380  1.00 37.36           H  
ATOM   2804 HD22 ASN A 290      10.144  -6.584  25.599  1.00 37.36           H  
ATOM   2805  N   MET A 291       7.174  -8.663  29.936  1.00 31.03           N  
ANISOU 2805  N   MET A 291     3171   3882   4737   -310    -72   -147       N  
ATOM   2806  CA  MET A 291       7.080  -8.702  31.394  1.00 32.60           C  
ANISOU 2806  CA  MET A 291     3368   4090   4929   -279     16   -149       C  
ATOM   2807  C   MET A 291       8.259  -9.533  31.901  1.00 32.46           C  
ANISOU 2807  C   MET A 291     3468   4015   4852   -296     44   -155       C  
ATOM   2808  O   MET A 291       8.396 -10.707  31.547  1.00 28.95           O  
ANISOU 2808  O   MET A 291     3067   3540   4395   -369     41   -146       O  
ATOM   2809  CB  MET A 291       5.743  -9.296  31.831  1.00 31.18           C  
ANISOU 2809  CB  MET A 291     3085   3974   4787   -332     66   -126       C  
ATOM   2810  CG  MET A 291       4.517  -8.586  31.220  1.00 33.98           C  
ANISOU 2810  CG  MET A 291     3297   4404   5208   -313     25   -117       C  
ATOM   2811  SD  MET A 291       4.539  -6.763  31.447  1.00 32.51           S  
ANISOU 2811  SD  MET A 291     3088   4221   5043   -156     20   -133       S  
ATOM   2812  CE  MET A 291       4.160  -6.671  33.199  1.00 38.56           C  
ANISOU 2812  CE  MET A 291     3833   5024   5794   -101    152   -147       C  
ATOM   2813  H   MET A 291       6.708  -9.270  29.545  1.00 37.24           H  
ATOM   2814  HA  MET A 291       7.123  -7.807  31.767  1.00 39.12           H  
ATOM   2815  HB2 MET A 291       5.712 -10.227  31.560  1.00 37.41           H  
ATOM   2816  HB3 MET A 291       5.673  -9.230  32.797  1.00 37.41           H  
ATOM   2817  HG2 MET A 291       4.493  -8.767  30.268  1.00 40.77           H  
ATOM   2818  HG3 MET A 291       3.714  -8.929  31.643  1.00 40.77           H  
ATOM   2819  HE1 MET A 291       4.057  -5.740  33.451  1.00 46.27           H  
ATOM   2820  HE2 MET A 291       3.335  -7.152  33.370  1.00 46.27           H  
ATOM   2821  HE3 MET A 291       4.887  -7.071  33.701  1.00 46.27           H  
ATOM   2822  N   ILE A 292       9.135  -8.920  32.689  1.00 34.70           N  
ANISOU 2822  N   ILE A 292     3804   4279   5101   -225     64   -176       N  
ATOM   2823  CA  ILE A 292      10.403  -9.553  33.016  1.00 30.29           C  
ANISOU 2823  CA  ILE A 292     3345   3676   4488   -222     67   -180       C  
ATOM   2824  C   ILE A 292      10.664  -9.512  34.514  1.00 32.60           C  
ANISOU 2824  C   ILE A 292     3672   3984   4729   -172    123   -186       C  
ATOM   2825  O   ILE A 292      10.116  -8.687  35.250  1.00 32.46           O  
ANISOU 2825  O   ILE A 292     3617   4004   4713   -124    155   -205       O  
ATOM   2826  CB  ILE A 292      11.583  -8.900  32.257  1.00 30.91           C  
ANISOU 2826  CB  ILE A 292     3459   3721   4563   -195      8   -201       C  
ATOM   2827  CG1 ILE A 292      11.714  -7.414  32.615  1.00 34.59           C  
ANISOU 2827  CG1 ILE A 292     3903   4190   5049   -133     -4   -229       C  
ATOM   2828  CG2 ILE A 292      11.394  -9.036  30.739  1.00 28.03           C  
ANISOU 2828  CG2 ILE A 292     3080   3349   4221   -241    -43   -190       C  
ATOM   2829  CD1 ILE A 292      12.754  -7.128  33.657  1.00 33.76           C  
ANISOU 2829  CD1 ILE A 292     3848   4075   4902    -91      3   -261       C  
ATOM   2830  H   ILE A 292       9.017  -8.145  33.042  1.00 41.64           H  
ATOM   2831  HA  ILE A 292      10.338 -10.489  32.771  1.00 36.35           H  
ATOM   2832  HB  ILE A 292      12.391  -9.363  32.528  1.00 37.09           H  
ATOM   2833 HG12 ILE A 292      11.955  -6.922  31.814  1.00 41.51           H  
ATOM   2834 HG13 ILE A 292      10.862  -7.099  32.954  1.00 41.51           H  
ATOM   2835 HG21 ILE A 292      12.138  -8.607  30.289  1.00 33.64           H  
ATOM   2836 HG22 ILE A 292      11.366  -9.978  30.508  1.00 33.64           H  
ATOM   2837 HG23 ILE A 292      10.562  -8.608  30.485  1.00 33.64           H  
ATOM   2838 HD11 ILE A 292      12.854  -6.167  33.748  1.00 40.51           H  
ATOM   2839 HD12 ILE A 292      12.470  -7.512  34.501  1.00 40.51           H  
ATOM   2840 HD13 ILE A 292      13.596  -7.523  33.381  1.00 40.51           H  
ATOM   2841  N   ASN A 293      11.481 -10.462  34.957  1.00 33.59           N  
ANISOU 2841  N   ASN A 293     3876   4082   4803   -176    135   -170       N  
ATOM   2842  CA  ASN A 293      12.227 -10.370  36.204  1.00 33.31           C  
ANISOU 2842  CA  ASN A 293     3897   4061   4697   -114    154   -179       C  
ATOM   2843  C   ASN A 293      13.650  -9.950  35.872  1.00 30.77           C  
ANISOU 2843  C   ASN A 293     3607   3719   4367    -80     87   -212       C  
ATOM   2844  O   ASN A 293      14.229 -10.422  34.895  1.00 30.10           O  
ANISOU 2844  O   ASN A 293     3534   3600   4303   -105     56   -202       O  
ATOM   2845  CB  ASN A 293      12.266 -11.703  36.951  1.00 42.13           C  
ANISOU 2845  CB  ASN A 293     5082   5167   5760   -127    205   -126       C  
ATOM   2846  CG  ASN A 293      11.175 -11.819  37.979  1.00 48.06           C  
ANISOU 2846  CG  ASN A 293     5814   5965   6482   -132    291    -95       C  
ATOM   2847  OD1 ASN A 293      11.267 -11.250  39.071  1.00 51.70           O  
ANISOU 2847  OD1 ASN A 293     6293   6474   6877    -67    317   -114       O  
ATOM   2848  ND2 ASN A 293      10.129 -12.559  37.639  1.00 46.70           N  
ANISOU 2848  ND2 ASN A 293     5603   5783   6356   -212    338    -52       N  
ATOM   2849  H   ASN A 293      11.625 -11.197  34.535  1.00 40.30           H  
ATOM   2850  HA  ASN A 293      11.804  -9.721  36.788  1.00 39.97           H  
ATOM   2851  HB2 ASN A 293      12.158 -12.427  36.315  1.00 50.56           H  
ATOM   2852  HB3 ASN A 293      13.118 -11.786  37.407  1.00 50.56           H  
ATOM   2853 HD21 ASN A 293       9.476 -12.659  38.190  1.00 56.04           H  
ATOM   2854 HD22 ASN A 293      10.104 -12.940  36.868  1.00 56.04           H  
ATOM   2855  N   LEU A 294      14.212  -9.070  36.684  1.00 31.64           N  
ANISOU 2855  N   LEU A 294     3726   3852   4443    -27     68   -254       N  
ATOM   2856  CA  LEU A 294      15.593  -8.623  36.536  1.00 28.02           C  
ANISOU 2856  CA  LEU A 294     3279   3386   3982     -6      4   -286       C  
ATOM   2857  C   LEU A 294      16.324  -9.001  37.814  1.00 28.06           C  
ANISOU 2857  C   LEU A 294     3335   3427   3898     45     -3   -292       C  
ATOM   2858  O   LEU A 294      15.814  -8.761  38.917  1.00 28.92           O  
ANISOU 2858  O   LEU A 294     3467   3571   3948     77     28   -307       O  
ATOM   2859  CB  LEU A 294      15.664  -7.116  36.284  1.00 30.31           C  
ANISOU 2859  CB  LEU A 294     3533   3664   4321     -3    -32   -340       C  
ATOM   2860  CG  LEU A 294      17.015  -6.550  35.860  1.00 30.41           C  
ANISOU 2860  CG  LEU A 294     3535   3660   4357    -13    -94   -367       C  
ATOM   2861  CD1 LEU A 294      17.375  -7.014  34.449  1.00 32.07           C  
ANISOU 2861  CD1 LEU A 294     3726   3850   4610    -52   -100   -325       C  
ATOM   2862  CD2 LEU A 294      17.002  -5.016  35.932  1.00 33.72           C  
ANISOU 2862  CD2 LEU A 294     3941   4048   4823    -14   -122   -422       C  
ATOM   2863  H   LEU A 294      13.805  -8.705  37.348  1.00 37.97           H  
ATOM   2864  HA  LEU A 294      16.022  -9.056  35.781  1.00 33.63           H  
ATOM   2865  HB2 LEU A 294      15.033  -6.901  35.579  1.00 36.38           H  
ATOM   2866  HB3 LEU A 294      15.412  -6.664  37.104  1.00 36.38           H  
ATOM   2867  HG  LEU A 294      17.697  -6.877  36.468  1.00 36.49           H  
ATOM   2868 HD11 LEU A 294      18.218  -6.611  34.189  1.00 38.49           H  
ATOM   2869 HD12 LEU A 294      17.455  -7.980  34.445  1.00 38.49           H  
ATOM   2870 HD13 LEU A 294      16.674  -6.737  33.837  1.00 38.49           H  
ATOM   2871 HD21 LEU A 294      17.870  -4.680  35.660  1.00 40.46           H  
ATOM   2872 HD22 LEU A 294      16.315  -4.678  35.338  1.00 40.46           H  
ATOM   2873 HD23 LEU A 294      16.814  -4.745  36.844  1.00 40.46           H  
ATOM   2874  N   PHE A 295      17.507  -9.591  37.671  1.00 26.10           N  
ANISOU 2874  N   PHE A 295     3104   3179   3634     61    -43   -278       N  
ATOM   2875  CA  PHE A 295      18.180 -10.114  38.847  1.00 31.57           C  
ANISOU 2875  CA  PHE A 295     3846   3914   4236    121    -59   -268       C  
ATOM   2876  C   PHE A 295      19.670 -10.254  38.594  1.00 31.15           C  
ANISOU 2876  C   PHE A 295     3770   3877   4188    148   -128   -276       C  
ATOM   2877  O   PHE A 295      20.126 -10.361  37.457  1.00 29.93           O  
ANISOU 2877  O   PHE A 295     3577   3695   4099    123   -136   -269       O  
ATOM   2878  CB  PHE A 295      17.576 -11.471  39.259  1.00 30.51           C  
ANISOU 2878  CB  PHE A 295     3777   3763   4053    131      5   -190       C  
ATOM   2879  CG  PHE A 295      17.509 -12.470  38.131  1.00 32.49           C  
ANISOU 2879  CG  PHE A 295     4037   3947   4363     94     27   -146       C  
ATOM   2880  CD1 PHE A 295      16.417 -12.491  37.277  1.00 33.29           C  
ANISOU 2880  CD1 PHE A 295     4110   4010   4528     23     66   -140       C  
ATOM   2881  CD2 PHE A 295      18.530 -13.383  37.929  1.00 30.95           C  
ANISOU 2881  CD2 PHE A 295     3876   3729   4156    139      3   -116       C  
ATOM   2882  CE1 PHE A 295      16.351 -13.413  36.228  1.00 33.34           C  
ANISOU 2882  CE1 PHE A 295     4136   3954   4578    -16     76   -116       C  
ATOM   2883  CE2 PHE A 295      18.473 -14.298  36.888  1.00 31.58           C  
ANISOU 2883  CE2 PHE A 295     3980   3737   4283    112     26    -91       C  
ATOM   2884  CZ  PHE A 295      17.376 -14.314  36.041  1.00 32.26           C  
ANISOU 2884  CZ  PHE A 295     4051   3783   4425     28     60    -96       C  
ATOM   2885  H   PHE A 295      17.924  -9.697  36.927  1.00 31.32           H  
ATOM   2886  HA  PHE A 295      18.077  -9.476  39.570  1.00 37.88           H  
ATOM   2887  HB2 PHE A 295      18.122 -11.854  39.964  1.00 36.61           H  
ATOM   2888  HB3 PHE A 295      16.673 -11.326  39.581  1.00 36.61           H  
ATOM   2889  HD1 PHE A 295      15.722 -11.887  37.403  1.00 39.95           H  
ATOM   2890  HD2 PHE A 295      19.265 -13.383  38.499  1.00 37.14           H  
ATOM   2891  HE1 PHE A 295      15.617 -13.417  35.658  1.00 40.01           H  
ATOM   2892  HE2 PHE A 295      19.169 -14.901  36.758  1.00 37.90           H  
ATOM   2893  HZ  PHE A 295      17.331 -14.932  35.347  1.00 38.72           H  
ATOM   2894  N   CYS A 296      20.418 -10.249  39.690  1.00 32.91           N  
ANISOU 2894  N   CYS A 296     3442   3905   5156   -107   -677   -786       N  
ATOM   2895  CA  CYS A 296      21.857 -10.513  39.696  1.00 38.64           C  
ANISOU 2895  CA  CYS A 296     4014   4632   6034   -104   -745   -771       C  
ATOM   2896  C   CYS A 296      22.079 -11.568  40.776  1.00 39.40           C  
ANISOU 2896  C   CYS A 296     4098   4690   6181     34   -786   -651       C  
ATOM   2897  O   CYS A 296      22.065 -11.253  41.970  1.00 33.43           O  
ANISOU 2897  O   CYS A 296     3442   3974   5287    114   -927   -576       O  
ATOM   2898  CB  CYS A 296      22.642  -9.250  39.956  1.00 37.92           C  
ANISOU 2898  CB  CYS A 296     3919   4587   5903   -171   -911   -795       C  
ATOM   2899  SG  CYS A 296      24.407  -9.497  40.043  1.00 42.19           S  
ANISOU 2899  SG  CYS A 296     4229   5140   6662   -173  -1016   -776       S  
ATOM   2900  H   CYS A 296      20.105 -10.090  40.475  1.00 39.49           H  
ATOM   2901  HA  CYS A 296      22.155 -10.861  38.841  1.00 46.36           H  
ATOM   2902  HB2 CYS A 296      22.466  -8.621  39.239  1.00 45.51           H  
ATOM   2903  HB3 CYS A 296      22.354  -8.874  40.803  1.00 45.51           H  
ATOM   2904  HG  CYS A 296      24.650 -10.280  40.919  1.00 50.63           H  
ATOM   2905  N   GLY A 297      22.249 -12.823  40.359  1.00 41.54           N  
ANISOU 2905  N   GLY A 297     4260   4884   6641     78   -659   -633       N  
ATOM   2906  CA  GLY A 297      22.300 -13.907  41.326  1.00 45.86           C  
ANISOU 2906  CA  GLY A 297     4807   5364   7254    220   -662   -484       C  
ATOM   2907  C   GLY A 297      20.989 -13.992  42.076  1.00 46.51           C  
ANISOU 2907  C   GLY A 297     5058   5428   7186    271   -610   -393       C  
ATOM   2908  O   GLY A 297      19.906 -13.997  41.478  1.00 45.89           O  
ANISOU 2908  O   GLY A 297     5022   5313   7100    202   -479   -462       O  
ATOM   2909  H   GLY A 297      22.336 -13.065  39.539  1.00 49.85           H  
ATOM   2910  HA2 GLY A 297      22.459 -14.749  40.872  1.00 55.03           H  
ATOM   2911  HA3 GLY A 297      23.016 -13.750  41.961  1.00 55.03           H  
ATOM   2912  N   LYS A 298      21.075 -14.029  43.406  1.00 47.43           N  
ANISOU 2912  N   LYS A 298     5267   5586   7170    403   -714   -237       N  
ATOM   2913  CA  LYS A 298      19.888 -14.089  44.252  1.00 43.96           C  
ANISOU 2913  CA  LYS A 298     4988   5151   6564    478   -644   -119       C  
ATOM   2914  C   LYS A 298      19.266 -12.723  44.517  1.00 43.26           C  
ANISOU 2914  C   LYS A 298     5050   5178   6210    438   -725   -204       C  
ATOM   2915  O   LYS A 298      18.250 -12.655  45.214  1.00 40.48           O  
ANISOU 2915  O   LYS A 298     4830   4850   5700    509   -655   -118       O  
ATOM   2916  CB  LYS A 298      20.226 -14.752  45.592  1.00 42.67           C  
ANISOU 2916  CB  LYS A 298     4877   5004   6330    674   -700    110       C  
ATOM   2917  CG  LYS A 298      20.320 -16.263  45.519  1.00 47.63           C  
ANISOU 2917  CG  LYS A 298     5402   5466   7229    744   -546    259       C  
ATOM   2918  CD  LYS A 298      20.829 -16.865  46.828  1.00 49.66           C  
ANISOU 2918  CD  LYS A 298     5710   5756   7404    963   -622    516       C  
ATOM   2919  CE  LYS A 298      22.126 -16.194  47.279  1.00 52.30           C  
ANISOU 2919  CE  LYS A 298     6014   6249   7607   1025   -908    467       C  
ATOM   2920  NZ  LYS A 298      22.872 -16.994  48.288  1.00 59.14           N  
ANISOU 2920  NZ  LYS A 298     6869   7137   8465   1248  -1002    702       N  
ATOM   2921  H   LYS A 298      21.816 -14.020  43.843  1.00 56.92           H  
ATOM   2922  HA  LYS A 298      19.227 -14.636  43.800  1.00 52.75           H  
ATOM   2923  HB2 LYS A 298      21.083 -14.416  45.899  1.00 51.20           H  
ATOM   2924  HB3 LYS A 298      19.534 -14.529  46.234  1.00 51.20           H  
ATOM   2925  HG2 LYS A 298      19.440 -16.630  45.338  1.00 57.16           H  
ATOM   2926  HG3 LYS A 298      20.935 -16.512  44.811  1.00 57.16           H  
ATOM   2927  HD2 LYS A 298      20.163 -16.739  47.521  1.00 59.60           H  
ATOM   2928  HD3 LYS A 298      21.002 -17.811  46.701  1.00 59.60           H  
ATOM   2929  HE2 LYS A 298      22.703 -16.072  46.509  1.00 62.76           H  
ATOM   2930  HE3 LYS A 298      21.916 -15.334  47.676  1.00 62.76           H  
ATOM   2931  HZ1 LYS A 298      23.602 -16.555  48.546  1.00 70.97           H  
ATOM   2932  HZ2 LYS A 298      22.358 -17.144  48.999  1.00 70.97           H  
ATOM   2933  HZ3 LYS A 298      23.115 -17.776  47.938  1.00 70.97           H  
ATOM   2934  N   SER A 299      19.846 -11.647  43.989  1.00 41.54           N  
ANISOU 2934  N   SER A 299     4810   5018   5957    334   -855   -360       N  
ATOM   2935  CA  SER A 299      19.332 -10.299  44.191  1.00 42.46           C  
ANISOU 2935  CA  SER A 299     5066   5208   5861    296   -939   -453       C  
ATOM   2936  C   SER A 299      18.323 -10.008  43.088  1.00 38.83           C  
ANISOU 2936  C   SER A 299     4607   4709   5438    181   -786   -546       C  
ATOM   2937  O   SER A 299      18.706  -9.761  41.942  1.00 35.98           O  
ANISOU 2937  O   SER A 299     4147   4329   5194     62   -765   -650       O  
ATOM   2938  CB  SER A 299      20.470  -9.287  44.190  1.00 41.09           C  
ANISOU 2938  CB  SER A 299     4854   5081   5679    234  -1154   -561       C  
ATOM   2939  OG  SER A 299      20.053  -8.062  44.757  1.00 51.72           O  
ANISOU 2939  OG  SER A 299     6359   6477   6815    242  -1270   -638       O  
ATOM   2940  H   SER A 299      20.553 -11.675  43.501  1.00 49.85           H  
ATOM   2941  HA  SER A 299      18.879 -10.240  45.047  1.00 50.96           H  
ATOM   2942  HB2 SER A 299      21.208  -9.641  44.711  1.00 49.31           H  
ATOM   2943  HB3 SER A 299      20.755  -9.132  43.276  1.00 49.31           H  
ATOM   2944  HG  SER A 299      20.690  -7.513  44.756  1.00 62.06           H  
ATOM   2945  N   ILE A 300      17.037 -10.039  43.438  1.00 32.12           N  
ANISOU 2945  N   ILE A 300     3860   3863   4480    230   -678   -502       N  
ATOM   2946  CA  ILE A 300      15.930  -9.913  42.494  1.00 34.13           C  
ANISOU 2946  CA  ILE A 300     4100   4092   4776    148   -542   -578       C  
ATOM   2947  C   ILE A 300      15.289  -8.548  42.685  1.00 31.40           C  
ANISOU 2947  C   ILE A 300     3893   3808   4230    149   -604   -645       C  
ATOM   2948  O   ILE A 300      14.959  -8.161  43.813  1.00 30.74           O  
ANISOU 2948  O   ILE A 300     3942   3773   3964    260   -647   -592       O  
ATOM   2949  CB  ILE A 300      14.899 -11.043  42.693  1.00 34.18           C  
ANISOU 2949  CB  ILE A 300     4074   4035   4879    194   -358   -478       C  
ATOM   2950  CG1 ILE A 300      15.572 -12.405  42.471  1.00 35.83           C  
ANISOU 2950  CG1 ILE A 300     4146   4140   5327    196   -296   -421       C  
ATOM   2951  CG2 ILE A 300      13.722 -10.872  41.756  1.00 30.70           C  
ANISOU 2951  CG2 ILE A 300     3596   3585   4484    112   -254   -580       C  
ATOM   2952  CD1 ILE A 300      14.763 -13.576  42.978  1.00 36.77           C  
ANISOU 2952  CD1 ILE A 300     4237   4158   5577    256   -126   -273       C  
ATOM   2953  H   ILE A 300      16.772 -10.135  44.251  1.00 38.54           H  
ATOM   2954  HA  ILE A 300      16.270  -9.963  41.587  1.00 40.96           H  
ATOM   2955  HB  ILE A 300      14.566 -10.999  43.603  1.00 41.02           H  
ATOM   2956 HG12 ILE A 300      15.712 -12.533  41.520  1.00 43.00           H  
ATOM   2957 HG13 ILE A 300      16.424 -12.412  42.935  1.00 43.00           H  
ATOM   2958 HG21 ILE A 300      13.180 -11.676  41.778  1.00 36.84           H  
ATOM   2959 HG22 ILE A 300      13.195 -10.110  42.046  1.00 36.84           H  
ATOM   2960 HG23 ILE A 300      14.053 -10.721  40.856  1.00 36.84           H  
ATOM   2961 HD11 ILE A 300      15.296 -14.383  42.908  1.00 44.13           H  
ATOM   2962 HD12 ILE A 300      14.524 -13.417  43.904  1.00 44.13           H  
ATOM   2963 HD13 ILE A 300      13.961 -13.662  42.439  1.00 44.13           H  
ATOM   2964  N   LEU A 301      15.111  -7.821  41.582  1.00 28.90           N  
ANISOU 2964  N   LEU A 301     3552   3492   3937     46   -603   -758       N  
ATOM   2965  CA  LEU A 301      14.686  -6.429  41.676  1.00 32.37           C  
ANISOU 2965  CA  LEU A 301     4117   3959   4222     47   -677   -821       C  
ATOM   2966  C   LEU A 301      13.320  -6.305  42.341  1.00 33.01           C  
ANISOU 2966  C   LEU A 301     4298   4071   4175    148   -594   -784       C  
ATOM   2967  O   LEU A 301      13.138  -5.503  43.264  1.00 30.91           O  
ANISOU 2967  O   LEU A 301     4173   3833   3737    236   -666   -793       O  
ATOM   2968  CB  LEU A 301      14.666  -5.799  40.284  1.00 32.91           C  
ANISOU 2968  CB  LEU A 301     4136   4020   4350    -65   -660   -905       C  
ATOM   2969  CG  LEU A 301      14.218  -4.336  40.209  1.00 30.05           C  
ANISOU 2969  CG  LEU A 301     3894   3652   3870    -65   -723   -954       C  
ATOM   2970  CD1 LEU A 301      15.021  -3.437  41.131  1.00 31.22           C  
ANISOU 2970  CD1 LEU A 301     4139   3765   3958    -50   -888   -982       C  
ATOM   2971  CD2 LEU A 301      14.345  -3.851  38.748  1.00 29.91           C  
ANISOU 2971  CD2 LEU A 301     3817   3634   3913   -163   -690   -989       C  
ATOM   2972  H   LEU A 301      15.229  -8.106  40.780  1.00 34.68           H  
ATOM   2973  HA  LEU A 301      15.325  -5.945  42.223  1.00 38.84           H  
ATOM   2974  HB2 LEU A 301      15.565  -5.842  39.921  1.00 39.50           H  
ATOM   2975  HB3 LEU A 301      14.059  -6.313  39.729  1.00 39.50           H  
ATOM   2976  HG  LEU A 301      13.296  -4.276  40.504  1.00 36.06           H  
ATOM   2977 HD11 LEU A 301      14.766  -2.514  40.973  1.00 37.46           H  
ATOM   2978 HD12 LEU A 301      14.833  -3.679  42.051  1.00 37.46           H  
ATOM   2979 HD13 LEU A 301      15.965  -3.555  40.945  1.00 37.46           H  
ATOM   2980 HD21 LEU A 301      14.048  -2.929  38.695  1.00 35.89           H  
ATOM   2981 HD22 LEU A 301      15.273  -3.916  38.473  1.00 35.89           H  
ATOM   2982 HD23 LEU A 301      13.791  -4.410  38.181  1.00 35.89           H  
ATOM   2983  N   ALA A 302      12.340  -7.086  41.881  1.00 31.04           N  
ANISOU 2983  N   ALA A 302     3964   3812   4017    140   -440   -758       N  
ATOM   2984  CA  ALA A 302      11.001  -6.988  42.454  1.00 31.38           C  
ANISOU 2984  CA  ALA A 302     4061   3887   3976    230   -336   -712       C  
ATOM   2985  C   ALA A 302      11.015  -7.308  43.943  1.00 35.91           C  
ANISOU 2985  C   ALA A 302     4731   4490   4421    370   -311   -585       C  
ATOM   2986  O   ALA A 302      10.281  -6.688  44.723  1.00 37.85           O  
ANISOU 2986  O   ALA A 302     5094   4792   4493    482   -282   -567       O  
ATOM   2987  CB  ALA A 302      10.029  -7.919  41.713  1.00 29.90           C  
ANISOU 2987  CB  ALA A 302     3720   3671   3969    179   -186   -711       C  
ATOM   2988  H   ALA A 302      12.424  -7.667  41.252  1.00 37.25           H  
ATOM   2989  HA  ALA A 302      10.683  -6.078  42.341  1.00 37.66           H  
ATOM   2990  HB1 ALA A 302       9.148  -7.835  42.110  1.00 35.88           H  
ATOM   2991  HB2 ALA A 302       9.997  -7.662  40.779  1.00 35.88           H  
ATOM   2992  HB3 ALA A 302      10.343  -8.833  41.795  1.00 35.88           H  
ATOM   2993  N   ASP A 303      11.850  -8.266  44.359  1.00 32.73           N  
ANISOU 2993  N   ASP A 303     4288   4061   4087    386   -318   -489       N  
ATOM   2994  CA  ASP A 303      11.914  -8.613  45.778  1.00 38.52           C  
ANISOU 2994  CA  ASP A 303     5125   4846   4665    546   -298   -339       C  
ATOM   2995  C   ASP A 303      12.470  -7.460  46.607  1.00 40.20           C  
ANISOU 2995  C   ASP A 303     5512   5146   4616    636   -488   -415       C  
ATOM   2996  O   ASP A 303      11.975  -7.182  47.701  1.00 46.69           O  
ANISOU 2996  O   ASP A 303     6476   6056   5210    794   -460   -359       O  
ATOM   2997  CB  ASP A 303      12.762  -9.875  45.972  1.00 39.22           C  
ANISOU 2997  CB  ASP A 303     5126   4879   4897    556   -282   -210       C  
ATOM   2998  CG  ASP A 303      13.060 -10.162  47.436  1.00 49.10           C  
ANISOU 2998  CG  ASP A 303     6500   6208   5946    745   -303    -38       C  
ATOM   2999  OD1 ASP A 303      12.123 -10.103  48.260  1.00 53.35           O  
ANISOU 2999  OD1 ASP A 303     7137   6812   6322    869   -175     70       O  
ATOM   3000  OD2 ASP A 303      14.232 -10.458  47.765  1.00 48.17           O  
ANISOU 3000  OD2 ASP A 303     6376   6103   5824    783   -444     -4       O  
ATOM   3001  H   ASP A 303      12.376  -8.718  43.852  1.00 39.28           H  
ATOM   3002  HA  ASP A 303      11.017  -8.803  46.093  1.00 46.23           H  
ATOM   3003  HB2 ASP A 303      12.284 -10.637  45.608  1.00 47.06           H  
ATOM   3004  HB3 ASP A 303      13.608  -9.763  45.510  1.00 47.06           H  
ATOM   3005  N   ARG A 304      13.492  -6.777  46.105  1.00 36.47           N  
ANISOU 3005  N   ARG A 304     5026   4650   4179    540   -677   -551       N  
ATOM   3006  CA  ARG A 304      14.099  -5.687  46.871  1.00 43.58           C  
ANISOU 3006  CA  ARG A 304     6071   5603   4885    604   -887   -657       C  
ATOM   3007  C   ARG A 304      13.195  -4.458  46.908  1.00 45.02           C  
ANISOU 3007  C   ARG A 304     6380   5790   4934    635   -883   -774       C  
ATOM   3008  O   ARG A 304      13.198  -3.716  47.896  1.00 47.62           O  
ANISOU 3008  O   ARG A 304     6873   6177   5043    759   -991   -846       O  
ATOM   3009  CB  ARG A 304      15.460  -5.324  46.277  1.00 40.35           C  
ANISOU 3009  CB  ARG A 304     5571   5140   4619    469  -1074   -760       C  
ATOM   3010  CG  ARG A 304      16.433  -6.496  46.163  1.00 48.00           C  
ANISOU 3010  CG  ARG A 304     6393   6099   5745    447  -1084   -660       C  
ATOM   3011  CD  ARG A 304      17.065  -6.829  47.510  1.00 55.26           C  
ANISOU 3011  CD  ARG A 304     7387   7111   6500    610  -1221   -586       C  
ATOM   3012  NE  ARG A 304      16.362  -7.893  48.224  1.00 56.71           N  
ANISOU 3012  NE  ARG A 304     7614   7337   6596    759  -1050   -385       N  
ATOM   3013  CZ  ARG A 304      16.533  -8.159  49.511  1.00 61.19           C  
ANISOU 3013  CZ  ARG A 304     8297   8016   6936    953  -1117   -278       C  
ATOM   3014  NH1 ARG A 304      17.308  -7.404  50.272  1.00 62.07           N  
ANISOU 3014  NH1 ARG A 304     8501   8223   6860   1028  -1378   -392       N  
ATOM   3015  NH2 ARG A 304      15.910  -9.205  50.046  1.00 65.75           N  
ANISOU 3015  NH2 ARG A 304     8894   8610   7477   1078   -919    -49       N  
ATOM   3016  H   ARG A 304      13.851  -6.919  45.336  1.00 43.76           H  
ATOM   3017  HA  ARG A 304      14.239  -5.986  47.783  1.00 52.30           H  
ATOM   3018  HB2 ARG A 304      15.323  -4.970  45.384  1.00 48.42           H  
ATOM   3019  HB3 ARG A 304      15.874  -4.653  46.840  1.00 48.42           H  
ATOM   3020  HG2 ARG A 304      15.957  -7.280  45.848  1.00 57.60           H  
ATOM   3021  HG3 ARG A 304      17.142  -6.266  45.543  1.00 57.60           H  
ATOM   3022  HD2 ARG A 304      17.979  -7.120  47.366  1.00 66.32           H  
ATOM   3023  HD3 ARG A 304      17.053  -6.037  48.069  1.00 66.32           H  
ATOM   3024  HE  ARG A 304      15.804  -8.375  47.782  1.00 68.05           H  
ATOM   3025 HH11 ARG A 304      17.713  -6.725  49.933  1.00 74.48           H  
ATOM   3026 HH12 ARG A 304      17.408  -7.592  51.105  1.00 74.48           H  
ATOM   3027 HH21 ARG A 304      15.403  -9.699  49.558  1.00 78.90           H  
ATOM   3028 HH22 ARG A 304      16.013  -9.387  50.880  1.00 78.90           H  
ATOM   3029  N   LEU A 305      12.429  -4.218  45.842  1.00 37.59           N  
ANISOU 3029  N   LEU A 305     5370   4793   4120    539   -771   -805       N  
ATOM   3030  CA  LEU A 305      11.459  -3.130  45.859  1.00 42.79           C  
ANISOU 3030  CA  LEU A 305     6136   5450   4674    594   -746   -890       C  
ATOM   3031  C   LEU A 305      10.305  -3.447  46.801  1.00 40.99           C  
ANISOU 3031  C   LEU A 305     5981   5310   4285    767   -582   -800       C  
ATOM   3032  O   LEU A 305       9.975  -2.657  47.688  1.00 48.80           O  
ANISOU 3032  O   LEU A 305     7132   6348   5060    911   -618   -865       O  
ATOM   3033  CB  LEU A 305      10.940  -2.878  44.447  1.00 38.84           C  
ANISOU 3033  CB  LEU A 305     5528   4888   4342    468   -677   -923       C  
ATOM   3034  CG  LEU A 305      11.904  -2.247  43.453  1.00 35.84           C  
ANISOU 3034  CG  LEU A 305     5101   4428   4088    318   -804  -1002       C  
ATOM   3035  CD1 LEU A 305      11.427  -2.511  42.033  1.00 31.55           C  
ANISOU 3035  CD1 LEU A 305     4427   3874   3684    219   -700   -986       C  
ATOM   3036  CD2 LEU A 305      12.036  -0.750  43.702  1.00 37.80           C  
ANISOU 3036  CD2 LEU A 305     5492   4608   4264    338   -938  -1118       C  
ATOM   3037  H   LEU A 305      12.453  -4.666  45.108  1.00 45.11           H  
ATOM   3038  HA  LEU A 305      11.895  -2.323  46.172  1.00 51.35           H  
ATOM   3039  HB2 LEU A 305      10.668  -3.731  44.073  1.00 46.61           H  
ATOM   3040  HB3 LEU A 305      10.175  -2.285  44.513  1.00 46.61           H  
ATOM   3041  HG  LEU A 305      12.783  -2.643  43.565  1.00 43.01           H  
ATOM   3042 HD11 LEU A 305      12.044  -2.095  41.410  1.00 37.86           H  
ATOM   3043 HD12 LEU A 305      11.400  -3.469  41.882  1.00 37.86           H  
ATOM   3044 HD13 LEU A 305      10.540  -2.134  41.923  1.00 37.86           H  
ATOM   3045 HD21 LEU A 305      12.626  -0.370  43.032  1.00 45.37           H  
ATOM   3046 HD22 LEU A 305      11.158  -0.342  43.640  1.00 45.37           H  
ATOM   3047 HD23 LEU A 305      12.406  -0.608  44.587  1.00 45.37           H  
ATOM   3048  N   GLN A 306       9.679  -4.607  46.611  1.00 44.83           N  
ANISOU 3048  N   GLN A 306     6340   5809   4885    758   -389   -654       N  
ATOM   3049  CA  GLN A 306       8.624  -5.061  47.513  1.00 45.32           C  
ANISOU 3049  CA  GLN A 306     6436   5948   4836    912   -191   -521       C  
ATOM   3050  C   GLN A 306       9.063  -4.979  48.969  1.00 48.51           C  
ANISOU 3050  C   GLN A 306     7021   6457   4955   1098   -246   -472       C  
ATOM   3051  O   GLN A 306       8.259  -4.677  49.858  1.00 46.62           O  
ANISOU 3051  O   GLN A 306     6896   6312   4506   1274   -134   -436       O  
ATOM   3052  CB  GLN A 306       8.225  -6.489  47.138  1.00 49.22           C  
ANISOU 3052  CB  GLN A 306     6744   6398   5558    844     -2   -360       C  
ATOM   3053  CG  GLN A 306       7.177  -7.117  48.028  1.00 54.22           C  
ANISOU 3053  CG  GLN A 306     7371   7088   6142    979    241   -174       C  
ATOM   3054  CD  GLN A 306       7.764  -7.726  49.284  1.00 55.26           C  
ANISOU 3054  CD  GLN A 306     7614   7287   6094   1128    264      1       C  
ATOM   3055  OE1 GLN A 306       8.902  -8.214  49.286  1.00 54.71           O  
ANISOU 3055  OE1 GLN A 306     7542   7185   6062   1090    134     26       O  
ATOM   3056  NE2 GLN A 306       6.992  -7.694  50.364  1.00 57.34           N  
ANISOU 3056  NE2 GLN A 306     7976   7659   6150   1318    434    132       N  
ATOM   3057  H   GLN A 306       9.846  -5.151  45.967  1.00 53.80           H  
ATOM   3058  HA  GLN A 306       7.846  -4.490  47.414  1.00 54.39           H  
ATOM   3059  HB2 GLN A 306       7.871  -6.481  46.235  1.00 59.06           H  
ATOM   3060  HB3 GLN A 306       9.015  -7.049  47.181  1.00 59.06           H  
ATOM   3061  HG2 GLN A 306       6.539  -6.436  48.295  1.00 65.06           H  
ATOM   3062  HG3 GLN A 306       6.725  -7.821  47.537  1.00 65.06           H  
ATOM   3063 HE21 GLN A 306       6.209  -7.342  50.322  1.00 68.81           H  
ATOM   3064 HE22 GLN A 306       7.276  -8.026  51.105  1.00 68.81           H  
ATOM   3065  N   ARG A 307      10.342  -5.248  49.236  1.00 48.53           N  
ANISOU 3065  N   ARG A 307     7046   6461   4932   1080   -421   -474       N  
ATOM   3066  CA  ARG A 307      10.841  -5.190  50.607  1.00 54.39           C  
ANISOU 3066  CA  ARG A 307     7960   7328   5377   1272   -517   -440       C  
ATOM   3067  C   ARG A 307      10.821  -3.775  51.173  1.00 59.43           C  
ANISOU 3067  C   ARG A 307     8791   8018   5770   1374   -678   -658       C  
ATOM   3068  O   ARG A 307      10.754  -3.607  52.397  1.00 53.16           O  
ANISOU 3068  O   ARG A 307     8172   7364   4662   1587   -701   -652       O  
ATOM   3069  CB  ARG A 307      12.261  -5.756  50.673  1.00 55.49           C  
ANISOU 3069  CB  ARG A 307     8048   7457   5578   1226   -704   -412       C  
ATOM   3070  CG  ARG A 307      12.751  -6.071  52.075  1.00 64.85           C  
ANISOU 3070  CG  ARG A 307     9378   8797   6467   1446   -787   -314       C  
ATOM   3071  CD  ARG A 307      14.158  -6.679  52.040  1.00 71.01           C  
ANISOU 3071  CD  ARG A 307    10066   9562   7353   1399   -981   -279       C  
ATOM   3072  NE  ARG A 307      14.490  -7.369  53.283  1.00 82.56           N  
ANISOU 3072  NE  ARG A 307    11629  11174   8567   1626  -1004    -95       N  
ATOM   3073  CZ  ARG A 307      14.548  -8.690  53.419  1.00 86.04           C  
ANISOU 3073  CZ  ARG A 307    11986  11595   9110   1677   -850    180       C  
ATOM   3074  NH1 ARG A 307      14.331  -9.507  52.399  1.00 81.77           N  
ANISOU 3074  NH1 ARG A 307    11252  10883   8932   1508   -674    272       N  
ATOM   3075  NH2 ARG A 307      14.833  -9.206  54.608  1.00 85.12           N  
ANISOU 3075  NH2 ARG A 307    11987  11630   8725   1914   -878    366       N  
ATOM   3076  H   ARG A 307      10.932  -5.463  48.649  1.00 58.24           H  
ATOM   3077  HA  ARG A 307      10.272  -5.741  51.168  1.00 65.27           H  
ATOM   3078  HB2 ARG A 307      12.289  -6.580  50.162  1.00 66.58           H  
ATOM   3079  HB3 ARG A 307      12.871  -5.107  50.289  1.00 66.58           H  
ATOM   3080  HG2 ARG A 307      12.782  -5.254  52.598  1.00 77.82           H  
ATOM   3081  HG3 ARG A 307      12.151  -6.709  52.492  1.00 77.82           H  
ATOM   3082  HD2 ARG A 307      14.210  -7.321  51.315  1.00 85.22           H  
ATOM   3083  HD3 ARG A 307      14.808  -5.972  51.904  1.00 85.22           H  
ATOM   3084  HE  ARG A 307      14.660  -6.887  53.975  1.00 99.07           H  
ATOM   3085 HH11 ARG A 307      14.147  -9.185  51.623  1.00 98.12           H  
ATOM   3086 HH12 ARG A 307      14.374 -10.358  52.512  1.00 98.12           H  
ATOM   3087 HH21 ARG A 307      14.978  -8.687  55.278  1.00102.15           H  
ATOM   3088 HH22 ARG A 307      14.873 -10.059  54.708  1.00102.15           H  
ATOM   3089  N   LYS A 308      10.872  -2.762  50.313  1.00 59.29           N  
ANISOU 3089  N   LYS A 308     8753   7886   5886   1238   -785   -848       N  
ATOM   3090  CA  LYS A 308      10.810  -1.373  50.739  1.00 60.50           C  
ANISOU 3090  CA  LYS A 308     9080   8034   5876   1317   -932  -1071       C  
ATOM   3091  C   LYS A 308       9.386  -0.854  50.879  1.00 58.33           C  
ANISOU 3091  C   LYS A 308     8875   7784   5504   1442   -736  -1083       C  
ATOM   3092  O   LYS A 308       9.199   0.326  51.181  1.00 61.85           O  
ANISOU 3092  O   LYS A 308     9466   8200   5835   1522   -832  -1277       O  
ATOM   3093  CB  LYS A 308      11.586  -0.487  49.757  1.00 61.97           C  
ANISOU 3093  CB  LYS A 308     9207   8054   6284   1115  -1129  -1242       C  
ATOM   3094  CG  LYS A 308      13.081  -0.794  49.737  1.00 63.26           C  
ANISOU 3094  CG  LYS A 308     9297   8197   6540   1007  -1346  -1266       C  
ATOM   3095  CD  LYS A 308      13.883   0.366  49.185  1.00 64.08           C  
ANISOU 3095  CD  LYS A 308     9391   8149   6807    854  -1561  -1464       C  
ATOM   3096  CE  LYS A 308      15.378   0.059  49.234  1.00 66.24           C  
ANISOU 3096  CE  LYS A 308     9559   8416   7193    752  -1776  -1489       C  
ATOM   3097  NZ  LYS A 308      15.884  -0.084  50.630  1.00 64.48           N  
ANISOU 3097  NZ  LYS A 308     9456   8336   6710    928  -1959  -1551       N  
ATOM   3098  H   LYS A 308      10.943  -2.858  49.461  1.00 71.14           H  
ATOM   3099  HA  LYS A 308      11.236  -1.299  51.607  1.00 72.61           H  
ATOM   3100  HB2 LYS A 308      11.238  -0.628  48.862  1.00 74.36           H  
ATOM   3101  HB3 LYS A 308      11.474   0.442  50.014  1.00 74.36           H  
ATOM   3102  HG2 LYS A 308      13.384  -0.971  50.641  1.00 75.91           H  
ATOM   3103  HG3 LYS A 308      13.241  -1.569  49.176  1.00 75.91           H  
ATOM   3104  HD2 LYS A 308      13.631   0.524  48.262  1.00 76.90           H  
ATOM   3105  HD3 LYS A 308      13.714   1.159  49.717  1.00 76.90           H  
ATOM   3106  HE2 LYS A 308      15.547  -0.774  48.766  1.00 79.49           H  
ATOM   3107  HE3 LYS A 308      15.865   0.782  48.810  1.00 79.49           H  
ATOM   3108  HZ1 LYS A 308      15.462  -0.753  51.040  1.00 77.38           H  
ATOM   3109  HZ2 LYS A 308      16.757  -0.256  50.621  1.00 77.38           H  
ATOM   3110  HZ3 LYS A 308      15.741   0.668  51.084  1.00 77.38           H  
ATOM   3111  N   GLY A 309       8.385  -1.703  50.685  1.00 55.80           N  
ANISOU 3111  N   GLY A 309     8442   7506   5253   1462   -467   -890       N  
ATOM   3112  CA  GLY A 309       7.010  -1.312  50.905  1.00 57.85           C  
ANISOU 3112  CA  GLY A 309     8734   7812   5433   1598   -262   -879       C  
ATOM   3113  C   GLY A 309       6.448  -0.333  49.904  1.00 57.92           C  
ANISOU 3113  C   GLY A 309     8696   7702   5611   1513   -284  -1014       C  
ATOM   3114  O   GLY A 309       5.323   0.144  50.092  1.00 57.66           O  
ANISOU 3114  O   GLY A 309     8688   7702   5517   1643   -138  -1030       O  
ATOM   3115  H   GLY A 309       8.481  -2.517  50.425  1.00 66.96           H  
ATOM   3116  HA2 GLY A 309       6.456  -2.107  50.882  1.00 69.42           H  
ATOM   3117  HA3 GLY A 309       6.942  -0.905  51.783  1.00 69.42           H  
ATOM   3118  N   VAL A 310       7.198  -0.010  48.844  1.00 52.10           N  
ANISOU 3118  N   VAL A 310     7886   6829   5079   1312   -452  -1095       N  
ATOM   3119  CA  VAL A 310       6.682   0.879  47.809  1.00 52.06           C  
ANISOU 3119  CA  VAL A 310     7835   6714   5232   1240   -466  -1180       C  
ATOM   3120  C   VAL A 310       5.815   0.152  46.793  1.00 48.25           C  
ANISOU 3120  C   VAL A 310     7139   6242   4952   1151   -296  -1052       C  
ATOM   3121  O   VAL A 310       5.183   0.804  45.950  1.00 45.64           O  
ANISOU 3121  O   VAL A 310     6758   5857   4726   1128   -288  -1096       O  
ATOM   3122  CB  VAL A 310       7.831   1.595  47.071  1.00 51.06           C  
ANISOU 3122  CB  VAL A 310     7722   6441   5236   1073   -694  -1297       C  
ATOM   3123  CG1 VAL A 310       8.584   2.507  48.028  1.00 51.34           C  
ANISOU 3123  CG1 VAL A 310     7955   6437   5117   1152   -893  -1476       C  
ATOM   3124  CG2 VAL A 310       8.778   0.582  46.428  1.00 49.89           C  
ANISOU 3124  CG2 VAL A 310     7424   6290   5243    891   -731  -1201       C  
ATOM   3125  H   VAL A 310       7.999  -0.292  48.707  1.00 62.51           H  
ATOM   3126  HA  VAL A 310       6.133   1.552  48.241  1.00 62.47           H  
ATOM   3127  HB  VAL A 310       7.457   2.141  46.361  1.00 61.27           H  
ATOM   3128 HG11 VAL A 310       9.288   2.963  47.542  1.00 61.61           H  
ATOM   3129 HG12 VAL A 310       7.965   3.155  48.400  1.00 61.61           H  
ATOM   3130 HG13 VAL A 310       8.968   1.970  48.740  1.00 61.61           H  
ATOM   3131 HG21 VAL A 310       9.484   1.060  45.965  1.00 59.87           H  
ATOM   3132 HG22 VAL A 310       9.158   0.021  47.122  1.00 59.87           H  
ATOM   3133 HG23 VAL A 310       8.279   0.038  45.799  1.00 59.87           H  
ATOM   3134  N   CYS A 311       5.775  -1.178  46.845  1.00 50.16           N  
ANISOU 3134  N   CYS A 311     7250   6546   5262   1106   -172   -901       N  
ATOM   3135  CA  CYS A 311       4.923  -1.965  45.966  1.00 47.36           C  
ANISOU 3135  CA  CYS A 311     6678   6196   5120   1020    -22   -810       C  
ATOM   3136  C   CYS A 311       4.651  -3.302  46.638  1.00 48.90           C  
ANISOU 3136  C   CYS A 311     6788   6452   5341   1053    163   -635       C  
ATOM   3137  O   CYS A 311       5.319  -3.685  47.598  1.00 50.10           O  
ANISOU 3137  O   CYS A 311     7046   6643   5347   1124    152   -566       O  
ATOM   3138  CB  CYS A 311       5.565  -2.170  44.593  1.00 41.28           C  
ANISOU 3138  CB  CYS A 311     5788   5349   4546    818   -134   -851       C  
ATOM   3139  SG  CYS A 311       7.139  -3.018  44.687  1.00 47.37           S  
ANISOU 3139  SG  CYS A 311     6556   6086   5355    703   -240   -815       S  
ATOM   3140  H   CYS A 311       6.240  -1.653  47.391  1.00 60.19           H  
ATOM   3141  HA  CYS A 311       4.081  -1.501  45.840  1.00 56.83           H  
ATOM   3142  HB2 CYS A 311       4.970  -2.702  44.042  1.00 49.53           H  
ATOM   3143  HB3 CYS A 311       5.714  -1.305  44.182  1.00 49.53           H  
ATOM   3144  HG  CYS A 311       7.618  -3.077  43.588  1.00 56.84           H  
ATOM   3145  N   GLU A 312       3.655  -4.010  46.118  1.00 53.05           N  
ANISOU 3145  N   GLU A 312     7111   6978   6065   1004    328   -558       N  
ATOM   3146  CA  GLU A 312       3.267  -5.317  46.626  1.00 55.69           C  
ANISOU 3146  CA  GLU A 312     7326   7328   6507   1010    534   -373       C  
ATOM   3147  C   GLU A 312       3.116  -6.278  45.455  1.00 47.86           C  
ANISOU 3147  C   GLU A 312     6094   6250   5839    817    552   -376       C  
ATOM   3148  O   GLU A 312       2.858  -5.868  44.319  1.00 45.43           O  
ANISOU 3148  O   GLU A 312     5697   5925   5640    726    456   -510       O  
ATOM   3149  CB  GLU A 312       1.947  -5.259  47.414  1.00 57.11           C  
ANISOU 3149  CB  GLU A 312     7472   7592   6634   1170    774   -268       C  
ATOM   3150  CG  GLU A 312       1.859  -4.132  48.433  1.00 67.45           C  
ANISOU 3150  CG  GLU A 312     9017   8999   7614   1387    762   -323       C  
ATOM   3151  CD  GLU A 312       2.829  -4.288  49.591  1.00 70.41           C  
ANISOU 3151  CD  GLU A 312     9604   9432   7717   1500    715   -261       C  
ATOM   3152  OE1 GLU A 312       3.643  -5.241  49.570  1.00 65.34           O  
ANISOU 3152  OE1 GLU A 312     8924   8748   7155   1408    681   -160       O  
ATOM   3153  OE2 GLU A 312       2.778  -3.451  50.523  1.00 69.64           O  
ANISOU 3153  OE2 GLU A 312     9710   9428   7322   1696    701   -325       O  
ATOM   3154  H   GLU A 312       3.178  -3.746  45.453  1.00 63.66           H  
ATOM   3155  HA  GLU A 312       3.956  -5.650  47.222  1.00 66.83           H  
ATOM   3156  HB2 GLU A 312       1.218  -5.141  46.786  1.00 68.53           H  
ATOM   3157  HB3 GLU A 312       1.839  -6.095  47.895  1.00 68.53           H  
ATOM   3158  HG2 GLU A 312       2.059  -3.292  47.990  1.00 80.95           H  
ATOM   3159  HG3 GLU A 312       0.961  -4.108  48.799  1.00 80.95           H  
ATOM   3160  N   TYR A 313       3.274  -7.564  45.739  1.00 50.68           N  
ANISOU 3160  N   TYR A 313     6354   6554   6347    770    675   -230       N  
ATOM   3161  CA  TYR A 313       3.089  -8.580  44.713  1.00 47.66           C  
ANISOU 3161  CA  TYR A 313     5742   6071   6297    596    701   -256       C  
ATOM   3162  C   TYR A 313       1.627  -8.638  44.285  1.00 48.09           C  
ANISOU 3162  C   TYR A 313     5590   6139   6544    574    827   -278       C  
ATOM   3163  O   TYR A 313       0.717  -8.386  45.076  1.00 48.56           O  
ANISOU 3163  O   TYR A 313     5645   6264   6544    698    994   -174       O  
ATOM   3164  CB  TYR A 313       3.545  -9.938  45.230  1.00 41.84           C  
ANISOU 3164  CB  TYR A 313     4952   5238   5707    569    822    -80       C  
ATOM   3165  CG  TYR A 313       5.047 -10.068  45.348  1.00 47.69           C  
ANISOU 3165  CG  TYR A 313     5826   5953   6341    560    665    -85       C  
ATOM   3166  CD1 TYR A 313       5.878  -9.774  44.271  1.00 47.19           C  
ANISOU 3166  CD1 TYR A 313     5755   5862   6313    442    466   -269       C  
ATOM   3167  CD2 TYR A 313       5.636 -10.469  46.539  1.00 46.01           C  
ANISOU 3167  CD2 TYR A 313     5740   5759   5984    684    719    104       C  
ATOM   3168  CE1 TYR A 313       7.256  -9.886  44.375  1.00 45.29           C  
ANISOU 3168  CE1 TYR A 313     5603   5601   6006    433    332   -271       C  
ATOM   3169  CE2 TYR A 313       7.016 -10.586  46.654  1.00 46.26           C  
ANISOU 3169  CE2 TYR A 313     5866   5777   5934    684    554     95       C  
ATOM   3170  CZ  TYR A 313       7.818 -10.294  45.570  1.00 44.46           C  
ANISOU 3170  CZ  TYR A 313     5602   5509   5782    552    365    -96       C  
ATOM   3171  OH  TYR A 313       9.186 -10.409  45.677  1.00 49.64           O  
ANISOU 3171  OH  TYR A 313     6317   6155   6390    550    213   -103       O  
ATOM   3172  H   TYR A 313       3.486  -7.873  46.513  1.00 60.81           H  
ATOM   3173  HA  TYR A 313       3.624  -8.363  43.933  1.00 57.20           H  
ATOM   3174  HB2 TYR A 313       3.165 -10.080  46.111  1.00 50.21           H  
ATOM   3175  HB3 TYR A 313       3.235 -10.625  44.619  1.00 50.21           H  
ATOM   3176  HD1 TYR A 313       5.503  -9.497  43.467  1.00 56.63           H  
ATOM   3177  HD2 TYR A 313       5.098 -10.663  47.273  1.00 55.22           H  
ATOM   3178  HE1 TYR A 313       7.798  -9.689  43.646  1.00 54.35           H  
ATOM   3179  HE2 TYR A 313       7.397 -10.860  47.457  1.00 55.52           H  
ATOM   3180  HH  TYR A 313       9.394 -10.661  46.450  1.00 59.57           H  
ATOM   3181  N   LEU A 314       1.412  -8.953  43.013  1.00 55.67           N  
ANISOU 3181  N   LEU A 314     6372   7051   7728    426    739   -425       N  
ATOM   3182  CA  LEU A 314       0.071  -9.174  42.486  1.00 58.81           C  
ANISOU 3182  CA  LEU A 314     6526   7457   8363    381    819   -472       C  
ATOM   3183  C   LEU A 314      -0.467 -10.487  43.055  1.00 66.66           C  
ANISOU 3183  C   LEU A 314     7335   8343   9649    332   1054   -306       C  
ATOM   3184  O   LEU A 314       0.173 -11.536  42.926  1.00 69.54           O  
ANISOU 3184  O   LEU A 314     7656   8576  10189    231   1066   -275       O  
ATOM   3185  CB  LEU A 314       0.072  -9.212  40.963  1.00 59.11           C  
ANISOU 3185  CB  LEU A 314     6434   7491   8533    248    632   -694       C  
ATOM   3186  CG  LEU A 314       0.199  -7.865  40.253  1.00 57.85           C  
ANISOU 3186  CG  LEU A 314     6398   7442   8140    304    440   -828       C  
ATOM   3187  CD1 LEU A 314       0.609  -8.047  38.797  1.00 53.51           C  
ANISOU 3187  CD1 LEU A 314     5779   6899   7652    185    260  -1013       C  
ATOM   3188  CD2 LEU A 314      -1.120  -7.093  40.334  1.00 56.58           C  
ANISOU 3188  CD2 LEU A 314     6152   7376   7970    411    484   -832       C  
ATOM   3189  OXT LEU A 314      -1.545 -10.535  43.651  1.00 70.32           O  
ANISOU 3189  OXT LEU A 314     7682   8836  10201    396   1249   -188       O  
ATOM   3190  H   LEU A 314       2.035  -9.045  42.427  1.00 66.81           H  
ATOM   3191  HA  LEU A 314      -0.513  -8.443  42.742  1.00 70.58           H  
ATOM   3192  HB2 LEU A 314       0.820  -9.759  40.675  1.00 70.93           H  
ATOM   3193  HB3 LEU A 314      -0.763  -9.611  40.671  1.00 70.93           H  
ATOM   3194  HG  LEU A 314       0.891  -7.348  40.695  1.00 69.42           H  
ATOM   3195 HD11 LEU A 314       0.736  -7.175  38.393  1.00 64.21           H  
ATOM   3196 HD12 LEU A 314       1.437  -8.552  38.763  1.00 64.21           H  
ATOM   3197 HD13 LEU A 314      -0.092  -8.529  38.330  1.00 64.21           H  
ATOM   3198 HD21 LEU A 314      -1.000  -6.219  39.929  1.00 67.90           H  
ATOM   3199 HD22 LEU A 314      -1.805  -7.587  39.857  1.00 67.90           H  
ATOM   3200 HD23 LEU A 314      -1.371  -6.994  41.265  1.00 67.90           H  
TER    3201      LEU A 314                                                      
ATOM   3202  N   GLU B  85      21.171  -5.804  54.695  1.00 69.39           N  
ANISOU 3202  N   GLU B  85     7226  12792   6348   1134  -1304  -2105       N  
ATOM   3203  CA  GLU B  85      20.809  -4.838  53.659  1.00 73.31           C  
ANISOU 3203  CA  GLU B  85     7855  13020   6980    971  -1126  -2227       C  
ATOM   3204  C   GLU B  85      21.734  -4.997  52.448  1.00 75.09           C  
ANISOU 3204  C   GLU B  85     7628  13591   7312    943  -1235  -2215       C  
ATOM   3205  O   GLU B  85      22.932  -4.735  52.526  1.00 68.08           O  
ANISOU 3205  O   GLU B  85     6499  13147   6220    649  -1419  -2223       O  
ATOM   3206  CB  GLU B  85      20.879  -3.416  54.213  1.00 76.73           C  
ANISOU 3206  CB  GLU B  85     8717  13305   7132    507  -1080  -2394       C  
ATOM   3207  CG  GLU B  85      20.492  -2.327  53.217  1.00 77.98           C  
ANISOU 3207  CG  GLU B  85     9071  13127   7431    322   -905  -2484       C  
ATOM   3208  CD  GLU B  85      19.129  -1.706  53.507  1.00 80.80           C  
ANISOU 3208  CD  GLU B  85     9935  12907   7858    442   -629  -2560       C  
ATOM   3209  OE1 GLU B  85      18.300  -2.348  54.190  1.00 81.82           O  
ANISOU 3209  OE1 GLU B  85    10162  12901   8023    768   -519  -2499       O  
ATOM   3210  OE2 GLU B  85      18.889  -0.568  53.048  1.00 79.95           O  
ANISOU 3210  OE2 GLU B  85    10115  12487   7777    218   -518  -2658       O  
ATOM   3211  HA  GLU B  85      19.898  -4.990  53.365  1.00 87.98           H  
ATOM   3212  HB2 GLU B  85      20.275  -3.349  54.969  1.00 92.08           H  
ATOM   3213  HB3 GLU B  85      21.789  -3.240  54.499  1.00 92.08           H  
ATOM   3214  HG2 GLU B  85      21.155  -1.620  53.251  1.00 93.58           H  
ATOM   3215  HG3 GLU B  85      20.461  -2.711  52.327  1.00 93.58           H  
ATOM   3216  N   SER B  86      21.158  -5.418  51.326  1.00 76.18           N  
ANISOU 3216  N   SER B  86     7642  13552   7753   1251  -1119  -2193       N  
ATOM   3217  CA  SER B  86      21.936  -5.730  50.141  1.00 72.42           C  
ANISOU 3217  CA  SER B  86     6737  13429   7352   1333  -1189  -2186       C  
ATOM   3218  C   SER B  86      22.543  -4.459  49.543  1.00 69.87           C  
ANISOU 3218  C   SER B  86     6429  13246   6874    865  -1139  -2227       C  
ATOM   3219  O   SER B  86      22.318  -3.336  50.007  1.00 68.89           O  
ANISOU 3219  O   SER B  86     6684  12868   6624    483  -1071  -2281       O  
ATOM   3220  CB  SER B  86      21.060  -6.424  49.092  1.00 67.94           C  
ANISOU 3220  CB  SER B  86     6111  12595   7109   1769  -1090  -2189       C  
ATOM   3221  OG  SER B  86      20.197  -5.486  48.468  1.00 62.88           O  
ANISOU 3221  OG  SER B  86     5770  11572   6549   1648   -890  -2230       O  
ATOM   3222  H   SER B  86      20.311  -5.532  51.228  1.00 91.42           H  
ATOM   3223  HA  SER B  86      22.654  -6.327  50.404  1.00 86.91           H  
ATOM   3224  HB2 SER B  86      21.630  -6.827  48.418  1.00 81.53           H  
ATOM   3225  HB3 SER B  86      20.526  -7.107  49.526  1.00 81.53           H  
ATOM   3226  HG  SER B  86      19.746  -5.865  47.869  1.00 75.46           H  
ATOM   3227  N   LEU B  87      23.330  -4.650  48.482  1.00 71.71           N  
ANISOU 3227  N   LEU B  87     6247  13886   7115    906  -1169  -2193       N  
ATOM   3228  CA  LEU B  87      23.809  -3.516  47.695  1.00 71.09           C  
ANISOU 3228  CA  LEU B  87     6148  13932   6932    490  -1086  -2166       C  
ATOM   3229  C   LEU B  87      22.646  -2.785  47.036  1.00 71.25           C  
ANISOU 3229  C   LEU B  87     6574  13398   7098    495   -870  -2185       C  
ATOM   3230  O   LEU B  87      22.527  -1.557  47.136  1.00 75.62           O  
ANISOU 3230  O   LEU B  87     7456  13696   7580     75   -798  -2182       O  
ATOM   3231  CB  LEU B  87      24.806  -4.007  46.642  1.00 74.40           C  
ANISOU 3231  CB  LEU B  87     6001  14953   7314    625  -1115  -2100       C  
ATOM   3232  CG  LEU B  87      25.508  -3.021  45.721  1.00 75.17           C  
ANISOU 3232  CG  LEU B  87     5931  15346   7284    216  -1025  -1996       C  
ATOM   3233  CD1 LEU B  87      26.574  -3.789  44.909  1.00 72.87           C  
ANISOU 3233  CD1 LEU B  87     5147  15600   6941    461   -979  -1894       C  
ATOM   3234  CD2 LEU B  87      24.571  -2.298  44.780  1.00 73.89           C  
ANISOU 3234  CD2 LEU B  87     6107  14747   7219    198   -816  -1976       C  
ATOM   3235  H   LEU B  87      23.598  -5.417  48.202  1.00 86.05           H  
ATOM   3236  HA  LEU B  87      24.266  -2.891  48.279  1.00 85.31           H  
ATOM   3237  HB2 LEU B  87      25.510  -4.478  47.115  1.00 89.28           H  
ATOM   3238  HB3 LEU B  87      24.328  -4.621  46.063  1.00 89.28           H  
ATOM   3239  HG  LEU B  87      25.912  -2.331  46.270  1.00 90.20           H  
ATOM   3240 HD11 LEU B  87      27.023  -3.170  44.313  1.00 87.44           H  
ATOM   3241 HD12 LEU B  87      27.214  -4.183  45.521  1.00 87.44           H  
ATOM   3242 HD13 LEU B  87      26.137  -4.486  44.394  1.00 87.44           H  
ATOM   3243 HD21 LEU B  87      25.091  -1.724  44.195  1.00 88.67           H  
ATOM   3244 HD22 LEU B  87      24.084  -2.952  44.254  1.00 88.67           H  
ATOM   3245 HD23 LEU B  87      23.950  -1.764  45.300  1.00 88.67           H  
ATOM   3246  N   LEU B  88      21.786  -3.527  46.332  1.00 58.85           N  
ANISOU 3246  N   LEU B  88     4987  11626   5745    972   -791  -2203       N  
ATOM   3247  CA  LEU B  88      20.686  -2.894  45.607  1.00 59.07           C  
ANISOU 3247  CA  LEU B  88     5338  11186   5919   1019   -614  -2197       C  
ATOM   3248  C   LEU B  88      19.758  -2.133  46.550  1.00 61.42           C  
ANISOU 3248  C   LEU B  88     6148  10932   6258    866   -516  -2234       C  
ATOM   3249  O   LEU B  88      19.225  -1.073  46.192  1.00 60.29           O  
ANISOU 3249  O   LEU B  88     6325  10438   6143    686   -382  -2214       O  
ATOM   3250  CB  LEU B  88      19.909  -3.948  44.823  1.00 51.02           C  
ANISOU 3250  CB  LEU B  88     4195  10059   5131   1558   -609  -2230       C  
ATOM   3251  CG  LEU B  88      18.759  -3.438  43.949  1.00 50.45           C  
ANISOU 3251  CG  LEU B  88     4380   9570   5218   1667   -469  -2209       C  
ATOM   3252  CD1 LEU B  88      19.280  -2.525  42.849  1.00 49.75           C  
ANISOU 3252  CD1 LEU B  88     4243   9694   4967   1416   -390  -2122       C  
ATOM   3253  CD2 LEU B  88      17.980  -4.606  43.346  1.00 46.33           C  
ANISOU 3253  CD2 LEU B  88     3731   8934   4938   2178   -535  -2269       C  
ATOM   3254  H   LEU B  88      21.818  -4.383  46.259  1.00 70.62           H  
ATOM   3255  HA  LEU B  88      21.053  -2.256  44.976  1.00 70.88           H  
ATOM   3256  HB2 LEU B  88      20.531  -4.407  44.237  1.00 61.22           H  
ATOM   3257  HB3 LEU B  88      19.528  -4.575  45.458  1.00 61.22           H  
ATOM   3258  HG  LEU B  88      18.151  -2.924  44.504  1.00 60.54           H  
ATOM   3259 HD11 LEU B  88      18.612  -2.460  42.149  1.00 59.70           H  
ATOM   3260 HD12 LEU B  88      19.454  -1.648  43.224  1.00 59.70           H  
ATOM   3261 HD13 LEU B  88      20.100  -2.900  42.490  1.00 59.70           H  
ATOM   3262 HD21 LEU B  88      18.222  -4.697  42.411  1.00 55.60           H  
ATOM   3263 HD22 LEU B  88      18.207  -5.418  43.827  1.00 55.60           H  
ATOM   3264 HD23 LEU B  88      17.030  -4.428  43.427  1.00 55.60           H  
ATOM   3265  N   ASP B  89      19.554  -2.662  47.757  1.00 61.51           N  
ANISOU 3265  N   ASP B  89     6248  10867   6257    966   -574  -2278       N  
ATOM   3266  CA  ASP B  89      18.820  -1.932  48.783  1.00 63.61           C  
ANISOU 3266  CA  ASP B  89     6989  10703   6476    828   -466  -2336       C  
ATOM   3267  C   ASP B  89      19.305  -0.493  48.883  1.00 67.71           C  
ANISOU 3267  C   ASP B  89     7792  11128   6807    309   -448  -2386       C  
ATOM   3268  O   ASP B  89      18.526   0.460  48.766  1.00 65.89           O  
ANISOU 3268  O   ASP B  89     7964  10428   6643    238   -291  -2417       O  
ATOM   3269  CB  ASP B  89      18.974  -2.625  50.142  1.00 68.42           C  
ANISOU 3269  CB  ASP B  89     7599  11436   6960    901   -566  -2353       C  
ATOM   3270  CG  ASP B  89      18.382  -4.010  50.149  1.00 70.86           C  
ANISOU 3270  CG  ASP B  89     7695  11729   7500   1385   -585  -2269       C  
ATOM   3271  OD1 ASP B  89      17.837  -4.410  49.110  1.00 65.12           O  
ANISOU 3271  OD1 ASP B  89     6834  10879   7030   1652   -538  -2239       O  
ATOM   3272  OD2 ASP B  89      18.457  -4.694  51.196  1.00 74.47           O  
ANISOU 3272  OD2 ASP B  89     8134  12284   7879   1485   -664  -2223       O  
ATOM   3273  H   ASP B  89      19.830  -3.438  48.003  1.00 73.81           H  
ATOM   3274  HA  ASP B  89      17.881  -1.932  48.541  1.00 76.33           H  
ATOM   3275  HB2 ASP B  89      19.917  -2.699  50.356  1.00 82.10           H  
ATOM   3276  HB3 ASP B  89      18.520  -2.100  50.820  1.00 82.10           H  
ATOM   3277  N   ALA B  90      20.607  -0.329  49.118  1.00 66.55           N  
ANISOU 3277  N   ALA B  90     7430  11415   6439    -61   -629  -2387       N  
ATOM   3278  CA  ALA B  90      21.180   1.003  49.270  1.00 65.37           C  
ANISOU 3278  CA  ALA B  90     7533  11179   6127   -633   -670  -2427       C  
ATOM   3279  C   ALA B  90      20.888   1.868  48.053  1.00 65.72           C  
ANISOU 3279  C   ALA B  90     7690  10973   6308   -752   -527  -2330       C  
ATOM   3280  O   ALA B  90      20.474   3.025  48.182  1.00 66.51           O  
ANISOU 3280  O   ALA B  90     8260  10595   6416  -1006   -448  -2378       O  
ATOM   3281  CB  ALA B  90      22.691   0.898  49.503  1.00 68.25           C  
ANISOU 3281  CB  ALA B  90     7500  12151   6281  -1009   -913  -2389       C  
ATOM   3282  H   ALA B  90      21.176  -0.969  49.193  1.00 79.86           H  
ATOM   3283  HA  ALA B  90      20.782   1.428  50.046  1.00 78.45           H  
ATOM   3284  HB1 ALA B  90      23.053   1.789  49.634  1.00 81.90           H  
ATOM   3285  HB2 ALA B  90      22.852   0.356  50.291  1.00 81.90           H  
ATOM   3286  HB3 ALA B  90      23.102   0.485  48.727  1.00 81.90           H  
ATOM   3287  N   LEU B  91      21.100   1.320  46.857  1.00 70.84           N  
ANISOU 3287  N   LEU B  91     7931  11936   7049   -548   -496  -2192       N  
ATOM   3288  CA  LEU B  91      20.771   2.058  45.642  1.00 72.30           C  
ANISOU 3288  CA  LEU B  91     8212  11926   7331   -612   -359  -2061       C  
ATOM   3289  C   LEU B  91      19.314   2.509  45.655  1.00 67.97           C  
ANISOU 3289  C   LEU B  91     8147  10705   6974   -360   -191  -2105       C  
ATOM   3290  O   LEU B  91      19.009   3.689  45.454  1.00 68.43           O  
ANISOU 3290  O   LEU B  91     8589  10348   7065   -610   -110  -2062       O  
ATOM   3291  CB  LEU B  91      21.041   1.193  44.411  1.00 71.23           C  
ANISOU 3291  CB  LEU B  91     7589  12249   7228   -294   -342  -1950       C  
ATOM   3292  CG  LEU B  91      22.364   0.437  44.308  1.00 70.73           C  
ANISOU 3292  CG  LEU B  91     6952  12917   7005   -335   -475  -1915       C  
ATOM   3293  CD1 LEU B  91      22.365  -0.437  43.045  1.00 59.86           C  
ANISOU 3293  CD1 LEU B  91     5196  11887   5660    110   -420  -1868       C  
ATOM   3294  CD2 LEU B  91      23.553   1.372  44.290  1.00 71.29           C  
ANISOU 3294  CD2 LEU B  91     6892  13297   6896   -964   -535  -1786       C  
ATOM   3295  H   LEU B  91      21.428   0.536  46.724  1.00 85.01           H  
ATOM   3296  HA  LEU B  91      21.339   2.843  45.594  1.00 86.76           H  
ATOM   3297  HB2 LEU B  91      20.340   0.524  44.366  1.00 85.48           H  
ATOM   3298  HB3 LEU B  91      20.996   1.773  43.634  1.00 85.48           H  
ATOM   3299  HG  LEU B  91      22.455  -0.126  45.092  1.00 84.88           H  
ATOM   3300 HD11 LEU B  91      23.227  -0.874  42.964  1.00 71.83           H  
ATOM   3301 HD12 LEU B  91      21.663  -1.103  43.122  1.00 71.83           H  
ATOM   3302 HD13 LEU B  91      22.204   0.125  42.271  1.00 71.83           H  
ATOM   3303 HD21 LEU B  91      24.367   0.847  44.263  1.00 85.54           H  
ATOM   3304 HD22 LEU B  91      23.497   1.938  43.504  1.00 85.54           H  
ATOM   3305 HD23 LEU B  91      23.537   1.917  45.092  1.00 85.54           H  
ATOM   3306  N   LEU B  92      18.398   1.568  45.894  1.00 63.14           N  
ANISOU 3306  N   LEU B  92     7505   9974   6512    140   -143  -2170       N  
ATOM   3307  CA  LEU B  92      16.981   1.903  45.874  1.00 60.07           C  
ANISOU 3307  CA  LEU B  92     7479   9017   6328    421     24  -2183       C  
ATOM   3308  C   LEU B  92      16.621   2.885  46.980  1.00 60.04           C  
ANISOU 3308  C   LEU B  92     7995   8560   6256    216    101  -2308       C  
ATOM   3309  O   LEU B  92      15.751   3.744  46.791  1.00 61.35           O  
ANISOU 3309  O   LEU B  92     8536   8227   6546    276    247  -2297       O  
ATOM   3310  CB  LEU B  92      16.133   0.635  46.001  1.00 55.48           C  
ANISOU 3310  CB  LEU B  92     6707   8438   5936    941     38  -2203       C  
ATOM   3311  CG  LEU B  92      16.202  -0.334  44.820  1.00 50.05           C  
ANISOU 3311  CG  LEU B  92     5601   8060   5356   1236    -42  -2134       C  
ATOM   3312  CD1 LEU B  92      15.522  -1.641  45.204  1.00 46.27           C  
ANISOU 3312  CD1 LEU B  92     4954   7553   5074   1661    -88  -2170       C  
ATOM   3313  CD2 LEU B  92      15.564   0.270  43.585  1.00 47.90           C  
ANISOU 3313  CD2 LEU B  92     5427   7578   5193   1318     41  -2029       C  
ATOM   3314  H   LEU B  92      18.571   0.744  46.067  1.00 75.77           H  
ATOM   3315  HA  LEU B  92      16.774   2.318  45.022  1.00 72.09           H  
ATOM   3316  HB2 LEU B  92      16.429   0.150  46.788  1.00 66.58           H  
ATOM   3317  HB3 LEU B  92      15.206   0.899  46.103  1.00 66.58           H  
ATOM   3318  HG  LEU B  92      17.129  -0.516  44.599  1.00 60.06           H  
ATOM   3319 HD11 LEU B  92      15.541  -2.242  44.443  1.00 55.53           H  
ATOM   3320 HD12 LEU B  92      15.997  -2.037  45.951  1.00 55.53           H  
ATOM   3321 HD13 LEU B  92      14.603  -1.457  45.457  1.00 55.53           H  
ATOM   3322 HD21 LEU B  92      15.538  -0.399  42.883  1.00 57.47           H  
ATOM   3323 HD22 LEU B  92      14.663   0.556  43.802  1.00 57.47           H  
ATOM   3324 HD23 LEU B  92      16.091   1.032  43.297  1.00 57.47           H  
ATOM   3325  N   GLY B  93      17.278   2.775  48.131  1.00 64.52           N  
ANISOU 3325  N   GLY B  93     8603   9298   6614      0     -5  -2437       N  
ATOM   3326  CA  GLY B  93      17.002   3.703  49.215  1.00 69.23           C  
ANISOU 3326  CA  GLY B  93     9729   9490   7083   -189     50  -2609       C  
ATOM   3327  C   GLY B  93      17.250   5.150  48.843  1.00 75.70           C  
ANISOU 3327  C   GLY B  93    10923   9953   7887   -613     51  -2617       C  
ATOM   3328  O   GLY B  93      16.476   6.036  49.212  1.00 76.08           O  
ANISOU 3328  O   GLY B  93    11485   9443   7978   -570    185  -2727       O  
ATOM   3329  H   GLY B  93      17.877   2.183  48.306  1.00 77.43           H  
ATOM   3330  HA2 GLY B  93      16.073   3.614  49.479  1.00 83.07           H  
ATOM   3331  HA3 GLY B  93      17.568   3.484  49.971  1.00 83.07           H  
ATOM   3332  N   LYS B  94      18.322   5.410  48.098  1.00 80.44           N  
ANISOU 3332  N   LYS B  94    11267  10863   8435  -1015    -89  -2483       N  
ATOM   3333  CA  LYS B  94      18.604   6.784  47.699  1.00 86.23           C  
ANISOU 3333  CA  LYS B  94    12343  11238   9181  -1476   -105  -2431       C  
ATOM   3334  C   LYS B  94      17.588   7.279  46.676  1.00 83.01           C  
ANISOU 3334  C   LYS B  94    12128  10393   9017  -1202     85  -2273       C  
ATOM   3335  O   LYS B  94      17.111   8.416  46.770  1.00 90.86           O  
ANISOU 3335  O   LYS B  94    13649  10785  10089  -1320    152  -2312       O  
ATOM   3336  CB  LYS B  94      20.034   6.913  47.154  1.00 93.74           C  
ANISOU 3336  CB  LYS B  94    12905  12694  10016  -2007   -288  -2266       C  
ATOM   3337  CG  LYS B  94      20.344   6.106  45.903  1.00 91.53           C  
ANISOU 3337  CG  LYS B  94    12038  12950   9789  -1800   -249  -2021       C  
ATOM   3338  CD  LYS B  94      21.347   6.829  44.994  1.00 99.82           C  
ANISOU 3338  CD  LYS B  94    12896  14241  10788  -2328   -303  -1766       C  
ATOM   3339  CE  LYS B  94      20.635   7.556  43.858  1.00100.48           C  
ANISOU 3339  CE  LYS B  94    13216  13932  11029  -2246   -139  -1548       C  
ATOM   3340  NZ  LYS B  94      21.562   7.891  42.736  1.00100.33           N  
ANISOU 3340  NZ  LYS B  94    12852  14333  10934  -2617   -141  -1220       N  
ATOM   3341  H   LYS B  94      18.886   4.825  47.818  1.00 96.53           H  
ATOM   3342  HA  LYS B  94      18.543   7.350  48.485  1.00103.47           H  
ATOM   3343  HB2 LYS B  94      20.195   7.846  46.941  1.00112.48           H  
ATOM   3344  HB3 LYS B  94      20.649   6.620  47.844  1.00112.48           H  
ATOM   3345  HG2 LYS B  94      20.727   5.252  46.159  1.00109.84           H  
ATOM   3346  HG3 LYS B  94      19.526   5.966  45.401  1.00109.84           H  
ATOM   3347  HD2 LYS B  94      21.840   7.483  45.514  1.00119.78           H  
ATOM   3348  HD3 LYS B  94      21.958   6.182  44.609  1.00119.78           H  
ATOM   3349  HE2 LYS B  94      19.930   6.988  43.509  1.00120.57           H  
ATOM   3350  HE3 LYS B  94      20.257   8.383  44.196  1.00120.57           H  
ATOM   3351  HZ1 LYS B  94      21.119   8.315  42.091  1.00120.39           H  
ATOM   3352  HZ2 LYS B  94      22.218   8.417  43.030  1.00120.39           H  
ATOM   3353  HZ3 LYS B  94      21.917   7.147  42.401  1.00120.39           H  
ATOM   3354  N   ALA B  95      17.219   6.430  45.715  1.00 69.68           N  
ANISOU 3354  N   ALA B  95    10043   8983   7450   -810    152  -2108       N  
ATOM   3355  CA  ALA B  95      16.216   6.827  44.732  1.00 69.58           C  
ANISOU 3355  CA  ALA B  95    10180   8607   7650   -520    297  -1947       C  
ATOM   3356  C   ALA B  95      14.897   7.216  45.391  1.00 65.90           C  
ANISOU 3356  C   ALA B  95    10170   7531   7340   -168    458  -2084       C  
ATOM   3357  O   ALA B  95      14.183   8.093  44.888  1.00 65.08           O  
ANISOU 3357  O   ALA B  95    10393   6942   7392    -79    559  -1983       O  
ATOM   3358  CB  ALA B  95      15.978   5.687  43.730  1.00 59.62           C  
ANISOU 3358  CB  ALA B  95     8419   7771   6463   -113    302  -1816       C  
ATOM   3359  H   ALA B  95      17.529   5.635  45.612  1.00 83.62           H  
ATOM   3360  HA  ALA B  95      16.552   7.597  44.249  1.00 83.50           H  
ATOM   3361  HB1 ALA B  95      15.284   5.954  43.107  1.00 71.55           H  
ATOM   3362  HB2 ALA B  95      16.803   5.511  43.250  1.00 71.55           H  
ATOM   3363  HB3 ALA B  95      15.701   4.894  44.214  1.00 71.55           H  
ATOM   3364  N   LEU B  96      14.554   6.572  46.500  1.00 73.39           N  
ANISOU 3364  N   LEU B  96    11128   8516   8240     59    494  -2286       N  
ATOM   3365  CA  LEU B  96      13.267   6.786  47.151  1.00 77.36           C  
ANISOU 3365  CA  LEU B  96    11973   8549   8871    460    690  -2399       C  
ATOM   3366  C   LEU B  96      13.357   7.879  48.210  1.00 78.30           C  
ANISOU 3366  C   LEU B  96    12681   8229   8841    216    725  -2635       C  
ATOM   3367  O   LEU B  96      12.381   8.571  48.485  1.00 83.95           O  
ANISOU 3367  O   LEU B  96    13811   8420   9666    479    905  -2713       O  
ATOM   3368  CB  LEU B  96      12.777   5.478  47.776  1.00 75.04           C  
ANISOU 3368  CB  LEU B  96    11369   8543   8599    852    739  -2450       C  
ATOM   3369  CG  LEU B  96      12.563   4.325  46.795  1.00 72.76           C  
ANISOU 3369  CG  LEU B  96    10549   8608   8488   1139    680  -2270       C  
ATOM   3370  CD1 LEU B  96      12.452   2.991  47.522  1.00 69.49           C  
ANISOU 3370  CD1 LEU B  96     9826   8506   8070   1378    654  -2314       C  
ATOM   3371  CD2 LEU B  96      11.324   4.570  45.943  1.00 67.90           C  
ANISOU 3371  CD2 LEU B  96     9977   7662   8161   1507    804  -2126       C  
ATOM   3372  H   LEU B  96      15.055   5.999  46.901  1.00 88.06           H  
ATOM   3373  HA  LEU B  96      12.617   7.074  46.491  1.00 92.83           H  
ATOM   3374  HB2 LEU B  96      13.434   5.186  48.427  1.00 90.05           H  
ATOM   3375  HB3 LEU B  96      11.928   5.648  48.213  1.00 90.05           H  
ATOM   3376  HG  LEU B  96      13.334   4.277  46.209  1.00 87.31           H  
ATOM   3377 HD11 LEU B  96      12.340   2.283  46.868  1.00 83.39           H  
ATOM   3378 HD12 LEU B  96      13.262   2.842  48.035  1.00 83.39           H  
ATOM   3379 HD13 LEU B  96      11.685   3.018  48.116  1.00 83.39           H  
ATOM   3380 HD21 LEU B  96      11.175   3.799  45.373  1.00 81.48           H  
ATOM   3381 HD22 LEU B  96      10.561   4.703  46.526  1.00 81.48           H  
ATOM   3382 HD23 LEU B  96      11.466   5.361  45.399  1.00 81.48           H  
TER    3383      LEU B  96                                                      
HETATM 3384  C1  GOL A 401       6.596 -13.271  22.317  1.00 42.71           C  
HETATM 3385  O1  GOL A 401       7.531 -13.549  21.305  1.00 52.43           O  
HETATM 3386  C2  GOL A 401       5.245 -13.009  21.682  1.00 43.66           C  
HETATM 3387  O2  GOL A 401       5.461 -12.644  20.340  1.00 54.63           O  
HETATM 3388  C3  GOL A 401       4.521 -11.910  22.435  1.00 44.95           C  
HETATM 3389  O3  GOL A 401       3.365 -11.580  21.694  1.00 56.87           O  
HETATM 3390  H11 GOL A 401       6.854 -12.493  22.837  1.00 51.26           H  
HETATM 3391  H12 GOL A 401       6.513 -14.011  22.938  1.00 51.26           H  
HETATM 3392  HO1 GOL A 401       7.555 -12.883  20.778  1.00 62.91           H  
HETATM 3393  H2  GOL A 401       4.712 -13.816  21.746  1.00 52.39           H  
HETATM 3394  HO2 GOL A 401       4.700 -12.566  19.970  1.00 65.56           H  
HETATM 3395  H31 GOL A 401       5.110 -11.146  22.537  1.00 53.94           H  
HETATM 3396  H32 GOL A 401       4.297 -12.222  23.326  1.00 53.94           H  
HETATM 3397  HO3 GOL A 401       2.837 -11.142  22.196  1.00 68.24           H  
HETATM 3398  C1  GOL A 402       7.152   5.798  33.395  1.00 50.52           C  
HETATM 3399  O1  GOL A 402       7.435   6.497  34.594  1.00 47.11           O  
HETATM 3400  C2  GOL A 402       6.384   4.542  33.744  1.00 49.98           C  
HETATM 3401  O2  GOL A 402       7.260   3.428  33.776  1.00 31.84           O  
HETATM 3402  C3  GOL A 402       5.250   4.288  32.750  1.00 51.49           C  
HETATM 3403  O3  GOL A 402       4.281   5.295  32.913  1.00 52.31           O  
HETATM 3404  H11 GOL A 402       7.963   5.552  32.923  1.00 60.62           H  
HETATM 3405  H12 GOL A 402       6.622   6.333  32.784  1.00 60.62           H  
HETATM 3406  HO1 GOL A 402       7.877   7.195  34.394  1.00 56.53           H  
HETATM 3407  H2  GOL A 402       5.996   4.704  34.618  1.00 59.98           H  
HETATM 3408  HO2 GOL A 402       7.651   3.432  34.531  1.00 38.20           H  
HETATM 3409  H31 GOL A 402       4.876   3.408  32.911  1.00 61.79           H  
HETATM 3410  H32 GOL A 402       5.610   4.287  31.849  1.00 61.79           H  
HETATM 3411  HO3 GOL A 402       3.802   5.327  32.211  1.00 62.77           H  
HETATM 3412  O   HOH A 501       0.934  -2.801  23.156  1.00 47.22           O  
HETATM 3413  O   HOH A 502       1.294   8.510  41.647  1.00 47.65           O  
HETATM 3414  O   HOH A 503      32.025  -2.380  38.724  1.00 39.95           O  
HETATM 3415  O   HOH A 504      22.502  -6.796  45.630  1.00 44.93           O  
HETATM 3416  O   HOH A 505      24.802   7.724  13.033  1.00 47.83           O  
HETATM 3417  O   HOH A 506      11.268   0.526  27.188  1.00 28.99           O  
HETATM 3418  O   HOH A 507       9.924   7.319   5.971  1.00 55.41           O  
HETATM 3419  O   HOH A 508      16.369 -10.634  46.298  1.00 37.93           O  
HETATM 3420  O   HOH A 509       3.017  -3.056  37.927  1.00 32.34           O  
HETATM 3421  O   HOH A 510       9.167   7.893  10.022  1.00 38.70           O  
HETATM 3422  O   HOH A 511       8.146   4.123  21.253  1.00 35.29           O  
HETATM 3423  O   HOH A 512       1.067  -3.380  27.306  1.00 37.87           O  
HETATM 3424  O   HOH A 513       7.902  -5.873  21.817  1.00 32.37           O  
HETATM 3425  O   HOH A 514      16.523   7.070   3.216  1.00 50.14           O  
HETATM 3426  O   HOH A 515       3.528   7.124  35.987  1.00 40.21           O  
HETATM 3427  O   HOH A 516      19.245 -10.189  20.231  1.00 48.07           O  
HETATM 3428  O   HOH A 517      24.854   0.143  23.155  1.00 41.51           O  
HETATM 3429  O   HOH A 518       6.326   7.702  36.979  1.00 40.30           O  
HETATM 3430  O   HOH A 519       9.090  -0.455  19.108  1.00 28.70           O  
HETATM 3431  O   HOH A 520      23.348  -0.532  32.425  1.00 39.91           O  
HETATM 3432  O   HOH A 521      16.433 -14.399  46.077  1.00 37.92           O  
HETATM 3433  O   HOH A 522       9.187  -7.340  17.106  1.00 39.75           O  
HETATM 3434  O   HOH A 523      11.523   9.987  39.588  1.00 37.23           O  
HETATM 3435  O   HOH A 524       0.801  -1.962  36.287  1.00 37.77           O  
HETATM 3436  O   HOH A 525      12.134   2.568   1.332  1.00 52.45           O  
HETATM 3437  O   HOH A 526      17.060  -6.743  23.528  1.00 26.52           O  
HETATM 3438  O   HOH A 527      13.720  15.186  10.494  1.00 45.11           O  
HETATM 3439  O   HOH A 528       1.261  -0.987  39.721  1.00 36.55           O  
HETATM 3440  O   HOH A 529      15.327  16.241   8.520  1.00 44.98           O  
HETATM 3441  O   HOH A 530      10.313  -5.362  22.851  1.00 30.55           O  
HETATM 3442  O   HOH A 531      13.823 -13.913  28.860  1.00 30.85           O  
HETATM 3443  O   HOH A 532      31.556  -9.953  39.799  1.00 45.66           O  
HETATM 3444  O   HOH A 533      22.515  -2.168  35.631  1.00 32.03           O  
HETATM 3445  O   HOH A 534      11.694   6.857   8.044  1.00 42.31           O  
HETATM 3446  O   HOH A 535      26.932  -6.357  17.643  1.00 39.99           O  
HETATM 3447  O   HOH A 536      24.046  -5.680  32.953  1.00 27.72           O  
HETATM 3448  O   HOH A 537      25.263  -0.878  35.415  1.00 33.10           O  
HETATM 3449  O   HOH A 538      20.416   2.634  16.580  1.00 30.44           O  
HETATM 3450  O   HOH A 539       5.783  -2.856  37.789  1.00 26.51           O  
HETATM 3451  O   HOH A 540      22.379   3.227  27.950  1.00 42.69           O  
HETATM 3452  O   HOH A 541      15.741   1.418  30.929  1.00 28.91           O  
HETATM 3453  O   HOH A 542       3.720  -5.616  37.237  1.00 41.17           O  
HETATM 3454  O   HOH A 543      21.098   1.398  14.161  1.00 32.65           O  
HETATM 3455  O   HOH A 544      16.862   6.824  30.347  1.00 32.52           O  
HETATM 3456  O   HOH A 545      12.682  12.921  25.674  1.00 29.44           O  
HETATM 3457  O   HOH A 546       7.403  -4.588  19.635  1.00 29.31           O  
HETATM 3458  O   HOH A 547      13.976   8.585  28.218  1.00 35.09           O  
HETATM 3459  O   HOH A 548      12.064  17.088  23.811  1.00 34.16           O  
HETATM 3460  O   HOH A 549       9.084 -16.834  23.958  1.00 37.44           O  
HETATM 3461  O   HOH A 550      23.008  14.291  18.299  1.00 41.24           O  
HETATM 3462  O   HOH A 551      15.900 -11.654  22.600  1.00 32.08           O  
HETATM 3463  O   HOH A 552      17.935 -17.883  35.572  1.00 36.60           O  
HETATM 3464  O   HOH A 553       9.178  -0.498  28.115  1.00 35.81           O  
HETATM 3465  O   HOH A 554      22.890  -3.117  33.034  1.00 27.48           O  
HETATM 3466  O   HOH A 555      23.665  15.459   7.350  1.00 43.44           O  
HETATM 3467  O   HOH A 556      21.874 -13.230  26.562  1.00 40.87           O  
HETATM 3468  O   HOH A 557      18.084  20.467  14.785  1.00 42.67           O  
HETATM 3469  O   HOH A 558      20.641  -8.360  21.020  1.00 40.35           O  
HETATM 3470  O   HOH A 559      14.073 -13.103  46.515  1.00 40.22           O  
HETATM 3471  O   HOH A 560      26.179  10.001  18.154  1.00 50.78           O  
HETATM 3472  O   HOH A 561      23.658  14.347  21.495  1.00 34.65           O  
HETATM 3473  O   HOH A 562      12.568  -8.568  39.337  1.00 26.48           O  
HETATM 3474  O   HOH A 563       8.429  16.861  22.867  1.00 36.30           O  
HETATM 3475  O   HOH A 564      11.177  12.714  37.316  1.00 53.90           O  
HETATM 3476  O   HOH A 565       1.891 -13.708  27.977  1.00 39.88           O  
HETATM 3477  O   HOH A 566      12.104 -10.315  18.254  1.00 33.57           O  
HETATM 3478  O   HOH A 567       1.073   5.474  12.692  1.00 46.86           O  
HETATM 3479  O   HOH A 568       0.495  -1.813  30.932  1.00 34.27           O  
HETATM 3480  O   HOH A 569       1.145 -10.722  31.006  1.00 45.49           O  
HETATM 3481  O   HOH A 570       6.409  -7.742  16.781  1.00 37.38           O  
HETATM 3482  O   HOH A 571      21.207 -16.026  38.962  1.00 41.96           O  
HETATM 3483  O   HOH A 572      16.716  -9.189  21.876  1.00 36.64           O  
HETATM 3484  O   HOH A 573       8.169  13.336  25.635  1.00 39.47           O  
HETATM 3485  O   HOH A 574      -1.535  -2.754  27.248  1.00 38.69           O  
HETATM 3486  O   HOH A 575      10.211  14.509  26.725  1.00 39.68           O  
HETATM 3487  O   HOH A 576      11.951 -13.520  45.132  1.00 41.56           O  
HETATM 3488  O   HOH B 201      15.320  -3.331  49.800  1.00 53.60           O  
CONECT 3384 3385 3386 3390 3391                                                 
CONECT 3385 3384 3392                                                           
CONECT 3386 3384 3387 3388 3393                                                 
CONECT 3387 3386 3394                                                           
CONECT 3388 3386 3389 3395 3396                                                 
CONECT 3389 3388 3397                                                           
CONECT 3390 3384                                                                
CONECT 3391 3384                                                                
CONECT 3392 3385                                                                
CONECT 3393 3386                                                                
CONECT 3394 3387                                                                
CONECT 3395 3388                                                                
CONECT 3396 3388                                                                
CONECT 3397 3389                                                                
CONECT 3398 3399 3400 3404 3405                                                 
CONECT 3399 3398 3406                                                           
CONECT 3400 3398 3401 3402 3407                                                 
CONECT 3401 3400 3408                                                           
CONECT 3402 3400 3403 3409 3410                                                 
CONECT 3403 3402 3411                                                           
CONECT 3404 3398                                                                
CONECT 3405 3398                                                                
CONECT 3406 3399                                                                
CONECT 3407 3400                                                                
CONECT 3408 3401                                                                
CONECT 3409 3402                                                                
CONECT 3410 3402                                                                
CONECT 3411 3403                                                                
MASTER      419    0    2    7   14    0    0    6 1761    2   28   19          
END                                                                             



If you find results from this site helpful for your research, please cite one of our papers:

elNémo is maintained by Yves-Henri Sanejouand.
It was developed by Karsten Suhre.
Between 2003 and 2014, it was hosted by IGS (Marseille).
Last modification: April 25th, 2023.