CNRS Nantes University US2B US2B
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elNémo ID: 2412301442281725092

Job options:

ID        	=	 2412301442281725092
JOBID     	=	 sad
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 on
DORMSD    	=	 on

NRBL      	=	 0
CUTOFF    	=	 3&cp /var/www/html/tools/elnemo/tmp/2412301441431723250.input2 fad.php&
CAONLY    	=	 0


Input data for this run:

HEADER sad

HEADER    FLUORESCENT PROTEIN                     23-MAY-13   4KW4              
TITLE     CRYSTAL STRUCTURE OF GREEN FLUORESCENT PROTEIN                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GREEN FLUORESCENT PROTEIN;                                 
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MUTATION: YES;                                                       
COMPND   6 OTHER_DETAILS: THE PROTEIN IN THIS STRUCTURE IS A VERSION OF GFP     
COMPND   7 CALLED EMERALD GFP                                                   
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: AEQUOREA VICTORIA;                              
SOURCE   3 ORGANISM_COMMON: JELLYFISH;                                          
SOURCE   4 ORGANISM_TAXID: 6100;                                                
SOURCE   5 GENE: GFP;                                                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)                                  
KEYWDS    BETA BARREL, FLUORESCENT PROTEIN, CHROMOPHORE                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.J.BARNARD,X.YU,N.NOINAJ,J.W.TARASKA                                 
REVDAT   1   09-APR-14 4KW4    0                                                
JRNL        AUTH   T.J.BARNARD,X.YU,N.NOINAJ,J.W.TARASKA                        
JRNL        TITL   CRYSTAL STRUCTURE OF GREEN FLUORESCENT PROTEIN               
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.75 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8.2_1309)                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.75                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 23.05                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.380                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 31868                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.172                           
REMARK   3   R VALUE            (WORKING SET) : 0.170                           
REMARK   3   FREE R VALUE                     : 0.204                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 6.280                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2000                            
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 23.0563 -  4.2001    1.00     2324   156  0.1575 0.1778        
REMARK   3     2  4.2001 -  3.3370    1.00     2191   146  0.1431 0.1788        
REMARK   3     3  3.3370 -  2.9161    1.00     2155   144  0.1502 0.1811        
REMARK   3     4  2.9161 -  2.6499    1.00     2150   144  0.1701 0.1971        
REMARK   3     5  2.6499 -  2.4602    1.00     2138   144  0.1570 0.2243        
REMARK   3     6  2.4602 -  2.3153    1.00     2134   143  0.1630 0.2033        
REMARK   3     7  2.3153 -  2.1995    1.00     2110   141  0.1675 0.2273        
REMARK   3     8  2.1995 -  2.1038    1.00     2104   141  0.1639 0.2313        
REMARK   3     9  2.1038 -  2.0228    1.00     2100   141  0.1793 0.2297        
REMARK   3    10  2.0228 -  1.9531    1.00     2120   141  0.1938 0.2131        
REMARK   3    11  1.9531 -  1.8920    1.00     2088   140  0.2226 0.2224        
REMARK   3    12  1.8920 -  1.8380    1.00     2097   140  0.2489 0.2530        
REMARK   3    13  1.8380 -  1.7896    1.00     2087   141  0.2680 0.3011        
REMARK   3    14  1.7896 -  1.7460    1.00     2070   138  0.3050 0.3455        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.190            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.680           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 29.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 26.00                          
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      :  0.011           1928                                  
REMARK   3   ANGLE     :  1.399           2631                                  
REMARK   3   CHIRALITY :  0.081            284                                  
REMARK   3   PLANARITY :  0.006            348                                  
REMARK   3   DIHEDRAL  : 14.575            707                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 8                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: chain 'A' and (resid 2 through 24 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):   5.8131  34.8751  10.6333              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1659 T22:   0.2248                                     
REMARK   3      T33:   0.1561 T12:  -0.0588                                     
REMARK   3      T13:   0.0471 T23:  -0.0606                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.9422 L22:   0.9654                                     
REMARK   3      L33:   1.2153 L12:   1.4834                                     
REMARK   3      L13:  -0.6529 L23:  -0.0309                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1399 S12:  -0.0676 S13:  -0.0329                       
REMARK   3      S21:   0.0429 S22:   0.0313 S23:  -0.0186                       
REMARK   3      S31:  -0.1517 S32:   0.1419 S33:  -0.1594                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: chain 'A' and (resid 25 through 68 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):   9.8511  41.3592   5.1179              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2276 T22:   0.1802                                     
REMARK   3      T33:   0.1739 T12:  -0.0837                                     
REMARK   3      T13:   0.0497 T23:  -0.0546                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0235 L22:   2.5201                                     
REMARK   3      L33:   1.5618 L12:   1.3662                                     
REMARK   3      L13:   0.0986 L23:   0.5919                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0724 S12:   0.0104 S13:   0.2630                       
REMARK   3      S21:  -0.0952 S22:   0.0666 S23:   0.0649                       
REMARK   3      S31:  -0.5582 S32:   0.2005 S33:  -0.0565                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: chain 'A' and (resid 69 through 81 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.3023  21.3211   1.2920              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1193 T22:   0.1521                                     
REMARK   3      T33:   0.1664 T12:  -0.0459                                     
REMARK   3      T13:  -0.0254 T23:   0.0217                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6696 L22:   5.6767                                     
REMARK   3      L33:   2.5332 L12:   1.5808                                     
REMARK   3      L13:   0.5822 L23:   2.1659                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0439 S12:  -0.1210 S13:  -0.1196                       
REMARK   3      S21:   0.0898 S22:  -0.0393 S23:   0.4711                       
REMARK   3      S31:   0.2803 S32:  -0.5372 S33:   0.0129                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: chain 'A' and (resid 82 through 128 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  12.5488  30.8642  10.1624              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1210 T22:   0.2715                                     
REMARK   3      T33:   0.1466 T12:  -0.0333                                     
REMARK   3      T13:  -0.0008 T23:  -0.0825                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1908 L22:   1.0013                                     
REMARK   3      L33:   0.6352 L12:   0.6221                                     
REMARK   3      L13:   0.4139 L23:   0.0700                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1092 S12:  -0.1426 S13:   0.0047                       
REMARK   3      S21:   0.1590 S22:   0.1229 S23:  -0.1214                       
REMARK   3      S31:   0.1274 S32:   0.4535 S33:  -0.1501                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: chain 'A' and (resid 129 through 147 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  21.6845  42.0788  -4.9024              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3275 T22:   0.5590                                     
REMARK   3      T33:   0.2898 T12:  -0.3814                                     
REMARK   3      T13:   0.1150 T23:  -0.0850                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4808 L22:   0.3889                                     
REMARK   3      L33:   0.3938 L12:   0.0409                                     
REMARK   3      L13:   0.4292 L23:   0.0646                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0938 S12:   0.2377 S13:   0.1269                       
REMARK   3      S21:  -0.0993 S22:   0.1807 S23:  -0.3286                       
REMARK   3      S31:  -0.5701 S32:   0.7063 S33:   0.3214                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: chain 'A' and (resid 148 through 170 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  13.5753  23.0041   0.0983              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1403 T22:   0.1898                                     
REMARK   3      T33:   0.1738 T12:   0.0328                                     
REMARK   3      T13:  -0.0524 T23:  -0.0755                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8710 L22:   6.2596                                     
REMARK   3      L33:   3.0751 L12:   2.0227                                     
REMARK   3      L13:  -1.3353 L23:  -2.7467                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0025 S12:   0.0609 S13:  -0.2071                       
REMARK   3      S21:   0.1030 S22:   0.0194 S23:  -0.4026                       
REMARK   3      S31:   0.1013 S32:   0.3749 S33:   0.0149                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: chain 'A' and (resid 171 through 187 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  18.4979  30.8766  -1.8321              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1772 T22:   0.3548                                     
REMARK   3      T33:   0.1539 T12:  -0.0510                                     
REMARK   3      T13:   0.0049 T23:  -0.1128                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8902 L22:   0.7366                                     
REMARK   3      L33:   1.0021 L12:  -0.2206                                     
REMARK   3      L13:  -0.6204 L23:   0.8338                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1094 S12:   0.1781 S13:  -0.1195                       
REMARK   3      S21:  -0.0944 S22:   0.0897 S23:  -0.3348                       
REMARK   3      S31:  -0.1789 S32:   0.7668 S33:  -0.0762                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: chain 'A' and (resid 188 through 231 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   5.1885  32.1855   1.0626              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1989 T22:   0.1305                                     
REMARK   3      T33:   0.1266 T12:  -0.0554                                     
REMARK   3      T13:   0.0165 T23:  -0.0149                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2240 L22:   1.2152                                     
REMARK   3      L33:   1.8489 L12:   0.1500                                     
REMARK   3      L13:   0.3857 L23:   0.6047                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2021 S12:  -0.1131 S13:   0.0922                       
REMARK   3      S21:   0.2790 S22:  -0.2053 S23:   0.1237                       
REMARK   3      S31:  -0.1936 S32:  -0.0112 S33:  -0.0317                       
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 4KW4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-JUN-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB079868.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-AUG-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 22-BM                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0000                             
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 31923                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.746                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 8.300                              
REMARK 200  R MERGE                    (I) : 0.08800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 8.7000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.81                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.82200                            
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: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.77                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.78                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 50 MM HEPES PH 8.2, 50 MM MGCL2, 22%     
REMARK 280  PEG4000, HANGING DROP, TEMPERATURE 294K                             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
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       56.98650            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       36.45200            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       36.45200            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       28.49325            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       36.45200            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       36.45200            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       85.47975            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       36.45200            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       36.45200            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       28.49325            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       36.45200            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       36.45200            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       85.47975            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       56.98650            
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A    -2                                                      
REMARK 465     SER A    -1                                                      
REMARK 465     MET A     0                                                      
REMARK 465     VAL A     1                                                      
REMARK 465     GLY A   232                                                      
REMARK 465     MET A   233                                                      
REMARK 465     ASP A   234                                                      
REMARK 465     GLU A   235                                                      
REMARK 465     LEU A   236                                                      
REMARK 465     TYR A   237                                                      
REMARK 465     LYS A   238                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A   3    CD   CE   NZ                                        
REMARK 470     GLU A   5    CD   OE1  OE2                                       
REMARK 470     GLU A   6    CD   OE1  OE2                                       
REMARK 470     LYS A  52    CE   NZ                                             
REMARK 470     LYS A 107    CE   NZ                                             
REMARK 470     LYS A 113    CE   NZ                                             
REMARK 470     LYS A 131    NZ                                                  
REMARK 470     GLU A 132    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 158    NZ                                                  
REMARK 470     LYS A 162    NZ                                                  
REMARK 470     LYS A 166    CD   CE   NZ                                        
REMARK 470     GLU A 172    CG   CD   OE1  OE2                                  
REMARK 470     LEU A 178    CG   CD1  CD2                                       
REMARK 470     GLN A 184    CD   OE1  NE2                                       
REMARK 470     LYS A 206    CE   NZ                                             
REMARK 470     LYS A 214    CD   CE   NZ                                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   HD1  HIS A   204     O    HOH A   373              1.46            
REMARK 500   O    HOH A   459     O    HOH A   539              2.19            
REMARK 500   O    HOH A   386     O    HOH A   416              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   OE1  GLU A   115     HE2  HIS A   204     3555     1.54            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4KW8   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4KW9   RELATED DB: PDB                                   
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 EMERALD GFP HAS LEU AT POSITION 64, THR AT 65, ALA AT 72, LYS AT     
REMARK 999 149, THR AT 153, 167, LEU AT 231. RESIDUES THR 65, TYR 66, GLY 67    
REMARK 999 FORM A CHROMOPHORE CRO 66                                            
DBREF  4KW4 A    2   238  UNP    P42212   GFP_AEQVI        2    238             
SEQADV 4KW4 GLY A   -2  UNP  P42212              EXPRESSION TAG                 
SEQADV 4KW4 SER A   -1  UNP  P42212              EXPRESSION TAG                 
SEQADV 4KW4 MET A    0  UNP  P42212              EXPRESSION TAG                 
SEQADV 4KW4 VAL A    1  UNP  P42212              EXPRESSION TAG                 
SEQADV 4KW4 LEU A   64  UNP  P42212    PHE    64 SEE REMARK 999                 
SEQADV 4KW4 CRO A   66  UNP  P42212    SER    65 CHROMOPHORE, REM 999           
SEQADV 4KW4 CRO A   66  UNP  P42212    TYR    66 CHROMOPHORE                    
SEQADV 4KW4 CRO A   66  UNP  P42212    GLY    67 CHROMOPHORE                    
SEQADV 4KW4 ALA A   72  UNP  P42212    SER    72 SEE REMARK 999                 
SEQADV 4KW4 HIS A  147  UNP  P42212    SER   147 ENGINEERED MUTATION            
SEQADV 4KW4 LYS A  149  UNP  P42212    ASN   149 SEE REMARK 999                 
SEQADV 4KW4 THR A  153  UNP  P42212    MET   153 SEE REMARK 999                 
SEQADV 4KW4 THR A  167  UNP  P42212    ILE   167 SEE REMARK 999                 
SEQADV 4KW4 HIS A  202  UNP  P42212    SER   202 ENGINEERED MUTATION            
SEQADV 4KW4 HIS A  204  UNP  P42212    GLN   204 ENGINEERED MUTATION            
SEQADV 4KW4 LYS A  206  UNP  P42212    ALA   206 ENGINEERED MUTATION            
SEQADV 4KW4 LEU A  231  UNP  P42212    HIS   231 SEE REMARK 999                 
SEQRES   1 A  239  GLY SER MET VAL SER LYS GLY GLU GLU LEU PHE THR GLY          
SEQRES   2 A  239  VAL VAL PRO ILE LEU VAL GLU LEU ASP GLY ASP VAL ASN          
SEQRES   3 A  239  GLY HIS LYS PHE SER VAL SER GLY GLU GLY GLU GLY ASP          
SEQRES   4 A  239  ALA THR TYR GLY LYS LEU THR LEU LYS PHE ILE CYS THR          
SEQRES   5 A  239  THR GLY LYS LEU PRO VAL PRO TRP PRO THR LEU VAL THR          
SEQRES   6 A  239  THR LEU CRO VAL GLN CYS PHE ALA ARG TYR PRO ASP HIS          
SEQRES   7 A  239  MET LYS GLN HIS ASP PHE PHE LYS SER ALA MET PRO GLU          
SEQRES   8 A  239  GLY TYR VAL GLN GLU ARG THR ILE PHE PHE LYS ASP ASP          
SEQRES   9 A  239  GLY ASN TYR LYS THR ARG ALA GLU VAL LYS PHE GLU GLY          
SEQRES  10 A  239  ASP THR LEU VAL ASN ARG ILE GLU LEU LYS GLY ILE ASP          
SEQRES  11 A  239  PHE LYS GLU ASP GLY ASN ILE LEU GLY HIS LYS LEU GLU          
SEQRES  12 A  239  TYR ASN TYR ASN HIS HIS LYS VAL TYR ILE THR ALA ASP          
SEQRES  13 A  239  LYS GLN LYS ASN GLY ILE LYS VAL ASN PHE LYS THR ARG          
SEQRES  14 A  239  HIS ASN ILE GLU ASP GLY SER VAL GLN LEU ALA ASP HIS          
SEQRES  15 A  239  TYR GLN GLN ASN THR PRO ILE GLY ASP GLY PRO VAL LEU          
SEQRES  16 A  239  LEU PRO ASP ASN HIS TYR LEU HIS THR HIS SER LYS LEU          
SEQRES  17 A  239  SER LYS ASP PRO ASN GLU LYS ARG ASP HIS MET VAL LEU          
SEQRES  18 A  239  LEU GLU PHE VAL THR ALA ALA GLY ILE THR LEU GLY MET          
SEQRES  19 A  239  ASP GLU LEU TYR LYS                                          
MODRES 4KW4 CRO A   66  GLY                                                     
MODRES 4KW4 CRO A   66  TYR                                                     
MODRES 4KW4 CRO A   66  GLY                                                     
HET    CRO  A  66      22                                                       
HETNAM     CRO {2-[(1R,2R)-1-AMINO-2-HYDROXYPROPYL]-4-(4-                       
HETNAM   2 CRO  HYDROXYBENZYLIDENE)-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-            
HETNAM   3 CRO  YL}ACETIC ACID                                                  
HETSYN     CRO PEPTIDE DERIVED CHROMOPHORE                                      
FORMUL   1  CRO    C15 H17 N3 O5                                                
FORMUL   2  HOH   *303(H2 O)                                                    
HELIX    1   1 LYS A    3  THR A    9  5                                   7    
HELIX    2   2 PRO A   56  VAL A   61  5                                   6    
HELIX    3   3 VAL A   68  ALA A   72  5                                   5    
HELIX    4   4 PRO A   75  HIS A   81  5                                   7    
HELIX    5   5 ASP A   82  ALA A   87  1                                   6    
HELIX    6   6 LYS A  156  ASN A  159  5                                   4    
SHEET    1   A12 VAL A  11  VAL A  22  0                                        
SHEET    2   A12 HIS A  25  ASP A  36 -1  O  GLY A  31   N  VAL A  16           
SHEET    3   A12 LYS A  41  CYS A  48 -1  O  LYS A  41   N  ASP A  36           
SHEET    4   A12 HIS A 217  ALA A 227 -1  O  LEU A 220   N  LEU A  44           
SHEET    5   A12 HIS A 199  SER A 208 -1  N  HIS A 202   O  THR A 225           
SHEET    6   A12 HIS A 147  ASP A 155 -1  N  ILE A 152   O  HIS A 199           
SHEET    7   A12 GLY A 160  ASN A 170 -1  O  GLY A 160   N  ASP A 155           
SHEET    8   A12 VAL A 176  PRO A 187 -1  O  HIS A 181   N  PHE A 165           
SHEET    9   A12 TYR A  92  PHE A 100 -1  N  GLU A  95   O  GLN A 184           
SHEET   10   A12 ASN A 105  GLU A 115 -1  O  TYR A 106   N  ILE A  98           
SHEET   11   A12 THR A 118  ILE A 128 -1  O  VAL A 120   N  LYS A 113           
SHEET   12   A12 VAL A  11  VAL A  22  1  N  ASP A  21   O  GLY A 127           
LINK         C   LEU A  64                 N1  CRO A  66     1555   1555  1.33  
LINK         C3  CRO A  66                 N   VAL A  68     1555   1555  1.35  
CISPEP   1 MET A   88    PRO A   89          0         6.13                     
CRYST1   72.904   72.904  113.973  90.00  90.00  90.00 P 41 21 2     8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.013717  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013717  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008774        0.00000                         
ATOM      1  N   SER A   2      -5.112  18.146   9.119  1.00 46.40           N  
ANISOU    1  N   SER A   2     4363   4730   8536   -491    249   -795       N  
ATOM      2  CA  SER A   2      -4.513  18.180  10.455  1.00 46.93           C  
ANISOU    2  CA  SER A   2     4424   4709   8699   -465    183   -414       C  
ATOM      3  C   SER A   2      -5.223  19.209  11.341  1.00 47.15           C  
ANISOU    3  C   SER A   2     4560   4948   8406   -524    144   -159       C  
ATOM      4  O   SER A   2      -5.829  20.157  10.842  1.00 47.19           O  
ANISOU    4  O   SER A   2     4682   5166   8083   -548    166   -294       O  
ATOM      5  CB  SER A   2      -3.006  18.498  10.372  1.00 36.38           C  
ANISOU    5  CB  SER A   2     3082   3364   7376   -425    177   -446       C  
ATOM      6  OG  SER A   2      -2.785  19.868  10.093  1.00 25.89           O  
ANISOU    6  OG  SER A   2     1885   2295   5659   -467    181   -526       O  
ATOM      7  HA  SER A   2      -4.613  17.308  10.868  1.00 56.32           H  
ATOM      8  HB2 SER A   2      -2.591  18.279  11.222  1.00 43.65           H  
ATOM      9  HB3 SER A   2      -2.610  17.965   9.665  1.00 43.65           H  
ATOM     10  HG  SER A   2      -1.961  20.024  10.051  1.00 31.07           H  
ATOM     11  N   LYS A   3      -5.149  19.014  12.655  1.00 44.41           N  
ANISOU   11  N   LYS A   3     4182   4579   8113   -524     88    221       N  
ATOM     12  CA  LYS A   3      -5.696  19.981  13.600  1.00 39.63           C  
ANISOU   12  CA  LYS A   3     3696   4231   7131   -554     65    445       C  
ATOM     13  C   LYS A   3      -5.092  21.382  13.346  1.00 22.64           C  
ANISOU   13  C   LYS A   3     1729   2305   4570   -519     81    313       C  
ATOM     14  O   LYS A   3      -5.801  22.379  13.343  1.00 24.47           O  
ANISOU   14  O   LYS A   3     2093   2728   4478   -523    107    265       O  
ATOM     15  CB  LYS A   3      -5.431  19.502  15.036  1.00 42.61           C  
ANISOU   15  CB  LYS A   3     3967   4613   7609   -581      0    873       C  
ATOM     16  CG  LYS A   3      -5.221  20.607  16.054  1.00 40.19           C  
ANISOU   16  CG  LYS A   3     3777   4631   6861   -602    -22   1047       C  
ATOM     17  H   LYS A   3      -4.785  18.328  13.026  1.00 53.29           H  
ATOM     18  HA  LYS A   3      -6.656  20.039  13.474  1.00 47.56           H  
ATOM     19  HB2 LYS A   3      -6.189  18.974  15.329  1.00 51.13           H  
ATOM     20  HB3 LYS A   3      -4.632  18.951  15.034  1.00 51.13           H  
ATOM     21  N   GLY A   4      -3.784  21.447  13.110  1.00 22.73           N  
ANISOU   21  N   GLY A   4     1729   2272   4637   -485     72    254       N  
ATOM     22  CA  GLY A   4      -3.152  22.729  12.830  1.00 21.03           C  
ANISOU   22  CA  GLY A   4     1668   2241   4079   -462     92    133       C  
ATOM     23  C   GLY A   4      -3.779  23.455  11.639  1.00 22.73           C  
ANISOU   23  C   GLY A   4     1985   2552   4100   -457    145   -137       C  
ATOM     24  O   GLY A   4      -3.896  24.685  11.625  1.00 18.50           O  
ANISOU   24  O   GLY A   4     1584   2186   3259   -447    167   -155       O  
ATOM     25  H   GLY A   4      -3.248  20.774  13.106  1.00 27.28           H  
ATOM     26  HA2 GLY A   4      -3.227  23.301  13.610  1.00 25.23           H  
ATOM     27  HA3 GLY A   4      -2.211  22.590  12.642  1.00 25.23           H  
ATOM     28  N   GLU A   5      -4.204  22.678  10.648  1.00 26.98           N  
ANISOU   28  N   GLU A   5     2427   2986   4837   -473    168   -339       N  
ATOM     29  CA  GLU A   5      -4.779  23.224   9.416  1.00 27.97           C  
ANISOU   29  CA  GLU A   5     2596   3256   4774   -489    206   -578       C  
ATOM     30  C   GLU A   5      -6.006  24.083   9.704  1.00 26.00           C  
ANISOU   30  C   GLU A   5     2450   3161   4270   -488    209   -470       C  
ATOM     31  O   GLU A   5      -6.292  25.051   8.993  1.00 22.42           O  
ANISOU   31  O   GLU A   5     2067   2873   3577   -480    229   -546       O  
ATOM     32  CB  GLU A   5      -5.157  22.070   8.479  1.00 39.76           C  
ANISOU   32  CB  GLU A   5     3925   4642   6539   -538    233   -825       C  
ATOM     33  CG  GLU A   5      -5.678  22.501   7.133  1.00 44.07           C  
ANISOU   33  CG  GLU A   5     4465   5407   6873   -583    265  -1079       C  
ATOM     34  H   GLU A   5      -4.172  21.818  10.663  1.00 32.37           H  
ATOM     35  HA  GLU A   5      -4.118  23.776   8.970  1.00 33.56           H  
ATOM     36  HB2 GLU A   5      -4.370  21.524   8.328  1.00 47.71           H  
ATOM     37  HB3 GLU A   5      -5.847  21.538   8.905  1.00 47.71           H  
ATOM     38  HG2 GLU A   5      -6.074  21.735   6.688  1.00 52.88           H  
ATOM     39  HG3 GLU A   5      -6.346  23.192   7.260  1.00 52.88           H  
ATOM     40  N   GLU A   6      -6.744  23.732  10.751  1.00 19.28           N  
ANISOU   40  N   GLU A   6     1582   2259   3484   -497    192   -273       N  
ATOM     41  CA  GLU A   6      -7.976  24.448  11.066  1.00 18.23           C  
ANISOU   41  CA  GLU A   6     1515   2259   3150   -497    207   -193       C  
ATOM     42  C   GLU A   6      -7.686  25.906  11.418  1.00 20.81           C  
ANISOU   42  C   GLU A   6     1977   2727   3202   -460    231   -142       C  
ATOM     43  O   GLU A   6      -8.556  26.781  11.285  1.00 24.77           O  
ANISOU   43  O   GLU A   6     2529   3334   3549   -441    260   -142       O  
ATOM     44  CB  GLU A   6      -8.708  23.737  12.221  1.00 19.06           C  
ANISOU   44  CB  GLU A   6     1556   2308   3377   -531    189     15       C  
ATOM     45  CG  GLU A   6      -8.909  22.242  11.972  1.00 27.45           C  
ANISOU   45  CG  GLU A   6     2461   3170   4800   -572    172    -10       C  
ATOM     46  H   GLU A   6      -6.557  23.089  11.290  1.00 23.13           H  
ATOM     47  HA  GLU A   6      -8.557  24.437  10.289  1.00 21.87           H  
ATOM     48  HB2 GLU A   6      -8.188  23.837  13.034  1.00 22.87           H  
ATOM     49  HB3 GLU A   6      -9.583  24.140  12.336  1.00 22.87           H  
ATOM     50  N   LEU A   7      -6.459  26.181  11.851  1.00 18.92           N  
ANISOU   50  N   LEU A   7     1776   2476   2936   -450    223   -105       N  
ATOM     51  CA  LEU A   7      -6.078  27.546  12.215  1.00 15.87           C  
ANISOU   51  CA  LEU A   7     1498   2198   2332   -431    259    -90       C  
ATOM     52  C   LEU A   7      -5.914  28.481  10.998  1.00 15.26           C  
ANISOU   52  C   LEU A   7     1477   2171   2150   -399    287   -221       C  
ATOM     53  O   LEU A   7      -5.780  29.692  11.166  1.00 18.66           O  
ANISOU   53  O   LEU A   7     1981   2654   2455   -381    328   -209       O  
ATOM     54  CB  LEU A   7      -4.777  27.547  13.019  1.00 15.99           C  
ANISOU   54  CB  LEU A   7     1519   2215   2340   -447    240    -20       C  
ATOM     55  CG  LEU A   7      -4.761  26.694  14.297  1.00 19.60           C  
ANISOU   55  CG  LEU A   7     1890   2682   2876   -493    198    182       C  
ATOM     56  CD1 LEU A   7      -3.339  26.613  14.843  1.00 20.58           C  
ANISOU   56  CD1 LEU A   7     1986   2829   3006   -508    162    258       C  
ATOM     57  CD2 LEU A   7      -5.704  27.238  15.360  1.00 25.52           C  
ANISOU   57  CD2 LEU A   7     2653   3589   3455   -533    232    273       C  
ATOM     58  H   LEU A   7      -5.831  25.600  11.943  1.00 22.70           H  
ATOM     59  HA  LEU A   7      -6.773  27.919  12.780  1.00 19.04           H  
ATOM     60  HB2 LEU A   7      -4.066  27.219  12.446  1.00 19.18           H  
ATOM     61  HB3 LEU A   7      -4.582  28.460  13.280  1.00 19.18           H  
ATOM     62  HG  LEU A   7      -5.047  25.794  14.077  1.00 23.52           H  
ATOM     63 HD11 LEU A   7      -3.341  26.073  15.648  1.00 24.70           H  
ATOM     64 HD12 LEU A   7      -2.767  26.207  14.173  1.00 24.70           H  
ATOM     65 HD13 LEU A   7      -3.028  27.509  15.045  1.00 24.70           H  
ATOM     66 HD21 LEU A   7      -5.658  26.668  16.143  1.00 30.63           H  
ATOM     67 HD22 LEU A   7      -5.433  28.140  15.590  1.00 30.63           H  
ATOM     68 HD23 LEU A   7      -6.607  27.244  15.007  1.00 30.63           H  
ATOM     69  N   PHE A   8      -5.933  27.930   9.787  1.00 15.59           N  
ANISOU   69  N   PHE A   8     1460   2212   2253   -407    270   -343       N  
ATOM     70  CA  PHE A   8      -5.649  28.735   8.587  1.00 15.43           C  
ANISOU   70  CA  PHE A   8     1457   2300   2105   -401    286   -428       C  
ATOM     71  C   PHE A   8      -6.845  28.861   7.651  1.00 17.31           C  
ANISOU   71  C   PHE A   8     1639   2662   2276   -409    284   -450       C  
ATOM     72  O   PHE A   8      -6.705  29.257   6.498  1.00 21.14           O  
ANISOU   72  O   PHE A   8     2086   3293   2652   -428    282   -504       O  
ATOM     73  CB  PHE A   8      -4.455  28.144   7.825  1.00 15.83           C  
ANISOU   73  CB  PHE A   8     1455   2345   2215   -428    276   -577       C  
ATOM     74  CG  PHE A   8      -3.159  28.224   8.591  1.00 15.48           C  
ANISOU   74  CG  PHE A   8     1455   2214   2212   -416    274   -538       C  
ATOM     75  CD1 PHE A   8      -2.281  29.264   8.384  1.00 15.00           C  
ANISOU   75  CD1 PHE A   8     1462   2216   2021   -410    296   -536       C  
ATOM     76  CD2 PHE A   8      -2.843  27.253   9.557  1.00 15.89           C  
ANISOU   76  CD2 PHE A   8     1459   2133   2445   -417    245   -472       C  
ATOM     77  CE1 PHE A   8      -1.068  29.344   9.124  1.00 15.80           C  
ANISOU   77  CE1 PHE A   8     1591   2263   2148   -409    292   -507       C  
ATOM     78  CE2 PHE A   8      -1.654  27.324  10.284  1.00 15.83           C  
ANISOU   78  CE2 PHE A   8     1466   2089   2459   -412    230   -406       C  
ATOM     79  CZ  PHE A   8      -0.772  28.360  10.073  1.00 15.23           C  
ANISOU   79  CZ  PHE A   8     1464   2090   2230   -410    255   -442       C  
ATOM     80  H   PHE A   8      -6.106  27.103   9.627  1.00 18.71           H  
ATOM     81  HA  PHE A   8      -5.402  29.630   8.869  1.00 18.51           H  
ATOM     82  HB2 PHE A   8      -4.634  27.209   7.638  1.00 19.00           H  
ATOM     83  HB3 PHE A   8      -4.341  28.632   6.995  1.00 19.00           H  
ATOM     84  HD1 PHE A   8      -2.480  29.917   7.754  1.00 18.00           H  
ATOM     85  HD2 PHE A   8      -3.432  26.549   9.709  1.00 19.07           H  
ATOM     86  HE1 PHE A   8      -0.475  30.045   8.975  1.00 18.96           H  
ATOM     87  HE2 PHE A   8      -1.457  26.670  10.915  1.00 18.99           H  
ATOM     88  HZ  PHE A   8       0.020  28.404  10.557  1.00 18.27           H  
ATOM     89  N   THR A   9      -8.035  28.552   8.145  1.00 21.85           N  
ANISOU   89  N   THR A   9     2190   3216   2896   -404    281   -390       N  
ATOM     90  CA  THR A   9      -9.191  28.522   7.246  1.00 27.23           C  
ANISOU   90  CA  THR A   9     2790   4034   3522   -422    269   -414       C  
ATOM     91  C   THR A   9      -9.616  29.918   6.795  1.00 28.84           C  
ANISOU   91  C   THR A   9     3015   4359   3584   -377    283   -289       C  
ATOM     92  O   THR A   9     -10.287  30.050   5.783  1.00 27.58           O  
ANISOU   92  O   THR A   9     2765   4378   3339   -398    261   -280       O  
ATOM     93  CB  THR A   9     -10.382  27.805   7.883  1.00 26.11           C  
ANISOU   93  CB  THR A   9     2604   3838   3480   -433    263   -379       C  
ATOM     94  OG1 THR A   9     -10.595  28.317   9.195  1.00 23.82           O  
ANISOU   94  OG1 THR A   9     2391   3469   3192   -393    291   -239       O  
ATOM     95  CG2 THR A   9     -10.106  26.317   7.962  1.00 35.34           C  
ANISOU   95  CG2 THR A   9     3693   4885   4849   -490    245   -496       C  
ATOM     96  H   THR A   9      -8.202  28.361   8.967  1.00 26.22           H  
ATOM     97  HA  THR A   9      -8.945  28.023   6.451  1.00 32.68           H  
ATOM     98  HB  THR A   9     -11.175  27.947   7.344  1.00 31.34           H  
ATOM     99  HG1 THR A   9     -10.754  29.141   9.159  1.00 28.59           H  
ATOM    100 HG21 THR A   9     -10.861  25.861   8.365  1.00 42.41           H  
ATOM    101 HG22 THR A   9      -9.961  25.959   7.072  1.00 42.41           H  
ATOM    102 HG23 THR A   9      -9.315  26.154   8.500  1.00 42.41           H  
ATOM    103  N   GLY A  10      -9.230  30.943   7.545  1.00 23.64           N  
ANISOU  103  N   GLY A  10     2448   3611   2923   -325    324   -189       N  
ATOM    104  CA  GLY A  10      -9.578  32.310   7.199  1.00 25.42           C  
ANISOU  104  CA  GLY A  10     2671   3880   3108   -274    352    -55       C  
ATOM    105  C   GLY A  10      -8.340  33.182   7.076  1.00 26.09           C  
ANISOU  105  C   GLY A  10     2816   3924   3173   -267    379    -35       C  
ATOM    106  O   GLY A  10      -7.225  32.685   6.866  1.00 19.90           O  
ANISOU  106  O   GLY A  10     2058   3149   2355   -308    362   -135       O  
ATOM    107  H   GLY A  10      -8.763  30.871   8.264  1.00 28.37           H  
ATOM    108  HA2 GLY A  10     -10.052  32.322   6.353  1.00 30.51           H  
ATOM    109  HA3 GLY A  10     -10.154  32.684   7.884  1.00 30.51           H  
ATOM    110  N   VAL A  11      -8.536  34.487   7.218  1.00 17.94           N  
ANISOU  110  N   VAL A  11     1789   2828   2198   -215    430     87       N  
ATOM    111  CA  VAL A  11      -7.437  35.444   7.112  1.00 21.14           C  
ANISOU  111  CA  VAL A  11     2238   3170   2624   -213    468    120       C  
ATOM    112  C   VAL A  11      -6.775  35.535   8.492  1.00 22.02           C  
ANISOU  112  C   VAL A  11     2444   3132   2789   -220    524      2       C  
ATOM    113  O   VAL A  11      -7.463  35.711   9.478  1.00 16.51           O  
ANISOU  113  O   VAL A  11     1751   2364   2158   -200    573    -25       O  
ATOM    114  CB  VAL A  11      -7.946  36.824   6.695  1.00 21.80           C  
ANISOU  114  CB  VAL A  11     2253   3210   2821   -158    509    313       C  
ATOM    115  CG1 VAL A  11      -6.808  37.853   6.705  1.00 19.85           C  
ANISOU  115  CG1 VAL A  11     2042   2852   2649   -165    563    343       C  
ATOM    116  CG2 VAL A  11      -8.580  36.774   5.296  1.00 24.91           C  
ANISOU  116  CG2 VAL A  11     2518   3827   3122   -168    437    485       C  
ATOM    117  H   VAL A  11      -9.300  34.848   7.377  1.00 21.52           H  
ATOM    118  HA  VAL A  11      -6.784  35.135   6.465  1.00 25.37           H  
ATOM    119  HB  VAL A  11      -8.623  37.117   7.324  1.00 26.16           H  
ATOM    120 HG11 VAL A  11      -7.161  38.715   6.437  1.00 23.82           H  
ATOM    121 HG12 VAL A  11      -6.441  37.909   7.601  1.00 23.82           H  
ATOM    122 HG13 VAL A  11      -6.121  37.568   6.082  1.00 23.82           H  
ATOM    123 HG21 VAL A  11      -8.893  37.662   5.060  1.00 29.90           H  
ATOM    124 HG22 VAL A  11      -7.913  36.477   4.658  1.00 29.90           H  
ATOM    125 HG23 VAL A  11      -9.326  36.154   5.310  1.00 29.90           H  
ATOM    126  N   VAL A  12      -5.458  35.399   8.539  1.00 15.48           N  
ANISOU  126  N   VAL A  12     1669   2297   1914   -261    518    -73       N  
ATOM    127  CA  VAL A  12      -4.697  35.315   9.779  1.00 16.91           C  
ANISOU  127  CA  VAL A  12     1915   2410   2101   -291    549   -177       C  
ATOM    128  C   VAL A  12      -3.711  36.468   9.818  1.00 15.31           C  
ANISOU  128  C   VAL A  12     1742   2138   1938   -305    609   -192       C  
ATOM    129  O   VAL A  12      -2.975  36.692   8.855  1.00 15.45           O  
ANISOU  129  O   VAL A  12     1753   2189   1928   -317    589   -150       O  
ATOM    130  CB  VAL A  12      -3.885  33.996   9.836  1.00 14.40           C  
ANISOU  130  CB  VAL A  12     1605   2141   1724   -331    480   -246       C  
ATOM    131  CG1 VAL A  12      -3.001  33.951  11.068  1.00 14.23           C  
ANISOU  131  CG1 VAL A  12     1620   2098   1687   -370    496   -299       C  
ATOM    132  CG2 VAL A  12      -4.839  32.773   9.809  1.00 14.82           C  
ANISOU  132  CG2 VAL A  12     1609   2225   1796   -329    428   -241       C  
ATOM    133  H   VAL A  12      -4.963  35.352   7.838  1.00 18.57           H  
ATOM    134  HA  VAL A  12      -5.288  35.367  10.546  1.00 20.30           H  
ATOM    135  HB  VAL A  12      -3.312  33.946   9.055  1.00 17.28           H  
ATOM    136 HG11 VAL A  12      -2.508  33.116  11.073  1.00 17.07           H  
ATOM    137 HG12 VAL A  12      -2.384  34.699  11.041  1.00 17.07           H  
ATOM    138 HG13 VAL A  12      -3.559  34.011  11.859  1.00 17.07           H  
ATOM    139 HG21 VAL A  12      -4.310  31.961   9.845  1.00 17.78           H  
ATOM    140 HG22 VAL A  12      -5.431  32.818  10.576  1.00 17.78           H  
ATOM    141 HG23 VAL A  12      -5.357  32.795   8.989  1.00 17.78           H  
ATOM    142  N   PRO A  13      -3.681  37.219  10.923  1.00 15.72           N  
ANISOU  142  N   PRO A  13     1808   2109   2055   -319    693   -271       N  
ATOM    143  CA  PRO A  13      -2.708  38.298  10.989  1.00 16.25           C  
ANISOU  143  CA  PRO A  13     1889   2094   2191   -349    760   -318       C  
ATOM    144  C   PRO A  13      -1.299  37.756  11.229  1.00 15.61           C  
ANISOU  144  C   PRO A  13     1852   2088   1991   -411    718   -396       C  
ATOM    145  O   PRO A  13      -1.111  36.719  11.876  1.00 15.58           O  
ANISOU  145  O   PRO A  13     1857   2175   1888   -437    663   -434       O  
ATOM    146  CB  PRO A  13      -3.202  39.136  12.186  1.00 17.21           C  
ANISOU  146  CB  PRO A  13     1983   2134   2424   -365    876   -448       C  
ATOM    147  CG  PRO A  13      -4.054  38.273  12.954  1.00 23.20           C  
ANISOU  147  CG  PRO A  13     2731   2995   3089   -369    851   -479       C  
ATOM    148  CD  PRO A  13      -4.620  37.248  12.058  1.00 16.09           C  
ANISOU  148  CD  PRO A  13     1833   2151   2129   -321    746   -337       C  
ATOM    149  HA  PRO A  13      -2.727  38.833  10.180  1.00 19.50           H  
ATOM    150  HB2 PRO A  13      -2.442  39.423  12.715  1.00 20.66           H  
ATOM    151  HB3 PRO A  13      -3.700  39.902  11.860  1.00 20.66           H  
ATOM    152  HG2 PRO A  13      -3.529  37.851  13.652  1.00 27.84           H  
ATOM    153  HG3 PRO A  13      -4.766  38.801  13.347  1.00 27.84           H  
ATOM    154  HD2 PRO A  13      -4.639  36.386  12.501  1.00 19.31           H  
ATOM    155  HD3 PRO A  13      -5.503  37.513  11.758  1.00 19.31           H  
ATOM    156  N   ILE A  14      -0.317  38.474  10.707  1.00 15.91           N  
ANISOU  156  N   ILE A  14     1898   2083   2064   -435    743   -392       N  
ATOM    157  CA  ILE A  14       1.062  38.055  10.753  1.00 15.46           C  
ANISOU  157  CA  ILE A  14     1866   2097   1910   -488    704   -454       C  
ATOM    158  C   ILE A  14       1.929  39.182  11.312  1.00 16.23           C  
ANISOU  158  C   ILE A  14     1968   2127   2074   -551    791   -555       C  
ATOM    159  O   ILE A  14       1.740  40.343  10.960  1.00 17.19           O  
ANISOU  159  O   ILE A  14     2064   2112   2354   -543    871   -523       O  
ATOM    160  CB  ILE A  14       1.584  37.742   9.323  1.00 15.25           C  
ANISOU  160  CB  ILE A  14     1826   2132   1837   -478    647   -368       C  
ATOM    161  CG1 ILE A  14       0.793  36.587   8.710  1.00 14.81           C  
ANISOU  161  CG1 ILE A  14     1742   2164   1723   -440    571   -328       C  
ATOM    162  CG2 ILE A  14       3.084  37.397   9.343  1.00 14.98           C  
ANISOU  162  CG2 ILE A  14     1801   2159   1733   -530    621   -448       C  
ATOM    163  CD1 ILE A  14       1.087  36.367   7.221  1.00 15.12           C  
ANISOU  163  CD1 ILE A  14     1728   2326   1690   -453    533   -280       C  
ATOM    164  H   ILE A  14      -0.434  39.229  10.311  1.00 19.09           H  
ATOM    165  HA  ILE A  14       1.158  37.267  11.311  1.00 18.55           H  
ATOM    166  HB  ILE A  14       1.457  38.529   8.770  1.00 18.30           H  
ATOM    167 HG12 ILE A  14       1.015  35.769   9.182  1.00 17.77           H  
ATOM    168 HG13 ILE A  14      -0.155  36.773   8.802  1.00 17.77           H  
ATOM    169 HG21 ILE A  14       3.377  37.207   8.438  1.00 17.98           H  
ATOM    170 HG22 ILE A  14       3.577  38.153   9.699  1.00 17.98           H  
ATOM    171 HG23 ILE A  14       3.221  36.618   9.905  1.00 17.98           H  
ATOM    172 HD11 ILE A  14       0.553  35.623   6.901  1.00 18.14           H  
ATOM    173 HD12 ILE A  14       0.859  37.173   6.732  1.00 18.14           H  
ATOM    174 HD13 ILE A  14       2.030  36.169   7.112  1.00 18.14           H  
ATOM    175  N   LEU A  15       2.889  38.813  12.151  1.00 16.08           N  
ANISOU  175  N   LEU A  15     1955   2202   1954   -616    774   -664       N  
ATOM    176  CA  LEU A  15       3.971  39.699  12.575  1.00 16.84           C  
ANISOU  176  CA  LEU A  15     2042   2280   2076   -698    841   -783       C  
ATOM    177  C   LEU A  15       5.297  39.050  12.273  1.00 16.30           C  
ANISOU  177  C   LEU A  15     1978   2315   1899   -727    765   -772       C  
ATOM    178  O   LEU A  15       5.497  37.869  12.550  1.00 15.70           O  
ANISOU  178  O   LEU A  15     1891   2353   1723   -715    675   -742       O  
ATOM    179  CB  LEU A  15       3.901  39.970  14.092  1.00 17.71           C  
ANISOU  179  CB  LEU A  15     2115   2475   2138   -782    903   -962       C  
ATOM    180  CG  LEU A  15       2.725  40.790  14.579  1.00 18.74           C  
ANISOU  180  CG  LEU A  15     2211   2504   2406   -776   1015  -1056       C  
ATOM    181  CD1 LEU A  15       2.729  40.816  16.144  1.00 22.96           C  
ANISOU  181  CD1 LEU A  15     2680   3233   2810   -891   1069  -1268       C  
ATOM    182  CD2 LEU A  15       2.784  42.211  14.035  1.00 22.26           C  
ANISOU  182  CD2 LEU A  15     2631   2711   3118   -773   1133  -1096       C  
ATOM    183  H   LEU A  15       2.937  38.029  12.501  1.00 19.30           H  
ATOM    184  HA  LEU A  15       3.915  40.543  12.100  1.00 20.21           H  
ATOM    185  HB2 LEU A  15       3.865  39.116  14.551  1.00 21.25           H  
ATOM    186  HB3 LEU A  15       4.707  40.441  14.354  1.00 21.25           H  
ATOM    187  HG  LEU A  15       1.899  40.380  14.280  1.00 22.49           H  
ATOM    188 HD11 LEU A  15       1.974  41.342  16.453  1.00 27.55           H  
ATOM    189 HD12 LEU A  15       2.656  39.907  16.475  1.00 27.55           H  
ATOM    190 HD13 LEU A  15       3.558  41.214  16.451  1.00 27.55           H  
ATOM    191 HD21 LEU A  15       2.019  42.707  14.365  1.00 26.72           H  
ATOM    192 HD22 LEU A  15       3.606  42.630  14.335  1.00 26.72           H  
ATOM    193 HD23 LEU A  15       2.765  42.179  13.065  1.00 26.72           H  
ATOM    194  N   VAL A  16       6.207  39.826  11.711  1.00 16.74           N  
ANISOU  194  N   VAL A  16     2032   2320   2008   -765    805   -787       N  
ATOM    195  CA  VAL A  16       7.551  39.367  11.418  1.00 16.46           C  
ANISOU  195  CA  VAL A  16     1985   2382   1886   -799    751   -800       C  
ATOM    196  C   VAL A  16       8.562  40.315  12.066  1.00 17.42           C  
ANISOU  196  C   VAL A  16     2085   2505   2029   -903    822   -936       C  
ATOM    197  O   VAL A  16       8.412  41.536  11.998  1.00 18.41           O  
ANISOU  197  O   VAL A  16     2203   2487   2303   -939    926   -979       O  
ATOM    198  CB  VAL A  16       7.799  39.343   9.911  1.00 16.28           C  
ANISOU  198  CB  VAL A  16     1959   2349   1876   -766    730   -689       C  
ATOM    199  CG1 VAL A  16       9.166  38.779   9.593  1.00 16.12           C  
ANISOU  199  CG1 VAL A  16     1909   2440   1775   -799    682   -732       C  
ATOM    200  CG2 VAL A  16       6.693  38.517   9.189  1.00 15.69           C  
ANISOU  200  CG2 VAL A  16     1884   2299   1779   -685    673   -590       C  
ATOM    201  H   VAL A  16       6.066  40.643  11.484  1.00 20.08           H  
ATOM    202  HA  VAL A  16       7.682  38.474  11.774  1.00 19.75           H  
ATOM    203  HB  VAL A  16       7.764  40.251   9.571  1.00 19.53           H  
ATOM    204 HG11 VAL A  16       9.291  38.777   8.631  1.00 19.34           H  
ATOM    205 HG12 VAL A  16       9.842  39.333  10.014  1.00 19.34           H  
ATOM    206 HG13 VAL A  16       9.220  37.873   9.935  1.00 19.34           H  
ATOM    207 HG21 VAL A  16       6.872  38.516   8.236  1.00 18.83           H  
ATOM    208 HG22 VAL A  16       6.706  37.608   9.529  1.00 18.83           H  
ATOM    209 HG23 VAL A  16       5.831  38.924   9.364  1.00 18.83           H  
ATOM    210  N   GLU A  17       9.595  39.732  12.671  1.00 18.42           N  
ANISOU  210  N   GLU A  17     2178   2785   2035   -954    767   -995       N  
ATOM    211  CA  GLU A  17      10.673  40.491  13.276  1.00 18.40           C  
ANISOU  211  CA  GLU A  17     2136   2837   2018  -1069    821  -1137       C  
ATOM    212  C   GLU A  17      11.973  39.835  12.881  1.00 18.08           C  
ANISOU  212  C   GLU A  17     2063   2908   1900  -1076    743  -1100       C  
ATOM    213  O   GLU A  17      12.101  38.609  12.958  1.00 17.55           O  
ANISOU  213  O   GLU A  17     1966   2939   1764  -1021    641  -1020       O  
ATOM    214  CB  GLU A  17      10.509  40.475  14.785  1.00 19.23           C  
ANISOU  214  CB  GLU A  17     2186   3098   2024  -1150    829  -1259       C  
ATOM    215  CG  GLU A  17       9.211  41.107  15.230  1.00 22.51           C  
ANISOU  215  CG  GLU A  17     2608   3413   2534  -1145    914  -1327       C  
ATOM    216  CD  GLU A  17       9.212  42.599  15.067  1.00 27.80           C  
ANISOU  216  CD  GLU A  17     3263   3887   3413  -1201   1065  -1473       C  
ATOM    217  OE1 GLU A  17      10.301  43.186  14.850  1.00 23.48           O  
ANISOU  217  OE1 GLU A  17     2690   3321   2912  -1267   1100  -1529       O  
ATOM    218  OE2 GLU A  17       8.115  43.179  15.199  1.00 38.66           O  
ANISOU  218  OE2 GLU A  17     4633   5120   4935  -1177   1156  -1532       O  
ATOM    219  H   GLU A  17       9.691  38.881  12.742  1.00 22.11           H  
ATOM    220  HA  GLU A  17      10.663  41.408  12.959  1.00 22.08           H  
ATOM    221  HB2 GLU A  17      10.519  39.556  15.095  1.00 23.08           H  
ATOM    222  HB3 GLU A  17      11.239  40.971  15.188  1.00 23.08           H  
ATOM    223  HG2 GLU A  17       8.485  40.747  14.698  1.00 27.02           H  
ATOM    224  HG3 GLU A  17       9.067  40.907  16.168  1.00 27.02           H  
ATOM    225  N  ALEU A  18      12.929  40.652  12.460  0.40 18.70           N  
ANISOU  225  N  ALEU A  18     2127   2953   2024  -1144    798  -1157       N  
ATOM    226  N  BLEU A  18      12.935  40.641  12.445  0.60 18.69           N  
ANISOU  226  N  BLEU A  18     2126   2952   2022  -1143    797  -1155       N  
ATOM    227  CA ALEU A  18      14.222  40.167  12.025  0.40 18.61           C  
ANISOU  227  CA ALEU A  18     2071   3046   1953  -1157    741  -1143       C  
ATOM    228  CA BLEU A  18      14.225  40.145  11.992  0.60 18.58           C  
ANISOU  228  CA BLEU A  18     2068   3043   1950  -1155    740  -1139       C  
ATOM    229  C  ALEU A  18      15.316  41.042  12.588  0.40 19.78           C  
ANISOU  229  C  ALEU A  18     2169   3253   2092  -1289    798  -1283       C  
ATOM    230  C  BLEU A  18      15.329  41.026  12.541  0.60 19.75           C  
ANISOU  230  C  BLEU A  18     2166   3248   2090  -1287    797  -1278       C  
ATOM    231  O  ALEU A  18      15.244  42.259  12.489  0.40 20.65           O  
ANISOU  231  O  ALEU A  18     2292   3230   2323  -1358    908  -1357       O  
ATOM    232  O  BLEU A  18      15.263  42.236  12.404  0.60 20.60           O  
ANISOU  232  O  BLEU A  18     2287   3221   2318  -1353    905  -1347       O  
ATOM    233  CB ALEU A  18      14.305  40.200  10.500  0.40 18.24           C  
ANISOU  233  CB ALEU A  18     2044   2928   1958  -1108    749  -1044       C  
ATOM    234  CB BLEU A  18      14.287  40.165  10.455  0.60 18.20           C  
ANISOU  234  CB BLEU A  18     2040   2924   1953  -1104    747  -1039       C  
ATOM    235  CG ALEU A  18      15.643  39.742   9.921  0.40 18.36           C  
ANISOU  235  CG ALEU A  18     1994   3058   1922  -1127    712  -1060       C  
ATOM    236  CG BLEU A  18      15.672  39.985   9.820  0.60 18.48           C  
ANISOU  236  CG BLEU A  18     2015   3059   1949  -1141    729  -1059       C  
ATOM    237  CD1ALEU A  18      15.381  39.130   8.572  0.40 17.93           C  
ANISOU  237  CD1ALEU A  18     1931   3023   1858  -1058    688   -983       C  
ATOM    238  CD1BLEU A  18      16.228  38.592  10.049  0.60 18.11           C  
ANISOU  238  CD1BLEU A  18     1899   3134   1847  -1085    629  -1070       C  
ATOM    239  CD2ALEU A  18      16.666  40.884   9.791  0.40 19.38           C  
ANISOU  239  CD2ALEU A  18     2099   3180   2083  -1242    789  -1119       C  
ATOM    240  CD2BLEU A  18      15.630  40.302   8.321  0.60 18.63           C  
ANISOU  240  CD2BLEU A  18     2034   3059   1987  -1133    763   -965       C  
ATOM    241  H  ALEU A  18      12.847  41.507  12.417  0.40 22.44           H  
ATOM    242  H  BLEU A  18      12.861  41.497  12.402  0.60 22.42           H  
ATOM    243  HA ALEU A  18      14.355  39.256  12.331  0.40 22.33           H  
ATOM    244  HA BLEU A  18      14.360  39.236  12.303  0.60 22.30           H  
ATOM    245  HB2ALEU A  18      13.617  39.619  10.140  0.40 21.89           H  
ATOM    246  HB2BLEU A  18      13.722  39.451  10.120  0.60 21.84           H  
ATOM    247  HB3ALEU A  18      14.153  41.110  10.201  0.40 21.89           H  
ATOM    248  HB3BLEU A  18      13.940  41.018  10.149  0.60 21.84           H  
ATOM    249  HG ALEU A  18      16.023  39.059  10.495  0.40 22.03           H  
ATOM    250  HG BLEU A  18      16.283  40.614  10.233  0.60 22.18           H  
ATOM    251 HD11ALEU A  18      16.222  38.834   8.191  0.40 21.52           H  
ATOM    252 HD11BLEU A  18      17.101  38.529   9.630  0.60 21.73           H  
ATOM    253 HD12ALEU A  18      14.782  38.375   8.680  0.40 21.52           H  
ATOM    254 HD12BLEU A  18      16.307  38.437  11.003  0.60 21.73           H  
ATOM    255 HD13ALEU A  18      14.973  39.797   7.998  0.40 21.52           H  
ATOM    256 HD13BLEU A  18      15.625  37.943   9.656  0.60 21.73           H  
ATOM    257 HD21ALEU A  18      17.489  40.529   9.420  0.40 23.25           H  
ATOM    258 HD21BLEU A  18      16.516  40.180   7.948  0.60 22.36           H  
ATOM    259 HD22ALEU A  18      16.305  41.566   9.204  0.40 23.25           H  
ATOM    260 HD22BLEU A  18      15.002  39.701   7.889  0.60 22.36           H  
ATOM    261 HD23ALEU A  18      16.834  41.258  10.670  0.40 23.25           H  
ATOM    262 HD23BLEU A  18      15.344  41.221   8.202  0.60 22.36           H  
ATOM    263  N   ASP A  19      16.329  40.408  13.170  1.00 20.05           N  
ANISOU  263  N   ASP A  19     2122   3475   2020  -1314    725  -1292       N  
ATOM    264  CA  ASP A  19      17.578  41.091  13.554  1.00 21.22           C  
ANISOU  264  CA  ASP A  19     2203   3710   2148  -1398    770  -1372       C  
ATOM    265  C   ASP A  19      18.665  40.532  12.666  1.00 22.77           C  
ANISOU  265  C   ASP A  19     2368   3957   2327  -1375    714  -1328       C  
ATOM    266  O   ASP A  19      18.895  39.309  12.651  1.00 20.44           O  
ANISOU  266  O   ASP A  19     2017   3759   1992  -1316    608  -1261       O  
ATOM    267  CB  ASP A  19      17.976  40.790  15.003  1.00 22.21           C  
ANISOU  267  CB  ASP A  19     2228   4069   2144  -1450    729  -1396       C  
ATOM    268  CG  ASP A  19      17.168  41.573  16.016  1.00 35.56           C  
ANISOU  268  CG  ASP A  19     3896   5766   3849  -1514    812  -1494       C  
ATOM    269  OD1 ASP A  19      16.575  42.613  15.638  1.00 23.46           O  
ANISOU  269  OD1 ASP A  19     2422   4028   2464  -1523    927  -1578       O  
ATOM    270  OD2 ASP A  19      17.155  41.154  17.202  1.00 36.38           O  
ANISOU  270  OD2 ASP A  19     3904   6100   3817  -1565    767  -1490       O  
ATOM    271  H  AASP A  19      16.323  39.569  13.359  0.40 24.06           H  
ATOM    272  H  BASP A  19      16.311  39.577  13.392  0.60 24.06           H  
ATOM    273  HA  ASP A  19      17.504  42.049  13.423  1.00 25.46           H  
ATOM    274  HB2 ASP A  19      17.839  39.845  15.177  1.00 26.66           H  
ATOM    275  HB3 ASP A  19      18.911  41.017  15.126  1.00 26.66           H  
ATOM    276  N   GLY A  20      19.329  41.417  11.925  1.00 25.73           N  
ANISOU  276  N   GLY A  20     2760   4260   2757  -1424    787  -1370       N  
ATOM    277  CA  GLY A  20      20.388  41.017  11.017  1.00 23.03           C  
ANISOU  277  CA  GLY A  20     2372   3981   2398  -1413    752  -1342       C  
ATOM    278  C   GLY A  20      21.732  41.678  11.300  1.00 23.54           C  
ANISOU  278  C   GLY A  20     2391   4121   2431  -1485    784  -1418       C  
ATOM    279  O   GLY A  20      21.810  42.748  11.938  1.00 23.72           O  
ANISOU  279  O   GLY A  20     2429   4102   2482  -1558    864  -1507       O  
ATOM    280  H   GLY A  20      19.179  42.264  11.933  1.00 30.88           H  
ATOM    281  HA2 GLY A  20      20.507  40.056  11.073  1.00 27.64           H  
ATOM    282  HA3 GLY A  20      20.128  41.238  10.109  1.00 27.64           H  
ATOM    283  N   ASP A  21      22.780  41.008  10.820  1.00 22.63           N  
ANISOU  283  N   ASP A  21     2204   4117   2278  -1460    730  -1402       N  
ATOM    284  CA  ASP A  21      24.172  41.428  10.912  1.00 23.74           C  
ANISOU  284  CA  ASP A  21     2287   4350   2383  -1518    744  -1462       C  
ATOM    285  C   ASP A  21      24.884  40.835   9.680  1.00 23.60           C  
ANISOU  285  C   ASP A  21     2218   4373   2374  -1479    717  -1435       C  
ATOM    286  O   ASP A  21      25.142  39.633   9.632  1.00 23.34           O  
ANISOU  286  O   ASP A  21     2102   4419   2347  -1396    643  -1415       O  
ATOM    287  CB  ASP A  21      24.816  40.878  12.192  1.00 24.43           C  
ANISOU  287  CB  ASP A  21     2280   4621   2381  -1521    676  -1474       C  
ATOM    288  CG  ASP A  21      26.275  41.282  12.348  1.00 39.60           C  
ANISOU  288  CG  ASP A  21     4130   6660   4255  -1586    687  -1537       C  
ATOM    289  OD1 ASP A  21      26.914  41.624  11.335  1.00 35.23           O  
ANISOU  289  OD1 ASP A  21     3583   6060   3742  -1602    723  -1557       O  
ATOM    290  OD2 ASP A  21      26.793  41.252  13.496  1.00 38.18           O  
ANISOU  290  OD2 ASP A  21     3876   6650   3982  -1630    656  -1561       O  
ATOM    291  H   ASP A  21      22.696  40.256  10.410  1.00 27.16           H  
ATOM    292  HA  ASP A  21      24.242  42.395  10.898  1.00 28.49           H  
ATOM    293  HB2 ASP A  21      24.329  41.215  12.960  1.00 29.32           H  
ATOM    294  HB3 ASP A  21      24.775  39.909  12.174  1.00 29.32           H  
ATOM    295  N   VAL A  22      25.170  41.670   8.687  1.00 24.07           N  
ANISOU  295  N   VAL A  22     2309   4378   2459  -1538    779  -1429       N  
ATOM    296  CA  VAL A  22      25.845  41.220   7.455  1.00 24.30           C  
ANISOU  296  CA  VAL A  22     2279   4490   2465  -1519    767  -1417       C  
ATOM    297  C   VAL A  22      27.187  41.932   7.335  1.00 25.57           C  
ANISOU  297  C   VAL A  22     2397   4714   2605  -1602    799  -1461       C  
ATOM    298  O   VAL A  22      27.246  43.156   7.313  1.00 26.35           O  
ANISOU  298  O   VAL A  22     2538   4723   2751  -1694    865  -1439       O  
ATOM    299  CB  VAL A  22      24.972  41.484   6.207  1.00 24.09           C  
ANISOU  299  CB  VAL A  22     2295   4410   2448  -1520    799  -1317       C  
ATOM    300  CG1 VAL A  22      25.709  41.086   4.917  1.00 24.79           C  
ANISOU  300  CG1 VAL A  22     2306   4643   2470  -1520    791  -1326       C  
ATOM    301  CG2 VAL A  22      23.638  40.702   6.308  1.00 22.89           C  
ANISOU  301  CG2 VAL A  22     2177   4207   2312  -1434    767  -1285       C  
ATOM    302  H   VAL A  22      24.985  42.510   8.695  1.00 28.88           H  
ATOM    303  HA  VAL A  22      26.011  40.267   7.512  1.00 29.16           H  
ATOM    304  HB  VAL A  22      24.765  42.430   6.157  1.00 28.91           H  
ATOM    305 HG11 VAL A  22      25.133  41.264   4.157  1.00 29.75           H  
ATOM    306 HG12 VAL A  22      26.524  41.608   4.845  1.00 29.75           H  
ATOM    307 HG13 VAL A  22      25.924  40.141   4.955  1.00 29.75           H  
ATOM    308 HG21 VAL A  22      23.107  40.881   5.516  1.00 27.46           H  
ATOM    309 HG22 VAL A  22      23.832  39.754   6.369  1.00 27.46           H  
ATOM    310 HG23 VAL A  22      23.161  40.994   7.100  1.00 27.46           H  
ATOM    311  N   ASN A  23      28.262  41.154   7.282  1.00 26.93           N  
ANISOU  311  N   ASN A  23     2468   5022   2741  -1566    758  -1520       N  
ATOM    312  CA  ASN A  23      29.615  41.710   7.332  1.00 27.26           C  
ANISOU  312  CA  ASN A  23     2455   5145   2756  -1641    780  -1572       C  
ATOM    313  C   ASN A  23      29.732  42.771   8.448  1.00 27.89           C  
ANISOU  313  C   ASN A  23     2577   5176   2844  -1730    819  -1607       C  
ATOM    314  O   ASN A  23      30.338  43.849   8.274  1.00 29.03           O  
ANISOU  314  O   ASN A  23     2728   5288   3014  -1832    881  -1630       O  
ATOM    315  CB  ASN A  23      30.008  42.268   5.970  1.00 28.02           C  
ANISOU  315  CB  ASN A  23     2546   5266   2836  -1704    827  -1538       C  
ATOM    316  CG  ASN A  23      30.533  41.189   5.033  1.00 28.25           C  
ANISOU  316  CG  ASN A  23     2479   5432   2824  -1639    797  -1592       C  
ATOM    317  OD1 ASN A  23      30.050  40.054   5.031  1.00 27.55           O  
ANISOU  317  OD1 ASN A  23     2357   5347   2764  -1533    755  -1628       O  
ATOM    318  ND2 ASN A  23      31.529  41.538   4.239  1.00 29.50           N  
ANISOU  318  ND2 ASN A  23     2579   5695   2934  -1704    825  -1612       N  
ATOM    319  H   ASN A  23      28.238  40.297   7.216  1.00 32.31           H  
ATOM    320  HA  ASN A  23      30.235  40.994   7.544  1.00 32.71           H  
ATOM    321  HB2 ASN A  23      29.229  42.674   5.557  1.00 33.63           H  
ATOM    322  HB3 ASN A  23      30.706  42.931   6.087  1.00 33.63           H  
ATOM    323 HD21 ASN A  23      31.844  42.338   4.270  1.00 35.40           H  
ATOM    324 HD22 ASN A  23      31.862  40.966   3.690  1.00 35.40           H  
ATOM    325  N   GLY A  24      29.097  42.483   9.582  1.00 27.51           N  
ANISOU  325  N   GLY A  24     2545   5123   2782  -1697    789  -1616       N  
ATOM    326  CA  GLY A  24      29.210  43.362  10.738  1.00 32.99           C  
ANISOU  326  CA  GLY A  24     3252   5824   3459  -1780    833  -1694       C  
ATOM    327  C   GLY A  24      28.265  44.546  10.706  1.00 30.46           C  
ANISOU  327  C   GLY A  24     3028   5300   3244  -1840    928  -1717       C  
ATOM    328  O   GLY A  24      28.157  45.283  11.696  1.00 30.72           O  
ANISOU  328  O   GLY A  24     3062   5320   3291  -1903    987  -1822       O  
ATOM    329  H   GLY A  24      28.601  41.792   9.705  1.00 33.01           H  
ATOM    330  HA2 GLY A  24      29.028  42.852  11.543  1.00 39.59           H  
ATOM    331  HA3 GLY A  24      30.117  43.701  10.793  1.00 39.59           H  
ATOM    332  N   HIS A  25      27.570  44.735   9.590  1.00 29.38           N  
ANISOU  332  N   HIS A  25     3216   4428   3520  -2027    483  -1240       N  
ATOM    333  CA  HIS A  25      26.552  45.773   9.495  1.00 28.77           C  
ANISOU  333  CA  HIS A  25     3351   4260   3320  -2066    583  -1214       C  
ATOM    334  C   HIS A  25      25.234  45.263  10.100  1.00 27.15           C  
ANISOU  334  C   HIS A  25     3211   4013   3094  -1960    520  -1143       C  
ATOM    335  O   HIS A  25      24.585  44.388   9.549  1.00 25.88           O  
ANISOU  335  O   HIS A  25     3017   3849   2967  -1855    506  -1105       O  
ATOM    336  CB  HIS A  25      26.302  46.188   8.047  1.00 28.61           C  
ANISOU  336  CB  HIS A  25     3417   4196   3257  -2092    722  -1224       C  
ATOM    337  CG  HIS A  25      27.519  46.678   7.336  1.00 30.28           C  
ANISOU  337  CG  HIS A  25     3582   4451   3474  -2207    806  -1301       C  
ATOM    338  ND1 HIS A  25      28.076  47.913   7.587  1.00 35.79           N  
ANISOU  338  ND1 HIS A  25     4364   5122   4113  -2346    867  -1340       N  
ATOM    339  CD2 HIS A  25      28.274  46.110   6.363  1.00 30.87           C  
ANISOU  339  CD2 HIS A  25     3537   4591   3603  -2211    850  -1356       C  
ATOM    340  CE1 HIS A  25      29.132  48.082   6.810  1.00 42.62           C  
ANISOU  340  CE1 HIS A  25     5162   6040   4993  -2435    941  -1412       C  
ATOM    341  NE2 HIS A  25      29.275  47.003   6.059  1.00 34.90           N  
ANISOU  341  NE2 HIS A  25     4058   5119   4083  -2356    937  -1428       N  
ATOM    342  H   HIS A  25      27.669  44.273   8.871  1.00 35.26           H  
ATOM    343  HA  HIS A  25      26.839  46.554   9.994  1.00 34.52           H  
ATOM    344  HB2 HIS A  25      25.962  45.422   7.558  1.00 34.33           H  
ATOM    345  HB3 HIS A  25      25.645  46.902   8.036  1.00 34.33           H  
ATOM    346  HD1 HIS A  25      27.786  48.482   8.164  1.00 42.95           H  
ATOM    347  HD2 HIS A  25      28.146  45.272   5.981  1.00 37.05           H  
ATOM    348  HE1 HIS A  25      29.681  48.833   6.794  1.00 51.15           H  
ATOM    349  HE2 HIS A  25      29.893  46.881   5.473  1.00 41.88           H  
ATOM    350  N   LYS A  26      24.849  45.846  11.230  1.00 27.39           N  
ANISOU  350  N   LYS A  26     3336   4012   3061  -1999    493  -1134       N  
ATOM    351  CA  LYS A  26      23.652  45.441  11.956  1.00 26.21           C  
ANISOU  351  CA  LYS A  26     3251   3829   2880  -1921    445  -1082       C  
ATOM    352  C   LYS A  26      22.402  46.213  11.514  1.00 25.48           C  
ANISOU  352  C   LYS A  26     3334   3618   2730  -1909    559  -1063       C  
ATOM    353  O   LYS A  26      22.479  47.365  11.091  1.00 27.28           O  
ANISOU  353  O   LYS A  26     3673   3771   2920  -1988    662  -1088       O  
ATOM    354  CB  LYS A  26      23.922  45.629  13.453  1.00 27.17           C  
ANISOU  354  CB  LYS A  26     3384   3983   2956  -1982    361  -1093       C  
ATOM    355  CG  LYS A  26      24.968  44.640  13.962  1.00 28.27           C  
ANISOU  355  CG  LYS A  26     3346   4221   3176  -1969    202  -1086       C  
ATOM    356  CD  LYS A  26      25.160  44.707  15.475  1.00 36.46           C  
ANISOU  356  CD  LYS A  26     4405   5295   4153  -2034     94  -1083       C  
ATOM    357  CE  LYS A  26      26.159  43.651  15.960  1.00 42.25           C  
ANISOU  357  CE  LYS A  26     4960   6105   4989  -2010    -96  -1059       C  
ATOM    358  NZ  LYS A  26      25.634  42.256  15.819  1.00 46.52           N  
ANISOU  358  NZ  LYS A  26     5422   6647   5607  -1873   -194   -989       N  
ATOM    359  H   LYS A  26      25.275  46.493  11.604  1.00 32.87           H  
ATOM    360  HA  LYS A  26      23.492  44.498  11.797  1.00 31.46           H  
ATOM    361  HB2 LYS A  26      24.252  46.528  13.609  1.00 32.61           H  
ATOM    362  HB3 LYS A  26      23.100  45.483  13.947  1.00 32.61           H  
ATOM    363  HG2 LYS A  26      24.688  43.740  13.735  1.00 33.93           H  
ATOM    364  HG3 LYS A  26      25.820  44.839  13.543  1.00 33.93           H  
ATOM    365  HD2 LYS A  26      25.502  45.582  15.716  1.00 43.75           H  
ATOM    366  HD3 LYS A  26      24.310  44.545  15.913  1.00 43.75           H  
ATOM    367  HE2 LYS A  26      26.973  43.721  15.437  1.00 50.70           H  
ATOM    368  HE3 LYS A  26      26.352  43.806  16.898  1.00 50.70           H  
ATOM    369  HZ1 LYS A  26      25.454  42.084  14.965  1.00 55.83           H  
ATOM    370  HZ2 LYS A  26      26.240  41.673  16.110  1.00 55.83           H  
ATOM    371  HZ3 LYS A  26      24.889  42.162  16.296  1.00 55.83           H  
ATOM    372  N   PHE A  27      21.248  45.574  11.604  1.00 24.15           N  
ANISOU  372  N   PHE A  27     3187   3420   2567  -1808    535  -1017       N  
ATOM    373  CA  PHE A  27      19.993  46.208  11.226  1.00 23.58           C  
ANISOU  373  CA  PHE A  27     3265   3225   2472  -1780    623   -998       C  
ATOM    374  C   PHE A  27      18.834  45.410  11.779  1.00 22.42           C  
ANISOU  374  C   PHE A  27     3116   3071   2331  -1682    575   -963       C  
ATOM    375  O   PHE A  27      19.016  44.282  12.215  1.00 21.91           O  
ANISOU  375  O   PHE A  27     2939   3100   2287  -1632    474   -941       O  
ATOM    376  CB  PHE A  27      19.845  46.285   9.709  1.00 23.20           C  
ANISOU  376  CB  PHE A  27     3239   3128   2446  -1760    686   -975       C  
ATOM    377  CG  PHE A  27      19.807  44.949   9.013  1.00 22.07           C  
ANISOU  377  CG  PHE A  27     2967   3062   2356  -1669    630   -946       C  
ATOM    378  CD1 PHE A  27      20.973  44.331   8.612  1.00 22.80           C  
ANISOU  378  CD1 PHE A  27     2917   3257   2489  -1681    600   -973       C  
ATOM    379  CD2 PHE A  27      18.598  44.343   8.710  1.00 21.48           C  
ANISOU  379  CD2 PHE A  27     2913   2948   2302  -1572    616   -901       C  
ATOM    380  CE1 PHE A  27      20.946  43.118   7.937  1.00 23.27           C  
ANISOU  380  CE1 PHE A  27     2860   3374   2610  -1593    560   -958       C  
ATOM    381  CE2 PHE A  27      18.560  43.124   8.028  1.00 24.37           C  
ANISOU  381  CE2 PHE A  27     3163   3381   2717  -1492    571   -880       C  
ATOM    382  CZ  PHE A  27      19.743  42.520   7.641  1.00 20.65           C  
ANISOU  382  CZ  PHE A  27     2555   3006   2286  -1501    546   -910       C  
ATOM    383  H   PHE A  27      21.161  44.765  11.884  1.00 28.98           H  
ATOM    384  HA  PHE A  27      19.956  47.106  11.589  1.00 28.30           H  
ATOM    385  HB2 PHE A  27      19.018  46.747   9.502  1.00 27.84           H  
ATOM    386  HB3 PHE A  27      20.596  46.782   9.349  1.00 27.84           H  
ATOM    387  HD1 PHE A  27      21.790  44.732   8.799  1.00 27.36           H  
ATOM    388  HD2 PHE A  27      17.803  44.754   8.961  1.00 25.78           H  
ATOM    389  HE1 PHE A  27      21.743  42.711   7.681  1.00 27.93           H  
ATOM    390  HE2 PHE A  27      17.744  42.721   7.837  1.00 29.25           H  
ATOM    391  HZ  PHE A  27      19.725  41.702   7.199  1.00 24.79           H  
ATOM    392  N  ASER A  28      17.643  45.990  11.730  0.82 22.17           N  
ANISOU  392  N  ASER A  28     3210   2919   2293  -1651    645   -958       N  
ATOM    393  N  BSER A  28      17.648  46.013  11.769  0.18 22.20           N  
ANISOU  393  N  BSER A  28     3216   2923   2296  -1654    645   -960       N  
ATOM    394  CA ASER A  28      16.441  45.310  12.186  0.82 21.21           C  
ANISOU  394  CA ASER A  28     3092   2783   2182  -1562    620   -938       C  
ATOM    395  CA BSER A  28      16.428  45.347  12.211  0.18 21.24           C  
ANISOU  395  CA BSER A  28     3101   2784   2185  -1564    622   -939       C  
ATOM    396  C  ASER A  28      15.275  45.664  11.284  0.82 20.70           C  
ANISOU  396  C  ASER A  28     3117   2583   2165  -1493    685   -918       C  
ATOM    397  C  BSER A  28      15.284  45.664  11.257  0.18 20.69           C  
ANISOU  397  C  BSER A  28     3116   2582   2165  -1493    685   -918       C  
ATOM    398  O  ASER A  28      15.159  46.804  10.825  0.82 21.51           O  
ANISOU  398  O  ASER A  28     3334   2560   2278  -1526    760   -928       O  
ATOM    399  O  BSER A  28      15.191  46.774  10.732  0.18 21.47           O  
ANISOU  399  O  BSER A  28     3326   2557   2274  -1525    758   -925       O  
ATOM    400  CB ASER A  28      16.121  45.683  13.649  0.82 21.97           C  
ANISOU  400  CB ASER A  28     3249   2877   2222  -1606    632   -977       C  
ATOM    401  CB BSER A  28      16.045  45.782  13.633  0.18 22.01           C  
ANISOU  401  CB BSER A  28     3266   2869   2228  -1606    642   -980       C  
ATOM    402  OG ASER A  28      15.198  44.766  14.202  0.82 21.17           O  
ANISOU  402  OG ASER A  28     3122   2806   2116  -1537    593   -958       O  
ATOM    403  OG BSER A  28      17.085  45.514  14.557  0.18 22.75           O  
ANISOU  403  OG BSER A  28     3297   3079   2267  -1683    567   -990       O  
ATOM    404  H  ASER A  28      17.503  46.785  11.433  0.82 26.60           H  
ATOM    405  H  BSER A  28      17.524  46.822  11.506  0.18 26.64           H  
ATOM    406  HA ASER A  28      16.580  44.351  12.140  0.82 25.45           H  
ATOM    407  HA BSER A  28      16.567  44.387  12.213  0.18 25.49           H  
ATOM    408  HB2ASER A  28      16.940  45.661  14.168  0.82 26.37           H  
ATOM    409  HB2BSER A  28      15.865  46.735  13.631  0.18 26.41           H  
ATOM    410  HB3ASER A  28      15.736  46.573  13.672  0.82 26.37           H  
ATOM    411  HB3BSER A  28      15.251  45.297  13.906  0.18 26.41           H  
ATOM    412  HG ASER A  28      15.028  44.974  14.998  0.82 25.41           H  
ATOM    413  HG BSER A  28      17.251  44.691  14.572  0.18 27.30           H  
ATOM    414  N   VAL A  29      14.426  44.674  11.042  1.00 19.52           N  
ANISOU  414  N   VAL A  29     2918   2450   2050  -1396    645   -887       N  
ATOM    415  CA  VAL A  29      13.241  44.814  10.196  1.00 19.05           C  
ANISOU  415  CA  VAL A  29     2928   2265   2046  -1317    682   -865       C  
ATOM    416  C   VAL A  29      11.997  44.299  10.926  1.00 23.06           C  
ANISOU  416  C   VAL A  29     3433   2755   2575  -1231    680   -882       C  
ATOM    417  O   VAL A  29      12.042  43.252  11.567  1.00 18.14           O  
ANISOU  417  O   VAL A  29     2718   2251   1923  -1217    616   -875       O  
ATOM    418  CB  VAL A  29      13.373  43.977   8.900  1.00 18.16           C  
ANISOU  418  CB  VAL A  29     2743   2199   1959  -1282    640   -815       C  
ATOM    419  CG1 VAL A  29      12.055  43.993   8.093  1.00 17.75           C  
ANISOU  419  CG1 VAL A  29     2763   2019   1962  -1197    655   -785       C  
ATOM    420  CG2 VAL A  29      14.504  44.488   8.082  1.00 18.84           C  
ANISOU  420  CG2 VAL A  29     2836   2303   2020  -1369    665   -807       C  
ATOM    421  H  AVAL A  29      14.516  43.883  11.367  0.82 23.43           H  
ATOM    422  H  BVAL A  29      14.509  43.889  11.384  0.18 23.43           H  
ATOM    423  HA  VAL A  29      13.108  45.745   9.960  1.00 22.87           H  
ATOM    424  HB  VAL A  29      13.567  43.057   9.137  1.00 21.80           H  
ATOM    425 HG11 VAL A  29      12.170  43.461   7.290  1.00 21.30           H  
ATOM    426 HG12 VAL A  29      11.346  43.618   8.640  1.00 21.30           H  
ATOM    427 HG13 VAL A  29      11.841  44.909   7.856  1.00 21.30           H  
ATOM    428 HG21 VAL A  29      14.575  43.955   7.274  1.00 22.61           H  
ATOM    429 HG22 VAL A  29      14.335  45.415   7.853  1.00 22.61           H  
ATOM    430 HG23 VAL A  29      15.323  44.417   8.598  1.00 22.61           H  
ATOM    431  N   SER A  30      10.906  45.048  10.828  1.00 18.99           N  
ANISOU  431  N   SER A  30     3018   2082   2116  -1171    749   -903       N  
ATOM    432  CA ASER A  30       9.620  44.614  11.366  0.69 18.82           C  
ANISOU  432  CA ASER A  30     2985   2033   2134  -1074    769   -930       C  
ATOM    433  CA CSER A  30       9.611  44.640  11.370  0.31 20.13           C  
ANISOU  433  CA CSER A  30     3153   2195   2301  -1074    771   -931       C  
ATOM    434  C   SER A  30       8.600  44.614  10.238  1.00 19.01           C  
ANISOU  434  C   SER A  30     3014   1950   2259   -931    762   -863       C  
ATOM    435  O   SER A  30       8.584  45.514   9.405  1.00 19.04           O  
ANISOU  435  O   SER A  30     3103   1822   2311   -919    779   -826       O  
ATOM    436  CB ASER A  30       9.166  45.537  12.505  0.69 24.53           C  
ANISOU  436  CB ASER A  30     3774   2685   2861  -1090    859  -1001       C  
ATOM    437  CB CSER A  30       9.152  45.623  12.453  0.31 23.90           C  
ANISOU  437  CB CSER A  30     3702   2593   2787  -1088    863  -1001       C  
ATOM    438  OG ASER A  30      10.018  45.441  13.642  0.69 20.36           O  
ANISOU  438  OG ASER A  30     3225   2283   2229  -1205    844  -1024       O  
ATOM    439  OG CSER A  30       7.795  45.410  12.817  0.31 24.57           O  
ANISOU  439  OG CSER A  30     3772   2626   2938   -983    911  -1037       O  
ATOM    440  H  ASER A  30      10.883  45.821  10.450  0.69 22.79           H  
ATOM    441  H  CSER A  30      10.888  45.817  10.442  0.31 22.79           H  
ATOM    442  HA ASER A  30       9.700  43.711  11.711  0.69 22.59           H  
ATOM    443  HA CSER A  30       9.677  43.753  11.755  0.31 24.16           H  
ATOM    444  HB2ASER A  30       9.173  46.453  12.186  0.69 29.43           H  
ATOM    445  HB2CSER A  30       9.708  45.505  13.239  0.31 28.68           H  
ATOM    446  HB3ASER A  30       8.266  45.289  12.768  0.69 29.43           H  
ATOM    447  HB3CSER A  30       9.247  46.527  12.116  0.31 28.68           H  
ATOM    448  HG ASER A  30      10.802  45.657  13.432  0.69 24.44           H  
ATOM    449  HG CSER A  30       7.298  45.511  12.147  0.31 29.49           H  
ATOM    450  N   GLY A  31       7.774  43.575  10.194  1.00 19.43           N  
ANISOU  450  N   GLY A  31     2969   2072   2340   -818    720   -822       N  
ATOM    451  CA  GLY A  31       6.732  43.476   9.193  1.00 19.05           C  
ANISOU  451  CA  GLY A  31     2898   1952   2388   -669    690   -743       C  
ATOM    452  C   GLY A  31       5.403  43.080   9.806  1.00 23.36           C  
ANISOU  452  C   GLY A  31     3383   2489   3005   -559    719   -773       C  
ATOM    453  O   GLY A  31       5.351  42.440  10.864  1.00 18.06           O  
ANISOU  453  O   GLY A  31     2668   1917   2278   -601    743   -830       O  
ATOM    454  H   GLY A  31       7.800  42.911  10.740  1.00 23.31           H  
ATOM    455  HA2 GLY A  31       6.625  44.331   8.748  1.00 22.86           H  
ATOM    456  HA3 GLY A  31       6.978  42.810   8.532  1.00 22.86           H  
ATOM    457  N   GLU A  32       4.323  43.467   9.143  1.00 17.75           N  
ANISOU  457  N   GLU A  32     2668   1659   2416   -426    712   -732       N  
ATOM    458  CA  GLU A  32       2.999  43.054   9.565  1.00 17.87           C  
ANISOU  458  CA  GLU A  32     2597   1670   2524   -313    740   -762       C  
ATOM    459  C   GLU A  32       2.113  42.970   8.350  1.00 17.92           C  
ANISOU  459  C   GLU A  32     2557   1613   2641   -171    655   -661       C  
ATOM    460  O   GLU A  32       2.390  43.583   7.317  1.00 18.33           O  
ANISOU  460  O   GLU A  32     2680   1576   2708   -160    595   -579       O  
ATOM    461  CB  GLU A  32       2.412  44.031  10.571  1.00 20.01           C  
ANISOU  461  CB  GLU A  32     2912   1819   2873   -309    868   -889       C  
ATOM    462  CG  GLU A  32       2.464  45.446  10.100  1.00 26.36           C  
ANISOU  462  CG  GLU A  32     3823   2421   3774   -285    889   -888       C  
ATOM    463  CD  GLU A  32       1.826  46.418  11.092  1.00 39.06           C  
ANISOU  463  CD  GLU A  32     5464   3887   5489   -271   1031  -1037       C  
ATOM    464  OE1 GLU A  32       1.684  47.602  10.735  1.00 40.06           O  
ANISOU  464  OE1 GLU A  32     5671   3812   5737   -227   1050  -1042       O  
ATOM    465  OE2 GLU A  32       1.457  46.005  12.210  1.00 35.93           O  
ANISOU  465  OE2 GLU A  32     5017   3579   5056   -310   1122  -1145       O  
ATOM    466  H   GLU A  32       4.331  43.968   8.444  1.00 21.30           H  
ATOM    467  HA  GLU A  32       3.047  42.177   9.976  1.00 21.45           H  
ATOM    468  HB2 GLU A  32       1.483  43.802  10.729  1.00 24.02           H  
ATOM    469  HB3 GLU A  32       2.914  43.972  11.399  1.00 24.02           H  
ATOM    470  HG2 GLU A  32       3.391  45.706   9.979  1.00 31.64           H  
ATOM    471  HG3 GLU A  32       1.986  45.518   9.259  1.00 31.64           H  
ATOM    472  N   GLY A  33       1.087  42.151   8.472  1.00 17.60           N  
ANISOU  472  N   GLY A  33     2399   1629   2661    -80    643   -663       N  
ATOM    473  CA  GLY A  33       0.112  41.967   7.410  1.00 17.79           C  
ANISOU  473  CA  GLY A  33     2356   1609   2795     55    550   -574       C  
ATOM    474  C   GLY A  33      -0.762  40.764   7.681  1.00 19.09           C  
ANISOU  474  C   GLY A  33     2379   1889   2985    108    542   -588       C  
ATOM    475  O   GLY A  33      -1.070  40.461   8.840  1.00 17.22           O  
ANISOU  475  O   GLY A  33     2100   1701   2742     76    640   -687       O  
ATOM    476  H   GLY A  33       0.927  41.681   9.174  1.00 21.13           H  
ATOM    477  HA2 GLY A  33      -0.451  42.753   7.341  1.00 21.35           H  
ATOM    478  HA3 GLY A  33       0.570  41.836   6.564  1.00 21.35           H  
ATOM    479  N   GLU A  34      -1.151  40.059   6.614  1.00 16.63           N  
ANISOU  479  N   GLU A  34     2005   1626   2689    171    427   -492       N  
ATOM    480  CA  GLU A  34      -2.030  38.912   6.757  1.00 16.14           C  
ANISOU  480  CA  GLU A  34     1809   1664   2662    219    412   -501       C  
ATOM    481  C   GLU A  34      -1.791  37.859   5.697  1.00 15.10           C  
ANISOU  481  C   GLU A  34     1643   1636   2458    211    294   -408       C  
ATOM    482  O   GLU A  34      -1.292  38.156   4.586  1.00 15.12           O  
ANISOU  482  O   GLU A  34     1715   1613   2416    201    211   -326       O  
ATOM    483  CB  GLU A  34      -3.498  39.351   6.736  1.00 24.16           C  
ANISOU  483  CB  GLU A  34     2726   2583   3871    354    419   -528       C  
ATOM    484  CG  GLU A  34      -3.921  40.077   5.498  1.00 32.09           C  
ANISOU  484  CG  GLU A  34     3749   3467   4977    455    295   -427       C  
ATOM    485  CD  GLU A  34      -5.255  40.795   5.668  1.00 35.26           C  
ANISOU  485  CD  GLU A  34     4052   3734   5611    597    309   -471       C  
ATOM    486  OE1 GLU A  34      -5.471  41.443   6.715  1.00 38.72           O  
ANISOU  486  OE1 GLU A  34     4484   4096   6132    602    450   -595       O  
ATOM    487  OE2 GLU A  34      -6.091  40.708   4.745  1.00 36.42           O  
ANISOU  487  OE2 GLU A  34     4121   3851   5864    700    178   -389       O  
ATOM    488  H   GLU A  34      -0.918  40.229   5.804  1.00 19.96           H  
ATOM    489  HA  GLU A  34      -1.860  38.501   7.619  1.00 19.37           H  
ATOM    490  HB2 GLU A  34      -4.057  38.562   6.818  1.00 28.99           H  
ATOM    491  HB3 GLU A  34      -3.655  39.941   7.490  1.00 28.99           H  
ATOM    492  HG2 GLU A  34      -3.250  40.741   5.275  1.00 38.51           H  
ATOM    493  HG3 GLU A  34      -4.013  39.440   4.772  1.00 38.51           H  
ATOM    494  N   GLY A  35      -2.142  36.627   6.055  1.00 14.87           N  
ANISOU  494  N   GLY A  35     1517   1720   2411    201    297   -429       N  
ATOM    495  CA  GLY A  35      -2.055  35.502   5.140  1.00 17.37           C  
ANISOU  495  CA  GLY A  35     1787   2132   2679    195    200   -365       C  
ATOM    496  C   GLY A  35      -3.408  34.838   5.007  1.00 18.21           C  
ANISOU  496  C   GLY A  35     1765   2265   2888    274    170   -366       C  
ATOM    497  O   GLY A  35      -4.192  34.813   5.956  1.00 17.93           O  
ANISOU  497  O   GLY A  35     1661   2225   2928    296    252   -435       O  
ATOM    498  H   GLY A  35      -2.438  36.418   6.835  1.00 17.84           H  
ATOM    499  HA2 GLY A  35      -1.766  35.807   4.265  1.00 20.84           H  
ATOM    500  HA3 GLY A  35      -1.417  34.852   5.474  1.00 20.84           H  
ATOM    501  N   ASP A  36      -3.701  34.337   3.811  1.00 13.74           N  
ANISOU  501  N   ASP A  36     1166   1732   2323    305     57   -297       N  
ATOM    502  CA  ASP A  36      -4.967  33.678   3.527  1.00 14.50           C  
ANISOU  502  CA  ASP A  36     1133   1861   2516    371      7   -294       C  
ATOM    503  C   ASP A  36      -4.619  32.396   2.819  1.00 13.23           C  
ANISOU  503  C   ASP A  36      955   1806   2267    316    -60   -264       C  
ATOM    504  O   ASP A  36      -4.451  32.373   1.591  1.00 14.25           O  
ANISOU  504  O   ASP A  36     1121   1946   2349    312   -160   -202       O  
ATOM    505  CB  ASP A  36      -5.823  34.579   2.635  1.00 15.64           C  
ANISOU  505  CB  ASP A  36     1259   1913   2772    474    -92   -234       C  
ATOM    506  CG  ASP A  36      -7.270  34.133   2.565  1.00 24.81           C  
ANISOU  506  CG  ASP A  36     2257   3093   4078    555   -134   -250       C  
ATOM    507  OD1 ASP A  36      -7.585  33.049   3.077  1.00 26.29           O  
ANISOU  507  OD1 ASP A  36     2358   3374   4258    517    -84   -302       O  
ATOM    508  OD2 ASP A  36      -8.097  34.885   2.016  1.00 29.69           O  
ANISOU  508  OD2 ASP A  36     2829   3625   4825    655   -222   -209       O  
ATOM    509  H   ASP A  36      -3.169  34.368   3.136  1.00 16.49           H  
ATOM    510  HA  ASP A  36      -5.444  33.481   4.348  1.00 17.40           H  
ATOM    511  HB2 ASP A  36      -5.805  35.483   2.988  1.00 18.77           H  
ATOM    512  HB3 ASP A  36      -5.462  34.567   1.735  1.00 18.77           H  
ATOM    513  N   ALA A  37      -4.423  31.331   3.590  1.00 14.38           N  
ANISOU  513  N   ALA A  37     1060   2025   2380    259     -3   -309       N  
ATOM    514  CA  ALA A  37      -3.825  30.116   3.037  1.00 13.95           C  
ANISOU  514  CA  ALA A  37     1002   2049   2249    200    -50   -297       C  
ATOM    515  C   ALA A  37      -4.763  29.443   2.006  1.00 17.11           C  
ANISOU  515  C   ALA A  37     1324   2488   2691    231   -144   -272       C  
ATOM    516  O   ALA A  37      -4.342  28.632   1.174  1.00 14.97           O  
ANISOU  516  O   ALA A  37     1062   2269   2359    187   -196   -264       O  
ATOM    517  CB  ALA A  37      -3.510  29.151   4.156  1.00 14.36           C  
ANISOU  517  CB  ALA A  37     1031   2146   2280    140     14   -336       C  
ATOM    518  H   ALA A  37      -4.623  31.284   4.425  1.00 17.26           H  
ATOM    519  HA  ALA A  37      -2.995  30.343   2.589  1.00 16.74           H  
ATOM    520  HB1 ALA A  37      -3.115  28.350   3.779  1.00 17.24           H  
ATOM    521  HB2 ALA A  37      -2.887  29.572   4.768  1.00 17.24           H  
ATOM    522  HB3 ALA A  37      -4.332  28.928   4.621  1.00 17.24           H  
ATOM    523  N   THR A  38      -6.041  29.753   2.112  1.00 15.07           N  
ANISOU  523  N   THR A  38      976   2206   2544    302   -158   -275       N  
ATOM    524  CA  THR A  38      -7.035  29.240   1.154  1.00 20.20           C  
ANISOU  524  CA  THR A  38     1581   2883   3211    318   -251   -231       C  
ATOM    525  C   THR A  38      -6.670  29.653  -0.264  1.00 16.50           C  
ANISOU  525  C   THR A  38     1151   2419   2699    326   -383   -179       C  
ATOM    526  O   THR A  38      -6.946  28.930  -1.238  1.00 21.01           O  
ANISOU  526  O   THR A  38     1702   3050   3231    295   -472   -161       O  
ATOM    527  CB  THR A  38      -8.433  29.767   1.475  1.00 25.86           C  
ANISOU  527  CB  THR A  38     2226   3559   4042    389   -242   -228       C  
ATOM    528  OG1 THR A  38      -8.849  29.272   2.753  1.00 23.44           O  
ANISOU  528  OG1 THR A  38     1900   3262   3744    353   -120   -279       O  
ATOM    529  CG2 THR A  38      -9.459  29.306   0.415  1.00 26.42           C  
ANISOU  529  CG2 THR A  38     2244   3667   4126    401   -351   -180       C  
ATOM    530  H   THR A  38      -6.370  30.257   2.725  1.00 18.08           H  
ATOM    531  HA  THR A  38      -7.055  28.272   1.197  1.00 24.24           H  
ATOM    532  HB  THR A  38      -8.420  30.737   1.491  1.00 31.03           H  
ATOM    533  HG1 THR A  38      -8.314  29.527   3.348  1.00 28.13           H  
ATOM    534 HG21 THR A  38     -10.339  29.649   0.634  1.00 31.70           H  
ATOM    535 HG22 THR A  38      -9.202  29.635  -0.461  1.00 31.70           H  
ATOM    536 HG23 THR A  38      -9.496  28.337   0.388  1.00 31.70           H  
ATOM    537  N   TYR A  39      -6.064  30.829  -0.390  1.00 16.31           N  
ANISOU  537  N   TYR A  39     1234   2322   2641    339   -381   -140       N  
ATOM    538  CA  TYR A  39      -5.652  31.335  -1.694  1.00 18.99           C  
ANISOU  538  CA  TYR A  39     1680   2650   2884    309   -484    -63       C  
ATOM    539  C   TYR A  39      -4.148  31.329  -1.844  1.00 19.61           C  
ANISOU  539  C   TYR A  39     1881   2749   2820    212   -419    -78       C  
ATOM    540  O   TYR A  39      -3.619  31.739  -2.876  1.00 17.60           O  
ANISOU  540  O   TYR A  39     1734   2494   2459    155   -473    -27       O  
ATOM    541  CB  TYR A  39      -6.214  32.735  -1.898  1.00 24.43           C  
ANISOU  541  CB  TYR A  39     2401   3225   3656    394   -553     10       C  
ATOM    542  CG  TYR A  39      -7.712  32.694  -1.905  1.00 27.78           C  
ANISOU  542  CG  TYR A  39     2677   3635   4244    496   -635     19       C  
ATOM    543  CD1 TYR A  39      -8.402  32.327  -3.050  1.00 27.35           C  
ANISOU  543  CD1 TYR A  39     2588   3627   4178    494   -796     82       C  
ATOM    544  CD2 TYR A  39      -8.439  32.944  -0.753  1.00 27.94           C  
ANISOU  544  CD2 TYR A  39     2580   3608   4429    578   -546    -50       C  
ATOM    545  CE1 TYR A  39      -9.766  32.260  -3.063  1.00 34.08           C  
ANISOU  545  CE1 TYR A  39     3305   4475   5167    573   -858     87       C  
ATOM    546  CE2 TYR A  39      -9.824  32.886  -0.762  1.00 26.40           C  
ANISOU  546  CE2 TYR A  39     2265   3410   4357    645   -583    -51       C  
ATOM    547  CZ  TYR A  39     -10.476  32.530  -1.916  1.00 35.29           C  
ANISOU  547  CZ  TYR A  39     3375   4585   5451    638   -728     19       C  
ATOM    548  OH  TYR A  39     -11.853  32.467  -1.938  1.00 45.28           O  
ANISOU  548  OH  TYR A  39     4539   5857   6807    684   -747     16       O  
ATOM    549  H   TYR A  39      -5.880  31.354   0.265  1.00 19.57           H  
ATOM    550  HA  TYR A  39      -6.022  30.762  -2.384  1.00 22.78           H  
ATOM    551  HB2 TYR A  39      -5.924  33.310  -1.173  1.00 29.31           H  
ATOM    552  HB3 TYR A  39      -5.911  33.084  -2.751  1.00 29.31           H  
ATOM    553  HD1 TYR A  39      -7.928  32.142  -3.829  1.00 32.82           H  
ATOM    554  HD2 TYR A  39      -7.994  33.183   0.028  1.00 33.53           H  
ATOM    555  HE1 TYR A  39     -10.213  32.026  -3.844  1.00 40.89           H  
ATOM    556  HE2 TYR A  39     -10.306  33.067   0.012  1.00 31.68           H  
ATOM    557  HH  TYR A  39     -12.161  32.652  -1.179  1.00 54.34           H  
ATOM    558  N   GLY A  40      -3.457  30.830  -0.827  1.00 13.07           N  
ANISOU  558  N   GLY A  40     1034   1944   1989    182   -307   -148       N  
ATOM    559  CA  GLY A  40      -2.010  30.824  -0.825  1.00 12.10           C  
ANISOU  559  CA  GLY A  40      994   1838   1764     98   -244   -175       C  
ATOM    560  C   GLY A  40      -1.397  32.212  -0.826  1.00 12.58           C  
ANISOU  560  C   GLY A  40     1169   1820   1789     85   -221   -140       C  
ATOM    561  O   GLY A  40      -0.278  32.384  -1.305  1.00 13.99           O  
ANISOU  561  O   GLY A  40     1430   2016   1869      1   -195   -146       O  
ATOM    562  H   GLY A  40      -3.810  30.487  -0.121  1.00 15.69           H  
ATOM    563  HA2 GLY A  40      -1.694  30.354  -0.038  1.00 14.52           H  
ATOM    564  HA3 GLY A  40      -1.692  30.352  -1.610  1.00 14.52           H  
ATOM    565  N   LYS A  41      -2.102  33.193  -0.248  1.00 13.16           N  
ANISOU  565  N   LYS A  41     1243   1803   1955    163   -217   -117       N  
ATOM    566  CA  LYS A  41      -1.802  34.607  -0.465  1.00 14.01           C  
ANISOU  566  CA  LYS A  41     1466   1805   2051    165   -223    -66       C  
ATOM    567  C   LYS A  41      -1.278  35.299   0.777  1.00 13.76           C  
ANISOU  567  C   LYS A  41     1464   1715   2050    159   -111   -122       C  
ATOM    568  O   LYS A  41      -1.895  35.198   1.859  1.00 13.67           O  
ANISOU  568  O   LYS A  41     1374   1690   2130    213    -53   -177       O  
ATOM    569  CB  LYS A  41      -3.080  35.320  -0.960  1.00 15.41           C  
ANISOU  569  CB  LYS A  41     1626   1895   2336    268   -330      9       C  
ATOM    570  CG  LYS A  41      -2.944  36.821  -1.214  1.00 16.64           C  
ANISOU  570  CG  LYS A  41     1904   1906   2512    286   -358     78       C  
ATOM    571  CD  LYS A  41      -4.273  37.391  -1.734  1.00 18.27           C  
ANISOU  571  CD  LYS A  41     2068   2018   2856    405   -495    161       C  
ATOM    572  CE  LYS A  41      -4.211  38.893  -1.920  1.00 33.90           C  
ANISOU  572  CE  LYS A  41     4169   3823   4891    439   -534    236       C  
ATOM    573  NZ  LYS A  41      -5.545  39.527  -2.248  1.00 35.10           N  
ANISOU  573  NZ  LYS A  41     4254   3851   5230    583   -674    311       N  
ATOM    574  H   LYS A  41      -2.767  33.059   0.281  1.00 15.80           H  
ATOM    575  HA  LYS A  41      -1.127  34.684  -1.158  1.00 16.81           H  
ATOM    576  HB2 LYS A  41      -3.358  34.909  -1.793  1.00 18.50           H  
ATOM    577  HB3 LYS A  41      -3.775  35.201  -0.293  1.00 18.50           H  
ATOM    578  HG2 LYS A  41      -2.718  37.271  -0.385  1.00 19.97           H  
ATOM    579  HG3 LYS A  41      -2.259  36.976  -1.883  1.00 19.97           H  
ATOM    580  HD2 LYS A  41      -4.479  36.988  -2.592  1.00 21.93           H  
ATOM    581  HD3 LYS A  41      -4.976  37.195  -1.095  1.00 21.93           H  
ATOM    582  HE2 LYS A  41      -3.886  39.296  -1.100  1.00 40.69           H  
ATOM    583  HE3 LYS A  41      -3.602  39.092  -2.648  1.00 40.69           H  
ATOM    584  HZ1 LYS A  41      -5.447  40.407  -2.346  1.00 42.11           H  
ATOM    585  HZ2 LYS A  41      -5.866  39.186  -3.004  1.00 42.11           H  
ATOM    586  HZ3 LYS A  41      -6.125  39.372  -1.591  1.00 42.11           H  
ATOM    587  N   LEU A  42      -0.153  35.991   0.628  1.00 13.96           N  
ANISOU  587  N   LEU A  42     1603   1710   1990     79    -74   -116       N  
ATOM    588  CA  LEU A  42       0.406  36.835   1.702  1.00 13.85           C  
ANISOU  588  CA  LEU A  42     1639   1630   1993     56     22   -167       C  
ATOM    589  C   LEU A  42       0.432  38.291   1.261  1.00 16.58           C  
ANISOU  589  C   LEU A  42     2110   1835   2356     61      4   -109       C  
ATOM    590  O   LEU A  42       0.823  38.592   0.131  1.00 15.62           O  
ANISOU  590  O   LEU A  42     2080   1702   2154      7    -57    -35       O  
ATOM    591  CB  LEU A  42       1.847  36.420   1.995  1.00 17.93           C  
ANISOU  591  CB  LEU A  42     2179   2229   2406    -60     83   -219       C  
ATOM    592  CG  LEU A  42       2.072  35.034   2.565  1.00 25.09           C  
ANISOU  592  CG  LEU A  42     2978   3250   3303    -76     97   -272       C  
ATOM    593  CD1 LEU A  42       3.519  34.655   2.383  1.00 28.01           C  
ANISOU  593  CD1 LEU A  42     3360   3689   3592   -179    120   -306       C  
ATOM    594  CD2 LEU A  42       1.711  35.012   4.022  1.00 24.59           C  
ANISOU  594  CD2 LEU A  42     2875   3177   3291    -53    157   -324       C  
ATOM    595  H   LEU A  42       0.317  35.993  -0.092  1.00 16.75           H  
ATOM    596  HA  LEU A  42      -0.124  36.751   2.510  1.00 16.62           H  
ATOM    597  HB2 LEU A  42       2.348  36.471   1.166  1.00 21.52           H  
ATOM    598  HB3 LEU A  42       2.218  37.052   2.630  1.00 21.52           H  
ATOM    599  HG  LEU A  42       1.518  34.391   2.095  1.00 30.10           H  
ATOM    600 HD11 LEU A  42       3.661  33.768   2.749  1.00 33.61           H  
ATOM    601 HD12 LEU A  42       3.731  34.662   1.437  1.00 33.61           H  
ATOM    602 HD13 LEU A  42       4.075  35.299   2.851  1.00 33.61           H  
ATOM    603 HD21 LEU A  42       1.860  34.119   4.371  1.00 29.51           H  
ATOM    604 HD22 LEU A  42       2.268  35.650   4.495  1.00 29.51           H  
ATOM    605 HD23 LEU A  42       0.776  35.253   4.119  1.00 29.51           H  
ATOM    606  N   THR A  43       0.061  39.188   2.163  1.00 15.76           N  
ANISOU  606  N   THR A  43     2018   1620   2349    112     63   -148       N  
ATOM    607  CA  THR A  43       0.221  40.626   1.949  1.00 17.05           C  
ANISOU  607  CA  THR A  43     2310   1624   2546    110     62   -108       C  
ATOM    608  C   THR A  43       0.904  41.184   3.192  1.00 19.99           C  
ANISOU  608  C   THR A  43     2720   1963   2914     51    192   -211       C  
ATOM    609  O   THR A  43       0.382  41.076   4.296  1.00 17.27           O  
ANISOU  609  O   THR A  43     2303   1618   2643     95    266   -299       O  
ATOM    610  CB  THR A  43      -1.134  41.321   1.739  1.00 21.36           C  
ANISOU  610  CB  THR A  43     2826   2025   3264    255     -9    -60       C  
ATOM    611  OG1 THR A  43      -1.940  41.141   2.898  1.00 34.36           O  
ANISOU  611  OG1 THR A  43     4350   3666   5038    336     74   -165       O  
ATOM    612  CG2 THR A  43      -1.883  40.707   0.560  1.00 24.30           C  
ANISOU  612  CG2 THR A  43     3149   2446   3638    308   -158     42       C  
ATOM    613  H   THR A  43      -0.293  38.989   2.921  1.00 18.91           H  
ATOM    614  HA  THR A  43       0.785  40.787   1.177  1.00 20.46           H  
ATOM    615  HB  THR A  43      -1.000  42.267   1.570  1.00 25.63           H  
ATOM    616  HG1 THR A  43      -1.558  41.474   3.568  1.00 41.23           H  
ATOM    617 HG21 THR A  43      -2.735  41.155   0.439  1.00 29.16           H  
ATOM    618 HG22 THR A  43      -1.359  40.801  -0.251  1.00 29.16           H  
ATOM    619 HG23 THR A  43      -2.043  39.764   0.724  1.00 29.16           H  
ATOM    620  N   LEU A  44       2.075  41.767   3.013  1.00 17.05           N  
ANISOU  620  N   LEU A  44     2464   1570   2444    -66    224   -206       N  
ATOM    621  CA  LEU A  44       2.901  42.186   4.145  1.00 19.32           C  
ANISOU  621  CA  LEU A  44     2788   1855   2699   -153    335   -306       C  
ATOM    622  C   LEU A  44       3.623  43.468   3.815  1.00 19.86           C  
ANISOU  622  C   LEU A  44     3009   1795   2743   -234    358   -282       C  
ATOM    623  O   LEU A  44       3.964  43.707   2.653  1.00 18.99           O  
ANISOU  623  O   LEU A  44     2979   1662   2573   -278    296   -188       O  
ATOM    624  CB  LEU A  44       3.941  41.101   4.433  1.00 20.19           C  
ANISOU  624  CB  LEU A  44     2837   2143   2690   -254    354   -349       C  
ATOM    625  CG  LEU A  44       3.397  39.809   5.042  1.00 21.08           C  
ANISOU  625  CG  LEU A  44     2815   2375   2821   -201    346   -384       C  
ATOM    626  CD1 LEU A  44       4.281  38.624   4.711  1.00 21.30           C  
ANISOU  626  CD1 LEU A  44     2780   2551   2762   -267    312   -381       C  
ATOM    627  CD2 LEU A  44       3.308  40.000   6.532  1.00 20.51           C  
ANISOU  627  CD2 LEU A  44     2731   2296   2764   -221    433   -479       C  
ATOM    628  H   LEU A  44       2.422  41.935   2.244  1.00 20.46           H  
ATOM    629  HA  LEU A  44       2.351  42.320   4.932  1.00 23.19           H  
ATOM    630  HB2 LEU A  44       4.379  40.867   3.600  1.00 24.22           H  
ATOM    631  HB3 LEU A  44       4.596  41.460   5.052  1.00 24.22           H  
ATOM    632  HG  LEU A  44       2.506  39.637   4.698  1.00 25.30           H  
ATOM    633 HD11 LEU A  44       3.903  37.826   5.114  1.00 25.56           H  
ATOM    634 HD12 LEU A  44       4.322  38.521   3.747  1.00 25.56           H  
ATOM    635 HD13 LEU A  44       5.170  38.785   5.065  1.00 25.56           H  
ATOM    636 HD21 LEU A  44       2.963  39.187   6.934  1.00 24.61           H  
ATOM    637 HD22 LEU A  44       4.193  40.191   6.879  1.00 24.61           H  
ATOM    638 HD23 LEU A  44       2.711  40.741   6.720  1.00 24.61           H  
ATOM    639  N   LYS A  45       3.844  44.297   4.832  1.00 18.83           N  
ANISOU  639  N   LYS A  45     2928   1579   2647   -268    451   -370       N  
ATOM    640  CA  LYS A  45       4.690  45.462   4.693  1.00 19.64           C  
ANISOU  640  CA  LYS A  45     3178   1569   2717   -374    491   -368       C  
ATOM    641  C   LYS A  45       5.793  45.351   5.738  1.00 21.01           C  
ANISOU  641  C   LYS A  45     3345   1840   2798   -511    580   -482       C  
ATOM    642  O   LYS A  45       5.532  45.030   6.912  1.00 18.78           O  
ANISOU  642  O   LYS A  45     2997   1606   2532   -497    635   -578       O  
ATOM    643  CB  LYS A  45       3.887  46.758   4.851  1.00 21.39           C  
ANISOU  643  CB  LYS A  45     3482   1554   3090   -289    509   -368       C  
ATOM    644  CG  LYS A  45       4.729  48.030   4.738  1.00 22.65           C  
ANISOU  644  CG  LYS A  45     3811   1569   3227   -407    553   -366       C  
ATOM    645  CD  LYS A  45       3.941  49.286   5.077  1.00 25.34           C  
ANISOU  645  CD  LYS A  45     4224   1656   3747   -316    584   -391       C  
ATOM    646  CE  LYS A  45       4.852  50.501   5.169  1.00 25.80           C  
ANISOU  646  CE  LYS A  45     4452   1571   3778   -453    648   -415       C  
ATOM    647  NZ  LYS A  45       4.132  51.701   5.603  1.00 27.76           N  
ANISOU  647  NZ  LYS A  45     4768   1558   4220   -366    693   -463       N  
ATOM    648  H   LYS A  45       3.509  44.200   5.618  1.00 22.59           H  
ATOM    649  HA  LYS A  45       5.099  45.460   3.813  1.00 23.57           H  
ATOM    650  HB2 LYS A  45       3.208  46.791   4.158  1.00 25.66           H  
ATOM    651  HB3 LYS A  45       3.465  46.759   5.724  1.00 25.66           H  
ATOM    652  HG2 LYS A  45       5.477  47.970   5.353  1.00 27.18           H  
ATOM    653  HG3 LYS A  45       5.053  48.116   3.828  1.00 27.18           H  
ATOM    654  HD2 LYS A  45       3.284  49.449   4.383  1.00 30.41           H  
ATOM    655  HD3 LYS A  45       3.503  49.168   5.935  1.00 30.41           H  
ATOM    656  HE2 LYS A  45       5.557  50.323   5.812  1.00 30.95           H  
ATOM    657  HE3 LYS A  45       5.235  50.678   4.295  1.00 30.95           H  
ATOM    658  HZ1 LYS A  45       3.482  51.891   5.026  1.00 33.31           H  
ATOM    659  HZ2 LYS A  45       3.775  51.567   6.407  1.00 33.31           H  
ATOM    660  HZ3 LYS A  45       4.691  52.392   5.646  1.00 33.31           H  
ATOM    661  N   PHE A  46       7.015  45.631   5.294  1.00 19.21           N  
ANISOU  661  N   PHE A  46     3187   1641   2470   -654    589   -469       N  
ATOM    662  CA  PHE A  46       8.207  45.591   6.123  1.00 18.95           C  
ANISOU  662  CA  PHE A  46     3145   1703   2353   -799    650   -565       C  
ATOM    663  C   PHE A  46       8.863  46.963   6.189  1.00 21.17           C  
ANISOU  663  C   PHE A  46     3573   1845   2626   -917    713   -594       C  
ATOM    664  O   PHE A  46       8.919  47.683   5.189  1.00 21.26           O  
ANISOU  664  O   PHE A  46     3695   1741   2643   -940    696   -510       O  
ATOM    665  CB  PHE A  46       9.209  44.587   5.551  1.00 17.97           C  
ANISOU  665  CB  PHE A  46     2937   1759   2134   -879    612   -548       C  
ATOM    666  CG  PHE A  46       8.661  43.191   5.430  1.00 16.70           C  
ANISOU  666  CG  PHE A  46     2638   1725   1984   -776    549   -522       C  
ATOM    667  CD1 PHE A  46       8.642  42.332   6.538  1.00 17.56           C  
ANISOU  667  CD1 PHE A  46     2642   1940   2090   -760    546   -584       C  
ATOM    668  CD2 PHE A  46       8.125  42.744   4.221  1.00 16.47           C  
ANISOU  668  CD2 PHE A  46     2596   1702   1959   -706    487   -432       C  
ATOM    669  CE1 PHE A  46       8.109  41.055   6.422  1.00 14.90           C  
ANISOU  669  CE1 PHE A  46     2189   1701   1770   -672    488   -556       C  
ATOM    670  CE2 PHE A  46       7.615  41.462   4.113  1.00 15.41           C  
ANISOU  670  CE2 PHE A  46     2338   1678   1839   -621    434   -418       C  
ATOM    671  CZ  PHE A  46       7.603  40.626   5.191  1.00 17.30           C  
ANISOU  671  CZ  PHE A  46     2474   2009   2091   -601    437   -479       C  
ATOM    672  H   PHE A  46       7.180  45.856   4.481  1.00 23.05           H  
ATOM    673  HA  PHE A  46       7.970  45.316   7.023  1.00 22.75           H  
ATOM    674  HB2 PHE A  46       9.475  44.880   4.665  1.00 21.57           H  
ATOM    675  HB3 PHE A  46       9.985  44.553   6.132  1.00 21.57           H  
ATOM    676  HD1 PHE A  46       8.982  42.620   7.354  1.00 21.07           H  
ATOM    677  HD2 PHE A  46       8.132  43.303   3.478  1.00 19.76           H  
ATOM    678  HE1 PHE A  46       8.106  40.481   7.154  1.00 17.88           H  
ATOM    679  HE2 PHE A  46       7.267  41.172   3.300  1.00 18.49           H  
ATOM    680  HZ  PHE A  46       7.249  39.769   5.108  1.00 20.76           H  
ATOM    681  N   ILE A  47       9.379  47.304   7.373  1.00 20.66           N  
ANISOU  681  N   ILE A  47     3519   1794   2538  -1007    782   -710       N  
ATOM    682  CA  ILE A  47      10.141  48.534   7.579  1.00 22.01           C  
ANISOU  682  CA  ILE A  47     3818   1853   2691  -1145    850   -760       C  
ATOM    683  C   ILE A  47      11.501  48.178   8.161  1.00 23.73           C  
ANISOU  683  C   ILE A  47     3946   2275   2795  -1268    848   -805       C  
ATOM    684  O   ILE A  47      11.596  47.323   9.042  1.00 21.25           O  
ANISOU  684  O   ILE A  47     3521   2106   2447  -1258    826   -850       O  
ATOM    685  CB  ILE A  47       9.469  49.427   8.625  1.00 28.21           C  
ANISOU  685  CB  ILE A  47     4648   2518   3552  -1088    916   -835       C  
ATOM    686  CG1 ILE A  47       8.023  49.749   8.244  1.00 35.14           C  
ANISOU  686  CG1 ILE A  47     5572   3192   4587   -926    916   -804       C  
ATOM    687  CG2 ILE A  47      10.286  50.692   8.845  1.00 38.54           C  
ANISOU  687  CG2 ILE A  47     6048   3762   4833  -1194    964   -857       C  
ATOM    688  CD1 ILE A  47       7.878  50.907   7.338  1.00 36.65           C  
ANISOU  688  CD1 ILE A  47     5904   3164   4858   -910    899   -718       C  
ATOM    689  H   ILE A  47       9.297  46.828   8.085  1.00 24.79           H  
ATOM    690  HA  ILE A  47      10.252  49.021   6.747  1.00 26.41           H  
ATOM    691  HB  ILE A  47       9.451  48.938   9.463  1.00 33.85           H  
ATOM    692 HG12 ILE A  47       7.640  48.976   7.800  1.00 42.16           H  
ATOM    693 HG13 ILE A  47       7.524  49.942   9.053  1.00 42.16           H  
ATOM    694 HG21 ILE A  47       9.843  51.242   9.510  1.00 46.25           H  
ATOM    695 HG22 ILE A  47      11.172  50.445   9.156  1.00 46.25           H  
ATOM    696 HG23 ILE A  47      10.352  51.175   8.006  1.00 46.25           H  
ATOM    697 HD11 ILE A  47       6.936  51.042   7.147  1.00 43.98           H  
ATOM    698 HD12 ILE A  47       8.244  51.694   7.771  1.00 43.98           H  
ATOM    699 HD13 ILE A  47       8.360  50.726   6.516  1.00 43.98           H  
ATOM    700  N   CYS A  48      12.548  48.857   7.719  1.00 22.51           N  
ANISOU  700  N   CYS A  48     3839   2126   2588  -1379    867   -789       N  
ATOM    701  CA  CYS A  48      13.806  48.841   8.448  1.00 22.74           C  
ANISOU  701  CA  CYS A  48     3795   2308   2539  -1484    875   -844       C  
ATOM    702  C   CYS A  48      13.696  49.874   9.570  1.00 23.97           C  
ANISOU  702  C   CYS A  48     4022   2381   2703  -1510    934   -913       C  
ATOM    703  O   CYS A  48      13.540  51.068   9.332  1.00 25.29           O  
ANISOU  703  O   CYS A  48     4316   2385   2907  -1529    984   -910       O  
ATOM    704  CB  CYS A  48      14.992  49.175   7.547  1.00 23.37           C  
ANISOU  704  CB  CYS A  48     3885   2432   2562  -1594    887   -819       C  
ATOM    705  SG  CYS A  48      16.579  49.059   8.445  1.00 25.80           S  
ANISOU  705  SG  CYS A  48     4077   2927   2801  -1706    885   -893       S  
ATOM    706  H   CYS A  48      12.557  49.333   7.003  1.00 27.01           H  
ATOM    707  HA  CYS A  48      13.947  47.965   8.841  1.00 27.29           H  
ATOM    708  HB2 CYS A  48      15.016  48.549   6.807  1.00 28.04           H  
ATOM    709  HB3 CYS A  48      14.896  50.082   7.217  1.00 28.04           H  
ATOM    710  HG  CYS A  48      17.474  49.331   7.692  1.00 30.97           H  
ATOM    711  N   THR A  49      13.743  49.406  10.800  1.00 23.69           N  
ANISOU  711  N   THR A  49     3912   2456   2634  -1515    925   -969       N  
ATOM    712  CA  THR A  49      13.518  50.288  11.933  1.00 24.93           C  
ANISOU  712  CA  THR A  49     4134   2548   2790  -1545    990  -1043       C  
ATOM    713  C   THR A  49      14.819  50.902  12.422  1.00 26.03           C  
ANISOU  713  C   THR A  49     4280   2757   2853  -1687   1005  -1082       C  
ATOM    714  O   THR A  49      14.805  51.762  13.298  1.00 28.32           O  
ANISOU  714  O   THR A  49     4636   2994   3132  -1740   1065  -1149       O  
ATOM    715  CB  THR A  49      12.902  49.501  13.078  1.00 24.38           C  
ANISOU  715  CB  THR A  49     3997   2568   2699  -1505    978  -1082       C  
ATOM    716  OG1 THR A  49      13.799  48.446  13.445  1.00 23.60           O  
ANISOU  716  OG1 THR A  49     3781   2665   2519  -1557    894  -1061       O  
ATOM    717  CG2 THR A  49      11.576  48.895  12.647  1.00 23.43           C  
ANISOU  717  CG2 THR A  49     3860   2382   2660  -1363    972  -1057       C  
ATOM    718  H   THR A  49      13.903  48.587  11.009  1.00 28.43           H  
ATOM    719  HA  THR A  49      12.910  51.000  11.680  1.00 29.92           H  
ATOM    720  HB  THR A  49      12.750  50.085  13.837  1.00 29.26           H  
ATOM    721  HG1 THR A  49      13.474  48.000  14.078  1.00 28.32           H  
ATOM    722 HG21 THR A  49      11.187  48.394  13.381  1.00 28.12           H  
ATOM    723 HG22 THR A  49      10.961  49.598  12.384  1.00 28.12           H  
ATOM    724 HG23 THR A  49      11.713  48.298  11.896  1.00 28.12           H  
ATOM    725  N   THR A  50      15.944  50.443  11.898  1.00 25.66           N  
ANISOU  725  N   THR A  50     4157   2834   2761  -1749    955  -1052       N  
ATOM    726  CA  THR A  50      17.255  50.909  12.370  1.00 28.74           C  
ANISOU  726  CA  THR A  50     4528   3307   3086  -1880    959  -1094       C  
ATOM    727  C   THR A  50      17.881  51.955  11.449  1.00 34.05           C  
ANISOU  727  C   THR A  50     5287   3890   3762  -1958   1014  -1087       C  
ATOM    728  O   THR A  50      18.966  52.448  11.739  1.00 33.22           O  
ANISOU  728  O   THR A  50     5172   3839   3610  -2073   1028  -1128       O  
ATOM    729  CB  THR A  50      18.243  49.725  12.498  1.00 26.03           C  
ANISOU  729  CB  THR A  50     4020   3163   2707  -1898    864  -1079       C  
ATOM    730  OG1 THR A  50      18.134  48.889  11.337  1.00 24.81           O  
ANISOU  730  OG1 THR A  50     3799   3037   2591  -1826    830  -1022       O  
ATOM    731  CG2 THR A  50      17.919  48.882  13.724  1.00 25.56           C  
ANISOU  731  CG2 THR A  50     3896   3197   2617  -1868    799  -1089       C  
ATOM    732  H   THR A  50      15.985  49.860  11.267  1.00 30.80           H  
ATOM    733  HA  THR A  50      17.149  51.308  13.248  1.00 34.49           H  
ATOM    734  HB  THR A  50      19.150  50.059  12.579  1.00 31.24           H  
ATOM    735  HG1 THR A  50      18.319  49.331  10.647  1.00 29.77           H  
ATOM    736 HG21 THR A  50      18.544  48.143  13.793  1.00 30.67           H  
ATOM    737 HG22 THR A  50      17.982  49.424  14.526  1.00 30.67           H  
ATOM    738 HG23 THR A  50      17.019  48.527  13.654  1.00 30.67           H  
ATOM    739  N   GLY A  51      17.209  52.283  10.345  1.00 27.80           N  
ANISOU  739  N   GLY A  51     4583   2957   3021  -1903   1038  -1030       N  
ATOM    740  CA  GLY A  51      17.719  53.249   9.387  1.00 29.02           C  
ANISOU  740  CA  GLY A  51     4841   3015   3168  -1983   1083  -1004       C  
ATOM    741  C   GLY A  51      17.688  52.689   7.972  1.00 33.12           C  
ANISOU  741  C   GLY A  51     5351   3548   3686  -1957   1055   -923       C  
ATOM    742  O   GLY A  51      16.703  52.082   7.564  1.00 29.75           O  
ANISOU  742  O   GLY A  51     4922   3080   3303  -1849   1019   -870       O  
ATOM    743  H   GLY A  51      16.445  51.952  10.131  1.00 33.35           H  
ATOM    744  HA2 GLY A  51      17.179  54.054   9.416  1.00 34.82           H  
ATOM    745  HA3 GLY A  51      18.634  53.480   9.611  1.00 34.82           H  
ATOM    746  N   LYS A  52      18.768  52.887   7.220  1.00 32.75           N  
ANISOU  746  N   LYS A  52     5297   3563   3582  -2065   1077   -919       N  
ATOM    747  CA  LYS A  52      18.867  52.328   5.863  1.00 33.84           C  
ANISOU  747  CA  LYS A  52     5423   3740   3695  -2066   1064   -856       C  
ATOM    748  C   LYS A  52      19.240  50.848   5.918  1.00 32.80           C  
ANISOU  748  C   LYS A  52     5094   3808   3560  -2018   1014   -880       C  
ATOM    749  O   LYS A  52      20.113  50.429   6.674  1.00 26.98           O  
ANISOU  749  O   LYS A  52     4224   3210   2817  -2045    996   -945       O  
ATOM    750  CB  LYS A  52      19.908  53.111   5.048  1.00 33.94           C  
ANISOU  750  CB  LYS A  52     5504   3751   3642  -2212   1122   -859       C  
ATOM    751  CG  LYS A  52      20.109  52.641   3.615  1.00 39.22           C  
ANISOU  751  CG  LYS A  52     6177   4468   4257  -2244   1126   -807       C  
ATOM    752  CD  LYS A  52      21.218  53.429   2.928  1.00 42.14           C  
ANISOU  752  CD  LYS A  52     6611   4850   4551  -2405   1196   -831       C  
ATOM    753  H   LYS A  52      19.457  53.338   7.466  1.00 39.30           H  
ATOM    754  HA  LYS A  52      18.008  52.409   5.419  1.00 40.61           H  
ATOM    755  HB2 LYS A  52      19.633  54.041   5.013  1.00 40.73           H  
ATOM    756  HB3 LYS A  52      20.764  53.044   5.499  1.00 40.73           H  
ATOM    757  HG2 LYS A  52      20.358  51.704   3.616  1.00 47.07           H  
ATOM    758  HG3 LYS A  52      19.288  52.772   3.116  1.00 47.07           H  
ATOM    759  N   LEU A  53      18.588  50.039   5.102  1.00 28.92           N  
ANISOU  759  N   LEU A  53     4582   3324   3080  -1944    982   -823       N  
ATOM    760  CA  LEU A  53      18.953  48.637   5.033  1.00 24.73           C  
ANISOU  760  CA  LEU A  53     3867   2969   2561  -1894    937   -847       C  
ATOM    761  C   LEU A  53      20.308  48.467   4.327  1.00 28.88           C  
ANISOU  761  C   LEU A  53     4311   3618   3045  -1990    975   -895       C  
ATOM    762  O   LEU A  53      20.506  48.992   3.245  1.00 29.90           O  
ANISOU  762  O   LEU A  53     4540   3704   3118  -2070   1028   -872       O  
ATOM    763  CB  LEU A  53      17.866  47.886   4.278  1.00 25.82           C  
ANISOU  763  CB  LEU A  53     4017   3074   2720  -1801    901   -779       C  
ATOM    764  CG  LEU A  53      17.835  46.388   4.469  1.00 22.15           C  
ANISOU  764  CG  LEU A  53     3370   2752   2294  -1711    841   -799       C  
ATOM    765  CD1 LEU A  53      17.465  46.060   5.933  1.00 21.45           C  
ANISOU  765  CD1 LEU A  53     3217   2683   2250  -1638    788   -825       C  
ATOM    766  CD2 LEU A  53      16.816  45.780   3.511  1.00 23.98           C  
ANISOU  766  CD2 LEU A  53     3632   2945   2533  -1648    819   -732       C  
ATOM    767  H   LEU A  53      17.940  50.272   4.586  1.00 34.70           H  
ATOM    768  HA  LEU A  53      19.020  48.271   5.929  1.00 29.68           H  
ATOM    769  HB2 LEU A  53      17.005  48.230   4.562  1.00 30.99           H  
ATOM    770  HB3 LEU A  53      17.984  48.053   3.330  1.00 30.99           H  
ATOM    771  HG  LEU A  53      18.709  46.014   4.275  1.00 26.58           H  
ATOM    772 HD11 LEU A  53      17.448  45.096   6.045  1.00 25.74           H  
ATOM    773 HD12 LEU A  53      18.130  46.450   6.522  1.00 25.74           H  
ATOM    774 HD13 LEU A  53      16.591  46.432   6.128  1.00 25.74           H  
ATOM    775 HD21 LEU A  53      16.800  44.818   3.637  1.00 28.77           H  
ATOM    776 HD22 LEU A  53      15.942  46.154   3.701  1.00 28.77           H  
ATOM    777 HD23 LEU A  53      17.075  45.990   2.600  1.00 28.77           H  
ATOM    778  N   PRO A  54      21.246  47.719   4.928  1.00 32.71           N  
ANISOU  778  N   PRO A  54     4615   4251   3563  -1981    943   -963       N  
ATOM    779  CA  PRO A  54      22.592  47.588   4.337  1.00 32.55           C  
ANISOU  779  CA  PRO A  54     4499   4338   3529  -2067    986  -1030       C  
ATOM    780  C   PRO A  54      22.696  46.567   3.198  1.00 27.05           C  
ANISOU  780  C   PRO A  54     3718   3719   2840  -2033    997  -1039       C  
ATOM    781  O   PRO A  54      23.767  46.435   2.594  1.00 28.78           O  
ANISOU  781  O   PRO A  54     3863   4021   3053  -2104   1049  -1110       O  
ATOM    782  CB  PRO A  54      23.434  47.106   5.513  1.00 35.55           C  
ANISOU  782  CB  PRO A  54     4713   4823   3973  -2048    921  -1087       C  
ATOM    783  CG  PRO A  54      22.443  46.323   6.352  1.00 30.64           C  
ANISOU  783  CG  PRO A  54     4054   4194   3394  -1919    828  -1040       C  
ATOM    784  CD  PRO A  54      21.158  47.072   6.245  1.00 25.37           C  
ANISOU  784  CD  PRO A  54     3572   3381   2686  -1904    861   -980       C  
ATOM    785  HA  PRO A  54      22.919  48.450   4.035  1.00 39.05           H  
ATOM    786  HB2 PRO A  54      24.151  46.535   5.197  1.00 42.67           H  
ATOM    787  HB3 PRO A  54      23.783  47.866   6.005  1.00 42.67           H  
ATOM    788  HG2 PRO A  54      22.348  45.427   5.992  1.00 36.77           H  
ATOM    789  HG3 PRO A  54      22.746  46.293   7.272  1.00 36.77           H  
ATOM    790  HD2 PRO A  54      20.406  46.460   6.271  1.00 30.44           H  
ATOM    791  HD3 PRO A  54      21.097  47.740   6.946  1.00 30.44           H  
ATOM    792  N   VAL A  55      21.604  45.860   2.940  1.00 24.63           N  
ANISOU  792  N   VAL A  55     3422   3387   2550  -1930    954   -980       N  
ATOM    793  CA  VAL A  55      21.517  44.883   1.865  1.00 26.80           C  
ANISOU  793  CA  VAL A  55     3633   3723   2825  -1895    963   -988       C  
ATOM    794  C   VAL A  55      20.233  45.190   1.082  1.00 23.77           C  
ANISOU  794  C   VAL A  55     3421   3228   2382  -1889    965   -892       C  
ATOM    795  O   VAL A  55      19.359  45.902   1.569  1.00 25.09           O  
ANISOU  795  O   VAL A  55     3712   3271   2548  -1869    942   -824       O  
ATOM    796  CB  VAL A  55      21.499  43.432   2.418  1.00 22.99           C  
ANISOU  796  CB  VAL A  55     2955   3333   2447  -1758    880  -1010       C  
ATOM    797  CG1 VAL A  55      22.762  43.143   3.227  1.00 25.78           C  
ANISOU  797  CG1 VAL A  55     3146   3773   2876  -1761    849  -1083       C  
ATOM    798  CG2 VAL A  55      20.222  43.155   3.286  1.00 21.52           C  
ANISOU  798  CG2 VAL A  55     2797   3087   2294  -1650    798   -937       C  
ATOM    799  H   VAL A  55      20.875  45.932   3.390  1.00 29.56           H  
ATOM    800  HA  VAL A  55      22.277  44.981   1.269  1.00 32.15           H  
ATOM    801  HB  VAL A  55      21.483  42.816   1.669  1.00 27.59           H  
ATOM    802 HG11 VAL A  55      22.722  42.233   3.559  1.00 30.94           H  
ATOM    803 HG12 VAL A  55      23.536  43.253   2.653  1.00 30.94           H  
ATOM    804 HG13 VAL A  55      22.809  43.765   3.970  1.00 30.94           H  
ATOM    805 HG21 VAL A  55      20.253  42.241   3.609  1.00 25.83           H  
ATOM    806 HG22 VAL A  55      20.211  43.771   4.035  1.00 25.83           H  
ATOM    807 HG23 VAL A  55      19.433  43.286   2.737  1.00 25.83           H  
ATOM    808  N   PRO A  56      20.120  44.681  -0.142  1.00 23.89           N  
ANISOU  808  N   PRO A  56     3448   3277   2350  -1910    990   -889       N  
ATOM    809  CA  PRO A  56      18.894  44.935  -0.901  1.00 23.66           C  
ANISOU  809  CA  PRO A  56     3583   3142   2266  -1908    970   -780       C  
ATOM    810  C   PRO A  56      17.718  44.149  -0.343  1.00 21.99           C  
ANISOU  810  C   PRO A  56     3316   2909   2131  -1768    891   -729       C  
ATOM    811  O   PRO A  56      17.889  43.015   0.117  1.00 21.00           O  
ANISOU  811  O   PRO A  56     3013   2887   2079  -1677    857   -784       O  
ATOM    812  CB  PRO A  56      19.246  44.439  -2.309  1.00 24.39           C  
ANISOU  812  CB  PRO A  56     3678   3310   2278  -1981   1015   -811       C  
ATOM    813  CG  PRO A  56      20.757  44.457  -2.334  1.00 25.53           C  
ANISOU  813  CG  PRO A  56     3719   3556   2423  -2060   1088   -940       C  
ATOM    814  CD  PRO A  56      21.153  44.040  -0.965  1.00 24.66           C  
ANISOU  814  CD  PRO A  56     3440   3496   2435  -1960   1046   -987       C  
ATOM    815  HA  PRO A  56      18.684  45.882  -0.923  1.00 28.40           H  
ATOM    816  HB2 PRO A  56      18.909  43.538  -2.436  1.00 29.27           H  
ATOM    817  HB3 PRO A  56      18.881  45.044  -2.974  1.00 29.27           H  
ATOM    818  HG2 PRO A  56      21.083  43.827  -2.995  1.00 30.63           H  
ATOM    819  HG3 PRO A  56      21.072  45.355  -2.526  1.00 30.63           H  
ATOM    820  HD2 PRO A  56      21.111  43.075  -0.876  1.00 29.60           H  
ATOM    821  HD3 PRO A  56      22.031  44.386  -0.743  1.00 29.60           H  
ATOM    822  N   TRP A  57      16.543  44.756  -0.412  1.00 21.89           N  
ANISOU  822  N   TRP A  57     3460   2749   2110  -1749    859   -621       N  
ATOM    823  CA  TRP A  57      15.330  44.151   0.099  1.00 20.55           C  
ANISOU  823  CA  TRP A  57     3258   2535   2015  -1628    791   -576       C  
ATOM    824  C   TRP A  57      15.079  42.775  -0.503  1.00 19.64           C  
ANISOU  824  C   TRP A  57     3017   2537   1907  -1576    766   -589       C  
ATOM    825  O   TRP A  57      14.708  41.849   0.219  1.00 18.42           O  
ANISOU  825  O   TRP A  57     2728   2435   1836  -1471    715   -619       O  
ATOM    826  CB  TRP A  57      14.137  45.066  -0.144  1.00 21.03           C  
ANISOU  826  CB  TRP A  57     3522   2392   2075  -1617    762   -453       C  
ATOM    827  CG  TRP A  57      14.008  46.145   0.890  1.00 21.51           C  
ANISOU  827  CG  TRP A  57     3664   2317   2191  -1599    771   -464       C  
ATOM    828  CD1 TRP A  57      14.297  47.480   0.744  1.00 25.14           C  
ANISOU  828  CD1 TRP A  57     4280   2653   2620  -1672    803   -431       C  
ATOM    829  CD2 TRP A  57      13.541  45.977   2.218  1.00 20.67           C  
ANISOU  829  CD2 TRP A  57     3487   2194   2173  -1495    747   -518       C  
ATOM    830  NE1 TRP A  57      14.032  48.153   1.925  1.00 23.90           N  
ANISOU  830  NE1 TRP A  57     4148   2395   2539  -1622    811   -471       N  
ATOM    831  CE2 TRP A  57      13.567  47.247   2.843  1.00 21.73           C  
ANISOU  831  CE2 TRP A  57     3741   2187   2329  -1524    781   -529       C  
ATOM    832  CE3 TRP A  57      13.096  44.874   2.945  1.00 19.28           C  
ANISOU  832  CE3 TRP A  57     3156   2120   2050  -1363    695   -554       C  
ATOM    833  CZ2 TRP A  57      13.161  47.435   4.166  1.00 24.82           C  
ANISOU  833  CZ2 TRP A  57     4107   2536   2787  -1454    784   -593       C  
ATOM    834  CZ3 TRP A  57      12.708  45.054   4.254  1.00 19.03           C  
ANISOU  834  CZ3 TRP A  57     3107   2050   2072  -1303    692   -604       C  
ATOM    835  CH2 TRP A  57      12.734  46.327   4.856  1.00 21.04           C  
ANISOU  835  CH2 TRP A  57     3491   2160   2342  -1362    744   -634       C  
ATOM    836  H   TRP A  57      16.423  45.534  -0.758  1.00 26.27           H  
ATOM    837  HA  TRP A  57      15.422  44.038   1.058  1.00 24.66           H  
ATOM    838  HB2 TRP A  57      14.238  45.492  -1.009  1.00 25.23           H  
ATOM    839  HB3 TRP A  57      13.325  44.537  -0.127  1.00 25.23           H  
ATOM    840  HD1 TRP A  57      14.621  47.874  -0.033  1.00 30.17           H  
ATOM    841  HE1 TRP A  57      14.141  48.995   2.059  1.00 28.68           H  
ATOM    842  HE3 TRP A  57      13.070  44.030   2.556  1.00 23.14           H  
ATOM    843  HZ2 TRP A  57      13.188  48.275   4.567  1.00 29.78           H  
ATOM    844  HZ3 TRP A  57      12.408  44.324   4.745  1.00 22.83           H  
ATOM    845  HH2 TRP A  57      12.464  46.418   5.741  1.00 25.25           H  
ATOM    846  N   PRO A  58      15.280  42.622  -1.821  1.00 20.37           N  
ANISOU  846  N   PRO A  58     3158   2673   1908  -1652    798   -571       N  
ATOM    847  CA  PRO A  58      14.972  41.293  -2.375  1.00 19.59           C  
ANISOU  847  CA  PRO A  58     2942   2682   1820  -1598    778   -595       C  
ATOM    848  C   PRO A  58      15.805  40.167  -1.779  1.00 18.90           C  
ANISOU  848  C   PRO A  58     2628   2727   1825  -1517    775   -721       C  
ATOM    849  O   PRO A  58      15.356  39.033  -1.838  1.00 18.01           O  
ANISOU  849  O   PRO A  58     2406   2672   1766  -1428    736   -736       O  
ATOM    850  CB  PRO A  58      15.262  41.437  -3.885  1.00 20.90           C  
ANISOU  850  CB  PRO A  58     3213   2879   1849  -1717    822   -581       C  
ATOM    851  CG  PRO A  58      15.067  42.904  -4.167  1.00 22.78           C  
ANISOU  851  CG  PRO A  58     3679   2973   2006  -1806    823   -472       C  
ATOM    852  CD  PRO A  58      15.522  43.634  -2.870  1.00 21.99           C  
ANISOU  852  CD  PRO A  58     3552   2813   1992  -1781    836   -513       C  
ATOM    853  HA  PRO A  58      14.031  41.091  -2.251  1.00 23.51           H  
ATOM    854  HB2 PRO A  58      16.175  41.168  -4.072  1.00 25.08           H  
ATOM    855  HB3 PRO A  58      14.633  40.901  -4.393  1.00 25.08           H  
ATOM    856  HG2 PRO A  58      15.618  43.168  -4.921  1.00 27.34           H  
ATOM    857  HG3 PRO A  58      14.130  43.080  -4.349  1.00 27.34           H  
ATOM    858  HD2 PRO A  58      16.466  43.855  -2.918  1.00 26.39           H  
ATOM    859  HD3 PRO A  58      14.978  44.421  -2.714  1.00 26.39           H  
ATOM    860  N   THR A  59      16.955  40.462  -1.176  1.00 19.40           N  
ANISOU  860  N   THR A  59     2628   2826   1918  -1537    804   -796       N  
ATOM    861  CA  THR A  59      17.729  39.394  -0.565  1.00 18.98           C  
ANISOU  861  CA  THR A  59     2373   2870   1969  -1445    778   -884       C  
ATOM    862  C   THR A  59      17.133  38.899   0.734  1.00 17.74           C  
ANISOU  862  C   THR A  59     2137   2697   1905  -1320    685   -849       C  
ATOM    863  O   THR A  59      17.569  37.870   1.250  1.00 17.39           O  
ANISOU  863  O   THR A  59     1942   2711   1953  -1227    633   -887       O  
ATOM    864  CB  THR A  59      19.198  39.774  -0.291  1.00 21.16           C  
ANISOU  864  CB  THR A  59     2588   3192   2261  -1506    824   -968       C  
ATOM    865  OG1 THR A  59      19.270  40.753   0.756  1.00 21.37           O  
ANISOU  865  OG1 THR A  59     2671   3163   2286  -1532    806   -935       O  
ATOM    866  CG2 THR A  59      19.864  40.306  -1.570  1.00 24.80           C  
ANISOU  866  CG2 THR A  59     3132   3671   2618  -1650    925  -1020       C  
ATOM    867  H   THR A  59      17.298  41.247  -1.110  1.00 23.28           H  
ATOM    868  HA  THR A  59      17.739  38.643  -1.179  1.00 22.78           H  
ATOM    869  HB  THR A  59      19.681  38.980  -0.012  1.00 25.39           H  
ATOM    870  HG1 THR A  59      18.848  41.444   0.532  1.00 25.64           H  
ATOM    871 HG21 THR A  59      20.787  40.543  -1.389  1.00 29.76           H  
ATOM    872 HG22 THR A  59      19.842  39.627  -2.262  1.00 29.76           H  
ATOM    873 HG23 THR A  59      19.392  41.093  -1.886  1.00 29.76           H  
ATOM    874  N   LEU A  60      16.171  39.633   1.289  1.00 17.38           N  
ANISOU  874  N   LEU A  60     2204   2559   1842  -1321    660   -777       N  
ATOM    875  CA  LEU A  60      15.544  39.235   2.549  1.00 16.33           C  
ANISOU  875  CA  LEU A  60     2018   2410   1777  -1222    581   -757       C  
ATOM    876  C   LEU A  60      14.170  38.587   2.381  1.00 15.33           C  
ANISOU  876  C   LEU A  60     1895   2256   1676  -1145    533   -710       C  
ATOM    877  O   LEU A  60      13.618  38.078   3.344  1.00 14.59           O  
ANISOU  877  O   LEU A  60     1750   2163   1630  -1052    469   -698       O  
ATOM    878  CB  LEU A  60      15.385  40.454   3.459  1.00 16.71           C  
ANISOU  878  CB  LEU A  60     2182   2368   1801  -1270    592   -742       C  
ATOM    879  CG  LEU A  60      16.662  41.199   3.816  1.00 17.78           C  
ANISOU  879  CG  LEU A  60     2317   2527   1911  -1353    631   -787       C  
ATOM    880  CD1 LEU A  60      16.324  42.342   4.760  1.00 18.16           C  
ANISOU  880  CD1 LEU A  60     2487   2477   1938  -1389    643   -776       C  
ATOM    881  CD2 LEU A  60      17.662  40.238   4.441  1.00 24.63           C  
ANISOU  881  CD2 LEU A  60     3008   3507   2842  -1304    575   -835       C  
ATOM    882  H   LEU A  60      15.863  40.364   0.957  1.00 20.86           H  
ATOM    883  HA  LEU A  60      16.121  38.598   3.000  1.00 19.60           H  
ATOM    884  HB2 LEU A  60      14.795  41.087   3.020  1.00 20.06           H  
ATOM    885  HB3 LEU A  60      14.980  40.163   4.291  1.00 20.06           H  
ATOM    886  HG  LEU A  60      17.055  41.571   3.011  1.00 21.34           H  
ATOM    887 HD11 LEU A  60      17.139  42.816   4.987  1.00 21.80           H  
ATOM    888 HD12 LEU A  60      15.703  42.943   4.319  1.00 21.80           H  
ATOM    889 HD13 LEU A  60      15.918  41.979   5.563  1.00 21.80           H  
ATOM    890 HD21 LEU A  60      18.470  40.725   4.663  1.00 29.55           H  
ATOM    891 HD22 LEU A  60      17.273  39.857   5.244  1.00 29.55           H  
ATOM    892 HD23 LEU A  60      17.863  39.534   3.804  1.00 29.55           H  
ATOM    893  N   VAL A  61      13.609  38.621   1.171  1.00 15.49           N  
ANISOU  893  N   VAL A  61     1990   2251   1643  -1143    552   -661       N  
ATOM    894  CA  VAL A  61      12.270  38.077   0.971  1.00 14.72           C  
ANISOU  894  CA  VAL A  61     1909   2126   1560  -1002    485   -587       C  
ATOM    895  C   VAL A  61      12.133  36.640   1.483  1.00 14.26           C  
ANISOU  895  C   VAL A  61     1686   2149   1584   -904    429   -622       C  
ATOM    896  O   VAL A  61      11.221  36.350   2.246  1.00 13.80           O  
ANISOU  896  O   VAL A  61     1618   2061   1565   -797    373   -583       O  
ATOM    897  CB  VAL A  61      11.864  38.180  -0.517  1.00 15.28           C  
ANISOU  897  CB  VAL A  61     2071   2185   1548  -1033    497   -532       C  
ATOM    898  CG1 VAL A  61      10.575  37.428  -0.812  1.00 15.19           C  
ANISOU  898  CG1 VAL A  61     2042   2171   1560   -898    417   -470       C  
ATOM    899  CG2 VAL A  61      11.684  39.633  -0.857  1.00 19.01           C  
ANISOU  899  CG2 VAL A  61     2733   2538   1953  -1100    517   -456       C  
ATOM    900  H   VAL A  61      13.976  38.946   0.464  1.00 18.58           H  
ATOM    901  HA  VAL A  61      11.645  38.620   1.476  1.00 17.67           H  
ATOM    902  HB  VAL A  61      12.570  37.816  -1.074  1.00 18.33           H  
ATOM    903 HG11 VAL A  61      10.363  37.522  -1.754  1.00 18.23           H  
ATOM    904 HG12 VAL A  61      10.699  36.492  -0.592  1.00 18.23           H  
ATOM    905 HG13 VAL A  61       9.861  37.803  -0.273  1.00 18.23           H  
ATOM    906 HG21 VAL A  61      11.429  39.709  -1.790  1.00 22.82           H  
ATOM    907 HG22 VAL A  61      10.988  40.005  -0.293  1.00 22.82           H  
ATOM    908 HG23 VAL A  61      12.520  40.099  -0.704  1.00 22.82           H  
ATOM    909  N   THR A  62      13.036  35.729   1.104  1.00 13.88           N  
ANISOU  909  N   THR A  62     1506   2195   1572   -944    447   -702       N  
ATOM    910  CA  THR A  62      12.846  34.333   1.509  1.00 15.71           C  
ANISOU  910  CA  THR A  62     1602   2472   1894   -831    380   -717       C  
ATOM    911  C   THR A  62      12.939  34.148   3.042  1.00 13.50           C  
ANISOU  911  C   THR A  62     1281   2180   1668   -768    311   -697       C  
ATOM    912  O   THR A  62      12.274  33.262   3.616  1.00 12.13           O  
ANISOU  912  O   THR A  62     1058   2006   1544   -676    243   -665       O  
ATOM    913  CB  THR A  62      13.830  33.404   0.810  1.00 13.63           C  
ANISOU  913  CB  THR A  62     1251   2261   1667   -807    402   -781       C  
ATOM    914  OG1 THR A  62      15.160  33.905   0.980  1.00 14.50           O  
ANISOU  914  OG1 THR A  62     1346   2385   1778   -866    442   -831       O  
ATOM    915  CG2 THR A  62      13.522  33.345  -0.695  1.00 14.04           C  
ANISOU  915  CG2 THR A  62     1347   2340   1646   -874    466   -806       C  
ATOM    916  H   THR A  62      13.738  35.885   0.632  1.00 16.65           H  
ATOM    917  HA  THR A  62      11.955  34.060   1.241  1.00 18.85           H  
ATOM    918  HB  THR A  62      13.763  32.510   1.181  1.00 16.36           H  
ATOM    919  HG1 THR A  62      15.349  33.945   1.798  1.00 17.40           H  
ATOM    920 HG21 THR A  62      14.149  32.753  -1.139  1.00 16.85           H  
ATOM    921 HG22 THR A  62      12.621  33.013  -0.836  1.00 16.85           H  
ATOM    922 HG23 THR A  62      13.596  34.231  -1.083  1.00 16.85           H  
ATOM    923  N   THR A  63      13.735  34.995   3.694  1.00 13.33           N  
ANISOU  923  N   THR A  63     1291   2148   1624   -832    329   -712       N  
ATOM    924  CA  THR A  63      13.903  34.918   5.138  1.00 13.26           C  
ANISOU  924  CA  THR A  63     1261   2138   1638   -808    263   -694       C  
ATOM    925  C   THR A  63      12.645  35.434   5.845  1.00 15.56           C  
ANISOU  925  C   THR A  63     1638   2380   1893   -813    259   -667       C  
ATOM    926  O   THR A  63      12.187  34.858   6.839  1.00 12.46           O  
ANISOU  926  O   THR A  63     1221   1998   1517   -767    198   -643       O  
ATOM    927  CB  THR A  63      15.115  35.756   5.553  1.00 14.23           C  
ANISOU  927  CB  THR A  63     1398   2270   1739   -891    287   -726       C  
ATOM    928  OG1 THR A  63      16.297  35.182   4.981  1.00 14.80           O  
ANISOU  928  OG1 THR A  63     1370   2386   1866   -881    290   -767       O  
ATOM    929  CG2 THR A  63      15.298  35.813   7.079  1.00 14.36           C  
ANISOU  929  CG2 THR A  63     1412   2290   1753   -896    215   -707       C  
ATOM    930  H   THR A  63      14.189  35.622   3.320  1.00 15.99           H  
ATOM    931  HA  THR A  63      14.055  33.998   5.402  1.00 15.91           H  
ATOM    932  HB  THR A  63      15.007  36.662   5.224  1.00 17.08           H  
ATOM    933  HG1 THR A  63      16.236  35.175   4.144  1.00 17.76           H  
ATOM    934 HG21 THR A  63      16.075  36.351   7.300  1.00 17.23           H  
ATOM    935 HG22 THR A  63      14.514  36.207   7.492  1.00 17.23           H  
ATOM    936 HG23 THR A  63      15.425  34.918   7.431  1.00 17.23           H  
ATOM    937  N   LEU A  64      12.096  36.524   5.319  1.00 13.01           N  
ANISOU  937  N   LEU A  64     1442   1982   1517   -835    324   -649       N  
ATOM    938  CA  LEU A  64      10.982  37.215   5.955  1.00 12.94           C  
ANISOU  938  CA  LEU A  64     1541   1888   1487   -783    337   -611       C  
ATOM    939  C   LEU A  64       9.696  36.436   5.696  1.00 16.68           C  
ANISOU  939  C   LEU A  64     1988   2353   1996   -656    302   -558       C  
ATOM    940  O   LEU A  64       8.892  36.255   6.598  1.00 15.59           O  
ANISOU  940  O   LEU A  64     1853   2200   1871   -604    290   -548       O  
ATOM    941  CB  LEU A  64      10.852  38.637   5.394  1.00 13.67           C  
ANISOU  941  CB  LEU A  64     1775   1876   1542   -827    404   -596       C  
ATOM    942  CG  LEU A  64      11.999  39.605   5.747  1.00 14.96           C  
ANISOU  942  CG  LEU A  64     1989   2027   1668   -967    453   -652       C  
ATOM    943  CD1 LEU A  64      11.983  40.870   4.885  1.00 20.00           C  
ANISOU  943  CD1 LEU A  64     2771   2555   2272  -1024    514   -624       C  
ATOM    944  CD2 LEU A  64      11.950  40.017   7.225  1.00 14.79           C  
ANISOU  944  CD2 LEU A  64     1998   1987   1636   -995    455   -693       C  
ATOM    945  H   LEU A  64      12.354  36.887   4.584  1.00 15.61           H  
ATOM    946  HA  LEU A  64      11.130  37.268   6.912  1.00 15.53           H  
ATOM    947  HB2 LEU A  64      10.807  38.581   4.427  1.00 16.40           H  
ATOM    948  HB3 LEU A  64      10.030  39.025   5.733  1.00 16.40           H  
ATOM    949  HG  LEU A  64      12.844  39.154   5.594  1.00 17.95           H  
ATOM    950 HD11 LEU A  64      12.722  41.441   5.149  1.00 24.00           H  
ATOM    951 HD12 LEU A  64      12.075  40.618   3.953  1.00 24.00           H  
ATOM    952 HD13 LEU A  64      11.142  41.334   5.021  1.00 24.00           H  
ATOM    953 HD21 LEU A  64      12.685  40.624   7.407  1.00 17.75           H  
ATOM    954 HD22 LEU A  64      11.105  40.459   7.401  1.00 17.75           H  
ATOM    955 HD23 LEU A  64      12.031  39.224   7.776  1.00 17.75           H  
HETATM  956  N1  CRO A  66       9.558  35.883   4.493  1.00 15.01           N  
ANISOU  956  N1  CRO A  66     1743   2166   1795   -624    290   -536       N  
HETATM  957  CA1 CRO A  66       8.415  35.088   4.161  1.00 11.75           C  
ANISOU  957  CA1 CRO A  66     1294   1755   1414   -519    250   -494       C  
HETATM  958  CB1 CRO A  66       7.463  35.719   3.145  1.00 20.94           C  
ANISOU  958  CB1 CRO A  66     2544   2850   2563   -474    252   -435       C  
HETATM  959  CG1 CRO A  66       7.020  37.003   3.745  1.00 20.14           C  
ANISOU  959  CG1 CRO A  66     2543   2643   2466   -465    285   -420       C  
HETATM  960  OG1 CRO A  66       8.090  36.070   1.959  1.00 23.20           O  
ANISOU  960  OG1 CRO A  66     2880   3143   2792   -548    272   -430       O  
HETATM  961  C1  CRO A  66       8.935  33.796   3.598  1.00 13.40           C  
ANISOU  961  C1  CRO A  66     1390   2049   1655   -518    218   -521       C  
HETATM  962  N2  CRO A  66       9.097  33.444   2.308  1.00 13.42           N  
ANISOU  962  N2  CRO A  66     1377   2081   1642   -535    229   -531       N  
HETATM  963  N3  CRO A  66       9.410  32.737   4.460  1.00 12.57           N  
ANISOU  963  N3  CRO A  66     1174   1997   1605   -509    170   -548       N  
HETATM  964  C2  CRO A  66       9.878  31.658   3.627  1.00 11.07           C  
ANISOU  964  C2  CRO A  66      883   1858   1465   -503    155   -585       C  
HETATM  965  O2  CRO A  66      10.323  30.600   4.024  1.00 14.57           O  
ANISOU  965  O2  CRO A  66     1263   2307   1968   -451    105   -579       O  
HETATM  966  CA2 CRO A  66       9.656  32.127   2.274  1.00 16.54           C  
ANISOU  966  CA2 CRO A  66     1640   2544   2102   -526    204   -584       C  
HETATM  967  CA3 CRO A  66       9.464  32.756   5.911  1.00 11.12           C  
ANISOU  967  CA3 CRO A  66      990   1812   1423   -520    140   -542       C  
HETATM  968  C3  CRO A  66       8.291  32.084   6.521  1.00 13.28           C  
ANISOU  968  C3  CRO A  66     1257   2076   1715   -447    108   -500       C  
HETATM  969  O3  CRO A  66       8.450  31.672   7.724  1.00 15.33           O  
ANISOU  969  O3  CRO A  66     1500   2356   1970   -471     65   -492       O  
HETATM  970  CB2 CRO A  66      10.007  31.340   1.172  1.00 16.67           C  
ANISOU  970  CB2 CRO A  66     1593   2607   2132   -544    222   -635       C  
HETATM  971  CG2 CRO A  66      10.044  31.819  -0.262  1.00 17.45           C  
ANISOU  971  CG2 CRO A  66     1771   2719   2140   -615    278   -644       C  
HETATM  972  CD1 CRO A  66      10.584  30.944  -1.222  1.00 14.23           C  
ANISOU  972  CD1 CRO A  66     1287   2373   1746   -657    317   -729       C  
HETATM  973  CD2 CRO A  66       9.569  33.081  -0.639  1.00 13.27           C  
ANISOU  973  CD2 CRO A  66     1391   2134   1516   -646    291   -573       C  
HETATM  974  CE1 CRO A  66      10.643  31.305  -2.555  1.00 15.13           C  
ANISOU  974  CE1 CRO A  66     1485   2513   1751   -750    376   -744       C  
HETATM  975  CE2 CRO A  66       9.634  33.442  -2.011  1.00 19.49           C  
ANISOU  975  CE2 CRO A  66     2267   2937   2202   -732    328   -566       C  
HETATM  976  CZ  CRO A  66      10.149  32.562  -2.956  1.00 18.25           C  
ANISOU  976  CZ  CRO A  66     2047   2860   2029   -792    372   -650       C  
HETATM  977  OH  CRO A  66      10.206  32.877  -4.329  1.00 17.46           O  
ANISOU  977  OH  CRO A  66     2049   2787   1796   -904    415   -649       O  
ATOM    978  N   VAL A  68       7.075  32.229   5.948  1.00 10.19           N  
ANISOU  978  N   VAL A  68      899   1647   1326   -378    130   -470       N  
ATOM    979  CA  VAL A  68       5.863  31.742   6.599  1.00  9.98           C  
ANISOU  979  CA  VAL A  68      861   1610   1319   -320    120   -442       C  
ATOM    980  C   VAL A  68       5.145  30.766   5.656  1.00 13.64           C  
ANISOU  980  C   VAL A  68     1262   2090   1831   -253     86   -421       C  
ATOM    981  O   VAL A  68       4.012  30.963   5.226  1.00 12.40           O  
ANISOU  981  O   VAL A  68     1116   1906   1690   -195     95   -399       O  
ATOM    982  CB  VAL A  68       4.981  32.898   7.093  1.00 10.37           C  
ANISOU  982  CB  VAL A  68      993   1596   1353   -303    184   -444       C  
ATOM    983  CG1 VAL A  68       5.624  33.569   8.323  1.00 11.96           C  
ANISOU  983  CG1 VAL A  68     1251   1793   1499   -387    217   -480       C  
ATOM    984  CG2 VAL A  68       4.744  33.921   5.994  1.00 10.68           C  
ANISOU  984  CG2 VAL A  68     1090   1573   1397   -274    207   -430       C  
ATOM    985  HA  VAL A  68       6.127  31.235   7.382  1.00 11.97           H  
ATOM    986  HB  VAL A  68       4.120  32.543   7.362  1.00 12.45           H  
ATOM    987 HG11 VAL A  68       5.053  34.295   8.619  1.00 14.35           H  
ATOM    988 HG12 VAL A  68       5.716  32.911   9.029  1.00 14.35           H  
ATOM    989 HG13 VAL A  68       6.496  33.914   8.074  1.00 14.35           H  
ATOM    990 HG21 VAL A  68       4.185  34.633   6.342  1.00 12.82           H  
ATOM    991 HG22 VAL A  68       5.598  34.280   5.707  1.00 12.82           H  
ATOM    992 HG23 VAL A  68       4.300  33.486   5.249  1.00 12.82           H  
ATOM    993  N   GLN A  69       5.816  29.658   5.389  1.00 12.29           N  
ANISOU  993  N   GLN A  69     1632   1483   1554    326    -29    -93       N  
ATOM    994  CA  GLN A  69       5.346  28.717   4.388  1.00 13.14           C  
ANISOU  994  CA  GLN A  69     1715   1585   1693    266    -59    -56       C  
ATOM    995  C   GLN A  69       4.116  27.931   4.822  1.00 13.26           C  
ANISOU  995  C   GLN A  69     1695   1669   1675    206    -52     27       C  
ATOM    996  O   GLN A  69       3.524  27.214   4.013  1.00 12.64           O  
ANISOU  996  O   GLN A  69     1581   1597   1625    150    -80     57       O  
ATOM    997  CB  GLN A  69       6.489  27.803   3.976  1.00 12.19           C  
ANISOU  997  CB  GLN A  69     1621   1363   1648    235   -119   -116       C  
ATOM    998  CG  GLN A  69       7.620  28.604   3.339  1.00 11.35           C  
ANISOU  998  CG  GLN A  69     1518   1194   1601    256    -73   -238       C  
ATOM    999  CD  GLN A  69       8.851  27.775   3.024  1.00 16.17           C  
ANISOU  999  CD  GLN A  69     2095   1748   2302    199    -90   -305       C  
ATOM   1000  OE1 GLN A  69       9.346  27.034   3.859  1.00 20.76           O  
ANISOU 1000  OE1 GLN A  69     2654   2297   2936    220   -190   -309       O  
ATOM   1001  NE2 GLN A  69       9.365  27.923   1.811  1.00 24.02           N  
ANISOU 1001  NE2 GLN A  69     3101   2736   3289    131     -4   -344       N  
ATOM   1002  H   GLN A  69       6.549  29.427   5.775  1.00 14.74           H  
ATOM   1003  HA  GLN A  69       5.092  29.223   3.600  1.00 15.77           H  
ATOM   1004  HB2 GLN A  69       6.838  27.350   4.760  1.00 14.63           H  
ATOM   1005  HB3 GLN A  69       6.168  27.157   3.328  1.00 14.63           H  
ATOM   1006  HG2 GLN A  69       7.301  28.990   2.509  1.00 13.62           H  
ATOM   1007  HG3 GLN A  69       7.886  29.310   3.950  1.00 13.62           H  
ATOM   1008 HE21 GLN A  69       9.000  28.467   1.253  1.00 28.82           H  
ATOM   1009 HE22 GLN A  69      10.062  27.475   1.581  1.00 28.82           H  
ATOM   1010  N   CYS A  70       3.719  28.103   6.083  1.00 10.41           N  
ANISOU 1010  N   CYS A  70     1352   1357   1247    196      3     49       N  
ATOM   1011  CA  CYS A  70       2.432  27.630   6.570  1.00 14.00           C  
ANISOU 1011  CA  CYS A  70     1759   1891   1671    112     80     92       C  
ATOM   1012  C   CYS A  70       1.252  28.276   5.864  1.00  9.11           C  
ANISOU 1012  C   CYS A  70      971   1350   1141    147    124     64       C  
ATOM   1013  O   CYS A  70       0.135  27.801   6.019  1.00 11.91           O  
ANISOU 1013  O   CYS A  70     1226   1769   1530     70    184     67       O  
ATOM   1014  CB  CYS A  70       2.313  27.849   8.094  1.00 15.60           C  
ANISOU 1014  CB  CYS A  70     2053   2122   1754     67    173     91       C  
ATOM   1015  SG  CYS A  70       2.800  29.481   8.660  1.00 15.97           S  
ANISOU 1015  SG  CYS A  70     2107   2184   1778    186    227     11       S  
ATOM   1016  H   CYS A  70       4.189  28.500   6.683  1.00 12.50           H  
ATOM   1017  HA  CYS A  70       2.377  26.675   6.409  1.00 16.80           H  
ATOM   1018  HB2 CYS A  70       1.389  27.712   8.355  1.00 18.72           H  
ATOM   1019  HB3 CYS A  70       2.878  27.202   8.544  1.00 18.72           H  
ATOM   1020  HG  CYS A  70       2.103  30.302   8.132  1.00 19.16           H  
ATOM   1021  N   PHE A  71       1.481  29.337   5.071  1.00 10.37           N  
ANISOU 1021  N   PHE A  71     1103   1487   1350    256     79     28       N  
ATOM   1022  CA  PHE A  71       0.401  29.957   4.318  1.00 12.93           C  
ANISOU 1022  CA  PHE A  71     1296   1844   1775    313     43      7       C  
ATOM   1023  C   PHE A  71       0.272  29.449   2.880  1.00 12.62           C  
ANISOU 1023  C   PHE A  71     1272   1758   1763    286    -93     41       C  
ATOM   1024  O   PHE A  71      -0.531  29.956   2.137  1.00 12.90           O  
ANISOU 1024  O   PHE A  71     1237   1789   1874    339   -188     31       O  
ATOM   1025  CB  PHE A  71       0.511  31.479   4.346  1.00 11.83           C  
ANISOU 1025  CB  PHE A  71     1157   1678   1660    442     47    -43       C  
ATOM   1026  CG  PHE A  71       0.137  32.054   5.677  1.00 13.19           C  
ANISOU 1026  CG  PHE A  71     1265   1912   1836    467    190   -105       C  
ATOM   1027  CD1 PHE A  71      -1.195  32.151   6.045  1.00 11.82           C  
ANISOU 1027  CD1 PHE A  71      899   1815   1780    470    266   -169       C  
ATOM   1028  CD2 PHE A  71       1.113  32.459   6.573  1.00 12.90           C  
ANISOU 1028  CD2 PHE A  71     1353   1854   1695    473    257   -122       C  
ATOM   1029  CE1 PHE A  71      -1.558  32.647   7.317  1.00 16.89           C  
ANISOU 1029  CE1 PHE A  71     1490   2514   2414    461    450   -258       C  
ATOM   1030  CE2 PHE A  71       0.754  32.957   7.845  1.00 12.87           C  
ANISOU 1030  CE2 PHE A  71     1329   1903   1659    470    403   -188       C  
ATOM   1031  CZ  PHE A  71      -0.574  33.053   8.195  1.00 12.91           C  
ANISOU 1031  CZ  PHE A  71     1159   1984   1761    458    517   -259       C  
ATOM   1032  H   PHE A  71       2.249  29.707   4.959  1.00 12.44           H  
ATOM   1033  HA  PHE A  71      -0.431  29.732   4.764  1.00 15.52           H  
ATOM   1034  HB2 PHE A  71       1.427  31.734   4.154  1.00 14.20           H  
ATOM   1035  HB3 PHE A  71      -0.085  31.852   3.678  1.00 14.20           H  
ATOM   1036  HD1 PHE A  71      -1.857  31.870   5.455  1.00 14.19           H  
ATOM   1037  HD2 PHE A  71       2.011  32.388   6.342  1.00 15.48           H  
ATOM   1038  HE1 PHE A  71      -2.455  32.717   7.553  1.00 20.27           H  
ATOM   1039  HE2 PHE A  71       1.413  33.235   8.440  1.00 15.45           H  
ATOM   1040  HZ  PHE A  71      -0.810  33.393   9.028  1.00 15.49           H  
ATOM   1041  N   ALA A  72       1.037  28.433   2.529  1.00 12.02           N  
ANISOU 1041  N   ALA A  72     1297   1635   1634    203   -116     69       N  
ATOM   1042  CA  ALA A  72       0.934  27.821   1.217  1.00 13.08           C  
ANISOU 1042  CA  ALA A  72     1473   1724   1772    147   -218     86       C  
ATOM   1043  C   ALA A  72      -0.451  27.211   1.042  1.00 10.21           C  
ANISOU 1043  C   ALA A  72      966   1426   1487     95   -270    103       C  
ATOM   1044  O   ALA A  72      -1.073  26.723   1.999  1.00 10.96           O  
ANISOU 1044  O   ALA A  72      952   1592   1620     44   -182    102       O  
ATOM   1045  CB  ALA A  72       1.974  26.767   1.075  1.00 11.54           C  
ANISOU 1045  CB  ALA A  72     1378   1463   1542     70   -205     80       C  
ATOM   1046  H   ALA A  72       1.631  28.075   3.037  1.00 14.42           H  
ATOM   1047  HA  ALA A  72       1.070  28.491   0.529  1.00 15.69           H  
ATOM   1048  HB1 ALA A  72       1.897  26.365   0.196  1.00 13.84           H  
ATOM   1049  HB2 ALA A  72       2.850  27.172   1.178  1.00 13.84           H  
ATOM   1050  HB3 ALA A  72       1.838  26.095   1.760  1.00 13.84           H  
ATOM   1051  N   ARG A  73      -0.953  27.258  -0.180  1.00 10.91           N  
ANISOU 1051  N   ARG A  73     1067   1483   1596     91   -412    108       N  
ATOM   1052  CA  ARG A  73      -2.189  26.554  -0.498  1.00 11.72           C  
ANISOU 1052  CA  ARG A  73     1022   1635   1796     29   -495    105       C  
ATOM   1053  C   ARG A  73      -1.826  25.125  -0.848  1.00 16.71           C  
ANISOU 1053  C   ARG A  73     1738   2236   2375   -111   -487    130       C  
ATOM   1054  O   ARG A  73      -1.149  24.904  -1.844  1.00 13.70           O  
ANISOU 1054  O   ARG A  73     1522   1772   1910   -145   -549    132       O  
ATOM   1055  CB  ARG A  73      -2.933  27.177  -1.691  1.00 13.20           C  
ANISOU 1055  CB  ARG A  73     1205   1779   2030     86   -716     99       C  
ATOM   1056  CG  ARG A  73      -4.275  26.505  -1.910  1.00 14.78           C  
ANISOU 1056  CG  ARG A  73     1196   2037   2381     31   -821     67       C  
ATOM   1057  CD  ARG A  73      -5.063  27.138  -3.049  1.00 29.85           C  
ANISOU 1057  CD  ARG A  73     3131   3883   4329    102  -1057     53       C  
ATOM   1058  NE  ARG A  73      -4.515  26.749  -4.334  1.00 34.37           N  
ANISOU 1058  NE  ARG A  73     3977   4352   4729     20  -1174    102       N  
ATOM   1059  CZ  ARG A  73      -4.893  25.673  -5.029  1.00 37.81           C  
ANISOU 1059  CZ  ARG A  73     4434   4783   5149    -98  -1240    100       C  
ATOM   1060  NH1 ARG A  73      -5.829  24.852  -4.566  1.00 30.15           N  
ANISOU 1060  NH1 ARG A  73     3223   3906   4328   -154  -1209     56       N  
ATOM   1061  NH2 ARG A  73      -4.322  25.420  -6.201  1.00 43.91           N  
ANISOU 1061  NH2 ARG A  73     5484   5451   5747   -178  -1311    129       N  
ATOM   1062  H   ARG A  73      -0.604  27.685  -0.840  1.00 13.09           H  
ATOM   1063  HA  ARG A  73      -2.777  26.551   0.273  1.00 14.06           H  
ATOM   1064  HB2 ARG A  73      -3.087  28.118  -1.517  1.00 15.84           H  
ATOM   1065  HB3 ARG A  73      -2.401  27.065  -2.495  1.00 15.84           H  
ATOM   1066  HG2 ARG A  73      -4.131  25.571  -2.127  1.00 17.73           H  
ATOM   1067  HG3 ARG A  73      -4.804  26.582  -1.100  1.00 17.73           H  
ATOM   1068  HD2 ARG A  73      -5.985  26.841  -3.007  1.00 35.82           H  
ATOM   1069  HD3 ARG A  73      -5.015  28.104  -2.976  1.00 35.82           H  
ATOM   1070  HE  ARG A  73      -3.901  27.247  -4.673  1.00 41.24           H  
ATOM   1071 HH11 ARG A  73      -6.204  25.011  -3.808  1.00 36.19           H  
ATOM   1072 HH12 ARG A  73      -6.061  24.162  -5.024  1.00 36.19           H  
ATOM   1073 HH21 ARG A  73      -3.714  25.947  -6.506  1.00 52.69           H  
ATOM   1074 HH22 ARG A  73      -4.558  24.728  -6.653  1.00 52.69           H  
ATOM   1075  N   TYR A  74      -2.256  24.179  -0.016  1.00 13.43           N  
ANISOU 1075  N   TYR A  74     1230   1872   2001   -204   -394    138       N  
ATOM   1076  CA  TYR A  74      -2.182  22.762  -0.337  1.00 12.00           C  
ANISOU 1076  CA  TYR A  74     1110   1648   1801   -341   -410    159       C  
ATOM   1077  C   TYR A  74      -3.540  22.325  -0.915  1.00 13.66           C  
ANISOU 1077  C   TYR A  74     1163   1909   2119   -420   -504    134       C  
ATOM   1078  O   TYR A  74      -4.567  22.464  -0.255  1.00 14.95           O  
ANISOU 1078  O   TYR A  74     1123   2160   2396   -442   -443     97       O  
ATOM   1079  CB  TYR A  74      -1.790  21.940   0.912  1.00 14.73           C  
ANISOU 1079  CB  TYR A  74     1510   1979   2108   -417   -279    193       C  
ATOM   1080  CG  TYR A  74      -0.289  21.869   1.113  1.00 12.58           C  
ANISOU 1080  CG  TYR A  74     1412   1606   1762   -361   -274    201       C  
ATOM   1081  CD1 TYR A  74       0.416  22.956   1.615  1.00 12.58           C  
ANISOU 1081  CD1 TYR A  74     1437   1612   1729   -244   -234    185       C  
ATOM   1082  CD2 TYR A  74       0.416  20.719   0.805  1.00 11.06           C  
ANISOU 1082  CD2 TYR A  74     1336   1302   1566   -422   -318    203       C  
ATOM   1083  CE1 TYR A  74       1.780  22.903   1.800  1.00 11.28           C  
ANISOU 1083  CE1 TYR A  74     1389   1355   1543   -194   -242    162       C  
ATOM   1084  CE2 TYR A  74       1.804  20.642   1.009  1.00 12.46           C  
ANISOU 1084  CE2 TYR A  74     1621   1373   1739   -356   -330    171       C  
ATOM   1085  CZ  TYR A  74       2.482  21.744   1.471  1.00 10.67           C  
ANISOU 1085  CZ  TYR A  74     1395   1164   1494   -245   -296    146       C  
ATOM   1086  OH  TYR A  74       3.843  21.716   1.639  1.00 11.45           O  
ANISOU 1086  OH  TYR A  74     1558   1161   1632   -179   -320     84       O  
ATOM   1087  H   TYR A  74      -2.601  24.340   0.755  1.00 16.12           H  
ATOM   1088  HA  TYR A  74      -1.504  22.623  -1.016  1.00 14.40           H  
ATOM   1089  HB2 TYR A  74      -2.179  22.354   1.698  1.00 17.68           H  
ATOM   1090  HB3 TYR A  74      -2.124  21.035   0.813  1.00 17.68           H  
ATOM   1091  HD1 TYR A  74      -0.041  23.739   1.822  1.00 15.09           H  
ATOM   1092  HD2 TYR A  74      -0.040  19.978   0.477  1.00 13.28           H  
ATOM   1093  HE1 TYR A  74       2.235  23.648   2.121  1.00 13.54           H  
ATOM   1094  HE2 TYR A  74       2.269  19.870   0.777  1.00 14.95           H  
ATOM   1095  HH  TYR A  74       4.111  22.453   1.942  1.00 13.74           H  
ATOM   1096  N   PRO A  75      -3.561  21.845  -2.177  1.00 13.82           N  
ANISOU 1096  N   PRO A  75     1267   1871   2114   -470   -652    131       N  
ATOM   1097  CA  PRO A  75      -4.780  21.283  -2.745  1.00 15.59           C  
ANISOU 1097  CA  PRO A  75     1350   2129   2445   -561   -773    100       C  
ATOM   1098  C   PRO A  75      -5.287  20.132  -1.881  1.00 16.35           C  
ANISOU 1098  C   PRO A  75     1345   2263   2605   -714   -634     97       C  
ATOM   1099  O   PRO A  75      -4.480  19.499  -1.184  1.00 15.42           O  
ANISOU 1099  O   PRO A  75     1366   2093   2398   -764   -505    143       O  
ATOM   1100  CB  PRO A  75      -4.322  20.721  -4.087  1.00 17.02           C  
ANISOU 1100  CB  PRO A  75     1739   2211   2515   -618   -898    102       C  
ATOM   1101  CG  PRO A  75      -3.099  21.492  -4.430  1.00 21.21           C  
ANISOU 1101  CG  PRO A  75     2476   2671   2911   -537   -879    116       C  
ATOM   1102  CD  PRO A  75      -2.437  21.783  -3.133  1.00 17.27           C  
ANISOU 1102  CD  PRO A  75     1939   2201   2422   -468   -697    133       C  
ATOM   1103  HA  PRO A  75      -5.468  21.957  -2.868  1.00 18.71           H  
ATOM   1104  HB2 PRO A  75      -4.118  19.777  -3.993  1.00 20.42           H  
ATOM   1105  HB3 PRO A  75      -5.014  20.859  -4.753  1.00 20.42           H  
ATOM   1106  HG2 PRO A  75      -2.522  20.955  -4.996  1.00 25.45           H  
ATOM   1107  HG3 PRO A  75      -3.347  22.315  -4.879  1.00 25.45           H  
ATOM   1108  HD2 PRO A  75      -1.830  21.064  -2.895  1.00 20.72           H  
ATOM   1109  HD3 PRO A  75      -1.979  22.637  -3.172  1.00 20.72           H  
ATOM   1110  N   ASP A  76      -6.581  19.848  -1.980  1.00 18.34           N  
ANISOU 1110  N   ASP A  76     1393   2580   2995   -779   -662     28       N  
ATOM   1111  CA  ASP A  76      -7.213  18.840  -1.134  1.00 23.18           C  
ANISOU 1111  CA  ASP A  76     1914   3226   3666   -951   -492      2       C  
ATOM   1112  C   ASP A  76      -6.496  17.502  -1.176  1.00 21.44           C  
ANISOU 1112  C   ASP A  76     1930   2892   3324  -1065   -451     66       C  
ATOM   1113  O   ASP A  76      -6.326  16.871  -0.134  1.00 20.69           O  
ANISOU 1113  O   ASP A  76     1910   2768   3184  -1171   -292    109       O  
ATOM   1114  CB  ASP A  76      -8.662  18.620  -1.547  1.00 29.75           C  
ANISOU 1114  CB  ASP A  76     2518   4137   4647  -1004   -537   -123       C  
ATOM   1115  CG  ASP A  76      -9.559  19.796  -1.208  1.00 35.46           C  
ANISOU 1115  CG  ASP A  76     2991   4980   5503   -898   -538   -187       C  
ATOM   1116  OD1 ASP A  76      -9.146  20.700  -0.452  1.00 34.35           O  
ANISOU 1116  OD1 ASP A  76     2831   4856   5366   -800   -444   -172       O  
ATOM   1117  OD2 ASP A  76     -10.699  19.795  -1.693  1.00 37.76           O  
ANISOU 1117  OD2 ASP A  76     3110   5320   5918   -897   -635   -257       O  
ATOM   1118  H   ASP A  76      -7.119  20.227  -2.533  1.00 22.01           H  
ATOM   1119  HA  ASP A  76      -7.208  19.152  -0.216  1.00 27.81           H  
ATOM   1120  HB2 ASP A  76      -8.700  18.481  -2.506  1.00 35.70           H  
ATOM   1121  HB3 ASP A  76      -9.006  17.839  -1.085  1.00 35.70           H  
ATOM   1122  N   HIS A  77      -6.068  17.060  -2.356  1.00 18.60           N  
ANISOU 1122  N   HIS A  77     1716   2452   2898  -1038   -586     68       N  
ATOM   1123  CA  HIS A  77      -5.412  15.752  -2.459  1.00 22.42           C  
ANISOU 1123  CA  HIS A  77     2400   2817   3301  -1113   -546     98       C  
ATOM   1124  C   HIS A  77      -3.995  15.726  -1.854  1.00 23.74           C  
ANISOU 1124  C   HIS A  77     2755   2894   3371  -1057   -490    162       C  
ATOM   1125  O   HIS A  77      -3.372  14.666  -1.770  1.00 22.02           O  
ANISOU 1125  O   HIS A  77     2689   2562   3115  -1083   -468    176       O  
ATOM   1126  CB  HIS A  77      -5.370  15.242  -3.912  1.00 19.50           C  
ANISOU 1126  CB  HIS A  77     2123   2390   2894  -1108   -672     55       C  
ATOM   1127  CG  HIS A  77      -4.336  15.915  -4.756  1.00 17.38           C  
ANISOU 1127  CG  HIS A  77     2008   2073   2523  -1003   -739     58       C  
ATOM   1128  ND1 HIS A  77      -4.491  17.198  -5.245  1.00 20.69           N  
ANISOU 1128  ND1 HIS A  77     2395   2541   2925   -914   -843     55       N  
ATOM   1129  CD2 HIS A  77      -3.145  15.476  -5.228  1.00 20.53           C  
ANISOU 1129  CD2 HIS A  77     2592   2368   2839   -977   -702     42       C  
ATOM   1130  CE1 HIS A  77      -3.416  17.538  -5.934  1.00 19.97           C  
ANISOU 1130  CE1 HIS A  77     2494   2376   2718   -868   -848     49       C  
ATOM   1131  NE2 HIS A  77      -2.595  16.505  -5.960  1.00 19.57           N  
ANISOU 1131  NE2 HIS A  77     2555   2242   2639   -905   -749     26       N  
ATOM   1132  H   HIS A  77      -6.142  17.485  -3.100  1.00 22.31           H  
ATOM   1133  HA  HIS A  77      -5.943  15.116  -1.954  1.00 26.90           H  
ATOM   1134  HB2 HIS A  77      -5.174  14.292  -3.905  1.00 23.40           H  
ATOM   1135  HB3 HIS A  77      -6.235  15.396  -4.323  1.00 23.40           H  
ATOM   1136  HD1 HIS A  77      -5.161  17.713  -5.084  1.00 24.83           H  
ATOM   1137  HD2 HIS A  77      -2.763  14.643  -5.073  1.00 24.63           H  
ATOM   1138  HE1 HIS A  77      -3.283  18.349  -6.368  1.00 23.96           H  
ATOM   1139  HE2 HIS A  77      -1.834  16.482  -6.360  1.00 23.49           H  
ATOM   1140  N   MET A  78      -3.487  16.879  -1.431  1.00 16.94           N  
ANISOU 1140  N   MET A  78     1871   2072   2492   -967   -483    187       N  
ATOM   1141  CA  MET A  78      -2.146  16.955  -0.875  1.00 16.44           C  
ANISOU 1141  CA  MET A  78     1963   1917   2366   -900   -452    221       C  
ATOM   1142  C   MET A  78      -2.149  17.390   0.583  1.00 16.72           C  
ANISOU 1142  C   MET A  78     1987   1997   2367   -878   -335    270       C  
ATOM   1143  O   MET A  78      -1.101  17.614   1.153  1.00 18.09           O  
ANISOU 1143  O   MET A  78     2278   2105   2491   -788   -326    289       O  
ATOM   1144  CB  MET A  78      -1.311  17.947  -1.669  1.00 14.85           C  
ANISOU 1144  CB  MET A  78     1805   1709   2131   -757   -498    176       C  
ATOM   1145  CG  MET A  78      -0.963  17.507  -3.056  1.00 20.35           C  
ANISOU 1145  CG  MET A  78     2600   2334   2799   -773   -560    111       C  
ATOM   1146  SD  MET A  78       0.108  18.703  -3.881  1.00 15.79           S  
ANISOU 1146  SD  MET A  78     2128   1723   2150   -679   -565     49       S  
ATOM   1147  CE  MET A  78       1.585  18.658  -2.845  1.00 15.12           C  
ANISOU 1147  CE  MET A  78     2083   1552   2108   -590   -466     22       C  
ATOM   1148  H   MET A  78      -3.901  17.632  -1.456  1.00 20.32           H  
ATOM   1149  HA  MET A  78      -1.724  16.084  -0.944  1.00 19.72           H  
ATOM   1150  HB2 MET A  78      -1.806  18.779  -1.740  1.00 17.83           H  
ATOM   1151  HB3 MET A  78      -0.480  18.103  -1.193  1.00 17.83           H  
ATOM   1152  HG2 MET A  78      -0.495  16.659  -3.015  1.00 24.42           H  
ATOM   1153  HG3 MET A  78      -1.776  17.418  -3.577  1.00 24.42           H  
ATOM   1154  HE1 MET A  78       2.241  19.277  -3.204  1.00 18.14           H  
ATOM   1155  HE2 MET A  78       1.345  18.918  -1.942  1.00 18.14           H  
ATOM   1156  HE3 MET A  78       1.944  17.757  -2.846  1.00 18.14           H  
ATOM   1157  N   LYS A  79      -3.312  17.473   1.202  1.00 16.61           N  
ANISOU 1157  N   LYS A  79     1838   2086   2388   -975   -239    270       N  
ATOM   1158  CA  LYS A  79      -3.364  17.997   2.564  1.00 17.84           C  
ANISOU 1158  CA  LYS A  79     2006   2290   2484   -975    -95    294       C  
ATOM   1159  C   LYS A  79      -2.572  17.170   3.586  1.00 24.08           C  
ANISOU 1159  C   LYS A  79     3059   2944   3149  -1046    -72    378       C  
ATOM   1160  O   LYS A  79      -2.105  17.718   4.584  1.00 19.78           O  
ANISOU 1160  O   LYS A  79     2608   2396   2511   -997    -17    405       O  
ATOM   1161  CB  LYS A  79      -4.811  18.281   2.993  1.00 20.20           C  
ANISOU 1161  CB  LYS A  79     2079   2727   2871  -1085     47    231       C  
ATOM   1162  CG  LYS A  79      -5.276  19.619   2.349  1.00 28.48           C  
ANISOU 1162  CG  LYS A  79     2891   3886   4044   -917    -16    148       C  
ATOM   1163  CD  LYS A  79      -6.645  20.077   2.745  1.00 37.12           C  
ANISOU 1163  CD  LYS A  79     3698   5108   5297   -974    105     36       C  
ATOM   1164  CE  LYS A  79      -7.063  21.286   1.911  1.00 33.14           C  
ANISOU 1164  CE  LYS A  79     2985   4661   4947   -780    -50    -40       C  
ATOM   1165  NZ  LYS A  79      -6.130  22.420   2.003  1.00 36.28           N  
ANISOU 1165  NZ  LYS A  79     3497   5033   5254   -585    -84     -4       N  
ATOM   1166  H   LYS A  79      -4.071  17.240   0.871  1.00 19.94           H  
ATOM   1167  HA  LYS A  79      -2.927  18.862   2.541  1.00 21.41           H  
ATOM   1168  HB2 LYS A  79      -5.391  17.568   2.684  1.00 24.24           H  
ATOM   1169  HB3 LYS A  79      -4.856  18.368   3.959  1.00 24.24           H  
ATOM   1170  HG2 LYS A  79      -4.651  20.316   2.602  1.00 34.18           H  
ATOM   1171  HG3 LYS A  79      -5.271  19.514   1.385  1.00 34.18           H  
ATOM   1172  HD2 LYS A  79      -7.283  19.362   2.591  1.00 44.54           H  
ATOM   1173  HD3 LYS A  79      -6.642  20.335   3.680  1.00 44.54           H  
ATOM   1174  HE2 LYS A  79      -7.116  21.020   0.979  1.00 39.77           H  
ATOM   1175  HE3 LYS A  79      -7.932  21.591   2.215  1.00 39.77           H  
ATOM   1176  HZ1 LYS A  79      -5.324  22.174   1.720  1.00 43.54           H  
ATOM   1177  HZ2 LYS A  79      -6.421  23.095   1.500  1.00 43.54           H  
ATOM   1178  HZ3 LYS A  79      -6.069  22.695   2.848  1.00 43.54           H  
ATOM   1179  N  AGLN A  80      -2.390  15.877   3.324  0.62 16.50           N  
ANISOU 1179  N  AGLN A  80     2235   1849   2184  -1152   -145    416       N  
ATOM   1180  N  BGLN A  80      -2.383  15.879   3.329  0.38 16.69           N  
ANISOU 1180  N  BGLN A  80     2261   1873   2208  -1151   -145    416       N  
ATOM   1181  CA AGLN A  80      -1.595  15.040   4.225  0.62 17.11           C  
ANISOU 1181  CA AGLN A  80     2579   1765   2157  -1152   -187    481       C  
ATOM   1182  CA BGLN A  80      -1.592  15.051   4.241  0.38 17.11           C  
ANISOU 1182  CA BGLN A  80     2581   1765   2155  -1152   -186    482       C  
ATOM   1183  C  AGLN A  80      -0.083  15.347   4.194  0.62 16.76           C  
ANISOU 1183  C  AGLN A  80     2643   1603   2122   -974   -336    484       C  
ATOM   1184  C  BGLN A  80      -0.072  15.229   4.082  0.38 16.95           C  
ANISOU 1184  C  BGLN A  80     2665   1619   2156   -972   -346    479       C  
ATOM   1185  O  AGLN A  80       0.680  14.828   5.015  0.62 16.38           O  
ANISOU 1185  O  AGLN A  80     2788   1428   2009   -931   -421    520       O  
ATOM   1186  O  BGLN A  80       0.709  14.498   4.700  0.38 18.04           O  
ANISOU 1186  O  BGLN A  80     2988   1614   2250   -928   -445    506       O  
ATOM   1187  CB AGLN A  80      -1.866  13.550   3.971  0.62 24.38           C  
ANISOU 1187  CB AGLN A  80     3591   2585   3085  -1234   -223    485       C  
ATOM   1188  CB BGLN A  80      -1.980  13.576   4.105  0.38 23.30           C  
ANISOU 1188  CB BGLN A  80     3456   2458   2938  -1251   -204    489       C  
ATOM   1189  CG AGLN A  80      -1.337  12.996   2.657  0.62 22.96           C  
ANISOU 1189  CG AGLN A  80     3374   2338   3010  -1144   -348    425       C  
ATOM   1190  CG BGLN A  80      -3.416  13.267   4.514  0.38 24.73           C  
ANISOU 1190  CG BGLN A  80     3558   2732   3107  -1440    -30    476       C  
ATOM   1191  CD AGLN A  80      -2.379  12.994   1.562  0.62 29.04           C  
ANISOU 1191  CD AGLN A  80     3955   3218   3862  -1207   -312    361       C  
ATOM   1192  CD BGLN A  80      -3.749  13.712   5.931  0.38 22.49           C  
ANISOU 1192  CD BGLN A  80     3363   2492   2690  -1527    128    505       C  
ATOM   1193  OE1AGLN A  80      -2.976  14.029   1.243  0.62 17.39           O  
ANISOU 1193  OE1AGLN A  80     2299   1883   2427  -1200   -277    328       O  
ATOM   1194  OE1BGLN A  80      -3.248  13.151   6.902  0.38 23.15           O  
ANISOU 1194  OE1BGLN A  80     3715   2456   2623  -1558     96    571       O  
ATOM   1195  NE2AGLN A  80      -2.625  11.815   0.996  0.62 26.02           N  
ANISOU 1195  NE2AGLN A  80     3612   2764   3510  -1264   -342    337       N  
ATOM   1196  NE2BGLN A  80      -4.606  14.721   6.050  0.38 22.13           N  
ANISOU 1196  NE2BGLN A  80     3092   2616   2702  -1558    288    436       N  
ATOM   1197  H  AGLN A  80      -2.711  15.464   2.641  0.62 19.80           H  
ATOM   1198  H  BGLN A  80      -2.695  15.462   2.644  0.38 20.03           H  
ATOM   1199  HA AGLN A  80      -1.893  15.224   5.129  0.62 20.53           H  
ATOM   1200  HA BGLN A  80      -1.811  15.317   5.147  0.38 20.53           H  
ATOM   1201  HB2AGLN A  80      -1.457  13.039   4.687  0.62 29.25           H  
ATOM   1202  HB2BGLN A  80      -1.873  13.310   3.178  0.38 27.96           H  
ATOM   1203  HB3AGLN A  80      -2.826  13.408   3.981  0.62 29.25           H  
ATOM   1204  HB3BGLN A  80      -1.393  13.046   4.667  0.38 27.96           H  
ATOM   1205  HG2AGLN A  80      -0.592  13.542   2.361  0.62 27.55           H  
ATOM   1206  HG2BGLN A  80      -4.020  13.725   3.908  0.38 29.68           H  
ATOM   1207  HG3AGLN A  80      -1.045  12.081   2.795  0.62 27.55           H  
ATOM   1208  HG3BGLN A  80      -3.559  12.309   4.461  0.38 29.68           H  
ATOM   1209 HE21AGLN A  80      -2.200  11.115   1.259  0.62 31.22           H  
ATOM   1210 HE21BGLN A  80      -4.941  15.087   5.348  0.38 26.56           H  
ATOM   1211 HE22AGLN A  80      -3.208  11.754   0.367  0.62 31.22           H  
ATOM   1212 HE22BGLN A  80      -4.826  15.009   6.831  0.38 26.56           H  
ATOM   1213  N   HIS A  81       0.344  16.205   3.277  1.00 14.23           N  
ANISOU 1213  N   HIS A  81     2178   1343   1886   -837   -367    411       N  
ATOM   1214  CA  HIS A  81       1.766  16.519   3.098  1.00 17.52           C  
ANISOU 1214  CA  HIS A  81     2640   1663   2353   -666   -470    357       C  
ATOM   1215  C   HIS A  81       2.151  17.916   3.567  1.00 13.09           C  
ANISOU 1215  C   HIS A  81     2018   1199   1756   -538   -421    335       C  
ATOM   1216  O   HIS A  81       3.254  18.400   3.253  1.00 13.89           O  
ANISOU 1216  O   HIS A  81     2103   1253   1922   -405   -474    259       O  
ATOM   1217  CB  HIS A  81       2.139  16.368   1.625  1.00 18.27           C  
ANISOU 1217  CB  HIS A  81     2656   1733   2553   -624   -506    255       C  
ATOM   1218  CG  HIS A  81       1.805  15.017   1.094  1.00 17.56           C  
ANISOU 1218  CG  HIS A  81     2601   1589   2483   -694   -524    243       C  
ATOM   1219  ND1 HIS A  81       2.565  13.913   1.395  1.00 16.64           N  
ANISOU 1219  ND1 HIS A  81     2591   1330   2401   -650   -598    230       N  
ATOM   1220  CD2 HIS A  81       0.758  14.569   0.361  1.00 16.40           C  
ANISOU 1220  CD2 HIS A  81     2393   1508   2330   -800   -488    239       C  
ATOM   1221  CE1 HIS A  81       2.024  12.843   0.843  1.00 18.74           C  
ANISOU 1221  CE1 HIS A  81     2873   1570   2678   -733   -590    223       C  
ATOM   1222  NE2 HIS A  81       0.925  13.214   0.208  1.00 18.27           N  
ANISOU 1222  NE2 HIS A  81     2715   1637   2592   -826   -521    225       N  
ATOM   1223  H  AHIS A  81      -0.174  16.628   2.736  0.62 17.08           H  
ATOM   1224  H  BHIS A  81      -0.182  16.707   2.818  0.38 17.08           H  
ATOM   1225  HA  HIS A  81       2.292  15.881   3.605  1.00 21.02           H  
ATOM   1226  HB2 HIS A  81       1.651  17.025   1.105  1.00 21.92           H  
ATOM   1227  HB3 HIS A  81       3.094  16.504   1.524  1.00 21.92           H  
ATOM   1228  HD1 HIS A  81       3.287  13.920   1.863  1.00 19.97           H  
ATOM   1229  HD2 HIS A  81       0.065  15.084   0.015  1.00 19.68           H  
ATOM   1230  HE1 HIS A  81       2.362  11.977   0.888  1.00 22.49           H  
ATOM   1231  HE2 HIS A  81       0.403  12.693  -0.234  1.00 21.93           H  
ATOM   1232  N   ASP A  82       1.246  18.575   4.291  1.00 14.39           N  
ANISOU 1232  N   ASP A  82     2282   1323   1862    145   -529    197       N  
ATOM   1233  CA  ASP A  82       1.485  19.938   4.749  1.00 10.38           C  
ANISOU 1233  CA  ASP A  82     1704    900   1340     70   -433    162       C  
ATOM   1234  C   ASP A  82       2.092  19.909   6.152  1.00 16.82           C  
ANISOU 1234  C   ASP A  82     2500   1787   2102    104   -457    139       C  
ATOM   1235  O   ASP A  82       1.380  20.000   7.151  1.00 15.17           O  
ANISOU 1235  O   ASP A  82     2330   1549   1885     67   -445    211       O  
ATOM   1236  CB  ASP A  82       0.159  20.738   4.710  1.00 10.45           C  
ANISOU 1236  CB  ASP A  82     1737    831   1402    -36   -356    252       C  
ATOM   1237  CG  ASP A  82       0.329  22.222   5.021  1.00 11.30           C  
ANISOU 1237  CG  ASP A  82     1771   1007   1515   -119   -254    210       C  
ATOM   1238  OD1 ASP A  82       1.415  22.660   5.496  1.00 13.98           O  
ANISOU 1238  OD1 ASP A  82     2046   1458   1806   -102   -240    121       O  
ATOM   1239  OD2 ASP A  82      -0.663  22.969   4.794  1.00 13.14           O  
ANISOU 1239  OD2 ASP A  82     2008   1175   1810   -203   -191    269       O  
ATOM   1240  H   ASP A  82       0.486  18.253   4.530  1.00 17.26           H  
ATOM   1241  HA  ASP A  82       2.118  20.369   4.153  1.00 12.46           H  
ATOM   1242  HB2 ASP A  82      -0.226  20.663   3.823  1.00 12.54           H  
ATOM   1243  HB3 ASP A  82      -0.450  20.365   5.366  1.00 12.54           H  
ATOM   1244  N   PHE A  83       3.412  19.755   6.218  1.00 13.48           N  
ANISOU 1244  N   PHE A  83     2016   1463   1641    170   -494     40       N  
ATOM   1245  CA  PHE A  83       4.117  19.760   7.496  1.00 12.00           C  
ANISOU 1245  CA  PHE A  83     1804   1355   1399    199   -527     14       C  
ATOM   1246  C   PHE A  83       3.884  21.049   8.262  1.00 13.61           C  
ANISOU 1246  C   PHE A  83     1977   1612   1584    102   -430     12       C  
ATOM   1247  O   PHE A  83       3.660  21.043   9.488  1.00 16.89           O  
ANISOU 1247  O   PHE A  83     2421   2040   1958     84   -441     51       O  
ATOM   1248  CB  PHE A  83       5.609  19.596   7.264  1.00 12.68           C  
ANISOU 1248  CB  PHE A  83     1808   1546   1464    275   -568   -105       C  
ATOM   1249  CG  PHE A  83       6.435  19.981   8.445  1.00 13.23           C  
ANISOU 1249  CG  PHE A  83     1829   1719   1480    279   -582   -147       C  
ATOM   1250  CD1 PHE A  83       6.740  19.039   9.418  1.00 18.06           C  
ANISOU 1250  CD1 PHE A  83     2475   2327   2061    350   -694   -115       C  
ATOM   1251  CD2 PHE A  83       6.901  21.278   8.595  1.00 14.71           C  
ANISOU 1251  CD2 PHE A  83     1940   2003   1647    207   -492   -212       C  
ATOM   1252  CE1 PHE A  83       7.514  19.388  10.547  1.00 19.07           C  
ANISOU 1252  CE1 PHE A  83     2562   2554   2132    346   -716   -148       C  
ATOM   1253  CE2 PHE A  83       7.679  21.648   9.712  1.00 14.58           C  
ANISOU 1253  CE2 PHE A  83     1879   2084   1575    205   -509   -253       C  
ATOM   1254  CZ  PHE A  83       7.978  20.700  10.694  1.00 17.21           C  
ANISOU 1254  CZ  PHE A  83     2248   2419   1871    273   -621   -221       C  
ATOM   1255  H   PHE A  83       3.924  19.645   5.535  1.00 16.17           H  
ATOM   1256  HA  PHE A  83       3.806  19.019   8.039  1.00 14.40           H  
ATOM   1257  HB2 PHE A  83       5.795  18.666   7.060  1.00 15.22           H  
ATOM   1258  HB3 PHE A  83       5.875  20.157   6.519  1.00 15.22           H  
ATOM   1259  HD1 PHE A  83       6.428  18.168   9.327  1.00 21.68           H  
ATOM   1260  HD2 PHE A  83       6.700  21.914   7.947  1.00 17.66           H  
ATOM   1261  HE1 PHE A  83       7.711  18.749  11.192  1.00 22.89           H  
ATOM   1262  HE2 PHE A  83       7.984  22.523   9.800  1.00 17.49           H  
ATOM   1263  HZ  PHE A  83       8.493  20.936  11.432  1.00 20.65           H  
ATOM   1264  N   PHE A  84       3.964  22.161   7.536  1.00 11.19           N  
ANISOU 1264  N   PHE A  84     1610   1337   1304     34   -338    -37       N  
ATOM   1265  CA  PHE A  84       3.982  23.495   8.126  1.00 12.32           C  
ANISOU 1265  CA  PHE A  84     1703   1538   1439    -53   -246    -67       C  
ATOM   1266  C   PHE A  84       2.733  23.776   8.983  1.00 11.67           C  
ANISOU 1266  C   PHE A  84     1678   1386   1371   -118   -201     19       C  
ATOM   1267  O   PHE A  84       2.823  24.220  10.138  1.00 12.65           O  
ANISOU 1267  O   PHE A  84     1795   1562   1451   -149   -176      4       O  
ATOM   1268  CB  PHE A  84       4.053  24.575   7.024  1.00 13.11           C  
ANISOU 1268  CB  PHE A  84     1743   1652   1586   -124   -163   -109       C  
ATOM   1269  CG  PHE A  84       5.184  24.393   6.033  1.00 14.62           C  
ANISOU 1269  CG  PHE A  84     1874   1917   1763    -79   -187   -196       C  
ATOM   1270  CD1 PHE A  84       6.484  24.749   6.361  1.00 11.36           C  
ANISOU 1270  CD1 PHE A  84     1378   1632   1306    -58   -189   -296       C  
ATOM   1271  CD2 PHE A  84       4.936  23.898   4.759  1.00 12.41           C  
ANISOU 1271  CD2 PHE A  84     1617   1585   1513    -66   -202   -180       C  
ATOM   1272  CE1 PHE A  84       7.507  24.628   5.444  1.00 13.76           C  
ANISOU 1272  CE1 PHE A  84     1615   2012   1600    -24   -199   -381       C  
ATOM   1273  CE2 PHE A  84       5.982  23.754   3.834  1.00 12.11           C  
ANISOU 1273  CE2 PHE A  84     1518   1627   1456    -33   -211   -271       C  
ATOM   1274  CZ  PHE A  84       7.254  24.116   4.190  1.00 13.76           C  
ANISOU 1274  CZ  PHE A  84     1639   1964   1625    -11   -207   -372       C  
ATOM   1275  H   PHE A  84       4.009  22.167   6.677  1.00 13.42           H  
ATOM   1276  HA  PHE A  84       4.765  23.585   8.691  1.00 14.78           H  
ATOM   1277  HB2 PHE A  84       3.222  24.564   6.525  1.00 15.73           H  
ATOM   1278  HB3 PHE A  84       4.169  25.441   7.445  1.00 15.73           H  
ATOM   1279  HD1 PHE A  84       6.664  25.099   7.204  1.00 13.63           H  
ATOM   1280  HD2 PHE A  84       4.071  23.655   4.519  1.00 14.89           H  
ATOM   1281  HE1 PHE A  84       8.374  24.862   5.684  1.00 16.51           H  
ATOM   1282  HE2 PHE A  84       5.812  23.417   2.985  1.00 14.53           H  
ATOM   1283  HZ  PHE A  84       7.950  24.022   3.580  1.00 16.51           H  
ATOM   1284  N   LYS A  85       1.554  23.516   8.442  1.00 14.36           N  
ANISOU 1284  N   LYS A  85     2075   1611   1771   -142   -189    106       N  
ATOM   1285  CA  LYS A  85       0.367  23.736   9.252  1.00 15.80           C  
ANISOU 1285  CA  LYS A  85     2301   1730   1971   -201   -143    183       C  
ATOM   1286  C   LYS A  85       0.248  22.704  10.358  1.00 18.20           C  
ANISOU 1286  C   LYS A  85     2671   2034   2210   -157   -215    235       C  
ATOM   1287  O   LYS A  85      -0.261  22.998  11.423  1.00 14.90           O  
ANISOU 1287  O   LYS A  85     2271   1626   1765   -207   -174    260       O  
ATOM   1288  CB  LYS A  85      -0.879  23.718   8.393  1.00 14.63           C  
ANISOU 1288  CB  LYS A  85     2189   1458   1912   -241   -116    267       C  
ATOM   1289  CG  LYS A  85      -0.969  24.896   7.431  1.00 12.10           C  
ANISOU 1289  CG  LYS A  85     1808   1126   1662   -310    -40    236       C  
ATOM   1290  CD  LYS A  85      -2.273  24.881   6.663  1.00 12.79           C  
ANISOU 1290  CD  LYS A  85     1897   1132   1830   -314     -3    297       C  
ATOM   1291  CE  LYS A  85      -2.269  25.863   5.470  1.00 10.72           C  
ANISOU 1291  CE  LYS A  85     1568    890   1613   -332     63    246       C  
ATOM   1292  NZ  LYS A  85      -1.118  25.656   4.536  1.00 11.63           N  
ANISOU 1292  NZ  LYS A  85     1694   1015   1710   -363     -9    231       N  
ATOM   1293  H   LYS A  85       1.415  23.226   7.644  1.00 17.23           H  
ATOM   1294  HA  LYS A  85       0.429  24.610   9.668  1.00 18.96           H  
ATOM   1295  HB2 LYS A  85      -0.886  22.903   7.866  1.00 17.56           H  
ATOM   1296  HB3 LYS A  85      -1.659  23.744   8.969  1.00 17.56           H  
ATOM   1297  HG2 LYS A  85      -0.921  25.725   7.934  1.00 14.52           H  
ATOM   1298  HG3 LYS A  85      -0.239  24.847   6.794  1.00 14.52           H  
ATOM   1299  HD2 LYS A  85      -2.427  23.988   6.317  1.00 15.35           H  
ATOM   1300  HD3 LYS A  85      -2.995  25.136   7.259  1.00 15.35           H  
ATOM   1301  HE2 LYS A  85      -3.088  25.745   4.964  1.00 12.86           H  
ATOM   1302  HE3 LYS A  85      -2.218  26.770   5.810  1.00 12.86           H  
ATOM   1303  HZ1 LYS A  85      -0.350  25.767   4.972  1.00 13.96           H  
ATOM   1304  HZ2 LYS A  85      -1.144  24.833   4.200  1.00 13.96           H  
ATOM   1305  HZ3 LYS A  85      -1.160  26.243   3.869  1.00 13.96           H  
ATOM   1306  N   SER A  86       0.706  21.491  10.101  1.00 13.71           N  
ANISOU 1306  N   SER A  86     2139   1452   1619    -69   -325    251       N  
ATOM   1307  CA  SER A  86       0.522  20.417  11.064  1.00 15.14           C  
ANISOU 1307  CA  SER A  86     2391   1615   1748    -31   -412    320       C  
ATOM   1308  C   SER A  86       1.294  20.700  12.362  1.00 15.80           C  
ANISOU 1308  C   SER A  86     2451   1811   1742    -38   -421    274       C  
ATOM   1309  O   SER A  86       0.932  20.202  13.434  1.00 14.88           O  
ANISOU 1309  O   SER A  86     2392   1694   1569    -52   -457    339       O  
ATOM   1310  CB  SER A  86       0.952  19.079  10.464  1.00 17.60           C  
ANISOU 1310  CB  SER A  86     2738   1880   2067     72   -537    336       C  
ATOM   1311  OG  SER A  86       2.343  18.884  10.542  1.00 16.88           O  
ANISOU 1311  OG  SER A  86     2595   1881   1939    145   -598    246       O  
ATOM   1312  H   SER A  86       1.124  21.263   9.384  1.00 16.45           H  
ATOM   1313  HA  SER A  86      -0.420  20.354  11.286  1.00 18.17           H  
ATOM   1314  HB2 SER A  86       0.509  18.365  10.948  1.00 21.12           H  
ATOM   1315  HB3 SER A  86       0.686  19.057   9.531  1.00 21.12           H  
ATOM   1316  HG  SER A  86       2.742  19.493  10.124  1.00 20.26           H  
ATOM   1317  N   ALA A  87       2.334  21.525  12.273  1.00 15.21           N  
ANISOU 1317  N   ALA A  87     2294   1836   1650    -39   -387    167       N  
ATOM   1318  CA  ALA A  87       3.142  21.866  13.445  1.00 17.26           C  
ANISOU 1318  CA  ALA A  87     2525   2208   1825    -51   -399    115       C  
ATOM   1319  C   ALA A  87       2.511  22.947  14.323  1.00 16.43           C  
ANISOU 1319  C   ALA A  87     2416   2131   1695   -157   -287    109       C  
ATOM   1320  O   ALA A  87       2.994  23.220  15.405  1.00 18.92           O  
ANISOU 1320  O   ALA A  87     2724   2535   1930   -183   -291     75       O  
ATOM   1321  CB  ALA A  87       4.535  22.301  13.010  1.00 18.08           C  
ANISOU 1321  CB  ALA A  87     2536   2410   1924    -11   -411      0       C  
ATOM   1322  H   ALA A  87       2.594  21.902  11.545  1.00 18.25           H  
ATOM   1323  HA  ALA A  87       3.242  21.070  13.990  1.00 20.71           H  
ATOM   1324  HB1 ALA A  87       5.056  22.523  13.798  1.00 21.70           H  
ATOM   1325  HB2 ALA A  87       4.956  21.573  12.528  1.00 21.70           H  
ATOM   1326  HB3 ALA A  87       4.457  23.078  12.435  1.00 21.70           H  
ATOM   1327  N   MET A  88       1.450  23.588  13.839  1.00 15.02           N  
ANISOU 1327  N   MET A  88     2239   1878   1591   -220   -187    135       N  
ATOM   1328  CA  MET A  88       0.822  24.675  14.572  1.00 17.74           C  
ANISOU 1328  CA  MET A  88     2569   2239   1935   -317    -72    115       C  
ATOM   1329  C   MET A  88      -0.171  24.096  15.571  1.00 19.26           C  
ANISOU 1329  C   MET A  88     2838   2397   2082   -351    -72    203       C  
ATOM   1330  O   MET A  88      -0.679  23.010  15.346  1.00 18.88           O  
ANISOU 1330  O   MET A  88     2854   2277   2044   -311   -143    297       O  
ATOM   1331  CB  MET A  88       0.119  25.599  13.579  1.00 12.96           C  
ANISOU 1331  CB  MET A  88     1922   1558   1445   -365     25    107       C  
ATOM   1332  CG  MET A  88       1.090  26.249  12.621  1.00 12.21           C  
ANISOU 1332  CG  MET A  88     1751   1506   1384   -351     32     24       C  
ATOM   1333  SD  MET A  88       2.316  27.268  13.462  1.00 14.67           S  
ANISOU 1333  SD  MET A  88     1990   1960   1626   -382     64   -102       S  
ATOM   1334  CE  MET A  88       3.583  27.383  12.185  1.00 15.27           C  
ANISOU 1334  CE  MET A  88     1990   2087   1725   -333     24   -172       C  
ATOM   1335  H   MET A  88       1.075  23.409  13.086  1.00 18.03           H  
ATOM   1336  HA  MET A  88       1.500  25.185  15.043  1.00 21.29           H  
ATOM   1337  HB2 MET A  88      -0.517  25.082  13.060  1.00 15.55           H  
ATOM   1338  HB3 MET A  88      -0.339  26.300  14.067  1.00 15.55           H  
ATOM   1339  HG2 MET A  88       1.560  25.558  12.129  1.00 14.66           H  
ATOM   1340  HG3 MET A  88       0.597  26.817  12.008  1.00 14.66           H  
ATOM   1341  HE1 MET A  88       4.319  27.920  12.519  1.00 18.32           H  
ATOM   1342  HE2 MET A  88       3.895  26.490  11.970  1.00 18.32           H  
ATOM   1343  HE3 MET A  88       3.200  27.799  11.397  1.00 18.32           H  
ATOM   1344  N   PRO A  89      -0.452  24.822  16.671  1.00 19.95           N  
ANISOU 1344  N   PRO A  89     2921   2539   2119   -429      9    170       N  
ATOM   1345  CA  PRO A  89       0.019  26.195  16.943  1.00 15.03           C  
ANISOU 1345  CA  PRO A  89     2225   1989   1498   -485    102     56       C  
ATOM   1346  C   PRO A  89       1.418  26.309  17.548  1.00 16.37           C  
ANISOU 1346  C   PRO A  89     2365   2287   1568   -464     44    -25       C  
ATOM   1347  O   PRO A  89       1.982  27.391  17.533  1.00 18.93           O  
ANISOU 1347  O   PRO A  89     2621   2666   1905   -499    103   -123       O  
ATOM   1348  CB  PRO A  89      -1.035  26.726  17.915  1.00 14.73           C  
ANISOU 1348  CB  PRO A  89     2206   1943   1446   -575    209     61       C  
ATOM   1349  CG  PRO A  89      -1.444  25.471  18.697  1.00 18.28           C  
ANISOU 1349  CG  PRO A  89     2746   2393   1804   -565    134    163       C  
ATOM   1350  CD  PRO A  89      -1.371  24.336  17.721  1.00 17.91           C  
ANISOU 1350  CD  PRO A  89     2734   2271   1802   -477     22    246       C  
ATOM   1351  HA  PRO A  89      -0.013  26.721  16.129  1.00 18.04           H  
ATOM   1352  HB2 PRO A  89      -0.643  27.392  18.501  1.00 17.67           H  
ATOM   1353  HB3 PRO A  89      -1.788  27.092  17.423  1.00 17.67           H  
ATOM   1354  HG2 PRO A  89      -0.824  25.329  19.430  1.00 21.93           H  
ATOM   1355  HG3 PRO A  89      -2.348  25.576  19.031  1.00 21.93           H  
ATOM   1356  HD2 PRO A  89      -1.004  23.546  18.149  1.00 21.50           H  
ATOM   1357  HD3 PRO A  89      -2.247  24.159  17.345  1.00 21.50           H  
ATOM   1358  N  AGLU A  90       1.959  25.201  18.039  0.60 18.72           N  
ANISOU 1358  N  AGLU A  90     2710   2624   1779   -409    -77     21       N  
ATOM   1359  N  BGLU A  90       1.972  25.219  18.075  0.40 18.42           N  
ANISOU 1359  N  BGLU A  90     2672   2589   1738   -411    -76     19       N  
ATOM   1360  CA AGLU A  90       3.241  25.199  18.733  0.60 19.60           C  
ANISOU 1360  CA AGLU A  90     2796   2855   1794   -391   -147    -42       C  
ATOM   1361  CA BGLU A  90       3.274  25.278  18.750  0.40 18.76           C  
ANISOU 1361  CA BGLU A  90     2686   2754   1687   -394   -142    -49       C  
ATOM   1362  C  AGLU A  90       4.374  25.720  17.844  0.60 19.34           C  
ANISOU 1362  C  AGLU A  90     2673   2865   1810   -346   -158   -134       C  
ATOM   1363  C  BGLU A  90       4.375  25.780  17.827  0.40 19.49           C  
ANISOU 1363  C  BGLU A  90     2688   2884   1831   -349   -153   -138       C  
ATOM   1364  O  AGLU A  90       5.302  26.382  18.335  0.60 19.57           O  
ANISOU 1364  O  AGLU A  90     2650   2997   1790   -368   -155   -221       O  
ATOM   1365  O  BGLU A  90       5.296  26.475  18.277  0.40 20.43           O  
ANISOU 1365  O  BGLU A  90     2753   3104   1904   -372   -146   -227       O  
ATOM   1366  CB AGLU A  90       3.536  23.782  19.259  0.60 26.94           C  
ANISOU 1366  CB AGLU A  90     3794   3793   2647   -331   -295     43       C  
ATOM   1367  CB BGLU A  90       3.656  23.911  19.334  0.40 24.63           C  
ANISOU 1367  CB BGLU A  90     3494   3516   2348   -336   -290     29       C  
ATOM   1368  CG AGLU A  90       2.477  23.243  20.256  0.60 29.43           C  
ANISOU 1368  CG AGLU A  90     4204   4084   2894   -390   -289    141       C  
ATOM   1369  CG BGLU A  90       2.771  23.469  20.488  0.40 28.75           C  
ANISOU 1369  CG BGLU A  90     4104   4036   2783   -401   -287    112       C  
ATOM   1370  CD AGLU A  90       1.248  22.567  19.604  0.60 27.31           C  
ANISOU 1370  CD AGLU A  90     3989   3683   2704   -377   -279    246       C  
ATOM   1371  CD BGLU A  90       3.056  22.046  20.939  0.40 31.15           C  
ANISOU 1371  CD BGLU A  90     4479   4336   3021   -345   -447    210       C  
ATOM   1372  OE1AGLU A  90       1.137  22.521  18.361  0.60 17.67           O  
ANISOU 1372  OE1AGLU A  90     2740   2383   1592   -325   -274    245       O  
ATOM   1373  OE1BGLU A  90       2.857  21.105  20.140  0.40 30.34           O  
ANISOU 1373  OE1BGLU A  90     4403   4140   2987   -268   -522    279       O  
ATOM   1374  OE2AGLU A  90       0.382  22.070  20.361  0.60 29.81           O  
ANISOU 1374  OE2AGLU A  90     4378   3979   2968   -427   -277    332       O  
ATOM   1375  OE2BGLU A  90       3.482  21.872  22.096  0.40 33.36           O  
ANISOU 1375  OE2BGLU A  90     4790   4703   3182   -381   -503    220       O  
ATOM   1376  H  AGLU A  90       1.596  24.423  17.981  0.60 22.47           H  
ATOM   1377  H  BGLU A  90       1.619  24.435  18.056  0.40 22.10           H  
ATOM   1378  HA AGLU A  90       3.177  25.788  19.501  0.60 23.51           H  
ATOM   1379  HA BGLU A  90       3.207  25.902  19.490  0.40 22.51           H  
ATOM   1380  HB2AGLU A  90       3.571  23.171  18.507  0.60 32.32           H  
ATOM   1381  HB2BGLU A  90       3.588  23.242  18.634  0.40 29.55           H  
ATOM   1382  HB3AGLU A  90       4.392  23.790  19.714  0.60 32.32           H  
ATOM   1383  HB3BGLU A  90       4.568  23.954  19.659  0.40 29.55           H  
ATOM   1384  HG2AGLU A  90       2.901  22.587  20.831  0.60 35.32           H  
ATOM   1385  HG2BGLU A  90       2.919  24.058  21.243  0.40 34.50           H  
ATOM   1386  HG3AGLU A  90       2.153  23.984  20.792  0.60 35.32           H  
ATOM   1387  HG3BGLU A  90       1.843  23.514  20.209  0.40 34.50           H  
ATOM   1388  N   GLY A  91       4.283  25.421  16.548  1.00 17.41           N  
ANISOU 1388  N   GLY A  91     2411   2546   1659   -291   -171   -115       N  
ATOM   1389  CA  GLY A  91       5.156  25.989  15.527  1.00 16.09           C  
ANISOU 1389  CA  GLY A  91     2157   2409   1547   -265   -158   -197       C  
ATOM   1390  C   GLY A  91       6.378  25.177  15.161  1.00 15.56           C  
ANISOU 1390  C   GLY A  91     2057   2395   1461   -166   -275   -225       C  
ATOM   1391  O   GLY A  91       6.489  23.993  15.484  1.00 17.96           O  
ANISOU 1391  O   GLY A  91     2412   2683   1730    -99   -384   -167       O  
ATOM   1392  H  AGLY A  91       3.703  24.873  16.228  0.60 20.90           H  
ATOM   1393  H  BGLY A  91       3.719  24.847  16.246  0.40 20.90           H  
ATOM   1394  HA2 GLY A  91       4.639  26.123  14.718  1.00 19.31           H  
ATOM   1395  HA3 GLY A  91       5.462  26.859  15.830  1.00 19.31           H  
ATOM   1396  N   TYR A  92       7.306  25.819  14.463  1.00 16.76           N  
ANISOU 1396  N   TYR A  92     2119   2608   1642   -159   -253   -315       N  
ATOM   1397  CA  TYR A  92       8.523  25.146  14.030  1.00 15.25           C  
ANISOU 1397  CA  TYR A  92     1876   2474   1445    -65   -350   -361       C  
ATOM   1398  C   TYR A  92       9.691  26.102  13.986  1.00 15.44           C  
ANISOU 1398  C   TYR A  92     1796   2615   1457    -90   -321   -472       C  
ATOM   1399  O   TYR A  92       9.493  27.301  13.906  1.00 15.64           O  
ANISOU 1399  O   TYR A  92     1787   2653   1501   -177   -219   -512       O  
ATOM   1400  CB  TYR A  92       8.356  24.511  12.656  1.00 17.13           C  
ANISOU 1400  CB  TYR A  92     2114   2638   1756     -3   -367   -342       C  
ATOM   1401  CG  TYR A  92       7.838  25.423  11.553  1.00 13.26           C  
ANISOU 1401  CG  TYR A  92     1596   2105   1335    -68   -257   -357       C  
ATOM   1402  CD1 TYR A  92       8.670  26.318  10.906  1.00 13.95           C  
ANISOU 1402  CD1 TYR A  92     1590   2270   1441    -98   -207   -447       C  
ATOM   1403  CD2 TYR A  92       6.519  25.331  11.131  1.00 17.44           C  
ANISOU 1403  CD2 TYR A  92     2194   2517   1916   -102   -215   -272       C  
ATOM   1404  CE1 TYR A  92       8.182  27.151   9.880  1.00 12.51           C  
ANISOU 1404  CE1 TYR A  92     1386   2044   1321   -167   -118   -447       C  
ATOM   1405  CE2 TYR A  92       6.033  26.121  10.129  1.00 15.93           C  
ANISOU 1405  CE2 TYR A  92     1980   2281   1792   -163   -132   -274       C  
ATOM   1406  CZ  TYR A  92       6.868  27.024   9.488  1.00 13.04           C  
ANISOU 1406  CZ  TYR A  92     1525   1989   1440   -196    -86   -359       C  
ATOM   1407  OH  TYR A  92       6.329  27.817   8.488  1.00 14.86           O  
ANISOU 1407  OH  TYR A  92     1739   2168   1739   -268    -12   -346       O  
ATOM   1408  H   TYR A  92       7.255  26.645  14.227  1.00 20.11           H  
ATOM   1409  HA  TYR A  92       8.736  24.442  14.662  1.00 18.30           H  
ATOM   1410  HB2 TYR A  92       9.219  24.174  12.370  1.00 20.55           H  
ATOM   1411  HB3 TYR A  92       7.732  23.773  12.737  1.00 20.55           H  
ATOM   1412  HD1 TYR A  92       9.558  26.392  11.172  1.00 16.74           H  
ATOM   1413  HD2 TYR A  92       5.951  24.724  11.547  1.00 20.93           H  
ATOM   1414  HE1 TYR A  92       8.747  27.755   9.454  1.00 15.01           H  
ATOM   1415  HE2 TYR A  92       5.143  26.047   9.870  1.00 19.12           H  
ATOM   1416  HH  TYR A  92       6.912  28.346   8.194  1.00 17.83           H  
ATOM   1417  N   VAL A  93      10.895  25.536  14.040  1.00 15.69           N  
ANISOU 1417  N   VAL A  93     1772   2723   1465    -12   -416   -520       N  
ATOM   1418  CA  VAL A  93      12.128  26.274  13.812  1.00 16.05           C  
ANISOU 1418  CA  VAL A  93     1706   2883   1510    -21   -401   -628       C  
ATOM   1419  C   VAL A  93      12.537  26.118  12.356  1.00 16.81           C  
ANISOU 1419  C   VAL A  93     1740   2974   1673     25   -385   -671       C  
ATOM   1420  O   VAL A  93      12.549  25.003  11.835  1.00 18.29           O  
ANISOU 1420  O   VAL A  93     1948   3114   1886    117   -455   -645       O  
ATOM   1421  CB  VAL A  93      13.243  25.728  14.681  1.00 17.60           C  
ANISOU 1421  CB  VAL A  93     1866   3171   1651     39   -517   -659       C  
ATOM   1422  CG1 VAL A  93      14.556  26.429  14.388  1.00 17.82           C  
ANISOU 1422  CG1 VAL A  93     1767   3319   1685     34   -506   -771       C  
ATOM   1423  CG2 VAL A  93      12.907  25.902  16.141  1.00 17.62           C  
ANISOU 1423  CG2 VAL A  93     1932   3194   1569    -20   -535   -620       C  
ATOM   1424  H   VAL A  93      11.022  24.703  14.213  1.00 18.82           H  
ATOM   1425  HA  VAL A  93      11.999  27.215  14.010  1.00 19.26           H  
ATOM   1426  HB  VAL A  93      13.356  24.781  14.503  1.00 21.12           H  
ATOM   1427 HG11 VAL A  93      15.246  26.057  14.959  1.00 21.39           H  
ATOM   1428 HG12 VAL A  93      14.787  26.290  13.456  1.00 21.39           H  
ATOM   1429 HG13 VAL A  93      14.454  27.377  14.566  1.00 21.39           H  
ATOM   1430 HG21 VAL A  93      13.634  25.547  16.677  1.00 21.15           H  
ATOM   1431 HG22 VAL A  93      12.790  26.847  16.328  1.00 21.15           H  
ATOM   1432 HG23 VAL A  93      12.087  25.422  16.335  1.00 21.15           H  
ATOM   1433  N   GLN A  94      12.865  27.230  11.714  1.00 15.45           N  
ANISOU 1433  N   GLN A  94     1493   2850   1526    -44   -296   -736       N  
ATOM   1434  CA  GLN A  94      13.240  27.218  10.304  1.00 15.23           C  
ANISOU 1434  CA  GLN A  94     1406   2833   1548    -25   -266   -779       C  
ATOM   1435  C   GLN A  94      14.638  27.800  10.221  1.00 15.91           C  
ANISOU 1435  C   GLN A  94     1368   3057   1621    -32   -264   -887       C  
ATOM   1436  O   GLN A  94      14.889  28.945  10.609  1.00 15.93           O  
ANISOU 1436  O   GLN A  94     1329   3117   1609   -121   -208   -925       O  
ATOM   1437  CB  GLN A  94      12.229  27.986   9.437  1.00 14.26           C  
ANISOU 1437  CB  GLN A  94     1315   2630   1474   -115   -163   -739       C  
ATOM   1438  CG  GLN A  94      12.694  28.164   7.968  1.00 14.15           C  
ANISOU 1438  CG  GLN A  94     1235   2648   1495   -123   -124   -788       C  
ATOM   1439  CD  GLN A  94      11.556  28.557   7.056  1.00 13.27           C  
ANISOU 1439  CD  GLN A  94     1177   2433   1433   -193    -54   -721       C  
ATOM   1440  OE1 GLN A  94      10.517  27.896   7.031  1.00 14.82           O  
ANISOU 1440  OE1 GLN A  94     1464   2518   1648   -168    -74   -638       O  
ATOM   1441  NE2 GLN A  94      11.731  29.657   6.323  1.00 13.08           N  
ANISOU 1441  NE2 GLN A  94     1097   2442   1433   -289     21   -751       N  
ATOM   1442  H   GLN A  94      12.879  28.011  12.073  1.00 18.54           H  
ATOM   1443  HA  GLN A  94      13.273  26.301   9.990  1.00 18.28           H  
ATOM   1444  HB2 GLN A  94      11.390  27.500   9.428  1.00 17.12           H  
ATOM   1445  HB3 GLN A  94      12.095  28.868   9.817  1.00 17.12           H  
ATOM   1446  HG2 GLN A  94      13.367  28.862   7.930  1.00 16.98           H  
ATOM   1447  HG3 GLN A  94      13.063  27.326   7.648  1.00 16.98           H  
ATOM   1448 HE21 GLN A  94      12.464  30.103   6.385  1.00 15.70           H  
ATOM   1449 HE22 GLN A  94      11.112  29.921   5.789  1.00 15.70           H  
ATOM   1450  N   GLU A  95      15.561  26.956   9.778  1.00 16.58           N  
ANISOU 1450  N   GLU A  95     1392   3194   1715     66   -332   -939       N  
ATOM   1451  CA  GLU A  95      16.940  27.341   9.627  1.00 17.37           C  
ANISOU 1451  CA  GLU A  95     1361   3428   1808     73   -337  -1044       C  
ATOM   1452  C   GLU A  95      17.343  27.253   8.174  1.00 17.37           C  
ANISOU 1452  C   GLU A  95     1295   3458   1846     87   -292  -1102       C  
ATOM   1453  O   GLU A  95      16.919  26.338   7.455  1.00 18.53           O  
ANISOU 1453  O   GLU A  95     1487   3535   2020    153   -313  -1077       O  
ATOM   1454  CB  GLU A  95      17.850  26.444  10.471  1.00 18.45           C  
ANISOU 1454  CB  GLU A  95     1463   3621   1929    179   -463  -1072       C  
ATOM   1455  CG  GLU A  95      17.574  26.572  11.968  1.00 21.33           C  
ANISOU 1455  CG  GLU A  95     1890   3978   2236    150   -512  -1019       C  
ATOM   1456  CD  GLU A  95      18.336  25.567  12.810  1.00 35.83           C  
ANISOU 1456  CD  GLU A  95     3712   5844   4059    252   -652  -1017       C  
ATOM   1457  OE1 GLU A  95      17.992  24.368  12.750  1.00 43.49           O  
ANISOU 1457  OE1 GLU A  95     4738   6738   5049    346   -737   -966       O  
ATOM   1458  OE2 GLU A  95      19.246  25.987  13.559  1.00 40.30           O  
ANISOU 1458  OE2 GLU A  95     4229   6481   4605    234   -667  -1044       O  
ATOM   1459  H   GLU A  95      15.402  26.140   9.556  1.00 19.90           H  
ATOM   1460  HA  GLU A  95      17.053  28.258   9.922  1.00 20.84           H  
ATOM   1461  HB2 GLU A  95      17.708  25.519  10.216  1.00 22.15           H  
ATOM   1462  HB3 GLU A  95      18.774  26.694  10.314  1.00 22.15           H  
ATOM   1463  HG2 GLU A  95      17.830  27.460  12.260  1.00 25.59           H  
ATOM   1464  HG3 GLU A  95      16.626  26.434  12.125  1.00 25.59           H  
ATOM   1465  N   ARG A  96      18.141  28.212   7.740  1.00 17.62           N  
ANISOU 1465  N   ARG A  96     1223   3596   1876     18   -229  -1178       N  
ATOM   1466  CA  ARG A  96      18.701  28.190   6.396  1.00 17.85           C  
ANISOU 1466  CA  ARG A  96     1184   3673   1927     22   -174  -1237       C  
ATOM   1467  C   ARG A  96      20.153  28.571   6.356  1.00 19.82           C  
ANISOU 1467  C   ARG A  96     1336   4027   2166     31   -149  -1317       C  
ATOM   1468  O   ARG A  96      20.630  29.319   7.200  1.00 19.73           O  
ANISOU 1468  O   ARG A  96     1310   4051   2135    -10   -139  -1317       O  
ATOM   1469  CB  ARG A  96      18.001  29.186   5.483  1.00 17.03           C  
ANISOU 1469  CB  ARG A  96     1108   3533   1830   -105    -66  -1202       C  
ATOM   1470  CG  ARG A  96      16.559  28.922   5.191  1.00 16.05           C  
ANISOU 1470  CG  ARG A  96     1099   3274   1725   -126    -57  -1107       C  
ATOM   1471  CD  ARG A  96      16.247  29.383   3.754  1.00 15.67           C  
ANISOU 1471  CD  ARG A  96     1046   3217   1690   -209     23  -1102       C  
ATOM   1472  NE  ARG A  96      14.855  29.108   3.368  1.00 16.69           N  
ANISOU 1472  NE  ARG A  96     1294   3201   1845   -227     33   -998       N  
ATOM   1473  CZ  ARG A  96      13.840  29.955   3.525  1.00 16.33           C  
ANISOU 1473  CZ  ARG A  96     1310   3069   1826   -324     79   -917       C  
ATOM   1474  NH1 ARG A  96      14.030  31.141   4.067  1.00 16.61           N  
ANISOU 1474  NH1 ARG A  96     1306   3140   1866   -412    120   -930       N  
ATOM   1475  NH2 ARG A  96      12.629  29.626   3.128  1.00 13.37           N  
ANISOU 1475  NH2 ARG A  96     1032   2566   1480   -333     81   -827       N  
ATOM   1476  H   ARG A  96      18.378  28.894   8.207  1.00 21.14           H  
ATOM   1477  HA  ARG A  96      18.603  27.302   6.017  1.00 21.43           H  
ATOM   1478  HB2 ARG A  96      18.055  30.063   5.893  1.00 20.44           H  
ATOM   1479  HB3 ARG A  96      18.469  29.200   4.633  1.00 20.44           H  
ATOM   1480  HG2 ARG A  96      16.379  27.971   5.259  1.00 19.26           H  
ATOM   1481  HG3 ARG A  96      16.002  29.423   5.807  1.00 19.26           H  
ATOM   1482  HD2 ARG A  96      16.394  30.339   3.689  1.00 18.80           H  
ATOM   1483  HD3 ARG A  96      16.829  28.913   3.137  1.00 18.80           H  
ATOM   1484  HE  ARG A  96      14.684  28.344   3.013  1.00 20.02           H  
ATOM   1485 HH11 ARG A  96      14.817  31.374   4.326  1.00 19.93           H  
ATOM   1486 HH12 ARG A  96      13.368  31.680   4.165  1.00 19.93           H  
ATOM   1487 HH21 ARG A  96      12.487  28.855   2.774  1.00 16.04           H  
ATOM   1488 HH22 ARG A  96      11.976  30.176   3.238  1.00 16.04           H  
ATOM   1489  N   THR A  97      20.841  28.088   5.318  1.00 19.55           N  
ANISOU 1489  N   THR A  97     1243   4044   2140     78   -134  -1389       N  
ATOM   1490  CA  THR A  97      22.012  28.781   4.803  1.00 24.10           C  
ANISOU 1490  CA  THR A  97     1755   4711   2693     32    -74  -1459       C  
ATOM   1491  C   THR A  97      21.680  29.190   3.352  1.00 24.97           C  
ANISOU 1491  C   THR A  97     1887   4813   2787    -55      7  -1461       C  
ATOM   1492  O   THR A  97      21.149  28.402   2.582  1.00 21.90           O  
ANISOU 1492  O   THR A  97     1512   4394   2414    -17     -2  -1464       O  
ATOM   1493  CB  THR A  97      23.283  27.932   4.870  1.00 21.62           C  
ANISOU 1493  CB  THR A  97     1356   4467   2393    144   -135  -1550       C  
ATOM   1494  OG1 THR A  97      23.472  27.467   6.215  1.00 26.79           O  
ANISOU 1494  OG1 THR A  97     2007   5108   3063    221   -229  -1528       O  
ATOM   1495  CG2 THR A  97      24.499  28.755   4.457  1.00 26.15           C  
ANISOU 1495  CG2 THR A  97     1866   5134   2936     80    -79  -1617       C  
ATOM   1496  H   THR A  97      20.646  27.363   4.899  1.00 23.45           H  
ATOM   1497  HA  THR A  97      22.159  29.588   5.320  1.00 28.92           H  
ATOM   1498  HB  THR A  97      23.202  27.174   4.271  1.00 25.95           H  
ATOM   1499  HG1 THR A  97      24.168  26.999   6.262  1.00 32.15           H  
ATOM   1500 HG21 THR A  97      25.300  28.209   4.503  1.00 31.38           H  
ATOM   1501 HG22 THR A  97      24.388  29.076   3.548  1.00 31.38           H  
ATOM   1502 HG23 THR A  97      24.602  29.516   5.050  1.00 31.38           H  
ATOM   1503  N   ILE A  98      21.920  30.452   3.025  1.00 20.09           N  
ANISOU 1503  N   ILE A  98     1285   4210   2137   -174     76  -1445       N  
ATOM   1504  CA  ILE A  98      21.685  30.945   1.679  1.00 19.52           C  
ANISOU 1504  CA  ILE A  98     1245   4127   2045   -269    137  -1431       C  
ATOM   1505  C   ILE A  98      23.039  31.333   1.134  1.00 20.64           C  
ANISOU 1505  C   ILE A  98     1320   4369   2153   -297    155  -1508       C  
ATOM   1506  O   ILE A  98      23.702  32.231   1.675  1.00 21.63           O  
ANISOU 1506  O   ILE A  98     1428   4528   2262   -338    170  -1512       O  
ATOM   1507  CB  ILE A  98      20.734  32.162   1.667  1.00 19.30           C  
ANISOU 1507  CB  ILE A  98     1307   4009   2019   -386    189  -1328       C  
ATOM   1508  CG1 ILE A  98      19.436  31.835   2.415  1.00 17.56           C  
ANISOU 1508  CG1 ILE A  98     1144   3690   1837   -362    169  -1253       C  
ATOM   1509  CG2 ILE A  98      20.472  32.610   0.222  1.00 20.68           C  
ANISOU 1509  CG2 ILE A  98     1520   4164   2174   -476    237  -1299       C  
ATOM   1510  CD1 ILE A  98      18.517  33.037   2.614  1.00 16.73           C  
ANISOU 1510  CD1 ILE A  98     1125   3483   1749   -463    211  -1157       C  
ATOM   1511  H   ILE A  98      22.221  31.046   3.569  1.00 24.10           H  
ATOM   1512  HA  ILE A  98      21.309  30.242   1.126  1.00 23.43           H  
ATOM   1513  HB  ILE A  98      21.173  32.891   2.132  1.00 23.16           H  
ATOM   1514 HG12 ILE A  98      18.944  31.168   1.910  1.00 21.07           H  
ATOM   1515 HG13 ILE A  98      19.660  31.485   3.291  1.00 21.07           H  
ATOM   1516 HG21 ILE A  98      19.874  33.374   0.232  1.00 24.82           H  
ATOM   1517 HG22 ILE A  98      21.316  32.855  -0.190  1.00 24.82           H  
ATOM   1518 HG23 ILE A  98      20.066  31.877  -0.266  1.00 24.82           H  
ATOM   1519 HD11 ILE A  98      17.723  32.751   3.092  1.00 20.08           H  
ATOM   1520 HD12 ILE A  98      18.988  33.711   3.129  1.00 20.08           H  
ATOM   1521 HD13 ILE A  98      18.272  33.394   1.747  1.00 20.08           H  
ATOM   1522  N   PHE A  99      23.479  30.614   0.099  1.00 24.99           N  
ANISOU 1522  N   PHE A  99     1826   4972   2697   -270    152  -1574       N  
ATOM   1523  CA  PHE A  99      24.761  30.879  -0.548  1.00 23.05           C  
ANISOU 1523  CA  PHE A  99     1508   4829   2422   -300    172  -1654       C  
ATOM   1524  C   PHE A  99      24.553  31.699  -1.799  1.00 23.92           C  
ANISOU 1524  C   PHE A  99     1656   4939   2492   -429    234  -1620       C  
ATOM   1525  O   PHE A  99      24.013  31.196  -2.786  1.00 22.24           O  
ANISOU 1525  O   PHE A  99     1463   4712   2277   -445    245  -1616       O  
ATOM   1526  CB  PHE A  99      25.447  29.570  -0.954  1.00 23.55           C  
ANISOU 1526  CB  PHE A  99     1489   4952   2507   -191    131  -1755       C  
ATOM   1527  CG  PHE A  99      25.746  28.658   0.199  1.00 23.89           C  
ANISOU 1527  CG  PHE A  99     1493   4989   2594    -47     57  -1790       C  
ATOM   1528  CD1 PHE A  99      26.888  28.830   0.958  1.00 24.84           C  
ANISOU 1528  CD1 PHE A  99     1544   5175   2718    -10     34  -1841       C  
ATOM   1529  CD2 PHE A  99      24.881  27.635   0.521  1.00 27.85           C  
ANISOU 1529  CD2 PHE A  99     2030   5417   3136     50      6  -1765       C  
ATOM   1530  CE1 PHE A  99      27.162  27.989   2.016  1.00 25.25           C  
ANISOU 1530  CE1 PHE A  99     1563   5215   2814    120    -44  -1862       C  
ATOM   1531  CE2 PHE A  99      25.140  26.791   1.582  1.00 25.43           C  
ANISOU 1531  CE2 PHE A  99     1696   5094   2871    184    -75  -1784       C  
ATOM   1532  CZ  PHE A  99      26.291  26.965   2.326  1.00 30.08           C  
ANISOU 1532  CZ  PHE A  99     2218   5747   3466    217   -102  -1831       C  
ATOM   1533  H   PHE A  99      23.044  29.960  -0.251  1.00 29.99           H  
ATOM   1534  HA  PHE A  99      25.342  31.367   0.057  1.00 27.66           H  
ATOM   1535  HB2 PHE A  99      24.868  29.091  -1.568  1.00 28.26           H  
ATOM   1536  HB3 PHE A  99      26.287  29.780  -1.391  1.00 28.26           H  
ATOM   1537  HD1 PHE A  99      27.481  29.515   0.749  1.00 29.80           H  
ATOM   1538  HD2 PHE A  99      24.108  27.513   0.018  1.00 33.42           H  
ATOM   1539  HE1 PHE A  99      27.934  28.111   2.519  1.00 30.30           H  
ATOM   1540  HE2 PHE A  99      24.550  26.102   1.787  1.00 30.51           H  
ATOM   1541  HZ  PHE A  99      26.472  26.400   3.043  1.00 36.10           H  
ATOM   1542  N   PHE A 100      24.975  32.960  -1.760  1.00 24.64           N  
ANISOU 1542  N   PHE A 100     1760   5047   2554   -520    271  -1593       N  
ATOM   1543  CA  PHE A 100      24.881  33.820  -2.935  1.00 22.70           C  
ANISOU 1543  CA  PHE A 100     1551   4805   2268   -640    323  -1556       C  
ATOM   1544  C   PHE A 100      26.070  33.484  -3.858  1.00 26.60           C  
ANISOU 1544  C   PHE A 100     1954   5426   2728   -649    336  -1661       C  
ATOM   1545  O   PHE A 100      27.233  33.498  -3.443  1.00 25.11           O  
ANISOU 1545  O   PHE A 100     1683   5321   2537   -616    326  -1735       O  
ATOM   1546  CB  PHE A 100      24.855  35.304  -2.523  1.00 22.85           C  
ANISOU 1546  CB  PHE A 100     1620   4783   2280   -723    351  -1482       C  
ATOM   1547  CG  PHE A 100      23.565  35.728  -1.827  1.00 23.85           C  
ANISOU 1547  CG  PHE A 100     1841   4774   2447   -730    347  -1374       C  
ATOM   1548  CD1 PHE A 100      23.431  35.629  -0.443  1.00 23.82           C  
ANISOU 1548  CD1 PHE A 100     1834   4739   2476   -669    318  -1370       C  
ATOM   1549  CD2 PHE A 100      22.483  36.207  -2.564  1.00 20.32           C  
ANISOU 1549  CD2 PHE A 100     1483   4233   2006   -798    371  -1277       C  
ATOM   1550  CE1 PHE A 100      22.230  36.008   0.198  1.00 24.35           C  
ANISOU 1550  CE1 PHE A 100     1983   4685   2583   -680    317  -1278       C  
ATOM   1551  CE2 PHE A 100      21.276  36.588  -1.939  1.00 20.35           C  
ANISOU 1551  CE2 PHE A 100     1567   4104   2059   -799    365  -1178       C  
ATOM   1552  CZ  PHE A 100      21.147  36.482  -0.552  1.00 21.80           C  
ANISOU 1552  CZ  PHE A 100     1745   4261   2277   -742    341  -1183       C  
ATOM   1553  H   PHE A 100      25.318  33.339  -1.069  1.00 29.56           H  
ATOM   1554  HA  PHE A 100      24.060  33.622  -3.412  1.00 27.24           H  
ATOM   1555  HB2 PHE A 100      25.590  35.472  -1.913  1.00 27.42           H  
ATOM   1556  HB3 PHE A 100      24.956  35.850  -3.318  1.00 27.42           H  
ATOM   1557  HD1 PHE A 100      24.141  35.308   0.065  1.00 28.58           H  
ATOM   1558  HD2 PHE A 100      22.557  36.273  -3.488  1.00 24.39           H  
ATOM   1559  HE1 PHE A 100      22.157  35.937   1.122  1.00 29.22           H  
ATOM   1560  HE2 PHE A 100      20.567  36.906  -2.450  1.00 24.42           H  
ATOM   1561  HZ  PHE A 100      20.359  36.739  -0.130  1.00 26.16           H  
ATOM   1562  N   LYS A 101      25.784  33.125  -5.103  1.00 24.25           N  
ANISOU 1562  N   LYS A 101     1663   5144   2405   -693    357  -1670       N  
ATOM   1563  CA  LYS A 101      26.840  32.653  -5.971  1.00 25.68           C  
ANISOU 1563  CA  LYS A 101     1749   5445   2561   -695    370  -1778       C  
ATOM   1564  C   LYS A 101      27.872  33.750  -6.142  1.00 26.58           C  
ANISOU 1564  C   LYS A 101     1829   5640   2631   -777    405  -1796       C  
ATOM   1565  O   LYS A 101      27.521  34.920  -6.338  1.00 26.14           O  
ANISOU 1565  O   LYS A 101     1843   5545   2545   -876    434  -1711       O  
ATOM   1566  CB  LYS A 101      26.288  32.214  -7.327  1.00 25.76           C  
ANISOU 1566  CB  LYS A 101     1781   5461   2547   -749    395  -1777       C  
ATOM   1567  CG  LYS A 101      27.364  31.709  -8.255  1.00 27.37           C  
ANISOU 1567  CG  LYS A 101     1882   5791   2727   -754    416  -1893       C  
ATOM   1568  CD  LYS A 101      26.788  31.456  -9.633  1.00 34.20           C  
ANISOU 1568  CD  LYS A 101     2774   6664   3555   -833    450  -1883       C  
ATOM   1569  CE  LYS A 101      27.855  30.977 -10.617  1.00 41.85           C  
ANISOU 1569  CE  LYS A 101     3639   7764   4497   -846    482  -2004       C  
ATOM   1570  NZ  LYS A 101      28.256  29.563 -10.349  1.00 53.56           N  
ANISOU 1570  NZ  LYS A 101     5040   9264   6047   -694    453  -2103       N  
ATOM   1571  H   LYS A 101      25.001  33.146  -5.459  1.00 29.09           H  
ATOM   1572  HA  LYS A 101      27.274  31.889  -5.560  1.00 30.81           H  
ATOM   1573  HB2 LYS A 101      25.647  31.499  -7.191  1.00 30.92           H  
ATOM   1574  HB3 LYS A 101      25.855  32.971  -7.752  1.00 30.92           H  
ATOM   1575  HG2 LYS A 101      28.065  32.374  -8.332  1.00 32.85           H  
ATOM   1576  HG3 LYS A 101      27.722  30.875  -7.913  1.00 32.85           H  
ATOM   1577  HD2 LYS A 101      26.104  30.771  -9.572  1.00 41.04           H  
ATOM   1578  HD3 LYS A 101      26.408  32.279  -9.976  1.00 41.04           H  
ATOM   1579  HE2 LYS A 101      27.503  31.027 -11.520  1.00 50.22           H  
ATOM   1580  HE3 LYS A 101      28.642  31.537 -10.533  1.00 50.22           H  
ATOM   1581  HZ1 LYS A 101      28.877  29.307 -10.934  1.00 64.27           H  
ATOM   1582  HZ2 LYS A 101      28.587  29.492  -9.526  1.00 64.27           H  
ATOM   1583  HZ3 LYS A 101      27.549  29.027 -10.425  1.00 64.27           H  
ATOM   1584  N   ASP A 102      29.142  33.359  -6.035  0.83 27.92           N  
ANISOU 1584  N   ASP A 102     1888   5915   2803   -727    399  -1904       N  
ATOM   1585  CA  ASP A 102      30.276  34.277  -6.137  0.83 28.99           C  
ANISOU 1585  CA  ASP A 102     1970   6143   2903   -794    430  -1936       C  
ATOM   1586  C   ASP A 102      30.319  35.334  -5.037  0.83 32.15           C  
ANISOU 1586  C   ASP A 102     2406   6497   3313   -811    424  -1869       C  
ATOM   1587  O   ASP A 102      30.960  36.371  -5.184  0.83 29.03           O  
ANISOU 1587  O   ASP A 102     1997   6148   2885   -893    454  -1858       O  
ATOM   1588  CB  ASP A 102      30.290  34.959  -7.507  0.83 30.75           C  
ANISOU 1588  CB  ASP A 102     2215   6413   3058   -930    483  -1918       C  
ATOM   1589  CG  ASP A 102      30.505  33.977  -8.626  0.83 33.92           C  
ANISOU 1589  CG  ASP A 102     2557   6887   3443   -924    498  -2005       C  
ATOM   1590  OD1 ASP A 102      31.458  33.195  -8.504  0.83 31.59           O  
ANISOU 1590  OD1 ASP A 102     2155   6672   3175   -844    489  -2117       O  
ATOM   1591  OD2 ASP A 102      29.722  33.962  -9.602  0.83 30.10           O  
ANISOU 1591  OD2 ASP A 102     2132   6379   2926   -996    519  -1963       O  
ATOM   1592  H   ASP A 102      29.378  32.543  -5.900  0.83 33.50           H  
ATOM   1593  HA  ASP A 102      31.092  33.757  -6.066  0.83 34.79           H  
ATOM   1594  HB2 ASP A 102      29.438  35.399  -7.652  0.83 36.91           H  
ATOM   1595  HB3 ASP A 102      31.010  35.608  -7.533  0.83 36.91           H  
ATOM   1596  N   ASP A 103      29.649  35.083  -3.924  1.00 29.88           N  
ANISOU 1596  N   ASP A 103     2162   6120   3071   -738    385  -1824       N  
ATOM   1597  CA  ASP A 103      29.581  36.111  -2.898  1.00 27.50           C  
ANISOU 1597  CA  ASP A 103     1899   5769   2781   -762    383  -1758       C  
ATOM   1598  C   ASP A 103      29.355  35.456  -1.538  1.00 28.22           C  
ANISOU 1598  C   ASP A 103     1985   5817   2922   -651    331  -1763       C  
ATOM   1599  O   ASP A 103      29.613  34.267  -1.374  1.00 26.84           O  
ANISOU 1599  O   ASP A 103     1753   5673   2772   -548    294  -1832       O  
ATOM   1600  CB  ASP A 103      28.470  37.098  -3.245  1.00 28.44           C  
ANISOU 1600  CB  ASP A 103     2133   5783   2891   -855    410  -1637       C  
ATOM   1601  CG  ASP A 103      28.735  38.490  -2.736  1.00 28.16           C  
ANISOU 1601  CG  ASP A 103     2118   5726   2856   -923    426  -1582       C  
ATOM   1602  OD1 ASP A 103      29.450  38.632  -1.724  1.00 30.13           O  
ANISOU 1602  OD1 ASP A 103     2315   6011   3122   -885    408  -1619       O  
ATOM   1603  OD2 ASP A 103      28.210  39.453  -3.338  1.00 28.75           O  
ANISOU 1603  OD2 ASP A 103     2261   5744   2919  -1013    452  -1498       O  
ATOM   1604  H   ASP A 103      29.237  34.351  -3.740  0.83 35.86           H  
ATOM   1605  HA  ASP A 103      30.422  36.594  -2.869  1.00 33.00           H  
ATOM   1606  HB2 ASP A 103      28.381  37.144  -4.210  1.00 34.13           H  
ATOM   1607  HB3 ASP A 103      27.639  36.788  -2.851  1.00 34.13           H  
ATOM   1608  N   GLY A 104      28.890  36.227  -0.564  1.00 30.53           N  
ANISOU 1608  N   GLY A 104     2331   6037   3230   -669    326  -1691       N  
ATOM   1609  CA  GLY A 104      28.773  35.723   0.785  1.00 25.23           C  
ANISOU 1609  CA  GLY A 104     1650   5341   2596   -577    279  -1697       C  
ATOM   1610  C   GLY A 104      27.541  34.864   1.002  1.00 24.44           C  
ANISOU 1610  C   GLY A 104     1611   5152   2524   -516    253  -1655       C  
ATOM   1611  O   GLY A 104      26.833  34.479   0.049  1.00 23.67           O  
ANISOU 1611  O   GLY A 104     1555   5019   2422   -533    267  -1634       O  
ATOM   1612  H   GLY A 104      28.637  37.043  -0.662  1.00 36.63           H  
ATOM   1613  HA2 GLY A 104      29.556  35.191   0.996  1.00 30.28           H  
ATOM   1614  HA3 GLY A 104      28.736  36.470   1.403  1.00 30.28           H  
ATOM   1615  N   ASN A 105      27.279  34.539   2.265  1.00 23.77           N  
ANISOU 1615  N   ASN A 105     1529   5035   2468   -448    212  -1642       N  
ATOM   1616  CA  ASN A 105      26.134  33.716   2.600  1.00 22.81           C  
ANISOU 1616  CA  ASN A 105     1460   4834   2374   -386    183  -1600       C  
ATOM   1617  C   ASN A 105      25.394  34.251   3.800  1.00 23.90           C  
ANISOU 1617  C   ASN A 105     1654   4900   2528   -401    176  -1530       C  
ATOM   1618  O   ASN A 105      25.989  34.929   4.659  1.00 23.06           O  
ANISOU 1618  O   ASN A 105     1522   4825   2417   -420    172  -1538       O  
ATOM   1619  CB  ASN A 105      26.577  32.293   2.919  1.00 23.45           C  
ANISOU 1619  CB  ASN A 105     1472   4957   2481   -251    119  -1670       C  
ATOM   1620  CG  ASN A 105      27.494  32.235   4.129  1.00 29.41           C  
ANISOU 1620  CG  ASN A 105     2159   5765   3248   -191     72  -1706       C  
ATOM   1621  OD1 ASN A 105      27.028  32.202   5.274  1.00 26.95           O  
ANISOU 1621  OD1 ASN A 105     1874   5412   2952   -163     36  -1661       O  
ATOM   1622  ND2 ASN A 105      28.802  32.229   3.884  1.00 28.22           N  
ANISOU 1622  ND2 ASN A 105     1920   5709   3093   -178     69  -1786       N  
ATOM   1623  H   ASN A 105      27.750  34.784   2.941  1.00 28.53           H  
ATOM   1624  HA  ASN A 105      25.523  33.688   1.848  1.00 27.38           H  
ATOM   1625  HB2 ASN A 105      25.795  31.751   3.106  1.00 28.14           H  
ATOM   1626  HB3 ASN A 105      27.059  31.932   2.158  1.00 28.14           H  
ATOM   1627 HD21 ASN A 105      29.088  32.257   3.074  1.00 33.86           H  
ATOM   1628 HD22 ASN A 105      29.361  32.197   4.537  1.00 33.86           H  
ATOM   1629  N   TYR A 106      24.103  33.935   3.862  1.00 23.65           N  
ANISOU 1629  N   TYR A 106     1694   4775   2517   -394    173  -1465       N  
ATOM   1630  CA  TYR A 106      23.316  34.175   5.064  1.00 20.90           C  
ANISOU 1630  CA  TYR A 106     1390   4362   2188   -393    158  -1408       C  
ATOM   1631  C   TYR A 106      23.092  32.877   5.802  1.00 24.50           C  
ANISOU 1631  C   TYR A 106     1823   4822   2666   -279     89  -1420       C  
ATOM   1632  O   TYR A 106      22.815  31.845   5.188  1.00 20.22           O  
ANISOU 1632  O   TYR A 106     1275   4270   2138   -214     65  -1434       O  
ATOM   1633  CB  TYR A 106      21.937  34.732   4.718  1.00 19.20           C  
ANISOU 1633  CB  TYR A 106     1275   4028   1991   -466    197  -1317       C  
ATOM   1634  CG  TYR A 106      21.885  36.118   4.106  1.00 19.95           C  
ANISOU 1634  CG  TYR A 106     1417   4082   2081   -575    251  -1274       C  
ATOM   1635  CD1 TYR A 106      22.972  36.983   4.150  1.00 19.79           C  
ANISOU 1635  CD1 TYR A 106     1355   4126   2038   -616    266  -1311       C  
ATOM   1636  CD2 TYR A 106      20.720  36.563   3.488  1.00 18.11           C  
ANISOU 1636  CD2 TYR A 106     1270   3736   1875   -630    279  -1189       C  
ATOM   1637  CE1 TYR A 106      22.896  38.254   3.592  1.00 21.60           C  
ANISOU 1637  CE1 TYR A 106     1627   4310   2271   -708    305  -1264       C  
ATOM   1638  CE2 TYR A 106      20.629  37.822   2.946  1.00 18.29           C  
ANISOU 1638  CE2 TYR A 106     1336   3707   1905   -715    313  -1138       C  
ATOM   1639  CZ  TYR A 106      21.720  38.667   2.990  1.00 24.40           C  
ANISOU 1639  CZ  TYR A 106     2067   4549   2656   -753    325  -1175       C  
ATOM   1640  OH  TYR A 106      21.622  39.925   2.435  1.00 18.90           O  
ANISOU 1640  OH  TYR A 106     1409   3797   1973   -831    351  -1119       O  
ATOM   1641  H   TYR A 106      23.659  33.578   3.218  1.00 28.38           H  
ATOM   1642  HA  TYR A 106      23.776  34.799   5.647  1.00 25.08           H  
ATOM   1643  HB2 TYR A 106      21.516  34.126   4.088  1.00 23.04           H  
ATOM   1644  HB3 TYR A 106      21.411  34.761   5.533  1.00 23.04           H  
ATOM   1645  HD1 TYR A 106      23.761  36.707   4.557  1.00 23.75           H  
ATOM   1646  HD2 TYR A 106      19.979  36.001   3.458  1.00 21.73           H  
ATOM   1647  HE1 TYR A 106      23.630  38.825   3.628  1.00 25.92           H  
ATOM   1648  HE2 TYR A 106      19.841  38.097   2.536  1.00 21.95           H  
ATOM   1649  HH  TYR A 106      20.856  40.036   2.108  1.00 22.68           H  
ATOM   1650  N   LYS A 107      23.179  32.936   7.126  1.00 20.92           N  
ANISOU 1650  N   LYS A 107     1359   4375   2214   -255     48  -1411       N  
ATOM   1651  CA  LYS A 107      22.658  31.877   7.959  1.00 20.29           C  
ANISOU 1651  CA  LYS A 107     1291   4266   2153   -167    -32  -1387       C  
ATOM   1652  C   LYS A 107      21.535  32.475   8.781  1.00 19.44           C  
ANISOU 1652  C   LYS A 107     1261   4082   2044   -234    -18  -1314       C  
ATOM   1653  O   LYS A 107      21.698  33.539   9.395  1.00 19.53           O  
ANISOU 1653  O   LYS A 107     1279   4100   2040   -307     17  -1309       O  
ATOM   1654  CB  LYS A 107      23.751  31.310   8.853  1.00 22.82           C  
ANISOU 1654  CB  LYS A 107     1543   4657   2470    -84   -116  -1432       C  
ATOM   1655  CG  LYS A 107      24.807  30.526   8.092  1.00 28.41           C  
ANISOU 1655  CG  LYS A 107     2171   5429   3193      0   -140  -1512       C  
ATOM   1656  CD  LYS A 107      25.895  30.017   9.035  1.00 34.84           C  
ANISOU 1656  CD  LYS A 107     2919   6300   4017     80   -231  -1548       C  
ATOM   1657  H   LYS A 107      23.538  33.584   7.563  1.00 25.10           H  
ATOM   1658  HA  LYS A 107      22.301  31.165   7.405  1.00 24.35           H  
ATOM   1659  HB2 LYS A 107      24.194  32.042   9.309  1.00 27.38           H  
ATOM   1660  HB3 LYS A 107      23.347  30.713   9.503  1.00 27.38           H  
ATOM   1661  HG2 LYS A 107      24.393  29.761   7.662  1.00 34.09           H  
ATOM   1662  HG3 LYS A 107      25.221  31.102   7.431  1.00 34.09           H  
ATOM   1663  N   THR A 108      20.402  31.792   8.793  1.00 18.71           N  
ANISOU 1663  N   THR A 108     1227   3914   1967   -208    -46  -1261       N  
ATOM   1664  CA  THR A 108      19.228  32.303   9.464  1.00 17.92           C  
ANISOU 1664  CA  THR A 108     1208   3734   1868   -276    -27  -1197       C  
ATOM   1665  C   THR A 108      18.607  31.250  10.354  1.00 18.59           C  
ANISOU 1665  C   THR A 108     1347   3781   1935   -208   -123  -1161       C  
ATOM   1666  O   THR A 108      18.663  30.060  10.060  1.00 18.03           O  
ANISOU 1666  O   THR A 108     1276   3706   1871   -110   -195  -1163       O  
ATOM   1667  CB  THR A 108      18.177  32.788   8.482  1.00 16.96           C  
ANISOU 1667  CB  THR A 108     1140   3526   1777   -348     48  -1149       C  
ATOM   1668  OG1 THR A 108      17.698  31.667   7.726  1.00 17.26           O  
ANISOU 1668  OG1 THR A 108     1192   3535   1832   -285     11  -1136       O  
ATOM   1669  CG2 THR A 108      18.766  33.855   7.534  1.00 17.13           C  
ANISOU 1669  CG2 THR A 108     1147   3565   1798   -418    127  -1168       C  
ATOM   1670  H   THR A 108      20.289  31.027   8.416  1.00 22.45           H  
ATOM   1671  HA  THR A 108      19.486  33.053  10.022  1.00 21.51           H  
ATOM   1672  HB  THR A 108      17.439  33.186   8.971  1.00 20.35           H  
ATOM   1673  HG1 THR A 108      17.359  31.096   8.241  1.00 20.71           H  
ATOM   1674 HG21 THR A 108      18.085  34.157   6.912  1.00 20.56           H  
ATOM   1675 HG22 THR A 108      19.084  34.614   8.047  1.00 20.56           H  
ATOM   1676 HG23 THR A 108      19.507  33.480   7.033  1.00 20.56           H  
ATOM   1677  N   ARG A 109      18.016  31.715  11.452  1.00 17.68           N  
ANISOU 1677  N   ARG A 109     1289   3634   1793   -261   -122  -1128       N  
ATOM   1678  CA  ARG A 109      17.268  30.857  12.326  1.00 17.59           C  
ANISOU 1678  CA  ARG A 109     1360   3577   1746   -219   -201  -1081       C  
ATOM   1679  C   ARG A 109      16.042  31.624  12.736  1.00 16.86           C  
ANISOU 1679  C   ARG A 109     1345   3411   1649   -318   -133  -1042       C  
ATOM   1680  O   ARG A 109      16.144  32.760  13.211  1.00 20.14           O  
ANISOU 1680  O   ARG A 109     1747   3840   2066   -401    -68  -1062       O  
ATOM   1681  CB  ARG A 109      18.078  30.459  13.568  1.00 18.61           C  
ANISOU 1681  CB  ARG A 109     1479   3766   1823   -171   -290  -1090       C  
ATOM   1682  CG  ARG A 109      17.298  29.582  14.525  1.00 18.64           C  
ANISOU 1682  CG  ARG A 109     1583   3723   1774   -138   -374  -1027       C  
ATOM   1683  CD  ARG A 109      17.986  29.399  15.889  1.00 21.02           C  
ANISOU 1683  CD  ARG A 109     1891   4080   2016   -124   -456  -1022       C  
ATOM   1684  NE  ARG A 109      17.301  28.338  16.628  1.00 27.39           N  
ANISOU 1684  NE  ARG A 109     2795   4841   2771    -79   -549   -948       N  
ATOM   1685  CZ  ARG A 109      16.215  28.509  17.383  1.00 30.06           C  
ANISOU 1685  CZ  ARG A 109     3231   5140   3050   -146   -525   -901       C  
ATOM   1686  NH1 ARG A 109      15.682  29.719  17.563  1.00 25.98           N  
ANISOU 1686  NH1 ARG A 109     2727   4616   2528   -257   -408   -927       N  
ATOM   1687  NH2 ARG A 109      15.661  27.457  17.969  1.00 30.27           N  
ANISOU 1687  NH2 ARG A 109     3350   5111   3039    -99   -605   -813       N  
ATOM   1688  H   ARG A 109      18.041  32.536  11.705  1.00 21.21           H  
ATOM   1689  HA  ARG A 109      16.996  30.054  11.854  1.00 21.11           H  
ATOM   1690  HB2 ARG A 109      18.866  29.969  13.286  1.00 22.33           H  
ATOM   1691  HB3 ARG A 109      18.340  31.262  14.044  1.00 22.33           H  
ATOM   1692  HG2 ARG A 109      16.429  29.983  14.682  1.00 22.36           H  
ATOM   1693  HG3 ARG A 109      17.188  28.704  14.127  1.00 22.36           H  
ATOM   1694  HD2 ARG A 109      18.912  29.140  15.758  1.00 25.23           H  
ATOM   1695  HD3 ARG A 109      17.928  30.222  16.399  1.00 25.23           H  
ATOM   1696  HE  ARG A 109      17.623  27.542  16.571  1.00 32.87           H  
ATOM   1697 HH11 ARG A 109      16.030  30.404  17.177  1.00 31.18           H  
ATOM   1698 HH12 ARG A 109      14.985  29.812  18.059  1.00 31.18           H  
ATOM   1699 HH21 ARG A 109      16.006  26.676  17.866  1.00 36.32           H  
ATOM   1700 HH22 ARG A 109      14.972  27.559  18.474  1.00 36.32           H  
ATOM   1701  N   ALA A 110      14.897  30.976  12.572  1.00 16.22           N  
ANISOU 1701  N   ALA A 110     1357   3225   1581   -294   -135   -967       N  
ATOM   1702  CA  ALA A 110      13.615  31.587  12.832  1.00 15.82           C  
ANISOU 1702  CA  ALA A 110     1384   3074   1551   -372    -57   -913       C  
ATOM   1703  C   ALA A 110      12.700  30.649  13.617  1.00 16.32           C  
ANISOU 1703  C   ALA A 110     1557   3062   1581   -328   -102   -829       C  
ATOM   1704  O   ALA A 110      12.776  29.408  13.488  1.00 16.68           O  
ANISOU 1704  O   ALA A 110     1633   3089   1616   -231   -186   -787       O  
ATOM   1705  CB  ALA A 110      12.949  31.987  11.496  1.00 15.39           C  
ANISOU 1705  CB  ALA A 110     1331   2940   1577   -412     19   -883       C  
ATOM   1706  H   ALA A 110      14.842  30.160  12.304  1.00 19.46           H  
ATOM   1707  HA  ALA A 110      13.747  32.391  13.358  1.00 18.98           H  
ATOM   1708  HB1 ALA A 110      12.089  32.396  11.683  1.00 18.47           H  
ATOM   1709  HB2 ALA A 110      13.522  32.618  11.034  1.00 18.47           H  
ATOM   1710  HB3 ALA A 110      12.826  31.191  10.954  1.00 18.47           H  
ATOM   1711  N   GLU A 111      11.808  31.252  14.392  1.00 15.27           N  
ANISOU 1711  N   GLU A 111     1482   2883   1438   -402    -42   -805       N  
ATOM   1712  CA  GLU A 111      10.742  30.521  15.025  1.00 16.38           C  
ANISOU 1712  CA  GLU A 111     1726   2943   1554   -385    -58   -719       C  
ATOM   1713  C   GLU A 111       9.443  31.067  14.496  1.00 17.64           C  
ANISOU 1713  C   GLU A 111     1924   2986   1792   -444     40   -673       C  
ATOM   1714  O   GLU A 111       9.200  32.274  14.556  1.00 14.13           O  
ANISOU 1714  O   GLU A 111     1452   2533   1385   -532    128   -715       O  
ATOM   1715  CB  GLU A 111      10.807  30.642  16.559  1.00 16.01           C  
ANISOU 1715  CB  GLU A 111     1715   2955   1414   -422    -78   -733       C  
ATOM   1716  CG  GLU A 111      12.089  30.005  17.097  1.00 20.67           C  
ANISOU 1716  CG  GLU A 111     2268   3655   1931   -359   -196   -765       C  
ATOM   1717  CD  GLU A 111      12.095  29.863  18.607  1.00 30.32           C  
ANISOU 1717  CD  GLU A 111     3545   4931   3045   -391   -240   -755       C  
ATOM   1718  OE1 GLU A 111      11.057  30.169  19.255  1.00 30.53           O  
ANISOU 1718  OE1 GLU A 111     3642   4911   3046   -459   -172   -725       O  
ATOM   1719  OE2 GLU A 111      13.158  29.448  19.129  1.00 26.28           O  
ANISOU 1719  OE2 GLU A 111     3000   4511   2476   -352   -343   -780       O  
ATOM   1720  H   GLU A 111      11.805  32.095  14.564  1.00 18.33           H  
ATOM   1721  HA  GLU A 111      10.804  29.583  14.786  1.00 19.65           H  
ATOM   1722  HB2 GLU A 111      10.802  31.579  16.809  1.00 19.22           H  
ATOM   1723  HB3 GLU A 111      10.048  30.182  16.951  1.00 19.22           H  
ATOM   1724  HG2 GLU A 111      12.186  29.120  16.714  1.00 24.80           H  
ATOM   1725  HG3 GLU A 111      12.845  30.559  16.847  1.00 24.80           H  
ATOM   1726  N   VAL A 112       8.626  30.157  13.983  1.00 14.34           N  
ANISOU 1726  N   VAL A 112     1569   2474   1405   -395     18   -586       N  
ATOM   1727  CA  VAL A 112       7.324  30.486  13.432  1.00 13.02           C  
ANISOU 1727  CA  VAL A 112     1442   2186   1320   -441     95   -526       C  
ATOM   1728  C   VAL A 112       6.240  29.779  14.237  1.00 18.52           C  
ANISOU 1728  C   VAL A 112     2232   2814   1989   -434     86   -443       C  
ATOM   1729  O   VAL A 112       6.230  28.553  14.339  1.00 13.22           O  
ANISOU 1729  O   VAL A 112     1613   2130   1280   -360     -1   -385       O  
ATOM   1730  CB  VAL A 112       7.236  30.024  11.968  1.00 13.59           C  
ANISOU 1730  CB  VAL A 112     1506   2201   1457   -400     77   -490       C  
ATOM   1731  CG1 VAL A 112       5.906  30.427  11.353  1.00 11.69           C  
ANISOU 1731  CG1 VAL A 112     1301   1834   1308   -454    148   -423       C  
ATOM   1732  CG2 VAL A 112       8.413  30.569  11.154  1.00 16.60           C  
ANISOU 1732  CG2 VAL A 112     1792   2667   1848   -405     80   -571       C  
ATOM   1733  H   VAL A 112       8.811  29.318  13.943  1.00 17.21           H  
ATOM   1734  HA  VAL A 112       7.177  31.444  13.473  1.00 15.63           H  
ATOM   1735  HB  VAL A 112       7.288  29.056  11.945  1.00 16.31           H  
ATOM   1736 HG11 VAL A 112       5.879  30.123  10.432  1.00 14.03           H  
ATOM   1737 HG12 VAL A 112       5.187  30.015  11.859  1.00 14.03           H  
ATOM   1738 HG13 VAL A 112       5.822  31.393  11.386  1.00 14.03           H  
ATOM   1739 HG21 VAL A 112       8.331  30.263  10.237  1.00 19.92           H  
ATOM   1740 HG22 VAL A 112       8.394  31.538  11.182  1.00 19.92           H  
ATOM   1741 HG23 VAL A 112       9.241  30.242  11.540  1.00 19.92           H  
ATOM   1742  N   LYS A 113       5.318  30.537  14.817  1.00 13.85           N  
ANISOU 1742  N   LYS A 113     1662   2179   1421   -512    174   -440       N  
ATOM   1743  CA  LYS A 113       4.313  29.938  15.705  1.00 14.07           C  
ANISOU 1743  CA  LYS A 113     1773   2162   1413   -519    178   -369       C  
ATOM   1744  C   LYS A 113       3.144  30.865  15.903  1.00 14.06           C  
ANISOU 1744  C   LYS A 113     1776   2085   1483   -603    296   -369       C  
ATOM   1745  O   LYS A 113       3.235  32.054  15.587  1.00 14.87           O  
ANISOU 1745  O   LYS A 113     1816   2181   1653   -659    368   -434       O  
ATOM   1746  CB  LYS A 113       4.932  29.651  17.085  1.00 17.05           C  
ANISOU 1746  CB  LYS A 113     2173   2645   1660   -521    129   -399       C  
ATOM   1747  CG  LYS A 113       5.286  30.903  17.881  1.00 22.26           C  
ANISOU 1747  CG  LYS A 113     2788   3379   2289   -603    203   -502       C  
ATOM   1748  CD  LYS A 113       5.961  30.547  19.205  1.00 27.72           C  
ANISOU 1748  CD  LYS A 113     3508   4184   2841   -608    140   -526       C  
ATOM   1749  H   LYS A 113       5.249  31.389  14.720  1.00 16.62           H  
ATOM   1750  HA  LYS A 113       3.992  29.105  15.326  1.00 16.89           H  
ATOM   1751  HB2 LYS A 113       4.299  29.137  17.610  1.00 20.46           H  
ATOM   1752  HB3 LYS A 113       5.747  29.140  16.960  1.00 20.46           H  
ATOM   1753  HG2 LYS A 113       5.899  31.449  17.364  1.00 26.71           H  
ATOM   1754  HG3 LYS A 113       4.476  31.399  18.076  1.00 26.71           H  
ATOM   1755  N   PHE A 114       2.055  30.331  16.454  1.00 14.81           N  
ANISOU 1755  N   PHE A 114     1937   2122   1567   -614    314   -297       N  
ATOM   1756  CA  PHE A 114       0.939  31.174  16.850  1.00 14.41           C  
ANISOU 1756  CA  PHE A 114     1884   2010   1580   -692    430   -307       C  
ATOM   1757  C   PHE A 114       1.085  31.746  18.254  1.00 14.34           C  
ANISOU 1757  C   PHE A 114     1878   2089   1483   -754    484   -386       C  
ATOM   1758  O   PHE A 114       1.469  31.035  19.203  1.00 19.86           O  
ANISOU 1758  O   PHE A 114     2626   2870   2050   -742    426   -375       O  
ATOM   1759  CB  PHE A 114      -0.346  30.384  16.803  1.00 20.54           C  
ANISOU 1759  CB  PHE A 114     2723   2689   2390   -684    436   -198       C  
ATOM   1760  CG  PHE A 114      -1.011  30.407  15.464  1.00 16.46           C  
ANISOU 1760  CG  PHE A 114     2192   2052   2008   -670    444   -137       C  
ATOM   1761  CD1 PHE A 114      -0.804  29.389  14.576  1.00 18.21           C  
ANISOU 1761  CD1 PHE A 114     2445   2243   2232   -599    350    -66       C  
ATOM   1762  CD2 PHE A 114      -1.844  31.461  15.110  1.00 15.80           C  
ANISOU 1762  CD2 PHE A 114     2064   1885   2054   -730    542   -153       C  
ATOM   1763  CE1 PHE A 114      -1.434  29.404  13.330  1.00 15.22           C  
ANISOU 1763  CE1 PHE A 114     2058   1756   1967   -595    354     -9       C  
ATOM   1764  CE2 PHE A 114      -2.471  31.482  13.894  1.00 21.37           C  
ANISOU 1764  CE2 PHE A 114     2756   2500   2863   -655    489    -82       C  
ATOM   1765  CZ  PHE A 114      -2.262  30.452  12.998  1.00 16.17           C  
ANISOU 1765  CZ  PHE A 114     2132   1810   2202   -629    423    -13       C  
ATOM   1766  H   PHE A 114       1.941  29.493  16.606  1.00 17.77           H  
ATOM   1767  HA  PHE A 114       0.863  31.915  16.228  1.00 17.29           H  
ATOM   1768  HB2 PHE A 114      -0.153  29.459  17.024  1.00 24.64           H  
ATOM   1769  HB3 PHE A 114      -0.966  30.755  17.450  1.00 24.64           H  
ATOM   1770  HD1 PHE A 114      -0.248  28.679  14.805  1.00 21.85           H  
ATOM   1771  HD2 PHE A 114      -1.991  32.153  15.715  1.00 18.96           H  
ATOM   1772  HE1 PHE A 114      -1.293  28.710  12.726  1.00 18.26           H  
ATOM   1773  HE2 PHE A 114      -3.027  32.193  13.668  1.00 25.64           H  
ATOM   1774  HZ  PHE A 114      -2.679  30.468  12.167  1.00 19.41           H  
ATOM   1775  N   GLU A 115       0.745  33.022  18.370  1.00 14.32           N  
ANISOU 1775  N   GLU A 115     1824   2061   1554   -824    591   -464       N  
ATOM   1776  CA  GLU A 115       0.583  33.685  19.653  1.00 16.22           C  
ANISOU 1776  CA  GLU A 115     2068   2362   1735   -896    670   -548       C  
ATOM   1777  C   GLU A 115      -0.815  34.307  19.621  1.00 19.82           C  
ANISOU 1777  C   GLU A 115     2510   2706   2313   -947    790   -545       C  
ATOM   1778  O   GLU A 115      -1.048  35.344  19.022  1.00 16.65           O  
ANISOU 1778  O   GLU A 115     2066   2221   2039   -921    804   -581       O  
ATOM   1779  CB  GLU A 115       1.738  34.681  19.909  1.00 18.75           C  
ANISOU 1779  CB  GLU A 115     2329   2771   2025   -928    677   -670       C  
ATOM   1780  CG  GLU A 115       3.050  33.920  20.149  1.00 20.60           C  
ANISOU 1780  CG  GLU A 115     2577   3123   2126   -877    555   -667       C  
ATOM   1781  CD  GLU A 115       4.248  34.788  20.496  1.00 31.63           C  
ANISOU 1781  CD  GLU A 115     3917   4622   3479   -910    549   -783       C  
ATOM   1782  OE1 GLU A 115       4.230  36.002  20.187  1.00 20.20           O  
ANISOU 1782  OE1 GLU A 115     2409   3141   2125   -962    625   -860       O  
ATOM   1783  OE2 GLU A 115       5.207  34.230  21.103  1.00 32.45           O  
ANISOU 1783  OE2 GLU A 115     4036   4836   3456   -887    459   -792       O  
ATOM   1784  H   GLU A 115       0.599  33.538  17.698  1.00 17.18           H  
ATOM   1785  HA  GLU A 115       0.600  33.020  20.359  1.00 19.47           H  
ATOM   1786  HB2 GLU A 115       1.851  35.253  19.133  1.00 22.50           H  
ATOM   1787  HB3 GLU A 115       1.541  35.211  20.697  1.00 22.50           H  
ATOM   1788  HG2 GLU A 115       2.916  33.300  20.882  1.00 24.72           H  
ATOM   1789  HG3 GLU A 115       3.271  33.427  19.343  1.00 24.72           H  
ATOM   1790  N   GLY A 116      -1.763  33.613  20.241  1.00 19.37           N  
ANISOU 1790  N   GLY A 116     2511   2631   2216   -957    813   -483       N  
ATOM   1791  CA  GLY A 116      -3.158  33.973  20.113  1.00 18.29           C  
ANISOU 1791  CA  GLY A 116     2372   2372   2204   -931    855   -454       C  
ATOM   1792  C   GLY A 116      -3.587  33.814  18.657  1.00 14.11           C  
ANISOU 1792  C   GLY A 116     1827   1728   1807   -843    788   -362       C  
ATOM   1793  O   GLY A 116      -3.340  32.784  18.033  1.00 18.20           O  
ANISOU 1793  O   GLY A 116     2373   2239   2302   -823    727   -276       O  
ATOM   1794  H   GLY A 116      -1.619  32.929  20.741  1.00 23.24           H  
ATOM   1795  HA2 GLY A 116      -3.704  33.396  20.669  1.00 21.94           H  
ATOM   1796  HA3 GLY A 116      -3.291  34.895  20.384  1.00 21.94           H  
ATOM   1797  N   ASP A 117      -4.209  34.856  18.119  1.00 17.13           N  
ANISOU 1797  N   ASP A 117     2166   2029   2314   -791    794   -381       N  
ATOM   1798  CA  ASP A 117      -4.753  34.792  16.771  1.00 20.52           C  
ANISOU 1798  CA  ASP A 117     2578   2375   2844   -706    720   -285       C  
ATOM   1799  C   ASP A 117      -3.673  35.123  15.739  1.00 22.87           C  
ANISOU 1799  C   ASP A 117     2847   2687   3154   -683    664   -291       C  
ATOM   1800  O   ASP A 117      -3.937  35.049  14.546  1.00 18.51           O  
ANISOU 1800  O   ASP A 117     2284   2090   2658   -625    592   -213       O  
ATOM   1801  CB  ASP A 117      -5.964  35.731  16.613  1.00 24.72           C  
ANISOU 1801  CB  ASP A 117     3078   2837   3480   -666    739   -285       C  
ATOM   1802  CG  ASP A 117      -5.599  37.229  16.628  1.00 36.54           C  
ANISOU 1802  CG  ASP A 117     4533   4327   5025   -670    777   -382       C  
ATOM   1803  OD1 ASP A 117      -4.444  37.612  16.924  1.00 33.00           O  
ANISOU 1803  OD1 ASP A 117     4079   3934   4527   -711    796   -462       O  
ATOM   1804  OD2 ASP A 117      -6.502  38.055  16.356  1.00 48.96           O  
ANISOU 1804  OD2 ASP A 117     6077   5839   6686   -636    787   -379       O  
ATOM   1805  H   ASP A 117      -4.329  35.610  18.514  1.00 20.56           H  
ATOM   1806  HA  ASP A 117      -5.057  33.887  16.601  1.00 24.62           H  
ATOM   1807  HB2 ASP A 117      -6.398  35.541  15.766  1.00 29.67           H  
ATOM   1808  HB3 ASP A 117      -6.582  35.570  17.342  1.00 29.67           H  
ATOM   1809  N   THR A 118      -2.466  35.477  16.191  1.00 12.71           N  
ANISOU 1809  N   THR A 118     1547   1478   1803   -736    690   -385       N  
ATOM   1810  CA  THR A 118      -1.415  35.949  15.261  1.00 12.90           C  
ANISOU 1810  CA  THR A 118     1535   1524   1842   -718    645   -403       C  
ATOM   1811  C   THR A 118      -0.307  34.929  14.988  1.00 15.35           C  
ANISOU 1811  C   THR A 118     1849   1909   2073   -744    605   -398       C  
ATOM   1812  O   THR A 118       0.269  34.336  15.911  1.00 14.79           O  
ANISOU 1812  O   THR A 118     1788   1934   1897   -810    627   -442       O  
ATOM   1813  CB  THR A 118      -0.769  37.220  15.821  1.00 12.92           C  
ANISOU 1813  CB  THR A 118     1504   1568   1838   -754    690   -519       C  
ATOM   1814  OG1 THR A 118      -1.766  38.239  15.965  1.00 22.39           O  
ANISOU 1814  OG1 THR A 118     2694   2692   3121   -730    728   -530       O  
ATOM   1815  CG2 THR A 118       0.343  37.760  14.910  1.00 14.38           C  
ANISOU 1815  CG2 THR A 118     1650   1782   2030   -739    645   -535       C  
ATOM   1816  H   THR A 118      -2.226  35.455  17.017  1.00 15.25           H  
ATOM   1817  HA  THR A 118      -1.827  36.174  14.412  1.00 15.48           H  
ATOM   1818  HB  THR A 118      -0.382  37.026  16.689  1.00 15.51           H  
ATOM   1819  HG1 THR A 118      -2.368  37.980  16.491  1.00 26.87           H  
ATOM   1820 HG21 THR A 118       0.727  38.562  15.297  1.00 17.25           H  
ATOM   1821 HG22 THR A 118       1.041  37.094  14.809  1.00 17.25           H  
ATOM   1822 HG23 THR A 118      -0.019  37.973  14.036  1.00 17.25           H  
ATOM   1823  N   LEU A 119       0.011  34.760  13.710  1.00 14.65           N  
ANISOU 1823  N   LEU A 119     1746   1794   2024   -699    544   -346       N  
ATOM   1824  CA  LEU A 119       1.158  33.961  13.287  1.00 11.43           C  
ANISOU 1824  CA  LEU A 119     1323   1463   1556   -722    506   -362       C  
ATOM   1825  C   LEU A 119       2.394  34.852  13.329  1.00 13.68           C  
ANISOU 1825  C   LEU A 119     1547   1838   1811   -746    509   -462       C  
ATOM   1826  O   LEU A 119       2.462  35.874  12.641  1.00 14.73           O  
ANISOU 1826  O   LEU A 119     1662   1932   2002   -713    501   -459       O  
ATOM   1827  CB  LEU A 119       0.889  33.415  11.877  1.00 12.67           C  
ANISOU 1827  CB  LEU A 119     1494   1551   1768   -667    445   -271       C  
ATOM   1828  CG  LEU A 119       1.789  32.331  11.278  1.00 12.37           C  
ANISOU 1828  CG  LEU A 119     1456   1569   1675   -658    388   -270       C  
ATOM   1829  CD1 LEU A 119       3.107  32.976  10.826  1.00 14.62           C  
ANISOU 1829  CD1 LEU A 119     1668   1949   1938   -671    377   -355       C  
ATOM   1830  CD2 LEU A 119       2.023  31.196  12.295  1.00 13.83           C  
ANISOU 1830  CD2 LEU A 119     1698   1814   1743   -594    327   -256       C  
ATOM   1831  H   LEU A 119      -0.430  35.103  13.056  1.00 17.58           H  
ATOM   1832  HA  LEU A 119       1.285  33.216  13.895  1.00 13.71           H  
ATOM   1833  HB2 LEU A 119      -0.011  33.055  11.873  1.00 15.20           H  
ATOM   1834  HB3 LEU A 119       0.924  34.167  11.265  1.00 15.20           H  
ATOM   1835  HG  LEU A 119       1.354  31.953  10.497  1.00 14.85           H  
ATOM   1836 HD11 LEU A 119       3.679  32.290  10.446  1.00 17.54           H  
ATOM   1837 HD12 LEU A 119       2.914  33.654  10.160  1.00 17.54           H  
ATOM   1838 HD13 LEU A 119       3.540  33.380  11.594  1.00 17.54           H  
ATOM   1839 HD21 LEU A 119       2.594  30.524  11.891  1.00 16.60           H  
ATOM   1840 HD22 LEU A 119       2.450  31.564  13.084  1.00 16.60           H  
ATOM   1841 HD23 LEU A 119       1.168  30.805  12.533  1.00 16.60           H  
ATOM   1842  N  AVAL A 120       3.385  34.437  14.111  0.25 12.90           N  
ANISOU 1842  N  AVAL A 120     1431   1866   1604   -767    489   -529       N  
ATOM   1843  N  BVAL A 120       3.363  34.500  14.177  0.75 13.36           N  
ANISOU 1843  N  BVAL A 120     1489   1925   1663   -771    494   -533       N  
ATOM   1844  CA AVAL A 120       4.568  35.248  14.363  0.25 12.62           C  
ANISOU 1844  CA AVAL A 120     1332   1933   1531   -797    491   -632       C  
ATOM   1845  CA BVAL A 120       4.581  35.297  14.312  0.75 12.61           C  
ANISOU 1845  CA BVAL A 120     1326   1929   1534   -800    492   -633       C  
ATOM   1846  C  AVAL A 120       5.821  34.565  13.819  0.25 13.15           C  
ANISOU 1846  C  AVAL A 120     1372   2093   1531   -732    399   -640       C  
ATOM   1847  C  BVAL A 120       5.752  34.549  13.697  0.75 12.58           C  
ANISOU 1847  C  BVAL A 120     1301   2011   1469   -732    400   -633       C  
ATOM   1848  O  AVAL A 120       6.044  33.385  14.074  0.25 16.38           O  
ANISOU 1848  O  AVAL A 120     1824   2536   1863   -658    324   -602       O  
ATOM   1849  O  BVAL A 120       5.826  33.317  13.746  0.75 12.85           O  
ANISOU 1849  O  BVAL A 120     1381   2059   1441   -655    327   -581       O  
ATOM   1850  CB AVAL A 120       4.732  35.485  15.875  0.25 19.41           C  
ANISOU 1850  CB AVAL A 120     2208   2868   2299   -827    514   -700       C  
ATOM   1851  CB BVAL A 120       4.910  35.665  15.791  0.75 13.45           C  
ANISOU 1851  CB BVAL A 120     1439   2123   1550   -834    516   -714       C  
ATOM   1852  CG1AVAL A 120       5.902  36.394  16.148  0.25 13.96           C  
ANISOU 1852  CG1AVAL A 120     1451   2277   1578   -868    516   -807       C  
ATOM   1853  CG1BVAL A 120       3.717  36.351  16.440  0.75 19.28           C  
ANISOU 1853  CG1BVAL A 120     2198   2780   2348   -895    615   -727       C  
ATOM   1854  CG2AVAL A 120       3.445  36.071  16.465  0.25 17.70           C  
ANISOU 1854  CG2AVAL A 120     2015   2565   2147   -887    614   -701       C  
ATOM   1855  CG2BVAL A 120       5.314  34.427  16.586  0.75 24.61           C  
ANISOU 1855  CG2BVAL A 120     2908   3617   2827   -770    432   -686       C  
ATOM   1856  H  AVAL A 120       3.395  33.676  14.513  0.25 15.48           H  
ATOM   1857  H  BVAL A 120       3.337  33.806  14.684  0.75 16.03           H  
ATOM   1858  HA AVAL A 120       4.470  36.108  13.925  0.25 15.15           H  
ATOM   1859  HA BVAL A 120       4.468  36.125  13.819  0.75 15.13           H  
ATOM   1860  HB AVAL A 120       4.903  34.636  16.311  0.25 23.29           H  
ATOM   1861  HB BVAL A 120       5.656  36.285  15.803  0.75 16.14           H  
ATOM   1862 HG11AVAL A 120       5.981  36.526  17.105  0.25 16.76           H  
ATOM   1863 HG11BVAL A 120       3.941  36.572  17.358  0.75 23.14           H  
ATOM   1864 HG12AVAL A 120       6.709  35.982  15.802  0.25 16.76           H  
ATOM   1865 HG12BVAL A 120       3.511  37.160  15.946  0.75 23.14           H  
ATOM   1866 HG13AVAL A 120       5.749  37.245  15.707  0.25 16.76           H  
ATOM   1867 HG13BVAL A 120       2.957  35.748  16.421  0.75 23.14           H  
ATOM   1868 HG21AVAL A 120       3.571  36.212  17.416  0.25 21.24           H  
ATOM   1869 HG21BVAL A 120       5.511  34.688  17.498  0.75 29.53           H  
ATOM   1870 HG22AVAL A 120       3.254  36.915  16.027  0.25 21.24           H  
ATOM   1871 HG22BVAL A 120       4.580  33.792  16.574  0.75 29.53           H  
ATOM   1872 HG23AVAL A 120       2.718  35.448  16.315  0.25 21.24           H  
ATOM   1873 HG23BVAL A 120       6.100  34.032  16.177  0.75 29.53           H  
ATOM   1874  N   ASN A 121       6.623  35.311  13.063  1.00 13.56           N  
ANISOU 1874  N   ASN A 121     1351   2183   1620   -763    406   -691       N  
ATOM   1875  CA  ASN A 121       7.866  34.811  12.493  1.00 12.77           C  
ANISOU 1875  CA  ASN A 121     1207   2180   1467   -710    334   -717       C  
ATOM   1876  C   ASN A 121       8.984  35.699  13.047  1.00 15.74           C  
ANISOU 1876  C   ASN A 121     1511   2667   1803   -755    342   -822       C  
ATOM   1877  O   ASN A 121       9.119  36.849  12.646  1.00 17.95           O  
ANISOU 1877  O   ASN A 121     1781   2908   2130   -777    388   -830       O  
ATOM   1878  CB  ASN A 121       7.836  34.914  10.962  1.00 12.22           C  
ANISOU 1878  CB  ASN A 121     1107   2064   1472   -718    339   -683       C  
ATOM   1879  CG  ASN A 121       9.106  34.382  10.316  1.00 13.48           C  
ANISOU 1879  CG  ASN A 121     1214   2330   1580   -664    278   -721       C  
ATOM   1880  OD1 ASN A 121       9.896  33.684  10.958  1.00 13.00           O  
ANISOU 1880  OD1 ASN A 121     1145   2356   1437   -598    215   -755       O  
ATOM   1881  ND2 ASN A 121       9.326  34.734   9.045  1.00 14.37           N  
ANISOU 1881  ND2 ASN A 121     1307   2420   1732   -670    291   -701       N  
ATOM   1882  H  AASN A 121       6.461  36.132  12.863  0.25 16.28           H  
ATOM   1883  H  BASN A 121       6.513  36.156  12.945  0.75 16.28           H  
ATOM   1884  HA  ASN A 121       8.018  33.890  12.757  1.00 15.33           H  
ATOM   1885  HB2 ASN A 121       7.088  34.397  10.624  1.00 14.66           H  
ATOM   1886  HB3 ASN A 121       7.738  35.845  10.709  1.00 14.66           H  
ATOM   1887 HD21 ASN A 121       8.762  35.238   8.635  1.00 17.24           H  
ATOM   1888 HD22 ASN A 121      10.031  34.457   8.638  1.00 17.24           H  
ATOM   1889  N  AARG A 122       9.765  35.165  13.978  0.60 16.06           N  
ANISOU 1889  N  AARG A 122     1553   2808   1740   -713    282   -860       N  
ATOM   1890  N  BARG A 122       9.780  35.158  13.968  0.40 15.86           N  
ANISOU 1890  N  BARG A 122     1527   2784   1714   -712    281   -860       N  
ATOM   1891  CA AARG A 122      10.895  35.901  14.539  0.60 15.41           C  
ANISOU 1891  CA AARG A 122     1403   2840   1612   -752    275   -957       C  
ATOM   1892  CA BARG A 122      10.892  35.903  14.571  0.40 15.63           C  
ANISOU 1892  CA BARG A 122     1432   2869   1638   -753    275   -957       C  
ATOM   1893  C  AARG A 122      12.191  35.278  14.077  0.60 15.79           C  
ANISOU 1893  C  AARG A 122     1390   2995   1616   -686    194   -984       C  
ATOM   1894  C  BARG A 122      12.242  35.295  14.191  0.40 16.06           C  
ANISOU 1894  C  BARG A 122     1423   3036   1643   -687    191   -989       C  
ATOM   1895  O  AARG A 122      12.375  34.063  14.185  0.60 15.48           O  
ANISOU 1895  O  AARG A 122     1380   2974   1528   -594    115   -946       O  
ATOM   1896  O  BARG A 122      12.514  34.124  14.479  0.40 15.57           O  
ANISOU 1896  O  BARG A 122     1388   3005   1521   -599    109   -959       O  
ATOM   1897  CB AARG A 122      10.835  35.912  16.059  0.60 15.58           C  
ANISOU 1897  CB AARG A 122     1467   2906   1547   -771    268   -988       C  
ATOM   1898  CB BARG A 122      10.752  35.956  16.092  0.40 16.15           C  
ANISOU 1898  CB BARG A 122     1543   2972   1622   -775    274   -988       C  
ATOM   1899  CG AARG A 122       9.728  36.784  16.617  0.60 20.22           C  
ANISOU 1899  CG AARG A 122     2092   3411   2179   -852    366   -999       C  
ATOM   1900  CG BARG A 122       9.431  36.546  16.590  0.40 15.28           C  
ANISOU 1900  CG BARG A 122     1487   2761   1557   -839    366   -974       C  
ATOM   1901  CD AARG A 122       9.795  36.846  18.148  0.60 25.22           C  
ANISOU 1901  CD AARG A 122     2764   4112   2708   -882    364  -1048       C  
ATOM   1902  CD BARG A 122       9.659  37.514  17.771  0.40 22.43           C  
ANISOU 1902  CD BARG A 122     2382   3720   2421   -913    411  -1061       C  
ATOM   1903  NE AARG A 122       9.320  35.605  18.751  0.60 22.59           N  
ANISOU 1903  NE AARG A 122     2513   3776   2294   -825    312   -972       N  
ATOM   1904  NE BARG A 122       8.440  37.793  18.525  0.40 21.99           N  
ANISOU 1904  NE BARG A 122     2386   3593   2375   -965    489  -1065       N  
ATOM   1905  CZ AARG A 122       8.114  35.441  19.297  0.60 24.08           C  
ANISOU 1905  CZ AARG A 122     2774   3894   2482   -847    366   -930       C  
ATOM   1906  CZ BARG A 122       7.451  38.562  18.089  0.40 18.03           C  
ANISOU 1906  CZ BARG A 122     1883   2972   1995  -1001    580  -1052       C  
ATOM   1907  NH1AARG A 122       7.238  36.437  19.324  0.60 16.16           N  
ANISOU 1907  NH1AARG A 122     1765   2812   1561   -918    476   -963       N  
ATOM   1908  NH1BARG A 122       7.518  39.119  16.892  0.40 25.88           N  
ANISOU 1908  NH1BARG A 122     2865   3885   3081   -949    581  -1006       N  
ATOM   1909  NH2AARG A 122       7.787  34.271  19.825  0.60 30.34           N  
ANISOU 1909  NH2AARG A 122     3640   4693   3194   -800    306   -855       N  
ATOM   1910  NH2BARG A 122       6.386  38.761  18.836  0.40 15.94           N  
ANISOU 1910  NH2BARG A 122     1664   2652   1743  -1042    653  -1063       N  
ATOM   1911  H  AARG A 122       9.663  34.376  14.303  0.60 19.27           H  
ATOM   1912  H  BARG A 122       9.699  34.355  14.265  0.40 19.03           H  
ATOM   1913  HA AARG A 122      10.869  36.819  14.226  0.60 18.49           H  
ATOM   1914  HA BARG A 122      10.874  36.814  14.239  0.40 18.76           H  
ATOM   1915  HB2AARG A 122      10.687  35.007  16.373  0.60 18.70           H  
ATOM   1916  HB2BARG A 122      10.821  35.054  16.441  0.40 19.38           H  
ATOM   1917  HB3AARG A 122      11.679  36.246  16.403  0.60 18.70           H  
ATOM   1918  HB3BARG A 122      11.470  36.500  16.451  0.40 19.38           H  
ATOM   1919  HG2AARG A 122       9.823  37.685  16.270  0.60 24.26           H  
ATOM   1920  HG2BARG A 122       9.007  37.038  15.870  0.40 18.33           H  
ATOM   1921  HG3AARG A 122       8.868  36.414  16.363  0.60 24.26           H  
ATOM   1922  HG3BARG A 122       8.852  35.828  16.892  0.40 18.33           H  
ATOM   1923  HD2AARG A 122      10.714  36.987  18.424  0.60 30.27           H  
ATOM   1924  HD2BARG A 122      10.305  37.122  18.380  0.40 26.92           H  
ATOM   1925  HD3AARG A 122       9.234  37.572  18.464  0.60 30.27           H  
ATOM   1926  HD3BARG A 122       9.998  38.356  17.428  0.40 26.92           H  
ATOM   1927  HE AARG A 122       9.855  34.931  18.754  0.60 27.11           H  
ATOM   1928  HE BARG A 122       8.358  37.435  19.303  0.40 26.38           H  
ATOM   1929 HH11AARG A 122       7.444  37.200  18.986  0.60 19.39           H  
ATOM   1930 HH11BARG A 122       8.211  38.992  16.397  0.40 31.05           H  
ATOM   1931 HH12AARG A 122       6.464  36.319  19.679  0.60 19.39           H  
ATOM   1932 HH12BARG A 122       6.874  39.614  16.611  0.40 31.05           H  
ATOM   1933 HH21AARG A 122       8.349  33.620  19.810  0.60 36.40           H  
ATOM   1934 HH21BARG A 122       6.333  38.400  19.614  0.40 19.13           H  
ATOM   1935 HH22AARG A 122       7.009  34.160  20.176  0.60 36.40           H  
ATOM   1936 HH22BARG A 122       5.745  39.257  18.547  0.40 19.13           H  
ATOM   1937  N   ILE A 123      13.096  36.120  13.586  1.00 16.59           N  
ANISOU 1937  N   ILE A 123     1422   3137   1746   -701    224  -1016       N  
ATOM   1938  CA  ILE A 123      14.281  35.656  12.885  1.00 15.70           C  
ANISOU 1938  CA  ILE A 123     1242   3105   1616   -639    175  -1035       C  
ATOM   1939  C   ILE A 123      15.585  36.342  13.314  1.00 16.54           C  
ANISOU 1939  C   ILE A 123     1285   3305   1693   -646    175  -1092       C  
ATOM   1940  O   ILE A 123      15.600  37.531  13.593  1.00 17.07           O  
ANISOU 1940  O   ILE A 123     1357   3354   1776   -709    237  -1111       O  
ATOM   1941  CB  ILE A 123      14.156  35.991  11.370  1.00 16.33           C  
ANISOU 1941  CB  ILE A 123     1319   3126   1759   -646    223  -1002       C  
ATOM   1942  CG1 ILE A 123      12.799  35.585  10.788  1.00 18.76           C  
ANISOU 1942  CG1 ILE A 123     1691   3317   2120   -655    239   -930       C  
ATOM   1943  CG2 ILE A 123      15.228  35.325  10.608  1.00 15.48           C  
ANISOU 1943  CG2 ILE A 123     1149   3103   1632   -583    179  -1029       C  
ATOM   1944  CD1 ILE A 123      12.267  36.598   9.896  1.00 14.33           C  
ANISOU 1944  CD1 ILE A 123     1180   2643   1623   -691    299   -876       C  
ATOM   1945  H  AILE A 123      13.042  36.976  13.648  0.60 19.91           H  
ATOM   1946  H  BILE A 123      13.003  36.975  13.570  0.40 19.91           H  
ATOM   1947  HA  ILE A 123      14.377  34.696  12.991  1.00 18.83           H  
ATOM   1948  HB  ILE A 123      14.258  36.949  11.262  1.00 19.59           H  
ATOM   1949 HG12 ILE A 123      12.901  34.762  10.285  1.00 22.51           H  
ATOM   1950 HG13 ILE A 123      12.167  35.458  11.513  1.00 22.51           H  
ATOM   1951 HG21 ILE A 123      15.131  35.547   9.668  1.00 18.58           H  
ATOM   1952 HG22 ILE A 123      16.087  35.635  10.935  1.00 18.58           H  
ATOM   1953 HG23 ILE A 123      15.153  34.366  10.731  1.00 18.58           H  
ATOM   1954 HD11 ILE A 123      11.410  36.298   9.554  1.00 17.20           H  
ATOM   1955 HD12 ILE A 123      12.155  37.426  10.389  1.00 17.20           H  
ATOM   1956 HD13 ILE A 123      12.888  36.730   9.163  1.00 17.20           H  
ATOM   1957  N  AGLU A 124      16.659  35.559  13.388  0.46 17.15           N  
ANISOU 1957  N  AGLU A 124     1310   3477   1731   -574    100  -1118       N  
ATOM   1958  N  BGLU A 124      16.671  35.574  13.341  0.54 17.14           N  
ANISOU 1958  N  BGLU A 124     1307   3475   1732   -574    102  -1118       N  
ATOM   1959  CA AGLU A 124      18.022  36.067  13.474  0.46 17.97           C  
ANISOU 1959  CA AGLU A 124     1340   3670   1818   -571     96  -1170       C  
ATOM   1960  CA BGLU A 124      18.022  36.102  13.478  0.54 17.97           C  
ANISOU 1960  CA BGLU A 124     1340   3670   1818   -573     98  -1170       C  
ATOM   1961  C  AGLU A 124      18.724  35.746  12.155  0.46 19.33           C  
ANISOU 1961  C  AGLU A 124     1460   3873   2013   -527     99  -1183       C  
ATOM   1962  C  BGLU A 124      18.852  35.715  12.250  0.54 19.76           C  
ANISOU 1962  C  BGLU A 124     1508   3939   2062   -522     92  -1188       C  
ATOM   1963  O  AGLU A 124      18.578  34.647  11.633  0.46 19.29           O  
ANISOU 1963  O  AGLU A 124     1452   3866   2013   -457     53  -1169       O  
ATOM   1964  O  BGLU A 124      18.926  34.543  11.888  0.54 18.09           O  
ANISOU 1964  O  BGLU A 124     1283   3742   1849   -442     32  -1182       O  
ATOM   1965  CB AGLU A 124      18.767  35.423  14.658  0.46 18.88           C  
ANISOU 1965  CB AGLU A 124     1437   3864   1872   -521      4  -1190       C  
ATOM   1966  CB BGLU A 124      18.666  35.582  14.768  0.54 18.86           C  
ANISOU 1966  CB BGLU A 124     1441   3855   1869   -535     13  -1190       C  
ATOM   1967  CG AGLU A 124      20.283  35.510  14.574  0.46 20.82           C  
ANISOU 1967  CG AGLU A 124     1594   4208   2107   -489    -26  -1241       C  
ATOM   1968  CG BGLU A 124      17.855  35.958  16.011  0.54 23.91           C  
ANISOU 1968  CG BGLU A 124     2152   4460   2474   -594     25  -1177       C  
ATOM   1969  CD AGLU A 124      20.964  35.686  15.937  0.46 26.52           C  
ANISOU 1969  CD AGLU A 124     2306   4992   2777   -500    -81  -1264       C  
ATOM   1970  CD BGLU A 124      18.458  35.443  17.307  0.54 31.52           C  
ANISOU 1970  CD BGLU A 124     3126   5490   3360   -565    -65  -1185       C  
ATOM   1971  OE1AGLU A 124      20.778  34.830  16.835  0.46 21.51           O  
ANISOU 1971  OE1AGLU A 124     1716   4361   2096   -459   -165  -1238       O  
ATOM   1972  OE1BGLU A 124      18.940  34.283  17.306  0.54 28.93           O  
ANISOU 1972  OE1BGLU A 124     2789   5195   3007   -475   -162  -1168       O  
ATOM   1973  OE2AGLU A 124      21.703  36.685  16.101  0.46 28.48           O  
ANISOU 1973  OE2AGLU A 124     2512   5284   3026   -553    -43  -1304       O  
ATOM   1974  OE2BGLU A 124      18.449  36.206  18.315  0.54 25.93           O  
ANISOU 1974  OE2BGLU A 124     2438   4796   2618   -631    -42  -1206       O  
ATOM   1975  H  AGLU A 124      16.618  34.700  13.388  0.46 20.59           H  
ATOM   1976  H  BGLU A 124      16.647  34.716  13.281  0.54 20.57           H  
ATOM   1977  HA AGLU A 124      18.009  37.029  13.597  0.46 21.56           H  
ATOM   1978  HA BGLU A 124      17.984  37.070  13.526  0.54 21.56           H  
ATOM   1979  HB2AGLU A 124      18.492  35.867  15.475  0.46 22.66           H  
ATOM   1980  HB2BGLU A 124      18.724  34.615  14.727  0.54 22.63           H  
ATOM   1981  HB3AGLU A 124      18.529  34.484  14.700  0.46 22.66           H  
ATOM   1982  HB3BGLU A 124      19.553  35.966  14.858  0.54 22.63           H  
ATOM   1983  HG2AGLU A 124      20.622  34.694  14.176  0.46 24.98           H  
ATOM   1984  HG2BGLU A 124      17.803  36.925  16.071  0.54 28.70           H  
ATOM   1985  HG3AGLU A 124      20.523  36.271  14.022  0.46 24.98           H  
ATOM   1986  HG3BGLU A 124      16.964  35.585  15.929  0.54 28.70           H  
ATOM   1987  N   LEU A 125      19.469  36.714  11.623  1.00 18.28           N  
ANISOU 1987  N   LEU A 125     1295   3765   1885   -569    150  -1211       N  
ATOM   1988  CA  LEU A 125      20.265  36.517  10.414  1.00 18.50           C  
ANISOU 1988  CA  LEU A 125     1279   3833   1916   -541    156  -1234       C  
ATOM   1989  C   LEU A 125      21.690  37.024  10.565  1.00 19.50           C  
ANISOU 1989  C   LEU A 125     1336   4055   2018   -547    151  -1293       C  
ATOM   1990  O   LEU A 125      21.946  38.120  11.106  1.00 20.91           O  
ANISOU 1990  O   LEU A 125     1520   4236   2190   -611    179  -1304       O  
ATOM   1991  CB  LEU A 125      19.569  37.205   9.243  1.00 19.19           C  
ANISOU 1991  CB  LEU A 125     1429   3827   2035   -600    217  -1188       C  
ATOM   1992  CG  LEU A 125      20.262  37.187   7.880  1.00 18.02           C  
ANISOU 1992  CG  LEU A 125     1256   3710   1881   -598    231  -1203       C  
ATOM   1993  CD1 LEU A 125      19.214  37.377   6.792  1.00 17.19           C  
ANISOU 1993  CD1 LEU A 125     1225   3495   1810   -635    262  -1132       C  
ATOM   1994  CD2 LEU A 125      21.374  38.257   7.759  1.00 18.78           C  
ANISOU 1994  CD2 LEU A 125     1317   3860   1959   -648    253  -1239       C  
ATOM   1995  H  ALEU A 125      19.530  37.506  11.951  0.46 21.93           H  
ATOM   1996  H  BLEU A 125      19.441  37.532  11.886  0.54 21.93           H  
ATOM   1997  HA  LEU A 125      20.307  35.568  10.218  1.00 22.20           H  
ATOM   1998  HB2 LEU A 125      18.702  36.786   9.124  1.00 23.03           H  
ATOM   1999  HB3 LEU A 125      19.439  38.137   9.481  1.00 23.03           H  
ATOM   2000  HG  LEU A 125      20.672  36.318   7.749  1.00 21.63           H  
ATOM   2001 HD11 LEU A 125      19.653  37.365   5.927  1.00 20.62           H  
ATOM   2002 HD12 LEU A 125      18.569  36.654   6.846  1.00 20.62           H  
ATOM   2003 HD13 LEU A 125      18.770  38.228   6.927  1.00 20.62           H  
ATOM   2004 HD21 LEU A 125      21.775  38.197   6.878  1.00 22.54           H  
ATOM   2005 HD22 LEU A 125      20.982  39.135   7.885  1.00 22.54           H  
ATOM   2006 HD23 LEU A 125      22.045  38.093   8.440  1.00 22.54           H  
ATOM   2007  N   LYS A 126      22.622  36.200  10.100  1.00 20.33           N  
ANISOU 2007  N   LYS A 126     1373   4238   2113   -477    113  -1335       N  
ATOM   2008  CA  LYS A 126      24.027  36.541  10.104  1.00 21.48           C  
ANISOU 2008  CA  LYS A 126     1444   4478   2241   -476    105  -1394       C  
ATOM   2009  C   LYS A 126      24.577  36.320   8.707  1.00 22.94           C  
ANISOU 2009  C   LYS A 126     1599   4693   2425   -465    129  -1422       C  
ATOM   2010  O   LYS A 126      24.516  35.188   8.183  1.00 22.51           O  
ANISOU 2010  O   LYS A 126     1525   4648   2379   -389     99  -1437       O  
ATOM   2011  CB  LYS A 126      24.801  35.649  11.050  1.00 23.54           C  
ANISOU 2011  CB  LYS A 126     1640   4813   2490   -393     18  -1429       C  
ATOM   2012  CG  LYS A 126      26.295  35.931  10.991  1.00 31.80           C  
ANISOU 2012  CG  LYS A 126     2599   5956   3526   -388      7  -1492       C  
ATOM   2013  CD  LYS A 126      26.845  36.207  12.348  1.00 40.59           C  
ANISOU 2013  CD  LYS A 126     3687   7113   4622   -396    -45  -1502       C  
ATOM   2014  CE  LYS A 126      28.339  36.483  12.274  1.00 42.22           C  
ANISOU 2014  CE  LYS A 126     3801   7415   4824   -393    -59  -1562       C  
ATOM   2015  NZ  LYS A 126      28.958  36.170  13.571  1.00 41.88           N  
ANISOU 2015  NZ  LYS A 126     3722   7419   4771   -360   -150  -1571       N  
ATOM   2016  H   LYS A 126      22.456  35.423   9.771  1.00 24.40           H  
ATOM   2017  HA  LYS A 126      24.152  37.468  10.358  1.00 25.78           H  
ATOM   2018  HB2 LYS A 126      24.498  35.807  11.958  1.00 28.24           H  
ATOM   2019  HB3 LYS A 126      24.657  34.721  10.805  1.00 28.24           H  
ATOM   2020  HG2 LYS A 126      26.753  35.157  10.627  1.00 38.16           H  
ATOM   2021  HG3 LYS A 126      26.452  36.709  10.433  1.00 38.16           H  
ATOM   2022  HD2 LYS A 126      26.407  36.988  12.722  1.00 48.71           H  
ATOM   2023  HD3 LYS A 126      26.703  35.435  12.918  1.00 48.71           H  
ATOM   2024  HE2 LYS A 126      28.742  35.921  11.594  1.00 50.66           H  
ATOM   2025  HE3 LYS A 126      28.490  37.421  12.077  1.00 50.66           H  
ATOM   2026  HZ1 LYS A 126      29.833  36.328  13.537  1.00 50.26           H  
ATOM   2027  HZ2 LYS A 126      28.597  36.674  14.210  1.00 50.26           H  
ATOM   2028  HZ3 LYS A 126      28.827  35.313  13.772  1.00 50.26           H  
ATOM   2029  N   GLY A 127      25.123  37.393   8.131  1.00 21.67           N  
ANISOU 2029  N   GLY A 127     1435   4545   2253   -541    176  -1432       N  
ATOM   2030  CA  GLY A 127      25.738  37.338   6.821  1.00 22.06           C  
ANISOU 2030  CA  GLY A 127     1455   4634   2291   -551    199  -1461       C  
ATOM   2031  C   GLY A 127      27.231  37.535   6.945  1.00 23.75           C  
ANISOU 2031  C   GLY A 127     1577   4959   2487   -546    186  -1530       C  
ATOM   2032  O   GLY A 127      27.682  38.399   7.710  1.00 23.72           O  
ANISOU 2032  O   GLY A 127     1560   4975   2479   -589    188  -1534       O  
ATOM   2033  H   GLY A 127      25.145  38.173   8.491  1.00 26.00           H  
ATOM   2034  HA2 GLY A 127      25.567  36.476   6.410  1.00 26.47           H  
ATOM   2035  HA3 GLY A 127      25.374  38.035   6.254  1.00 26.47           H  
ATOM   2036  N   ILE A 128      27.999  36.746   6.195  1.00 24.50           N  
ANISOU 2036  N   ILE A 128     1607   5127   2576   -494    173  -1589       N  
ATOM   2037  CA  ILE A 128      29.466  36.827   6.254  1.00 25.85           C  
ANISOU 2037  CA  ILE A 128     1678   5406   2737   -483    158  -1661       C  
ATOM   2038  C   ILE A 128      30.066  36.621   4.872  1.00 31.52           C  
ANISOU 2038  C   ILE A 128     2357   6180   3439   -496    188  -1708       C  
ATOM   2039  O   ILE A 128      29.415  36.058   3.965  1.00 28.83           O  
ANISOU 2039  O   ILE A 128     2054   5804   3097   -485    201  -1698       O  
ATOM   2040  CB  ILE A 128      30.089  35.764   7.211  1.00 30.30           C  
ANISOU 2040  CB  ILE A 128     2166   6025   3323   -370     81  -1709       C  
ATOM   2041  CG1 ILE A 128      29.925  34.340   6.645  1.00 36.14           C  
ANISOU 2041  CG1 ILE A 128     2885   6763   4082   -266     46  -1742       C  
ATOM   2042  CG2 ILE A 128      29.456  35.850   8.613  1.00 36.84           C  
ANISOU 2042  CG2 ILE A 128     3034   6805   4159   -359     41  -1660       C  
ATOM   2043  CD1 ILE A 128      30.636  33.266   7.450  1.00 39.30           C  
ANISOU 2043  CD1 ILE A 128     3209   7207   4518   -146    -43  -1786       C  
ATOM   2044  H   ILE A 128      27.701  36.156   5.645  1.00 29.40           H  
ATOM   2045  HA  ILE A 128      29.724  37.707   6.569  1.00 31.02           H  
ATOM   2046  HB  ILE A 128      31.037  35.950   7.294  1.00 36.37           H  
ATOM   2047 HG12 ILE A 128      28.980  34.119   6.628  1.00 43.36           H  
ATOM   2048 HG13 ILE A 128      30.283  34.320   5.744  1.00 43.36           H  
ATOM   2049 HG21 ILE A 128      29.863  35.179   9.184  1.00 44.21           H  
ATOM   2050 HG22 ILE A 128      29.615  36.735   8.977  1.00 44.21           H  
ATOM   2051 HG23 ILE A 128      28.503  35.688   8.540  1.00 44.21           H  
ATOM   2052 HD11 ILE A 128      30.483  32.405   7.030  1.00 47.16           H  
ATOM   2053 HD12 ILE A 128      31.585  33.462   7.468  1.00 47.16           H  
ATOM   2054 HD13 ILE A 128      30.281  33.261   8.353  1.00 47.16           H  
ATOM   2055  N   ASP A 129      31.310  37.087   4.744  1.00 35.42           N  
ANISOU 2055  N   ASP A 129     3306   6318   3834  -2309    374  -1305       N  
ATOM   2056  CA  ASP A 129      32.134  36.916   3.539  1.00 36.40           C  
ANISOU 2056  CA  ASP A 129     3353   6555   3921  -2351    420  -1363       C  
ATOM   2057  C   ASP A 129      31.548  37.519   2.265  1.00 36.19           C  
ANISOU 2057  C   ASP A 129     3394   6516   3841  -2398    481  -1322       C  
ATOM   2058  O   ASP A 129      31.819  37.042   1.165  1.00 36.47           O  
ANISOU 2058  O   ASP A 129     3370   6632   3853  -2385    504  -1355       O  
ATOM   2059  CB  ASP A 129      32.480  35.438   3.346  1.00 36.24           C  
ANISOU 2059  CB  ASP A 129     3218   6614   3939  -2235    372  -1415       C  
ATOM   2060  CG  ASP A 129      33.578  34.983   4.283  1.00 37.18           C  
ANISOU 2060  CG  ASP A 129     3246   6786   4094  -2230    332  -1484       C  
ATOM   2061  OD1 ASP A 129      34.571  35.714   4.453  1.00 42.95           O  
ANISOU 2061  OD1 ASP A 129     3954   7563   4804  -2340    366  -1527       O  
ATOM   2062  OD2 ASP A 129      33.452  33.891   4.859  1.00 37.69           O  
ANISOU 2062  OD2 ASP A 129     3263   6844   4212  -2117    263  -1493       O  
ATOM   2063  H   ASP A 129      31.715  37.524   5.365  1.00 42.50           H  
ATOM   2064  HA  ASP A 129      32.973  37.375   3.695  1.00 43.68           H  
ATOM   2065  HB2 ASP A 129      31.691  34.901   3.522  1.00 43.49           H  
ATOM   2066  HB3 ASP A 129      32.783  35.298   2.435  1.00 43.49           H  
ATOM   2067  N   PHE A 130      30.806  38.606   2.417  1.00 35.84           N  
ANISOU 2067  N   PHE A 130     3472   6370   3774  -2456    508  -1256       N  
ATOM   2068  CA  PHE A 130      30.329  39.368   1.281  1.00 35.98           C  
ANISOU 2068  CA  PHE A 130     3566   6376   3728  -2529    574  -1224       C  
ATOM   2069  C   PHE A 130      31.372  40.338   0.738  1.00 37.78           C  
ANISOU 2069  C   PHE A 130     3786   6677   3894  -2685    644  -1268       C  
ATOM   2070  O   PHE A 130      32.174  40.912   1.472  1.00 38.75           O  
ANISOU 2070  O   PHE A 130     3896   6804   4023  -2758    647  -1294       O  
ATOM   2071  CB  PHE A 130      29.048  40.117   1.625  1.00 35.04           C  
ANISOU 2071  CB  PHE A 130     3589   6127   3596  -2535    579  -1143       C  
ATOM   2072  CG  PHE A 130      27.855  39.218   1.728  1.00 33.29           C  
ANISOU 2072  CG  PHE A 130     3385   5845   3419  -2394    526  -1092       C  
ATOM   2073  CD1 PHE A 130      27.108  38.898   0.592  1.00 32.67           C  
ANISOU 2073  CD1 PHE A 130     3327   5772   3313  -2359    545  -1065       C  
ATOM   2074  CD2 PHE A 130      27.497  38.662   2.941  1.00 32.32           C  
ANISOU 2074  CD2 PHE A 130     3254   5659   3366  -2295    454  -1069       C  
ATOM   2075  CE1 PHE A 130      26.013  38.060   0.673  1.00 31.09           C  
ANISOU 2075  CE1 PHE A 130     3141   5515   3157  -2230    494  -1017       C  
ATOM   2076  CE2 PHE A 130      26.403  37.825   3.034  1.00 30.78           C  
ANISOU 2076  CE2 PHE A 130     3074   5409   3212  -2168    403  -1020       C  
ATOM   2077  CZ  PHE A 130      25.664  37.512   1.890  1.00 30.14           C  
ANISOU 2077  CZ  PHE A 130     3011   5332   3108  -2133    423   -992       C  
ATOM   2078  H   PHE A 130      30.564  38.925   3.178  1.00 43.00           H  
ATOM   2079  HA  PHE A 130      30.116  38.746   0.567  1.00 43.17           H  
ATOM   2080  HB2 PHE A 130      29.163  40.561   2.480  1.00 42.05           H  
ATOM   2081  HB3 PHE A 130      28.870  40.772   0.932  1.00 42.05           H  
ATOM   2082  HD1 PHE A 130      27.346  39.262  -0.230  1.00 39.20           H  
ATOM   2083  HD2 PHE A 130      27.989  38.864   3.704  1.00 38.78           H  
ATOM   2084  HE1 PHE A 130      25.521  37.857  -0.090  1.00 37.31           H  
ATOM   2085  HE2 PHE A 130      26.166  37.457   3.855  1.00 36.94           H  
ATOM   2086  HZ  PHE A 130      24.925  36.951   1.952  1.00 36.17           H  
ATOM   2087  N   LYS A 131      31.330  40.515  -0.571  1.00 38.25           N  
ANISOU 2087  N   LYS A 131     3851   6789   3892  -2736    698  -1274       N  
ATOM   2088  CA  LYS A 131      32.244  41.405  -1.255  1.00 39.97           C  
ANISOU 2088  CA  LYS A 131     4064   7077   4047  -2884    766  -1309       C  
ATOM   2089  C   LYS A 131      31.687  42.820  -1.204  1.00 40.26           C  
ANISOU 2089  C   LYS A 131     4247   7010   4041  -2990    808  -1247       C  
ATOM   2090  O   LYS A 131      30.502  43.042  -1.467  1.00 39.25           O  
ANISOU 2090  O   LYS A 131     4222   6791   3902  -2958    809  -1181       O  
ATOM   2091  CB  LYS A 131      32.459  40.918  -2.697  1.00 40.39           C  
ANISOU 2091  CB  LYS A 131     4057   7236   4056  -2888    800  -1342       C  
ATOM   2092  CG  LYS A 131      32.831  39.437  -2.739  1.00 39.91           C  
ANISOU 2092  CG  LYS A 131     3863   7260   4043  -2759    750  -1397       C  
ATOM   2093  CD  LYS A 131      33.330  38.960  -4.087  1.00 40.67           C  
ANISOU 2093  CD  LYS A 131     3877   7482   4092  -2773    784  -1451       C  
ATOM   2094  CE  LYS A 131      33.635  37.468  -4.031  1.00 40.12           C  
ANISOU 2094  CE  LYS A 131     3685   7479   4078  -2630    726  -1503       C  
ATOM   2095  H   LYS A 131      30.770  40.124  -1.094  1.00 45.90           H  
ATOM   2096  HA  LYS A 131      33.101  41.397  -0.800  1.00 47.97           H  
ATOM   2097  HB2 LYS A 131      31.639  41.040  -3.201  1.00 48.47           H  
ATOM   2098  HB3 LYS A 131      33.180  41.424  -3.102  1.00 48.47           H  
ATOM   2099  HG2 LYS A 131      33.534  39.274  -2.090  1.00 47.90           H  
ATOM   2100  HG3 LYS A 131      32.048  38.912  -2.511  1.00 47.90           H  
ATOM   2101  HD2 LYS A 131      32.646  39.110  -4.759  1.00 48.80           H  
ATOM   2102  HD3 LYS A 131      34.144  39.433  -4.319  1.00 48.80           H  
ATOM   2103  N   GLU A 132      32.553  43.765  -0.843  1.00 41.80           N  
ANISOU 2103  N   GLU A 132     4450   7215   4217  -3111    838  -1268       N  
ATOM   2104  CA  GLU A 132      32.162  45.156  -0.636  1.00 43.35           C  
ANISOU 2104  CA  GLU A 132     4784   7308   4381  -3212    870  -1214       C  
ATOM   2105  C   GLU A 132      31.607  45.771  -1.924  1.00 43.47           C  
ANISOU 2105  C   GLU A 132     4884   7300   4333  -3273    924  -1171       C  
ATOM   2106  O   GLU A 132      30.773  46.679  -1.888  1.00 49.16           O  
ANISOU 2106  O   GLU A 132     5740   7902   5036  -3304    937  -1105       O  
ATOM   2107  CB  GLU A 132      33.367  45.965  -0.129  1.00 43.90           C  
ANISOU 2107  CB  GLU A 132     4825   7411   4442  -3335    892  -1253       C  
ATOM   2108  H   GLU A 132      33.390  43.621  -0.709  1.00 50.16           H  
ATOM   2109  HA  GLU A 132      31.467  45.193   0.040  1.00 52.03           H  
ATOM   2110  N   ASP A 133      32.081  45.267  -3.056  1.00 45.27           N  
ANISOU 2110  N   ASP A 133     5031   7640   4530  -3285    951  -1208       N  
ATOM   2111  CA  ASP A 133      31.644  45.738  -4.364  1.00 50.48           C  
ANISOU 2111  CA  ASP A 133     5756   8292   5134  -3338    998  -1171       C  
ATOM   2112  C   ASP A 133      30.706  44.730  -5.038  1.00 47.59           C  
ANISOU 2112  C   ASP A 133     5379   7926   4778  -3216    975  -1152       C  
ATOM   2113  O   ASP A 133      30.357  44.876  -6.210  1.00 51.91           O  
ANISOU 2113  O   ASP A 133     5959   8481   5284  -3240   1007  -1127       O  
ATOM   2114  CB  ASP A 133      32.868  45.999  -5.254  1.00 56.21           C  
ANISOU 2114  CB  ASP A 133     6401   9146   5809  -3455   1051  -1225       C  
ATOM   2115  CG  ASP A 133      33.766  44.765  -5.408  1.00 60.34           C  
ANISOU 2115  CG  ASP A 133     6756   9821   6349  -3397   1034  -1312       C  
ATOM   2116  OD1 ASP A 133      34.055  44.091  -4.394  1.00 61.41           O  
ANISOU 2116  OD1 ASP A 133     6823   9969   6541  -3321    985  -1348       O  
ATOM   2117  OD2 ASP A 133      34.181  44.465  -6.549  1.00 70.01           O  
ANISOU 2117  OD2 ASP A 133     7917  11151   7534  -3425   1066  -1345       O  
ATOM   2118  H   ASP A 133      32.668  44.639  -3.093  1.00 54.33           H  
ATOM   2119  HA  ASP A 133      31.164  46.574  -4.258  1.00 60.58           H  
ATOM   2120  HB2 ASP A 133      32.566  46.261  -6.138  1.00 67.45           H  
ATOM   2121  HB3 ASP A 133      33.399  46.709  -4.861  1.00 67.45           H  
ATOM   2122  N   GLY A 134      30.297  43.701  -4.302  1.00 40.44           N  
ANISOU 2122  N   GLY A 134     4426   7010   3929  -3083    916  -1160       N  
ATOM   2123  CA  GLY A 134      29.426  42.678  -4.858  1.00 39.06           C  
ANISOU 2123  CA  GLY A 134     4234   6836   3772  -2961    886  -1142       C  
ATOM   2124  C   GLY A 134      28.023  43.198  -5.133  1.00 38.04           C  
ANISOU 2124  C   GLY A 134     4249   6569   3635  -2939    889  -1053       C  
ATOM   2125  O   GLY A 134      27.727  44.361  -4.876  1.00 38.41           O  
ANISOU 2125  O   GLY A 134     4413   6518   3664  -3014    913  -1006       O  
ATOM   2126  H   GLY A 134      30.510  43.575  -3.479  1.00 48.53           H  
ATOM   2127  HA2 GLY A 134      29.801  42.352  -5.691  1.00 46.87           H  
ATOM   2128  HA3 GLY A 134      29.363  41.935  -4.238  1.00 46.87           H  
ATOM   2129  N   ASN A 135      27.152  42.341  -5.660  1.00 36.78           N  
ANISOU 2129  N   ASN A 135     4083   6399   3492  -2832    862  -1029       N  
ATOM   2130  CA  ASN A 135      25.799  42.757  -5.960  1.00 35.78           C  
ANISOU 2130  CA  ASN A 135     4088   6142   3364  -2801    861   -944       C  
ATOM   2131  C   ASN A 135      24.954  43.000  -4.699  1.00 34.66           C  
ANISOU 2131  C   ASN A 135     4032   5871   3266  -2744    822   -894       C  
ATOM   2132  O   ASN A 135      23.941  43.684  -4.770  1.00 34.14           O  
ANISOU 2132  O   ASN A 135     4094   5680   3196  -2741    828   -824       O  
ATOM   2133  CB  ASN A 135      25.109  41.711  -6.829  1.00 34.72           C  
ANISOU 2133  CB  ASN A 135     3916   6034   3243  -2698    839   -932       C  
ATOM   2134  CG  ASN A 135      25.691  41.641  -8.239  1.00 35.79           C  
ANISOU 2134  CG  ASN A 135     3997   6275   3328  -2757    883   -965       C  
ATOM   2135  OD1 ASN A 135      26.253  42.614  -8.746  1.00 37.19           O  
ANISOU 2135  OD1 ASN A 135     4209   6465   3456  -2881    936   -967       O  
ATOM   2136  ND2 ASN A 135      25.540  40.489  -8.879  1.00 35.16           N  
ANISOU 2136  ND2 ASN A 135     3831   6269   3260  -2667    858   -990       N  
ATOM   2137  H   ASN A 135      27.325  41.521  -5.851  1.00 44.13           H  
ATOM   2138  HA  ASN A 135      25.831  43.587  -6.461  1.00 42.93           H  
ATOM   2139  HB2 ASN A 135      25.212  40.839  -6.418  1.00 41.66           H  
ATOM   2140  HB3 ASN A 135      24.167  41.934  -6.904  1.00 41.66           H  
ATOM   2141 HD21 ASN A 135      25.133  39.834  -8.497  1.00 42.19           H  
ATOM   2142 HD22 ASN A 135      25.850  40.396  -9.676  1.00 42.19           H  
ATOM   2143  N   ILE A 136      25.355  42.438  -3.559  1.00 34.32           N  
ANISOU 2143  N   ILE A 136     3918   5856   3268  -2693    780   -929       N  
ATOM   2144  CA  ILE A 136      24.559  42.601  -2.331  1.00 33.28           C  
ANISOU 2144  CA  ILE A 136     3858   5608   3177  -2635    740   -883       C  
ATOM   2145  C   ILE A 136      24.970  43.891  -1.621  1.00 34.31           C  
ANISOU 2145  C   ILE A 136     4065   5684   3286  -2745    768   -879       C  
ATOM   2146  O   ILE A 136      24.206  44.844  -1.590  1.00 34.20           O  
ANISOU 2146  O   ILE A 136     4184   5555   3255  -2775    784   -822       O  
ATOM   2147  CB  ILE A 136      24.653  41.384  -1.390  1.00 32.32           C  
ANISOU 2147  CB  ILE A 136     3635   5524   3123  -2517    674   -909       C  
ATOM   2148  CG1 ILE A 136      23.895  40.177  -1.965  1.00 31.01           C  
ANISOU 2148  CG1 ILE A 136     3423   5373   2987  -2391    636   -890       C  
ATOM   2149  CG2 ILE A 136      23.979  41.683  -0.040  1.00 31.51           C  
ANISOU 2149  CG2 ILE A 136     3604   5309   3058  -2477    636   -866       C  
ATOM   2150  CD1 ILE A 136      24.512  39.553  -3.197  1.00 31.59           C  
ANISOU 2150  CD1 ILE A 136     3402   5567   3035  -2396    657   -940       C  
ATOM   2151  H   ILE A 136      26.069  41.967  -3.466  1.00 41.19           H  
ATOM   2152  HA  ILE A 136      23.627  42.695  -2.584  1.00 39.93           H  
ATOM   2153  HB  ILE A 136      25.584  41.150  -1.247  1.00 38.79           H  
ATOM   2154 HG12 ILE A 136      23.847  39.490  -1.283  1.00 37.21           H  
ATOM   2155 HG13 ILE A 136      22.998  40.462  -2.201  1.00 37.21           H  
ATOM   2156 HG21 ILE A 136      24.054  40.901   0.530  1.00 37.81           H  
ATOM   2157 HG22 ILE A 136      24.424  42.439   0.374  1.00 37.81           H  
ATOM   2158 HG23 ILE A 136      23.045  41.892  -0.194  1.00 37.81           H  
ATOM   2159 HD11 ILE A 136      23.963  38.805  -3.480  1.00 37.91           H  
ATOM   2160 HD12 ILE A 136      24.554  40.219  -3.901  1.00 37.91           H  
ATOM   2161 HD13 ILE A 136      25.406  39.244  -2.979  1.00 37.91           H  
ATOM   2162  N   LEU A 137      26.188  43.942  -1.096  1.00 40.34           N  
ANISOU 2162  N   LEU A 137     4747   6527   4054  -2803    771   -940       N  
ATOM   2163  CA  LEU A 137      26.645  45.146  -0.385  1.00 41.29           C  
ANISOU 2163  CA  LEU A 137     4933   6599   4158  -2908    794   -939       C  
ATOM   2164  C   LEU A 137      26.717  46.343  -1.330  1.00 38.62           C  
ANISOU 2164  C   LEU A 137     4684   6232   3758  -3030    856   -915       C  
ATOM   2165  O   LEU A 137      26.571  47.482  -0.893  1.00 38.11           O  
ANISOU 2165  O   LEU A 137     4724   6079   3679  -3098    872   -884       O  
ATOM   2166  CB  LEU A 137      27.998  44.919   0.306  1.00 39.07           C  
ANISOU 2166  CB  LEU A 137     4536   6413   3897  -2946    783  -1011       C  
ATOM   2167  CG  LEU A 137      28.030  43.936   1.490  1.00 36.46           C  
ANISOU 2167  CG  LEU A 137     4128   6089   3637  -2835    714  -1031       C  
ATOM   2168  CD1 LEU A 137      29.452  43.843   2.061  1.00 44.77           C  
ANISOU 2168  CD1 LEU A 137     5073   7230   4708  -2884    707  -1102       C  
ATOM   2169  CD2 LEU A 137      27.020  44.313   2.588  1.00 36.41           C  
ANISOU 2169  CD2 LEU A 137     4226   5952   3657  -2788    681   -974       C  
ATOM   2170  H   LEU A 137      26.767  43.307  -1.134  1.00 48.41           H  
ATOM   2171  HA  LEU A 137      25.997  45.358   0.306  1.00 49.55           H  
ATOM   2172  HB2 LEU A 137      28.622  44.585  -0.358  1.00 46.89           H  
ATOM   2173  HB3 LEU A 137      28.314  45.774   0.637  1.00 46.89           H  
ATOM   2174  HG  LEU A 137      27.789  43.054   1.164  1.00 43.76           H  
ATOM   2175 HD11 LEU A 137      29.454  43.221   2.805  1.00 53.72           H  
ATOM   2176 HD12 LEU A 137      30.051  43.530   1.365  1.00 53.72           H  
ATOM   2177 HD13 LEU A 137      29.728  44.722   2.364  1.00 53.72           H  
ATOM   2178 HD21 LEU A 137      27.079  43.665   3.307  1.00 43.69           H  
ATOM   2179 HD22 LEU A 137      27.232  45.199   2.921  1.00 43.69           H  
ATOM   2180 HD23 LEU A 137      26.126  44.307   2.210  1.00 43.69           H  
ATOM   2181  N   GLY A 138      26.909  46.077  -2.625  1.00 37.99           N  
ANISOU 2181  N   GLY A 138     4567   6224   3646  -3051    887   -926       N  
ATOM   2182  CA  GLY A 138      26.932  47.126  -3.631  1.00 39.08           C  
ANISOU 2182  CA  GLY A 138     4785   6334   3728  -3157    942   -897       C  
ATOM   2183  C   GLY A 138      25.569  47.557  -4.147  1.00 38.20           C  
ANISOU 2183  C   GLY A 138     4808   6093   3611  -3115    944   -815       C  
ATOM   2184  O   GLY A 138      25.486  48.436  -5.008  1.00 39.04           O  
ANISOU 2184  O   GLY A 138     4991   6162   3679  -3192    986   -782       O  
ATOM   2185  H   GLY A 138      27.029  45.287  -2.943  1.00 45.59           H  
ATOM   2186  HA2 GLY A 138      27.370  47.907  -3.259  1.00 46.89           H  
ATOM   2187  HA3 GLY A 138      27.455  46.822  -4.389  1.00 46.89           H  
ATOM   2188  N   HIS A 139      24.509  46.933  -3.635  1.00 36.55           N  
ANISOU 2188  N   HIS A 139     4627   5815   3444  -2991    898   -782       N  
ATOM   2189  CA  HIS A 139      23.127  47.279  -4.001  1.00 35.57           C  
ANISOU 2189  CA  HIS A 139     4630   5558   3326  -2932    893   -704       C  
ATOM   2190  C   HIS A 139      22.901  47.342  -5.520  1.00 35.89           C  
ANISOU 2190  C   HIS A 139     4689   5611   3336  -2951    926   -678       C  
ATOM   2191  O   HIS A 139      22.472  48.362  -6.057  1.00 36.39           O  
ANISOU 2191  O   HIS A 139     4864   5585   3377  -2998    955   -627       O  
ATOM   2192  CB  HIS A 139      22.728  48.610  -3.371  1.00 35.95           C  
ANISOU 2192  CB  HIS A 139     4816   5478   3367  -2982    902   -660       C  
ATOM   2193  CG  HIS A 139      22.678  48.578  -1.877  1.00 35.45           C  
ANISOU 2193  CG  HIS A 139     4755   5378   3336  -2948    865   -672       C  
ATOM   2194  ND1 HIS A 139      21.569  48.151  -1.180  1.00 33.92           N  
ANISOU 2194  ND1 HIS A 139     4604   5102   3182  -2832    821   -634       N  
ATOM   2195  CD2 HIS A 139      23.597  48.928  -0.946  1.00 36.31           C  
ANISOU 2195  CD2 HIS A 139     4828   5522   3445  -3015    865   -714       C  
ATOM   2196  CE1 HIS A 139      21.808  48.234   0.119  1.00 33.87           C  
ANISOU 2196  CE1 HIS A 139     4588   5084   3196  -2830    796   -654       C  
ATOM   2197  NE2 HIS A 139      23.031  48.708   0.287  1.00 35.29           N  
ANISOU 2197  NE2 HIS A 139     4722   5332   3356  -2939    821   -702       N  
ATOM   2198  H   HIS A 139      24.562  46.293  -3.064  1.00 43.85           H  
ATOM   2199  HA  HIS A 139      22.535  46.598  -3.645  1.00 42.68           H  
ATOM   2200  HB2 HIS A 139      23.374  49.285  -3.632  1.00 43.15           H  
ATOM   2201  HB3 HIS A 139      21.847  48.857  -3.693  1.00 43.15           H  
ATOM   2202  HD1 HIS A 139      20.837  47.871  -1.533  1.00 40.70           H  
ATOM   2203  HD2 HIS A 139      24.450  49.258  -1.110  1.00 43.57           H  
ATOM   2204  HE1 HIS A 139      21.215  48.004   0.798  1.00 40.64           H  
ATOM   2205  HE2 HIS A 139      23.413  48.848   1.045  1.00 42.35           H  
ATOM   2206  N   LYS A 140      23.182  46.239  -6.195  1.00 35.61           N  
ANISOU 2206  N   LYS A 140     4541   5685   3302  -2908    920   -714       N  
ATOM   2207  CA  LYS A 140      23.080  46.196  -7.647  1.00 35.99           C  
ANISOU 2207  CA  LYS A 140     4589   5763   3321  -2927    952   -697       C  
ATOM   2208  C   LYS A 140      21.891  45.347  -8.093  1.00 34.40           C  
ANISOU 2208  C   LYS A 140     4401   5514   3153  -2797    918   -653       C  
ATOM   2209  O   LYS A 140      21.689  45.132  -9.286  1.00 34.49           O  
ANISOU 2209  O   LYS A 140     4406   5549   3149  -2790    937   -636       O  
ATOM   2210  CB  LYS A 140      24.384  45.654  -8.223  1.00 37.12           C  
ANISOU 2210  CB  LYS A 140     4592   6079   3434  -2988    976   -776       C  
ATOM   2211  CG  LYS A 140      25.626  46.370  -7.687  1.00 38.67           C  
ANISOU 2211  CG  LYS A 140     4757   6333   3604  -3109   1005   -825       C  
ATOM   2212  CD  LYS A 140      26.911  45.853  -8.340  1.00 39.89           C  
ANISOU 2212  CD  LYS A 140     4769   6659   3727  -3168   1031   -903       C  
ATOM   2213  CE  LYS A 140      28.162  46.535  -7.761  1.00 41.44           C  
ANISOU 2213  CE  LYS A 140     4928   6912   3903  -3286   1057   -952       C  
ATOM   2214  NZ  LYS A 140      29.431  46.008  -8.389  1.00 43.28           N  
ANISOU 2214  NZ  LYS A 140     5017   7319   4107  -3337   1083  -1032       N  
ATOM   2215  H   LYS A 140      23.433  45.498  -5.837  1.00 42.73           H  
ATOM   2216  HA  LYS A 140      22.951  47.097  -7.984  1.00 43.19           H  
ATOM   2217  HB2 LYS A 140      24.461  44.714  -7.998  1.00 44.55           H  
ATOM   2218  HB3 LYS A 140      24.371  45.763  -9.187  1.00 44.55           H  
ATOM   2219  HG2 LYS A 140      25.553  47.319  -7.873  1.00 46.41           H  
ATOM   2220  HG3 LYS A 140      25.692  46.220  -6.731  1.00 46.41           H  
ATOM   2221  HD2 LYS A 140      26.986  44.899  -8.184  1.00 47.86           H  
ATOM   2222  HD3 LYS A 140      26.880  46.035  -9.292  1.00 47.86           H  
ATOM   2223  HE2 LYS A 140      28.114  47.489  -7.931  1.00 49.72           H  
ATOM   2224  HE3 LYS A 140      28.205  46.367  -6.806  1.00 49.72           H  
ATOM   2225  HZ1 LYS A 140      29.502  45.133  -8.243  1.00 51.93           H  
ATOM   2226  HZ2 LYS A 140      29.419  46.154  -9.267  1.00 51.93           H  
ATOM   2227  HZ3 LYS A 140      30.138  46.418  -8.037  1.00 51.93           H  
ATOM   2228  N   LEU A 141      21.093  44.863  -7.139  1.00 32.96           N  
ANISOU 2228  N   LEU A 141     4239   5265   3020  -2693    868   -632       N  
ATOM   2229  CA  LEU A 141      19.934  44.046  -7.493  1.00 31.42           C  
ANISOU 2229  CA  LEU A 141     4057   5020   2863  -2568    832   -586       C  
ATOM   2230  C   LEU A 141      18.756  44.945  -7.815  1.00 31.04           C  
ANISOU 2230  C   LEU A 141     4160   4812   2820  -2545    841   -499       C  
ATOM   2231  O   LEU A 141      18.532  45.940  -7.143  1.00 31.30           O  
ANISOU 2231  O   LEU A 141     4290   4750   2851  -2577    847   -474       O  
ATOM   2232  CB  LEU A 141      19.561  43.099  -6.342  1.00 30.07           C  
ANISOU 2232  CB  LEU A 141     3835   4847   2743  -2462    772   -595       C  
ATOM   2233  CG  LEU A 141      20.654  42.136  -5.865  1.00 30.32           C  
ANISOU 2233  CG  LEU A 141     3712   5024   2783  -2456    752   -678       C  
ATOM   2234  CD1 LEU A 141      20.032  41.118  -4.936  1.00 31.59           C  
ANISOU 2234  CD1 LEU A 141     3834   5166   3004  -2329    687   -667       C  
ATOM   2235  CD2 LEU A 141      21.343  41.439  -7.035  1.00 36.88           C  
ANISOU 2235  CD2 LEU A 141     4435   5990   3589  -2469    770   -727       C  
ATOM   2236  H   LEU A 141      21.198  44.991  -6.295  1.00 39.55           H  
ATOM   2237  HA  LEU A 141      20.140  43.513  -8.278  1.00 37.71           H  
ATOM   2238  HB2 LEU A 141      19.300  43.639  -5.579  1.00 36.08           H  
ATOM   2239  HB3 LEU A 141      18.806  42.560  -6.625  1.00 36.08           H  
ATOM   2240  HG  LEU A 141      21.324  42.632  -5.368  1.00 36.38           H  
ATOM   2241 HD11 LEU A 141      20.721  40.506  -4.632  1.00 37.91           H  
ATOM   2242 HD12 LEU A 141      19.641  41.580  -4.178  1.00 37.91           H  
ATOM   2243 HD13 LEU A 141      19.345  40.630  -5.417  1.00 37.91           H  
ATOM   2244 HD21 LEU A 141      22.025  40.842  -6.690  1.00 44.26           H  
ATOM   2245 HD22 LEU A 141      20.683  40.934  -7.535  1.00 44.26           H  
ATOM   2246 HD23 LEU A 141      21.750  42.110  -7.607  1.00 44.26           H  
ATOM   2247  N   GLU A 142      17.989  44.585  -8.833  1.00 30.42           N  
ANISOU 2247  N   GLU A 142     4102   4703   2753  -2482    840   -455       N  
ATOM   2248  CA  GLU A 142      16.770  45.315  -9.147  1.00 29.90           C  
ANISOU 2248  CA  GLU A 142     4173   4483   2705  -2433    841   -371       C  
ATOM   2249  C   GLU A 142      15.724  45.082  -8.057  1.00 28.44           C  
ANISOU 2249  C   GLU A 142     4037   4196   2572  -2324    790   -335       C  
ATOM   2250  O   GLU A 142      15.714  44.034  -7.431  1.00 27.52           O  
ANISOU 2250  O   GLU A 142     3839   4132   2485  -2260    750   -360       O  
ATOM   2251  CB  GLU A 142      16.206  44.854 -10.494  1.00 29.53           C  
ANISOU 2251  CB  GLU A 142     4123   4435   2664  -2379    848   -332       C  
ATOM   2252  CG  GLU A 142      17.152  45.156 -11.682  1.00 31.05           C  
ANISOU 2252  CG  GLU A 142     4276   4722   2800  -2487    902   -359       C  
ATOM   2253  CD  GLU A 142      16.544  44.876 -13.068  1.00 30.82           C  
ANISOU 2253  CD  GLU A 142     4261   4678   2771  -2439    916   -311       C  
ATOM   2254  OE1 GLU A 142      15.569  44.107 -13.189  1.00 29.43           O  
ANISOU 2254  OE1 GLU A 142     4086   4455   2640  -2317    880   -273       O  
ATOM   2255  OE2 GLU A 142      17.065  45.437 -14.059  1.00 35.08           O  
ANISOU 2255  OE2 GLU A 142     4809   5254   3265  -2525    963   -310       O  
ATOM   2256  H   GLU A 142      18.151  43.923  -9.358  1.00 36.50           H  
ATOM   2257  HA  GLU A 142      16.960  46.265  -9.197  1.00 35.88           H  
ATOM   2258  HB2 GLU A 142      16.061  43.895 -10.463  1.00 35.44           H  
ATOM   2259  HB3 GLU A 142      15.366  45.310 -10.657  1.00 35.44           H  
ATOM   2260  HG2 GLU A 142      17.397  46.094 -11.652  1.00 37.26           H  
ATOM   2261  HG3 GLU A 142      17.947  44.607 -11.592  1.00 37.26           H  
ATOM   2262  N   TYR A 143      14.837  46.056  -7.882  1.00 28.27           N  
ANISOU 2262  N   TYR A 143     4144   4035   2563  -2299    791   -275       N  
ATOM   2263  CA  TYR A 143      13.744  45.951  -6.926  1.00 26.96           C  
ANISOU 2263  CA  TYR A 143     4033   3766   2445  -2191    746   -236       C  
ATOM   2264  C   TYR A 143      12.569  45.223  -7.568  1.00 30.59           C  
ANISOU 2264  C   TYR A 143     4501   4172   2950  -2060    718   -179       C  
ATOM   2265  O   TYR A 143      11.563  45.815  -7.958  1.00 25.33           O  
ANISOU 2265  O   TYR A 143     3930   3393   2301  -2003    718   -120       O  
ATOM   2266  CB  TYR A 143      13.321  47.330  -6.422  1.00 27.44           C  
ANISOU 2266  CB  TYR A 143     4219   3707   2498  -2216    758   -206       C  
ATOM   2267  CG  TYR A 143      12.343  47.258  -5.260  1.00 26.25           C  
ANISOU 2267  CG  TYR A 143     4115   3469   2390  -2115    714   -179       C  
ATOM   2268  CD1 TYR A 143      12.765  46.870  -3.987  1.00 26.01           C  
ANISOU 2268  CD1 TYR A 143     4037   3481   2364  -2124    690   -219       C  
ATOM   2269  CD2 TYR A 143      11.017  47.594  -5.434  1.00 25.65           C  
ANISOU 2269  CD2 TYR A 143     4140   3276   2328  -2034    701   -126       C  
ATOM   2270  CE1 TYR A 143      11.881  46.813  -2.934  1.00 25.00           C  
ANISOU 2270  CE1 TYR A 143     3951   3277   2271  -2037    652   -194       C  
ATOM   2271  CE2 TYR A 143      10.112  47.522  -4.368  1.00 24.68           C  
ANISOU 2271  CE2 TYR A 143     4061   3082   2236  -1948    663   -108       C  
ATOM   2272  CZ  TYR A 143      10.559  47.136  -3.136  1.00 24.33           C  
ANISOU 2272  CZ  TYR A 143     3959   3079   2207  -1948    639   -138       C  
ATOM   2273  OH  TYR A 143       9.666  47.077  -2.094  1.00 23.45           O  
ANISOU 2273  OH  TYR A 143     3889   2899   2120  -1867    603   -119       O  
ATOM   2274  H   TYR A 143      14.848  46.800  -8.314  1.00 33.93           H  
ATOM   2275  HA  TYR A 143      14.040  45.430  -6.164  1.00 32.35           H  
ATOM   2276  HB2 TYR A 143      14.108  47.811  -6.122  1.00 32.92           H  
ATOM   2277  HB3 TYR A 143      12.892  47.813  -7.145  1.00 32.92           H  
ATOM   2278  HD1 TYR A 143      13.657  46.647  -3.849  1.00 31.21           H  
ATOM   2279  HD2 TYR A 143      10.715  47.851  -6.275  1.00 30.77           H  
ATOM   2280  HE1 TYR A 143      12.174  46.546  -2.092  1.00 30.00           H  
ATOM   2281  HE2 TYR A 143       9.218  47.746  -4.495  1.00 29.62           H  
ATOM   2282  HH  TYR A 143       8.900  47.298  -2.359  1.00 28.13           H  
ATOM   2283  N   ASN A 144      12.714  43.909  -7.640  1.00 24.88           N  
ANISOU 2283  N   ASN A 144     3671   3535   2245  -2012    691   -202       N  
ATOM   2284  CA  ASN A 144      11.673  43.040  -8.161  1.00 23.56           C  
ANISOU 2284  CA  ASN A 144     3495   3331   2125  -1886    659   -152       C  
ATOM   2285  C   ASN A 144      12.009  41.616  -7.747  1.00 22.79           C  
ANISOU 2285  C   ASN A 144     3273   3341   2047  -1847    619   -192       C  
ATOM   2286  O   ASN A 144      12.962  41.380  -6.979  1.00 23.24           O  
ANISOU 2286  O   ASN A 144     3256   3489   2085  -1906    613   -256       O  
ATOM   2287  CB  ASN A 144      11.519  43.177  -9.679  1.00 23.97           C  
ANISOU 2287  CB  ASN A 144     3564   3380   2162  -1889    692   -121       C  
ATOM   2288  CG  ASN A 144      12.828  43.033 -10.419  1.00 26.61           C  
ANISOU 2288  CG  ASN A 144     3815   3853   2442  -2003    732   -183       C  
ATOM   2289  OD1 ASN A 144      13.704  42.264 -10.015  1.00 25.37           O  
ANISOU 2289  OD1 ASN A 144     3548   3819   2274  -2036    721   -249       O  
ATOM   2290  ND2 ASN A 144      12.977  43.781 -11.519  1.00 26.24           N  
ANISOU 2290  ND2 ASN A 144     3816   3793   2362  -2061    778   -163       N  
ATOM   2291  H   ASN A 144      13.421  43.489  -7.388  1.00 29.85           H  
ATOM   2292  HA  ASN A 144      10.827  43.280  -7.752  1.00 28.27           H  
ATOM   2293  HB2 ASN A 144      10.918  42.486  -9.998  1.00 28.76           H  
ATOM   2294  HB3 ASN A 144      11.156  44.053  -9.882  1.00 28.76           H  
ATOM   2295 HD21 ASN A 144      12.346  44.308 -11.770  1.00 31.49           H  
ATOM   2296 HD22 ASN A 144      13.705  43.735 -11.975  1.00 31.49           H  
ATOM   2297  N   TYR A 145      11.214  40.669  -8.223  1.00 22.88           N  
ANISOU 2297  N   TYR A 145     3255   3340   2097  -1741    587   -153       N  
ATOM   2298  CA  TYR A 145      11.270  39.318  -7.686  1.00 25.74           C  
ANISOU 2298  CA  TYR A 145     3509   3782   2488  -1681    535   -177       C  
ATOM   2299  C   TYR A 145      10.726  38.308  -8.672  1.00 25.36           C  
ANISOU 2299  C   TYR A 145     3412   3758   2464  -1599    517   -148       C  
ATOM   2300  O   TYR A 145       9.716  38.536  -9.339  1.00 21.65           O  
ANISOU 2300  O   TYR A 145     3021   3187   2019  -1529    521    -77       O  
ATOM   2301  CB  TYR A 145      10.529  39.207  -6.337  1.00 20.25           C  
ANISOU 2301  CB  TYR A 145     2849   3009   1836  -1609    487   -148       C  
ATOM   2302  CG  TYR A 145      11.239  38.241  -5.420  1.00 19.45           C  
ANISOU 2302  CG  TYR A 145     2628   3020   1743  -1611    447   -205       C  
ATOM   2303  CD1 TYR A 145      12.363  38.638  -4.712  1.00 23.92           C  
ANISOU 2303  CD1 TYR A 145     3157   3654   2276  -1702    465   -271       C  
ATOM   2304  CD2 TYR A 145      10.822  36.921  -5.302  1.00 18.31           C  
ANISOU 2304  CD2 TYR A 145     2399   2916   1641  -1515    389   -193       C  
ATOM   2305  CE1 TYR A 145      13.047  37.751  -3.896  1.00 20.31           C  
ANISOU 2305  CE1 TYR A 145     2583   3298   1836  -1685    426   -322       C  
ATOM   2306  CE2 TYR A 145      11.500  36.035  -4.500  1.00 18.18           C  
ANISOU 2306  CE2 TYR A 145     2264   3001   1641  -1500    347   -244       C  
ATOM   2307  CZ  TYR A 145      12.612  36.449  -3.807  1.00 19.18           C  
ANISOU 2307  CZ  TYR A 145     2356   3188   1742  -1578    366   -309       C  
ATOM   2308  OH  TYR A 145      13.309  35.570  -3.007  1.00 22.30           O  
ANISOU 2308  OH  TYR A 145     2631   3671   2170  -1541    320   -357       O  
ATOM   2309  H   TYR A 145      10.638  40.781  -8.852  1.00 27.45           H  
ATOM   2310  HA  TYR A 145      12.199  39.093  -7.525  1.00 30.89           H  
ATOM   2311  HB2 TYR A 145      10.506  40.076  -5.908  1.00 24.30           H  
ATOM   2312  HB3 TYR A 145       9.629  38.880  -6.489  1.00 24.30           H  
ATOM   2313  HD1 TYR A 145      12.663  39.515  -4.786  1.00 28.70           H  
ATOM   2314  HD2 TYR A 145      10.078  36.631  -5.780  1.00 21.97           H  
ATOM   2315  HE1 TYR A 145      13.802  38.028  -3.429  1.00 24.37           H  
ATOM   2316  HE2 TYR A 145      11.211  35.154  -4.432  1.00 21.81           H  
ATOM   2317  HH  TYR A 145      12.951  34.811  -3.034  1.00 26.76           H  
ATOM   2318  N   ASN A 146      11.413  37.181  -8.741  1.00 20.94           N  
ANISOU 2318  N   ASN A 146     2717   3338   1900  -1597    492   -205       N  
ATOM   2319  CA  ASN A 146      11.089  36.143  -9.703  1.00 19.26           C  
ANISOU 2319  CA  ASN A 146     2437   3179   1702  -1529    474   -192       C  
ATOM   2320  C   ASN A 146      10.195  35.076  -9.090  1.00 20.97           C  
ANISOU 2320  C   ASN A 146     2619   3370   1977  -1408    402   -152       C  
ATOM   2321  O   ASN A 146       9.728  35.228  -7.971  1.00 23.43           O  
ANISOU 2321  O   ASN A 146     2973   3608   2320  -1377    372   -126       O  
ATOM   2322  CB  ASN A 146      12.391  35.571 -10.253  1.00 25.69           C  
ANISOU 2322  CB  ASN A 146     3115   4172   2475  -1588    487   -285       C  
ATOM   2323  CG  ASN A 146      12.911  36.379 -11.433  1.00 39.91           C  
ANISOU 2323  CG  ASN A 146     4950   5991   4221  -1679    556   -296       C  
ATOM   2324  OD1 ASN A 146      12.178  36.622 -12.391  1.00 41.81           O  
ANISOU 2324  OD1 ASN A 146     5262   6159   4466  -1649    578   -233       O  
ATOM   2325  ND2 ASN A 146      14.164  36.829 -11.354  1.00 37.65           N  
ANISOU 2325  ND2 ASN A 146     4619   5798   3888  -1788    591   -371       N  
ATOM   2326  H   ASN A 146      12.082  36.991  -8.235  1.00 25.13           H  
ATOM   2327  HA  ASN A 146      10.606  36.543 -10.442  1.00 23.11           H  
ATOM   2328  HB2 ASN A 146      13.065  35.584  -9.556  1.00 30.83           H  
ATOM   2329  HB3 ASN A 146      12.237  34.661 -10.553  1.00 30.83           H  
ATOM   2330 HD21 ASN A 146      14.639  36.658 -10.658  1.00 45.18           H  
ATOM   2331 HD22 ASN A 146      14.497  37.289 -11.999  1.00 45.18           H  
ATOM   2332  N   HIS A 147       9.947  34.005  -9.828  1.00 17.14           N  
ANISOU 2332  N   HIS A 147     2055   2950   1508  -1340    374   -146       N  
ATOM   2333  CA  HIS A 147       9.051  32.941  -9.370  1.00 15.70           C  
ANISOU 2333  CA  HIS A 147     1834   2748   1383  -1222    301   -101       C  
ATOM   2334  C   HIS A 147       9.874  31.675  -9.274  1.00 20.73           C  
ANISOU 2334  C   HIS A 147     2296   3550   2032  -1183    248   -180       C  
ATOM   2335  O   HIS A 147      10.699  31.400 -10.166  1.00 16.52           O  
ANISOU 2335  O   HIS A 147     1682   3133   1462  -1210    272   -244       O  
ATOM   2336  CB  HIS A 147       7.920  32.733 -10.367  1.00 14.93           C  
ANISOU 2336  CB  HIS A 147     1798   2570   1306  -1142    303    -16       C  
ATOM   2337  CG  HIS A 147       8.394  32.671 -11.779  1.00 21.39           C  
ANISOU 2337  CG  HIS A 147     2580   3466   2081  -1173    348    -43       C  
ATOM   2338  ND1 HIS A 147       8.623  31.482 -12.431  1.00 26.08           N  
ANISOU 2338  ND1 HIS A 147     3042   4196   2673  -1124    313    -79       N  
ATOM   2339  CD2 HIS A 147       8.709  33.650 -12.652  1.00 25.78           C  
ANISOU 2339  CD2 HIS A 147     3208   3992   2595  -1244    419    -44       C  
ATOM   2340  CE1 HIS A 147       9.054  31.731 -13.653  1.00 27.20           C  
ANISOU 2340  CE1 HIS A 147     3181   4386   2769  -1167    368   -101       C  
ATOM   2341  NE2 HIS A 147       9.104  33.041 -13.818  1.00 24.52           N  
ANISOU 2341  NE2 HIS A 147     2966   3944   2405  -1243    432    -76       N  
ATOM   2342  H   HIS A 147      10.286  33.865 -10.605  1.00 20.57           H  
ATOM   2343  HA  HIS A 147       8.682  33.156  -8.499  1.00 18.84           H  
ATOM   2344  HB2 HIS A 147       7.472  31.897 -10.164  1.00 17.92           H  
ATOM   2345  HB3 HIS A 147       7.295  33.471 -10.293  1.00 17.92           H  
ATOM   2346  HD1 HIS A 147       8.507  30.700 -12.094  1.00 31.30           H  
ATOM   2347  HD2 HIS A 147       8.655  34.566 -12.499  1.00 30.94           H  
ATOM   2348  HE1 HIS A 147       9.269  31.093 -14.295  1.00 32.65           H  
ATOM   2349  HE2 HIS A 147       9.355  33.445 -14.534  1.00 29.42           H  
ATOM   2350  N   HIS A 148       9.664  30.912  -8.202  1.00 14.83           N  
ANISOU 2350  N   HIS A 148     1626   2363   1646   -423   -347   -115       N  
ATOM   2351  CA  HIS A 148      10.576  29.830  -7.859  1.00 14.31           C  
ANISOU 2351  CA  HIS A 148     1611   2314   1513   -373   -311   -334       C  
ATOM   2352  C   HIS A 148       9.852  28.536  -7.549  1.00 16.31           C  
ANISOU 2352  C   HIS A 148     1891   2533   1772   -356   -403   -330       C  
ATOM   2353  O   HIS A 148       8.631  28.518  -7.466  1.00 14.49           O  
ANISOU 2353  O   HIS A 148     1614   2271   1620   -383   -498   -151       O  
ATOM   2354  CB  HIS A 148      11.443  30.266  -6.688  1.00 13.49           C  
ANISOU 2354  CB  HIS A 148     1450   2186   1492   -265   -213   -437       C  
ATOM   2355  CG  HIS A 148      12.221  31.515  -6.974  1.00 14.60           C  
ANISOU 2355  CG  HIS A 148     1573   2351   1622   -310   -129   -447       C  
ATOM   2356  ND1 HIS A 148      12.006  32.705  -6.308  1.00 14.17           N  
ANISOU 2356  ND1 HIS A 148     1512   2226   1646   -295    -69   -374       N  
ATOM   2357  CD2 HIS A 148      13.159  31.775  -7.918  1.00 16.74           C  
ANISOU 2357  CD2 HIS A 148     1856   2691   1814   -381    -69   -511       C  
ATOM   2358  CE1 HIS A 148      12.819  33.629  -6.793  1.00 14.21           C  
ANISOU 2358  CE1 HIS A 148     1517   2264   1617   -364     -5   -399       C  
ATOM   2359  NE2 HIS A 148      13.528  33.088  -7.770  1.00 14.66           N  
ANISOU 2359  NE2 HIS A 148     1569   2415   1588   -414     -6   -476       N  
ATOM   2360  H   HIS A 148       9.002  31.001  -7.661  1.00 17.80           H  
ATOM   2361  HA  HIS A 148      11.162  29.666  -8.614  1.00 17.17           H  
ATOM   2362  HB2 HIS A 148      10.875  30.435  -5.920  1.00 16.19           H  
ATOM   2363  HB3 HIS A 148      12.075  29.559  -6.483  1.00 16.19           H  
ATOM   2364  HD1 HIS A 148      11.454  32.819  -5.659  1.00 17.00           H  
ATOM   2365  HD2 HIS A 148      13.512  31.168  -8.528  1.00 20.09           H  
ATOM   2366  HE1 HIS A 148      12.876  34.511  -6.503  1.00 17.05           H  
ATOM   2367  HE2 HIS A 148      14.119  33.496  -8.243  1.00 17.60           H  
ATOM   2368  N   LYS A 149      10.615  27.447  -7.447  1.00 14.18           N  
ANISOU 2368  N   LYS A 149     1684   2259   1443   -316   -364   -504       N  
ATOM   2369  CA  LYS A 149      10.095  26.137  -7.073  1.00 14.16           C  
ANISOU 2369  CA  LYS A 149     1731   2205   1444   -292   -427   -529       C  
ATOM   2370  C   LYS A 149      10.863  25.695  -5.839  1.00 13.49           C  
ANISOU 2370  C   LYS A 149     1585   2088   1452   -133   -361   -640       C  
ATOM   2371  O   LYS A 149      12.085  25.585  -5.876  1.00 16.38           O  
ANISOU 2371  O   LYS A 149     1931   2475   1819    -81   -272   -756       O  
ATOM   2372  CB  LYS A 149      10.264  25.112  -8.216  1.00 16.14           C  
ANISOU 2372  CB  LYS A 149     2175   2440   1519   -413   -428   -620       C  
ATOM   2373  CG  LYS A 149       9.203  25.201  -9.244  1.00 24.50           C  
ANISOU 2373  CG  LYS A 149     3337   3514   2456   -627   -585   -471       C  
ATOM   2374  CD  LYS A 149       9.425  24.220 -10.402  1.00 27.03           C  
ANISOU 2374  CD  LYS A 149     3942   3782   2546   -786   -560   -579       C  
ATOM   2375  CE  LYS A 149       8.998  22.805 -10.098  1.00 22.45           C  
ANISOU 2375  CE  LYS A 149     3455   3102   1973   -771   -586   -621       C  
ATOM   2376  NZ  LYS A 149       8.770  22.062 -11.428  1.00 23.99           N  
ANISOU 2376  NZ  LYS A 149     3921   3220   1975   -956   -578   -615       N  
ATOM   2377  H   LYS A 149      11.463  27.445  -7.595  1.00 17.01           H  
ATOM   2378  HA  LYS A 149       9.154  26.207  -6.850  1.00 16.99           H  
ATOM   2379  HB2 LYS A 149      11.116  25.265  -8.653  1.00 19.37           H  
ATOM   2380  HB3 LYS A 149      10.241  24.217  -7.841  1.00 19.37           H  
ATOM   2381  HG2 LYS A 149       8.348  24.996  -8.835  1.00 29.39           H  
ATOM   2382  HG3 LYS A 149       9.191  26.100  -9.609  1.00 29.39           H  
ATOM   2383  HD2 LYS A 149       8.915  24.524 -11.170  1.00 32.43           H  
ATOM   2384  HD3 LYS A 149      10.370  24.204 -10.621  1.00 32.43           H  
ATOM   2385  HE2 LYS A 149       9.697  22.350  -9.601  1.00 26.94           H  
ATOM   2386  HE3 LYS A 149       8.168  22.812  -9.597  1.00 26.94           H  
ATOM   2387  HZ1 LYS A 149       9.522  22.052 -11.904  1.00 28.79           H  
ATOM   2388  HZ2 LYS A 149       8.517  21.223 -11.268  1.00 28.79           H  
ATOM   2389  HZ3 LYS A 149       8.135  22.470 -11.899  1.00 28.79           H  
ATOM   2390  N   VAL A 150      10.137  25.499  -4.741  1.00 14.31           N  
ANISOU 2390  N   VAL A 150     1651   2138   1648    -65   -406   -574       N  
ATOM   2391  CA  VAL A 150      10.699  25.175  -3.435  1.00 15.10           C  
ANISOU 2391  CA  VAL A 150     1726   2201   1811     52   -384   -638       C  
ATOM   2392  C   VAL A 150      10.536  23.669  -3.172  1.00 13.60           C  
ANISOU 2392  C   VAL A 150     1590   1954   1623     99   -421   -686       C  
ATOM   2393  O   VAL A 150       9.432  23.200  -2.998  1.00 14.69           O  
ANISOU 2393  O   VAL A 150     1759   2042   1780     76   -472   -606       O  
ATOM   2394  CB  VAL A 150       9.922  25.997  -2.383  1.00 11.69           C  
ANISOU 2394  CB  VAL A 150     1285   1707   1449     79   -362   -533       C  
ATOM   2395  CG1 VAL A 150      10.311  25.624  -0.967  1.00 11.52           C  
ANISOU 2395  CG1 VAL A 150     1312   1628   1438    151   -363   -581       C  
ATOM   2396  CG2 VAL A 150      10.115  27.493  -2.652  1.00 15.74           C  
ANISOU 2396  CG2 VAL A 150     1776   2240   1966     34   -295   -490       C  
ATOM   2397  H   VAL A 150       9.278  25.552  -4.730  1.00 17.17           H  
ATOM   2398  HA  VAL A 150      11.639  25.410  -3.402  1.00 18.12           H  
ATOM   2399  HB  VAL A 150       8.976  25.805  -2.483  1.00 14.02           H  
ATOM   2400 HG11 VAL A 150       9.798  26.165  -0.346  1.00 13.82           H  
ATOM   2401 HG12 VAL A 150      10.118  24.684  -0.824  1.00 13.82           H  
ATOM   2402 HG13 VAL A 150      11.259  25.790  -0.846  1.00 13.82           H  
ATOM   2403 HG21 VAL A 150       9.624  28.000  -1.987  1.00 18.89           H  
ATOM   2404 HG22 VAL A 150      11.061  27.704  -2.598  1.00 18.89           H  
ATOM   2405 HG23 VAL A 150       9.781  27.700  -3.539  1.00 18.89           H  
ATOM   2406  N   TYR A 151      11.628  22.912  -3.185  1.00 12.90           N  
ANISOU 2406  N   TYR A 151     1499   1862   1541    167   -380   -792       N  
ATOM   2407  CA  TYR A 151      11.538  21.460  -3.094  1.00 13.45           C  
ANISOU 2407  CA  TYR A 151     1642   1849   1617    216   -380   -839       C  
ATOM   2408  C   TYR A 151      11.532  21.014  -1.643  1.00 13.06           C  
ANISOU 2408  C   TYR A 151     1564   1753   1647    316   -438   -804       C  
ATOM   2409  O   TYR A 151      12.348  21.488  -0.854  1.00 14.08           O  
ANISOU 2409  O   TYR A 151     1613   1914   1822    364   -461   -793       O  
ATOM   2410  CB  TYR A 151      12.719  20.843  -3.831  1.00 14.74           C  
ANISOU 2410  CB  TYR A 151     1819   1992   1792    267   -250   -943       C  
ATOM   2411  CG  TYR A 151      12.603  21.056  -5.308  1.00 15.58           C  
ANISOU 2411  CG  TYR A 151     2050   2107   1762    137   -170   -992       C  
ATOM   2412  CD1 TYR A 151      11.745  20.281  -6.054  1.00 17.90           C  
ANISOU 2412  CD1 TYR A 151     2550   2328   1923     13   -193  -1012       C  
ATOM   2413  CD2 TYR A 151      13.320  22.053  -5.948  1.00 18.65           C  
ANISOU 2413  CD2 TYR A 151     2380   2574   2133    104    -91  -1006       C  
ATOM   2414  CE1 TYR A 151      11.614  20.470  -7.412  1.00 21.24           C  
ANISOU 2414  CE1 TYR A 151     3151   2752   2168   -158   -151  -1045       C  
ATOM   2415  CE2 TYR A 151      13.213  22.240  -7.315  1.00 22.24           C  
ANISOU 2415  CE2 TYR A 151     2995   3028   2428    -37    -16  -1045       C  
ATOM   2416  CZ  TYR A 151      12.350  21.442  -8.037  1.00 23.23           C  
ANISOU 2416  CZ  TYR A 151     3358   3077   2392   -177    -55  -1064       C  
ATOM   2417  OH  TYR A 151      12.193  21.616  -9.395  1.00 29.13           O  
ANISOU 2417  OH  TYR A 151     4327   3816   2927   -371    -15  -1089       O  
ATOM   2418  H   TYR A 151      12.431  23.214  -3.244  1.00 15.48           H  
ATOM   2419  HA  TYR A 151      10.718  21.157  -3.515  1.00 16.14           H  
ATOM   2420  HB2 TYR A 151      13.541  21.259  -3.526  1.00 17.69           H  
ATOM   2421  HB3 TYR A 151      12.741  19.888  -3.661  1.00 17.69           H  
ATOM   2422  HD1 TYR A 151      11.249  19.615  -5.635  1.00 21.48           H  
ATOM   2423  HD2 TYR A 151      13.907  22.582  -5.458  1.00 22.38           H  
ATOM   2424  HE1 TYR A 151      11.036  19.933  -7.904  1.00 25.49           H  
ATOM   2425  HE2 TYR A 151      13.701  22.909  -7.738  1.00 26.69           H  
ATOM   2426  HH  TYR A 151      12.693  22.235  -9.665  1.00 34.96           H  
ATOM   2427  N   ILE A 152      10.604  20.132  -1.296  1.00 14.34           N  
ANISOU 2427  N   ILE A 152     1805   1835   1807    316   -477   -773       N  
ATOM   2428  CA  ILE A 152      10.447  19.664   0.083  1.00 12.81           C  
ANISOU 2428  CA  ILE A 152     1626   1581   1661    392   -523   -730       C  
ATOM   2429  C   ILE A 152      10.557  18.153   0.169  1.00 16.03           C  
ANISOU 2429  C   ILE A 152     2100   1893   2100    458   -520   -765       C  
ATOM   2430  O   ILE A 152       9.954  17.458  -0.636  1.00 15.08           O  
ANISOU 2430  O   ILE A 152     2071   1718   1939    394   -499   -794       O  
ATOM   2431  CB  ILE A 152       9.070  20.082   0.609  1.00 16.48           C  
ANISOU 2431  CB  ILE A 152     2124   2009   2129    341   -532   -625       C  
ATOM   2432  CG1 ILE A 152       8.953  21.617   0.597  1.00 12.30           C  
ANISOU 2432  CG1 ILE A 152     1548   1531   1594    299   -488   -576       C  
ATOM   2433  CG2 ILE A 152       8.814  19.473   1.985  1.00 14.45           C  
ANISOU 2433  CG2 ILE A 152     1937   1662   1889    403   -546   -587       C  
ATOM   2434  CD1 ILE A 152       7.516  22.144   0.847  1.00 12.85           C  
ANISOU 2434  CD1 ILE A 152     1610   1542   1731    267   -429   -432       C  
ATOM   2435  H   ILE A 152      10.043  19.783  -1.846  1.00 17.20           H  
ATOM   2436  HA  ILE A 152      11.130  20.060   0.645  1.00 15.38           H  
ATOM   2437  HB  ILE A 152       8.401  19.729   0.001  1.00 19.78           H  
ATOM   2438 HG12 ILE A 152       9.525  21.978   1.292  1.00 14.76           H  
ATOM   2439 HG13 ILE A 152       9.242  21.945  -0.269  1.00 14.76           H  
ATOM   2440 HG21 ILE A 152       7.938  19.752   2.296  1.00 17.33           H  
ATOM   2441 HG22 ILE A 152       8.848  18.506   1.914  1.00 17.33           H  
ATOM   2442 HG23 ILE A 152       9.497  19.784   2.599  1.00 17.33           H  
ATOM   2443 HD11 ILE A 152       7.528  23.114   0.824  1.00 15.42           H  
ATOM   2444 HD12 ILE A 152       6.930  21.804   0.153  1.00 15.42           H  
ATOM   2445 HD13 ILE A 152       7.214  21.837   1.716  1.00 15.42           H  
ATOM   2446  N   THR A 153      11.313  17.649   1.156  1.00 14.11           N  
ANISOU 2446  N   THR A 153     1826   1614   1919    564   -554   -747       N  
ATOM   2447  CA  THR A 153      11.382  16.216   1.452  1.00 15.03           C  
ANISOU 2447  CA  THR A 153     2005   1614   2092    648   -546   -749       C  
ATOM   2448  C   THR A 153      11.326  16.034   2.966  1.00 19.03           C  
ANISOU 2448  C   THR A 153     2533   2087   2609    690   -648   -657       C  
ATOM   2449  O   THR A 153      11.638  16.964   3.732  1.00 16.88           O  
ANISOU 2449  O   THR A 153     2235   1881   2299    656   -720   -609       O  
ATOM   2450  CB  THR A 153      12.674  15.585   0.901  1.00 17.76           C  
ANISOU 2450  CB  THR A 153     2277   1923   2549    763   -450   -790       C  
ATOM   2451  OG1 THR A 153      12.606  14.149   0.965  1.00 19.90           O  
ANISOU 2451  OG1 THR A 153     2646   2037   2879    846   -389   -800       O  
ATOM   2452  CG2 THR A 153      13.916  16.107   1.646  1.00 17.19           C  
ANISOU 2452  CG2 THR A 153     2016   1929   2587    836   -531   -701       C  
ATOM   2453  H   THR A 153      11.803  18.130   1.674  1.00 16.93           H  
ATOM   2454  HA  THR A 153      10.621  15.763   1.056  1.00 18.03           H  
ATOM   2455  HB  THR A 153      12.766  15.844  -0.030  1.00 21.31           H  
ATOM   2456  HG1 THR A 153      11.957  13.871   0.510  1.00 23.89           H  
ATOM   2457 HG21 THR A 153      14.716  15.697   1.283  1.00 20.63           H  
ATOM   2458 HG22 THR A 153      13.981  17.069   1.547  1.00 20.63           H  
ATOM   2459 HG23 THR A 153      13.851  15.891   2.590  1.00 20.63           H  
ATOM   2460  N   ALA A 154      10.918  14.846   3.397  1.00 17.31           N  
ANISOU 2460  N   ALA A 154     2406   1752   2417    737   -652   -634       N  
ATOM   2461  CA  ALA A 154      10.871  14.537   4.817  1.00 19.48           C  
ANISOU 2461  CA  ALA A 154     2744   1979   2680    765   -746   -538       C  
ATOM   2462  C   ALA A 154      12.266  14.377   5.382  1.00 17.35           C  
ANISOU 2462  C   ALA A 154     2365   1733   2496    850   -849   -461       C  
ATOM   2463  O   ALA A 154      13.217  13.972   4.692  1.00 18.40           O  
ANISOU 2463  O   ALA A 154     2360   1861   2768    948   -798   -469       O  
ATOM   2464  CB  ALA A 154      10.070  13.269   5.058  1.00 19.27           C  
ANISOU 2464  CB  ALA A 154     2840   1813   2668    788   -717   -522       C  
ATOM   2465  H   ALA A 154      10.665  14.202   2.886  1.00 20.77           H  
ATOM   2466  HA  ALA A 154      10.435  15.265   5.287  1.00 23.38           H  
ATOM   2467  HB1 ALA A 154      10.052  13.084   6.010  1.00 23.12           H  
ATOM   2468  HB2 ALA A 154       9.167  13.399   4.729  1.00 23.12           H  
ATOM   2469  HB3 ALA A 154      10.493  12.535   4.585  1.00 23.12           H  
ATOM   2470  N   ASP A 155      12.349  14.666   6.675  1.00 17.77           N  
ANISOU 2470  N   ASP A 155     2493   1793   2468    799   -986   -364       N  
ATOM   2471  CA  ASP A 155      13.512  14.354   7.488  1.00 20.22           C  
ANISOU 2471  CA  ASP A 155     2721   2114   2849    837  -1164   -221       C  
ATOM   2472  C   ASP A 155      12.975  13.639   8.729  1.00 20.33           C  
ANISOU 2472  C   ASP A 155     2934   2022   2768    816  -1249   -130       C  
ATOM   2473  O   ASP A 155      12.888  14.233   9.814  1.00 21.02           O  
ANISOU 2473  O   ASP A 155     3188   2120   2680    682  -1367    -68       O  
ATOM   2474  CB  ASP A 155      14.199  15.662   7.883  1.00 21.44           C  
ANISOU 2474  CB  ASP A 155     2837   2393   2918    703  -1300   -179       C  
ATOM   2475  CG  ASP A 155      15.587  15.460   8.467  1.00 29.73           C  
ANISOU 2475  CG  ASP A 155     3717   3491   4089    708  -1532     12       C  
ATOM   2476  OD1 ASP A 155      16.016  14.300   8.691  1.00 31.92           O  
ANISOU 2476  OD1 ASP A 155     3901   3698   4528    832  -1571    136       O  
ATOM   2477  OD2 ASP A 155      16.251  16.492   8.712  1.00 28.45           O  
ANISOU 2477  OD2 ASP A 155     3508   3434   3868    566  -1666     60       O  
ATOM   2478  H   ASP A 155      11.722  15.056   7.116  1.00 21.33           H  
ATOM   2479  HA  ASP A 155      14.131  13.780   7.010  1.00 24.27           H  
ATOM   2480  HB2 ASP A 155      14.287  16.221   7.095  1.00 25.73           H  
ATOM   2481  HB3 ASP A 155      13.658  16.112   8.549  1.00 25.73           H  
ATOM   2482  N   LYS A 156      12.622  12.368   8.578  1.00 20.69           N  
ANISOU 2482  N   LYS A 156     3006   1945   2910    928  -1174   -124       N  
ATOM   2483  CA  LYS A 156      11.877  11.652   9.607  1.00 21.13           C  
ANISOU 2483  CA  LYS A 156     3272   1884   2872    905  -1204    -59       C  
ATOM   2484  C   LYS A 156      12.611  11.570  10.961  1.00 23.13           C  
ANISOU 2484  C   LYS A 156     3594   2137   3056    853  -1444    129       C  
ATOM   2485  O   LYS A 156      11.971  11.622  11.998  1.00 23.40           O  
ANISOU 2485  O   LYS A 156     3881   2111   2898    746  -1476    167       O  
ATOM   2486  CB  LYS A 156      11.490  10.230   9.151  1.00 21.52           C  
ANISOU 2486  CB  LYS A 156     3337   1787   3053   1027  -1088    -78       C  
ATOM   2487  CG  LYS A 156      12.621   9.303   8.829  1.00 23.41           C  
ANISOU 2487  CG  LYS A 156     3400   1991   3505   1163  -1072      5       C  
ATOM   2488  CD  LYS A 156      12.117   7.909   8.348  1.00 23.99           C  
ANISOU 2488  CD  LYS A 156     3549   1911   3657   1221   -879    -38       C  
ATOM   2489  CE  LYS A 156      13.278   6.939   8.228  1.00 31.53           C  
ANISOU 2489  CE  LYS A 156     4352   2787   4840   1378   -810     91       C  
ATOM   2490  NZ  LYS A 156      12.997   5.623   7.523  1.00 29.46           N  
ANISOU 2490  NZ  LYS A 156     4182   2337   4676   1446   -565     32       N  
ATOM   2491  H   LYS A 156      12.804  11.893   7.884  1.00 24.83           H  
ATOM   2492  HA  LYS A 156      11.049  12.133   9.763  1.00 25.35           H  
ATOM   2493  HB2 LYS A 156      10.970   9.816   9.857  1.00 25.82           H  
ATOM   2494  HB3 LYS A 156      10.943  10.306   8.353  1.00 25.82           H  
ATOM   2495  HG2 LYS A 156      13.158   9.691   8.121  1.00 28.09           H  
ATOM   2496  HG3 LYS A 156      13.160   9.171   9.624  1.00 28.09           H  
ATOM   2497  HD2 LYS A 156      11.485   7.554   8.991  1.00 28.79           H  
ATOM   2498  HD3 LYS A 156      11.701   7.999   7.476  1.00 28.79           H  
ATOM   2499  HE2 LYS A 156      13.991   7.380   7.740  1.00 37.83           H  
ATOM   2500  HE3 LYS A 156      13.587   6.726   9.122  1.00 37.83           H  
ATOM   2501  HZ1 LYS A 156      13.735   5.126   7.503  1.00 35.36           H  
ATOM   2502  HZ2 LYS A 156      12.359   5.178   7.955  1.00 35.36           H  
ATOM   2503  HZ3 LYS A 156      12.729   5.777   6.689  1.00 35.36           H  
ATOM   2504  N   GLN A 157      13.930  11.445  10.949  1.00 24.89           N  
ANISOU 2504  N   GLN A 157     3596   2424   3435    903  -1594    264       N  
ATOM   2505  CA  GLN A 157      14.645  11.159  12.196  1.00 27.42           C  
ANISOU 2505  CA  GLN A 157     3942   2764   3711    804  -1804    477       C  
ATOM   2506  C   GLN A 157      14.682  12.420  13.075  1.00 27.70           C  
ANISOU 2506  C   GLN A 157     4175   2880   3471    553  -1962    489       C  
ATOM   2507  O   GLN A 157      14.968  12.349  14.282  1.00 29.84           O  
ANISOU 2507  O   GLN A 157     4597   3142   3597    394  -2124    626       O  
ATOM   2508  CB  GLN A 157      16.036  10.571  11.896  1.00 29.81           C  
ANISOU 2508  CB  GLN A 157     3899   3125   4301    916  -1837    652       C  
ATOM   2509  CG  GLN A 157      16.481   9.380  12.805  1.00 35.37           C  
ANISOU 2509  CG  GLN A 157     4585   3765   5087    961  -1933    876       C  
ATOM   2510  CD  GLN A 157      15.582   8.114  12.743  1.00 38.96           C  
ANISOU 2510  CD  GLN A 157     5183   4040   5579   1098  -1762    825       C  
ATOM   2511  OE1 GLN A 157      14.855   7.884  11.766  1.00 30.15           O  
ANISOU 2511  OE1 GLN A 157     4106   2842   4508   1194  -1535    635       O  
ATOM   2512  NE2 GLN A 157      15.642   7.291  13.804  1.00 34.25           N  
ANISOU 2512  NE2 GLN A 157     4682   3383   4949   1077  -1876    997       N  
ATOM   2513  H   GLN A 157      14.430  11.517  10.253  1.00 29.86           H  
ATOM   2514  HA  GLN A 157      14.147  10.484  12.684  1.00 32.90           H  
ATOM   2515  HB2 GLN A 157      16.042  10.255  10.979  1.00 35.77           H  
ATOM   2516  HB3 GLN A 157      16.694  11.276  11.999  1.00 35.77           H  
ATOM   2517  HG2 GLN A 157      17.376   9.113  12.544  1.00 42.44           H  
ATOM   2518  HG3 GLN A 157      16.490   9.684  13.726  1.00 42.44           H  
ATOM   2519 HE21 GLN A 157      16.158   7.479  14.466  1.00 41.10           H  
ATOM   2520 HE22 GLN A 157      15.165   6.576  13.820  1.00 41.10           H  
ATOM   2521  N   LYS A 158      14.359  13.566  12.471  1.00 25.84           N  
ANISOU 2521  N   LYS A 158     3969   2702   3146    502  -1886    335       N  
ATOM   2522  CA  LYS A 158      14.257  14.842  13.197  1.00 32.05           C  
ANISOU 2522  CA  LYS A 158     4999   3524   3655    256  -1939    302       C  
ATOM   2523  C   LYS A 158      12.805  15.288  13.270  1.00 24.24           C  
ANISOU 2523  C   LYS A 158     4315   2429   2465    231  -1709    142       C  
ATOM   2524  O   LYS A 158      12.499  16.370  13.777  1.00 24.39           O  
ANISOU 2524  O   LYS A 158     4591   2424   2251     55  -1653     83       O  
ATOM   2525  CB  LYS A 158      15.092  15.936  12.515  1.00 25.92           C  
ANISOU 2525  CB  LYS A 158     4009   2891   2948    190  -1959    268       C  
ATOM   2526  CG  LYS A 158      16.570  15.857  12.886  1.00 38.55           C  
ANISOU 2526  CG  LYS A 158     5375   4597   4677    110  -2161    469       C  
ATOM   2527  CD  LYS A 158      17.384  17.023  12.348  1.00 43.26           C  
ANISOU 2527  CD  LYS A 158     5802   5324   5313     12  -2178    451       C  
ATOM   2528  CE  LYS A 158      18.882  16.809  12.585  1.00 43.69           C  
ANISOU 2528  CE  LYS A 158     5568   5478   5555    -28  -2368    678       C  
ATOM   2529  H   LYS A 158      14.191  13.635  11.631  1.00 31.00           H  
ATOM   2530  HA  LYS A 158      14.587  14.725  14.101  1.00 38.46           H  
ATOM   2531  HB2 LYS A 158      15.018  15.838  11.552  1.00 31.10           H  
ATOM   2532  HB3 LYS A 158      14.759  16.805  12.787  1.00 31.10           H  
ATOM   2533  HG2 LYS A 158      16.652  15.857  13.853  1.00 46.26           H  
ATOM   2534  HG3 LYS A 158      16.943  15.039  12.522  1.00 46.26           H  
ATOM   2535  HD2 LYS A 158      17.235  17.105  11.393  1.00 51.92           H  
ATOM   2536  HD3 LYS A 158      17.117  17.838  12.802  1.00 51.92           H  
ATOM   2537  HE2 LYS A 158      19.086  17.001  13.514  1.00 52.43           H  
ATOM   2538  HE3 LYS A 158      19.106  15.887  12.381  1.00 52.43           H  
ATOM   2539  N   ASN A 159      11.915  14.445  12.752  1.00 22.86           N  
ANISOU 2539  N   ASN A 159     4088   2179   2419    392  -1507     76       N  
ATOM   2540  CA  ASN A 159      10.483  14.723  12.752  1.00 21.48           C  
ANISOU 2540  CA  ASN A 159     4093   1908   2160    379  -1227    -32       C  
ATOM   2541  C   ASN A 159      10.153  16.042  12.025  1.00 20.02           C  
ANISOU 2541  C   ASN A 159     3855   1785   1967    337  -1065   -151       C  
ATOM   2542  O   ASN A 159       9.259  16.784  12.434  1.00 20.02           O  
ANISOU 2542  O   ASN A 159     4065   1698   1845    263   -864   -189       O  
ATOM   2543  CB  ASN A 159       9.919  14.743  14.178  1.00 28.13           C  
ANISOU 2543  CB  ASN A 159     5330   2611   2748    244  -1193     27       C  
ATOM   2544  CG  ASN A 159       8.435  14.367  14.231  1.00 22.17           C  
ANISOU 2544  CG  ASN A 159     4681   1720   2022    301   -896    -11       C  
ATOM   2545  OD1 ASN A 159       7.976  13.504  13.485  1.00 23.25           O  
ANISOU 2545  OD1 ASN A 159     4621   1852   2361    432   -836    -23       O  
ATOM   2546  ND2 ASN A 159       7.688  15.005  15.136  1.00 27.36           N  
ANISOU 2546  ND2 ASN A 159     5670   2246   2479    187   -695    -16       N  
ATOM   2547  H   ASN A 159      12.120  13.693  12.390  1.00 27.43           H  
ATOM   2548  HA  ASN A 159      10.034  14.009  12.274  1.00 25.78           H  
ATOM   2549  HB2 ASN A 159      10.410  14.107  14.721  1.00 33.76           H  
ATOM   2550  HB3 ASN A 159      10.016  15.637  14.544  1.00 33.76           H  
ATOM   2551 HD21 ASN A 159       8.046  15.593  15.652  1.00 32.83           H  
ATOM   2552 HD22 ASN A 159       6.849  14.828  15.204  1.00 32.83           H  
ATOM   2553  N   GLY A 160      10.879  16.308  10.939  1.00 20.39           N  
ANISOU 2553  N   GLY A 160     3623   1961   2162    397  -1124   -194       N  
ATOM   2554  CA  GLY A 160      10.732  17.558  10.226  1.00 20.30           C  
ANISOU 2554  CA  GLY A 160     3551   2017   2145    352  -1007   -285       C  
ATOM   2555  C   GLY A 160      10.942  17.373   8.738  1.00 16.84           C  
ANISOU 2555  C   GLY A 160     2819   1675   1905    464   -969   -349       C  
ATOM   2556  O   GLY A 160      10.723  16.286   8.203  1.00 21.45           O  
ANISOU 2556  O   GLY A 160     3310   2229   2613    571   -942   -355       O  
ATOM   2557  H   GLY A 160      11.462  15.775  10.600  1.00 24.46           H  
ATOM   2558  HA2 GLY A 160       9.842  17.915  10.372  1.00 24.36           H  
ATOM   2559  HA3 GLY A 160      11.382  18.199  10.554  1.00 24.36           H  
ATOM   2560  N   ILE A 161      11.396  18.438   8.089  1.00 17.26           N  
ANISOU 2560  N   ILE A 161     2769   1825   1964    419   -957   -399       N  
ATOM   2561  CA  ILE A 161      11.602  18.449   6.633  1.00 18.85           C  
ANISOU 2561  CA  ILE A 161     2745   2111   2307    492   -895   -467       C  
ATOM   2562  C   ILE A 161      12.911  19.154   6.292  1.00 17.99           C  
ANISOU 2562  C   ILE A 161     2483   2118   2234    457   -993   -464       C  
ATOM   2563  O   ILE A 161      13.460  19.921   7.101  1.00 19.54           O  
ANISOU 2563  O   ILE A 161     2759   2339   2327    337  -1109   -418       O  
ATOM   2564  CB  ILE A 161      10.450  19.189   5.882  1.00 14.08           C  
ANISOU 2564  CB  ILE A 161     2151   1501   1697    462   -722   -517       C  
ATOM   2565  CG1 ILE A 161      10.292  20.622   6.420  1.00 14.29           C  
ANISOU 2565  CG1 ILE A 161     2301   1517   1613    359   -658   -512       C  
ATOM   2566  CG2 ILE A 161       9.179  18.410   6.007  1.00 15.66           C  
ANISOU 2566  CG2 ILE A 161     2422   1601   1928    491   -635   -485       C  
ATOM   2567  CD1 ILE A 161       9.271  21.450   5.670  1.00 14.84           C  
ANISOU 2567  CD1 ILE A 161     2331   1574   1733    351   -487   -510       C  
ATOM   2568  H   ILE A 161      11.598  19.182   8.471  1.00 20.71           H  
ATOM   2569  HA  ILE A 161      11.648  17.537   6.305  1.00 22.62           H  
ATOM   2570  HB  ILE A 161      10.684  19.242   4.942  1.00 16.89           H  
ATOM   2571 HG12 ILE A 161      10.013  20.578   7.348  1.00 17.15           H  
ATOM   2572 HG13 ILE A 161      11.147  21.076   6.355  1.00 17.15           H  
ATOM   2573 HG21 ILE A 161       8.473  18.881   5.537  1.00 18.79           H  
ATOM   2574 HG22 ILE A 161       9.308  17.531   5.617  1.00 18.79           H  
ATOM   2575 HG23 ILE A 161       8.952  18.325   6.946  1.00 18.79           H  
ATOM   2576 HD11 ILE A 161       9.229  22.334   6.066  1.00 17.80           H  
ATOM   2577 HD12 ILE A 161       9.540  21.515   4.741  1.00 17.80           H  
ATOM   2578 HD13 ILE A 161       8.405  21.017   5.735  1.00 17.80           H  
ATOM   2579  N   LYS A 162      13.406  18.847   5.099  1.00 15.87           N  
ANISOU 2579  N   LYS A 162     2021   1905   2105    542   -937   -507       N  
ATOM   2580  CA  LYS A 162      14.515  19.520   4.481  1.00 16.41           C  
ANISOU 2580  CA  LYS A 162     1908   2079   2249    525   -959   -508       C  
ATOM   2581  C   LYS A 162      13.977  20.114   3.186  1.00 15.12           C  
ANISOU 2581  C   LYS A 162     1727   1951   2069    511   -795   -613       C  
ATOM   2582  O   LYS A 162      13.178  19.499   2.473  1.00 14.50           O  
ANISOU 2582  O   LYS A 162     1696   1821   1992    551   -693   -667       O  
ATOM   2583  CB  LYS A 162      15.678  18.559   4.183  1.00 18.07           C  
ANISOU 2583  CB  LYS A 162     1907   2293   2667    654   -985   -439       C  
ATOM   2584  CG  LYS A 162      16.609  18.319   5.397  1.00 23.15           C  
ANISOU 2584  CG  LYS A 162     2476   2950   3370    630  -1222   -260       C  
ATOM   2585  CD  LYS A 162      17.831  17.445   5.032  1.00 29.67           C  
ANISOU 2585  CD  LYS A 162     3012   3770   4492    789  -1216   -133       C  
ATOM   2586  CE  LYS A 162      18.828  17.360   6.191  1.00 40.16           C  
ANISOU 2586  CE  LYS A 162     4235   5145   5878    704  -1458    111       C  
ATOM   2587  H   LYS A 162      13.088  18.215   4.610  1.00 19.05           H  
ATOM   2588  HA  LYS A 162      14.832  20.236   5.053  1.00 19.70           H  
ATOM   2589  HB2 LYS A 162      15.314  17.701   3.913  1.00 21.69           H  
ATOM   2590  HB3 LYS A 162      16.215  18.929   3.465  1.00 21.69           H  
ATOM   2591  HG2 LYS A 162      16.934  19.173   5.721  1.00 27.78           H  
ATOM   2592  HG3 LYS A 162      16.111  17.865   6.095  1.00 27.78           H  
ATOM   2593  HD2 LYS A 162      17.531  16.546   4.823  1.00 35.61           H  
ATOM   2594  HD3 LYS A 162      18.286  17.833   4.268  1.00 35.61           H  
ATOM   2595  N   VAL A 163      14.436  21.316   2.893  1.00 15.08           N  
ANISOU 2595  N   VAL A 163     1667   2029   2036    426   -794   -625       N  
ATOM   2596  CA  VAL A 163      13.912  22.110   1.791  1.00 15.81           C  
ANISOU 2596  CA  VAL A 163     1762   2157   2090    384   -667   -692       C  
ATOM   2597  C   VAL A 163      15.110  22.700   1.035  1.00 18.80           C  
ANISOU 2597  C   VAL A 163     1973   2631   2540    365   -643   -704       C  
ATOM   2598  O   VAL A 163      16.119  23.079   1.647  1.00 17.05           O  
ANISOU 2598  O   VAL A 163     1657   2457   2364    322   -754   -640       O  
ATOM   2599  CB  VAL A 163      13.022  23.242   2.370  1.00 13.41           C  
ANISOU 2599  CB  VAL A 163     1605   1819   1671    287   -644   -674       C  
ATOM   2600  CG1 VAL A 163      12.533  24.169   1.290  1.00 13.30           C  
ANISOU 2600  CG1 VAL A 163     1565   1841   1648    244   -536   -694       C  
ATOM   2601  CG2 VAL A 163      11.845  22.629   3.196  1.00 16.39           C  
ANISOU 2601  CG2 VAL A 163     2132   2084   2011    315   -622   -639       C  
ATOM   2602  H   VAL A 163      15.067  21.706   3.328  1.00 18.10           H  
ATOM   2603  HA  VAL A 163      13.387  21.558   1.190  1.00 18.98           H  
ATOM   2604  HB  VAL A 163      13.559  23.770   2.982  1.00 16.09           H  
ATOM   2605 HG11 VAL A 163      11.983  24.859   1.691  1.00 15.96           H  
ATOM   2606 HG12 VAL A 163      13.298  24.570   0.849  1.00 15.96           H  
ATOM   2607 HG13 VAL A 163      12.011  23.660   0.650  1.00 15.96           H  
ATOM   2608 HG21 VAL A 163      11.300  23.349   3.550  1.00 19.67           H  
ATOM   2609 HG22 VAL A 163      11.312  22.066   2.614  1.00 19.67           H  
ATOM   2610 HG23 VAL A 163      12.211  22.102   3.923  1.00 19.67           H  
ATOM   2611  N   ASN A 164      15.042  22.740  -0.294  1.00 18.86           N  
ANISOU 2611  N   ASN A 164     1950   2661   2556    377   -509   -768       N  
ATOM   2612  CA  ASN A 164      16.097  23.372  -1.065  1.00 16.51           C  
ANISOU 2612  CA  ASN A 164     1513   2440   2321    354   -440   -778       C  
ATOM   2613  C   ASN A 164      15.508  24.057  -2.275  1.00 14.67           C  
ANISOU 2613  C   ASN A 164     1357   2231   1986    281   -328   -835       C  
ATOM   2614  O   ASN A 164      14.504  23.588  -2.824  1.00 14.13           O  
ANISOU 2614  O   ASN A 164     1415   2116   1838    269   -295   -864       O  
ATOM   2615  CB  ASN A 164      17.182  22.363  -1.494  1.00 17.11           C  
ANISOU 2615  CB  ASN A 164     1438   2493   2570    479   -343   -769       C  
ATOM   2616  CG  ASN A 164      16.697  21.363  -2.560  1.00 21.66           C  
ANISOU 2616  CG  ASN A 164     2147   2976   3108    538   -161   -865       C  
ATOM   2617  OD1 ASN A 164      16.042  20.362  -2.244  1.00 28.33           O  
ANISOU 2617  OD1 ASN A 164     3104   3730   3930    588   -184   -879       O  
ATOM   2618  ND2 ASN A 164      17.072  21.606  -3.811  1.00 22.96           N  
ANISOU 2618  ND2 ASN A 164     2329   3145   3251    513     25   -930       N  
ATOM   2619  H   ASN A 164      14.401  22.412  -0.765  1.00 22.63           H  
ATOM   2620  HA  ASN A 164      16.522  24.050  -0.517  1.00 19.81           H  
ATOM   2621  HB2 ASN A 164      17.936  22.849  -1.863  1.00 20.53           H  
ATOM   2622  HB3 ASN A 164      17.464  21.856  -0.717  1.00 20.53           H  
ATOM   2623 HD21 ASN A 164      17.560  22.292  -3.989  1.00 27.55           H  
ATOM   2624 HD22 ASN A 164      16.828  21.077  -4.444  1.00 27.55           H  
ATOM   2625  N   PHE A 165      16.122  25.166  -2.671  1.00 17.88           N  
ANISOU 2625  N   PHE A 165     1690   2710   2395    207   -295   -828       N  
ATOM   2626  CA  PHE A 165      15.720  25.882  -3.878  1.00 16.10           C  
ANISOU 2626  CA  PHE A 165     1530   2511   2074    128   -197   -858       C  
ATOM   2627  C   PHE A 165      16.706  26.962  -4.231  1.00 19.55           C  
ANISOU 2627  C   PHE A 165     1858   3021   2549     63   -146   -847       C  
ATOM   2628  O   PHE A 165      17.492  27.379  -3.395  1.00 17.36           O  
ANISOU 2628  O   PHE A 165     1468   2776   2352     41   -229   -802       O  
ATOM   2629  CB  PHE A 165      14.325  26.499  -3.751  1.00 14.76           C  
ANISOU 2629  CB  PHE A 165     1484   2315   1810     64   -252   -810       C  
ATOM   2630  CG  PHE A 165      14.159  27.441  -2.564  1.00 12.95           C  
ANISOU 2630  CG  PHE A 165     1273   2062   1586     33   -313   -759       C  
ATOM   2631  CD1 PHE A 165      13.940  26.949  -1.301  1.00 12.81           C  
ANISOU 2631  CD1 PHE A 165     1304   1984   1578     73   -388   -743       C  
ATOM   2632  CD2 PHE A 165      14.207  28.815  -2.745  1.00 18.49           C  
ANISOU 2632  CD2 PHE A 165     1989   2776   2261    -52   -272   -729       C  
ATOM   2633  CE1 PHE A 165      13.768  27.817  -0.221  1.00 16.33           C  
ANISOU 2633  CE1 PHE A 165     1855   2370   1979     13   -406   -712       C  
ATOM   2634  CE2 PHE A 165      14.011  29.676  -1.697  1.00 18.56           C  
ANISOU 2634  CE2 PHE A 165     2089   2715   2247    -98   -279   -699       C  
ATOM   2635  CZ  PHE A 165      13.823  29.181  -0.422  1.00 13.66           C  
ANISOU 2635  CZ  PHE A 165     1557   2024   1608    -76   -340   -698       C  
ATOM   2636  H   PHE A 165      16.781  25.529  -2.254  1.00 21.46           H  
ATOM   2637  HA  PHE A 165      15.697  25.253  -4.616  1.00 19.32           H  
ATOM   2638  HB2 PHE A 165      14.134  27.004  -4.557  1.00 17.71           H  
ATOM   2639  HB3 PHE A 165      13.676  25.784  -3.652  1.00 17.71           H  
ATOM   2640  HD1 PHE A 165      13.908  26.030  -1.163  1.00 15.37           H  
ATOM   2641  HD2 PHE A 165      14.337  29.158  -3.600  1.00 22.19           H  
ATOM   2642  HE1 PHE A 165      13.628  27.477   0.633  1.00 19.59           H  
ATOM   2643  HE2 PHE A 165      14.059  30.594  -1.835  1.00 22.27           H  
ATOM   2644  HZ  PHE A 165      13.705  29.764   0.293  1.00 16.39           H  
ATOM   2645  N   LYS A 166      16.667  27.404  -5.487  1.00 15.63           N  
ANISOU 2645  N   LYS A 166     1412   2548   1980      3    -25   -874       N  
ATOM   2646  CA  LYS A 166      17.541  28.473  -5.934  1.00 16.38           C  
ANISOU 2646  CA  LYS A 166     1415   2705   2103    -71     45   -860       C  
ATOM   2647  C   LYS A 166      16.648  29.650  -6.283  1.00 21.34           C  
ANISOU 2647  C   LYS A 166     2160   3337   2610   -177     19   -821       C  
ATOM   2648  O   LYS A 166      15.638  29.474  -6.944  1.00 25.48           O  
ANISOU 2648  O   LYS A 166     2812   3837   3031   -204     16   -805       O  
ATOM   2649  CB  LYS A 166      18.305  28.066  -7.222  1.00 21.52           C  
ANISOU 2649  CB  LYS A 166     2054   3357   2765    -56    263   -913       C  
ATOM   2650  CG  LYS A 166      18.852  26.656  -7.248  1.00 28.18           C  
ANISOU 2650  CG  LYS A 166     2852   4135   3722     81    380   -952       C  
ATOM   2651  H   LYS A 166      16.142  27.099  -6.096  1.00 18.76           H  
ATOM   2652  HA  LYS A 166      18.169  28.726  -5.239  1.00 19.66           H  
ATOM   2653  HB2 LYS A 166      17.701  28.157  -7.976  1.00 25.82           H  
ATOM   2654  HB3 LYS A 166      19.055  28.670  -7.335  1.00 25.82           H  
ATOM   2655  N   THR A 167      17.037  30.852  -5.907  1.00 20.23           N  
ANISOU 2655  N   THR A 167     1976   3218   2492   -253     -1   -784       N  
ATOM   2656  CA  THR A 167      16.329  32.032  -6.357  1.00 15.73           C  
ANISOU 2656  CA  THR A 167     1503   2628   1844   -337     22   -728       C  
ATOM   2657  C   THR A 167      17.194  32.794  -7.361  1.00 21.55           C  
ANISOU 2657  C   THR A 167     2197   3421   2569   -423    135   -732       C  
ATOM   2658  O   THR A 167      18.425  32.683  -7.354  1.00 19.14           O  
ANISOU 2658  O   THR A 167     1754   3165   2355   -428    187   -763       O  
ATOM   2659  CB  THR A 167      15.956  32.953  -5.174  1.00 16.75           C  
ANISOU 2659  CB  THR A 167     1694   2684   1986   -372    -33   -685       C  
ATOM   2660  OG1 THR A 167      17.138  33.347  -4.473  1.00 16.28           O  
ANISOU 2660  OG1 THR A 167     1565   2650   1972   -445    -77   -711       O  
ATOM   2661  CG2 THR A 167      15.030  32.243  -4.190  1.00 13.95           C  
ANISOU 2661  CG2 THR A 167     1409   2253   1636   -290   -100   -672       C  
ATOM   2662  H   THR A 167      17.707  31.013  -5.392  1.00 24.27           H  
ATOM   2663  HA  THR A 167      15.510  31.764  -6.802  1.00 18.87           H  
ATOM   2664  HB  THR A 167      15.501  33.742  -5.509  1.00 20.10           H  
ATOM   2665  HG1 THR A 167      17.654  33.761  -4.991  1.00 19.54           H  
ATOM   2666 HG21 THR A 167      14.808  32.837  -3.456  1.00 16.74           H  
ATOM   2667 HG22 THR A 167      14.213  31.976  -4.639  1.00 16.74           H  
ATOM   2668 HG23 THR A 167      15.468  31.453  -3.836  1.00 16.74           H  
ATOM   2669  N   ARG A 168      16.520  33.564  -8.215  1.00 17.54           N  
ANISOU 2669  N   ARG A 168     1790   2902   1972   -491    172   -669       N  
ATOM   2670  CA  ARG A 168      17.142  34.323  -9.301  1.00 21.59           C  
ANISOU 2670  CA  ARG A 168     2310   3455   2437   -587    288   -659       C  
ATOM   2671  C   ARG A 168      16.812  35.794  -9.118  1.00 17.23           C  
ANISOU 2671  C   ARG A 168     1799   2857   1890   -661    282   -569       C  
ATOM   2672  O   ARG A 168      15.649  36.168  -9.155  1.00 19.48           O  
ANISOU 2672  O   ARG A 168     2166   3082   2154   -652    237   -464       O  
ATOM   2673  CB  ARG A 168      16.598  33.831 -10.662  1.00 21.04           C  
ANISOU 2673  CB  ARG A 168     2384   3397   2213   -633    329   -644       C  
ATOM   2674  CG  ARG A 168      16.778  32.329 -10.885  1.00 27.96           C  
ANISOU 2674  CG  ARG A 168     3299   4267   3057   -570    374   -745       C  
ATOM   2675  CD  ARG A 168      16.142  31.813 -12.189  1.00 30.82           C  
ANISOU 2675  CD  ARG A 168     3895   4612   3202   -677    392   -739       C  
ATOM   2676  NE  ARG A 168      14.749  32.241 -12.389  1.00 41.54           N  
ANISOU 2676  NE  ARG A 168     5336   5966   4481   -763    197   -583       N  
ATOM   2677  CZ  ARG A 168      13.670  31.604 -11.913  1.00 39.82           C  
ANISOU 2677  CZ  ARG A 168     5125   5722   4284   -736     34   -520       C  
ATOM   2678  NH1 ARG A 168      13.791  30.476 -11.207  1.00 37.97           N  
ANISOU 2678  NH1 ARG A 168     4861   5458   4110   -629     38   -626       N  
ATOM   2679  NH2 ARG A 168      12.458  32.091 -12.171  1.00 34.43           N  
ANISOU 2679  NH2 ARG A 168     4461   5035   3585   -817   -130   -323       N  
ATOM   2680  H   ARG A 168      15.666  33.665  -8.184  1.00 21.05           H  
ATOM   2681  HA  ARG A 168      18.105  34.207  -9.282  1.00 25.91           H  
ATOM   2682  HB2 ARG A 168      15.650  34.027 -10.710  1.00 25.25           H  
ATOM   2683  HB3 ARG A 168      17.067  34.295 -11.374  1.00 25.25           H  
ATOM   2684  HG2 ARG A 168      17.726  32.129 -10.919  1.00 33.55           H  
ATOM   2685  HG3 ARG A 168      16.368  31.852 -10.146  1.00 33.55           H  
ATOM   2686  HD2 ARG A 168      16.662  32.139 -12.939  1.00 36.98           H  
ATOM   2687  HD3 ARG A 168      16.154  30.843 -12.178  1.00 36.98           H  
ATOM   2688  HE  ARG A 168      14.616  32.957 -12.847  1.00 49.85           H  
ATOM   2689 HH11 ARG A 168      14.571  30.155 -11.040  1.00 45.57           H  
ATOM   2690 HH12 ARG A 168      13.089  30.077 -10.910  1.00 45.57           H  
ATOM   2691 HH21 ARG A 168      12.374  32.815 -12.627  1.00 41.31           H  
ATOM   2692 HH22 ARG A 168      11.760  31.688 -11.872  1.00 41.31           H  
ATOM   2693  N   HIS A 169      17.828  36.619  -8.895  1.00 19.45           N  
ANISOU 2693  N   HIS A 169     2014   3150   2225   -737    334   -588       N  
ATOM   2694  CA  HIS A 169      17.632  38.052  -8.631  1.00 18.21           C  
ANISOU 2694  CA  HIS A 169     1933   2915   2072   -822    357   -520       C  
ATOM   2695  C   HIS A 169      18.224  38.876  -9.766  1.00 20.79           C  
ANISOU 2695  C   HIS A 169     2261   3278   2361   -928    470   -486       C  
ATOM   2696  O   HIS A 169      19.429  38.843  -9.995  1.00 26.81           O  
ANISOU 2696  O   HIS A 169     2909   4111   3168   -987    534   -537       O  
ATOM   2697  CB  HIS A 169      18.276  38.469  -7.303  1.00 18.52           C  
ANISOU 2697  CB  HIS A 169     1960   2907   2169   -885    300   -565       C  
ATOM   2698  CG  HIS A 169      17.837  37.625  -6.152  1.00 20.81           C  
ANISOU 2698  CG  HIS A 169     2275   3160   2472   -802    194   -601       C  
ATOM   2699  ND1 HIS A 169      16.619  37.800  -5.534  1.00 20.54           N  
ANISOU 2699  ND1 HIS A 169     2390   2996   2417   -738    207   -560       N  
ATOM   2700  CD2 HIS A 169      18.429  36.574  -5.534  1.00 23.63           C  
ANISOU 2700  CD2 HIS A 169     2521   3581   2876   -764     91   -653       C  
ATOM   2701  CE1 HIS A 169      16.478  36.893  -4.582  1.00 21.07           C  
ANISOU 2701  CE1 HIS A 169     2464   3054   2488   -678    118   -605       C  
ATOM   2702  NE2 HIS A 169      17.564  36.136  -4.562  1.00 22.15           N  
ANISOU 2702  NE2 HIS A 169     2446   3310   2659   -695     28   -659       N  
ATOM   2703  H   HIS A 169      18.653  36.377  -8.891  1.00 23.34           H  
ATOM   2704  HA  HIS A 169      16.682  38.242  -8.581  1.00 21.86           H  
ATOM   2705  HB2 HIS A 169      19.239  38.391  -7.381  1.00 22.22           H  
ATOM   2706  HB3 HIS A 169      18.032  39.388  -7.110  1.00 22.22           H  
ATOM   2707  HD1 HIS A 169      16.037  38.398  -5.742  1.00 24.65           H  
ATOM   2708  HD2 HIS A 169      19.261  36.212  -5.737  1.00 28.35           H  
ATOM   2709  HE1 HIS A 169      15.746  36.809  -4.014  1.00 25.29           H  
ATOM   2710  HE2 HIS A 169      17.710  35.485  -4.018  1.00 26.58           H  
ATOM   2711  N   ASN A 170      17.362  39.616 -10.456  1.00 23.54           N  
ANISOU 2711  N   ASN A 170     2722   3572   2651   -952    498   -370       N  
ATOM   2712  CA  ASN A 170      17.800  40.466 -11.558  1.00 23.89           C  
ANISOU 2712  CA  ASN A 170     2804   3636   2635  -1063    602   -316       C  
ATOM   2713  C   ASN A 170      18.814  41.469 -11.074  1.00 26.40           C  
ANISOU 2713  C   ASN A 170     3082   3925   3025  -1167    668   -349       C  
ATOM   2714  O   ASN A 170      18.625  42.085 -10.031  1.00 24.43           O  
ANISOU 2714  O   ASN A 170     2884   3569   2829  -1182    638   -347       O  
ATOM   2715  CB  ASN A 170      16.614  41.199 -12.174  1.00 33.06           C  
ANISOU 2715  CB  ASN A 170     4080   4724   3757  -1071    581   -132       C  
ATOM   2716  CG  ASN A 170      15.784  40.304 -13.066  1.00 33.14           C  
ANISOU 2716  CG  ASN A 170     4144   4792   3654  -1060    484    -59       C  
ATOM   2717  OD1 ASN A 170      15.908  39.076 -13.019  1.00 29.64           O  
ANISOU 2717  OD1 ASN A 170     3684   4413   3166  -1019    446   -170       O  
ATOM   2718  ND2 ASN A 170      14.941  40.910 -13.893  1.00 37.25           N  
ANISOU 2718  ND2 ASN A 170     4742   5283   4128  -1117    431    146       N  
ATOM   2719  H   ASN A 170      16.516  39.644 -10.306  1.00 28.25           H  
ATOM   2720  HA  ASN A 170      18.212  39.918 -12.244  1.00 28.66           H  
ATOM   2721  HB2 ASN A 170      16.043  41.531 -11.464  1.00 39.67           H  
ATOM   2722  HB3 ASN A 170      16.942  41.938 -12.711  1.00 39.67           H  
ATOM   2723 HD21 ASN A 170      14.889  41.769 -13.901  1.00 44.70           H  
ATOM   2724 HD22 ASN A 170      14.446  40.445 -14.420  1.00 44.70           H  
ATOM   2725  N   ILE A 171      19.898  41.604 -11.834  1.00 28.94           N  
ANISOU 2725  N   ILE A 171     3872   4811   2312  -1474   1250   -428       N  
ATOM   2726  CA  ILE A 171      20.938  42.582 -11.558  1.00 30.46           C  
ANISOU 2726  CA  ILE A 171     4029   4997   2548  -1641   1350   -445       C  
ATOM   2727  C   ILE A 171      20.766  43.725 -12.535  1.00 37.37           C  
ANISOU 2727  C   ILE A 171     5028   5789   3381  -1654   1468   -301       C  
ATOM   2728  O   ILE A 171      20.389  43.515 -13.693  1.00 38.00           O  
ANISOU 2728  O   ILE A 171     5154   5915   3368  -1545   1492   -223       O  
ATOM   2729  CB  ILE A 171      22.318  41.950 -11.713  1.00 31.56           C  
ANISOU 2729  CB  ILE A 171     3980   5334   2680  -1693   1379   -580       C  
ATOM   2730  CG1 ILE A 171      22.452  40.799 -10.726  1.00 34.78           C  
ANISOU 2730  CG1 ILE A 171     4254   5831   3131  -1656   1257   -715       C  
ATOM   2731  CG2 ILE A 171      23.424  42.976 -11.508  1.00 35.16           C  
ANISOU 2731  CG2 ILE A 171     4395   5786   3179  -1861   1488   -610       C  
ATOM   2732  CD1 ILE A 171      23.508  39.813 -11.098  1.00 43.98           C  
ANISOU 2732  CD1 ILE A 171     5230   7205   4277  -1630   1248   -844       C  
ATOM   2733  H   ILE A 171      20.055  41.127 -12.532  1.00 34.73           H  
ATOM   2734  HA  ILE A 171      20.845  42.921 -10.654  1.00 36.56           H  
ATOM   2735  HB  ILE A 171      22.393  41.594 -12.612  1.00 37.88           H  
ATOM   2736 HG12 ILE A 171      22.676  41.160  -9.854  1.00 41.74           H  
ATOM   2737 HG13 ILE A 171      21.607  40.326 -10.680  1.00 41.74           H  
ATOM   2738 HG21 ILE A 171      24.283  42.539 -11.614  1.00 42.19           H  
ATOM   2739 HG22 ILE A 171      23.327  43.681 -12.167  1.00 42.19           H  
ATOM   2740 HG23 ILE A 171      23.349  43.346 -10.614  1.00 42.19           H  
ATOM   2741 HD11 ILE A 171      23.535  39.113 -10.427  1.00 52.78           H  
ATOM   2742 HD12 ILE A 171      23.294  39.434 -11.964  1.00 52.78           H  
ATOM   2743 HD13 ILE A 171      24.364  40.268 -11.138  1.00 52.78           H  
ATOM   2744  N   GLU A 172      21.050  44.935 -12.060  1.00 35.72           N  
ANISOU 2744  N   GLU A 172     4868   5464   3241  -1778   1540   -267       N  
ATOM   2745  CA  GLU A 172      20.784  46.159 -12.812  1.00 35.27           C  
ANISOU 2745  CA  GLU A 172     4937   5296   3167  -1789   1649   -115       C  
ATOM   2746  C   GLU A 172      21.324  46.137 -14.249  1.00 41.80           C  
ANISOU 2746  C   GLU A 172     5746   6246   3889  -1757   1757    -54       C  
ATOM   2747  O   GLU A 172      20.802  46.833 -15.117  1.00 40.59           O  
ANISOU 2747  O   GLU A 172     5706   6036   3682  -1700   1824     99       O  
ATOM   2748  CB  GLU A 172      21.378  47.361 -12.060  1.00 37.85           C  
ANISOU 2748  CB  GLU A 172     5267   5514   3599  -1943   1724   -133       C  
ATOM   2749  H   GLU A 172      21.404  45.076 -11.289  1.00 42.87           H  
ATOM   2750  HA  GLU A 172      19.824  46.288 -12.862  1.00 42.32           H  
ATOM   2751  N   ASP A 173      22.355  45.335 -14.501  1.00 42.04           N  
ANISOU 2751  N   ASP A 173     5630   6453   3889  -1786   1771   -174       N  
ATOM   2752  CA  ASP A 173      23.005  45.326 -15.804  1.00 45.82           C  
ANISOU 2752  CA  ASP A 173     6078   7057   4273  -1772   1880   -137       C  
ATOM   2753  C   ASP A 173      22.483  44.225 -16.712  1.00 44.14           C  
ANISOU 2753  C   ASP A 173     5856   6968   3949  -1602   1818   -132       C  
ATOM   2754  O   ASP A 173      22.985  44.055 -17.806  1.00 42.15           O  
ANISOU 2754  O   ASP A 173     5570   6838   3608  -1573   1894   -118       O  
ATOM   2755  CB  ASP A 173      24.526  45.186 -15.650  1.00 51.23           C  
ANISOU 2755  CB  ASP A 173     6601   7870   4994  -1908   1944   -282       C  
ATOM   2756  CG  ASP A 173      24.953  43.805 -15.154  1.00 54.58           C  
ANISOU 2756  CG  ASP A 173     6860   8447   5430  -1877   1826   -461       C  
ATOM   2757  OD1 ASP A 173      24.083  42.961 -14.831  1.00 47.20           O  
ANISOU 2757  OD1 ASP A 173     5938   7507   4489  -1759   1699   -474       O  
ATOM   2758  OD2 ASP A 173      26.180  43.570 -15.071  1.00 55.58           O  
ANISOU 2758  OD2 ASP A 173     6838   8701   5579  -1968   1861   -591       O  
ATOM   2759  H   ASP A 173      22.695  44.787 -13.932  1.00 50.44           H  
ATOM   2760  HA  ASP A 173      22.831  46.174 -16.242  1.00 54.98           H  
ATOM   2761  HB2 ASP A 173      24.944  45.337 -16.512  1.00 61.47           H  
ATOM   2762  HB3 ASP A 173      24.839  45.844 -15.010  1.00 61.47           H  
ATOM   2763  N   GLY A 174      21.504  43.460 -16.243  1.00 41.25           N  
ANISOU 2763  N   GLY A 174     5514   6570   3591  -1490   1680   -158       N  
ATOM   2764  CA  GLY A 174      20.903  42.408 -17.048  1.00 37.22           C  
ANISOU 2764  CA  GLY A 174     4996   6159   2988  -1316   1611   -169       C  
ATOM   2765  C   GLY A 174      21.309  40.982 -16.708  1.00 41.85           C  
ANISOU 2765  C   GLY A 174     5421   6878   3601  -1276   1508   -345       C  
ATOM   2766  O   GLY A 174      20.684  40.038 -17.185  1.00 40.76           O  
ANISOU 2766  O   GLY A 174     5276   6795   3417  -1125   1428   -374       O  
ATOM   2767  H   GLY A 174      21.167  43.533 -15.455  1.00 49.51           H  
ATOM   2768  HA2 GLY A 174      19.939  42.467 -16.963  1.00 44.66           H  
ATOM   2769  HA3 GLY A 174      21.128  42.564 -17.978  1.00 44.66           H  
ATOM   2770  N   SER A 175      22.341  40.806 -15.886  1.00 38.13           N  
ANISOU 2770  N   SER A 175     4815   6463   3211  -1399   1505   -468       N  
ATOM   2771  CA  SER A 175      22.720  39.474 -15.449  1.00 35.66           C  
ANISOU 2771  CA  SER A 175     4337   6273   2937  -1350   1400   -629       C  
ATOM   2772  C   SER A 175      21.800  39.055 -14.284  1.00 32.11           C  
ANISOU 2772  C   SER A 175     3923   5719   2559  -1296   1274   -645       C  
ATOM   2773  O   SER A 175      20.874  39.788 -13.917  1.00 31.23           O  
ANISOU 2773  O   SER A 175     3961   5445   2460  -1300   1267   -538       O  
ATOM   2774  CB  SER A 175      24.203  39.434 -15.053  1.00 42.97           C  
ANISOU 2774  CB  SER A 175     5094   7320   3913  -1484   1442   -758       C  
ATOM   2775  OG  SER A 175      24.536  40.461 -14.120  1.00 43.15           O  
ANISOU 2775  OG  SER A 175     5147   7243   4004  -1636   1488   -744       O  
ATOM   2776  H   SER A 175      22.831  41.439 -15.571  1.00 45.76           H  
ATOM   2777  HA  SER A 175      22.586  38.849 -16.180  1.00 42.79           H  
ATOM   2778  HB2 SER A 175      24.394  38.572 -14.650  1.00 51.57           H  
ATOM   2779  HB3 SER A 175      24.742  39.550 -15.851  1.00 51.57           H  
ATOM   2780  HG  SER A 175      24.080  40.373 -13.420  1.00 51.78           H  
ATOM   2781  N   VAL A 176      22.051  37.874 -13.726  1.00 30.32           N  
ANISOU 2781  N   VAL A 176     3555   5584   2383  -1239   1174   -778       N  
ATOM   2782  CA  VAL A 176      21.212  37.309 -12.676  1.00 30.02           C  
ANISOU 2782  CA  VAL A 176     3537   5460   2409  -1169   1055   -799       C  
ATOM   2783  C   VAL A 176      22.087  36.785 -11.544  1.00 34.94           C  
ANISOU 2783  C   VAL A 176     3995   6170   3109  -1226   1005   -931       C  
ATOM   2784  O   VAL A 176      23.030  36.026 -11.768  1.00 30.25           O  
ANISOU 2784  O   VAL A 176     3233   5736   2524  -1205    995  -1047       O  
ATOM   2785  CB  VAL A 176      20.338  36.154 -13.208  1.00 30.14           C  
ANISOU 2785  CB  VAL A 176     3556   5483   2411   -973    961   -820       C  
ATOM   2786  CG1 VAL A 176      19.479  35.569 -12.107  1.00 34.72           C  
ANISOU 2786  CG1 VAL A 176     4163   5960   3069   -898    844   -840       C  
ATOM   2787  CG2 VAL A 176      19.468  36.637 -14.342  1.00 32.51           C  
ANISOU 2787  CG2 VAL A 176     4007   5721   2623   -901   1002   -701       C  
ATOM   2788  H   VAL A 176      22.715  37.372 -13.944  1.00 36.39           H  
ATOM   2789  HA  VAL A 176      20.629  37.999 -12.322  1.00 36.02           H  
ATOM   2790  HB  VAL A 176      20.914  35.451 -13.548  1.00 36.17           H  
ATOM   2791 HG11 VAL A 176      18.944  34.847 -12.475  1.00 41.67           H  
ATOM   2792 HG12 VAL A 176      20.054  35.229 -11.404  1.00 41.67           H  
ATOM   2793 HG13 VAL A 176      18.900  36.263 -11.755  1.00 41.67           H  
ATOM   2794 HG21 VAL A 176      18.928  35.898 -14.662  1.00 39.01           H  
ATOM   2795 HG22 VAL A 176      18.895  37.350 -14.018  1.00 39.01           H  
ATOM   2796 HG23 VAL A 176      20.035  36.966 -15.057  1.00 39.01           H  
ATOM   2797  N   GLN A 177      21.749  37.190 -10.325  1.00 27.08           N  
ANISOU 2797  N   GLN A 177     3046   5074   2168  -1289    969   -917       N  
ATOM   2798  CA  GLN A 177      22.442  36.721  -9.138  1.00 26.85           C  
ANISOU 2798  CA  GLN A 177     2869   5129   2202  -1325    912  -1033       C  
ATOM   2799  C   GLN A 177      21.693  35.503  -8.610  1.00 26.93           C  
ANISOU 2799  C   GLN A 177     2859   5123   2251  -1158    785  -1069       C  
ATOM   2800  O   GLN A 177      20.512  35.600  -8.293  1.00 28.02           O  
ANISOU 2800  O   GLN A 177     3142   5106   2401  -1105    738   -990       O  
ATOM   2801  CB  GLN A 177      22.460  37.841  -8.098  1.00 26.77           C  
ANISOU 2801  CB  GLN A 177     2924   5020   2229  -1481    942  -1001       C  
ATOM   2802  CG  GLN A 177      22.923  37.418  -6.692  1.00 31.06           C  
ANISOU 2802  CG  GLN A 177     3336   5637   2827  -1505    868  -1108       C  
ATOM   2803  CD  GLN A 177      24.395  37.064  -6.681  1.00 29.64           C  
ANISOU 2803  CD  GLN A 177     2947   5658   2656  -1541    881  -1245       C  
ATOM   2804  OE1 GLN A 177      25.231  37.900  -6.989  1.00 33.81           O  
ANISOU 2804  OE1 GLN A 177     3458   6211   3177  -1667    969  -1263       O  
ATOM   2805  NE2 GLN A 177      24.712  35.810  -6.371  1.00 31.64           N  
ANISOU 2805  NE2 GLN A 177     3047   6046   2930  -1412    792  -1344       N  
ATOM   2806  H   GLN A 177      21.113  37.744 -10.160  1.00 32.49           H  
ATOM   2807  HA  GLN A 177      23.353  36.469  -9.356  1.00 32.22           H  
ATOM   2808  HB2 GLN A 177      23.061  38.537  -8.405  1.00 32.13           H  
ATOM   2809  HB3 GLN A 177      21.563  38.199  -8.014  1.00 32.13           H  
ATOM   2810  HG2 GLN A 177      22.781  38.151  -6.074  1.00 37.27           H  
ATOM   2811  HG3 GLN A 177      22.420  36.638  -6.410  1.00 37.27           H  
ATOM   2812 HE21 GLN A 177      24.093  35.242  -6.189  1.00 37.97           H  
ATOM   2813 HE22 GLN A 177      25.537  35.567  -6.354  1.00 37.97           H  
ATOM   2814  N   LEU A 178      22.378  34.364  -8.536  1.00 25.39           N  
ANISOU 2814  N   LEU A 178     2487   5073   2086  -1066    729  -1190       N  
ATOM   2815  CA  LEU A 178      21.796  33.140  -7.995  1.00 24.21           C  
ANISOU 2815  CA  LEU A 178     2306   4897   1994   -893    608  -1233       C  
ATOM   2816  C   LEU A 178      21.982  33.075  -6.468  1.00 23.59           C  
ANISOU 2816  C   LEU A 178     2179   4825   1961   -917    543  -1276       C  
ATOM   2817  O   LEU A 178      23.007  33.515  -5.933  1.00 24.59           O  
ANISOU 2817  O   LEU A 178     2189   5071   2082  -1035    580  -1340       O  
ATOM   2818  CB  LEU A 178      22.435  31.902  -8.644  1.00 24.86           C  
ANISOU 2818  CB  LEU A 178     2223   5120   2102   -763    573  -1343       C  
ATOM   2819  H   LEU A 178      23.193  34.274  -8.796  1.00 30.46           H  
ATOM   2820  HA  LEU A 178      20.846  33.127  -8.186  1.00 29.05           H  
ATOM   2821  N   ALA A 179      20.995  32.504  -5.787  1.00 22.14           N  
ANISOU 2821  N   ALA A 179     2079   4507   1826   -800    440  -1243       N  
ATOM   2822  CA  ALA A 179      21.129  32.228  -4.365  1.00 21.69           C  
ANISOU 2822  CA  ALA A 179     1977   4442   1821   -781    343  -1272       C  
ATOM   2823  C   ALA A 179      20.602  30.829  -4.054  1.00 20.85           C  
ANISOU 2823  C   ALA A 179     1853   4273   1797   -570    222  -1291       C  
ATOM   2824  O   ALA A 179      19.417  30.552  -4.203  1.00 20.44           O  
ANISOU 2824  O   ALA A 179     1937   4051   1777   -485    188  -1222       O  
ATOM   2825  CB  ALA A 179      20.396  33.277  -3.558  1.00 28.57           C  
ANISOU 2825  CB  ALA A 179     3005   5158   2692   -896    343  -1175       C  
ATOM   2826  H   ALA A 179      20.240  32.268  -6.124  1.00 26.57           H  
ATOM   2827  HA  ALA A 179      22.067  32.259  -4.120  1.00 26.03           H  
ATOM   2828  HB1 ALA A 179      20.496  33.077  -2.614  1.00 34.28           H  
ATOM   2829  HB2 ALA A 179      20.776  34.148  -3.753  1.00 34.28           H  
ATOM   2830  HB3 ALA A 179      19.457  33.263  -3.801  1.00 34.28           H  
ATOM   2831  N   ASP A 180      21.502  29.944  -3.645  1.00 21.75           N  
ANISOU 2831  N   ASP A 180     1791   4506   1967   -479    160  -1370       N  
ATOM   2832  CA  ASP A 180      21.141  28.584  -3.285  1.00 23.64           C  
ANISOU 2832  CA  ASP A 180     1999   4683   2300   -277     55  -1386       C  
ATOM   2833  C   ASP A 180      20.672  28.554  -1.846  1.00 20.43           C  
ANISOU 2833  C   ASP A 180     1660   4161   1941   -252    -42  -1313       C  
ATOM   2834  O   ASP A 180      21.423  28.924  -0.948  1.00 21.06           O  
ANISOU 2834  O   ASP A 180     1659   4332   2012   -315    -71  -1321       O  
ATOM   2835  CB  ASP A 180      22.353  27.666  -3.383  1.00 25.35           C  
ANISOU 2835  CB  ASP A 180     1996   5074   2561   -180     29  -1494       C  
ATOM   2836  CG  ASP A 180      22.528  27.073  -4.732  1.00 27.70           C  
ANISOU 2836  CG  ASP A 180     2224   5447   2855   -115     88  -1578       C  
ATOM   2837  OD1 ASP A 180      21.567  27.054  -5.521  1.00 28.78           O  
ANISOU 2837  OD1 ASP A 180     2481   5485   2969    -92    124  -1554       O  
ATOM   2838  OD2 ASP A 180      23.647  26.606  -5.005  1.00 25.94           O  
ANISOU 2838  OD2 ASP A 180     1814   5395   2648    -81     96  -1679       O  
ATOM   2839  H   ASP A 180      22.342  30.112  -3.567  1.00 26.10           H  
ATOM   2840  HA  ASP A 180      20.436  28.254  -3.864  1.00 28.37           H  
ATOM   2841  HB2 ASP A 180      23.151  28.175  -3.174  1.00 30.42           H  
ATOM   2842  HB3 ASP A 180      22.249  26.939  -2.749  1.00 30.42           H  
ATOM   2843  N   HIS A 181      19.438  28.112  -1.643  1.00 18.99           N  
ANISOU 2843  N   HIS A 181     1619   3791   1807   -160    -87  -1252       N  
ATOM   2844  CA  HIS A 181      18.868  27.989  -0.295  1.00 18.19           C  
ANISOU 2844  CA  HIS A 181     1594   3567   1750   -126   -175  -1178       C  
ATOM   2845  C   HIS A 181      18.845  26.542   0.154  1.00 19.03           C  
ANISOU 2845  C   HIS A 181     1637   3634   1959     78   -258  -1187       C  
ATOM   2846  O   HIS A 181      18.310  25.669  -0.545  1.00 18.40           O  
ANISOU 2846  O   HIS A 181     1574   3475   1941    199   -251  -1217       O  
ATOM   2847  CB  HIS A 181      17.425  28.491  -0.272  1.00 17.71           C  
ANISOU 2847  CB  HIS A 181     1744   3300   1686   -165   -163  -1095       C  
ATOM   2848  CG  HIS A 181      17.269  29.959  -0.518  1.00 17.79           C  
ANISOU 2848  CG  HIS A 181     1849   3277   1633   -345    -79  -1028       C  
ATOM   2849  ND1 HIS A 181      17.580  30.558  -1.720  1.00 17.09           N  
ANISOU 2849  ND1 HIS A 181     1750   3265   1480   -426     18  -1052       N  
ATOM   2850  CD2 HIS A 181      16.779  30.943   0.278  1.00 15.88           C  
ANISOU 2850  CD2 HIS A 181     1720   2925   1390   -449    -75   -936       C  
ATOM   2851  CE1 HIS A 181      17.309  31.850  -1.648  1.00 16.89           C  
ANISOU 2851  CE1 HIS A 181     1826   3175   1415   -575     77   -980       C  
ATOM   2852  NE2 HIS A 181      16.811  32.106  -0.450  1.00 17.12           N  
ANISOU 2852  NE2 HIS A 181     1928   3088   1490   -588     21   -913       N  
ATOM   2853  H   HIS A 181      18.902  27.873  -2.271  1.00 22.79           H  
ATOM   2854  HA  HIS A 181      19.392  28.507   0.335  1.00 21.83           H  
ATOM   2855  HB2 HIS A 181      16.924  28.023  -0.958  1.00 21.25           H  
ATOM   2856  HB3 HIS A 181      17.045  28.297   0.599  1.00 21.25           H  
ATOM   2857  HD1 HIS A 181      17.907  30.155  -2.406  1.00 20.51           H  
ATOM   2858  HD2 HIS A 181      16.473  30.846   1.151  1.00 19.06           H  
ATOM   2859  HE1 HIS A 181      17.439  32.472  -2.327  1.00 20.27           H  
ATOM   2860  HE2 HIS A 181      16.568  32.880  -0.165  1.00 20.55           H  
ATOM   2861  N   TYR A 182      19.410  26.284   1.333  1.00 18.91           N  
ANISOU 2861  N   TYR A 182     1549   3673   1962    120   -335  -1163       N  
ATOM   2862  CA  TYR A 182      19.297  24.992   1.986  1.00 19.02           C  
ANISOU 2862  CA  TYR A 182     1531   3621   2073    314   -416  -1137       C  
ATOM   2863  C   TYR A 182      18.682  25.197   3.368  1.00 18.34           C  
ANISOU 2863  C   TYR A 182     1555   3433   1982    306   -481  -1034       C  
ATOM   2864  O   TYR A 182      19.163  26.008   4.151  1.00 18.69           O  
ANISOU 2864  O   TYR A 182     1571   3576   1953    200   -504  -1018       O  
ATOM   2865  CB  TYR A 182      20.673  24.346   2.064  1.00 20.67           C  
ANISOU 2865  CB  TYR A 182     1529   4021   2303    406   -451  -1204       C  
ATOM   2866  CG  TYR A 182      21.256  24.169   0.669  1.00 21.36           C  
ANISOU 2866  CG  TYR A 182     1507   4216   2393    403   -379  -1316       C  
ATOM   2867  CD1 TYR A 182      22.219  25.037   0.172  1.00 23.03           C  
ANISOU 2867  CD1 TYR A 182     1617   4616   2519    259   -320  -1387       C  
ATOM   2868  CD2 TYR A 182      20.798  23.163  -0.150  1.00 22.16           C  
ANISOU 2868  CD2 TYR A 182     1610   4227   2582    535   -359  -1357       C  
ATOM   2869  CE1 TYR A 182      22.727  24.870  -1.126  1.00 24.00           C  
ANISOU 2869  CE1 TYR A 182     1643   4841   2635    253   -246  -1488       C  
ATOM   2870  CE2 TYR A 182      21.286  22.999  -1.418  1.00 27.01           C  
ANISOU 2870  CE2 TYR A 182     2124   4948   3190    532   -292  -1465       C  
ATOM   2871  CZ  TYR A 182      22.242  23.852  -1.894  1.00 22.71           C  
ANISOU 2871  CZ  TYR A 182     1484   4596   2550    392   -237  -1525       C  
ATOM   2872  OH  TYR A 182      22.679  23.660  -3.162  1.00 23.42           O  
ANISOU 2872  OH  TYR A 182     1479   4792   2627    391   -165  -1630       O  
ATOM   2873  H   TYR A 182      19.872  26.856   1.779  1.00 22.69           H  
ATOM   2874  HA  TYR A 182      18.712  24.416   1.469  1.00 22.82           H  
ATOM   2875  HB2 TYR A 182      21.268  24.913   2.577  1.00 24.80           H  
ATOM   2876  HB3 TYR A 182      20.596  23.472   2.478  1.00 24.80           H  
ATOM   2877  HD1 TYR A 182      22.538  25.728   0.706  1.00 27.64           H  
ATOM   2878  HD2 TYR A 182      20.145  22.581   0.165  1.00 26.59           H  
ATOM   2879  HE1 TYR A 182      23.373  25.450  -1.461  1.00 28.80           H  
ATOM   2880  HE2 TYR A 182      20.965  22.312  -1.956  1.00 32.41           H  
ATOM   2881  HH  TYR A 182      23.254  24.240  -3.359  1.00 28.10           H  
ATOM   2882  N   GLN A 183      17.631  24.439   3.646  1.00 17.65           N  
ANISOU 2882  N   GLN A 183     1582   3151   1973    418   -505   -977       N  
ATOM   2883  CA  GLN A 183      16.696  24.771   4.706  1.00 16.67           C  
ANISOU 2883  CA  GLN A 183     1607   2889   1839    382   -539   -882       C  
ATOM   2884  C   GLN A 183      16.279  23.521   5.461  1.00 18.58           C  
ANISOU 2884  C   GLN A 183     1876   3007   2178    565   -593   -816       C  
ATOM   2885  O   GLN A 183      16.183  22.422   4.891  1.00 18.56           O  
ANISOU 2885  O   GLN A 183     1839   2936   2279    709   -579   -847       O  
ATOM   2886  CB  GLN A 183      15.486  25.452   4.067  1.00 15.23           C  
ANISOU 2886  CB  GLN A 183     1588   2555   1644    279   -479   -880       C  
ATOM   2887  CG  GLN A 183      14.302  25.699   4.972  1.00 14.08           C  
ANISOU 2887  CG  GLN A 183     1608   2233   1507    250   -503   -799       C  
ATOM   2888  CD  GLN A 183      13.079  26.210   4.220  1.00 16.93           C  
ANISOU 2888  CD  GLN A 183     2118   2442   1871    181   -447   -812       C  
ATOM   2889  OE1 GLN A 183      13.172  26.794   3.130  1.00 13.86           O  
ANISOU 2889  OE1 GLN A 183     1725   2092   1451    104   -374   -830       O  
ATOM   2890  NE2 GLN A 183      11.917  25.955   4.787  1.00 16.14           N  
ANISOU 2890  NE2 GLN A 183     2146   2157   1829    209   -451   -744       N  
ATOM   2891  H   GLN A 183      17.437  23.713   3.227  1.00 21.18           H  
ATOM   2892  HA  GLN A 183      17.110  25.389   5.329  1.00 20.01           H  
ATOM   2893  HB2 GLN A 183      15.769  26.313   3.722  1.00 18.28           H  
ATOM   2894  HB3 GLN A 183      15.178  24.897   3.334  1.00 18.28           H  
ATOM   2895  HG2 GLN A 183      14.059  24.867   5.408  1.00 16.89           H  
ATOM   2896  HG3 GLN A 183      14.545  26.363   5.636  1.00 16.89           H  
ATOM   2897 HE21 GLN A 183      11.888  25.526   5.532  1.00 19.37           H  
ATOM   2898 HE22 GLN A 183      11.189  26.217   4.413  1.00 19.37           H  
ATOM   2899  N   GLN A 184      16.062  23.695   6.759  1.00 16.95           N  
ANISOU 2899  N   GLN A 184     1726   2775   1937    557   -649   -728       N  
ATOM   2900  CA  GLN A 184      15.635  22.618   7.640  1.00 20.26           C  
ANISOU 2900  CA  GLN A 184     2192   3073   2433    719   -694   -640       C  
ATOM   2901  C   GLN A 184      14.533  23.168   8.534  1.00 19.92           C  
ANISOU 2901  C   GLN A 184     2318   2894   2357    635   -701   -562       C  
ATOM   2902  O   GLN A 184      14.667  24.289   9.049  1.00 19.79           O  
ANISOU 2902  O   GLN A 184     2317   2968   2236    486   -717   -557       O  
ATOM   2903  CB  GLN A 184      16.824  22.169   8.512  1.00 26.62           C  
ANISOU 2903  CB  GLN A 184     2854   4053   3207    826   -772   -603       C  
ATOM   2904  CG  GLN A 184      17.133  20.698   8.425  1.00 40.92           C  
ANISOU 2904  CG  GLN A 184     4594   5816   5137   1050   -788   -582       C  
ATOM   2905  H   GLN A 184      16.158  24.449   7.163  1.00 20.34           H  
ATOM   2906  HA  GLN A 184      15.299  21.866   7.128  1.00 24.31           H  
ATOM   2907  HB2 GLN A 184      17.616  22.654   8.232  1.00 31.94           H  
ATOM   2908  HB3 GLN A 184      16.625  22.375   9.439  1.00 31.94           H  
ATOM   2909  N   ASN A 185      13.464  22.402   8.743  1.00 16.43           N  
ANISOU 2909  N   ASN A 185     1996   2239   2008    724   -684   -510       N  
ATOM   2910  CA  ASN A 185      12.403  22.816   9.652  1.00 14.41           C  
ANISOU 2910  CA  ASN A 185     1896   1852   1728    656   -689   -439       C  
ATOM   2911  C   ASN A 185      12.170  21.693  10.646  1.00 15.09           C  
ANISOU 2911  C   ASN A 185     2017   1839   1877    817   -717   -333       C  
ATOM   2912  O   ASN A 185      12.118  20.522  10.256  1.00 17.31           O  
ANISOU 2912  O   ASN A 185     2276   2021   2281    971   -692   -332       O  
ATOM   2913  CB  ASN A 185      11.089  23.116   8.939  1.00 14.59           C  
ANISOU 2913  CB  ASN A 185     2057   1685   1800    581   -625   -484       C  
ATOM   2914  CG  ASN A 185      11.172  24.316   7.984  1.00 16.08           C  
ANISOU 2914  CG  ASN A 185     2241   1951   1917    420   -590   -566       C  
ATOM   2915  OD1 ASN A 185      11.934  24.309   7.035  1.00 21.86           O  
ANISOU 2915  OD1 ASN A 185     2866   2797   2642    427   -570   -633       O  
ATOM   2916  ND2 ASN A 185      10.337  25.309   8.211  1.00 12.77           N  
ANISOU 2916  ND2 ASN A 185     1943   1458   1452    282   -576   -558       N  
ATOM   2917  H   ASN A 185      13.331  21.638   8.370  1.00 19.71           H  
ATOM   2918  HA  ASN A 185      12.681  23.608  10.138  1.00 17.29           H  
ATOM   2919  HB2 ASN A 185      10.830  22.340   8.419  1.00 17.51           H  
ATOM   2920  HB3 ASN A 185      10.409  23.311   9.603  1.00 17.51           H  
ATOM   2921 HD21 ASN A 185       9.783  25.264   8.867  1.00 15.33           H  
ATOM   2922 HD22 ASN A 185      10.346  26.003   7.703  1.00 15.33           H  
ATOM   2923  N  ATHR A 186      12.056  22.031  11.928  0.48 15.15           N  
ANISOU 2923  N  ATHR A 186     2075   1877   1803    786   -764   -244       N  
ATOM   2924  N  BTHR A 186      11.996  22.067  11.908  0.52 14.91           N  
ANISOU 2924  N  BTHR A 186     2052   1839   1773    779   -761   -246       N  
ATOM   2925  CA ATHR A 186      11.800  21.038  12.982  0.48 18.76           C  
ANISOU 2925  CA ATHR A 186     2583   2245   2299    935   -786   -120       C  
ATOM   2926  CA BTHR A 186      11.801  21.119  13.000  0.52 18.44           C  
ANISOU 2926  CA BTHR A 186     2544   2212   2251    924   -787   -122       C  
ATOM   2927  C  ATHR A 186      10.709  21.525  13.925  0.48 16.50           C  
ANISOU 2927  C  ATHR A 186     2453   1846   1969    842   -779    -58       C  
ATOM   2928  C  BTHR A 186      10.604  21.578  13.827  0.52 15.85           C  
ANISOU 2928  C  BTHR A 186     2382   1749   1893    829   -771    -68       C  
ATOM   2929  O  ATHR A 186      10.709  22.684  14.318  0.48 17.50           O  
ANISOU 2929  O  ATHR A 186     2593   2073   1982    685   -804    -82       O  
ATOM   2930  O  BTHR A 186      10.411  22.772  14.018  0.52 14.48           O  
ANISOU 2930  O  BTHR A 186     2240   1639   1625    659   -782   -106       O  
ATOM   2931  CB ATHR A 186      13.059  20.716  13.829  0.48 23.81           C  
ANISOU 2931  CB ATHR A 186     3091   3095   2859   1045   -868    -49       C  
ATOM   2932  CB BTHR A 186      13.044  21.056  13.912  0.52 22.90           C  
ANISOU 2932  CB BTHR A 186     2982   3009   2712    998   -875    -59       C  
ATOM   2933  OG1ATHR A 186      13.786  21.917  14.113  0.48 17.70           O  
ANISOU 2933  OG1ATHR A 186     2236   2550   1939    903   -919   -100       O  
ATOM   2934  OG1BTHR A 186      14.229  20.922  13.114  0.52 25.55           O  
ANISOU 2934  OG1BTHR A 186     3147   3506   3054   1044   -892   -138       O  
ATOM   2935  CG2ATHR A 186      13.963  19.738  13.102  0.48 18.76           C  
ANISOU 2935  CG2ATHR A 186     2319   2499   2311   1168   -841    -78       C  
ATOM   2936  CG2BTHR A 186      12.942  19.876  14.877  0.52 26.39           C  
ANISOU 2936  CG2BTHR A 186     3455   3369   3204   1118   -841     80       C  
ATOM   2937  H  ATHR A 186      12.122  22.837  12.221  0.48 18.18           H  
ATOM   2938  H  BTHR A 186      11.987  22.888  12.164  0.52 17.89           H  
ATOM   2939  HA ATHR A 186      11.496  20.213  12.571  0.48 22.51           H  
ATOM   2940  HA BTHR A 186      11.622  20.234  12.646  0.52 22.13           H  
ATOM   2941  HB ATHR A 186      12.784  20.307  14.664  0.48 28.57           H  
ATOM   2942  HB BTHR A 186      13.100  21.872  14.434  0.52 27.48           H  
ATOM   2943  HG1ATHR A 186      13.301  22.451  14.542  0.48 21.24           H  
ATOM   2944  HG1BTHR A 186      14.303  21.580  12.597  0.52 30.66           H  
ATOM   2945 HG21ATHR A 186      14.745  19.546  13.642  0.48 22.52           H  
ATOM   2946 HG21BTHR A 186      13.727  19.845  15.446  0.52 31.67           H  
ATOM   2947 HG22ATHR A 186      13.486  18.911  12.931  0.48 22.52           H  
ATOM   2948 HG22BTHR A 186      12.153  19.971  15.433  0.52 31.67           H  
ATOM   2949 HG23ATHR A 186      14.249  20.117  12.256  0.48 22.52           H  
ATOM   2950 HG23BTHR A 186      12.880  19.046  14.379  0.52 31.67           H  
ATOM   2951  N   PRO A 187       9.777  20.639  14.303  1.00 15.07           N  
ANISOU 2951  N   PRO A 187     2354   1492   1880    855   -679      4       N  
ATOM   2952  CA  PRO A 187       8.683  21.099  15.159  1.00 14.77           C  
ANISOU 2952  CA  PRO A 187     2438   1370   1806    741   -645     39       C  
ATOM   2953  C   PRO A 187       9.185  21.584  16.544  1.00 15.07           C  
ANISOU 2953  C   PRO A 187     2478   1546   1703    750   -737    130       C  
ATOM   2954  O   PRO A 187      10.157  21.025  17.066  1.00 18.28           O  
ANISOU 2954  O   PRO A 187     2785   2086   2074    863   -778    204       O  
ATOM   2955  CB  PRO A 187       7.776  19.859  15.282  1.00 19.75           C  
ANISOU 2955  CB  PRO A 187     3061   1879   2563    736   -500     88       C  
ATOM   2956  CG  PRO A 187       8.546  18.732  14.815  1.00 24.73           C  
ANISOU 2956  CG  PRO A 187     3593   2518   3285    861   -478    116       C  
ATOM   2957  CD  PRO A 187       9.683  19.210  13.986  1.00 23.23           C  
ANISOU 2957  CD  PRO A 187     3334   2442   3048    924   -572     39       C  
ATOM   2958  HA  PRO A 187       8.193  21.814  14.725  1.00 17.73           H  
ATOM   2959  HB2 PRO A 187       7.524  19.735  16.210  1.00 23.70           H  
ATOM   2960  HB3 PRO A 187       6.987  19.981  14.731  1.00 23.70           H  
ATOM   2961  HG2 PRO A 187       8.881  18.242  15.582  1.00 29.67           H  
ATOM   2962  HG3 PRO A 187       7.971  18.158  14.284  1.00 29.67           H  
ATOM   2963  HD2 PRO A 187      10.501  18.754  14.242  1.00 27.87           H  
ATOM   2964  HD3 PRO A 187       9.489  19.086  13.044  1.00 27.87           H  
ATOM   2965  N   ILE A 188       8.538  22.615  17.071  1.00 23.61           N  
ANISOU 2965  N   ILE A 188     4691   2760   1521  -1699   -396    335       N  
ATOM   2966  CA  ILE A 188       8.810  23.107  18.431  1.00 24.90           C  
ANISOU 2966  CA  ILE A 188     4933   2947   1580  -1776   -381    323       C  
ATOM   2967  C   ILE A 188       8.140  22.237  19.475  1.00 27.65           C  
ANISOU 2967  C   ILE A 188     5394   3275   1836  -1871   -363    357       C  
ATOM   2968  O   ILE A 188       8.689  21.992  20.554  1.00 30.98           O  
ANISOU 2968  O   ILE A 188     5910   3690   2171  -1914   -428    397       O  
ATOM   2969  CB  ILE A 188       8.371  24.578  18.555  1.00 24.57           C  
ANISOU 2969  CB  ILE A 188     4848   2961   1527  -1806   -243    226       C  
ATOM   2970  CG1 ILE A 188       9.369  25.433  17.785  1.00 23.49           C  
ANISOU 2970  CG1 ILE A 188     4626   2839   1458  -1724   -292    207       C  
ATOM   2971  CG2 ILE A 188       8.321  25.037  20.031  1.00 26.11           C  
ANISOU 2971  CG2 ILE A 188     5132   3183   1604  -1900   -200    202       C  
ATOM   2972  CD1 ILE A 188       8.922  26.825  17.458  1.00 22.87           C  
ANISOU 2972  CD1 ILE A 188     4491   2793   1404  -1725   -166    114       C  
ATOM   2973  H   ILE A 188       7.926  23.058  16.660  1.00 28.34           H  
ATOM   2974  HA  ILE A 188       9.766  23.071  18.589  1.00 29.88           H  
ATOM   2975  HB  ILE A 188       7.491  24.682  18.160  1.00 29.49           H  
ATOM   2976 HG12 ILE A 188      10.180  25.505  18.312  1.00 28.18           H  
ATOM   2977 HG13 ILE A 188       9.568  24.989  16.946  1.00 28.18           H  
ATOM   2978 HG21 ILE A 188       8.041  25.965  20.063  1.00 31.33           H  
ATOM   2979 HG22 ILE A 188       7.686  24.483  20.512  1.00 31.33           H  
ATOM   2980 HG23 ILE A 188       9.204  24.943  20.421  1.00 31.33           H  
ATOM   2981 HD11 ILE A 188       9.629  27.277  16.971  1.00 27.44           H  
ATOM   2982 HD12 ILE A 188       8.121  26.780  16.914  1.00 27.44           H  
ATOM   2983 HD13 ILE A 188       8.735  27.298  18.285  1.00 27.44           H  
ATOM   2984  N   GLY A 189       6.947  21.756  19.160  1.00 26.63           N  
ANISOU 2984  N   GLY A 189     5254   3143   1722  -1904   -274    343       N  
ATOM   2985  CA  GLY A 189       6.208  20.903  20.072  1.00 33.97           C  
ANISOU 2985  CA  GLY A 189     6281   4060   2565  -2002   -243    375       C  
ATOM   2986  C   GLY A 189       6.592  19.447  19.917  1.00 33.00           C  
ANISOU 2986  C   GLY A 189     6226   3858   2457  -1979   -381    474       C  
ATOM   2987  O   GLY A 189       7.313  19.087  18.992  1.00 32.93           O  
ANISOU 2987  O   GLY A 189     6171   3806   2537  -1877   -491    507       O  
ATOM   2988  H   GLY A 189       6.542  21.910  18.417  1.00 31.96           H  
ATOM   2989  HA2 GLY A 189       6.385  21.174  20.986  1.00 40.76           H  
ATOM   2990  HA3 GLY A 189       5.257  20.992  19.902  1.00 40.76           H  
ATOM   2991  N  AASP A 190       6.114  18.605  20.824  0.58 40.93           N  
ANISOU 2991  N  AASP A 190     7341   4838   3372  -2072   -377    519       N  
ATOM   2992  N  BASP A 190       6.082  18.619  20.826  0.42 40.42           N  
ANISOU 2992  N  BASP A 190     7275   4775   3307  -2074   -372    517       N  
ATOM   2993  CA AASP A 190       6.440  17.184  20.789  0.58 42.58           C  
ANISOU 2993  CA AASP A 190     7635   4956   3586  -2058   -510    614       C  
ATOM   2994  CA BASP A 190       6.396  17.195  20.866  0.42 42.07           C  
ANISOU 2994  CA BASP A 190     7576   4895   3514  -2066   -504    613       C  
ATOM   2995  C  AASP A 190       5.380  16.397  20.015  0.58 42.32           C  
ANISOU 2995  C  AASP A 190     7566   4900   3613  -2068   -453    618       C  
ATOM   2996  C  BASP A 190       5.239  16.350  20.334  0.42 43.13           C  
ANISOU 2996  C  BASP A 190     7696   5008   3685  -2101   -437    621       C  
ATOM   2997  O  AASP A 190       5.624  15.262  19.612  0.58 43.44           O  
ANISOU 2997  O  AASP A 190     7752   4958   3797  -2031   -564    685       O  
ATOM   2998  O  BASP A 190       5.265  15.125  20.438  0.42 43.42           O  
ANISOU 2998  O  BASP A 190     7822   4965   3712  -2117   -524    697       O  
ATOM   2999  CB AASP A 190       6.572  16.627  22.215  0.58 42.84           C  
ANISOU 2999  CB AASP A 190     7828   4966   3484  -2156   -550    674       C  
ATOM   3000  CB BASP A 190       6.720  16.765  22.303  0.42 42.18           C  
ANISOU 3000  CB BASP A 190     7744   4887   3394  -2152   -557    672       C  
ATOM   3001  CG AASP A 190       7.682  17.298  23.012  0.58 41.57           C  
ANISOU 3001  CG AASP A 190     7706   4827   3263  -2139   -622    679       C  
ATOM   3002  CG BASP A 190       5.473  16.464  23.126  0.42 45.59           C  
ANISOU 3002  CG BASP A 190     8247   5349   3728  -2295   -427    666       C  
ATOM   3003  OD1AASP A 190       8.726  17.651  22.418  0.58 48.66           O  
ANISOU 3003  OD1AASP A 190     8535   5718   4235  -2027   -717    676       O  
ATOM   3004  OD1BASP A 190       4.438  17.146  22.942  0.42 36.91           O  
ANISOU 3004  OD1BASP A 190     7061   4323   2638  -2337   -263    585       O  
ATOM   3005  OD2AASP A 190       7.508  17.469  24.237  0.58 46.23           O  
ANISOU 3005  OD2AASP A 190     8391   5447   3727  -2237   -581    684       O  
ATOM   3006  OD2BASP A 190       5.536  15.540  23.969  0.42 53.18           O  
ANISOU 3006  OD2BASP A 190     9348   6258   4600  -2364   -490    744       O  
ATOM   3007  H  AASP A 190       5.597  18.831  21.473  0.58 49.11           H  
ATOM   3008  H  BASP A 190       5.539  18.867  21.446  0.42 48.50           H  
ATOM   3009  HA AASP A 190       7.291  17.065  20.339  0.58 51.09           H  
ATOM   3010  HA BASP A 190       7.175  17.024  20.314  0.42 50.48           H  
ATOM   3011  HB2AASP A 190       5.736  16.767  22.688  0.58 51.41           H  
ATOM   3012  HB2BASP A 190       7.263  15.961  22.277  0.42 50.61           H  
ATOM   3013  HB3AASP A 190       6.769  15.678  22.166  0.58 51.41           H  
ATOM   3014  HB3BASP A 190       7.205  17.479  22.744  0.42 50.61           H  
ATOM   3015  N   GLY A 191       4.218  17.012  19.795  1.00 44.03           N  
ANISOU 3015  N   GLY A 191     7699   5190   3842  -2112   -282    542       N  
ATOM   3016  CA  GLY A 191       3.080  16.326  19.203  1.00 43.26           C  
ANISOU 3016  CA  GLY A 191     7558   5085   3794  -2137   -205    539       C  
ATOM   3017  C   GLY A 191       3.362  15.877  17.771  1.00 38.74           C  
ANISOU 3017  C   GLY A 191     6901   4460   3356  -2017   -284    558       C  
ATOM   3018  O   GLY A 191       4.367  16.293  17.193  1.00 35.92           O  
ANISOU 3018  O   GLY A 191     6503   4091   3054  -1915   -376    558       O  
ATOM   3019  H  AGLY A 191       4.066  17.837  19.984  0.58 52.84           H  
ATOM   3020  H  BGLY A 191       4.163  17.870  19.761  0.42 52.84           H  
ATOM   3021  HA2 GLY A 191       2.861  15.544  19.733  1.00 51.91           H  
ATOM   3022  HA3 GLY A 191       2.312  16.918  19.195  1.00 51.91           H  
ATOM   3023  N   PRO A 192       2.496  15.010  17.209  1.00 38.02           N  
ANISOU 3023  N   PRO A 192     6786   4340   3322  -2034   -249    574       N  
ATOM   3024  CA  PRO A 192       2.686  14.452  15.853  1.00 34.12           C  
ANISOU 3024  CA  PRO A 192     6218   3787   2959  -1926   -325    593       C  
ATOM   3025  C   PRO A 192       2.602  15.511  14.764  1.00 29.08           C  
ANISOU 3025  C   PRO A 192     5421   3208   2420  -1834   -258    519       C  
ATOM   3026  O   PRO A 192       1.874  16.496  14.907  1.00 31.55           O  
ANISOU 3026  O   PRO A 192     5661   3607   2720  -1868   -110    443       O  
ATOM   3027  CB  PRO A 192       1.531  13.454  15.711  1.00 38.93           C  
ANISOU 3027  CB  PRO A 192     6831   4367   3592  -1999   -262    611       C  
ATOM   3028  CG  PRO A 192       0.504  13.895  16.713  1.00 44.73           C  
ANISOU 3028  CG  PRO A 192     7579   5185   4231  -2133   -101    566       C  
ATOM   3029  CD  PRO A 192       1.264  14.510  17.845  1.00 37.69           C  
ANISOU 3029  CD  PRO A 192     6781   4320   3221  -2165   -132    572       C  
ATOM   3030  HA  PRO A 192       3.532  13.983  15.790  1.00 40.94           H  
ATOM   3031  HB2 PRO A 192       1.172  13.497  14.811  1.00 46.71           H  
ATOM   3032  HB3 PRO A 192       1.846  12.559  15.913  1.00 46.71           H  
ATOM   3033  HG2 PRO A 192      -0.087  14.547  16.306  1.00 53.67           H  
ATOM   3034  HG3 PRO A 192       0.001  13.125  17.021  1.00 53.67           H  
ATOM   3035  HD2 PRO A 192       0.760  15.245  18.229  1.00 45.23           H  
ATOM   3036  HD3 PRO A 192       1.477  13.840  18.512  1.00 45.23           H  
ATOM   3037  N   VAL A 193       3.353  15.308  13.685  1.00 25.54           N  
ANISOU 3037  N   VAL A 193     4923   2711   2070  -1716   -369    540       N  
ATOM   3038  CA  VAL A 193       3.312  16.219  12.550  1.00 23.04           C  
ANISOU 3038  CA  VAL A 193     4463   2439   1854  -1627   -317    480       C  
ATOM   3039  C   VAL A 193       3.193  15.387  11.291  1.00 22.41           C  
ANISOU 3039  C   VAL A 193     4318   2292   1903  -1549   -378    498       C  
ATOM   3040  O   VAL A 193       3.371  14.170  11.327  1.00 23.24           O  
ANISOU 3040  O   VAL A 193     4501   2313   2015  -1551   -482    557       O  
ATOM   3041  CB  VAL A 193       4.566  17.100  12.431  1.00 25.20           C  
ANISOU 3041  CB  VAL A 193     4725   2730   2119  -1554   -395    476       C  
ATOM   3042  CG1 VAL A 193       4.759  17.945  13.693  1.00 24.45           C  
ANISOU 3042  CG1 VAL A 193     4695   2693   1904  -1630   -344    451       C  
ATOM   3043  CG2 VAL A 193       5.813  16.243  12.114  1.00 24.00           C  
ANISOU 3043  CG2 VAL A 193     4626   2495   1997  -1472   -596    546       C  
ATOM   3044  H   VAL A 193       3.895  14.648  13.587  1.00 30.65           H  
ATOM   3045  HA  VAL A 193       2.534  16.793  12.619  1.00 27.65           H  
ATOM   3046  HB  VAL A 193       4.440  17.712  11.689  1.00 30.24           H  
ATOM   3047 HG11 VAL A 193       5.556  18.489  13.589  1.00 29.35           H  
ATOM   3048 HG12 VAL A 193       3.983  18.514  13.813  1.00 29.35           H  
ATOM   3049 HG13 VAL A 193       4.859  17.355  14.456  1.00 29.35           H  
ATOM   3050 HG21 VAL A 193       6.586  16.824  12.045  1.00 28.80           H  
ATOM   3051 HG22 VAL A 193       5.945  15.601  12.830  1.00 28.80           H  
ATOM   3052 HG23 VAL A 193       5.672  15.778  11.275  1.00 28.80           H  
ATOM   3053  N   LEU A 194       2.857  16.049  10.190  1.00 20.99           N  
ANISOU 3053  N   LEU A 194     4000   2147   1828  -1483   -314    439       N  
ATOM   3054  CA  LEU A 194       2.717  15.350   8.930  1.00 20.37           C  
ANISOU 3054  CA  LEU A 194     3848   2009   1882  -1407   -370    437       C  
ATOM   3055  C   LEU A 194       4.084  15.346   8.269  1.00 19.53           C  
ANISOU 3055  C   LEU A 194     3742   1857   1820  -1292   -528    466       C  
ATOM   3056  O   LEU A 194       4.664  16.401   8.036  1.00 19.47           O  
ANISOU 3056  O   LEU A 194     3684   1898   1814  -1249   -519    440       O  
ATOM   3057  CB  LEU A 194       1.676  16.052   8.044  1.00 19.49           C  
ANISOU 3057  CB  LEU A 194     3581   1957   1868  -1391   -235    350       C  
ATOM   3058  CG  LEU A 194       0.223  15.923   8.508  1.00 20.44           C  
ANISOU 3058  CG  LEU A 194     3674   2121   1972  -1496    -86    311       C  
ATOM   3059  CD1 LEU A 194      -0.668  16.797   7.631  1.00 23.15           C  
ANISOU 3059  CD1 LEU A 194     3856   2530   2410  -1465     32    214       C  
ATOM   3060  CD2 LEU A 194      -0.270  14.482   8.472  1.00 26.39           C  
ANISOU 3060  CD2 LEU A 194     4474   2802   2752  -1545   -130    353       C  
ATOM   3061  H   LEU A 194       2.707  16.895  10.150  1.00 25.19           H  
ATOM   3062  HA  LEU A 194       2.437  14.434   9.085  1.00 24.44           H  
ATOM   3063  HB2 LEU A 194       1.888  16.998   8.013  1.00 23.39           H  
ATOM   3064  HB3 LEU A 194       1.731  15.678   7.151  1.00 23.39           H  
ATOM   3065  HG  LEU A 194       0.152  16.243   9.421  1.00 24.53           H  
ATOM   3066 HD11 LEU A 194      -1.587  16.710   7.930  1.00 27.78           H  
ATOM   3067 HD12 LEU A 194      -0.380  17.720   7.709  1.00 27.78           H  
ATOM   3068 HD13 LEU A 194      -0.590  16.502   6.710  1.00 27.78           H  
ATOM   3069 HD21 LEU A 194      -1.191  14.457   8.774  1.00 31.67           H  
ATOM   3070 HD22 LEU A 194      -0.210  14.151   7.563  1.00 31.67           H  
ATOM   3071 HD23 LEU A 194       0.286  13.944   9.058  1.00 31.67           H  
ATOM   3072  N   LEU A 195       4.613  14.162   7.989  1.00 19.99           N  
ANISOU 3072  N   LEU A 195     3860   1821   1916  -1242   -676    516       N  
ATOM   3073  CA  LEU A 195       5.886  14.057   7.279  1.00 19.35           C  
ANISOU 3073  CA  LEU A 195     3767   1695   1892  -1117   -838    534       C  
ATOM   3074  C   LEU A 195       5.608  13.790   5.804  1.00 18.46           C  
ANISOU 3074  C   LEU A 195     3517   1571   1926  -1007   -851    470       C  
ATOM   3075  O   LEU A 195       5.029  12.765   5.464  1.00 19.00           O  
ANISOU 3075  O   LEU A 195     3613   1556   2052  -1026   -879    479       O  
ATOM   3076  CB  LEU A 195       6.716  12.924   7.863  1.00 20.58           C  
ANISOU 3076  CB  LEU A 195     4050   1767   2004  -1089  -1006    600       C  
ATOM   3077  CG  LEU A 195       7.140  13.164   9.319  1.00 21.59           C  
ANISOU 3077  CG  LEU A 195     4288   1925   1991  -1170  -1010    636       C  
ATOM   3078  CD1 LEU A 195       7.839  11.927   9.843  1.00 27.32           C  
ANISOU 3078  CD1 LEU A 195     5129   2552   2698  -1141  -1172    686       C  
ATOM   3079  CD2 LEU A 195       8.039  14.399   9.439  1.00 20.78           C  
ANISOU 3079  CD2 LEU A 195     4137   1906   1853  -1131  -1012    616       C  
ATOM   3080  H   LEU A 195       4.259  13.406   8.196  1.00 23.99           H  
ATOM   3081  HA  LEU A 195       6.381  14.887   7.362  1.00 23.23           H  
ATOM   3082  HB2 LEU A 195       6.194  12.107   7.836  1.00 24.70           H  
ATOM   3083  HB3 LEU A 195       7.521  12.819   7.332  1.00 24.70           H  
ATOM   3084  HG  LEU A 195       6.348  13.314   9.859  1.00 25.91           H  
ATOM   3085 HD11 LEU A 195       8.106  12.082  10.762  1.00 32.78           H  
ATOM   3086 HD12 LEU A 195       7.228  11.176   9.797  1.00 32.78           H  
ATOM   3087 HD13 LEU A 195       8.621  11.752   9.296  1.00 32.78           H  
ATOM   3088 HD21 LEU A 195       8.287  14.519  10.369  1.00 24.94           H  
ATOM   3089 HD22 LEU A 195       8.834  14.263   8.899  1.00 24.94           H  
ATOM   3090 HD23 LEU A 195       7.552  15.176   9.122  1.00 24.94           H  
ATOM   3091  N   PRO A 196       6.018  14.707   4.932  1.00 17.21           N  
ANISOU 3091  N   PRO A 196     3209   1507   1823   -890   -827    399       N  
ATOM   3092  CA  PRO A 196       5.429  14.614   3.590  1.00 16.44           C  
ANISOU 3092  CA  PRO A 196     2973   1427   1846   -806   -795    327       C  
ATOM   3093  C   PRO A 196       6.189  13.708   2.607  1.00 16.38           C  
ANISOU 3093  C   PRO A 196     2927   1373   1922   -661   -946    311       C  
ATOM   3094  O   PRO A 196       7.369  13.471   2.797  1.00 16.64           O  
ANISOU 3094  O   PRO A 196     2996   1394   1931   -590  -1069    338       O  
ATOM   3095  CB  PRO A 196       5.516  16.043   3.098  1.00 15.29           C  
ANISOU 3095  CB  PRO A 196     2700   1399   1710   -751   -701    265       C  
ATOM   3096  CG  PRO A 196       6.772  16.579   3.748  1.00 16.59           C  
ANISOU 3096  CG  PRO A 196     2909   1597   1797   -735   -763    298       C  
ATOM   3097  CD  PRO A 196       6.809  15.938   5.114  1.00 16.54           C  
ANISOU 3097  CD  PRO A 196     3075   1519   1692   -853   -804    378       C  
ATOM   3098  HA  PRO A 196       4.499  14.341   3.640  1.00 19.73           H  
ATOM   3099  HB2 PRO A 196       5.595  16.055   2.131  1.00 18.34           H  
ATOM   3100  HB3 PRO A 196       4.736  16.541   3.389  1.00 18.34           H  
ATOM   3101  HG2 PRO A 196       7.547  16.320   3.226  1.00 19.91           H  
ATOM   3102  HG3 PRO A 196       6.715  17.545   3.823  1.00 19.91           H  
ATOM   3103  HD2 PRO A 196       7.721  15.721   5.361  1.00 19.85           H  
ATOM   3104  HD3 PRO A 196       6.390  16.516   5.770  1.00 19.85           H  
ATOM   3105  N   ASP A 197       5.511  13.219   1.572  1.00 16.14           N  
ANISOU 3105  N   ASP A 197     2819   1325   1990   -615   -937    258       N  
ATOM   3106  CA  ASP A 197       6.186  12.735   0.370  1.00 15.80           C  
ANISOU 3106  CA  ASP A 197     2689   1283   2029   -453  -1045    207       C  
ATOM   3107  C   ASP A 197       6.865  13.925  -0.307  1.00 14.67           C  
ANISOU 3107  C   ASP A 197     2414   1273   1888   -352  -1009    159       C  
ATOM   3108  O   ASP A 197       6.520  15.098  -0.050  1.00 14.09           O  
ANISOU 3108  O   ASP A 197     2304   1274   1775   -406   -888    153       O  
ATOM   3109  CB  ASP A 197       5.180  12.066  -0.599  1.00 15.82           C  
ANISOU 3109  CB  ASP A 197     2634   1250   2129   -438  -1029    150       C  
ATOM   3110  CG  ASP A 197       4.619  10.755  -0.057  1.00 20.43           C  
ANISOU 3110  CG  ASP A 197     3353   1687   2722   -537  -1084    196       C  
ATOM   3111  OD1 ASP A 197       5.125  10.243   0.960  1.00 22.36           O  
ANISOU 3111  OD1 ASP A 197     3745   1847   2903   -593  -1158    277       O  
ATOM   3112  OD2 ASP A 197       3.672  10.226  -0.658  1.00 25.23           O  
ANISOU 3112  OD2 ASP A 197     3924   2261   3401   -563  -1058    152       O  
ATOM   3113  H   ASP A 197       4.653  13.156   1.540  1.00 19.37           H  
ATOM   3114  HA  ASP A 197       6.864  12.086   0.614  1.00 18.96           H  
ATOM   3115  HB2 ASP A 197       4.436  12.671  -0.749  1.00 18.99           H  
ATOM   3116  HB3 ASP A 197       5.628  11.877  -1.438  1.00 18.99           H  
ATOM   3117  N   ASN A 198       7.831  13.641  -1.181  1.00 14.49           N  
ANISOU 3117  N   ASN A 198     2319   1278   1908   -208  -1109    121       N  
ATOM   3118  CA  ASN A 198       8.519  14.689  -1.924  1.00 13.60           C  
ANISOU 3118  CA  ASN A 198     2080   1293   1795   -121  -1076     78       C  
ATOM   3119  C   ASN A 198       7.534  15.473  -2.789  1.00 12.77           C  
ANISOU 3119  C   ASN A 198     1875   1251   1725   -119   -950     28       C  
ATOM   3120  O   ASN A 198       6.680  14.903  -3.454  1.00 12.81           O  
ANISOU 3120  O   ASN A 198     1851   1225   1791   -102   -943     -9       O  
ATOM   3121  CB  ASN A 198       9.644  14.112  -2.799  1.00 13.76           C  
ANISOU 3121  CB  ASN A 198     2026   1343   1860     30  -1160     31       C  
ATOM   3122  CG  ASN A 198      10.817  13.586  -2.001  1.00 23.00           C  
ANISOU 3122  CG  ASN A 198     3258   2481   3001     49  -1225     60       C  
ATOM   3123  OD1 ASN A 198      10.786  13.477  -0.756  1.00 15.18           O  
ANISOU 3123  OD1 ASN A 198     2392   1425   1952    -44  -1275    131       O  
ATOM   3124  ND2 ASN A 198      11.887  13.262  -2.721  1.00 18.20           N  
ANISOU 3124  ND2 ASN A 198     2562   1929   2422    162  -1219      3       N  
ATOM   3125  H   ASN A 198       8.106  12.846  -1.360  1.00 17.39           H  
ATOM   3126  HA  ASN A 198       8.920  15.308  -1.294  1.00 16.32           H  
ATOM   3127  HB2 ASN A 198       9.289  13.379  -3.325  1.00 16.51           H  
ATOM   3128  HB3 ASN A 198       9.974  14.810  -3.387  1.00 16.51           H  
ATOM   3129 HD21 ASN A 198      11.876  13.360  -3.575  1.00 21.84           H  
ATOM   3130 HD22 ASN A 198      12.590  12.956  -2.332  1.00 21.84           H  
ATOM   3131  N   HIS A 199       7.631  16.800  -2.720  1.00 12.14           N  
ANISOU 3131  N   HIS A 199     1752   1255   1605   -141   -857     28       N  
ATOM   3132  CA  HIS A 199       6.763  17.686  -3.484  1.00 11.86           C  
ANISOU 3132  CA  HIS A 199     1634   1278   1596   -129   -746    -13       C  
ATOM   3133  C   HIS A 199       7.451  19.045  -3.519  1.00 11.44           C  
ANISOU 3133  C   HIS A 199     1543   1307   1496   -121   -692     -7       C  
ATOM   3134  O   HIS A 199       8.612  19.177  -3.077  1.00 11.45           O  
ANISOU 3134  O   HIS A 199     1565   1332   1455   -121   -747     18       O  
ATOM   3135  CB  HIS A 199       5.344  17.725  -2.860  1.00 11.68           C  
ANISOU 3135  CB  HIS A 199     1655   1209   1576   -238   -651     -9       C  
ATOM   3136  CG  HIS A 199       5.288  18.384  -1.514  1.00 11.92           C  
ANISOU 3136  CG  HIS A 199     1771   1228   1530   -355   -584     34       C  
ATOM   3137  ND1 HIS A 199       5.701  17.749  -0.359  1.00 12.64           N  
ANISOU 3137  ND1 HIS A 199     1980   1258   1565   -435   -639     92       N  
ATOM   3138  CD2 HIS A 199       4.909  19.631  -1.145  1.00 11.84           C  
ANISOU 3138  CD2 HIS A 199     1754   1261   1484   -401   -474     25       C  
ATOM   3139  CE1 HIS A 199       5.569  18.575   0.666  1.00 16.61           C  
ANISOU 3139  CE1 HIS A 199     2541   1776   1995   -530   -559    114       C  
ATOM   3140  NE2 HIS A 199       5.078  19.719   0.221  1.00 14.19           N  
ANISOU 3140  NE2 HIS A 199     2158   1529   1703   -510   -456     69       N  
ATOM   3141  H   HIS A 199       8.203  17.215  -2.229  1.00 14.57           H  
ATOM   3142  HA  HIS A 199       6.688  17.358  -4.394  1.00 14.24           H  
ATOM   3143  HB2 HIS A 199       4.756  18.216  -3.455  1.00 14.02           H  
ATOM   3144  HB3 HIS A 199       5.023  16.815  -2.759  1.00 14.02           H  
ATOM   3145  HD1 HIS A 199       6.001  16.944  -0.314  1.00 15.17           H  
ATOM   3146  HD2 HIS A 199       4.581  20.297  -1.705  1.00 14.21           H  
ATOM   3147  HE1 HIS A 199       5.768  18.377   1.553  1.00 19.93           H  
ATOM   3148  HE2 HIS A 199       4.905  20.410   0.702  1.00 17.02           H  
ATOM   3149  N   TYR A 200       6.777  20.054  -4.038  1.00 10.62           N  
ANISOU 3149  N   TYR A 200     1388   1246   1402   -114   -594    -31       N  
ATOM   3150  CA  TYR A 200       7.337  21.388  -4.051  1.00 10.29           C  
ANISOU 3150  CA  TYR A 200     1330   1263   1318   -121   -539    -22       C  
ATOM   3151  C   TYR A 200       6.247  22.453  -3.960  1.00 14.27           C  
ANISOU 3151  C   TYR A 200     1837   1764   1822   -158   -421    -36       C  
ATOM   3152  O   TYR A 200       5.061  22.150  -4.073  1.00 12.70           O  
ANISOU 3152  O   TYR A 200     1624   1539   1662   -162   -383    -63       O  
ATOM   3153  CB  TYR A 200       8.195  21.594  -5.279  1.00 12.11           C  
ANISOU 3153  CB  TYR A 200     1471   1571   1559    -21   -576    -42       C  
ATOM   3154  CG  TYR A 200       7.430  21.444  -6.525  1.00 12.32           C  
ANISOU 3154  CG  TYR A 200     1426   1620   1635     62   -561    -82       C  
ATOM   3155  CD1 TYR A 200       7.400  20.249  -7.189  1.00 13.01           C  
ANISOU 3155  CD1 TYR A 200     1476   1701   1767    134   -639   -116       C  
ATOM   3156  CD2 TYR A 200       6.719  22.511  -7.037  1.00 19.75           C  
ANISOU 3156  CD2 TYR A 200     2344   2583   2577     74   -476    -91       C  
ATOM   3157  CE1 TYR A 200       6.671  20.113  -8.376  1.00 16.96           C  
ANISOU 3157  CE1 TYR A 200     1909   2228   2306    211   -631   -161       C  
ATOM   3158  CE2 TYR A 200       5.998  22.391  -8.180  1.00 28.79           C  
ANISOU 3158  CE2 TYR A 200     3427   3754   3761    155   -473   -129       C  
ATOM   3159  CZ  TYR A 200       5.973  21.189  -8.851  1.00 26.28           C  
ANISOU 3159  CZ  TYR A 200     3065   3440   3481    220   -549   -165       C  
ATOM   3160  OH  TYR A 200       5.242  21.102 -10.007  1.00 32.34           O  
ANISOU 3160  OH  TYR A 200     3769   4240   4280    300   -549   -208       O  
ATOM   3161  H   TYR A 200       5.994  19.993  -4.388  1.00 12.75           H  
ATOM   3162  HA  TYR A 200       7.910  21.489  -3.275  1.00 12.35           H  
ATOM   3163  HB2 TYR A 200       8.567  22.489  -5.260  1.00 14.53           H  
ATOM   3164  HB3 TYR A 200       8.908  20.936  -5.283  1.00 14.53           H  
ATOM   3165  HD1 TYR A 200       7.877  19.524  -6.855  1.00 15.62           H  
ATOM   3166  HD2 TYR A 200       6.730  23.325  -6.587  1.00 23.70           H  
ATOM   3167  HE1 TYR A 200       6.651  19.300  -8.828  1.00 20.35           H  
ATOM   3168  HE2 TYR A 200       5.527  23.121  -8.512  1.00 34.55           H  
ATOM   3169  HH  TYR A 200       4.872  21.838 -10.169  1.00 38.81           H  
ATOM   3170  N   LEU A 201       6.672  23.685  -3.709  1.00 10.70           N  
ANISOU 3170  N   LEU A 201     1402   1335   1328   -186   -369    -24       N  
ATOM   3171  CA  LEU A 201       5.782  24.847  -3.730  1.00 12.05           C  
ANISOU 3171  CA  LEU A 201     1576   1499   1502   -198   -267    -43       C  
ATOM   3172  C   LEU A 201       6.194  25.728  -4.902  1.00 11.30           C  
ANISOU 3172  C   LEU A 201     1429   1451   1413   -122   -258    -45       C  
ATOM   3173  O   LEU A 201       7.385  25.931  -5.108  1.00 11.86           O  
ANISOU 3173  O   LEU A 201     1492   1561   1454   -121   -296    -21       O  
ATOM   3174  CB  LEU A 201       5.949  25.666  -2.455  1.00 12.16           C  
ANISOU 3174  CB  LEU A 201     1675   1488   1458   -298   -213    -29       C  
ATOM   3175  CG  LEU A 201       5.925  24.901  -1.130  1.00 11.03           C  
ANISOU 3175  CG  LEU A 201     1609   1309   1274   -394   -230    -11       C  
ATOM   3176  CD1 LEU A 201       6.193  25.826   0.052  1.00 13.90           C  
ANISOU 3176  CD1 LEU A 201     2056   1661   1566   -487   -179     -4       C  
ATOM   3177  CD2 LEU A 201       4.593  24.123  -0.971  1.00 13.80           C  
ANISOU 3177  CD2 LEU A 201     1955   1630   1660   -413   -195    -34       C  
ATOM   3178  H   LEU A 201       7.488  23.881  -3.521  1.00 12.84           H  
ATOM   3179  HA  LEU A 201       4.857  24.574  -3.830  1.00 14.46           H  
ATOM   3180  HB2 LEU A 201       6.801  26.128  -2.503  1.00 14.59           H  
ATOM   3181  HB3 LEU A 201       5.233  26.319  -2.421  1.00 14.59           H  
ATOM   3182  HG  LEU A 201       6.639  24.245  -1.146  1.00 13.24           H  
ATOM   3183 HD11 LEU A 201       6.170  25.307   0.871  1.00 16.68           H  
ATOM   3184 HD12 LEU A 201       7.067  26.233  -0.058  1.00 16.68           H  
ATOM   3185 HD13 LEU A 201       5.509  26.513   0.076  1.00 16.68           H  
ATOM   3186 HD21 LEU A 201       4.603  23.649  -0.125  1.00 16.56           H  
ATOM   3187 HD22 LEU A 201       3.856  24.754  -0.988  1.00 16.56           H  
ATOM   3188 HD23 LEU A 201       4.507  23.493  -1.703  1.00 16.56           H  
ATOM   3189  N   HIS A 202       5.211  26.230  -5.648  1.00 10.24           N  
ANISOU 3189  N   HIS A 202     1260   1317   1315    -62   -211    -72       N  
ATOM   3190  CA  HIS A 202       5.416  27.305  -6.616  1.00 14.79           C  
ANISOU 3190  CA  HIS A 202     1818   1918   1883     -5   -188    -63       C  
ATOM   3191  C   HIS A 202       5.248  28.629  -5.884  1.00 12.69           C  
ANISOU 3191  C   HIS A 202     1626   1606   1592    -62   -114    -57       C  
ATOM   3192  O   HIS A 202       4.247  28.826  -5.183  1.00 17.13           O  
ANISOU 3192  O   HIS A 202     2212   2127   2170    -85    -61    -90       O  
ATOM   3193  CB  HIS A 202       4.320  27.311  -7.653  1.00 18.33           C  
ANISOU 3193  CB  HIS A 202     2212   2377   2377     91   -179    -95       C  
ATOM   3194  CG  HIS A 202       4.336  26.151  -8.588  1.00 21.16           C  
ANISOU 3194  CG  HIS A 202     2497   2780   2763    161   -249   -114       C  
ATOM   3195  ND1 HIS A 202       5.370  25.923  -9.467  1.00 26.58           N  
ANISOU 3195  ND1 HIS A 202     3148   3527   3424    206   -300    -97       N  
ATOM   3196  CD2 HIS A 202       3.404  25.198  -8.837  1.00 25.61           C  
ANISOU 3196  CD2 HIS A 202     3013   3340   3378    195   -273   -158       C  
ATOM   3197  CE1 HIS A 202       5.091  24.855 -10.196  1.00 26.73           C  
ANISOU 3197  CE1 HIS A 202     3107   3573   3477    272   -356   -133       C  
ATOM   3198  NE2 HIS A 202       3.904  24.399  -9.835  1.00 23.09           N  
ANISOU 3198  NE2 HIS A 202     2640   3070   3065    264   -344   -168       N  
ATOM   3199  H   HIS A 202       4.396  25.957  -5.610  1.00 12.29           H  
ATOM   3200  HA  HIS A 202       6.289  27.252  -7.037  1.00 17.75           H  
ATOM   3201  HB2 HIS A 202       3.463  27.308  -7.197  1.00 22.00           H  
ATOM   3202  HB3 HIS A 202       4.402  28.117  -8.185  1.00 22.00           H  
ATOM   3203  HD1 HIS A 202       6.088  26.392  -9.524  1.00 31.90           H  
ATOM   3204  HD2 HIS A 202       2.587  25.098  -8.405  1.00 30.74           H  
ATOM   3205  HE1 HIS A 202       5.638  24.487 -10.852  1.00 32.08           H  
ATOM   3206  HE2 HIS A 202       3.511  23.708 -10.166  1.00 27.71           H  
ATOM   3207  N   THR A 203       6.168  29.557  -6.107  1.00 13.16           N  
ANISOU 3207  N   THR A 203     1715   1674   1613    -82   -107    -24       N  
ATOM   3208  CA  THR A 203       6.048  30.887  -5.531  1.00 11.03           C  
ANISOU 3208  CA  THR A 203     1522   1346   1322   -131    -44    -23       C  
ATOM   3209  C   THR A 203       6.041  31.923  -6.619  1.00 13.10           C  
ANISOU 3209  C   THR A 203     1795   1598   1584    -73    -27     -1       C  
ATOM   3210  O   THR A 203       6.624  31.720  -7.695  1.00 15.69           O  
ANISOU 3210  O   THR A 203     2077   1983   1901    -30    -64     28       O  
ATOM   3211  CB  THR A 203       7.247  31.168  -4.632  1.00 13.66           C  
ANISOU 3211  CB  THR A 203     1906   1681   1603   -238    -53      1       C  
ATOM   3212  OG1 THR A 203       8.434  31.130  -5.444  1.00 16.94           O  
ANISOU 3212  OG1 THR A 203     2280   2161   1997   -234    -97     36       O  
ATOM   3213  CG2 THR A 203       7.328  30.128  -3.555  1.00 14.48           C  
ANISOU 3213  CG2 THR A 203     2017   1792   1694   -294    -83    -10       C  
ATOM   3214  H   THR A 203       6.871  29.442  -6.589  1.00 15.80           H  
ATOM   3215  HA  THR A 203       5.232  30.959  -5.013  1.00 13.23           H  
ATOM   3216  HB  THR A 203       7.154  32.041  -4.220  1.00 16.39           H  
ATOM   3217  HG1 THR A 203       9.111  31.282  -4.971  1.00 20.33           H  
ATOM   3218 HG21 THR A 203       8.090  30.304  -2.981  1.00 17.38           H  
ATOM   3219 HG22 THR A 203       6.520  30.142  -3.019  1.00 17.38           H  
ATOM   3220 HG23 THR A 203       7.428  29.248  -3.951  1.00 17.38           H  
ATOM   3221  N   HIS A 204       5.330  33.017  -6.385  1.00 11.53           N  
ANISOU 3221  N   HIS A 204     1658   1326   1396    -63     26    -18       N  
ATOM   3222  CA  HIS A 204       5.588  34.222  -7.155  1.00 14.57           C  
ANISOU 3222  CA  HIS A 204     2096   1675   1765    -40     39     19       C  
ATOM   3223  C   HIS A 204       5.194  35.438  -6.322  1.00 15.72           C  
ANISOU 3223  C   HIS A 204     2342   1719   1913    -76     94     -5       C  
ATOM   3224  O   HIS A 204       4.232  35.403  -5.559  1.00 14.69           O  
ANISOU 3224  O   HIS A 204     2216   1556   1811    -61    129    -64       O  
ATOM   3225  CB  HIS A 204       4.960  34.194  -8.559  1.00 22.28           C  
ANISOU 3225  CB  HIS A 204     3031   2673   2763     83     15     30       C  
ATOM   3226  CG  HIS A 204       3.470  34.210  -8.586  1.00 19.79           C  
ANISOU 3226  CG  HIS A 204     2693   2323   2503    179     29    -25       C  
ATOM   3227  ND1 HIS A 204       2.750  35.356  -8.839  1.00 17.58           N  
ANISOU 3227  ND1 HIS A 204     2473   1965   2239    245     50    -33       N  
ATOM   3228  CD2 HIS A 204       2.560  33.211  -8.464  1.00 26.60           C  
ANISOU 3228  CD2 HIS A 204     3473   3223   3410    223     19    -80       C  
ATOM   3229  CE1 HIS A 204       1.458  35.073  -8.826  1.00 23.88           C  
ANISOU 3229  CE1 HIS A 204     3215   2766   3093    331     54    -98       C  
ATOM   3230  NE2 HIS A 204       1.315  33.775  -8.614  1.00 22.65           N  
ANISOU 3230  NE2 HIS A 204     2970   2683   2954    311     39   -126       N  
ATOM   3231  H   HIS A 204       4.705  33.088  -5.798  1.00 13.84           H  
ATOM   3232  HA  HIS A 204       6.547  34.281  -7.288  1.00 17.49           H  
ATOM   3233  HB2 HIS A 204       5.270  34.971  -9.051  1.00 26.74           H  
ATOM   3234  HB3 HIS A 204       5.252  33.386  -9.011  1.00 26.74           H  
ATOM   3235  HD1 HIS A 204       3.087  36.138  -8.959  1.00 21.09           H  
ATOM   3236  HD2 HIS A 204       2.743  32.315  -8.299  1.00 31.92           H  
ATOM   3237  HE1 HIS A 204       0.767  35.681  -8.963  1.00 28.66           H  
ATOM   3238  HE2 HIS A 204       0.566  33.355  -8.563  1.00 27.18           H  
ATOM   3239  N   SER A 205       6.000  36.487  -6.455  1.00 18.19           N  
ANISOU 3239  N   SER A 205     2733   1987   2191   -133    104     37       N  
ATOM   3240  CA  SER A 205       5.965  37.627  -5.556  1.00 19.71           C  
ANISOU 3240  CA  SER A 205     3033   2079   2376   -195    148     14       C  
ATOM   3241  C   SER A 205       6.020  38.916  -6.346  1.00 19.11           C  
ANISOU 3241  C   SER A 205     3048   1917   2297   -169    155     56       C  
ATOM   3242  O   SER A 205       6.644  38.978  -7.407  1.00 18.96           O  
ANISOU 3242  O   SER A 205     3019   1932   2252   -166    130    123       O  
ATOM   3243  CB  SER A 205       7.157  37.572  -4.606  1.00 16.78           C  
ANISOU 3243  CB  SER A 205     2686   1731   1957   -338    146     22       C  
ATOM   3244  OG  SER A 205       7.159  36.388  -3.860  1.00 19.59           O  
ANISOU 3244  OG  SER A 205     2978   2158   2309   -362    129     -6       O  
ATOM   3245  H   SER A 205       6.590  36.560  -7.077  1.00 21.83           H  
ATOM   3246  HA  SER A 205       5.147  37.613  -5.035  1.00 23.65           H  
ATOM   3247  HB2 SER A 205       7.975  37.618  -5.125  1.00 20.13           H  
ATOM   3248  HB3 SER A 205       7.110  38.327  -3.998  1.00 20.13           H  
ATOM   3249  HG  SER A 205       7.201  35.725  -4.374  1.00 23.51           H  
ATOM   3250  N   LYS A 206       5.344  39.939  -5.841  1.00 17.99           N  
ANISOU 3250  N   LYS A 206     2998   1658   2178   -147    188     15       N  
ATOM   3251  CA  LYS A 206       5.445  41.284  -6.388  1.00 18.17           C  
ANISOU 3251  CA  LYS A 206     3142   1564   2197   -137    190     55       C  
ATOM   3252  C   LYS A 206       5.888  42.243  -5.296  1.00 18.74           C  
ANISOU 3252  C   LYS A 206     3327   1538   2255   -247    223     24       C  
ATOM   3253  O   LYS A 206       5.255  42.317  -4.231  1.00 19.47           O  
ANISOU 3253  O   LYS A 206     3434   1598   2368   -240    256    -61       O  
ATOM   3254  CB  LYS A 206       4.106  41.764  -6.966  1.00 25.28           C  
ANISOU 3254  CB  LYS A 206     4065   2391   3150     27    182     28       C  
ATOM   3255  CG  LYS A 206       4.235  43.119  -7.696  1.00 34.79           C  
ANISOU 3255  CG  LYS A 206     5411   3461   4344     49    167     88       C  
ATOM   3256  CD  LYS A 206       2.958  43.538  -8.389  1.00 40.99           C  
ANISOU 3256  CD  LYS A 206     6215   4180   5178    230    138     69       C  
ATOM   3257  H   LYS A 206       4.811  39.878  -5.169  1.00 21.59           H  
ATOM   3258  HA  LYS A 206       6.108  41.297  -7.096  1.00 21.80           H  
ATOM   3259  HB2 LYS A 206       3.782  41.108  -7.603  1.00 30.34           H  
ATOM   3260  HB3 LYS A 206       3.469  41.871  -6.243  1.00 30.34           H  
ATOM   3261  HG2 LYS A 206       4.464  43.806  -7.050  1.00 41.74           H  
ATOM   3262  HG3 LYS A 206       4.931  43.051  -8.368  1.00 41.74           H  
ATOM   3263  N   LEU A 207       6.960  42.981  -5.561  1.00 18.45           N  
ANISOU 3263  N   LEU A 207     3370   1460   2181   -355    219     87       N  
ATOM   3264  CA  LEU A 207       7.455  43.969  -4.607  1.00 21.13           C  
ANISOU 3264  CA  LEU A 207     3826   1697   2506   -472    244     57       C  
ATOM   3265  C   LEU A 207       6.991  45.353  -5.039  1.00 20.66           C  
ANISOU 3265  C   LEU A 207     3917   1462   2471   -421    246     71       C  
ATOM   3266  O   LEU A 207       6.962  45.653  -6.237  1.00 20.93           O  
ANISOU 3266  O   LEU A 207     3982   1470   2502   -367    222    150       O  
ATOM   3267  CB  LEU A 207       8.990  43.936  -4.518  1.00 18.51           C  
ANISOU 3267  CB  LEU A 207     3485   1428   2119   -645    235    108       C  
ATOM   3268  CG  LEU A 207       9.692  42.585  -4.427  1.00 17.05           C  
ANISOU 3268  CG  LEU A 207     3153   1420   1906   -686    212    117       C  
ATOM   3269  CD1 LEU A 207      11.185  42.763  -4.158  1.00 25.24           C  
ANISOU 3269  CD1 LEU A 207     4186   2509   2896   -857    203    144       C  
ATOM   3270  CD2 LEU A 207       9.055  41.703  -3.388  1.00 17.74           C  
ANISOU 3270  CD2 LEU A 207     3179   1554   2006   -647    216     41       C  
ATOM   3271  H   LEU A 207       7.419  42.929  -6.286  1.00 22.14           H  
ATOM   3272  HA  LEU A 207       7.091  43.782  -3.728  1.00 25.36           H  
ATOM   3273  HB2 LEU A 207       9.341  44.381  -5.305  1.00 22.21           H  
ATOM   3274  HB3 LEU A 207       9.251  44.439  -3.731  1.00 22.21           H  
ATOM   3275  HG  LEU A 207       9.603  42.136  -5.283  1.00 20.46           H  
ATOM   3276 HD11 LEU A 207      11.602  41.888  -4.106  1.00 30.29           H  
ATOM   3277 HD12 LEU A 207      11.577  43.274  -4.882  1.00 30.29           H  
ATOM   3278 HD13 LEU A 207      11.300  43.235  -3.318  1.00 30.29           H  
ATOM   3279 HD21 LEU A 207       9.527  40.856  -3.360  1.00 21.29           H  
ATOM   3280 HD22 LEU A 207       9.112  42.142  -2.524  1.00 21.29           H  
ATOM   3281 HD23 LEU A 207       8.126  41.557  -3.624  1.00 21.29           H  
ATOM   3282  N   SER A 208       6.640  46.205  -4.073  1.00 19.76           N  
ANISOU 3282  N   SER A 208     3906   1224   2377   -435    271     -5       N  
ATOM   3283  CA  SER A 208       6.198  47.567  -4.366  1.00 21.20           C  
ANISOU 3283  CA  SER A 208     4249   1215   2589   -381    265     -3       C  
ATOM   3284  C   SER A 208       6.560  48.495  -3.215  1.00 22.80           C  
ANISOU 3284  C   SER A 208     4573   1304   2788   -491    289    -72       C  
ATOM   3285  O   SER A 208       7.197  48.069  -2.255  1.00 22.70           O  
ANISOU 3285  O   SER A 208     4508   1377   2739   -610    308   -112       O  
ATOM   3286  CB  SER A 208       4.685  47.603  -4.596  1.00 23.94           C  
ANISOU 3286  CB  SER A 208     4578   1518   2998   -173    258    -63       C  
ATOM   3287  OG  SER A 208       4.015  47.027  -3.490  1.00 21.95           O  
ANISOU 3287  OG  SER A 208     4243   1331   2765   -142    297   -180       O  
ATOM   3288  H   SER A 208       6.651  46.016  -3.235  1.00 23.71           H  
ATOM   3289  HA  SER A 208       6.640  47.885  -5.169  1.00 25.43           H  
ATOM   3290  HB2 SER A 208       4.400  48.525  -4.697  1.00 28.72           H  
ATOM   3291  HB3 SER A 208       4.472  47.098  -5.396  1.00 28.72           H  
ATOM   3292  HG  SER A 208       3.185  47.047  -3.615  1.00 26.34           H  
ATOM   3293  N   LYS A 209       6.153  49.755  -3.328  1.00 25.65           N  
ANISOU 3293  N   LYS A 209     5039   1525   3180   -429    273    -83       N  
ATOM   3294  CA  LYS A 209       6.408  50.744  -2.282  1.00 26.06           C  
ANISOU 3294  CA  LYS A 209     5159   1509   3232   -500    283   -153       C  
ATOM   3295  C   LYS A 209       5.110  51.408  -1.874  1.00 30.93           C  
ANISOU 3295  C   LYS A 209     5822   2017   3912   -340    287   -255       C  
ATOM   3296  O   LYS A 209       4.189  51.522  -2.670  1.00 32.15           O  
ANISOU 3296  O   LYS A 209     5984   2119   4114   -179    262   -243       O  
ATOM   3297  CB  LYS A 209       7.404  51.801  -2.760  1.00 26.06           C  
ANISOU 3297  CB  LYS A 209     5249   1441   3212   -612    256    -69       C  
ATOM   3298  CG  LYS A 209       8.762  51.249  -3.149  1.00 28.86           C  
ANISOU 3298  CG  LYS A 209     5536   1924   3505   -774    255     18       C  
ATOM   3299  CD  LYS A 209       9.601  50.845  -1.961  1.00 26.24           C  
ANISOU 3299  CD  LYS A 209     5136   1700   3133   -910    272    -40       C  
ATOM   3300  CE  LYS A 209      10.997  50.498  -2.396  1.00 24.65           C  
ANISOU 3300  CE  LYS A 209     4862   1623   2881  -1057    262     38       C  
ATOM   3301  NZ  LYS A 209      11.882  49.995  -1.329  1.00 24.38           N  
ANISOU 3301  NZ  LYS A 209     4745   1713   2806  -1175    262    -12       N  
ATOM   3302  H   LYS A 209       5.725  50.066  -4.006  1.00 30.77           H  
ATOM   3303  HA  LYS A 209       6.782  50.301  -1.504  1.00 31.27           H  
ATOM   3304  HB2 LYS A 209       7.033  52.248  -3.537  1.00 31.27           H  
ATOM   3305  HB3 LYS A 209       7.540  52.445  -2.047  1.00 31.27           H  
ATOM   3306  HG2 LYS A 209       8.636  50.464  -3.706  1.00 34.63           H  
ATOM   3307  HG3 LYS A 209       9.249  51.928  -3.641  1.00 34.63           H  
ATOM   3308  HD2 LYS A 209       9.649  51.583  -1.333  1.00 31.48           H  
ATOM   3309  HD3 LYS A 209       9.208  50.065  -1.538  1.00 31.48           H  
ATOM   3310  HE2 LYS A 209      10.945  49.811  -3.079  1.00 29.58           H  
ATOM   3311  HE3 LYS A 209      11.410  51.294  -2.766  1.00 29.58           H  
ATOM   3312  HZ1 LYS A 209      11.966  50.608  -0.689  1.00 29.26           H  
ATOM   3313  HZ2 LYS A 209      11.541  49.253  -0.975  1.00 29.26           H  
ATOM   3314  HZ3 LYS A 209      12.687  49.813  -1.662  1.00 29.26           H  
ATOM   3315  N   ASP A 210       5.047  51.807  -0.608  1.00 27.94           N  
ANISOU 3315  N   ASP A 210     5459   1624   3532   -379    313   -361       N  
ATOM   3316  CA  ASP A 210       4.004  52.665  -0.073  1.00 27.79           C  
ANISOU 3316  CA  ASP A 210     5486   1502   3571   -252    317   -471       C  
ATOM   3317  C   ASP A 210       4.362  54.124  -0.335  1.00 29.61           C  
ANISOU 3317  C   ASP A 210     5853   1573   3825   -276    275   -437       C  
ATOM   3318  O   ASP A 210       5.365  54.622   0.184  1.00 31.07           O  
ANISOU 3318  O   ASP A 210     6091   1742   3973   -429    276   -426       O  
ATOM   3319  CB  ASP A 210       3.919  52.412   1.427  1.00 27.72           C  
ANISOU 3319  CB  ASP A 210     5437   1563   3533   -308    366   -594       C  
ATOM   3320  CG  ASP A 210       2.855  53.244   2.118  1.00 34.59           C  
ANISOU 3320  CG  ASP A 210     6336   2349   4458   -183    378   -729       C  
ATOM   3321  OD1 ASP A 210       2.306  54.196   1.519  1.00 32.29           O  
ANISOU 3321  OD1 ASP A 210     6110   1925   4234    -66    338   -729       O  
ATOM   3322  OD2 ASP A 210       2.597  52.947   3.308  1.00 36.03           O  
ANISOU 3322  OD2 ASP A 210     6473   2606   4611   -207    426   -837       O  
ATOM   3323  H   ASP A 210       5.627  51.580  -0.016  1.00 33.53           H  
ATOM   3324  HA  ASP A 210       3.150  52.460  -0.485  1.00 33.35           H  
ATOM   3325  HB2 ASP A 210       3.711  51.476   1.577  1.00 33.26           H  
ATOM   3326  HB3 ASP A 210       4.775  52.628   1.831  1.00 33.26           H  
ATOM   3327  N   PRO A 211       3.543  54.828  -1.131  1.00 38.64           N  
ANISOU 3327  N   PRO A 211     7052   2599   5032   -122    235   -423       N  
ATOM   3328  CA  PRO A 211       3.892  56.217  -1.468  1.00 43.21           C  
ANISOU 3328  CA  PRO A 211     7772   3013   5631   -148    191   -379       C  
ATOM   3329  C   PRO A 211       3.965  57.154  -0.254  1.00 43.27           C  
ANISOU 3329  C   PRO A 211     7846   2936   5658   -193    203   -492       C  
ATOM   3330  O   PRO A 211       4.613  58.203  -0.314  1.00 48.59           O  
ANISOU 3330  O   PRO A 211     8636   3492   6332   -279    176   -454       O  
ATOM   3331  CB  PRO A 211       2.766  56.644  -2.421  1.00 42.85           C  
ANISOU 3331  CB  PRO A 211     7752   2876   5653     57    142   -364       C  
ATOM   3332  CG  PRO A 211       1.656  55.653  -2.187  1.00 40.59           C  
ANISOU 3332  CG  PRO A 211     7323   2701   5397    203    169   -456       C  
ATOM   3333  CD  PRO A 211       2.311  54.382  -1.811  1.00 34.27           C  
ANISOU 3333  CD  PRO A 211     6429   2063   4530     77    220   -440       C  
ATOM   3334  HA  PRO A 211       4.738  56.244  -1.942  1.00 51.85           H  
ATOM   3335  HB2 PRO A 211       2.475  57.544  -2.202  1.00 51.42           H  
ATOM   3336  HB3 PRO A 211       3.079  56.598  -3.338  1.00 51.42           H  
ATOM   3337  HG2 PRO A 211       1.087  55.968  -1.466  1.00 48.70           H  
ATOM   3338  HG3 PRO A 211       1.142  55.543  -3.002  1.00 48.70           H  
ATOM   3339  HD2 PRO A 211       1.750  53.879  -1.201  1.00 41.13           H  
ATOM   3340  HD3 PRO A 211       2.529  53.867  -2.604  1.00 41.13           H  
ATOM   3341  N   ASN A 212       3.322  56.757   0.836  1.00 42.79           N  
ANISOU 3341  N   ASN A 212     7711   2941   5607   -143    245   -630       N  
ATOM   3342  CA  ASN A 212       3.283  57.559   2.045  1.00 43.39           C  
ANISOU 3342  CA  ASN A 212     7838   2953   5695   -171    259   -754       C  
ATOM   3343  C   ASN A 212       4.293  57.117   3.100  1.00 42.76           C  
ANISOU 3343  C   ASN A 212     7732   2982   5533   -358    296   -776       C  
ATOM   3344  O   ASN A 212       4.276  57.619   4.223  1.00 40.97           O  
ANISOU 3344  O   ASN A 212     7535   2731   5301   -387    313   -887       O  
ATOM   3345  CB  ASN A 212       1.873  57.508   2.626  1.00 47.97           C  
ANISOU 3345  CB  ASN A 212     8349   3545   6334     10    283   -908       C  
ATOM   3346  CG  ASN A 212       0.841  58.057   1.666  1.00 52.23           C  
ANISOU 3346  CG  ASN A 212     8903   3978   6964    206    238   -902       C  
ATOM   3347  OD1 ASN A 212       1.049  59.106   1.051  1.00 54.15           O  
ANISOU 3347  OD1 ASN A 212     9268   4064   7243    218    184   -839       O  
ATOM   3348  ND2 ASN A 212      -0.269  57.342   1.512  1.00 54.10           N  
ANISOU 3348  ND2 ASN A 212     9013   4307   7237    358    257   -963       N  
ATOM   3349  H   ASN A 212       2.894  56.014   0.899  1.00 51.35           H  
ATOM   3350  HA  ASN A 212       3.477  58.481   1.815  1.00 52.07           H  
ATOM   3351  HB2 ASN A 212       1.643  56.586   2.822  1.00 57.57           H  
ATOM   3352  HB3 ASN A 212       1.844  58.039   3.437  1.00 57.57           H  
ATOM   3353 HD21 ASN A 212      -0.371  56.607   1.947  1.00 64.92           H  
ATOM   3354 HD22 ASN A 212      -0.885  57.614   0.977  1.00 64.92           H  
ATOM   3355  N   GLU A 213       5.163  56.174   2.755  1.00 32.75           N  
ANISOU 3355  N   GLU A 213     6404   1840   4201   -477    306   -675       N  
ATOM   3356  CA  GLU A 213       6.132  55.664   3.727  1.00 32.07           C  
ANISOU 3356  CA  GLU A 213     6276   1875   4036   -646    331   -691       C  
ATOM   3357  C   GLU A 213       7.507  56.253   3.474  1.00 32.92           C  
ANISOU 3357  C   GLU A 213     6445   1951   4111   -815    300   -603       C  
ATOM   3358  O   GLU A 213       8.089  56.062   2.402  1.00 32.18           O  
ANISOU 3358  O   GLU A 213     6344   1875   4008   -860    280   -481       O  
ATOM   3359  CB  GLU A 213       6.204  54.140   3.695  1.00 29.99           C  
ANISOU 3359  CB  GLU A 213     5883   1791   3722   -669    361   -659       C  
ATOM   3360  CG  GLU A 213       7.178  53.558   4.704  1.00 29.39           C  
ANISOU 3360  CG  GLU A 213     5757   1847   3562   -829    376   -672       C  
ATOM   3361  CD  GLU A 213       6.838  53.924   6.146  1.00 30.34           C  
ANISOU 3361  CD  GLU A 213     5902   1966   3660   -834    404   -807       C  
ATOM   3362  OE1 GLU A 213       5.813  53.437   6.650  1.00 30.06           O  
ANISOU 3362  OE1 GLU A 213     5816   1978   3627   -736    445   -893       O  
ATOM   3363  OE2 GLU A 213       7.599  54.706   6.768  1.00 31.48           O  
ANISOU 3363  OE2 GLU A 213     6112   2068   3782   -938    386   -830       O  
ATOM   3364  H   GLU A 213       5.215  55.815   1.976  1.00 39.30           H  
ATOM   3365  HA  GLU A 213       5.853  55.930   4.617  1.00 38.49           H  
ATOM   3366  HB2 GLU A 213       5.324  53.781   3.889  1.00 35.99           H  
ATOM   3367  HB3 GLU A 213       6.488  53.859   2.811  1.00 35.99           H  
ATOM   3368  HG2 GLU A 213       7.166  52.591   4.631  1.00 35.26           H  
ATOM   3369  HG3 GLU A 213       8.068  53.893   4.512  1.00 35.26           H  
ATOM   3370  N   LYS A 214       8.019  56.956   4.482  1.00 34.65           N  
ANISOU 3370  N   LYS A 214     6719   2135   4311   -908    299   -672       N  
ATOM   3371  CA  LYS A 214       9.296  57.641   4.373  1.00 34.87           C  
ANISOU 3371  CA  LYS A 214     6805   2129   4315  -1071    271   -610       C  
ATOM   3372  C   LYS A 214      10.465  56.736   4.787  1.00 34.90           C  
ANISOU 3372  C   LYS A 214     6708   2316   4237  -1227    278   -575       C  
ATOM   3373  O   LYS A 214      11.599  56.900   4.327  1.00 35.08           O  
ANISOU 3373  O   LYS A 214     6727   2368   4235  -1356    258   -495       O  
ATOM   3374  CB  LYS A 214       9.259  58.910   5.232  1.00 36.91           C  
ANISOU 3374  CB  LYS A 214     7176   2248   4601  -1089    259   -709       C  
ATOM   3375  CG  LYS A 214       8.217  59.928   4.777  1.00 45.90           C  
ANISOU 3375  CG  LYS A 214     8419   3192   5829   -936    239   -743       C  
ATOM   3376  H   LYS A 214       7.639  57.049   5.247  1.00 41.58           H  
ATOM   3377  HA  LYS A 214       9.434  57.906   3.451  1.00 41.84           H  
ATOM   3378  HB2 LYS A 214       9.053  58.662   6.147  1.00 44.29           H  
ATOM   3379  HB3 LYS A 214      10.129  59.338   5.195  1.00 44.29           H  
ATOM   3380  N   ARG A 215      10.198  55.774   5.657  1.00 32.49           N  
ANISOU 3380  N   ARG A 215     6317   2139   3888  -1212    305   -638       N  
ATOM   3381  CA  ARG A 215      11.242  54.853   6.057  1.00 31.43           C  
ANISOU 3381  CA  ARG A 215     6085   2179   3679  -1339    300   -605       C  
ATOM   3382  C   ARG A 215      11.560  53.869   4.927  1.00 29.87           C  
ANISOU 3382  C   ARG A 215     5793   2082   3475  -1338    293   -493       C  
ATOM   3383  O   ARG A 215      10.768  53.669   4.008  1.00 29.31           O  
ANISOU 3383  O   ARG A 215     5722   1968   3448  -1225    301   -454       O  
ATOM   3384  CB  ARG A 215      10.821  54.097   7.316  1.00 30.84           C  
ANISOU 3384  CB  ARG A 215     5957   2207   3552  -1322    327   -697       C  
ATOM   3385  CG  ARG A 215      10.744  54.994   8.543  1.00 32.45           C  
ANISOU 3385  CG  ARG A 215     6242   2344   3743  -1350    332   -811       C  
ATOM   3386  CD  ARG A 215      10.058  54.263   9.674  1.00 35.38           C  
ANISOU 3386  CD  ARG A 215     6569   2810   4062  -1307    370   -902       C  
ATOM   3387  NE  ARG A 215       8.684  53.962   9.300  1.00 43.46           N  
ANISOU 3387  NE  ARG A 215     7574   3803   5134  -1149    410   -935       N  
ATOM   3388  CZ  ARG A 215       7.770  53.448  10.119  1.00 51.46           C  
ANISOU 3388  CZ  ARG A 215     8553   4879   6119  -1082    458  -1025       C  
ATOM   3389  NH1 ARG A 215       8.083  53.170  11.382  1.00 48.64           N  
ANISOU 3389  NH1 ARG A 215     8188   4616   5679  -1162    471  -1082       N  
ATOM   3390  NH2 ARG A 215       6.538  53.214   9.671  1.00 49.46           N  
ANISOU 3390  NH2 ARG A 215     8270   4604   5919   -935    492  -1057       N  
ATOM   3391  H   ARG A 215       9.433  55.635   6.023  1.00 38.99           H  
ATOM   3392  HA  ARG A 215      12.048  55.353   6.259  1.00 37.72           H  
ATOM   3393  HB2 ARG A 215       9.944  53.708   7.173  1.00 37.00           H  
ATOM   3394  HB3 ARG A 215      11.469  53.398   7.496  1.00 37.00           H  
ATOM   3395  HG2 ARG A 215      11.640  55.233   8.828  1.00 38.94           H  
ATOM   3396  HG3 ARG A 215      10.230  55.789   8.333  1.00 38.94           H  
ATOM   3397  HD2 ARG A 215      10.520  53.429   9.852  1.00 42.45           H  
ATOM   3398  HD3 ARG A 215      10.048  54.824  10.466  1.00 42.45           H  
ATOM   3399  HE  ARG A 215       8.445  54.128   8.491  1.00 52.15           H  
ATOM   3400 HH11 ARG A 215       8.878  53.322  11.671  1.00 58.37           H  
ATOM   3401 HH12 ARG A 215       7.489  52.838  11.908  1.00 58.37           H  
ATOM   3402 HH21 ARG A 215       6.336  53.394   8.854  1.00 59.35           H  
ATOM   3403 HH22 ARG A 215       5.945  52.881  10.197  1.00 59.35           H  
ATOM   3404  N   ASP A 216      12.739  53.273   5.010  1.00 29.31           N  
ANISOU 3404  N   ASP A 216     5639   2148   3349  -1460    273   -448       N  
ATOM   3405  CA  ASP A 216      13.166  52.255   4.066  1.00 27.91           C  
ANISOU 3405  CA  ASP A 216     5355   2089   3160  -1467    262   -356       C  
ATOM   3406  C   ASP A 216      12.281  51.046   4.313  1.00 26.39           C  
ANISOU 3406  C   ASP A 216     5091   1977   2960  -1368    282   -382       C  
ATOM   3407  O   ASP A 216      12.176  50.571   5.451  1.00 26.17           O  
ANISOU 3407  O   ASP A 216     5037   2017   2888  -1382    290   -449       O  
ATOM   3408  CB  ASP A 216      14.633  51.911   4.332  1.00 27.91           C  
ANISOU 3408  CB  ASP A 216     5274   2225   3106  -1612    231   -330       C  
ATOM   3409  CG  ASP A 216      15.312  51.258   3.143  1.00 27.88           C  
ANISOU 3409  CG  ASP A 216     5174   2318   3100  -1639    217   -233       C  
ATOM   3410  OD1 ASP A 216      14.648  51.085   2.097  1.00 26.50           O  
ANISOU 3410  OD1 ASP A 216     5006   2102   2962  -1550    231   -179       O  
ATOM   3411  OD2 ASP A 216      16.518  50.940   3.274  1.00 27.16           O  
ANISOU 3411  OD2 ASP A 216     5002   2348   2971  -1747    190   -216       O  
ATOM   3412  H   ASP A 216      13.322  53.445   5.618  1.00 35.17           H  
ATOM   3413  HA  ASP A 216      13.058  52.562   3.152  1.00 33.49           H  
ATOM   3414  HB2 ASP A 216      15.115  52.726   4.541  1.00 33.49           H  
ATOM   3415  HB3 ASP A 216      14.682  51.295   5.080  1.00 33.49           H  
ATOM   3416  N   HIS A 217      11.631  50.548   3.270  1.00 25.48           N  
ANISOU 3416  N   HIS A 217     4947   1851   2881  -1272    291   -330       N  
ATOM   3417  CA  HIS A 217      10.585  49.549   3.458  1.00 24.30           C  
ANISOU 3417  CA  HIS A 217     4747   1748   2739  -1167    317   -366       C  
ATOM   3418  C   HIS A 217      10.379  48.746   2.183  1.00 23.13           C  
ANISOU 3418  C   HIS A 217     4534   1637   2616  -1105    310   -284       C  
ATOM   3419  O   HIS A 217      10.942  49.050   1.113  1.00 23.31           O  
ANISOU 3419  O   HIS A 217     4562   1644   2651  -1132    290   -199       O  
ATOM   3420  CB  HIS A 217       9.265  50.239   3.812  1.00 25.08           C  
ANISOU 3420  CB  HIS A 217     4930   1718   2884  -1047    351   -452       C  
ATOM   3421  CG  HIS A 217       8.715  51.062   2.690  1.00 25.75           C  
ANISOU 3421  CG  HIS A 217     5088   1660   3036   -951    343   -412       C  
ATOM   3422  ND1 HIS A 217       9.315  52.229   2.274  1.00 27.07           N  
ANISOU 3422  ND1 HIS A 217     5344   1723   3217  -1006    317   -370       N  
ATOM   3423  CD2 HIS A 217       7.655  50.868   1.864  1.00 25.38           C  
ANISOU 3423  CD2 HIS A 217     5040   1562   3042   -804    351   -401       C  
ATOM   3424  CE1 HIS A 217       8.636  52.734   1.261  1.00 27.52           C  
ANISOU 3424  CE1 HIS A 217     5461   1666   3330   -896    307   -330       C  
ATOM   3425  NE2 HIS A 217       7.622  51.937   0.999  1.00 26.52           N  
ANISOU 3425  NE2 HIS A 217     5278   1569   3228   -766    324   -350       N  
ATOM   3426  H   HIS A 217      11.773  50.767   2.451  1.00 30.57           H  
ATOM   3427  HA  HIS A 217      10.829  48.945   4.177  1.00 29.16           H  
ATOM   3428  HB2 HIS A 217       8.606  49.563   4.037  1.00 30.10           H  
ATOM   3429  HB3 HIS A 217       9.409  50.826   4.570  1.00 30.10           H  
ATOM   3430  HD1 HIS A 217      10.016  52.580   2.627  1.00 32.48           H  
ATOM   3431  HD2 HIS A 217       7.051  50.162   1.895  1.00 30.46           H  
ATOM   3432  HE1 HIS A 217       8.835  53.524   0.813  1.00 33.03           H  
ATOM   3433  HE2 HIS A 217       7.042  52.056   0.376  1.00 31.82           H  
ATOM   3434  N   MET A 218       9.531  47.734   2.321  1.00 22.06           N  
ANISOU 3434  N   MET A 218     4342   1554   2487  -1024    331   -314       N  
ATOM   3435  CA  MET A 218       9.163  46.867   1.218  1.00 21.87           C  
ANISOU 3435  CA  MET A 218     4256   1564   2491   -951    326   -252       C  
ATOM   3436  C   MET A 218       7.739  46.420   1.444  1.00 20.57           C  
ANISOU 3436  C   MET A 218     4085   1370   2360   -821    366   -325       C  
ATOM   3437  O   MET A 218       7.392  45.914   2.510  1.00 20.37           O  
ANISOU 3437  O   MET A 218     4030   1405   2306   -832    392   -400       O  
ATOM   3438  CB  MET A 218      10.077  45.649   1.145  1.00 21.56           C  
ANISOU 3438  CB  MET A 218     4099   1684   2409  -1031    296   -201       C  
ATOM   3439  CG  MET A 218       9.615  44.597   0.122  1.00 24.36           C  
ANISOU 3439  CG  MET A 218     4370   2094   2791   -944    290   -148       C  
ATOM   3440  SD  MET A 218      10.745  43.211  -0.016  1.00 19.36           S  
ANISOU 3440  SD  MET A 218     3585   1656   2116  -1014    240    -90       S  
ATOM   3441  CE  MET A 218      10.650  42.406   1.583  1.00 20.05           C  
ANISOU 3441  CE  MET A 218     3648   1815   2156  -1059    237   -168       C  
ATOM   3442  H   MET A 218       9.149  47.527   3.063  1.00 26.48           H  
ATOM   3443  HA  MET A 218       9.225  47.355   0.382  1.00 26.25           H  
ATOM   3444  HB2 MET A 218      10.967  45.940   0.891  1.00 25.87           H  
ATOM   3445  HB3 MET A 218      10.104  45.225   2.016  1.00 25.87           H  
ATOM   3446  HG2 MET A 218       8.750  44.252   0.393  1.00 29.23           H  
ATOM   3447  HG3 MET A 218       9.546  45.015  -0.751  1.00 29.23           H  
ATOM   3448  HE1 MET A 218      11.242  41.638   1.585  1.00 24.06           H  
ATOM   3449  HE2 MET A 218      10.921  43.035   2.270  1.00 24.06           H  
ATOM   3450  HE3 MET A 218       9.736  42.121   1.738  1.00 24.06           H  
ATOM   3451  N   VAL A 219       6.910  46.636   0.435  1.00 20.62           N  
ANISOU 3451  N   VAL A 219     4115   1294   2424   -692    369   -304       N  
ATOM   3452  CA  VAL A 219       5.587  46.057   0.402  1.00 20.19           C  
ANISOU 3452  CA  VAL A 219     3981   1281   2408   -536    393   -357       C  
ATOM   3453  C   VAL A 219       5.635  44.796  -0.462  1.00 18.85           C  
ANISOU 3453  C   VAL A 219     3668   1255   2241   -493    365   -279       C  
ATOM   3454  O   VAL A 219       6.260  44.776  -1.540  1.00 18.61           O  
ANISOU 3454  O   VAL A 219     3625   1236   2208   -503    327   -182       O  
ATOM   3455  CB  VAL A 219       4.570  47.035  -0.172  1.00 21.20           C  
ANISOU 3455  CB  VAL A 219     4187   1265   2603   -385    396   -387       C  
ATOM   3456  CG1 VAL A 219       3.199  46.373  -0.303  1.00 20.81           C  
ANISOU 3456  CG1 VAL A 219     4027   1282   2600   -221    417   -446       C  
ATOM   3457  CG2 VAL A 219       4.479  48.308   0.716  1.00 22.70           C  
ANISOU 3457  CG2 VAL A 219     4497   1329   2797   -407    413   -471       C  
ATOM   3458  H   VAL A 219       7.096  47.122  -0.249  1.00 24.74           H  
ATOM   3459  HA  VAL A 219       5.313  45.811   1.299  1.00 24.22           H  
ATOM   3460  HB  VAL A 219       4.858  47.307  -1.058  1.00 25.44           H  
ATOM   3461 HG11 VAL A 219       2.572  47.016  -0.670  1.00 24.98           H  
ATOM   3462 HG12 VAL A 219       3.273  45.608  -0.894  1.00 24.98           H  
ATOM   3463 HG13 VAL A 219       2.902  46.086   0.575  1.00 24.98           H  
ATOM   3464 HG21 VAL A 219       3.827  48.915   0.332  1.00 27.24           H  
ATOM   3465 HG22 VAL A 219       4.205  48.050   1.610  1.00 27.24           H  
ATOM   3466 HG23 VAL A 219       5.350  48.734   0.747  1.00 27.24           H  
ATOM   3467  N   LEU A 220       4.956  43.755  -0.004  1.00 18.68           N  
ANISOU 3467  N   LEU A 220     3540   1337   2220   -447    385   -326       N  
ATOM   3468  CA  LEU A 220       5.095  42.444  -0.608  1.00 16.94           C  
ANISOU 3468  CA  LEU A 220     3188   1252   1996   -428    355   -265       C  
ATOM   3469  C   LEU A 220       3.740  41.780  -0.811  1.00 19.19           C  
ANISOU 3469  C   LEU A 220     3380   1583   2329   -292    375   -313       C  
ATOM   3470  O   LEU A 220       2.888  41.761   0.086  1.00 17.27           O  
ANISOU 3470  O   LEU A 220     3132   1340   2092   -271    427   -406       O  
ATOM   3471  CB  LEU A 220       5.970  41.569   0.294  1.00 19.12           C  
ANISOU 3471  CB  LEU A 220     3425   1631   2210   -559    344   -259       C  
ATOM   3472  CG  LEU A 220       6.114  40.098  -0.109  1.00 25.07           C  
ANISOU 3472  CG  LEU A 220     4049   2516   2959   -541    308   -211       C  
ATOM   3473  CD1 LEU A 220       6.821  39.979  -1.456  1.00 23.11           C  
ANISOU 3473  CD1 LEU A 220     3759   2299   2722   -520    259   -121       C  
ATOM   3474  CD2 LEU A 220       6.861  39.307   0.947  1.00 25.55           C  
ANISOU 3474  CD2 LEU A 220     4093   2656   2957   -657    290   -215       C  
ATOM   3475  H   LEU A 220       4.408  43.783   0.658  1.00 22.41           H  
ATOM   3476  HA  LEU A 220       5.529  42.529  -1.471  1.00 20.33           H  
ATOM   3477  HB2 LEU A 220       6.862  41.950   0.313  1.00 22.95           H  
ATOM   3478  HB3 LEU A 220       5.596  41.585   1.189  1.00 22.95           H  
ATOM   3479  HG  LEU A 220       5.230  39.711  -0.202  1.00 30.08           H  
ATOM   3480 HD11 LEU A 220       6.900  39.040  -1.688  1.00 27.73           H  
ATOM   3481 HD12 LEU A 220       6.299  40.444  -2.128  1.00 27.73           H  
ATOM   3482 HD13 LEU A 220       7.702  40.378  -1.386  1.00 27.73           H  
ATOM   3483 HD21 LEU A 220       6.932  38.384   0.658  1.00 30.65           H  
ATOM   3484 HD22 LEU A 220       7.745  39.688   1.060  1.00 30.65           H  
ATOM   3485 HD23 LEU A 220       6.370  39.355   1.783  1.00 30.65           H  
ATOM   3486  N   LEU A 221       3.542  41.238  -2.000  1.00 16.89           N  
ANISOU 3486  N   LEU A 221     3011   1339   2068   -207    338   -255       N  
ATOM   3487  CA  LEU A 221       2.369  40.444  -2.279  1.00 16.57           C  
ANISOU 3487  CA  LEU A 221     2862   1362   2072    -94    346   -296       C  
ATOM   3488  C   LEU A 221       2.876  39.133  -2.822  1.00 15.33           C  
ANISOU 3488  C   LEU A 221     2603   1322   1900   -118    302   -232       C  
ATOM   3489  O   LEU A 221       3.609  39.115  -3.834  1.00 20.30           O  
ANISOU 3489  O   LEU A 221     3227   1966   2519   -114    255   -152       O  
ATOM   3490  CB  LEU A 221       1.452  41.131  -3.300  1.00 16.82           C  
ANISOU 3490  CB  LEU A 221     2901   1327   2164     64    329   -303       C  
ATOM   3491  CG  LEU A 221       0.295  40.255  -3.798  1.00 16.03           C  
ANISOU 3491  CG  LEU A 221     2669   1309   2114    182    323   -341       C  
ATOM   3492  CD1 LEU A 221      -0.669  39.934  -2.684  1.00 20.35           C  
ANISOU 3492  CD1 LEU A 221     3162   1892   2679    181    389   -453       C  
ATOM   3493  CD2 LEU A 221      -0.451  40.948  -4.942  1.00 21.24           C  
ANISOU 3493  CD2 LEU A 221     3339   1907   2824    343    283   -335       C  
ATOM   3494  H   LEU A 221       4.080  41.318  -2.666  1.00 20.27           H  
ATOM   3495  HA  LEU A 221       1.872  40.281  -1.462  1.00 19.89           H  
ATOM   3496  HB2 LEU A 221       1.067  41.922  -2.890  1.00 20.19           H  
ATOM   3497  HB3 LEU A 221       1.982  41.386  -4.071  1.00 20.19           H  
ATOM   3498  HG  LEU A 221       0.653  39.420  -4.136  1.00 19.24           H  
ATOM   3499 HD11 LEU A 221      -1.385  39.381  -3.036  1.00 24.42           H  
ATOM   3500 HD12 LEU A 221      -0.196  39.458  -1.985  1.00 24.42           H  
ATOM   3501 HD13 LEU A 221      -1.033  40.762  -2.333  1.00 24.42           H  
ATOM   3502 HD21 LEU A 221      -1.175  40.376  -5.239  1.00 25.49           H  
ATOM   3503 HD22 LEU A 221      -0.805  41.792  -4.622  1.00 25.49           H  
ATOM   3504 HD23 LEU A 221       0.168  41.105  -5.673  1.00 25.49           H  
ATOM   3505  N   GLU A 222       2.466  38.028  -2.219  1.00 14.09           N  
ANISOU 3505  N   GLU A 222     2367   1247   1741   -139    318   -267       N  
ATOM   3506  CA  GLU A 222       3.056  36.741  -2.580  1.00 13.64           C  
ANISOU 3506  CA  GLU A 222     2229   1287   1668   -171    269   -212       C  
ATOM   3507  C   GLU A 222       2.023  35.631  -2.643  1.00 12.85           C  
ANISOU 3507  C   GLU A 222     2025   1251   1605   -115    275   -251       C  
ATOM   3508  O   GLU A 222       1.072  35.597  -1.834  1.00 16.00           O  
ANISOU 3508  O   GLU A 222     2414   1649   2016   -117    333   -325       O  
ATOM   3509  CB  GLU A 222       4.125  36.430  -1.526  1.00 16.73           C  
ANISOU 3509  CB  GLU A 222     2660   1702   1994   -311    263   -195       C  
ATOM   3510  CG  GLU A 222       4.888  35.141  -1.701  1.00 20.87           C  
ANISOU 3510  CG  GLU A 222     3118   2315   2499   -348    203   -144       C  
ATOM   3511  CD  GLU A 222       6.021  35.044  -0.669  1.00 35.31           C  
ANISOU 3511  CD  GLU A 222     4997   4160   4261   -477    184   -128       C  
ATOM   3512  OE1 GLU A 222       6.898  35.937  -0.670  1.00 38.09           O  
ANISOU 3512  OE1 GLU A 222     5405   4482   4588   -532    177   -108       O  
ATOM   3513  OE2 GLU A 222       6.016  34.096   0.146  1.00 32.77           O  
ANISOU 3513  OE2 GLU A 222     4663   3878   3911   -526    171   -135       O  
ATOM   3514  H   GLU A 222       1.861  37.991  -1.608  1.00 16.91           H  
ATOM   3515  HA  GLU A 222       3.486  36.812  -3.446  1.00 16.37           H  
ATOM   3516  HB2 GLU A 222       4.774  37.151  -1.531  1.00 20.08           H  
ATOM   3517  HB3 GLU A 222       3.693  36.393  -0.658  1.00 20.08           H  
ATOM   3518  HG2 GLU A 222       4.288  34.390  -1.570  1.00 25.05           H  
ATOM   3519  HG3 GLU A 222       5.278  35.113  -2.588  1.00 25.05           H  
ATOM   3520  N   PHE A 223       2.223  34.716  -3.585  1.00 12.55           N  
ANISOU 3520  N   PHE A 223     1910   1275   1583    -74    219   -207       N  
ATOM   3521  CA  PHE A 223       1.363  33.551  -3.779  1.00 11.92           C  
ANISOU 3521  CA  PHE A 223     1731   1255   1541    -33    210   -237       C  
ATOM   3522  C   PHE A 223       2.192  32.285  -3.758  1.00 17.10           C  
ANISOU 3522  C   PHE A 223     2355   1971   2173    -93    155   -191       C  
ATOM   3523  O   PHE A 223       3.220  32.192  -4.436  1.00 14.69           O  
ANISOU 3523  O   PHE A 223     2047   1687   1848    -90    102   -134       O  
ATOM   3524  CB  PHE A 223       0.629  33.612  -5.125  1.00 12.55           C  
ANISOU 3524  CB  PHE A 223     1744   1348   1675    104    180   -244       C  
ATOM   3525  CG  PHE A 223      -0.321  34.746  -5.202  1.00 12.75           C  
ANISOU 3525  CG  PHE A 223     1793   1316   1736    189    218   -296       C  
ATOM   3526  CD1 PHE A 223      -1.619  34.592  -4.787  1.00 14.75           C  
ANISOU 3526  CD1 PHE A 223     1982   1585   2035    230    262   -384       C  
ATOM   3527  CD2 PHE A 223       0.115  35.991  -5.595  1.00 14.27           C  
ANISOU 3527  CD2 PHE A 223     2076   1432   1914    219    211   -262       C  
ATOM   3528  CE1 PHE A 223      -2.501  35.670  -4.833  1.00 14.65           C  
ANISOU 3528  CE1 PHE A 223     1985   1521   2061    326    292   -446       C  
ATOM   3529  CE2 PHE A 223      -0.744  37.063  -5.616  1.00 18.35           C  
ANISOU 3529  CE2 PHE A 223     2628   1877   2466    308    236   -313       C  
ATOM   3530  CZ  PHE A 223      -2.044  36.903  -5.233  1.00 14.57           C  
ANISOU 3530  CZ  PHE A 223     2076   1420   2038    370    273   -409       C  
ATOM   3531  H   PHE A 223       2.875  34.750  -4.145  1.00 15.06           H  
ATOM   3532  HA  PHE A 223       0.706  33.507  -3.067  1.00 14.30           H  
ATOM   3533  HB2 PHE A 223       1.280  33.715  -5.836  1.00 15.05           H  
ATOM   3534  HB3 PHE A 223       0.128  32.790  -5.249  1.00 15.05           H  
ATOM   3535  HD1 PHE A 223      -1.922  33.757  -4.512  1.00 17.69           H  
ATOM   3536  HD2 PHE A 223       1.001  36.107  -5.852  1.00 17.13           H  
ATOM   3537  HE1 PHE A 223      -3.385  35.563  -4.565  1.00 17.58           H  
ATOM   3538  HE2 PHE A 223      -0.443  37.895  -5.903  1.00 22.02           H  
ATOM   3539  HZ  PHE A 223      -2.628  37.626  -5.265  1.00 17.48           H  
ATOM   3540  N   VAL A 224       1.710  31.303  -3.015  1.00 14.77           N  
ANISOU 3540  N   VAL A 224     2031   1701   1879   -143    169   -218       N  
ATOM   3541  CA  VAL A 224       2.432  30.065  -2.812  1.00 12.71           C  
ANISOU 3541  CA  VAL A 224     1757   1475   1595   -200    111   -178       C  
ATOM   3542  C   VAL A 224       1.456  28.903  -2.924  1.00 15.70           C  
ANISOU 3542  C   VAL A 224     2066   1881   2018   -184    107   -209       C  
ATOM   3543  O   VAL A 224       0.445  28.877  -2.223  1.00 15.25           O  
ANISOU 3543  O   VAL A 224     2003   1820   1971   -218    173   -260       O  
ATOM   3544  CB  VAL A 224       3.092  30.039  -1.433  1.00 16.45           C  
ANISOU 3544  CB  VAL A 224     2315   1935   2002   -322    124   -163       C  
ATOM   3545  CG1 VAL A 224       3.904  28.737  -1.253  1.00 15.33           C  
ANISOU 3545  CG1 VAL A 224     2167   1820   1837   -365     44   -117       C  
ATOM   3546  CG2 VAL A 224       3.965  31.262  -1.254  1.00 20.16           C  
ANISOU 3546  CG2 VAL A 224     2852   2375   2432   -351    134   -146       C  
ATOM   3547  H   VAL A 224       0.951  31.333  -2.610  1.00 17.72           H  
ATOM   3548  HA  VAL A 224       3.118  29.967  -3.491  1.00 15.25           H  
ATOM   3549  HB  VAL A 224       2.402  30.059  -0.752  1.00 19.75           H  
ATOM   3550 HG11 VAL A 224       4.313  28.741  -0.373  1.00 18.39           H  
ATOM   3551 HG12 VAL A 224       3.306  27.978  -1.337  1.00 18.39           H  
ATOM   3552 HG13 VAL A 224       4.590  28.696  -1.937  1.00 18.39           H  
ATOM   3553 HG21 VAL A 224       4.376  31.231  -0.376  1.00 24.19           H  
ATOM   3554 HG22 VAL A 224       4.651  31.264  -1.940  1.00 24.19           H  
ATOM   3555 HG23 VAL A 224       3.415  32.057  -1.334  1.00 24.19           H  
ATOM   3556  N   THR A 225       1.754  27.953  -3.811  1.00 12.80           N  
ANISOU 3556  N   THR A 225     1643   1544   1677   -137     33   -186       N  
ATOM   3557  CA  THR A 225       0.886  26.818  -4.074  1.00 11.08           C  
ANISOU 3557  CA  THR A 225     1358   1344   1508   -123     16   -217       C  
ATOM   3558  C   THR A 225       1.667  25.511  -4.130  1.00 14.11           C  
ANISOU 3558  C   THR A 225     1745   1732   1884   -149    -69   -178       C  
ATOM   3559  O   THR A 225       2.660  25.395  -4.873  1.00 14.43           O  
ANISOU 3559  O   THR A 225     1774   1793   1917    -98   -136   -146       O  
ATOM   3560  CB  THR A 225       0.153  26.981  -5.443  1.00 17.71           C  
ANISOU 3560  CB  THR A 225     2109   2212   2408      2     -1   -252       C  
ATOM   3561  OG1 THR A 225      -0.678  28.132  -5.386  1.00 22.39           O  
ANISOU 3561  OG1 THR A 225     2696   2793   3016     42     67   -294       O  
ATOM   3562  CG2 THR A 225      -0.720  25.767  -5.738  1.00 20.26           C  
ANISOU 3562  CG2 THR A 225     2357   2556   2785      7    -25   -292       C  
ATOM   3563  H   THR A 225       2.474  27.949  -4.282  1.00 15.36           H  
ATOM   3564  HA  THR A 225       0.219  26.749  -3.373  1.00 13.30           H  
ATOM   3565  HB  THR A 225       0.804  27.080  -6.155  1.00 21.25           H  
ATOM   3566  HG1 THR A 225      -1.080  28.233  -6.117  1.00 26.86           H  
ATOM   3567 HG21 THR A 225      -1.169  25.882  -6.590  1.00 24.31           H  
ATOM   3568 HG22 THR A 225      -0.174  24.967  -5.774  1.00 24.31           H  
ATOM   3569 HG23 THR A 225      -1.387  25.662  -5.042  1.00 24.31           H  
ATOM   3570  N   ALA A 226       1.231  24.520  -3.352  1.00 13.22           N  
ANISOU 3570  N   ALA A 226     1651   1598   1772   -229    -66   -182       N  
ATOM   3571  CA  ALA A 226       1.906  23.222  -3.357  1.00 13.95           C  
ANISOU 3571  CA  ALA A 226     1763   1674   1864   -248   -158   -147       C  
ATOM   3572  C   ALA A 226       1.543  22.404  -4.590  1.00 10.55           C  
ANISOU 3572  C   ALA A 226     1248   1259   1500   -161   -217   -177       C  
ATOM   3573  O   ALA A 226       0.413  22.459  -5.069  1.00 12.80           O  
ANISOU 3573  O   ALA A 226     1467   1562   1835   -131   -180   -228       O  
ATOM   3574  CB  ALA A 226       1.543  22.412  -2.081  1.00 11.31           C  
ANISOU 3574  CB  ALA A 226     1501   1298   1500   -374   -140   -130       C  
ATOM   3575  H   ALA A 226       0.558  24.572  -2.819  1.00 15.86           H  
ATOM   3576  HA  ALA A 226       2.866  23.363  -3.361  1.00 16.74           H  
ATOM   3577  HB1 ALA A 226       2.002  21.557  -2.109  1.00 13.57           H  
ATOM   3578  HB2 ALA A 226       1.823  22.913  -1.299  1.00 13.57           H  
ATOM   3579  HB3 ALA A 226       0.584  22.272  -2.059  1.00 13.57           H  
ATOM   3580  N   ALA A 227       2.510  21.649  -5.107  1.00 10.20           N  
ANISOU 3580  N   ALA A 227     1202   1216   1458   -115   -314   -154       N  
ATOM   3581  CA  ALA A 227       2.271  20.784  -6.240  1.00 13.12           C  
ANISOU 3581  CA  ALA A 227     1503   1598   1885    -33   -379   -190       C  
ATOM   3582  C   ALA A 227       3.296  19.659  -6.220  1.00 10.29           C  
ANISOU 3582  C   ALA A 227     1177   1211   1522    -22   -485   -166       C  
ATOM   3583  O   ALA A 227       4.043  19.504  -5.249  1.00 10.46           O  
ANISOU 3583  O   ALA A 227     1275   1199   1499    -84   -508   -119       O  
ATOM   3584  CB  ALA A 227       2.346  21.572  -7.555  1.00 17.42           C  
ANISOU 3584  CB  ALA A 227     1972   2208   2437     83   -377   -213       C  
ATOM   3585  H   ALA A 227       3.317  21.626  -4.812  1.00 12.24           H  
ATOM   3586  HA  ALA A 227       1.386  20.393  -6.166  1.00 15.75           H  
ATOM   3587  HB1 ALA A 227       2.182  20.967  -8.295  1.00 20.90           H  
ATOM   3588  HB2 ALA A 227       1.672  22.270  -7.542  1.00 20.90           H  
ATOM   3589  HB3 ALA A 227       3.229  21.965  -7.637  1.00 20.90           H  
ATOM   3590  N   GLY A 228       3.305  18.845  -7.281  1.00 10.81           N  
ANISOU 3590  N   GLY A 228     1186   1287   1634     63   -557   -205       N  
ATOM   3591  CA  GLY A 228       4.332  17.830  -7.406  1.00 15.36           C  
ANISOU 3591  CA  GLY A 228     1783   1840   2213    103   -666   -197       C  
ATOM   3592  C   GLY A 228       3.868  16.453  -6.953  1.00 23.03           C  
ANISOU 3592  C   GLY A 228     2809   2715   3224     51   -724   -202       C  
ATOM   3593  O   GLY A 228       4.639  15.494  -6.927  1.00 18.78           O  
ANISOU 3593  O   GLY A 228     2307   2132   2695     84   -826   -196       O  
ATOM   3594  H   GLY A 228       2.736  18.864  -7.925  1.00 12.97           H  
ATOM   3595  HA2 GLY A 228       4.611  17.769  -8.334  1.00 18.43           H  
ATOM   3596  HA3 GLY A 228       5.101  18.084  -6.873  1.00 18.43           H  
ATOM   3597  N   ILE A 229       2.602  16.373  -6.579  1.00 14.11           N  
ANISOU 3597  N   ILE A 229     1686   1554   2120    -33   -660   -214       N  
ATOM   3598  CA  ILE A 229       1.940  15.099  -6.291  1.00 15.34           C  
ANISOU 3598  CA  ILE A 229     1887   1620   2321   -101   -701   -223       C  
ATOM   3599  C   ILE A 229       0.692  15.059  -7.132  1.00 16.41           C  
ANISOU 3599  C   ILE A 229     1927   1788   2518    -85   -663   -296       C  
ATOM   3600  O   ILE A 229      -0.156  15.951  -7.053  1.00 21.01           O  
ANISOU 3600  O   ILE A 229     2458   2425   3099   -112   -564   -314       O  
ATOM   3601  CB  ILE A 229       1.626  14.973  -4.803  1.00 20.25           C  
ANISOU 3601  CB  ILE A 229     2617   2177   2901   -254   -652   -163       C  
ATOM   3602  CG1 ILE A 229       2.954  14.779  -4.055  1.00 23.03           C  
ANISOU 3602  CG1 ILE A 229     3068   2489   3194   -254   -727    -95       C  
ATOM   3603  CG2 ILE A 229       0.664  13.805  -4.542  1.00 22.91           C  
ANISOU 3603  CG2 ILE A 229     2994   2428   3284   -354   -665   -173       C  
ATOM   3604  CD1 ILE A 229       2.833  14.699  -2.589  1.00 21.87           C  
ANISOU 3604  CD1 ILE A 229     3042   2285   2983   -396   -692    -27       C  
ATOM   3605  H   ILE A 229       2.088  17.056  -6.480  1.00 16.93           H  
ATOM   3606  HA  ILE A 229       2.516  14.364  -6.552  1.00 18.41           H  
ATOM   3607  HB  ILE A 229       1.212  15.796  -4.499  1.00 24.30           H  
ATOM   3608 HG12 ILE A 229       3.364  13.954  -4.361  1.00 27.64           H  
ATOM   3609 HG13 ILE A 229       3.537  15.527  -4.260  1.00 27.64           H  
ATOM   3610 HG21 ILE A 229       0.485  13.751  -3.590  1.00 27.50           H  
ATOM   3611 HG22 ILE A 229      -0.161  13.962  -5.026  1.00 27.50           H  
ATOM   3612 HG23 ILE A 229       1.077  12.983  -4.848  1.00 27.50           H  
ATOM   3613 HD11 ILE A 229       3.716  14.577  -2.206  1.00 26.24           H  
ATOM   3614 HD12 ILE A 229       2.439  15.522  -2.260  1.00 26.24           H  
ATOM   3615 HD13 ILE A 229       2.266  13.946  -2.361  1.00 26.24           H  
ATOM   3616  N   THR A 230       0.612  14.027  -7.963  1.00 19.63           N  
ANISOU 3616  N   THR A 230     2311   2165   2985    -30   -750   -345       N  
ATOM   3617  CA  THR A 230      -0.365  13.952  -9.033  1.00 29.87           C  
ANISOU 3617  CA  THR A 230     3502   3508   4339     18   -743   -427       C  
ATOM   3618  C   THR A 230      -1.766  13.725  -8.525  1.00 31.95           C  
ANISOU 3618  C   THR A 230     3750   3748   4641   -108   -674   -451       C  
ATOM   3619  O   THR A 230      -1.983  12.946  -7.600  1.00 36.23           O  
ANISOU 3619  O   THR A 230     4379   4201   5188   -235   -675   -416       O  
ATOM   3620  CB  THR A 230      -0.003  12.797  -9.976  1.00 37.77           C  
ANISOU 3620  CB  THR A 230     4494   4472   5387    103   -864   -481       C  
ATOM   3621  OG1 THR A 230       1.136  13.183 -10.754  1.00 52.32           O  
ANISOU 3621  OG1 THR A 230     6313   6380   7186    239   -892   -479       O  
ATOM   3622  CG2 THR A 230      -1.168  12.430 -10.910  1.00 32.85           C  
ANISOU 3622  CG2 THR A 230     3779   3875   4830    119   -871   -572       C  
ATOM   3623  H   THR A 230       1.129  13.341  -7.924  1.00 23.56           H  
ATOM   3624  HA  THR A 230      -0.352  14.779  -9.541  1.00 35.84           H  
ATOM   3625  HB  THR A 230       0.222  12.014  -9.449  1.00 45.33           H  
ATOM   3626  HG1 THR A 230       1.786  13.350 -10.248  1.00 62.78           H  
ATOM   3627 HG21 THR A 230      -0.909  11.698 -11.492  1.00 39.43           H  
ATOM   3628 HG22 THR A 230      -1.939  12.159 -10.387  1.00 39.43           H  
ATOM   3629 HG23 THR A 230      -1.410  13.195 -11.454  1.00 39.43           H  
ATOM   3630  N   LEU A 231      -2.708  14.403  -9.167  1.00 39.25           N  
ANISOU 3630  N   LEU A 231     4564   4759   5592    -71   -618   -512       N  
ATOM   3631  CA  LEU A 231      -4.122  14.281  -8.869  1.00 40.15           C  
ANISOU 3631  CA  LEU A 231     4621   4882   5751   -173   -549   -559       C  
ATOM   3632  C   LEU A 231      -4.776  13.248  -9.789  1.00 46.12           C  
ANISOU 3632  C   LEU A 231     5315   5624   6584   -159   -622   -641       C  
ATOM   3633  O   LEU A 231      -4.788  12.052  -9.492  1.00 52.60           O  
ANISOU 3633  O   LEU A 231     6203   6347   7437   -244   -675   -636       O  
ATOM   3634  CB  LEU A 231      -4.779  15.650  -9.051  1.00 37.22           C  
ANISOU 3634  CB  LEU A 231     4156   4616   5369   -123   -457   -589       C  
ATOM   3635  CG  LEU A 231      -6.294  15.754  -8.871  1.00 46.02           C  
ANISOU 3635  CG  LEU A 231     5174   5779   6534   -198   -378   -660       C  
ATOM   3636  CD1 LEU A 231      -6.819  14.891  -7.702  1.00 46.37           C  
ANISOU 3636  CD1 LEU A 231     5275   5756   6586   -392   -329   -642       C  
ATOM   3637  CD2 LEU A 231      -6.668  17.234  -8.695  1.00 46.85           C  
ANISOU 3637  CD2 LEU A 231     5225   5964   6613   -146   -285   -670       C  
ATOM   3638  H   LEU A 231      -2.543  14.960  -9.802  1.00 47.10           H  
ATOM   3639  HA  LEU A 231      -4.240  13.998  -7.949  1.00 48.18           H  
ATOM   3640  HB2 LEU A 231      -4.377  16.260  -8.413  1.00 44.66           H  
ATOM   3641  HB3 LEU A 231      -4.581  15.958  -9.950  1.00 44.66           H  
ATOM   3642  HG  LEU A 231      -6.724  15.439  -9.681  1.00 55.23           H  
ATOM   3643 HD11 LEU A 231      -7.781  14.998  -7.638  1.00 55.64           H  
ATOM   3644 HD12 LEU A 231      -6.599  13.962  -7.874  1.00 55.64           H  
ATOM   3645 HD13 LEU A 231      -6.397  15.184  -6.879  1.00 55.64           H  
ATOM   3646 HD21 LEU A 231      -7.628  17.305  -8.580  1.00 56.22           H  
ATOM   3647 HD22 LEU A 231      -6.214  17.583  -7.913  1.00 56.22           H  
ATOM   3648 HD23 LEU A 231      -6.392  17.724  -9.485  1.00 56.22           H  
TER    3649      LEU A 231                                                      
HETATM 3650  O   HOH A 301      16.109  35.961   2.353  1.00 13.96           O  
HETATM 3651  O   HOH A 302       8.126  29.114   7.029  1.00 13.38           O  
HETATM 3652  O   HOH A 303       8.473  34.452  -5.601  1.00 13.09           O  
HETATM 3653  O   HOH A 304      10.775  31.631   9.097  1.00 12.25           O  
HETATM 3654  O   HOH A 305      -4.928  31.430   6.331  1.00 14.29           O  
HETATM 3655  O   HOH A 306      16.385  32.304   5.352  1.00 11.56           O  
HETATM 3656  O   HOH A 307       5.189  20.177   3.855  1.00 11.63           O  
HETATM 3657  O   HOH A 308       6.194  32.265   3.178  1.00 16.11           O  
HETATM 3658  O   HOH A 309      16.356  47.181  -2.364  1.00 14.97           O  
HETATM 3659  O   HOH A 310      15.116  36.430  -1.081  1.00 13.91           O  
HETATM 3660  O   HOH A 311       5.272  21.705  16.943  1.00 20.08           O  
HETATM 3661  O   HOH A 312      13.116  10.994   6.040  1.00 14.86           O  
HETATM 3662  O   HOH A 313       8.353  42.688  -8.098  1.00 18.49           O  
HETATM 3663  O   HOH A 314      15.261  30.973   8.676  1.00 19.18           O  
HETATM 3664  O   HOH A 315      13.035  32.228   7.646  1.00 12.84           O  
HETATM 3665  O   HOH A 316      13.731  36.867  -7.210  1.00 14.30           O  
HETATM 3666  O   HOH A 317       9.761  12.825   1.621  1.00 15.51           O  
HETATM 3667  O   HOH A 318      14.554  39.598  -9.940  1.00 21.63           O  
HETATM 3668  O   HOH A 319      -1.402  20.425   7.929  1.00 16.37           O  
HETATM 3669  O   HOH A 320      -3.182  19.467   6.309  1.00 19.89           O  
HETATM 3670  O   HOH A 321      20.034  46.500  -4.849  1.00 23.37           O  
HETATM 3671  O   HOH A 322      -6.081  31.119  13.643  1.00 18.53           O  
HETATM 3672  O   HOH A 323      -3.734  24.895   2.364  1.00 21.28           O  
HETATM 3673  O   HOH A 324      17.429  35.329  -1.519  1.00 18.08           O  
HETATM 3674  O   HOH A 325      -7.962  31.194  10.238  1.00 21.36           O  
HETATM 3675  O   HOH A 326      28.129  31.653  -0.902  1.00 23.47           O  
HETATM 3676  O   HOH A 327      -7.528  30.794   4.420  1.00 24.02           O  
HETATM 3677  O   HOH A 328      16.826  41.559  -7.913  1.00 19.08           O  
HETATM 3678  O   HOH A 329       3.451  44.516  -3.793  1.00 19.13           O  
HETATM 3679  O   HOH A 330      -1.697  19.478  13.713  1.00 27.39           O  
HETATM 3680  O   HOH A 331      -6.980  18.334  -4.978  1.00 21.76           O  
HETATM 3681  O   HOH A 332      14.568  25.915  -7.101  1.00 17.77           O  
HETATM 3682  O   HOH A 333      16.066  32.620  16.324  1.00 30.32           O  
HETATM 3683  O   HOH A 334      15.078  39.755  -6.899  1.00 17.53           O  
HETATM 3684  O   HOH A 335      19.809  49.945   9.481  1.00 26.78           O  
HETATM 3685  O   HOH A 336       8.254  10.773  -1.468  1.00 19.25           O  
HETATM 3686  O   HOH A 337       9.946  15.880  -6.140  1.00 22.36           O  
HETATM 3687  O   HOH A 338      -2.166  42.553  10.542  1.00 27.35           O  
HETATM 3688  O   HOH A 339      15.806  11.381   8.626  1.00 21.45           O  
HETATM 3689  O   HOH A 340      28.145  41.892  -1.918  1.00 26.80           O  
HETATM 3690  O   HOH A 341      14.343  49.709  -2.321  1.00 25.75           O  
HETATM 3691  O   HOH A 342      18.439  21.394   3.165  1.00 31.79           O  
HETATM 3692  O   HOH A 343      -3.208  38.130   2.149  1.00 23.03           O  
HETATM 3693  O   HOH A 344       9.387  11.263  13.317  1.00 25.71           O  
HETATM 3694  O   HOH A 345      26.574  33.505   7.666  1.00 21.15           O  
HETATM 3695  O   HOH A 346      17.754  38.720  18.381  1.00 22.94           O  
HETATM 3696  O   HOH A 347       0.024  43.393  -7.655  1.00 26.29           O  
HETATM 3697  O   HOH A 348      -5.901  33.644  13.486  1.00 20.15           O  
HETATM 3698  O   HOH A 349      -2.185  43.430   4.962  1.00 39.40           O  
HETATM 3699  O   HOH A 350       6.368  12.437  -4.573  1.00 20.74           O  
HETATM 3700  O   HOH A 351      10.918  17.254  -3.526  1.00 26.35           O  
HETATM 3701  O   HOH A 352      19.200  48.199  -2.583  1.00 28.85           O  
HETATM 3702  O   HOH A 353      18.096  19.870   0.908  1.00 24.42           O  
HETATM 3703  O   HOH A 354      11.822  21.911 -12.343  1.00 21.57           O  
HETATM 3704  O   HOH A 355       6.183  38.366  21.683  1.00 24.62           O  
HETATM 3705  O   HOH A 356       1.840  48.539  -3.217  1.00 33.22           O  
HETATM 3706  O   HOH A 357      12.557  51.987   0.715  1.00 23.55           O  
HETATM 3707  O   HOH A 358      15.204  23.368  12.131  1.00 24.06           O  
HETATM 3708  O   HOH A 359       6.952  28.357  -9.664  1.00 28.42           O  
HETATM 3709  O   HOH A 360      26.394  48.010  12.417  1.00 24.10           O  
HETATM 3710  O   HOH A 361      16.204  50.200  -0.046  1.00 35.65           O  
HETATM 3711  O   HOH A 362       6.351  43.539  13.415  1.00 26.40           O  
HETATM 3712  O   HOH A 363      34.420  33.610   7.504  1.00 28.90           O  
HETATM 3713  O   HOH A 364       1.162  20.368  16.159  1.00 32.01           O  
HETATM 3714  O   HOH A 365      -0.347  41.843  12.397  1.00 22.41           O  
HETATM 3715  O   HOH A 366     -11.179  35.345   7.805  1.00 41.19           O  
HETATM 3716  O   HOH A 367      29.751  32.155   0.982  1.00 29.74           O  
HETATM 3717  O   HOH A 368      24.840  24.486  -3.800  1.00 33.28           O  
HETATM 3718  O   HOH A 369       7.440  36.621  -9.220  1.00 21.44           O  
HETATM 3719  O   HOH A 370       1.262  44.542  -5.359  1.00 29.09           O  
HETATM 3720  O   HOH A 371      -5.633  38.385   2.912  1.00 31.46           O  
HETATM 3721  O   HOH A 372      15.160  48.400  -9.468  1.00 29.82           O  
HETATM 3722  O   HOH A 373       3.086  37.544  -9.336  1.00 32.88           O  
HETATM 3723  O   HOH A 374       6.664  31.514   0.715  1.00 32.87           O  
HETATM 3724  O   HOH A 375      27.662  29.031  -5.063  1.00 36.45           O  
HETATM 3725  O   HOH A 376       0.787  43.761   0.099  1.00 27.97           O  
HETATM 3726  O   HOH A 377       4.255  10.789  -3.890  1.00 37.06           O  
HETATM 3727  O   HOH A 378      -8.039  21.684  -3.447  1.00 31.45           O  
HETATM 3728  O   HOH A 379      12.864  22.403  17.020  1.00 34.28           O  
HETATM 3729  O   HOH A 380       0.094  44.963   4.974  1.00 44.64           O  
HETATM 3730  O   HOH A 381       6.407  57.591   6.894  1.00 33.26           O  
HETATM 3731  O   HOH A 382      -1.343  31.071  21.675  1.00 25.33           O  
HETATM 3732  O   HOH A 383      13.269  27.770  -8.581  1.00 27.74           O  
HETATM 3733  O   HOH A 384      -9.527  29.409  11.897  1.00 36.57           O  
HETATM 3734  O   HOH A 385      -0.123  18.683  -7.960  1.00 29.69           O  
HETATM 3735  O   HOH A 386       6.667  10.370   5.043  1.00 33.14           O  
HETATM 3736  O   HOH A 387      14.493  19.053  -0.296  1.00 25.20           O  
HETATM 3737  O   HOH A 388      -0.548  23.398  -9.136  1.00 30.45           O  
HETATM 3738  O   HOH A 389     -12.154  30.512   9.216  1.00 37.19           O  
HETATM 3739  O   HOH A 390       7.532  16.484  -6.776  1.00 28.87           O  
HETATM 3740  O   HOH A 391       9.186  47.189  15.746  1.00 38.04           O  
HETATM 3741  O   HOH A 392      22.462  38.624  13.975  1.00 38.23           O  
HETATM 3742  O   HOH A 393       5.680  50.632  -6.054  1.00 30.69           O  
HETATM 3743  O   HOH A 394      18.439  25.897  16.308  1.00 40.17           O  
HETATM 3744  O   HOH A 395      24.313  25.339  -7.068  1.00 35.20           O  
HETATM 3745  O   HOH A 396      -3.927  41.742  14.869  1.00 34.70           O  
HETATM 3746  O   HOH A 397      -1.464  40.838  15.209  1.00 32.29           O  
HETATM 3747  O   HOH A 398      27.759  32.412  10.159  1.00 27.67           O  
HETATM 3748  O   HOH A 399      25.229  29.863  -4.938  1.00 28.08           O  
HETATM 3749  O   HOH A 400      -6.386  25.297   5.957  1.00 38.93           O  
HETATM 3750  O   HOH A 401      -7.747  37.462   1.609  1.00 28.26           O  
HETATM 3751  O   HOH A 402       8.854  45.740  -8.376  1.00 34.24           O  
HETATM 3752  O   HOH A 403       5.993  47.615  -8.104  1.00 39.84           O  
HETATM 3753  O   HOH A 404      27.691  39.476  -5.757  1.00 32.46           O  
HETATM 3754  O   HOH A 405       0.165  17.948  16.582  1.00 36.20           O  
HETATM 3755  O   HOH A 406      12.705  45.977  13.791  1.00 32.30           O  
HETATM 3756  O   HOH A 407      -0.114  44.362  13.169  1.00 43.09           O  
HETATM 3757  O   HOH A 408      29.720  44.977  13.838  1.00 41.32           O  
HETATM 3758  O   HOH A 409      28.408  48.735  10.643  1.00 45.07           O  
HETATM 3759  O   HOH A 410      13.678  23.643 -10.704  1.00 45.45           O  
HETATM 3760  O   HOH A 411      21.298  53.935   8.502  1.00 35.33           O  
HETATM 3761  O   HOH A 412      -1.625  45.000   9.292  1.00 42.19           O  
HETATM 3762  O   HOH A 413      11.217   9.504   4.949  1.00 19.36           O  
HETATM 3763  O   HOH A 414       7.902  29.167  -0.335  1.00 26.22           O  
HETATM 3764  O   HOH A 415      -0.278  11.239  -1.719  1.00 30.85           O  
HETATM 3765  O   HOH A 416       7.245   9.828   3.001  1.00 45.11           O  
HETATM 3766  O   HOH A 417      15.727  28.570 -10.388  1.00 34.32           O  
HETATM 3767  O   HOH A 418       0.847  30.405  23.734  1.00 29.68           O  
HETATM 3768  O   HOH A 419       3.676  31.012   2.267  1.00 33.06           O  
HETATM 3769  O   HOH A 420      -0.110  44.634  -2.494  1.00 45.59           O  
HETATM 3770  O   HOH A 421      31.744  32.367   4.664  1.00 39.39           O  
HETATM 3771  O   HOH A 422       1.422  32.365   0.959  1.00 30.44           O  
HETATM 3772  O   HOH A 423      28.363  39.239  10.231  1.00 32.15           O  
HETATM 3773  O   HOH A 424      29.057  30.871  -2.866  1.00 29.47           O  
HETATM 3774  O   HOH A 425      -2.308  43.006  -7.624  1.00 39.20           O  
HETATM 3775  O   HOH A 426       5.042  30.278  -9.625  1.00 30.24           O  
HETATM 3776  O   HOH A 427       2.185  10.699  -2.621  1.00 39.82           O  
HETATM 3777  O   HOH A 428      -7.760  26.201  -1.115  1.00 37.98           O  
HETATM 3778  O   HOH A 429      19.045  50.552   1.456  1.00 43.46           O  
HETATM 3779  O   HOH A 430      14.323  50.642  -4.704  1.00 35.86           O  
HETATM 3780  O   HOH A 431      28.704  45.684  16.238  1.00 34.46           O  
HETATM 3781  O   HOH A 432       0.702  45.430   2.504  1.00 34.56           O  
HETATM 3782  O   HOH A 433       8.142  49.709  -6.614  1.00 43.16           O  
HETATM 3783  O   HOH A 434      -3.013  43.345   7.334  1.00 44.70           O  
HETATM 3784  O   HOH A 435       3.746  19.774  17.171  1.00 43.44           O  
HETATM 3785  O   HOH A 436      -8.811  33.658  10.524  1.00 40.11           O  
HETATM 3786  O   HOH A 437      16.609   7.093   9.753  1.00 42.27           O  
HETATM 3787  O   HOH A 438       7.442  40.199  -9.683  1.00 38.41           O  
HETATM 3788  O   HOH A 439      29.709  33.450  11.711  1.00 44.23           O  
HETATM 3789  O   HOH A 440      -6.104  40.261   9.578  1.00 39.15           O  
HETATM 3790  O   HOH A 441       8.970   9.884   6.468  1.00 35.58           O  
HETATM 3791  O   HOH A 442      12.809  23.910  19.458  1.00 33.02           O  
HETATM 3792  O   HOH A 443      -5.715  14.500   1.201  1.00 37.85           O  
HETATM 3793  O   HOH A 444      -5.053  26.481  18.956  1.00 37.39           O  
HETATM 3794  O   HOH A 445       2.662  48.531   8.325  1.00 38.48           O  
HETATM 3795  O   HOH A 446      25.999  32.120  12.039  1.00 33.19           O  
HETATM 3796  O   HOH A 447      20.142  21.276   4.645  1.00 37.33           O  
HETATM 3797  O   HOH A 448      35.563  37.367   2.666  1.00 47.47           O  
HETATM 3798  O   HOH A 449      13.149  26.400  20.051  1.00 40.56           O  
HETATM 3799  O   HOH A 450      -8.579  30.063  14.213  1.00 38.58           O  
HETATM 3800  O   HOH A 451      29.282  41.435  13.988  1.00 36.18           O  
HETATM 3801  O   HOH A 452      16.560  24.044  -7.285  1.00 40.05           O  
HETATM 3802  O   HOH A 453      16.585  46.492  -5.045  1.00 33.85           O  
HETATM 3803  O   HOH A 454      27.181  35.373  -9.596  1.00 36.07           O  
HETATM 3804  O   HOH A 455      14.475  53.336   7.412  1.00 37.57           O  
HETATM 3805  O   HOH A 456       5.335  47.415   8.745  1.00 31.30           O  
HETATM 3806  O   HOH A 457      18.036  48.440   0.218  1.00 36.95           O  
HETATM 3807  O   HOH A 458      16.540  18.043   1.035  1.00 33.95           O  
HETATM 3808  O   HOH A 459      -4.273  28.891  18.404  1.00 41.53           O  
HETATM 3809  O   HOH A 460      27.326  43.262 -10.939  1.00 38.78           O  
HETATM 3810  O   HOH A 461      -8.429  37.713  13.414  1.00 45.86           O  
HETATM 3811  O   HOH A 462      11.282  22.621  21.115  1.00 33.00           O  
HETATM 3812  O   HOH A 463       0.878  48.196   2.454  1.00 42.75           O  
HETATM 3813  O   HOH A 464      -7.974  35.118  13.194  1.00 47.30           O  
HETATM 3814  O   HOH A 465      22.028  40.861  15.063  1.00 43.96           O  
HETATM 3815  O   HOH A 466      -5.123  30.954  16.408  1.00 38.64           O  
HETATM 3816  O   HOH A 467      -4.589  31.758  -5.520  1.00 27.92           O  
HETATM 3817  O   HOH A 468      33.013  35.996  -0.988  1.00 43.74           O  
HETATM 3818  O   HOH A 469      16.656  24.496  17.243  1.00 54.22           O  
HETATM 3819  O   HOH A 470      12.897  43.078  15.244  1.00 30.73           O  
HETATM 3820  O   HOH A 471      15.055  18.939   9.562  1.00 30.85           O  
HETATM 3821  O   HOH A 472      13.339   4.058   9.695  1.00 50.77           O  
HETATM 3822  O   HOH A 473       7.747  29.054  21.177  1.00 42.97           O  
HETATM 3823  O   HOH A 474       3.337  11.721   8.580  1.00 41.98           O  
HETATM 3824  O   HOH A 475      18.126  23.704  -4.842  1.00 36.02           O  
HETATM 3825  O   HOH A 476      -2.652  12.194  -2.717  1.00 42.79           O  
HETATM 3826  O   HOH A 477      17.372  22.834  14.986  1.00 49.56           O  
HETATM 3827  O   HOH A 478       2.498  30.631  22.031  1.00 43.08           O  
HETATM 3828  O   HOH A 479       1.568  25.233   4.387  1.00 10.65           O  
HETATM 3829  O   HOH A 480      24.934  34.540  -9.973  1.00 24.30           O  
HETATM 3830  O   HOH A 481      14.211  33.673  16.999  1.00 31.69           O  
HETATM 3831  O   HOH A 482      -3.570  32.017  23.499  1.00 31.91           O  
HETATM 3832  O   HOH A 483       1.608  12.152   5.566  1.00 31.76           O  
HETATM 3833  O   HOH A 484       5.048  51.662  12.029  1.00 40.34           O  
HETATM 3834  O   HOH A 485      12.626  25.843 -11.726  1.00 43.88           O  
HETATM 3835  O   HOH A 486       8.565  28.920 -11.766  1.00 33.04           O  
HETATM 3836  O   HOH A 487      14.228  25.869  -9.907  1.00 35.68           O  
HETATM 3837  O   HOH A 488      23.836  48.512   8.838  1.00 26.41           O  
HETATM 3838  O   HOH A 489      26.076  49.952   8.665  1.00 38.32           O  
HETATM 3839  O   HOH A 490      22.701  50.585   7.446  1.00 43.53           O  
HETATM 3840  O   HOH A 491       8.973  19.330 -10.968  1.00 36.49           O  
HETATM 3841  O   HOH A 492      22.071  24.844   6.276  1.00 51.24           O  
HETATM 3842  O   HOH A 493       7.054  48.311  14.125  1.00 37.90           O  
HETATM 3843  O   HOH A 494      15.637  34.724 -14.264  1.00 38.56           O  
HETATM 3844  O   HOH A 495      -1.756  11.378   6.941  1.00 42.29           O  
HETATM 3845  O   HOH A 496      11.605  19.437 -11.301  1.00 45.19           O  
HETATM 3846  O   HOH A 497      17.811  33.485 -14.890  1.00 42.95           O  
HETATM 3847  O   HOH A 498      15.339  17.301  -1.997  1.00 41.79           O  
HETATM 3848  O   HOH A 499      26.846  39.917 -11.448  1.00 46.47           O  
HETATM 3849  O   HOH A 500      18.981  50.358  -3.698  1.00 42.85           O  
HETATM 3850  O   HOH A 501      17.309  43.480 -16.097  1.00 38.52           O  
HETATM 3851  O   HOH A 502       2.641  51.104   7.991  1.00 38.65           O  
HETATM 3852  O   HOH A 503      23.878  50.492   2.587  1.00 37.75           O  
HETATM 3853  O   HOH A 504      -6.358  29.766  -5.180  1.00 47.79           O  
HETATM 3854  O   HOH A 505      13.610  18.426 -10.147  1.00 45.15           O  
HETATM 3855  O   HOH A 506       4.578  19.976  23.046  1.00 46.91           O  
HETATM 3856  O   HOH A 507      26.054  48.060   2.002  1.00 48.69           O  
HETATM 3857  O   HOH A 508      19.552  31.538 -14.059  1.00 46.01           O  
HETATM 3858  O   HOH A 509      -7.322  26.995   4.404  1.00 43.96           O  
HETATM 3859  O   HOH A 510      -0.513  13.625  12.477  1.00 42.96           O  
HETATM 3860  O   HOH A 511      -9.175  16.778  -5.052  1.00 43.93           O  
HETATM 3861  O   HOH A 512       6.542  36.976 -11.686  1.00 40.78           O  
HETATM 3862  O   HOH A 513      -0.589  16.199  12.501  1.00 48.92           O  
HETATM 3863  O   HOH A 514      -2.407  21.376  16.433  1.00 33.94           O  
HETATM 3864  O   HOH A 515      30.608  48.809  11.596  1.00 49.83           O  
HETATM 3865  O   HOH A 516      23.826  49.580  12.514  1.00 39.87           O  
HETATM 3866  O   HOH A 517      17.982  27.980 -11.547  1.00 47.77           O  
HETATM 3867  O   HOH A 518      21.263  28.050  12.694  1.00 50.42           O  
HETATM 3868  O   HOH A 519      34.100  35.787   8.464  1.00 48.88           O  
HETATM 3869  O   HOH A 520      23.761  36.033 -15.365  1.00 40.05           O  
HETATM 3870  O   HOH A 521      15.805   3.602  10.499  1.00 54.00           O  
HETATM 3871  O   HOH A 522       6.760  59.548   1.417  1.00 46.91           O  
HETATM 3872  O   HOH A 523      -1.121  21.688  -7.220  1.00 22.96           O  
HETATM 3873  O   HOH A 524       2.338  12.003  -7.509  1.00 33.26           O  
HETATM 3874  O   HOH A 525      20.559  28.296 -12.813  1.00 39.76           O  
HETATM 3875  O   HOH A 526      -3.429  27.888  -6.783  1.00 50.39           O  
HETATM 3876  O   HOH A 527      -7.001  24.112  -2.013  1.00 50.30           O  
HETATM 3877  O   HOH A 528      24.425  50.815   5.072  1.00 37.94           O  
HETATM 3878  O   HOH A 529      18.557  40.957 -15.020  1.00 45.61           O  
HETATM 3879  O   HOH A 530      -8.133  38.007  10.648  1.00 38.65           O  
HETATM 3880  O   HOH A 531      34.514  40.013   2.980  1.00 50.69           O  
HETATM 3881  O   HOH A 532       7.679  55.825  -0.462  1.00 49.44           O  
HETATM 3882  O   HOH A 533       0.636  41.062  -8.721  1.00 26.58           O  
HETATM 3883  O   HOH A 534      -2.556  24.892  -9.377  1.00 28.17           O  
HETATM 3884  O   HOH A 535      21.193  28.586  10.425  1.00 32.20           O  
HETATM 3885  O   HOH A 536      19.758  25.191  -3.944  1.00 45.88           O  
HETATM 3886  O   HOH A 537      31.375  46.337   3.991  1.00 40.06           O  
HETATM 3887  O   HOH A 538      32.515  45.285  10.510  1.00 50.15           O  
HETATM 3888  O   HOH A 539      -2.803  29.844  19.714  1.00 45.26           O  
HETATM 3889  O   HOH A 540      29.936  31.030  -5.205  1.00 45.67           O  
HETATM 3890  O   HOH A 541       5.688  46.370  11.507  1.00 46.50           O  
HETATM 3891  O   HOH A 542     -10.578  35.243   2.061  1.00 47.98           O  
HETATM 3892  O   HOH A 543       2.778  61.195   1.595  1.00 55.00           O  
HETATM 3893  O   HOH A 544       3.350  39.778 -10.200  1.00 46.61           O  
HETATM 3894  O   HOH A 545       3.304  51.568  10.036  1.00 54.60           O  
HETATM 3895  O   HOH A 546      18.688  16.789   9.357  1.00 43.85           O  
HETATM 3896  O   HOH A 547      23.323  34.026 -14.220  1.00 53.49           O  
HETATM 3897  O   HOH A 548       1.988   8.015   0.572  1.00 49.21           O  
HETATM 3898  O   HOH A 549      16.368  20.154  11.125  1.00 58.56           O  
HETATM 3899  O   HOH A 550     -11.758  18.437  -3.562  1.00 48.47           O  
HETATM 3900  O   HOH A 551      -6.461  14.114   3.347  1.00 60.09           O  
HETATM 3901  O   HOH A 552       4.239  10.569   3.630  1.00 50.88           O  
HETATM 3902  O   HOH A 553      10.271  50.981  -6.588  1.00 47.68           O  
HETATM 3903  O   HOH A 554      12.428  50.948  -5.939  1.00 47.14           O  
HETATM 3904  O   HOH A 555      15.044  37.058 -14.884  1.00 45.17           O  
HETATM 3905  O   HOH A 556      -1.742  28.501  21.171  1.00 43.82           O  
HETATM 3906  O   HOH A 557       1.343  12.448  11.831  1.00 47.02           O  
HETATM 3907  O   HOH A 558       1.558  28.611  20.295  1.00 47.38           O  
HETATM 3908  O   HOH A 559       1.204  38.903  -8.294  1.00 47.86           O  
HETATM 3909  O   HOH A 560       3.060  27.722  22.147  1.00 48.45           O  
HETATM 3910  O   HOH A 561       0.607  47.486   6.778  1.00 45.73           O  
HETATM 3911  O   HOH A 562      13.736  43.909 -15.190  1.00 50.29           O  
HETATM 3912  O   HOH A 563      21.774  31.665 -14.651  1.00 48.62           O  
HETATM 3913  O   HOH A 564      27.540  41.354 -13.553  1.00 50.28           O  
HETATM 3914  O   HOH A 565       1.577  10.345   3.360  1.00 57.14           O  
HETATM 3915  O   HOH A 566       0.545  26.888  21.447  1.00 44.79           O  
HETATM 3916  O   HOH A 567      22.179  27.124   9.013  1.00 44.39           O  
HETATM 3917  O   HOH A 568      30.933  46.601   9.105  1.00 58.26           O  
HETATM 3918  O   HOH A 569      14.098  55.247   1.519  1.00 52.33           O  
HETATM 3919  O   HOH A 570       7.256  51.538  13.671  1.00 41.33           O  
HETATM 3920  O   HOH A 571      10.472  40.470 -12.056  1.00 40.56           O  
HETATM 3921  O   HOH A 572       6.308   9.148  -3.016  1.00 43.86           O  
HETATM 3922  O   HOH A 573      31.432  49.249   9.583  1.00 56.70           O  
HETATM 3923  O   HOH A 574      -4.531  42.021  10.626  1.00 50.52           O  
HETATM 3924  O   HOH A 575      17.088  48.547  -5.947  1.00 53.23           O  
HETATM 3925  O   HOH A 576      12.334  39.277 -12.017  1.00 43.21           O  
HETATM 3926  O   HOH A 577      14.046  53.779  -0.512  1.00 57.31           O  
HETATM 3927  O   HOH A 578      32.611  44.353   4.536  1.00 56.03           O  
HETATM 3928  O   HOH A 579      -7.077  24.854   1.028  1.00 48.13           O  
HETATM 3929  O   HOH A 580      -2.041  11.113  -5.885  1.00 48.03           O  
HETATM 3930  O   HOH A 581     -11.017  27.276  13.176  1.00 53.67           O  
HETATM 3931  O   HOH A 582     -11.744  37.885   7.361  1.00 55.43           O  
HETATM 3932  O   HOH A 583     -10.006  38.479   2.477  1.00 47.42           O  
HETATM 3933  O   HOH A 584      32.540  38.308   6.847  1.00 49.77           O  
HETATM 3934  O   HOH A 585       5.306  12.623  13.526  1.00 29.43           O  
HETATM 3935  O   HOH A 586      -3.803  20.861  -8.119  1.00 35.40           O  
HETATM 3936  O   HOH A 587      -7.852  21.113  -5.674  1.00 38.38           O  
HETATM 3937  O   HOH A 588       5.467  24.511  22.351  1.00 38.44           O  
HETATM 3938  O   HOH A 589      -5.292  23.368   4.498  1.00 35.79           O  
HETATM 3939  O   HOH A 590       5.525  27.164  20.864  1.00 28.83           O  
HETATM 3940  O   HOH A 591       9.673  10.153   2.623  1.00 29.24           O  
HETATM 3941  O   HOH A 592       1.758  22.449 -11.067  1.00 32.43           O  
HETATM 3942  O   HOH A 593       9.352  51.695  14.799  1.00 48.40           O  
HETATM 3943  O   HOH A 594      13.924  30.699  21.391  1.00 36.69           O  
HETATM 3944  O   HOH A 595      -6.572  19.374   7.255  1.00 41.16           O  
HETATM 3945  O   HOH A 596       7.010  16.779  17.469  1.00 38.67           O  
HETATM 3946  O   HOH A 597      16.943  38.935 -16.242  1.00 51.85           O  
HETATM 3947  O   HOH A 598      -6.979  41.259  13.536  1.00 48.11           O  
HETATM 3948  O   HOH A 599      11.541  49.998  -9.050  1.00 49.26           O  
HETATM 3949  O   HOH A 600     -11.878  33.990  10.136  1.00 46.44           O  
HETATM 3950  O   HOH A 601      -6.822  17.137   7.018  1.00 53.44           O  
HETATM 3951  O   HOH A 602      19.274  37.480 -18.007  1.00 47.85           O  
HETATM 3952  O   HOH A 603      34.798  38.614   5.740  1.00 52.75           O  
CONECT  939  956                                                                
CONECT  956  939  957                                                           
CONECT  957  956  958  961                                                      
CONECT  958  957  959  960                                                      
CONECT  959  958                                                                
CONECT  960  958                                                                
CONECT  961  957  962  963                                                      
CONECT  962  961  966                                                           
CONECT  963  961  964  967                                                      
CONECT  964  963  965  966                                                      
CONECT  965  964                                                                
CONECT  966  962  964  970                                                      
CONECT  967  963  968                                                           
CONECT  968  967  969  978                                                      
CONECT  969  968                                                                
CONECT  970  966  971                                                           
CONECT  971  970  972  973                                                      
CONECT  972  971  974                                                           
CONECT  973  971  975                                                           
CONECT  974  972  976                                                           
CONECT  975  973  976                                                           
CONECT  976  974  975  977                                                      
CONECT  977  976                                                                
CONECT  978  968                                                                
MASTER      419    0    1    6   12    0    0    6 2098    1   24   19          
END                                                                             


A second structure was input as follows:


HEADER    FLUORESCENT PROTEIN                     23-MAY-13   4KW4              
TITLE     CRYSTAL STRUCTURE OF GREEN FLUORESCENT PROTEIN                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GREEN FLUORESCENT PROTEIN;                                 
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MUTATION: YES;                                                       
COMPND   6 OTHER_DETAILS: THE PROTEIN IN THIS STRUCTURE IS A VERSION OF GFP     
COMPND   7 CALLED EMERALD GFP                                                   
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: AEQUOREA VICTORIA;                              
SOURCE   3 ORGANISM_COMMON: JELLYFISH;                                          
SOURCE   4 ORGANISM_TAXID: 6100;                                                
SOURCE   5 GENE: GFP;                                                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)                                  
KEYWDS    BETA BARREL, FLUORESCENT PROTEIN, CHROMOPHORE                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.J.BARNARD,X.YU,N.NOINAJ,J.W.TARASKA                                 
REVDAT   1   09-APR-14 4KW4    0                                                
JRNL        AUTH   T.J.BARNARD,X.YU,N.NOINAJ,J.W.TARASKA                        
JRNL        TITL   CRYSTAL STRUCTURE OF GREEN FLUORESCENT PROTEIN               
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.75 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8.2_1309)                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.75                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 23.05                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.380                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 31868                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.172                           
REMARK   3   R VALUE            (WORKING SET) : 0.170                           
REMARK   3   FREE R VALUE                     : 0.204                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 6.280                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2000                            
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 23.0563 -  4.2001    1.00     2324   156  0.1575 0.1778        
REMARK   3     2  4.2001 -  3.3370    1.00     2191   146  0.1431 0.1788        
REMARK   3     3  3.3370 -  2.9161    1.00     2155   144  0.1502 0.1811        
REMARK   3     4  2.9161 -  2.6499    1.00     2150   144  0.1701 0.1971        
REMARK   3     5  2.6499 -  2.4602    1.00     2138   144  0.1570 0.2243        
REMARK   3     6  2.4602 -  2.3153    1.00     2134   143  0.1630 0.2033        
REMARK   3     7  2.3153 -  2.1995    1.00     2110   141  0.1675 0.2273        
REMARK   3     8  2.1995 -  2.1038    1.00     2104   141  0.1639 0.2313        
REMARK   3     9  2.1038 -  2.0228    1.00     2100   141  0.1793 0.2297        
REMARK   3    10  2.0228 -  1.9531    1.00     2120   141  0.1938 0.2131        
REMARK   3    11  1.9531 -  1.8920    1.00     2088   140  0.2226 0.2224        
REMARK   3    12  1.8920 -  1.8380    1.00     2097   140  0.2489 0.2530        
REMARK   3    13  1.8380 -  1.7896    1.00     2087   141  0.2680 0.3011        
REMARK   3    14  1.7896 -  1.7460    1.00     2070   138  0.3050 0.3455        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.190            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.680           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 29.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 26.00                          
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      :  0.011           1928                                  
REMARK   3   ANGLE     :  1.399           2631                                  
REMARK   3   CHIRALITY :  0.081            284                                  
REMARK   3   PLANARITY :  0.006            348                                  
REMARK   3   DIHEDRAL  : 14.575            707                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 8                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: chain 'A' and (resid 2 through 24 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):   5.8131  34.8751  10.6333              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1659 T22:   0.2248                                     
REMARK   3      T33:   0.1561 T12:  -0.0588                                     
REMARK   3      T13:   0.0471 T23:  -0.0606                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.9422 L22:   0.9654                                     
REMARK   3      L33:   1.2153 L12:   1.4834                                     
REMARK   3      L13:  -0.6529 L23:  -0.0309                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1399 S12:  -0.0676 S13:  -0.0329                       
REMARK   3      S21:   0.0429 S22:   0.0313 S23:  -0.0186                       
REMARK   3      S31:  -0.1517 S32:   0.1419 S33:  -0.1594                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: chain 'A' and (resid 25 through 68 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):   9.8511  41.3592   5.1179              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2276 T22:   0.1802                                     
REMARK   3      T33:   0.1739 T12:  -0.0837                                     
REMARK   3      T13:   0.0497 T23:  -0.0546                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0235 L22:   2.5201                                     
REMARK   3      L33:   1.5618 L12:   1.3662                                     
REMARK   3      L13:   0.0986 L23:   0.5919                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0724 S12:   0.0104 S13:   0.2630                       
REMARK   3      S21:  -0.0952 S22:   0.0666 S23:   0.0649                       
REMARK   3      S31:  -0.5582 S32:   0.2005 S33:  -0.0565                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: chain 'A' and (resid 69 through 81 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.3023  21.3211   1.2920              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1193 T22:   0.1521                                     
REMARK   3      T33:   0.1664 T12:  -0.0459                                     
REMARK   3      T13:  -0.0254 T23:   0.0217                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6696 L22:   5.6767                                     
REMARK   3      L33:   2.5332 L12:   1.5808                                     
REMARK   3      L13:   0.5822 L23:   2.1659                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0439 S12:  -0.1210 S13:  -0.1196                       
REMARK   3      S21:   0.0898 S22:  -0.0393 S23:   0.4711                       
REMARK   3      S31:   0.2803 S32:  -0.5372 S33:   0.0129                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: chain 'A' and (resid 82 through 128 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  12.5488  30.8642  10.1624              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1210 T22:   0.2715                                     
REMARK   3      T33:   0.1466 T12:  -0.0333                                     
REMARK   3      T13:  -0.0008 T23:  -0.0825                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1908 L22:   1.0013                                     
REMARK   3      L33:   0.6352 L12:   0.6221                                     
REMARK   3      L13:   0.4139 L23:   0.0700                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1092 S12:  -0.1426 S13:   0.0047                       
REMARK   3      S21:   0.1590 S22:   0.1229 S23:  -0.1214                       
REMARK   3      S31:   0.1274 S32:   0.4535 S33:  -0.1501                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: chain 'A' and (resid 129 through 147 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  21.6845  42.0788  -4.9024              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3275 T22:   0.5590                                     
REMARK   3      T33:   0.2898 T12:  -0.3814                                     
REMARK   3      T13:   0.1150 T23:  -0.0850                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4808 L22:   0.3889                                     
REMARK   3      L33:   0.3938 L12:   0.0409                                     
REMARK   3      L13:   0.4292 L23:   0.0646                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0938 S12:   0.2377 S13:   0.1269                       
REMARK   3      S21:  -0.0993 S22:   0.1807 S23:  -0.3286                       
REMARK   3      S31:  -0.5701 S32:   0.7063 S33:   0.3214                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: chain 'A' and (resid 148 through 170 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  13.5753  23.0041   0.0983              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1403 T22:   0.1898                                     
REMARK   3      T33:   0.1738 T12:   0.0328                                     
REMARK   3      T13:  -0.0524 T23:  -0.0755                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8710 L22:   6.2596                                     
REMARK   3      L33:   3.0751 L12:   2.0227                                     
REMARK   3      L13:  -1.3353 L23:  -2.7467                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0025 S12:   0.0609 S13:  -0.2071                       
REMARK   3      S21:   0.1030 S22:   0.0194 S23:  -0.4026                       
REMARK   3      S31:   0.1013 S32:   0.3749 S33:   0.0149                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: chain 'A' and (resid 171 through 187 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  18.4979  30.8766  -1.8321              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1772 T22:   0.3548                                     
REMARK   3      T33:   0.1539 T12:  -0.0510                                     
REMARK   3      T13:   0.0049 T23:  -0.1128                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8902 L22:   0.7366                                     
REMARK   3      L33:   1.0021 L12:  -0.2206                                     
REMARK   3      L13:  -0.6204 L23:   0.8338                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1094 S12:   0.1781 S13:  -0.1195                       
REMARK   3      S21:  -0.0944 S22:   0.0897 S23:  -0.3348                       
REMARK   3      S31:  -0.1789 S32:   0.7668 S33:  -0.0762                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: chain 'A' and (resid 188 through 231 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   5.1885  32.1855   1.0626              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1989 T22:   0.1305                                     
REMARK   3      T33:   0.1266 T12:  -0.0554                                     
REMARK   3      T13:   0.0165 T23:  -0.0149                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2240 L22:   1.2152                                     
REMARK   3      L33:   1.8489 L12:   0.1500                                     
REMARK   3      L13:   0.3857 L23:   0.6047                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2021 S12:  -0.1131 S13:   0.0922                       
REMARK   3      S21:   0.2790 S22:  -0.2053 S23:   0.1237                       
REMARK   3      S31:  -0.1936 S32:  -0.0112 S33:  -0.0317                       
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 4KW4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-JUN-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB079868.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-AUG-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 22-BM                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0000                             
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 31923                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.746                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 8.300                              
REMARK 200  R MERGE                    (I) : 0.08800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 8.7000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.81                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.82200                            
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: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.77                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.78                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 50 MM HEPES PH 8.2, 50 MM MGCL2, 22%     
REMARK 280  PEG4000, HANGING DROP, TEMPERATURE 294K                             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
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       56.98650            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       36.45200            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       36.45200            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       28.49325            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       36.45200            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       36.45200            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       85.47975            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       36.45200            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       36.45200            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       28.49325            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       36.45200            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       36.45200            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       85.47975            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       56.98650            
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A    -2                                                      
REMARK 465     SER A    -1                                                      
REMARK 465     MET A     0                                                      
REMARK 465     VAL A     1                                                      
REMARK 465     GLY A   232                                                      
REMARK 465     MET A   233                                                      
REMARK 465     ASP A   234                                                      
REMARK 465     GLU A   235                                                      
REMARK 465     LEU A   236                                                      
REMARK 465     TYR A   237                                                      
REMARK 465     LYS A   238                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A   3    CD   CE   NZ                                        
REMARK 470     GLU A   5    CD   OE1  OE2                                       
REMARK 470     GLU A   6    CD   OE1  OE2                                       
REMARK 470     LYS A  52    CE   NZ                                             
REMARK 470     LYS A 107    CE   NZ                                             
REMARK 470     LYS A 113    CE   NZ                                             
REMARK 470     LYS A 131    NZ                                                  
REMARK 470     GLU A 132    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 158    NZ                                                  
REMARK 470     LYS A 162    NZ                                                  
REMARK 470     LYS A 166    CD   CE   NZ                                        
REMARK 470     GLU A 172    CG   CD   OE1  OE2                                  
REMARK 470     LEU A 178    CG   CD1  CD2                                       
REMARK 470     GLN A 184    CD   OE1  NE2                                       
REMARK 470     LYS A 206    CE   NZ                                             
REMARK 470     LYS A 214    CD   CE   NZ                                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   HD1  HIS A   204     O    HOH A   373              1.46            
REMARK 500   O    HOH A   459     O    HOH A   539              2.19            
REMARK 500   O    HOH A   386     O    HOH A   416              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   OE1  GLU A   115     HE2  HIS A   204     3555     1.54            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4KW8   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4KW9   RELATED DB: PDB                                   
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 EMERALD GFP HAS LEU AT POSITION 64, THR AT 65, ALA AT 72, LYS AT     
REMARK 999 149, THR AT 153, 167, LEU AT 231. RESIDUES THR 65, TYR 66, GLY 67    
REMARK 999 FORM A CHROMOPHORE CRO 66                                            
DBREF  4KW4 A    2   238  UNP    P42212   GFP_AEQVI        2    238             
SEQADV 4KW4 GLY A   -2  UNP  P42212              EXPRESSION TAG                 
SEQADV 4KW4 SER A   -1  UNP  P42212              EXPRESSION TAG                 
SEQADV 4KW4 MET A    0  UNP  P42212              EXPRESSION TAG                 
SEQADV 4KW4 VAL A    1  UNP  P42212              EXPRESSION TAG                 
SEQADV 4KW4 LEU A   64  UNP  P42212    PHE    64 SEE REMARK 999                 
SEQADV 4KW4 CRO A   66  UNP  P42212    SER    65 CHROMOPHORE, REM 999           
SEQADV 4KW4 CRO A   66  UNP  P42212    TYR    66 CHROMOPHORE                    
SEQADV 4KW4 CRO A   66  UNP  P42212    GLY    67 CHROMOPHORE                    
SEQADV 4KW4 ALA A   72  UNP  P42212    SER    72 SEE REMARK 999                 
SEQADV 4KW4 HIS A  147  UNP  P42212    SER   147 ENGINEERED MUTATION            
SEQADV 4KW4 LYS A  149  UNP  P42212    ASN   149 SEE REMARK 999                 
SEQADV 4KW4 THR A  153  UNP  P42212    MET   153 SEE REMARK 999                 
SEQADV 4KW4 THR A  167  UNP  P42212    ILE   167 SEE REMARK 999                 
SEQADV 4KW4 HIS A  202  UNP  P42212    SER   202 ENGINEERED MUTATION            
SEQADV 4KW4 HIS A  204  UNP  P42212    GLN   204 ENGINEERED MUTATION            
SEQADV 4KW4 LYS A  206  UNP  P42212    ALA   206 ENGINEERED MUTATION            
SEQADV 4KW4 LEU A  231  UNP  P42212    HIS   231 SEE REMARK 999                 
SEQRES   1 A  239  GLY SER MET VAL SER LYS GLY GLU GLU LEU PHE THR GLY          
SEQRES   2 A  239  VAL VAL PRO ILE LEU VAL GLU LEU ASP GLY ASP VAL ASN          
SEQRES   3 A  239  GLY HIS LYS PHE SER VAL SER GLY GLU GLY GLU GLY ASP          
SEQRES   4 A  239  ALA THR TYR GLY LYS LEU THR LEU LYS PHE ILE CYS THR          
SEQRES   5 A  239  THR GLY LYS LEU PRO VAL PRO TRP PRO THR LEU VAL THR          
SEQRES   6 A  239  THR LEU CRO VAL GLN CYS PHE ALA ARG TYR PRO ASP HIS          
SEQRES   7 A  239  MET LYS GLN HIS ASP PHE PHE LYS SER ALA MET PRO GLU          
SEQRES   8 A  239  GLY TYR VAL GLN GLU ARG THR ILE PHE PHE LYS ASP ASP          
SEQRES   9 A  239  GLY ASN TYR LYS THR ARG ALA GLU VAL LYS PHE GLU GLY          
SEQRES  10 A  239  ASP THR LEU VAL ASN ARG ILE GLU LEU LYS GLY ILE ASP          
SEQRES  11 A  239  PHE LYS GLU ASP GLY ASN ILE LEU GLY HIS LYS LEU GLU          
SEQRES  12 A  239  TYR ASN TYR ASN HIS HIS LYS VAL TYR ILE THR ALA ASP          
SEQRES  13 A  239  LYS GLN LYS ASN GLY ILE LYS VAL ASN PHE LYS THR ARG          
SEQRES  14 A  239  HIS ASN ILE GLU ASP GLY SER VAL GLN LEU ALA ASP HIS          
SEQRES  15 A  239  TYR GLN GLN ASN THR PRO ILE GLY ASP GLY PRO VAL LEU          
SEQRES  16 A  239  LEU PRO ASP ASN HIS TYR LEU HIS THR HIS SER LYS LEU          
SEQRES  17 A  239  SER LYS ASP PRO ASN GLU LYS ARG ASP HIS MET VAL LEU          
SEQRES  18 A  239  LEU GLU PHE VAL THR ALA ALA GLY ILE THR LEU GLY MET          
SEQRES  19 A  239  ASP GLU LEU TYR LYS                                          
MODRES 4KW4 CRO A   66  GLY                                                     
MODRES 4KW4 CRO A   66  TYR                                                     
MODRES 4KW4 CRO A   66  GLY                                                     
HET    CRO  A  66      22                                                       
HETNAM     CRO {2-[(1R,2R)-1-AMINO-2-HYDROXYPROPYL]-4-(4-                       
HETNAM   2 CRO  HYDROXYBENZYLIDENE)-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-            
HETNAM   3 CRO  YL}ACETIC ACID                                                  
HETSYN     CRO PEPTIDE DERIVED CHROMOPHORE                                      
FORMUL   1  CRO    C15 H17 N3 O5                                                
FORMUL   2  HOH   *303(H2 O)                                                    
HELIX    1   1 LYS A    3  THR A    9  5                                   7    
HELIX    2   2 PRO A   56  VAL A   61  5                                   6    
HELIX    3   3 VAL A   68  ALA A   72  5                                   5    
HELIX    4   4 PRO A   75  HIS A   81  5                                   7    
HELIX    5   5 ASP A   82  ALA A   87  1                                   6    
HELIX    6   6 LYS A  156  ASN A  159  5                                   4    
SHEET    1   A12 VAL A  11  VAL A  22  0                                        
SHEET    2   A12 HIS A  25  ASP A  36 -1  O  GLY A  31   N  VAL A  16           
SHEET    3   A12 LYS A  41  CYS A  48 -1  O  LYS A  41   N  ASP A  36           
SHEET    4   A12 HIS A 217  ALA A 227 -1  O  LEU A 220   N  LEU A  44           
SHEET    5   A12 HIS A 199  SER A 208 -1  N  HIS A 202   O  THR A 225           
SHEET    6   A12 HIS A 147  ASP A 155 -1  N  ILE A 152   O  HIS A 199           
SHEET    7   A12 GLY A 160  ASN A 170 -1  O  GLY A 160   N  ASP A 155           
SHEET    8   A12 VAL A 176  PRO A 187 -1  O  HIS A 181   N  PHE A 165           
SHEET    9   A12 TYR A  92  PHE A 100 -1  N  GLU A  95   O  GLN A 184           
SHEET   10   A12 ASN A 105  GLU A 115 -1  O  TYR A 106   N  ILE A  98           
SHEET   11   A12 THR A 118  ILE A 128 -1  O  VAL A 120   N  LYS A 113           
SHEET   12   A12 VAL A  11  VAL A  22  1  N  ASP A  21   O  GLY A 127           
LINK         C   LEU A  64                 N1  CRO A  66     1555   1555  1.33  
LINK         C3  CRO A  66                 N   VAL A  68     1555   1555  1.35  
CISPEP   1 MET A   88    PRO A   89          0         6.13                     
CRYST1   72.904   72.904  113.973  90.00  90.00  90.00 P 41 21 2     8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.013717  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013717  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008774        0.00000                         
ATOM      1  N   SER A   2      -5.112  18.146   9.119  1.00 46.40           N  
ANISOU    1  N   SER A   2     4363   4730   8536   -491    249   -795       N  
ATOM      2  CA  SER A   2      -4.513  18.180  10.455  1.00 46.93           C  
ANISOU    2  CA  SER A   2     4424   4709   8699   -465    183   -414       C  
ATOM      3  C   SER A   2      -5.223  19.209  11.341  1.00 47.15           C  
ANISOU    3  C   SER A   2     4560   4948   8406   -524    144   -159       C  
ATOM      4  O   SER A   2      -5.829  20.157  10.842  1.00 47.19           O  
ANISOU    4  O   SER A   2     4682   5166   8083   -548    166   -294       O  
ATOM      5  CB  SER A   2      -3.006  18.498  10.372  1.00 36.38           C  
ANISOU    5  CB  SER A   2     3082   3364   7376   -425    177   -446       C  
ATOM      6  OG  SER A   2      -2.785  19.868  10.093  1.00 25.89           O  
ANISOU    6  OG  SER A   2     1885   2295   5659   -467    181   -526       O  
ATOM      7  HA  SER A   2      -4.613  17.308  10.868  1.00 56.32           H  
ATOM      8  HB2 SER A   2      -2.591  18.279  11.222  1.00 43.65           H  
ATOM      9  HB3 SER A   2      -2.610  17.965   9.665  1.00 43.65           H  
ATOM     10  HG  SER A   2      -1.961  20.024  10.051  1.00 31.07           H  
ATOM     11  N   LYS A   3      -5.149  19.014  12.655  1.00 44.41           N  
ANISOU   11  N   LYS A   3     4182   4579   8113   -524     88    221       N  
ATOM     12  CA  LYS A   3      -5.696  19.981  13.600  1.00 39.63           C  
ANISOU   12  CA  LYS A   3     3696   4231   7131   -554     65    445       C  
ATOM     13  C   LYS A   3      -5.092  21.382  13.346  1.00 22.64           C  
ANISOU   13  C   LYS A   3     1729   2305   4570   -519     81    313       C  
ATOM     14  O   LYS A   3      -5.801  22.379  13.343  1.00 24.47           O  
ANISOU   14  O   LYS A   3     2093   2728   4478   -523    107    265       O  
ATOM     15  CB  LYS A   3      -5.431  19.502  15.036  1.00 42.61           C  
ANISOU   15  CB  LYS A   3     3967   4613   7609   -581      0    873       C  
ATOM     16  CG  LYS A   3      -5.221  20.607  16.054  1.00 40.19           C  
ANISOU   16  CG  LYS A   3     3777   4631   6861   -602    -22   1047       C  
ATOM     17  H   LYS A   3      -4.785  18.328  13.026  1.00 53.29           H  
ATOM     18  HA  LYS A   3      -6.656  20.039  13.474  1.00 47.56           H  
ATOM     19  HB2 LYS A   3      -6.189  18.974  15.329  1.00 51.13           H  
ATOM     20  HB3 LYS A   3      -4.632  18.951  15.034  1.00 51.13           H  
ATOM     21  N   GLY A   4      -3.784  21.447  13.110  1.00 22.73           N  
ANISOU   21  N   GLY A   4     1729   2272   4637   -485     72    254       N  
ATOM     22  CA  GLY A   4      -3.152  22.729  12.830  1.00 21.03           C  
ANISOU   22  CA  GLY A   4     1668   2241   4079   -462     92    133       C  
ATOM     23  C   GLY A   4      -3.779  23.455  11.639  1.00 22.73           C  
ANISOU   23  C   GLY A   4     1985   2552   4100   -457    145   -137       C  
ATOM     24  O   GLY A   4      -3.896  24.685  11.625  1.00 18.50           O  
ANISOU   24  O   GLY A   4     1584   2186   3259   -447    167   -155       O  
ATOM     25  H   GLY A   4      -3.248  20.774  13.106  1.00 27.28           H  
ATOM     26  HA2 GLY A   4      -3.227  23.301  13.610  1.00 25.23           H  
ATOM     27  HA3 GLY A   4      -2.211  22.590  12.642  1.00 25.23           H  
ATOM     28  N   GLU A   5      -4.204  22.678  10.648  1.00 26.98           N  
ANISOU   28  N   GLU A   5     2427   2986   4837   -473    168   -339       N  
ATOM     29  CA  GLU A   5      -4.779  23.224   9.416  1.00 27.97           C  
ANISOU   29  CA  GLU A   5     2596   3256   4774   -489    206   -578       C  
ATOM     30  C   GLU A   5      -6.006  24.083   9.704  1.00 26.00           C  
ANISOU   30  C   GLU A   5     2450   3161   4270   -488    209   -470       C  
ATOM     31  O   GLU A   5      -6.292  25.051   8.993  1.00 22.42           O  
ANISOU   31  O   GLU A   5     2067   2873   3577   -480    229   -546       O  
ATOM     32  CB  GLU A   5      -5.157  22.070   8.479  1.00 39.76           C  
ANISOU   32  CB  GLU A   5     3925   4642   6539   -538    233   -825       C  
ATOM     33  CG  GLU A   5      -5.678  22.501   7.133  1.00 44.07           C  
ANISOU   33  CG  GLU A   5     4465   5407   6873   -583    265  -1079       C  
ATOM     34  H   GLU A   5      -4.172  21.818  10.663  1.00 32.37           H  
ATOM     35  HA  GLU A   5      -4.118  23.776   8.970  1.00 33.56           H  
ATOM     36  HB2 GLU A   5      -4.370  21.524   8.328  1.00 47.71           H  
ATOM     37  HB3 GLU A   5      -5.847  21.538   8.905  1.00 47.71           H  
ATOM     38  HG2 GLU A   5      -6.074  21.735   6.688  1.00 52.88           H  
ATOM     39  HG3 GLU A   5      -6.346  23.192   7.260  1.00 52.88           H  
ATOM     40  N   GLU A   6      -6.744  23.732  10.751  1.00 19.28           N  
ANISOU   40  N   GLU A   6     1582   2259   3484   -497    192   -273       N  
ATOM     41  CA  GLU A   6      -7.976  24.448  11.066  1.00 18.23           C  
ANISOU   41  CA  GLU A   6     1515   2259   3150   -497    207   -193       C  
ATOM     42  C   GLU A   6      -7.686  25.906  11.418  1.00 20.81           C  
ANISOU   42  C   GLU A   6     1977   2727   3202   -460    231   -142       C  
ATOM     43  O   GLU A   6      -8.556  26.781  11.285  1.00 24.77           O  
ANISOU   43  O   GLU A   6     2529   3334   3549   -441    260   -142       O  
ATOM     44  CB  GLU A   6      -8.708  23.737  12.221  1.00 19.06           C  
ANISOU   44  CB  GLU A   6     1556   2308   3377   -531    189     15       C  
ATOM     45  CG  GLU A   6      -8.909  22.242  11.972  1.00 27.45           C  
ANISOU   45  CG  GLU A   6     2461   3170   4800   -572    172    -10       C  
ATOM     46  H   GLU A   6      -6.557  23.089  11.290  1.00 23.13           H  
ATOM     47  HA  GLU A   6      -8.557  24.437  10.289  1.00 21.87           H  
ATOM     48  HB2 GLU A   6      -8.188  23.837  13.034  1.00 22.87           H  
ATOM     49  HB3 GLU A   6      -9.583  24.140  12.336  1.00 22.87           H  
ATOM     50  N   LEU A   7      -6.459  26.181  11.851  1.00 18.92           N  
ANISOU   50  N   LEU A   7     1776   2476   2936   -450    223   -105       N  
ATOM     51  CA  LEU A   7      -6.078  27.546  12.215  1.00 15.87           C  
ANISOU   51  CA  LEU A   7     1498   2198   2332   -431    259    -90       C  
ATOM     52  C   LEU A   7      -5.914  28.481  10.998  1.00 15.26           C  
ANISOU   52  C   LEU A   7     1477   2171   2150   -399    287   -221       C  
ATOM     53  O   LEU A   7      -5.780  29.692  11.166  1.00 18.66           O  
ANISOU   53  O   LEU A   7     1981   2654   2455   -381    328   -209       O  
ATOM     54  CB  LEU A   7      -4.777  27.547  13.019  1.00 15.99           C  
ANISOU   54  CB  LEU A   7     1519   2215   2340   -447    240    -20       C  
ATOM     55  CG  LEU A   7      -4.761  26.694  14.297  1.00 19.60           C  
ANISOU   55  CG  LEU A   7     1890   2682   2876   -493    198    182       C  
ATOM     56  CD1 LEU A   7      -3.339  26.613  14.843  1.00 20.58           C  
ANISOU   56  CD1 LEU A   7     1986   2829   3006   -508    162    258       C  
ATOM     57  CD2 LEU A   7      -5.704  27.238  15.360  1.00 25.52           C  
ANISOU   57  CD2 LEU A   7     2653   3589   3455   -533    232    273       C  
ATOM     58  H   LEU A   7      -5.831  25.600  11.943  1.00 22.70           H  
ATOM     59  HA  LEU A   7      -6.773  27.919  12.780  1.00 19.04           H  
ATOM     60  HB2 LEU A   7      -4.066  27.219  12.446  1.00 19.18           H  
ATOM     61  HB3 LEU A   7      -4.582  28.460  13.280  1.00 19.18           H  
ATOM     62  HG  LEU A   7      -5.047  25.794  14.077  1.00 23.52           H  
ATOM     63 HD11 LEU A   7      -3.341  26.073  15.648  1.00 24.70           H  
ATOM     64 HD12 LEU A   7      -2.767  26.207  14.173  1.00 24.70           H  
ATOM     65 HD13 LEU A   7      -3.028  27.509  15.045  1.00 24.70           H  
ATOM     66 HD21 LEU A   7      -5.658  26.668  16.143  1.00 30.63           H  
ATOM     67 HD22 LEU A   7      -5.433  28.140  15.590  1.00 30.63           H  
ATOM     68 HD23 LEU A   7      -6.607  27.244  15.007  1.00 30.63           H  
ATOM     69  N   PHE A   8      -5.933  27.930   9.787  1.00 15.59           N  
ANISOU   69  N   PHE A   8     1460   2212   2253   -407    270   -343       N  
ATOM     70  CA  PHE A   8      -5.649  28.735   8.587  1.00 15.43           C  
ANISOU   70  CA  PHE A   8     1457   2300   2105   -401    286   -428       C  
ATOM     71  C   PHE A   8      -6.845  28.861   7.651  1.00 17.31           C  
ANISOU   71  C   PHE A   8     1639   2662   2276   -409    284   -450       C  
ATOM     72  O   PHE A   8      -6.705  29.257   6.498  1.00 21.14           O  
ANISOU   72  O   PHE A   8     2086   3293   2652   -428    282   -504       O  
ATOM     73  CB  PHE A   8      -4.455  28.144   7.825  1.00 15.83           C  
ANISOU   73  CB  PHE A   8     1455   2345   2215   -428    276   -577       C  
ATOM     74  CG  PHE A   8      -3.159  28.224   8.591  1.00 15.48           C  
ANISOU   74  CG  PHE A   8     1455   2214   2212   -416    274   -538       C  
ATOM     75  CD1 PHE A   8      -2.281  29.264   8.384  1.00 15.00           C  
ANISOU   75  CD1 PHE A   8     1462   2216   2021   -410    296   -536       C  
ATOM     76  CD2 PHE A   8      -2.843  27.253   9.557  1.00 15.89           C  
ANISOU   76  CD2 PHE A   8     1459   2133   2445   -417    245   -472       C  
ATOM     77  CE1 PHE A   8      -1.068  29.344   9.124  1.00 15.80           C  
ANISOU   77  CE1 PHE A   8     1591   2263   2148   -409    292   -507       C  
ATOM     78  CE2 PHE A   8      -1.654  27.324  10.284  1.00 15.83           C  
ANISOU   78  CE2 PHE A   8     1466   2089   2459   -412    230   -406       C  
ATOM     79  CZ  PHE A   8      -0.772  28.360  10.073  1.00 15.23           C  
ANISOU   79  CZ  PHE A   8     1464   2090   2230   -410    255   -442       C  
ATOM     80  H   PHE A   8      -6.106  27.103   9.627  1.00 18.71           H  
ATOM     81  HA  PHE A   8      -5.402  29.630   8.869  1.00 18.51           H  
ATOM     82  HB2 PHE A   8      -4.634  27.209   7.638  1.00 19.00           H  
ATOM     83  HB3 PHE A   8      -4.341  28.632   6.995  1.00 19.00           H  
ATOM     84  HD1 PHE A   8      -2.480  29.917   7.754  1.00 18.00           H  
ATOM     85  HD2 PHE A   8      -3.432  26.549   9.709  1.00 19.07           H  
ATOM     86  HE1 PHE A   8      -0.475  30.045   8.975  1.00 18.96           H  
ATOM     87  HE2 PHE A   8      -1.457  26.670  10.915  1.00 18.99           H  
ATOM     88  HZ  PHE A   8       0.020  28.404  10.557  1.00 18.27           H  
ATOM     89  N   THR A   9      -8.035  28.552   8.145  1.00 21.85           N  
ANISOU   89  N   THR A   9     2190   3216   2896   -404    281   -390       N  
ATOM     90  CA  THR A   9      -9.191  28.522   7.246  1.00 27.23           C  
ANISOU   90  CA  THR A   9     2790   4034   3522   -422    269   -414       C  
ATOM     91  C   THR A   9      -9.616  29.918   6.795  1.00 28.84           C  
ANISOU   91  C   THR A   9     3015   4359   3584   -377    283   -289       C  
ATOM     92  O   THR A   9     -10.287  30.050   5.783  1.00 27.58           O  
ANISOU   92  O   THR A   9     2765   4378   3339   -398    261   -280       O  
ATOM     93  CB  THR A   9     -10.382  27.805   7.883  1.00 26.11           C  
ANISOU   93  CB  THR A   9     2604   3838   3480   -433    263   -379       C  
ATOM     94  OG1 THR A   9     -10.595  28.317   9.195  1.00 23.82           O  
ANISOU   94  OG1 THR A   9     2391   3469   3192   -393    291   -239       O  
ATOM     95  CG2 THR A   9     -10.106  26.317   7.962  1.00 35.34           C  
ANISOU   95  CG2 THR A   9     3693   4885   4849   -490    245   -496       C  
ATOM     96  H   THR A   9      -8.202  28.361   8.967  1.00 26.22           H  
ATOM     97  HA  THR A   9      -8.945  28.023   6.451  1.00 32.68           H  
ATOM     98  HB  THR A   9     -11.175  27.947   7.344  1.00 31.34           H  
ATOM     99  HG1 THR A   9     -10.754  29.141   9.159  1.00 28.59           H  
ATOM    100 HG21 THR A   9     -10.861  25.861   8.365  1.00 42.41           H  
ATOM    101 HG22 THR A   9      -9.961  25.959   7.072  1.00 42.41           H  
ATOM    102 HG23 THR A   9      -9.315  26.154   8.500  1.00 42.41           H  
ATOM    103  N   GLY A  10      -9.230  30.943   7.545  1.00 23.64           N  
ANISOU  103  N   GLY A  10     2448   3611   2923   -325    324   -189       N  
ATOM    104  CA  GLY A  10      -9.578  32.310   7.199  1.00 25.42           C  
ANISOU  104  CA  GLY A  10     2671   3880   3108   -274    352    -55       C  
ATOM    105  C   GLY A  10      -8.340  33.182   7.076  1.00 26.09           C  
ANISOU  105  C   GLY A  10     2816   3924   3173   -267    379    -35       C  
ATOM    106  O   GLY A  10      -7.225  32.685   6.866  1.00 19.90           O  
ANISOU  106  O   GLY A  10     2058   3149   2355   -308    362   -135       O  
ATOM    107  H   GLY A  10      -8.763  30.871   8.264  1.00 28.37           H  
ATOM    108  HA2 GLY A  10     -10.052  32.322   6.353  1.00 30.51           H  
ATOM    109  HA3 GLY A  10     -10.154  32.684   7.884  1.00 30.51           H  
ATOM    110  N   VAL A  11      -8.536  34.487   7.218  1.00 17.94           N  
ANISOU  110  N   VAL A  11     1789   2828   2198   -215    430     87       N  
ATOM    111  CA  VAL A  11      -7.437  35.444   7.112  1.00 21.14           C  
ANISOU  111  CA  VAL A  11     2238   3170   2624   -213    468    120       C  
ATOM    112  C   VAL A  11      -6.775  35.535   8.492  1.00 22.02           C  
ANISOU  112  C   VAL A  11     2444   3132   2789   -220    524      2       C  
ATOM    113  O   VAL A  11      -7.463  35.711   9.478  1.00 16.51           O  
ANISOU  113  O   VAL A  11     1751   2364   2158   -200    573    -25       O  
ATOM    114  CB  VAL A  11      -7.946  36.824   6.695  1.00 21.80           C  
ANISOU  114  CB  VAL A  11     2253   3210   2821   -158    509    313       C  
ATOM    115  CG1 VAL A  11      -6.808  37.853   6.705  1.00 19.85           C  
ANISOU  115  CG1 VAL A  11     2042   2852   2649   -165    563    343       C  
ATOM    116  CG2 VAL A  11      -8.580  36.774   5.296  1.00 24.91           C  
ANISOU  116  CG2 VAL A  11     2518   3827   3122   -168    437    485       C  
ATOM    117  H   VAL A  11      -9.300  34.848   7.377  1.00 21.52           H  
ATOM    118  HA  VAL A  11      -6.784  35.135   6.465  1.00 25.37           H  
ATOM    119  HB  VAL A  11      -8.623  37.117   7.324  1.00 26.16           H  
ATOM    120 HG11 VAL A  11      -7.161  38.715   6.437  1.00 23.82           H  
ATOM    121 HG12 VAL A  11      -6.441  37.909   7.601  1.00 23.82           H  
ATOM    122 HG13 VAL A  11      -6.121  37.568   6.082  1.00 23.82           H  
ATOM    123 HG21 VAL A  11      -8.893  37.662   5.060  1.00 29.90           H  
ATOM    124 HG22 VAL A  11      -7.913  36.477   4.658  1.00 29.90           H  
ATOM    125 HG23 VAL A  11      -9.326  36.154   5.310  1.00 29.90           H  
ATOM    126  N   VAL A  12      -5.458  35.399   8.539  1.00 15.48           N  
ANISOU  126  N   VAL A  12     1669   2297   1914   -261    518    -73       N  
ATOM    127  CA  VAL A  12      -4.697  35.315   9.779  1.00 16.91           C  
ANISOU  127  CA  VAL A  12     1915   2410   2101   -291    549   -177       C  
ATOM    128  C   VAL A  12      -3.711  36.468   9.818  1.00 15.31           C  
ANISOU  128  C   VAL A  12     1742   2138   1938   -305    609   -192       C  
ATOM    129  O   VAL A  12      -2.975  36.692   8.855  1.00 15.45           O  
ANISOU  129  O   VAL A  12     1753   2189   1928   -317    589   -150       O  
ATOM    130  CB  VAL A  12      -3.885  33.996   9.836  1.00 14.40           C  
ANISOU  130  CB  VAL A  12     1605   2141   1724   -331    480   -246       C  
ATOM    131  CG1 VAL A  12      -3.001  33.951  11.068  1.00 14.23           C  
ANISOU  131  CG1 VAL A  12     1620   2098   1687   -370    496   -299       C  
ATOM    132  CG2 VAL A  12      -4.839  32.773   9.809  1.00 14.82           C  
ANISOU  132  CG2 VAL A  12     1609   2225   1796   -329    428   -241       C  
ATOM    133  H   VAL A  12      -4.963  35.352   7.838  1.00 18.57           H  
ATOM    134  HA  VAL A  12      -5.288  35.367  10.546  1.00 20.30           H  
ATOM    135  HB  VAL A  12      -3.312  33.946   9.055  1.00 17.28           H  
ATOM    136 HG11 VAL A  12      -2.508  33.116  11.073  1.00 17.07           H  
ATOM    137 HG12 VAL A  12      -2.384  34.699  11.041  1.00 17.07           H  
ATOM    138 HG13 VAL A  12      -3.559  34.011  11.859  1.00 17.07           H  
ATOM    139 HG21 VAL A  12      -4.310  31.961   9.845  1.00 17.78           H  
ATOM    140 HG22 VAL A  12      -5.431  32.818  10.576  1.00 17.78           H  
ATOM    141 HG23 VAL A  12      -5.357  32.795   8.989  1.00 17.78           H  
ATOM    142  N   PRO A  13      -3.681  37.219  10.923  1.00 15.72           N  
ANISOU  142  N   PRO A  13     1808   2109   2055   -319    693   -271       N  
ATOM    143  CA  PRO A  13      -2.708  38.298  10.989  1.00 16.25           C  
ANISOU  143  CA  PRO A  13     1889   2094   2191   -349    760   -318       C  
ATOM    144  C   PRO A  13      -1.299  37.756  11.229  1.00 15.61           C  
ANISOU  144  C   PRO A  13     1852   2088   1991   -411    718   -396       C  
ATOM    145  O   PRO A  13      -1.111  36.719  11.876  1.00 15.58           O  
ANISOU  145  O   PRO A  13     1857   2175   1888   -437    663   -434       O  
ATOM    146  CB  PRO A  13      -3.202  39.136  12.186  1.00 17.21           C  
ANISOU  146  CB  PRO A  13     1983   2134   2424   -365    876   -448       C  
ATOM    147  CG  PRO A  13      -4.054  38.273  12.954  1.00 23.20           C  
ANISOU  147  CG  PRO A  13     2731   2995   3089   -369    851   -479       C  
ATOM    148  CD  PRO A  13      -4.620  37.248  12.058  1.00 16.09           C  
ANISOU  148  CD  PRO A  13     1833   2151   2129   -321    746   -337       C  
ATOM    149  HA  PRO A  13      -2.727  38.833  10.180  1.00 19.50           H  
ATOM    150  HB2 PRO A  13      -2.442  39.423  12.715  1.00 20.66           H  
ATOM    151  HB3 PRO A  13      -3.700  39.902  11.860  1.00 20.66           H  
ATOM    152  HG2 PRO A  13      -3.529  37.851  13.652  1.00 27.84           H  
ATOM    153  HG3 PRO A  13      -4.766  38.801  13.347  1.00 27.84           H  
ATOM    154  HD2 PRO A  13      -4.639  36.386  12.501  1.00 19.31           H  
ATOM    155  HD3 PRO A  13      -5.503  37.513  11.758  1.00 19.31           H  
ATOM    156  N   ILE A  14      -0.317  38.474  10.707  1.00 15.91           N  
ANISOU  156  N   ILE A  14     1898   2083   2064   -435    743   -392       N  
ATOM    157  CA  ILE A  14       1.062  38.055  10.753  1.00 15.46           C  
ANISOU  157  CA  ILE A  14     1866   2097   1910   -488    704   -454       C  
ATOM    158  C   ILE A  14       1.929  39.182  11.312  1.00 16.23           C  
ANISOU  158  C   ILE A  14     1968   2127   2074   -551    791   -555       C  
ATOM    159  O   ILE A  14       1.740  40.343  10.960  1.00 17.19           O  
ANISOU  159  O   ILE A  14     2064   2112   2354   -543    871   -523       O  
ATOM    160  CB  ILE A  14       1.584  37.742   9.323  1.00 15.25           C  
ANISOU  160  CB  ILE A  14     1826   2132   1837   -478    647   -368       C  
ATOM    161  CG1 ILE A  14       0.793  36.587   8.710  1.00 14.81           C  
ANISOU  161  CG1 ILE A  14     1742   2164   1723   -440    571   -328       C  
ATOM    162  CG2 ILE A  14       3.084  37.397   9.343  1.00 14.98           C  
ANISOU  162  CG2 ILE A  14     1801   2159   1733   -530    621   -448       C  
ATOM    163  CD1 ILE A  14       1.087  36.367   7.221  1.00 15.12           C  
ANISOU  163  CD1 ILE A  14     1728   2326   1690   -453    533   -280       C  
ATOM    164  H   ILE A  14      -0.434  39.229  10.311  1.00 19.09           H  
ATOM    165  HA  ILE A  14       1.158  37.267  11.311  1.00 18.55           H  
ATOM    166  HB  ILE A  14       1.457  38.529   8.770  1.00 18.30           H  
ATOM    167 HG12 ILE A  14       1.015  35.769   9.182  1.00 17.77           H  
ATOM    168 HG13 ILE A  14      -0.155  36.773   8.802  1.00 17.77           H  
ATOM    169 HG21 ILE A  14       3.377  37.207   8.438  1.00 17.98           H  
ATOM    170 HG22 ILE A  14       3.577  38.153   9.699  1.00 17.98           H  
ATOM    171 HG23 ILE A  14       3.221  36.618   9.905  1.00 17.98           H  
ATOM    172 HD11 ILE A  14       0.553  35.623   6.901  1.00 18.14           H  
ATOM    173 HD12 ILE A  14       0.859  37.173   6.732  1.00 18.14           H  
ATOM    174 HD13 ILE A  14       2.030  36.169   7.112  1.00 18.14           H  
ATOM    175  N   LEU A  15       2.889  38.813  12.151  1.00 16.08           N  
ANISOU  175  N   LEU A  15     1955   2202   1954   -616    774   -664       N  
ATOM    176  CA  LEU A  15       3.971  39.699  12.575  1.00 16.84           C  
ANISOU  176  CA  LEU A  15     2042   2280   2076   -698    841   -783       C  
ATOM    177  C   LEU A  15       5.297  39.050  12.273  1.00 16.30           C  
ANISOU  177  C   LEU A  15     1978   2315   1899   -727    765   -772       C  
ATOM    178  O   LEU A  15       5.497  37.869  12.550  1.00 15.70           O  
ANISOU  178  O   LEU A  15     1891   2353   1723   -715    675   -742       O  
ATOM    179  CB  LEU A  15       3.901  39.970  14.092  1.00 17.71           C  
ANISOU  179  CB  LEU A  15     2115   2475   2138   -782    903   -962       C  
ATOM    180  CG  LEU A  15       2.725  40.790  14.579  1.00 18.74           C  
ANISOU  180  CG  LEU A  15     2211   2504   2406   -776   1015  -1056       C  
ATOM    181  CD1 LEU A  15       2.729  40.816  16.144  1.00 22.96           C  
ANISOU  181  CD1 LEU A  15     2680   3233   2810   -891   1069  -1268       C  
ATOM    182  CD2 LEU A  15       2.784  42.211  14.035  1.00 22.26           C  
ANISOU  182  CD2 LEU A  15     2631   2711   3118   -773   1133  -1096       C  
ATOM    183  H   LEU A  15       2.937  38.029  12.501  1.00 19.30           H  
ATOM    184  HA  LEU A  15       3.915  40.543  12.100  1.00 20.21           H  
ATOM    185  HB2 LEU A  15       3.865  39.116  14.551  1.00 21.25           H  
ATOM    186  HB3 LEU A  15       4.707  40.441  14.354  1.00 21.25           H  
ATOM    187  HG  LEU A  15       1.899  40.380  14.280  1.00 22.49           H  
ATOM    188 HD11 LEU A  15       1.974  41.342  16.453  1.00 27.55           H  
ATOM    189 HD12 LEU A  15       2.656  39.907  16.475  1.00 27.55           H  
ATOM    190 HD13 LEU A  15       3.558  41.214  16.451  1.00 27.55           H  
ATOM    191 HD21 LEU A  15       2.019  42.707  14.365  1.00 26.72           H  
ATOM    192 HD22 LEU A  15       3.606  42.630  14.335  1.00 26.72           H  
ATOM    193 HD23 LEU A  15       2.765  42.179  13.065  1.00 26.72           H  
ATOM    194  N   VAL A  16       6.207  39.826  11.711  1.00 16.74           N  
ANISOU  194  N   VAL A  16     2032   2320   2008   -765    805   -787       N  
ATOM    195  CA  VAL A  16       7.551  39.367  11.418  1.00 16.46           C  
ANISOU  195  CA  VAL A  16     1985   2382   1886   -799    751   -800       C  
ATOM    196  C   VAL A  16       8.562  40.315  12.066  1.00 17.42           C  
ANISOU  196  C   VAL A  16     2085   2505   2029   -903    822   -936       C  
ATOM    197  O   VAL A  16       8.412  41.536  11.998  1.00 18.41           O  
ANISOU  197  O   VAL A  16     2203   2487   2303   -939    926   -979       O  
ATOM    198  CB  VAL A  16       7.799  39.343   9.911  1.00 16.28           C  
ANISOU  198  CB  VAL A  16     1959   2349   1876   -766    730   -689       C  
ATOM    199  CG1 VAL A  16       9.166  38.779   9.593  1.00 16.12           C  
ANISOU  199  CG1 VAL A  16     1909   2440   1775   -799    682   -732       C  
ATOM    200  CG2 VAL A  16       6.693  38.517   9.189  1.00 15.69           C  
ANISOU  200  CG2 VAL A  16     1884   2299   1779   -685    673   -590       C  
ATOM    201  H   VAL A  16       6.066  40.643  11.484  1.00 20.08           H  
ATOM    202  HA  VAL A  16       7.682  38.474  11.774  1.00 19.75           H  
ATOM    203  HB  VAL A  16       7.764  40.251   9.571  1.00 19.53           H  
ATOM    204 HG11 VAL A  16       9.291  38.777   8.631  1.00 19.34           H  
ATOM    205 HG12 VAL A  16       9.842  39.333  10.014  1.00 19.34           H  
ATOM    206 HG13 VAL A  16       9.220  37.873   9.935  1.00 19.34           H  
ATOM    207 HG21 VAL A  16       6.872  38.516   8.236  1.00 18.83           H  
ATOM    208 HG22 VAL A  16       6.706  37.608   9.529  1.00 18.83           H  
ATOM    209 HG23 VAL A  16       5.831  38.924   9.364  1.00 18.83           H  
ATOM    210  N   GLU A  17       9.595  39.732  12.671  1.00 18.42           N  
ANISOU  210  N   GLU A  17     2178   2785   2035   -954    767   -995       N  
ATOM    211  CA  GLU A  17      10.673  40.491  13.276  1.00 18.40           C  
ANISOU  211  CA  GLU A  17     2136   2837   2018  -1069    821  -1137       C  
ATOM    212  C   GLU A  17      11.973  39.835  12.881  1.00 18.08           C  
ANISOU  212  C   GLU A  17     2063   2908   1900  -1076    743  -1100       C  
ATOM    213  O   GLU A  17      12.101  38.609  12.958  1.00 17.55           O  
ANISOU  213  O   GLU A  17     1966   2939   1764  -1021    641  -1020       O  
ATOM    214  CB  GLU A  17      10.509  40.475  14.785  1.00 19.23           C  
ANISOU  214  CB  GLU A  17     2186   3098   2024  -1150    829  -1259       C  
ATOM    215  CG  GLU A  17       9.211  41.107  15.230  1.00 22.51           C  
ANISOU  215  CG  GLU A  17     2608   3413   2534  -1145    914  -1327       C  
ATOM    216  CD  GLU A  17       9.212  42.599  15.067  1.00 27.80           C  
ANISOU  216  CD  GLU A  17     3263   3887   3413  -1201   1065  -1473       C  
ATOM    217  OE1 GLU A  17      10.301  43.186  14.850  1.00 23.48           O  
ANISOU  217  OE1 GLU A  17     2690   3321   2912  -1267   1100  -1529       O  
ATOM    218  OE2 GLU A  17       8.115  43.179  15.199  1.00 38.66           O  
ANISOU  218  OE2 GLU A  17     4633   5120   4935  -1177   1156  -1532       O  
ATOM    219  H   GLU A  17       9.691  38.881  12.742  1.00 22.11           H  
ATOM    220  HA  GLU A  17      10.663  41.408  12.959  1.00 22.08           H  
ATOM    221  HB2 GLU A  17      10.519  39.556  15.095  1.00 23.08           H  
ATOM    222  HB3 GLU A  17      11.239  40.971  15.188  1.00 23.08           H  
ATOM    223  HG2 GLU A  17       8.485  40.747  14.698  1.00 27.02           H  
ATOM    224  HG3 GLU A  17       9.067  40.907  16.168  1.00 27.02           H  
ATOM    225  N  ALEU A  18      12.929  40.652  12.460  0.40 18.70           N  
ANISOU  225  N  ALEU A  18     2127   2953   2024  -1144    798  -1157       N  
ATOM    226  N  BLEU A  18      12.935  40.641  12.445  0.60 18.69           N  
ANISOU  226  N  BLEU A  18     2126   2952   2022  -1143    797  -1155       N  
ATOM    227  CA ALEU A  18      14.222  40.167  12.025  0.40 18.61           C  
ANISOU  227  CA ALEU A  18     2071   3046   1953  -1157    741  -1143       C  
ATOM    228  CA BLEU A  18      14.225  40.145  11.992  0.60 18.58           C  
ANISOU  228  CA BLEU A  18     2068   3043   1950  -1155    740  -1139       C  
ATOM    229  C  ALEU A  18      15.316  41.042  12.588  0.40 19.78           C  
ANISOU  229  C  ALEU A  18     2169   3253   2092  -1289    798  -1283       C  
ATOM    230  C  BLEU A  18      15.329  41.026  12.541  0.60 19.75           C  
ANISOU  230  C  BLEU A  18     2166   3248   2090  -1287    797  -1278       C  
ATOM    231  O  ALEU A  18      15.244  42.259  12.489  0.40 20.65           O  
ANISOU  231  O  ALEU A  18     2292   3230   2323  -1358    908  -1357       O  
ATOM    232  O  BLEU A  18      15.263  42.236  12.404  0.60 20.60           O  
ANISOU  232  O  BLEU A  18     2287   3221   2318  -1353    905  -1347       O  
ATOM    233  CB ALEU A  18      14.305  40.200  10.500  0.40 18.24           C  
ANISOU  233  CB ALEU A  18     2044   2928   1958  -1108    749  -1044       C  
ATOM    234  CB BLEU A  18      14.287  40.165  10.455  0.60 18.20           C  
ANISOU  234  CB BLEU A  18     2040   2924   1953  -1104    747  -1039       C  
ATOM    235  CG ALEU A  18      15.643  39.742   9.921  0.40 18.36           C  
ANISOU  235  CG ALEU A  18     1994   3058   1922  -1127    712  -1060       C  
ATOM    236  CG BLEU A  18      15.672  39.985   9.820  0.60 18.48           C  
ANISOU  236  CG BLEU A  18     2015   3059   1949  -1141    729  -1059       C  
ATOM    237  CD1ALEU A  18      15.381  39.130   8.572  0.40 17.93           C  
ANISOU  237  CD1ALEU A  18     1931   3023   1858  -1058    688   -983       C  
ATOM    238  CD1BLEU A  18      16.228  38.592  10.049  0.60 18.11           C  
ANISOU  238  CD1BLEU A  18     1899   3134   1847  -1085    629  -1070       C  
ATOM    239  CD2ALEU A  18      16.666  40.884   9.791  0.40 19.38           C  
ANISOU  239  CD2ALEU A  18     2099   3180   2083  -1242    789  -1119       C  
ATOM    240  CD2BLEU A  18      15.630  40.302   8.321  0.60 18.63           C  
ANISOU  240  CD2BLEU A  18     2034   3059   1987  -1133    763   -965       C  
ATOM    241  H  ALEU A  18      12.847  41.507  12.417  0.40 22.44           H  
ATOM    242  H  BLEU A  18      12.861  41.497  12.402  0.60 22.42           H  
ATOM    243  HA ALEU A  18      14.355  39.256  12.331  0.40 22.33           H  
ATOM    244  HA BLEU A  18      14.360  39.236  12.303  0.60 22.30           H  
ATOM    245  HB2ALEU A  18      13.617  39.619  10.140  0.40 21.89           H  
ATOM    246  HB2BLEU A  18      13.722  39.451  10.120  0.60 21.84           H  
ATOM    247  HB3ALEU A  18      14.153  41.110  10.201  0.40 21.89           H  
ATOM    248  HB3BLEU A  18      13.940  41.018  10.149  0.60 21.84           H  
ATOM    249  HG ALEU A  18      16.023  39.059  10.495  0.40 22.03           H  
ATOM    250  HG BLEU A  18      16.283  40.614  10.233  0.60 22.18           H  
ATOM    251 HD11ALEU A  18      16.222  38.834   8.191  0.40 21.52           H  
ATOM    252 HD11BLEU A  18      17.101  38.529   9.630  0.60 21.73           H  
ATOM    253 HD12ALEU A  18      14.782  38.375   8.680  0.40 21.52           H  
ATOM    254 HD12BLEU A  18      16.307  38.437  11.003  0.60 21.73           H  
ATOM    255 HD13ALEU A  18      14.973  39.797   7.998  0.40 21.52           H  
ATOM    256 HD13BLEU A  18      15.625  37.943   9.656  0.60 21.73           H  
ATOM    257 HD21ALEU A  18      17.489  40.529   9.420  0.40 23.25           H  
ATOM    258 HD21BLEU A  18      16.516  40.180   7.948  0.60 22.36           H  
ATOM    259 HD22ALEU A  18      16.305  41.566   9.204  0.40 23.25           H  
ATOM    260 HD22BLEU A  18      15.002  39.701   7.889  0.60 22.36           H  
ATOM    261 HD23ALEU A  18      16.834  41.258  10.670  0.40 23.25           H  
ATOM    262 HD23BLEU A  18      15.344  41.221   8.202  0.60 22.36           H  
ATOM    263  N   ASP A  19      16.329  40.408  13.170  1.00 20.05           N  
ANISOU  263  N   ASP A  19     2122   3475   2020  -1314    725  -1292       N  
ATOM    264  CA  ASP A  19      17.578  41.091  13.554  1.00 21.22           C  
ANISOU  264  CA  ASP A  19     2203   3710   2148  -1398    770  -1372       C  
ATOM    265  C   ASP A  19      18.665  40.532  12.666  1.00 22.77           C  
ANISOU  265  C   ASP A  19     2368   3957   2327  -1375    714  -1328       C  
ATOM    266  O   ASP A  19      18.895  39.309  12.651  1.00 20.44           O  
ANISOU  266  O   ASP A  19     2017   3759   1992  -1316    608  -1261       O  
ATOM    267  CB  ASP A  19      17.976  40.790  15.003  1.00 22.21           C  
ANISOU  267  CB  ASP A  19     2228   4069   2144  -1450    729  -1396       C  
ATOM    268  CG  ASP A  19      17.168  41.573  16.016  1.00 35.56           C  
ANISOU  268  CG  ASP A  19     3896   5766   3849  -1514    812  -1494       C  
ATOM    269  OD1 ASP A  19      16.575  42.613  15.638  1.00 23.46           O  
ANISOU  269  OD1 ASP A  19     2422   4028   2464  -1523    927  -1578       O  
ATOM    270  OD2 ASP A  19      17.155  41.154  17.202  1.00 36.38           O  
ANISOU  270  OD2 ASP A  19     3904   6100   3817  -1565    767  -1490       O  
ATOM    271  H  AASP A  19      16.323  39.569  13.359  0.40 24.06           H  
ATOM    272  H  BASP A  19      16.311  39.577  13.392  0.60 24.06           H  
ATOM    273  HA  ASP A  19      17.504  42.049  13.423  1.00 25.46           H  
ATOM    274  HB2 ASP A  19      17.839  39.845  15.177  1.00 26.66           H  
ATOM    275  HB3 ASP A  19      18.911  41.017  15.126  1.00 26.66           H  
ATOM    276  N   GLY A  20      19.329  41.417  11.925  1.00 25.73           N  
ANISOU  276  N   GLY A  20     2760   4260   2757  -1424    787  -1370       N  
ATOM    277  CA  GLY A  20      20.388  41.017  11.017  1.00 23.03           C  
ANISOU  277  CA  GLY A  20     2372   3981   2398  -1413    752  -1342       C  
ATOM    278  C   GLY A  20      21.732  41.678  11.300  1.00 23.54           C  
ANISOU  278  C   GLY A  20     2391   4121   2431  -1485    784  -1418       C  
ATOM    279  O   GLY A  20      21.810  42.748  11.938  1.00 23.72           O  
ANISOU  279  O   GLY A  20     2429   4102   2482  -1558    864  -1507       O  
ATOM    280  H   GLY A  20      19.179  42.264  11.933  1.00 30.88           H  
ATOM    281  HA2 GLY A  20      20.507  40.056  11.073  1.00 27.64           H  
ATOM    282  HA3 GLY A  20      20.128  41.238  10.109  1.00 27.64           H  
ATOM    283  N   ASP A  21      22.780  41.008  10.820  1.00 22.63           N  
ANISOU  283  N   ASP A  21     2204   4117   2278  -1460    730  -1402       N  
ATOM    284  CA  ASP A  21      24.172  41.428  10.912  1.00 23.74           C  
ANISOU  284  CA  ASP A  21     2287   4350   2383  -1518    744  -1462       C  
ATOM    285  C   ASP A  21      24.884  40.835   9.680  1.00 23.60           C  
ANISOU  285  C   ASP A  21     2218   4373   2374  -1479    717  -1435       C  
ATOM    286  O   ASP A  21      25.142  39.633   9.632  1.00 23.34           O  
ANISOU  286  O   ASP A  21     2102   4419   2347  -1396    643  -1415       O  
ATOM    287  CB  ASP A  21      24.816  40.878  12.192  1.00 24.43           C  
ANISOU  287  CB  ASP A  21     2280   4621   2381  -1521    676  -1474       C  
ATOM    288  CG  ASP A  21      26.275  41.282  12.348  1.00 39.60           C  
ANISOU  288  CG  ASP A  21     4130   6660   4255  -1586    687  -1537       C  
ATOM    289  OD1 ASP A  21      26.914  41.624  11.335  1.00 35.23           O  
ANISOU  289  OD1 ASP A  21     3583   6060   3742  -1602    723  -1557       O  
ATOM    290  OD2 ASP A  21      26.793  41.252  13.496  1.00 38.18           O  
ANISOU  290  OD2 ASP A  21     3876   6650   3982  -1630    656  -1561       O  
ATOM    291  H   ASP A  21      22.696  40.256  10.410  1.00 27.16           H  
ATOM    292  HA  ASP A  21      24.242  42.395  10.898  1.00 28.49           H  
ATOM    293  HB2 ASP A  21      24.329  41.215  12.960  1.00 29.32           H  
ATOM    294  HB3 ASP A  21      24.775  39.909  12.174  1.00 29.32           H  
ATOM    295  N   VAL A  22      25.170  41.670   8.687  1.00 24.07           N  
ANISOU  295  N   VAL A  22     2309   4378   2459  -1538    779  -1429       N  
ATOM    296  CA  VAL A  22      25.845  41.220   7.455  1.00 24.30           C  
ANISOU  296  CA  VAL A  22     2279   4490   2465  -1519    767  -1417       C  
ATOM    297  C   VAL A  22      27.187  41.932   7.335  1.00 25.57           C  
ANISOU  297  C   VAL A  22     2397   4714   2605  -1602    799  -1461       C  
ATOM    298  O   VAL A  22      27.246  43.156   7.313  1.00 26.35           O  
ANISOU  298  O   VAL A  22     2538   4723   2751  -1694    865  -1439       O  
ATOM    299  CB  VAL A  22      24.972  41.484   6.207  1.00 24.09           C  
ANISOU  299  CB  VAL A  22     2295   4410   2448  -1520    799  -1317       C  
ATOM    300  CG1 VAL A  22      25.709  41.086   4.917  1.00 24.79           C  
ANISOU  300  CG1 VAL A  22     2306   4643   2470  -1520    791  -1326       C  
ATOM    301  CG2 VAL A  22      23.638  40.702   6.308  1.00 22.89           C  
ANISOU  301  CG2 VAL A  22     2177   4207   2312  -1434    767  -1285       C  
ATOM    302  H   VAL A  22      24.985  42.510   8.695  1.00 28.88           H  
ATOM    303  HA  VAL A  22      26.011  40.267   7.512  1.00 29.16           H  
ATOM    304  HB  VAL A  22      24.765  42.430   6.157  1.00 28.91           H  
ATOM    305 HG11 VAL A  22      25.133  41.264   4.157  1.00 29.75           H  
ATOM    306 HG12 VAL A  22      26.524  41.608   4.845  1.00 29.75           H  
ATOM    307 HG13 VAL A  22      25.924  40.141   4.955  1.00 29.75           H  
ATOM    308 HG21 VAL A  22      23.107  40.881   5.516  1.00 27.46           H  
ATOM    309 HG22 VAL A  22      23.832  39.754   6.369  1.00 27.46           H  
ATOM    310 HG23 VAL A  22      23.161  40.994   7.100  1.00 27.46           H  
ATOM    311  N   ASN A  23      28.262  41.154   7.282  1.00 26.93           N  
ANISOU  311  N   ASN A  23     2468   5022   2741  -1566    758  -1520       N  
ATOM    312  CA  ASN A  23      29.615  41.710   7.332  1.00 27.26           C  
ANISOU  312  CA  ASN A  23     2455   5145   2756  -1641    780  -1572       C  
ATOM    313  C   ASN A  23      29.732  42.771   8.448  1.00 27.89           C  
ANISOU  313  C   ASN A  23     2577   5176   2844  -1730    819  -1607       C  
ATOM    314  O   ASN A  23      30.338  43.849   8.274  1.00 29.03           O  
ANISOU  314  O   ASN A  23     2728   5288   3014  -1832    881  -1630       O  
ATOM    315  CB  ASN A  23      30.008  42.268   5.970  1.00 28.02           C  
ANISOU  315  CB  ASN A  23     2546   5266   2836  -1704    827  -1538       C  
ATOM    316  CG  ASN A  23      30.533  41.189   5.033  1.00 28.25           C  
ANISOU  316  CG  ASN A  23     2479   5432   2824  -1639    797  -1592       C  
ATOM    317  OD1 ASN A  23      30.050  40.054   5.031  1.00 27.55           O  
ANISOU  317  OD1 ASN A  23     2357   5347   2764  -1533    755  -1628       O  
ATOM    318  ND2 ASN A  23      31.529  41.538   4.239  1.00 29.50           N  
ANISOU  318  ND2 ASN A  23     2579   5695   2934  -1704    825  -1612       N  
ATOM    319  H   ASN A  23      28.238  40.297   7.216  1.00 32.31           H  
ATOM    320  HA  ASN A  23      30.235  40.994   7.544  1.00 32.71           H  
ATOM    321  HB2 ASN A  23      29.229  42.674   5.557  1.00 33.63           H  
ATOM    322  HB3 ASN A  23      30.706  42.931   6.087  1.00 33.63           H  
ATOM    323 HD21 ASN A  23      31.844  42.338   4.270  1.00 35.40           H  
ATOM    324 HD22 ASN A  23      31.862  40.966   3.690  1.00 35.40           H  
ATOM    325  N   GLY A  24      29.097  42.483   9.582  1.00 27.51           N  
ANISOU  325  N   GLY A  24     2545   5123   2782  -1697    789  -1616       N  
ATOM    326  CA  GLY A  24      29.210  43.362  10.738  1.00 32.99           C  
ANISOU  326  CA  GLY A  24     3252   5824   3459  -1780    833  -1694       C  
ATOM    327  C   GLY A  24      28.265  44.546  10.706  1.00 30.46           C  
ANISOU  327  C   GLY A  24     3028   5300   3244  -1840    928  -1717       C  
ATOM    328  O   GLY A  24      28.157  45.283  11.696  1.00 30.72           O  
ANISOU  328  O   GLY A  24     3062   5320   3291  -1903    987  -1822       O  
ATOM    329  H   GLY A  24      28.601  41.792   9.705  1.00 33.01           H  
ATOM    330  HA2 GLY A  24      29.028  42.852  11.543  1.00 39.59           H  
ATOM    331  HA3 GLY A  24      30.117  43.701  10.793  1.00 39.59           H  
ATOM    332  N   HIS A  25      27.570  44.735   9.590  1.00 29.38           N  
ANISOU  332  N   HIS A  25     3216   4428   3520  -2027    483  -1240       N  
ATOM    333  CA  HIS A  25      26.552  45.773   9.495  1.00 28.77           C  
ANISOU  333  CA  HIS A  25     3351   4260   3320  -2066    583  -1214       C  
ATOM    334  C   HIS A  25      25.234  45.263  10.100  1.00 27.15           C  
ANISOU  334  C   HIS A  25     3211   4013   3094  -1960    520  -1143       C  
ATOM    335  O   HIS A  25      24.585  44.388   9.549  1.00 25.88           O  
ANISOU  335  O   HIS A  25     3017   3849   2967  -1855    506  -1105       O  
ATOM    336  CB  HIS A  25      26.302  46.188   8.047  1.00 28.61           C  
ANISOU  336  CB  HIS A  25     3417   4196   3257  -2092    722  -1224       C  
ATOM    337  CG  HIS A  25      27.519  46.678   7.336  1.00 30.28           C  
ANISOU  337  CG  HIS A  25     3582   4451   3474  -2207    806  -1301       C  
ATOM    338  ND1 HIS A  25      28.076  47.913   7.587  1.00 35.79           N  
ANISOU  338  ND1 HIS A  25     4364   5122   4113  -2346    867  -1340       N  
ATOM    339  CD2 HIS A  25      28.274  46.110   6.363  1.00 30.87           C  
ANISOU  339  CD2 HIS A  25     3537   4591   3603  -2211    850  -1356       C  
ATOM    340  CE1 HIS A  25      29.132  48.082   6.810  1.00 42.62           C  
ANISOU  340  CE1 HIS A  25     5162   6040   4993  -2435    941  -1412       C  
ATOM    341  NE2 HIS A  25      29.275  47.003   6.059  1.00 34.90           N  
ANISOU  341  NE2 HIS A  25     4058   5119   4083  -2356    937  -1428       N  
ATOM    342  H   HIS A  25      27.669  44.273   8.871  1.00 35.26           H  
ATOM    343  HA  HIS A  25      26.839  46.554   9.994  1.00 34.52           H  
ATOM    344  HB2 HIS A  25      25.962  45.422   7.558  1.00 34.33           H  
ATOM    345  HB3 HIS A  25      25.645  46.902   8.036  1.00 34.33           H  
ATOM    346  HD1 HIS A  25      27.786  48.482   8.164  1.00 42.95           H  
ATOM    347  HD2 HIS A  25      28.146  45.272   5.981  1.00 37.05           H  
ATOM    348  HE1 HIS A  25      29.681  48.833   6.794  1.00 51.15           H  
ATOM    349  HE2 HIS A  25      29.893  46.881   5.473  1.00 41.88           H  
ATOM    350  N   LYS A  26      24.849  45.846  11.230  1.00 27.39           N  
ANISOU  350  N   LYS A  26     3336   4012   3061  -1999    493  -1134       N  
ATOM    351  CA  LYS A  26      23.652  45.441  11.956  1.00 26.21           C  
ANISOU  351  CA  LYS A  26     3251   3829   2880  -1921    445  -1082       C  
ATOM    352  C   LYS A  26      22.402  46.213  11.514  1.00 25.48           C  
ANISOU  352  C   LYS A  26     3334   3618   2730  -1909    559  -1063       C  
ATOM    353  O   LYS A  26      22.479  47.365  11.091  1.00 27.28           O  
ANISOU  353  O   LYS A  26     3673   3771   2920  -1988    662  -1088       O  
ATOM    354  CB  LYS A  26      23.922  45.629  13.453  1.00 27.17           C  
ANISOU  354  CB  LYS A  26     3384   3983   2956  -1982    361  -1093       C  
ATOM    355  CG  LYS A  26      24.968  44.640  13.962  1.00 28.27           C  
ANISOU  355  CG  LYS A  26     3346   4221   3176  -1969    202  -1086       C  
ATOM    356  CD  LYS A  26      25.160  44.707  15.475  1.00 36.46           C  
ANISOU  356  CD  LYS A  26     4405   5295   4153  -2034     94  -1083       C  
ATOM    357  CE  LYS A  26      26.159  43.651  15.960  1.00 42.25           C  
ANISOU  357  CE  LYS A  26     4960   6105   4989  -2010    -96  -1059       C  
ATOM    358  NZ  LYS A  26      25.634  42.256  15.819  1.00 46.52           N  
ANISOU  358  NZ  LYS A  26     5422   6647   5607  -1873   -194   -989       N  
ATOM    359  H   LYS A  26      25.275  46.493  11.604  1.00 32.87           H  
ATOM    360  HA  LYS A  26      23.492  44.498  11.797  1.00 31.46           H  
ATOM    361  HB2 LYS A  26      24.252  46.528  13.609  1.00 32.61           H  
ATOM    362  HB3 LYS A  26      23.100  45.483  13.947  1.00 32.61           H  
ATOM    363  HG2 LYS A  26      24.688  43.740  13.735  1.00 33.93           H  
ATOM    364  HG3 LYS A  26      25.820  44.839  13.543  1.00 33.93           H  
ATOM    365  HD2 LYS A  26      25.502  45.582  15.716  1.00 43.75           H  
ATOM    366  HD3 LYS A  26      24.310  44.545  15.913  1.00 43.75           H  
ATOM    367  HE2 LYS A  26      26.973  43.721  15.437  1.00 50.70           H  
ATOM    368  HE3 LYS A  26      26.352  43.806  16.898  1.00 50.70           H  
ATOM    369  HZ1 LYS A  26      25.454  42.084  14.965  1.00 55.83           H  
ATOM    370  HZ2 LYS A  26      26.240  41.673  16.110  1.00 55.83           H  
ATOM    371  HZ3 LYS A  26      24.889  42.162  16.296  1.00 55.83           H  
ATOM    372  N   PHE A  27      21.248  45.574  11.604  1.00 24.15           N  
ANISOU  372  N   PHE A  27     3187   3420   2567  -1808    535  -1017       N  
ATOM    373  CA  PHE A  27      19.993  46.208  11.226  1.00 23.58           C  
ANISOU  373  CA  PHE A  27     3265   3225   2472  -1780    623   -998       C  
ATOM    374  C   PHE A  27      18.834  45.410  11.779  1.00 22.42           C  
ANISOU  374  C   PHE A  27     3116   3071   2331  -1682    575   -963       C  
ATOM    375  O   PHE A  27      19.016  44.282  12.215  1.00 21.91           O  
ANISOU  375  O   PHE A  27     2939   3100   2287  -1632    474   -941       O  
ATOM    376  CB  PHE A  27      19.845  46.285   9.709  1.00 23.20           C  
ANISOU  376  CB  PHE A  27     3239   3128   2446  -1760    686   -975       C  
ATOM    377  CG  PHE A  27      19.807  44.949   9.013  1.00 22.07           C  
ANISOU  377  CG  PHE A  27     2967   3062   2356  -1669    630   -946       C  
ATOM    378  CD1 PHE A  27      20.973  44.331   8.612  1.00 22.80           C  
ANISOU  378  CD1 PHE A  27     2917   3257   2489  -1681    600   -973       C  
ATOM    379  CD2 PHE A  27      18.598  44.343   8.710  1.00 21.48           C  
ANISOU  379  CD2 PHE A  27     2913   2948   2302  -1572    616   -901       C  
ATOM    380  CE1 PHE A  27      20.946  43.118   7.937  1.00 23.27           C  
ANISOU  380  CE1 PHE A  27     2860   3374   2610  -1593    560   -958       C  
ATOM    381  CE2 PHE A  27      18.560  43.124   8.028  1.00 24.37           C  
ANISOU  381  CE2 PHE A  27     3163   3381   2717  -1492    571   -880       C  
ATOM    382  CZ  PHE A  27      19.743  42.520   7.641  1.00 20.65           C  
ANISOU  382  CZ  PHE A  27     2555   3006   2286  -1501    546   -910       C  
ATOM    383  H   PHE A  27      21.161  44.765  11.884  1.00 28.98           H  
ATOM    384  HA  PHE A  27      19.956  47.106  11.589  1.00 28.30           H  
ATOM    385  HB2 PHE A  27      19.018  46.747   9.502  1.00 27.84           H  
ATOM    386  HB3 PHE A  27      20.596  46.782   9.349  1.00 27.84           H  
ATOM    387  HD1 PHE A  27      21.790  44.732   8.799  1.00 27.36           H  
ATOM    388  HD2 PHE A  27      17.803  44.754   8.961  1.00 25.78           H  
ATOM    389  HE1 PHE A  27      21.743  42.711   7.681  1.00 27.93           H  
ATOM    390  HE2 PHE A  27      17.744  42.721   7.837  1.00 29.25           H  
ATOM    391  HZ  PHE A  27      19.725  41.702   7.199  1.00 24.79           H  
ATOM    392  N  ASER A  28      17.643  45.990  11.730  0.82 22.17           N  
ANISOU  392  N  ASER A  28     3210   2919   2293  -1651    645   -958       N  
ATOM    393  N  BSER A  28      17.648  46.013  11.769  0.18 22.20           N  
ANISOU  393  N  BSER A  28     3216   2923   2296  -1654    645   -960       N  
ATOM    394  CA ASER A  28      16.441  45.310  12.186  0.82 21.21           C  
ANISOU  394  CA ASER A  28     3092   2783   2182  -1562    620   -938       C  
ATOM    395  CA BSER A  28      16.428  45.347  12.211  0.18 21.24           C  
ANISOU  395  CA BSER A  28     3101   2784   2185  -1564    622   -939       C  
ATOM    396  C  ASER A  28      15.275  45.664  11.284  0.82 20.70           C  
ANISOU  396  C  ASER A  28     3117   2583   2165  -1493    685   -918       C  
ATOM    397  C  BSER A  28      15.284  45.664  11.257  0.18 20.69           C  
ANISOU  397  C  BSER A  28     3116   2582   2165  -1493    685   -918       C  
ATOM    398  O  ASER A  28      15.159  46.804  10.825  0.82 21.51           O  
ANISOU  398  O  ASER A  28     3334   2560   2278  -1526    760   -928       O  
ATOM    399  O  BSER A  28      15.191  46.774  10.732  0.18 21.47           O  
ANISOU  399  O  BSER A  28     3326   2557   2274  -1525    758   -925       O  
ATOM    400  CB ASER A  28      16.121  45.683  13.649  0.82 21.97           C  
ANISOU  400  CB ASER A  28     3249   2877   2222  -1606    632   -977       C  
ATOM    401  CB BSER A  28      16.045  45.782  13.633  0.18 22.01           C  
ANISOU  401  CB BSER A  28     3266   2869   2228  -1606    642   -980       C  
ATOM    402  OG ASER A  28      15.198  44.766  14.202  0.82 21.17           O  
ANISOU  402  OG ASER A  28     3122   2806   2116  -1537    593   -958       O  
ATOM    403  OG BSER A  28      17.085  45.514  14.557  0.18 22.75           O  
ANISOU  403  OG BSER A  28     3297   3079   2267  -1683    567   -990       O  
ATOM    404  H  ASER A  28      17.503  46.785  11.433  0.82 26.60           H  
ATOM    405  H  BSER A  28      17.524  46.822  11.506  0.18 26.64           H  
ATOM    406  HA ASER A  28      16.580  44.351  12.140  0.82 25.45           H  
ATOM    407  HA BSER A  28      16.567  44.387  12.213  0.18 25.49           H  
ATOM    408  HB2ASER A  28      16.940  45.661  14.168  0.82 26.37           H  
ATOM    409  HB2BSER A  28      15.865  46.735  13.631  0.18 26.41           H  
ATOM    410  HB3ASER A  28      15.736  46.573  13.672  0.82 26.37           H  
ATOM    411  HB3BSER A  28      15.251  45.297  13.906  0.18 26.41           H  
ATOM    412  HG ASER A  28      15.028  44.974  14.998  0.82 25.41           H  
ATOM    413  HG BSER A  28      17.251  44.691  14.572  0.18 27.30           H  
ATOM    414  N   VAL A  29      14.426  44.674  11.042  1.00 19.52           N  
ANISOU  414  N   VAL A  29     2918   2450   2050  -1396    645   -887       N  
ATOM    415  CA  VAL A  29      13.241  44.814  10.196  1.00 19.05           C  
ANISOU  415  CA  VAL A  29     2928   2265   2046  -1317    682   -865       C  
ATOM    416  C   VAL A  29      11.997  44.299  10.926  1.00 23.06           C  
ANISOU  416  C   VAL A  29     3433   2755   2575  -1231    680   -882       C  
ATOM    417  O   VAL A  29      12.042  43.252  11.567  1.00 18.14           O  
ANISOU  417  O   VAL A  29     2718   2251   1923  -1217    616   -875       O  
ATOM    418  CB  VAL A  29      13.373  43.977   8.900  1.00 18.16           C  
ANISOU  418  CB  VAL A  29     2743   2199   1959  -1282    640   -815       C  
ATOM    419  CG1 VAL A  29      12.055  43.993   8.093  1.00 17.75           C  
ANISOU  419  CG1 VAL A  29     2763   2019   1962  -1197    655   -785       C  
ATOM    420  CG2 VAL A  29      14.504  44.488   8.082  1.00 18.84           C  
ANISOU  420  CG2 VAL A  29     2836   2303   2020  -1369    665   -807       C  
ATOM    421  H  AVAL A  29      14.516  43.883  11.367  0.82 23.43           H  
ATOM    422  H  BVAL A  29      14.509  43.889  11.384  0.18 23.43           H  
ATOM    423  HA  VAL A  29      13.108  45.745   9.960  1.00 22.87           H  
ATOM    424  HB  VAL A  29      13.567  43.057   9.137  1.00 21.80           H  
ATOM    425 HG11 VAL A  29      12.170  43.461   7.290  1.00 21.30           H  
ATOM    426 HG12 VAL A  29      11.346  43.618   8.640  1.00 21.30           H  
ATOM    427 HG13 VAL A  29      11.841  44.909   7.856  1.00 21.30           H  
ATOM    428 HG21 VAL A  29      14.575  43.955   7.274  1.00 22.61           H  
ATOM    429 HG22 VAL A  29      14.335  45.415   7.853  1.00 22.61           H  
ATOM    430 HG23 VAL A  29      15.323  44.417   8.598  1.00 22.61           H  
ATOM    431  N   SER A  30      10.906  45.048  10.828  1.00 18.99           N  
ANISOU  431  N   SER A  30     3018   2082   2116  -1171    749   -903       N  
ATOM    432  CA ASER A  30       9.620  44.614  11.366  0.69 18.82           C  
ANISOU  432  CA ASER A  30     2985   2033   2134  -1074    769   -930       C  
ATOM    433  CA CSER A  30       9.611  44.640  11.370  0.31 20.13           C  
ANISOU  433  CA CSER A  30     3153   2195   2301  -1074    771   -931       C  
ATOM    434  C   SER A  30       8.600  44.614  10.238  1.00 19.01           C  
ANISOU  434  C   SER A  30     3014   1950   2259   -931    762   -863       C  
ATOM    435  O   SER A  30       8.584  45.514   9.405  1.00 19.04           O  
ANISOU  435  O   SER A  30     3103   1822   2311   -919    779   -826       O  
ATOM    436  CB ASER A  30       9.166  45.537  12.505  0.69 24.53           C  
ANISOU  436  CB ASER A  30     3774   2685   2861  -1090    859  -1001       C  
ATOM    437  CB CSER A  30       9.152  45.623  12.453  0.31 23.90           C  
ANISOU  437  CB CSER A  30     3702   2593   2787  -1088    863  -1001       C  
ATOM    438  OG ASER A  30      10.018  45.441  13.642  0.69 20.36           O  
ANISOU  438  OG ASER A  30     3225   2283   2229  -1205    844  -1024       O  
ATOM    439  OG CSER A  30       7.795  45.410  12.817  0.31 24.57           O  
ANISOU  439  OG CSER A  30     3772   2626   2938   -983    911  -1037       O  
ATOM    440  H  ASER A  30      10.883  45.821  10.450  0.69 22.79           H  
ATOM    441  H  CSER A  30      10.888  45.817  10.442  0.31 22.79           H  
ATOM    442  HA ASER A  30       9.700  43.711  11.711  0.69 22.59           H  
ATOM    443  HA CSER A  30       9.677  43.753  11.755  0.31 24.16           H  
ATOM    444  HB2ASER A  30       9.173  46.453  12.186  0.69 29.43           H  
ATOM    445  HB2CSER A  30       9.708  45.505  13.239  0.31 28.68           H  
ATOM    446  HB3ASER A  30       8.266  45.289  12.768  0.69 29.43           H  
ATOM    447  HB3CSER A  30       9.247  46.527  12.116  0.31 28.68           H  
ATOM    448  HG ASER A  30      10.802  45.657  13.432  0.69 24.44           H  
ATOM    449  HG CSER A  30       7.298  45.511  12.147  0.31 29.49           H  
ATOM    450  N   GLY A  31       7.774  43.575  10.194  1.00 19.43           N  
ANISOU  450  N   GLY A  31     2969   2072   2340   -818    720   -822       N  
ATOM    451  CA  GLY A  31       6.732  43.476   9.193  1.00 19.05           C  
ANISOU  451  CA  GLY A  31     2898   1952   2388   -669    690   -743       C  
ATOM    452  C   GLY A  31       5.403  43.080   9.806  1.00 23.36           C  
ANISOU  452  C   GLY A  31     3383   2489   3005   -559    719   -773       C  
ATOM    453  O   GLY A  31       5.351  42.440  10.864  1.00 18.06           O  
ANISOU  453  O   GLY A  31     2668   1917   2278   -601    743   -830       O  
ATOM    454  H   GLY A  31       7.800  42.911  10.740  1.00 23.31           H  
ATOM    455  HA2 GLY A  31       6.625  44.331   8.748  1.00 22.86           H  
ATOM    456  HA3 GLY A  31       6.978  42.810   8.532  1.00 22.86           H  
ATOM    457  N   GLU A  32       4.323  43.467   9.143  1.00 17.75           N  
ANISOU  457  N   GLU A  32     2668   1659   2416   -426    712   -732       N  
ATOM    458  CA  GLU A  32       2.999  43.054   9.565  1.00 17.87           C  
ANISOU  458  CA  GLU A  32     2597   1670   2524   -313    740   -762       C  
ATOM    459  C   GLU A  32       2.113  42.970   8.350  1.00 17.92           C  
ANISOU  459  C   GLU A  32     2557   1613   2641   -171    655   -661       C  
ATOM    460  O   GLU A  32       2.390  43.583   7.317  1.00 18.33           O  
ANISOU  460  O   GLU A  32     2680   1576   2708   -160    595   -579       O  
ATOM    461  CB  GLU A  32       2.412  44.031  10.571  1.00 20.01           C  
ANISOU  461  CB  GLU A  32     2912   1819   2873   -309    868   -889       C  
ATOM    462  CG  GLU A  32       2.464  45.446  10.100  1.00 26.36           C  
ANISOU  462  CG  GLU A  32     3823   2421   3774   -285    889   -888       C  
ATOM    463  CD  GLU A  32       1.826  46.418  11.092  1.00 39.06           C  
ANISOU  463  CD  GLU A  32     5464   3887   5489   -271   1031  -1037       C  
ATOM    464  OE1 GLU A  32       1.684  47.602  10.735  1.00 40.06           O  
ANISOU  464  OE1 GLU A  32     5671   3812   5737   -227   1050  -1042       O  
ATOM    465  OE2 GLU A  32       1.457  46.005  12.210  1.00 35.93           O  
ANISOU  465  OE2 GLU A  32     5017   3579   5056   -310   1122  -1145       O  
ATOM    466  H   GLU A  32       4.331  43.968   8.444  1.00 21.30           H  
ATOM    467  HA  GLU A  32       3.047  42.177   9.976  1.00 21.45           H  
ATOM    468  HB2 GLU A  32       1.483  43.802  10.729  1.00 24.02           H  
ATOM    469  HB3 GLU A  32       2.914  43.972  11.399  1.00 24.02           H  
ATOM    470  HG2 GLU A  32       3.391  45.706   9.979  1.00 31.64           H  
ATOM    471  HG3 GLU A  32       1.986  45.518   9.259  1.00 31.64           H  
ATOM    472  N   GLY A  33       1.087  42.151   8.472  1.00 17.60           N  
ANISOU  472  N   GLY A  33     2399   1629   2661    -80    643   -663       N  
ATOM    473  CA  GLY A  33       0.112  41.967   7.410  1.00 17.79           C  
ANISOU  473  CA  GLY A  33     2356   1609   2795     55    550   -574       C  
ATOM    474  C   GLY A  33      -0.762  40.764   7.681  1.00 19.09           C  
ANISOU  474  C   GLY A  33     2379   1889   2985    108    542   -588       C  
ATOM    475  O   GLY A  33      -1.070  40.461   8.840  1.00 17.22           O  
ANISOU  475  O   GLY A  33     2100   1701   2742     76    640   -687       O  
ATOM    476  H   GLY A  33       0.927  41.681   9.174  1.00 21.13           H  
ATOM    477  HA2 GLY A  33      -0.451  42.753   7.341  1.00 21.35           H  
ATOM    478  HA3 GLY A  33       0.570  41.836   6.564  1.00 21.35           H  
ATOM    479  N   GLU A  34      -1.151  40.059   6.614  1.00 16.63           N  
ANISOU  479  N   GLU A  34     2005   1626   2689    171    427   -492       N  
ATOM    480  CA  GLU A  34      -2.030  38.912   6.757  1.00 16.14           C  
ANISOU  480  CA  GLU A  34     1809   1664   2662    219    412   -501       C  
ATOM    481  C   GLU A  34      -1.791  37.859   5.697  1.00 15.10           C  
ANISOU  481  C   GLU A  34     1643   1636   2458    211    294   -408       C  
ATOM    482  O   GLU A  34      -1.292  38.156   4.586  1.00 15.12           O  
ANISOU  482  O   GLU A  34     1715   1613   2416    201    211   -326       O  
ATOM    483  CB  GLU A  34      -3.498  39.351   6.736  1.00 24.16           C  
ANISOU  483  CB  GLU A  34     2726   2583   3871    354    419   -528       C  
ATOM    484  CG  GLU A  34      -3.921  40.077   5.498  1.00 32.09           C  
ANISOU  484  CG  GLU A  34     3749   3467   4977    455    295   -427       C  
ATOM    485  CD  GLU A  34      -5.255  40.795   5.668  1.00 35.26           C  
ANISOU  485  CD  GLU A  34     4052   3734   5611    597    309   -471       C  
ATOM    486  OE1 GLU A  34      -5.471  41.443   6.715  1.00 38.72           O  
ANISOU  486  OE1 GLU A  34     4484   4096   6132    602    450   -595       O  
ATOM    487  OE2 GLU A  34      -6.091  40.708   4.745  1.00 36.42           O  
ANISOU  487  OE2 GLU A  34     4121   3851   5864    700    178   -389       O  
ATOM    488  H   GLU A  34      -0.918  40.229   5.804  1.00 19.96           H  
ATOM    489  HA  GLU A  34      -1.860  38.501   7.619  1.00 19.37           H  
ATOM    490  HB2 GLU A  34      -4.057  38.562   6.818  1.00 28.99           H  
ATOM    491  HB3 GLU A  34      -3.655  39.941   7.490  1.00 28.99           H  
ATOM    492  HG2 GLU A  34      -3.250  40.741   5.275  1.00 38.51           H  
ATOM    493  HG3 GLU A  34      -4.013  39.440   4.772  1.00 38.51           H  
ATOM    494  N   GLY A  35      -2.142  36.627   6.055  1.00 14.87           N  
ANISOU  494  N   GLY A  35     1517   1720   2411    201    297   -429       N  
ATOM    495  CA  GLY A  35      -2.055  35.502   5.140  1.00 17.37           C  
ANISOU  495  CA  GLY A  35     1787   2132   2679    195    200   -365       C  
ATOM    496  C   GLY A  35      -3.408  34.838   5.007  1.00 18.21           C  
ANISOU  496  C   GLY A  35     1765   2265   2888    274    170   -366       C  
ATOM    497  O   GLY A  35      -4.192  34.813   5.956  1.00 17.93           O  
ANISOU  497  O   GLY A  35     1661   2225   2928    296    252   -435       O  
ATOM    498  H   GLY A  35      -2.438  36.418   6.835  1.00 17.84           H  
ATOM    499  HA2 GLY A  35      -1.766  35.807   4.265  1.00 20.84           H  
ATOM    500  HA3 GLY A  35      -1.417  34.852   5.474  1.00 20.84           H  
ATOM    501  N   ASP A  36      -3.701  34.337   3.811  1.00 13.74           N  
ANISOU  501  N   ASP A  36     1166   1732   2323    305     57   -297       N  
ATOM    502  CA  ASP A  36      -4.967  33.678   3.527  1.00 14.50           C  
ANISOU  502  CA  ASP A  36     1133   1861   2516    371      7   -294       C  
ATOM    503  C   ASP A  36      -4.619  32.396   2.819  1.00 13.23           C  
ANISOU  503  C   ASP A  36      955   1806   2267    316    -60   -264       C  
ATOM    504  O   ASP A  36      -4.451  32.373   1.591  1.00 14.25           O  
ANISOU  504  O   ASP A  36     1121   1946   2349    312   -160   -202       O  
ATOM    505  CB  ASP A  36      -5.823  34.579   2.635  1.00 15.64           C  
ANISOU  505  CB  ASP A  36     1259   1913   2772    474    -92   -234       C  
ATOM    506  CG  ASP A  36      -7.270  34.133   2.565  1.00 24.81           C  
ANISOU  506  CG  ASP A  36     2257   3093   4078    555   -134   -250       C  
ATOM    507  OD1 ASP A  36      -7.585  33.049   3.077  1.00 26.29           O  
ANISOU  507  OD1 ASP A  36     2358   3374   4258    517    -84   -302       O  
ATOM    508  OD2 ASP A  36      -8.097  34.885   2.016  1.00 29.69           O  
ANISOU  508  OD2 ASP A  36     2829   3625   4825    655   -222   -209       O  
ATOM    509  H   ASP A  36      -3.169  34.368   3.136  1.00 16.49           H  
ATOM    510  HA  ASP A  36      -5.444  33.481   4.348  1.00 17.40           H  
ATOM    511  HB2 ASP A  36      -5.805  35.483   2.988  1.00 18.77           H  
ATOM    512  HB3 ASP A  36      -5.462  34.567   1.735  1.00 18.77           H  
ATOM    513  N   ALA A  37      -4.423  31.331   3.590  1.00 14.38           N  
ANISOU  513  N   ALA A  37     1060   2025   2380    259     -3   -309       N  
ATOM    514  CA  ALA A  37      -3.825  30.116   3.037  1.00 13.95           C  
ANISOU  514  CA  ALA A  37     1002   2049   2249    200    -50   -297       C  
ATOM    515  C   ALA A  37      -4.763  29.443   2.006  1.00 17.11           C  
ANISOU  515  C   ALA A  37     1324   2488   2691    231   -144   -272       C  
ATOM    516  O   ALA A  37      -4.342  28.632   1.174  1.00 14.97           O  
ANISOU  516  O   ALA A  37     1062   2269   2359    187   -196   -264       O  
ATOM    517  CB  ALA A  37      -3.510  29.151   4.156  1.00 14.36           C  
ANISOU  517  CB  ALA A  37     1031   2146   2280    140     14   -336       C  
ATOM    518  H   ALA A  37      -4.623  31.284   4.425  1.00 17.26           H  
ATOM    519  HA  ALA A  37      -2.995  30.343   2.589  1.00 16.74           H  
ATOM    520  HB1 ALA A  37      -3.115  28.350   3.779  1.00 17.24           H  
ATOM    521  HB2 ALA A  37      -2.887  29.572   4.768  1.00 17.24           H  
ATOM    522  HB3 ALA A  37      -4.332  28.928   4.621  1.00 17.24           H  
ATOM    523  N   THR A  38      -6.041  29.753   2.112  1.00 15.07           N  
ANISOU  523  N   THR A  38      976   2206   2544    302   -158   -275       N  
ATOM    524  CA  THR A  38      -7.035  29.240   1.154  1.00 20.20           C  
ANISOU  524  CA  THR A  38     1581   2883   3211    318   -251   -231       C  
ATOM    525  C   THR A  38      -6.670  29.653  -0.264  1.00 16.50           C  
ANISOU  525  C   THR A  38     1151   2419   2699    326   -383   -179       C  
ATOM    526  O   THR A  38      -6.946  28.930  -1.238  1.00 21.01           O  
ANISOU  526  O   THR A  38     1702   3050   3231    295   -472   -161       O  
ATOM    527  CB  THR A  38      -8.433  29.767   1.475  1.00 25.86           C  
ANISOU  527  CB  THR A  38     2226   3559   4042    389   -242   -228       C  
ATOM    528  OG1 THR A  38      -8.849  29.272   2.753  1.00 23.44           O  
ANISOU  528  OG1 THR A  38     1900   3262   3744    353   -120   -279       O  
ATOM    529  CG2 THR A  38      -9.459  29.306   0.415  1.00 26.42           C  
ANISOU  529  CG2 THR A  38     2244   3667   4126    401   -351   -180       C  
ATOM    530  H   THR A  38      -6.370  30.257   2.725  1.00 18.08           H  
ATOM    531  HA  THR A  38      -7.055  28.272   1.197  1.00 24.24           H  
ATOM    532  HB  THR A  38      -8.420  30.737   1.491  1.00 31.03           H  
ATOM    533  HG1 THR A  38      -8.314  29.527   3.348  1.00 28.13           H  
ATOM    534 HG21 THR A  38     -10.339  29.649   0.634  1.00 31.70           H  
ATOM    535 HG22 THR A  38      -9.202  29.635  -0.461  1.00 31.70           H  
ATOM    536 HG23 THR A  38      -9.496  28.337   0.388  1.00 31.70           H  
ATOM    537  N   TYR A  39      -6.064  30.829  -0.390  1.00 16.31           N  
ANISOU  537  N   TYR A  39     1234   2322   2641    339   -381   -140       N  
ATOM    538  CA  TYR A  39      -5.652  31.335  -1.694  1.00 18.99           C  
ANISOU  538  CA  TYR A  39     1680   2650   2884    309   -484    -63       C  
ATOM    539  C   TYR A  39      -4.148  31.329  -1.844  1.00 19.61           C  
ANISOU  539  C   TYR A  39     1881   2749   2820    212   -419    -78       C  
ATOM    540  O   TYR A  39      -3.619  31.739  -2.876  1.00 17.60           O  
ANISOU  540  O   TYR A  39     1734   2494   2459    155   -473    -27       O  
ATOM    541  CB  TYR A  39      -6.214  32.735  -1.898  1.00 24.43           C  
ANISOU  541  CB  TYR A  39     2401   3225   3656    394   -553     10       C  
ATOM    542  CG  TYR A  39      -7.712  32.694  -1.905  1.00 27.78           C  
ANISOU  542  CG  TYR A  39     2677   3635   4244    496   -635     19       C  
ATOM    543  CD1 TYR A  39      -8.402  32.327  -3.050  1.00 27.35           C  
ANISOU  543  CD1 TYR A  39     2588   3627   4178    494   -796     82       C  
ATOM    544  CD2 TYR A  39      -8.439  32.944  -0.753  1.00 27.94           C  
ANISOU  544  CD2 TYR A  39     2580   3608   4429    578   -546    -50       C  
ATOM    545  CE1 TYR A  39      -9.766  32.260  -3.063  1.00 34.08           C  
ANISOU  545  CE1 TYR A  39     3305   4475   5167    573   -858     87       C  
ATOM    546  CE2 TYR A  39      -9.824  32.886  -0.762  1.00 26.40           C  
ANISOU  546  CE2 TYR A  39     2265   3410   4357    645   -583    -51       C  
ATOM    547  CZ  TYR A  39     -10.476  32.530  -1.916  1.00 35.29           C  
ANISOU  547  CZ  TYR A  39     3375   4585   5451    638   -728     19       C  
ATOM    548  OH  TYR A  39     -11.853  32.467  -1.938  1.00 45.28           O  
ANISOU  548  OH  TYR A  39     4539   5857   6807    684   -747     16       O  
ATOM    549  H   TYR A  39      -5.880  31.354   0.265  1.00 19.57           H  
ATOM    550  HA  TYR A  39      -6.022  30.762  -2.384  1.00 22.78           H  
ATOM    551  HB2 TYR A  39      -5.924  33.310  -1.173  1.00 29.31           H  
ATOM    552  HB3 TYR A  39      -5.911  33.084  -2.751  1.00 29.31           H  
ATOM    553  HD1 TYR A  39      -7.928  32.142  -3.829  1.00 32.82           H  
ATOM    554  HD2 TYR A  39      -7.994  33.183   0.028  1.00 33.53           H  
ATOM    555  HE1 TYR A  39     -10.213  32.026  -3.844  1.00 40.89           H  
ATOM    556  HE2 TYR A  39     -10.306  33.067   0.012  1.00 31.68           H  
ATOM    557  HH  TYR A  39     -12.161  32.652  -1.179  1.00 54.34           H  
ATOM    558  N   GLY A  40      -3.457  30.830  -0.827  1.00 13.07           N  
ANISOU  558  N   GLY A  40     1034   1944   1989    182   -307   -148       N  
ATOM    559  CA  GLY A  40      -2.010  30.824  -0.825  1.00 12.10           C  
ANISOU  559  CA  GLY A  40      994   1838   1764     98   -244   -175       C  
ATOM    560  C   GLY A  40      -1.397  32.212  -0.826  1.00 12.58           C  
ANISOU  560  C   GLY A  40     1169   1820   1789     85   -221   -140       C  
ATOM    561  O   GLY A  40      -0.278  32.384  -1.305  1.00 13.99           O  
ANISOU  561  O   GLY A  40     1430   2016   1869      1   -195   -146       O  
ATOM    562  H   GLY A  40      -3.810  30.487  -0.121  1.00 15.69           H  
ATOM    563  HA2 GLY A  40      -1.694  30.354  -0.038  1.00 14.52           H  
ATOM    564  HA3 GLY A  40      -1.692  30.352  -1.610  1.00 14.52           H  
ATOM    565  N   LYS A  41      -2.102  33.193  -0.248  1.00 13.16           N  
ANISOU  565  N   LYS A  41     1243   1803   1955    163   -217   -117       N  
ATOM    566  CA  LYS A  41      -1.802  34.607  -0.465  1.00 14.01           C  
ANISOU  566  CA  LYS A  41     1466   1805   2051    165   -223    -66       C  
ATOM    567  C   LYS A  41      -1.278  35.299   0.777  1.00 13.76           C  
ANISOU  567  C   LYS A  41     1464   1715   2050    159   -111   -122       C  
ATOM    568  O   LYS A  41      -1.895  35.198   1.859  1.00 13.67           O  
ANISOU  568  O   LYS A  41     1374   1690   2130    213    -53   -177       O  
ATOM    569  CB  LYS A  41      -3.080  35.320  -0.960  1.00 15.41           C  
ANISOU  569  CB  LYS A  41     1626   1895   2336    268   -330      9       C  
ATOM    570  CG  LYS A  41      -2.944  36.821  -1.214  1.00 16.64           C  
ANISOU  570  CG  LYS A  41     1904   1906   2512    286   -358     78       C  
ATOM    571  CD  LYS A  41      -4.273  37.391  -1.734  1.00 18.27           C  
ANISOU  571  CD  LYS A  41     2068   2018   2856    405   -495    161       C  
ATOM    572  CE  LYS A  41      -4.211  38.893  -1.920  1.00 33.90           C  
ANISOU  572  CE  LYS A  41     4169   3823   4891    439   -534    236       C  
ATOM    573  NZ  LYS A  41      -5.545  39.527  -2.248  1.00 35.10           N  
ANISOU  573  NZ  LYS A  41     4254   3851   5230    583   -674    311       N  
ATOM    574  H   LYS A  41      -2.767  33.059   0.281  1.00 15.80           H  
ATOM    575  HA  LYS A  41      -1.127  34.684  -1.158  1.00 16.81           H  
ATOM    576  HB2 LYS A  41      -3.358  34.909  -1.793  1.00 18.50           H  
ATOM    577  HB3 LYS A  41      -3.775  35.201  -0.293  1.00 18.50           H  
ATOM    578  HG2 LYS A  41      -2.718  37.271  -0.385  1.00 19.97           H  
ATOM    579  HG3 LYS A  41      -2.259  36.976  -1.883  1.00 19.97           H  
ATOM    580  HD2 LYS A  41      -4.479  36.988  -2.592  1.00 21.93           H  
ATOM    581  HD3 LYS A  41      -4.976  37.195  -1.095  1.00 21.93           H  
ATOM    582  HE2 LYS A  41      -3.886  39.296  -1.100  1.00 40.69           H  
ATOM    583  HE3 LYS A  41      -3.602  39.092  -2.648  1.00 40.69           H  
ATOM    584  HZ1 LYS A  41      -5.447  40.407  -2.346  1.00 42.11           H  
ATOM    585  HZ2 LYS A  41      -5.866  39.186  -3.004  1.00 42.11           H  
ATOM    586  HZ3 LYS A  41      -6.125  39.372  -1.591  1.00 42.11           H  
ATOM    587  N   LEU A  42      -0.153  35.991   0.628  1.00 13.96           N  
ANISOU  587  N   LEU A  42     1603   1710   1990     79    -74   -116       N  
ATOM    588  CA  LEU A  42       0.406  36.835   1.702  1.00 13.85           C  
ANISOU  588  CA  LEU A  42     1639   1630   1993     56     22   -167       C  
ATOM    589  C   LEU A  42       0.432  38.291   1.261  1.00 16.58           C  
ANISOU  589  C   LEU A  42     2110   1835   2356     61      4   -109       C  
ATOM    590  O   LEU A  42       0.823  38.592   0.131  1.00 15.62           O  
ANISOU  590  O   LEU A  42     2080   1702   2154      7    -57    -35       O  
ATOM    591  CB  LEU A  42       1.847  36.420   1.995  1.00 17.93           C  
ANISOU  591  CB  LEU A  42     2179   2229   2406    -60     83   -219       C  
ATOM    592  CG  LEU A  42       2.072  35.034   2.565  1.00 25.09           C  
ANISOU  592  CG  LEU A  42     2978   3250   3303    -76     97   -272       C  
ATOM    593  CD1 LEU A  42       3.519  34.655   2.383  1.00 28.01           C  
ANISOU  593  CD1 LEU A  42     3360   3689   3592   -179    120   -306       C  
ATOM    594  CD2 LEU A  42       1.711  35.012   4.022  1.00 24.59           C  
ANISOU  594  CD2 LEU A  42     2875   3177   3291    -53    157   -324       C  
ATOM    595  H   LEU A  42       0.317  35.993  -0.092  1.00 16.75           H  
ATOM    596  HA  LEU A  42      -0.124  36.751   2.510  1.00 16.62           H  
ATOM    597  HB2 LEU A  42       2.348  36.471   1.166  1.00 21.52           H  
ATOM    598  HB3 LEU A  42       2.218  37.052   2.630  1.00 21.52           H  
ATOM    599  HG  LEU A  42       1.518  34.391   2.095  1.00 30.10           H  
ATOM    600 HD11 LEU A  42       3.661  33.768   2.749  1.00 33.61           H  
ATOM    601 HD12 LEU A  42       3.731  34.662   1.437  1.00 33.61           H  
ATOM    602 HD13 LEU A  42       4.075  35.299   2.851  1.00 33.61           H  
ATOM    603 HD21 LEU A  42       1.860  34.119   4.371  1.00 29.51           H  
ATOM    604 HD22 LEU A  42       2.268  35.650   4.495  1.00 29.51           H  
ATOM    605 HD23 LEU A  42       0.776  35.253   4.119  1.00 29.51           H  
ATOM    606  N   THR A  43       0.061  39.188   2.163  1.00 15.76           N  
ANISOU  606  N   THR A  43     2018   1620   2349    112     63   -148       N  
ATOM    607  CA  THR A  43       0.221  40.626   1.949  1.00 17.05           C  
ANISOU  607  CA  THR A  43     2310   1624   2546    110     62   -108       C  
ATOM    608  C   THR A  43       0.904  41.184   3.192  1.00 19.99           C  
ANISOU  608  C   THR A  43     2720   1963   2914     51    192   -211       C  
ATOM    609  O   THR A  43       0.382  41.076   4.296  1.00 17.27           O  
ANISOU  609  O   THR A  43     2303   1618   2643     95    266   -299       O  
ATOM    610  CB  THR A  43      -1.134  41.321   1.739  1.00 21.36           C  
ANISOU  610  CB  THR A  43     2826   2025   3264    255     -9    -60       C  
ATOM    611  OG1 THR A  43      -1.940  41.141   2.898  1.00 34.36           O  
ANISOU  611  OG1 THR A  43     4350   3666   5038    336     74   -165       O  
ATOM    612  CG2 THR A  43      -1.883  40.707   0.560  1.00 24.30           C  
ANISOU  612  CG2 THR A  43     3149   2446   3638    308   -158     42       C  
ATOM    613  H   THR A  43      -0.293  38.989   2.921  1.00 18.91           H  
ATOM    614  HA  THR A  43       0.785  40.787   1.177  1.00 20.46           H  
ATOM    615  HB  THR A  43      -1.000  42.267   1.570  1.00 25.63           H  
ATOM    616  HG1 THR A  43      -1.558  41.474   3.568  1.00 41.23           H  
ATOM    617 HG21 THR A  43      -2.735  41.155   0.439  1.00 29.16           H  
ATOM    618 HG22 THR A  43      -1.359  40.801  -0.251  1.00 29.16           H  
ATOM    619 HG23 THR A  43      -2.043  39.764   0.724  1.00 29.16           H  
ATOM    620  N   LEU A  44       2.075  41.767   3.013  1.00 17.05           N  
ANISOU  620  N   LEU A  44     2464   1570   2444    -66    224   -206       N  
ATOM    621  CA  LEU A  44       2.901  42.186   4.145  1.00 19.32           C  
ANISOU  621  CA  LEU A  44     2788   1855   2699   -153    335   -306       C  
ATOM    622  C   LEU A  44       3.623  43.468   3.815  1.00 19.86           C  
ANISOU  622  C   LEU A  44     3009   1795   2743   -234    358   -282       C  
ATOM    623  O   LEU A  44       3.964  43.707   2.653  1.00 18.99           O  
ANISOU  623  O   LEU A  44     2979   1662   2573   -278    296   -188       O  
ATOM    624  CB  LEU A  44       3.941  41.101   4.433  1.00 20.19           C  
ANISOU  624  CB  LEU A  44     2837   2143   2690   -254    354   -349       C  
ATOM    625  CG  LEU A  44       3.397  39.809   5.042  1.00 21.08           C  
ANISOU  625  CG  LEU A  44     2815   2375   2821   -201    346   -384       C  
ATOM    626  CD1 LEU A  44       4.281  38.624   4.711  1.00 21.30           C  
ANISOU  626  CD1 LEU A  44     2780   2551   2762   -267    312   -381       C  
ATOM    627  CD2 LEU A  44       3.308  40.000   6.532  1.00 20.51           C  
ANISOU  627  CD2 LEU A  44     2731   2296   2764   -221    433   -479       C  
ATOM    628  H   LEU A  44       2.422  41.935   2.244  1.00 20.46           H  
ATOM    629  HA  LEU A  44       2.351  42.320   4.932  1.00 23.19           H  
ATOM    630  HB2 LEU A  44       4.379  40.867   3.600  1.00 24.22           H  
ATOM    631  HB3 LEU A  44       4.596  41.460   5.052  1.00 24.22           H  
ATOM    632  HG  LEU A  44       2.506  39.637   4.698  1.00 25.30           H  
ATOM    633 HD11 LEU A  44       3.903  37.826   5.114  1.00 25.56           H  
ATOM    634 HD12 LEU A  44       4.322  38.521   3.747  1.00 25.56           H  
ATOM    635 HD13 LEU A  44       5.170  38.785   5.065  1.00 25.56           H  
ATOM    636 HD21 LEU A  44       2.963  39.187   6.934  1.00 24.61           H  
ATOM    637 HD22 LEU A  44       4.193  40.191   6.879  1.00 24.61           H  
ATOM    638 HD23 LEU A  44       2.711  40.741   6.720  1.00 24.61           H  
ATOM    639  N   LYS A  45       3.844  44.297   4.832  1.00 18.83           N  
ANISOU  639  N   LYS A  45     2928   1579   2647   -268    451   -370       N  
ATOM    640  CA  LYS A  45       4.690  45.462   4.693  1.00 19.64           C  
ANISOU  640  CA  LYS A  45     3178   1569   2717   -374    491   -368       C  
ATOM    641  C   LYS A  45       5.793  45.351   5.738  1.00 21.01           C  
ANISOU  641  C   LYS A  45     3345   1840   2798   -511    580   -482       C  
ATOM    642  O   LYS A  45       5.532  45.030   6.912  1.00 18.78           O  
ANISOU  642  O   LYS A  45     2997   1606   2532   -497    635   -578       O  
ATOM    643  CB  LYS A  45       3.887  46.758   4.851  1.00 21.39           C  
ANISOU  643  CB  LYS A  45     3482   1554   3090   -289    509   -368       C  
ATOM    644  CG  LYS A  45       4.729  48.030   4.738  1.00 22.65           C  
ANISOU  644  CG  LYS A  45     3811   1569   3227   -407    553   -366       C  
ATOM    645  CD  LYS A  45       3.941  49.286   5.077  1.00 25.34           C  
ANISOU  645  CD  LYS A  45     4224   1656   3747   -316    584   -391       C  
ATOM    646  CE  LYS A  45       4.852  50.501   5.169  1.00 25.80           C  
ANISOU  646  CE  LYS A  45     4452   1571   3778   -453    648   -415       C  
ATOM    647  NZ  LYS A  45       4.132  51.701   5.603  1.00 27.76           N  
ANISOU  647  NZ  LYS A  45     4768   1558   4220   -366    693   -463       N  
ATOM    648  H   LYS A  45       3.509  44.200   5.618  1.00 22.59           H  
ATOM    649  HA  LYS A  45       5.099  45.460   3.813  1.00 23.57           H  
ATOM    650  HB2 LYS A  45       3.208  46.791   4.158  1.00 25.66           H  
ATOM    651  HB3 LYS A  45       3.465  46.759   5.724  1.00 25.66           H  
ATOM    652  HG2 LYS A  45       5.477  47.970   5.353  1.00 27.18           H  
ATOM    653  HG3 LYS A  45       5.053  48.116   3.828  1.00 27.18           H  
ATOM    654  HD2 LYS A  45       3.284  49.449   4.383  1.00 30.41           H  
ATOM    655  HD3 LYS A  45       3.503  49.168   5.935  1.00 30.41           H  
ATOM    656  HE2 LYS A  45       5.557  50.323   5.812  1.00 30.95           H  
ATOM    657  HE3 LYS A  45       5.235  50.678   4.295  1.00 30.95           H  
ATOM    658  HZ1 LYS A  45       3.482  51.891   5.026  1.00 33.31           H  
ATOM    659  HZ2 LYS A  45       3.775  51.567   6.407  1.00 33.31           H  
ATOM    660  HZ3 LYS A  45       4.691  52.392   5.646  1.00 33.31           H  
ATOM    661  N   PHE A  46       7.015  45.631   5.294  1.00 19.21           N  
ANISOU  661  N   PHE A  46     3187   1641   2470   -654    589   -469       N  
ATOM    662  CA  PHE A  46       8.207  45.591   6.123  1.00 18.95           C  
ANISOU  662  CA  PHE A  46     3145   1703   2353   -799    650   -565       C  
ATOM    663  C   PHE A  46       8.863  46.963   6.189  1.00 21.17           C  
ANISOU  663  C   PHE A  46     3573   1845   2626   -917    713   -594       C  
ATOM    664  O   PHE A  46       8.919  47.683   5.189  1.00 21.26           O  
ANISOU  664  O   PHE A  46     3695   1741   2643   -940    696   -510       O  
ATOM    665  CB  PHE A  46       9.209  44.587   5.551  1.00 17.97           C  
ANISOU  665  CB  PHE A  46     2937   1759   2134   -879    612   -548       C  
ATOM    666  CG  PHE A  46       8.661  43.191   5.430  1.00 16.70           C  
ANISOU  666  CG  PHE A  46     2638   1725   1984   -776    549   -522       C  
ATOM    667  CD1 PHE A  46       8.642  42.332   6.538  1.00 17.56           C  
ANISOU  667  CD1 PHE A  46     2642   1940   2090   -760    546   -584       C  
ATOM    668  CD2 PHE A  46       8.125  42.744   4.221  1.00 16.47           C  
ANISOU  668  CD2 PHE A  46     2596   1702   1959   -706    487   -432       C  
ATOM    669  CE1 PHE A  46       8.109  41.055   6.422  1.00 14.90           C  
ANISOU  669  CE1 PHE A  46     2189   1701   1770   -672    488   -556       C  
ATOM    670  CE2 PHE A  46       7.615  41.462   4.113  1.00 15.41           C  
ANISOU  670  CE2 PHE A  46     2338   1678   1839   -621    434   -418       C  
ATOM    671  CZ  PHE A  46       7.603  40.626   5.191  1.00 17.30           C  
ANISOU  671  CZ  PHE A  46     2474   2009   2091   -601    437   -479       C  
ATOM    672  H   PHE A  46       7.180  45.856   4.481  1.00 23.05           H  
ATOM    673  HA  PHE A  46       7.970  45.316   7.023  1.00 22.75           H  
ATOM    674  HB2 PHE A  46       9.475  44.880   4.665  1.00 21.57           H  
ATOM    675  HB3 PHE A  46       9.985  44.553   6.132  1.00 21.57           H  
ATOM    676  HD1 PHE A  46       8.982  42.620   7.354  1.00 21.07           H  
ATOM    677  HD2 PHE A  46       8.132  43.303   3.478  1.00 19.76           H  
ATOM    678  HE1 PHE A  46       8.106  40.481   7.154  1.00 17.88           H  
ATOM    679  HE2 PHE A  46       7.267  41.172   3.300  1.00 18.49           H  
ATOM    680  HZ  PHE A  46       7.249  39.769   5.108  1.00 20.76           H  
ATOM    681  N   ILE A  47       9.379  47.304   7.373  1.00 20.66           N  
ANISOU  681  N   ILE A  47     3519   1794   2538  -1007    782   -710       N  
ATOM    682  CA  ILE A  47      10.141  48.534   7.579  1.00 22.01           C  
ANISOU  682  CA  ILE A  47     3818   1853   2691  -1145    850   -760       C  
ATOM    683  C   ILE A  47      11.501  48.178   8.161  1.00 23.73           C  
ANISOU  683  C   ILE A  47     3946   2275   2795  -1268    848   -805       C  
ATOM    684  O   ILE A  47      11.596  47.323   9.042  1.00 21.25           O  
ANISOU  684  O   ILE A  47     3521   2106   2447  -1258    826   -850       O  
ATOM    685  CB  ILE A  47       9.469  49.427   8.625  1.00 28.21           C  
ANISOU  685  CB  ILE A  47     4648   2518   3552  -1088    916   -835       C  
ATOM    686  CG1 ILE A  47       8.023  49.749   8.244  1.00 35.14           C  
ANISOU  686  CG1 ILE A  47     5572   3192   4587   -926    916   -804       C  
ATOM    687  CG2 ILE A  47      10.286  50.692   8.845  1.00 38.54           C  
ANISOU  687  CG2 ILE A  47     6048   3762   4833  -1194    964   -857       C  
ATOM    688  CD1 ILE A  47       7.878  50.907   7.338  1.00 36.65           C  
ANISOU  688  CD1 ILE A  47     5904   3164   4858   -910    899   -718       C  
ATOM    689  H   ILE A  47       9.297  46.828   8.085  1.00 24.79           H  
ATOM    690  HA  ILE A  47      10.252  49.021   6.747  1.00 26.41           H  
ATOM    691  HB  ILE A  47       9.451  48.938   9.463  1.00 33.85           H  
ATOM    692 HG12 ILE A  47       7.640  48.976   7.800  1.00 42.16           H  
ATOM    693 HG13 ILE A  47       7.524  49.942   9.053  1.00 42.16           H  
ATOM    694 HG21 ILE A  47       9.843  51.242   9.510  1.00 46.25           H  
ATOM    695 HG22 ILE A  47      11.172  50.445   9.156  1.00 46.25           H  
ATOM    696 HG23 ILE A  47      10.352  51.175   8.006  1.00 46.25           H  
ATOM    697 HD11 ILE A  47       6.936  51.042   7.147  1.00 43.98           H  
ATOM    698 HD12 ILE A  47       8.244  51.694   7.771  1.00 43.98           H  
ATOM    699 HD13 ILE A  47       8.360  50.726   6.516  1.00 43.98           H  
ATOM    700  N   CYS A  48      12.548  48.857   7.719  1.00 22.51           N  
ANISOU  700  N   CYS A  48     3839   2126   2588  -1379    867   -789       N  
ATOM    701  CA  CYS A  48      13.806  48.841   8.448  1.00 22.74           C  
ANISOU  701  CA  CYS A  48     3795   2308   2539  -1484    875   -844       C  
ATOM    702  C   CYS A  48      13.696  49.874   9.570  1.00 23.97           C  
ANISOU  702  C   CYS A  48     4022   2381   2703  -1510    934   -913       C  
ATOM    703  O   CYS A  48      13.540  51.068   9.332  1.00 25.29           O  
ANISOU  703  O   CYS A  48     4316   2385   2907  -1529    984   -910       O  
ATOM    704  CB  CYS A  48      14.992  49.175   7.547  1.00 23.37           C  
ANISOU  704  CB  CYS A  48     3885   2432   2562  -1594    887   -819       C  
ATOM    705  SG  CYS A  48      16.579  49.059   8.445  1.00 25.80           S  
ANISOU  705  SG  CYS A  48     4077   2927   2801  -1706    885   -893       S  
ATOM    706  H   CYS A  48      12.557  49.333   7.003  1.00 27.01           H  
ATOM    707  HA  CYS A  48      13.947  47.965   8.841  1.00 27.29           H  
ATOM    708  HB2 CYS A  48      15.016  48.549   6.807  1.00 28.04           H  
ATOM    709  HB3 CYS A  48      14.896  50.082   7.217  1.00 28.04           H  
ATOM    710  HG  CYS A  48      17.474  49.331   7.692  1.00 30.97           H  
ATOM    711  N   THR A  49      13.743  49.406  10.800  1.00 23.69           N  
ANISOU  711  N   THR A  49     3912   2456   2634  -1515    925   -969       N  
ATOM    712  CA  THR A  49      13.518  50.288  11.933  1.00 24.93           C  
ANISOU  712  CA  THR A  49     4134   2548   2790  -1545    990  -1043       C  
ATOM    713  C   THR A  49      14.819  50.902  12.422  1.00 26.03           C  
ANISOU  713  C   THR A  49     4280   2757   2853  -1687   1005  -1082       C  
ATOM    714  O   THR A  49      14.805  51.762  13.298  1.00 28.32           O  
ANISOU  714  O   THR A  49     4636   2994   3132  -1740   1065  -1149       O  
ATOM    715  CB  THR A  49      12.902  49.501  13.078  1.00 24.38           C  
ANISOU  715  CB  THR A  49     3997   2568   2699  -1505    978  -1082       C  
ATOM    716  OG1 THR A  49      13.799  48.446  13.445  1.00 23.60           O  
ANISOU  716  OG1 THR A  49     3781   2665   2519  -1557    894  -1061       O  
ATOM    717  CG2 THR A  49      11.576  48.895  12.647  1.00 23.43           C  
ANISOU  717  CG2 THR A  49     3860   2382   2660  -1363    972  -1057       C  
ATOM    718  H   THR A  49      13.903  48.587  11.009  1.00 28.43           H  
ATOM    719  HA  THR A  49      12.910  51.000  11.680  1.00 29.92           H  
ATOM    720  HB  THR A  49      12.750  50.085  13.837  1.00 29.26           H  
ATOM    721  HG1 THR A  49      13.474  48.000  14.078  1.00 28.32           H  
ATOM    722 HG21 THR A  49      11.187  48.394  13.381  1.00 28.12           H  
ATOM    723 HG22 THR A  49      10.961  49.598  12.384  1.00 28.12           H  
ATOM    724 HG23 THR A  49      11.713  48.298  11.896  1.00 28.12           H  
ATOM    725  N   THR A  50      15.944  50.443  11.898  1.00 25.66           N  
ANISOU  725  N   THR A  50     4157   2834   2761  -1749    955  -1052       N  
ATOM    726  CA  THR A  50      17.255  50.909  12.370  1.00 28.74           C  
ANISOU  726  CA  THR A  50     4528   3307   3086  -1880    959  -1094       C  
ATOM    727  C   THR A  50      17.881  51.955  11.449  1.00 34.05           C  
ANISOU  727  C   THR A  50     5287   3890   3762  -1958   1014  -1087       C  
ATOM    728  O   THR A  50      18.966  52.448  11.739  1.00 33.22           O  
ANISOU  728  O   THR A  50     5172   3839   3610  -2073   1028  -1128       O  
ATOM    729  CB  THR A  50      18.243  49.725  12.498  1.00 26.03           C  
ANISOU  729  CB  THR A  50     4020   3163   2707  -1898    864  -1079       C  
ATOM    730  OG1 THR A  50      18.134  48.889  11.337  1.00 24.81           O  
ANISOU  730  OG1 THR A  50     3799   3037   2591  -1826    830  -1022       O  
ATOM    731  CG2 THR A  50      17.919  48.882  13.724  1.00 25.56           C  
ANISOU  731  CG2 THR A  50     3896   3197   2617  -1868    799  -1089       C  
ATOM    732  H   THR A  50      15.985  49.860  11.267  1.00 30.80           H  
ATOM    733  HA  THR A  50      17.149  51.308  13.248  1.00 34.49           H  
ATOM    734  HB  THR A  50      19.150  50.059  12.579  1.00 31.24           H  
ATOM    735  HG1 THR A  50      18.319  49.331  10.647  1.00 29.77           H  
ATOM    736 HG21 THR A  50      18.544  48.143  13.793  1.00 30.67           H  
ATOM    737 HG22 THR A  50      17.982  49.424  14.526  1.00 30.67           H  
ATOM    738 HG23 THR A  50      17.019  48.527  13.654  1.00 30.67           H  
ATOM    739  N   GLY A  51      17.209  52.283  10.345  1.00 27.80           N  
ANISOU  739  N   GLY A  51     4583   2957   3021  -1903   1038  -1030       N  
ATOM    740  CA  GLY A  51      17.719  53.249   9.387  1.00 29.02           C  
ANISOU  740  CA  GLY A  51     4841   3015   3168  -1983   1083  -1004       C  
ATOM    741  C   GLY A  51      17.688  52.689   7.972  1.00 33.12           C  
ANISOU  741  C   GLY A  51     5351   3548   3686  -1957   1055   -923       C  
ATOM    742  O   GLY A  51      16.703  52.082   7.564  1.00 29.75           O  
ANISOU  742  O   GLY A  51     4922   3080   3303  -1849   1019   -870       O  
ATOM    743  H   GLY A  51      16.445  51.952  10.131  1.00 33.35           H  
ATOM    744  HA2 GLY A  51      17.179  54.054   9.416  1.00 34.82           H  
ATOM    745  HA3 GLY A  51      18.634  53.480   9.611  1.00 34.82           H  
ATOM    746  N   LYS A  52      18.768  52.887   7.220  1.00 32.75           N  
ANISOU  746  N   LYS A  52     5297   3563   3582  -2065   1077   -919       N  
ATOM    747  CA  LYS A  52      18.867  52.328   5.863  1.00 33.84           C  
ANISOU  747  CA  LYS A  52     5423   3740   3695  -2066   1064   -856       C  
ATOM    748  C   LYS A  52      19.240  50.848   5.918  1.00 32.80           C  
ANISOU  748  C   LYS A  52     5094   3808   3560  -2018   1014   -880       C  
ATOM    749  O   LYS A  52      20.113  50.429   6.674  1.00 26.98           O  
ANISOU  749  O   LYS A  52     4224   3210   2817  -2045    996   -945       O  
ATOM    750  CB  LYS A  52      19.908  53.111   5.048  1.00 33.94           C  
ANISOU  750  CB  LYS A  52     5504   3751   3642  -2212   1122   -859       C  
ATOM    751  CG  LYS A  52      20.109  52.641   3.615  1.00 39.22           C  
ANISOU  751  CG  LYS A  52     6177   4468   4257  -2244   1126   -807       C  
ATOM    752  CD  LYS A  52      21.218  53.429   2.928  1.00 42.14           C  
ANISOU  752  CD  LYS A  52     6611   4850   4551  -2405   1196   -831       C  
ATOM    753  H   LYS A  52      19.457  53.338   7.466  1.00 39.30           H  
ATOM    754  HA  LYS A  52      18.008  52.409   5.419  1.00 40.61           H  
ATOM    755  HB2 LYS A  52      19.633  54.041   5.013  1.00 40.73           H  
ATOM    756  HB3 LYS A  52      20.764  53.044   5.499  1.00 40.73           H  
ATOM    757  HG2 LYS A  52      20.358  51.704   3.616  1.00 47.07           H  
ATOM    758  HG3 LYS A  52      19.288  52.772   3.116  1.00 47.07           H  
ATOM    759  N   LEU A  53      18.588  50.039   5.102  1.00 28.92           N  
ANISOU  759  N   LEU A  53     4582   3324   3080  -1944    982   -823       N  
ATOM    760  CA  LEU A  53      18.953  48.637   5.033  1.00 24.73           C  
ANISOU  760  CA  LEU A  53     3867   2969   2561  -1894    937   -847       C  
ATOM    761  C   LEU A  53      20.308  48.467   4.327  1.00 28.88           C  
ANISOU  761  C   LEU A  53     4311   3618   3045  -1990    975   -895       C  
ATOM    762  O   LEU A  53      20.506  48.992   3.245  1.00 29.90           O  
ANISOU  762  O   LEU A  53     4540   3704   3118  -2070   1028   -872       O  
ATOM    763  CB  LEU A  53      17.866  47.886   4.278  1.00 25.82           C  
ANISOU  763  CB  LEU A  53     4017   3074   2720  -1801    901   -779       C  
ATOM    764  CG  LEU A  53      17.835  46.388   4.469  1.00 22.15           C  
ANISOU  764  CG  LEU A  53     3370   2752   2294  -1711    841   -799       C  
ATOM    765  CD1 LEU A  53      17.465  46.060   5.933  1.00 21.45           C  
ANISOU  765  CD1 LEU A  53     3217   2683   2250  -1638    788   -825       C  
ATOM    766  CD2 LEU A  53      16.816  45.780   3.511  1.00 23.98           C  
ANISOU  766  CD2 LEU A  53     3632   2945   2533  -1648    819   -732       C  
ATOM    767  H   LEU A  53      17.940  50.272   4.586  1.00 34.70           H  
ATOM    768  HA  LEU A  53      19.020  48.271   5.929  1.00 29.68           H  
ATOM    769  HB2 LEU A  53      17.005  48.230   4.562  1.00 30.99           H  
ATOM    770  HB3 LEU A  53      17.984  48.053   3.330  1.00 30.99           H  
ATOM    771  HG  LEU A  53      18.709  46.014   4.275  1.00 26.58           H  
ATOM    772 HD11 LEU A  53      17.448  45.096   6.045  1.00 25.74           H  
ATOM    773 HD12 LEU A  53      18.130  46.450   6.522  1.00 25.74           H  
ATOM    774 HD13 LEU A  53      16.591  46.432   6.128  1.00 25.74           H  
ATOM    775 HD21 LEU A  53      16.800  44.818   3.637  1.00 28.77           H  
ATOM    776 HD22 LEU A  53      15.942  46.154   3.701  1.00 28.77           H  
ATOM    777 HD23 LEU A  53      17.075  45.990   2.600  1.00 28.77           H  
ATOM    778  N   PRO A  54      21.246  47.719   4.928  1.00 32.71           N  
ANISOU  778  N   PRO A  54     4615   4251   3563  -1981    943   -963       N  
ATOM    779  CA  PRO A  54      22.592  47.588   4.337  1.00 32.55           C  
ANISOU  779  CA  PRO A  54     4499   4338   3529  -2067    986  -1030       C  
ATOM    780  C   PRO A  54      22.696  46.567   3.198  1.00 27.05           C  
ANISOU  780  C   PRO A  54     3718   3719   2840  -2033    997  -1039       C  
ATOM    781  O   PRO A  54      23.767  46.435   2.594  1.00 28.78           O  
ANISOU  781  O   PRO A  54     3863   4021   3053  -2104   1049  -1110       O  
ATOM    782  CB  PRO A  54      23.434  47.106   5.513  1.00 35.55           C  
ANISOU  782  CB  PRO A  54     4713   4823   3973  -2048    921  -1087       C  
ATOM    783  CG  PRO A  54      22.443  46.323   6.352  1.00 30.64           C  
ANISOU  783  CG  PRO A  54     4054   4194   3394  -1919    828  -1040       C  
ATOM    784  CD  PRO A  54      21.158  47.072   6.245  1.00 25.37           C  
ANISOU  784  CD  PRO A  54     3572   3381   2686  -1904    861   -980       C  
ATOM    785  HA  PRO A  54      22.919  48.450   4.035  1.00 39.05           H  
ATOM    786  HB2 PRO A  54      24.151  46.535   5.197  1.00 42.67           H  
ATOM    787  HB3 PRO A  54      23.783  47.866   6.005  1.00 42.67           H  
ATOM    788  HG2 PRO A  54      22.348  45.427   5.992  1.00 36.77           H  
ATOM    789  HG3 PRO A  54      22.746  46.293   7.272  1.00 36.77           H  
ATOM    790  HD2 PRO A  54      20.406  46.460   6.271  1.00 30.44           H  
ATOM    791  HD3 PRO A  54      21.097  47.740   6.946  1.00 30.44           H  
ATOM    792  N   VAL A  55      21.604  45.860   2.940  1.00 24.63           N  
ANISOU  792  N   VAL A  55     3422   3387   2550  -1930    954   -980       N  
ATOM    793  CA  VAL A  55      21.517  44.883   1.865  1.00 26.80           C  
ANISOU  793  CA  VAL A  55     3633   3723   2825  -1895    963   -988       C  
ATOM    794  C   VAL A  55      20.233  45.190   1.082  1.00 23.77           C  
ANISOU  794  C   VAL A  55     3421   3228   2382  -1889    965   -892       C  
ATOM    795  O   VAL A  55      19.359  45.902   1.569  1.00 25.09           O  
ANISOU  795  O   VAL A  55     3712   3271   2548  -1869    942   -824       O  
ATOM    796  CB  VAL A  55      21.499  43.432   2.418  1.00 22.99           C  
ANISOU  796  CB  VAL A  55     2955   3333   2447  -1758    880  -1010       C  
ATOM    797  CG1 VAL A  55      22.762  43.143   3.227  1.00 25.78           C  
ANISOU  797  CG1 VAL A  55     3146   3773   2876  -1761    849  -1083       C  
ATOM    798  CG2 VAL A  55      20.222  43.155   3.286  1.00 21.52           C  
ANISOU  798  CG2 VAL A  55     2797   3087   2294  -1650    798   -937       C  
ATOM    799  H   VAL A  55      20.875  45.932   3.390  1.00 29.56           H  
ATOM    800  HA  VAL A  55      22.277  44.981   1.269  1.00 32.15           H  
ATOM    801  HB  VAL A  55      21.483  42.816   1.669  1.00 27.59           H  
ATOM    802 HG11 VAL A  55      22.722  42.233   3.559  1.00 30.94           H  
ATOM    803 HG12 VAL A  55      23.536  43.253   2.653  1.00 30.94           H  
ATOM    804 HG13 VAL A  55      22.809  43.765   3.970  1.00 30.94           H  
ATOM    805 HG21 VAL A  55      20.253  42.241   3.609  1.00 25.83           H  
ATOM    806 HG22 VAL A  55      20.211  43.771   4.035  1.00 25.83           H  
ATOM    807 HG23 VAL A  55      19.433  43.286   2.737  1.00 25.83           H  
ATOM    808  N   PRO A  56      20.120  44.681  -0.142  1.00 23.89           N  
ANISOU  808  N   PRO A  56     3448   3277   2350  -1910    990   -889       N  
ATOM    809  CA  PRO A  56      18.894  44.935  -0.901  1.00 23.66           C  
ANISOU  809  CA  PRO A  56     3583   3142   2266  -1908    970   -780       C  
ATOM    810  C   PRO A  56      17.718  44.149  -0.343  1.00 21.99           C  
ANISOU  810  C   PRO A  56     3316   2909   2131  -1768    891   -729       C  
ATOM    811  O   PRO A  56      17.889  43.015   0.117  1.00 21.00           O  
ANISOU  811  O   PRO A  56     3013   2887   2079  -1677    857   -784       O  
ATOM    812  CB  PRO A  56      19.246  44.439  -2.309  1.00 24.39           C  
ANISOU  812  CB  PRO A  56     3678   3310   2278  -1981   1015   -811       C  
ATOM    813  CG  PRO A  56      20.757  44.457  -2.334  1.00 25.53           C  
ANISOU  813  CG  PRO A  56     3719   3556   2423  -2060   1088   -940       C  
ATOM    814  CD  PRO A  56      21.153  44.040  -0.965  1.00 24.66           C  
ANISOU  814  CD  PRO A  56     3440   3496   2435  -1960   1046   -987       C  
ATOM    815  HA  PRO A  56      18.684  45.882  -0.923  1.00 28.40           H  
ATOM    816  HB2 PRO A  56      18.909  43.538  -2.436  1.00 29.27           H  
ATOM    817  HB3 PRO A  56      18.881  45.044  -2.974  1.00 29.27           H  
ATOM    818  HG2 PRO A  56      21.083  43.827  -2.995  1.00 30.63           H  
ATOM    819  HG3 PRO A  56      21.072  45.355  -2.526  1.00 30.63           H  
ATOM    820  HD2 PRO A  56      21.111  43.075  -0.876  1.00 29.60           H  
ATOM    821  HD3 PRO A  56      22.031  44.386  -0.743  1.00 29.60           H  
ATOM    822  N   TRP A  57      16.543  44.756  -0.412  1.00 21.89           N  
ANISOU  822  N   TRP A  57     3460   2749   2110  -1749    859   -621       N  
ATOM    823  CA  TRP A  57      15.330  44.151   0.099  1.00 20.55           C  
ANISOU  823  CA  TRP A  57     3258   2535   2015  -1628    791   -576       C  
ATOM    824  C   TRP A  57      15.079  42.775  -0.503  1.00 19.64           C  
ANISOU  824  C   TRP A  57     3017   2537   1907  -1576    766   -589       C  
ATOM    825  O   TRP A  57      14.708  41.849   0.219  1.00 18.42           O  
ANISOU  825  O   TRP A  57     2728   2435   1836  -1471    715   -619       O  
ATOM    826  CB  TRP A  57      14.137  45.066  -0.144  1.00 21.03           C  
ANISOU  826  CB  TRP A  57     3522   2392   2075  -1617    762   -453       C  
ATOM    827  CG  TRP A  57      14.008  46.145   0.890  1.00 21.51           C  
ANISOU  827  CG  TRP A  57     3664   2317   2191  -1599    771   -464       C  
ATOM    828  CD1 TRP A  57      14.297  47.480   0.744  1.00 25.14           C  
ANISOU  828  CD1 TRP A  57     4280   2653   2620  -1672    803   -431       C  
ATOM    829  CD2 TRP A  57      13.541  45.977   2.218  1.00 20.67           C  
ANISOU  829  CD2 TRP A  57     3487   2194   2173  -1495    747   -518       C  
ATOM    830  NE1 TRP A  57      14.032  48.153   1.925  1.00 23.90           N  
ANISOU  830  NE1 TRP A  57     4148   2395   2539  -1622    811   -471       N  
ATOM    831  CE2 TRP A  57      13.567  47.247   2.843  1.00 21.73           C  
ANISOU  831  CE2 TRP A  57     3741   2187   2329  -1524    781   -529       C  
ATOM    832  CE3 TRP A  57      13.096  44.874   2.945  1.00 19.28           C  
ANISOU  832  CE3 TRP A  57     3156   2120   2050  -1363    695   -554       C  
ATOM    833  CZ2 TRP A  57      13.161  47.435   4.166  1.00 24.82           C  
ANISOU  833  CZ2 TRP A  57     4107   2536   2787  -1454    784   -593       C  
ATOM    834  CZ3 TRP A  57      12.708  45.054   4.254  1.00 19.03           C  
ANISOU  834  CZ3 TRP A  57     3107   2050   2072  -1303    692   -604       C  
ATOM    835  CH2 TRP A  57      12.734  46.327   4.856  1.00 21.04           C  
ANISOU  835  CH2 TRP A  57     3491   2160   2342  -1362    744   -634       C  
ATOM    836  H   TRP A  57      16.423  45.534  -0.758  1.00 26.27           H  
ATOM    837  HA  TRP A  57      15.422  44.038   1.058  1.00 24.66           H  
ATOM    838  HB2 TRP A  57      14.238  45.492  -1.009  1.00 25.23           H  
ATOM    839  HB3 TRP A  57      13.325  44.537  -0.127  1.00 25.23           H  
ATOM    840  HD1 TRP A  57      14.621  47.874  -0.033  1.00 30.17           H  
ATOM    841  HE1 TRP A  57      14.141  48.995   2.059  1.00 28.68           H  
ATOM    842  HE3 TRP A  57      13.070  44.030   2.556  1.00 23.14           H  
ATOM    843  HZ2 TRP A  57      13.188  48.275   4.567  1.00 29.78           H  
ATOM    844  HZ3 TRP A  57      12.408  44.324   4.745  1.00 22.83           H  
ATOM    845  HH2 TRP A  57      12.464  46.418   5.741  1.00 25.25           H  
ATOM    846  N   PRO A  58      15.280  42.622  -1.821  1.00 20.37           N  
ANISOU  846  N   PRO A  58     3158   2673   1908  -1652    798   -571       N  
ATOM    847  CA  PRO A  58      14.972  41.293  -2.375  1.00 19.59           C  
ANISOU  847  CA  PRO A  58     2942   2682   1820  -1598    778   -595       C  
ATOM    848  C   PRO A  58      15.805  40.167  -1.779  1.00 18.90           C  
ANISOU  848  C   PRO A  58     2628   2727   1825  -1517    775   -721       C  
ATOM    849  O   PRO A  58      15.356  39.033  -1.838  1.00 18.01           O  
ANISOU  849  O   PRO A  58     2406   2672   1766  -1428    736   -736       O  
ATOM    850  CB  PRO A  58      15.262  41.437  -3.885  1.00 20.90           C  
ANISOU  850  CB  PRO A  58     3213   2879   1849  -1717    822   -581       C  
ATOM    851  CG  PRO A  58      15.067  42.904  -4.167  1.00 22.78           C  
ANISOU  851  CG  PRO A  58     3679   2973   2006  -1806    823   -472       C  
ATOM    852  CD  PRO A  58      15.522  43.634  -2.870  1.00 21.99           C  
ANISOU  852  CD  PRO A  58     3552   2813   1992  -1781    836   -513       C  
ATOM    853  HA  PRO A  58      14.031  41.091  -2.251  1.00 23.51           H  
ATOM    854  HB2 PRO A  58      16.175  41.168  -4.072  1.00 25.08           H  
ATOM    855  HB3 PRO A  58      14.633  40.901  -4.393  1.00 25.08           H  
ATOM    856  HG2 PRO A  58      15.618  43.168  -4.921  1.00 27.34           H  
ATOM    857  HG3 PRO A  58      14.130  43.080  -4.349  1.00 27.34           H  
ATOM    858  HD2 PRO A  58      16.466  43.855  -2.918  1.00 26.39           H  
ATOM    859  HD3 PRO A  58      14.978  44.421  -2.714  1.00 26.39           H  
ATOM    860  N   THR A  59      16.955  40.462  -1.176  1.00 19.40           N  
ANISOU  860  N   THR A  59     2628   2826   1918  -1537    804   -796       N  
ATOM    861  CA  THR A  59      17.729  39.394  -0.565  1.00 18.98           C  
ANISOU  861  CA  THR A  59     2373   2870   1969  -1445    778   -884       C  
ATOM    862  C   THR A  59      17.133  38.899   0.734  1.00 17.74           C  
ANISOU  862  C   THR A  59     2137   2697   1905  -1320    685   -849       C  
ATOM    863  O   THR A  59      17.569  37.870   1.250  1.00 17.39           O  
ANISOU  863  O   THR A  59     1942   2711   1953  -1227    633   -887       O  
ATOM    864  CB  THR A  59      19.198  39.774  -0.291  1.00 21.16           C  
ANISOU  864  CB  THR A  59     2588   3192   2261  -1506    824   -968       C  
ATOM    865  OG1 THR A  59      19.270  40.753   0.756  1.00 21.37           O  
ANISOU  865  OG1 THR A  59     2671   3163   2286  -1532    806   -935       O  
ATOM    866  CG2 THR A  59      19.864  40.306  -1.570  1.00 24.80           C  
ANISOU  866  CG2 THR A  59     3132   3671   2618  -1650    925  -1020       C  
ATOM    867  H   THR A  59      17.298  41.247  -1.110  1.00 23.28           H  
ATOM    868  HA  THR A  59      17.739  38.643  -1.179  1.00 22.78           H  
ATOM    869  HB  THR A  59      19.681  38.980  -0.012  1.00 25.39           H  
ATOM    870  HG1 THR A  59      18.848  41.444   0.532  1.00 25.64           H  
ATOM    871 HG21 THR A  59      20.787  40.543  -1.389  1.00 29.76           H  
ATOM    872 HG22 THR A  59      19.842  39.627  -2.262  1.00 29.76           H  
ATOM    873 HG23 THR A  59      19.392  41.093  -1.886  1.00 29.76           H  
ATOM    874  N   LEU A  60      16.171  39.633   1.289  1.00 17.38           N  
ANISOU  874  N   LEU A  60     2204   2559   1842  -1321    660   -777       N  
ATOM    875  CA  LEU A  60      15.544  39.235   2.549  1.00 16.33           C  
ANISOU  875  CA  LEU A  60     2018   2410   1777  -1222    581   -757       C  
ATOM    876  C   LEU A  60      14.170  38.587   2.381  1.00 15.33           C  
ANISOU  876  C   LEU A  60     1895   2256   1676  -1145    533   -710       C  
ATOM    877  O   LEU A  60      13.618  38.078   3.344  1.00 14.59           O  
ANISOU  877  O   LEU A  60     1750   2163   1630  -1052    469   -698       O  
ATOM    878  CB  LEU A  60      15.385  40.454   3.459  1.00 16.71           C  
ANISOU  878  CB  LEU A  60     2182   2368   1801  -1270    592   -742       C  
ATOM    879  CG  LEU A  60      16.662  41.199   3.816  1.00 17.78           C  
ANISOU  879  CG  LEU A  60     2317   2527   1911  -1353    631   -787       C  
ATOM    880  CD1 LEU A  60      16.324  42.342   4.760  1.00 18.16           C  
ANISOU  880  CD1 LEU A  60     2487   2477   1938  -1389    643   -776       C  
ATOM    881  CD2 LEU A  60      17.662  40.238   4.441  1.00 24.63           C  
ANISOU  881  CD2 LEU A  60     3008   3507   2842  -1304    575   -835       C  
ATOM    882  H   LEU A  60      15.863  40.364   0.957  1.00 20.86           H  
ATOM    883  HA  LEU A  60      16.121  38.598   3.000  1.00 19.60           H  
ATOM    884  HB2 LEU A  60      14.795  41.087   3.020  1.00 20.06           H  
ATOM    885  HB3 LEU A  60      14.980  40.163   4.291  1.00 20.06           H  
ATOM    886  HG  LEU A  60      17.055  41.571   3.011  1.00 21.34           H  
ATOM    887 HD11 LEU A  60      17.139  42.816   4.987  1.00 21.80           H  
ATOM    888 HD12 LEU A  60      15.703  42.943   4.319  1.00 21.80           H  
ATOM    889 HD13 LEU A  60      15.918  41.979   5.563  1.00 21.80           H  
ATOM    890 HD21 LEU A  60      18.470  40.725   4.663  1.00 29.55           H  
ATOM    891 HD22 LEU A  60      17.273  39.857   5.244  1.00 29.55           H  
ATOM    892 HD23 LEU A  60      17.863  39.534   3.804  1.00 29.55           H  
ATOM    893  N   VAL A  61      13.609  38.621   1.171  1.00 15.49           N  
ANISOU  893  N   VAL A  61     1990   2251   1643  -1143    552   -661       N  
ATOM    894  CA  VAL A  61      12.270  38.077   0.971  1.00 14.72           C  
ANISOU  894  CA  VAL A  61     1909   2126   1560  -1002    485   -587       C  
ATOM    895  C   VAL A  61      12.133  36.640   1.483  1.00 14.26           C  
ANISOU  895  C   VAL A  61     1686   2149   1584   -904    429   -622       C  
ATOM    896  O   VAL A  61      11.221  36.350   2.246  1.00 13.80           O  
ANISOU  896  O   VAL A  61     1618   2061   1565   -797    373   -583       O  
ATOM    897  CB  VAL A  61      11.864  38.180  -0.517  1.00 15.28           C  
ANISOU  897  CB  VAL A  61     2071   2185   1548  -1033    497   -532       C  
ATOM    898  CG1 VAL A  61      10.575  37.428  -0.812  1.00 15.19           C  
ANISOU  898  CG1 VAL A  61     2042   2171   1560   -898    417   -470       C  
ATOM    899  CG2 VAL A  61      11.684  39.633  -0.857  1.00 19.01           C  
ANISOU  899  CG2 VAL A  61     2733   2538   1953  -1100    517   -456       C  
ATOM    900  H   VAL A  61      13.976  38.946   0.464  1.00 18.58           H  
ATOM    901  HA  VAL A  61      11.645  38.620   1.476  1.00 17.67           H  
ATOM    902  HB  VAL A  61      12.570  37.816  -1.074  1.00 18.33           H  
ATOM    903 HG11 VAL A  61      10.363  37.522  -1.754  1.00 18.23           H  
ATOM    904 HG12 VAL A  61      10.699  36.492  -0.592  1.00 18.23           H  
ATOM    905 HG13 VAL A  61       9.861  37.803  -0.273  1.00 18.23           H  
ATOM    906 HG21 VAL A  61      11.429  39.709  -1.790  1.00 22.82           H  
ATOM    907 HG22 VAL A  61      10.988  40.005  -0.293  1.00 22.82           H  
ATOM    908 HG23 VAL A  61      12.520  40.099  -0.704  1.00 22.82           H  
ATOM    909  N   THR A  62      13.036  35.729   1.104  1.00 13.88           N  
ANISOU  909  N   THR A  62     1506   2195   1572   -944    447   -702       N  
ATOM    910  CA  THR A  62      12.846  34.333   1.509  1.00 15.71           C  
ANISOU  910  CA  THR A  62     1602   2472   1894   -831    380   -717       C  
ATOM    911  C   THR A  62      12.939  34.148   3.042  1.00 13.50           C  
ANISOU  911  C   THR A  62     1281   2180   1668   -768    311   -697       C  
ATOM    912  O   THR A  62      12.274  33.262   3.616  1.00 12.13           O  
ANISOU  912  O   THR A  62     1058   2006   1544   -676    243   -665       O  
ATOM    913  CB  THR A  62      13.830  33.404   0.810  1.00 13.63           C  
ANISOU  913  CB  THR A  62     1251   2261   1667   -807    402   -781       C  
ATOM    914  OG1 THR A  62      15.160  33.905   0.980  1.00 14.50           O  
ANISOU  914  OG1 THR A  62     1346   2385   1778   -866    442   -831       O  
ATOM    915  CG2 THR A  62      13.522  33.345  -0.695  1.00 14.04           C  
ANISOU  915  CG2 THR A  62     1347   2340   1646   -874    466   -806       C  
ATOM    916  H   THR A  62      13.738  35.885   0.632  1.00 16.65           H  
ATOM    917  HA  THR A  62      11.955  34.060   1.241  1.00 18.85           H  
ATOM    918  HB  THR A  62      13.763  32.510   1.181  1.00 16.36           H  
ATOM    919  HG1 THR A  62      15.349  33.945   1.798  1.00 17.40           H  
ATOM    920 HG21 THR A  62      14.149  32.753  -1.139  1.00 16.85           H  
ATOM    921 HG22 THR A  62      12.621  33.013  -0.836  1.00 16.85           H  
ATOM    922 HG23 THR A  62      13.596  34.231  -1.083  1.00 16.85           H  
ATOM    923  N   THR A  63      13.735  34.995   3.694  1.00 13.33           N  
ANISOU  923  N   THR A  63     1291   2148   1624   -832    329   -712       N  
ATOM    924  CA  THR A  63      13.903  34.918   5.138  1.00 13.26           C  
ANISOU  924  CA  THR A  63     1261   2138   1638   -808    263   -694       C  
ATOM    925  C   THR A  63      12.645  35.434   5.845  1.00 15.56           C  
ANISOU  925  C   THR A  63     1638   2380   1893   -813    259   -667       C  
ATOM    926  O   THR A  63      12.187  34.858   6.839  1.00 12.46           O  
ANISOU  926  O   THR A  63     1221   1998   1517   -767    198   -643       O  
ATOM    927  CB  THR A  63      15.115  35.756   5.553  1.00 14.23           C  
ANISOU  927  CB  THR A  63     1398   2270   1739   -891    287   -726       C  
ATOM    928  OG1 THR A  63      16.297  35.182   4.981  1.00 14.80           O  
ANISOU  928  OG1 THR A  63     1370   2386   1866   -881    290   -767       O  
ATOM    929  CG2 THR A  63      15.298  35.813   7.079  1.00 14.36           C  
ANISOU  929  CG2 THR A  63     1412   2290   1753   -896    215   -707       C  
ATOM    930  H   THR A  63      14.189  35.622   3.320  1.00 15.99           H  
ATOM    931  HA  THR A  63      14.055  33.998   5.402  1.00 15.91           H  
ATOM    932  HB  THR A  63      15.007  36.662   5.224  1.00 17.08           H  
ATOM    933  HG1 THR A  63      16.236  35.175   4.144  1.00 17.76           H  
ATOM    934 HG21 THR A  63      16.075  36.351   7.300  1.00 17.23           H  
ATOM    935 HG22 THR A  63      14.514  36.207   7.492  1.00 17.23           H  
ATOM    936 HG23 THR A  63      15.425  34.918   7.431  1.00 17.23           H  
ATOM    937  N   LEU A  64      12.096  36.524   5.319  1.00 13.01           N  
ANISOU  937  N   LEU A  64     1442   1982   1517   -835    324   -649       N  
ATOM    938  CA  LEU A  64      10.982  37.215   5.955  1.00 12.94           C  
ANISOU  938  CA  LEU A  64     1541   1888   1487   -783    337   -611       C  
ATOM    939  C   LEU A  64       9.696  36.436   5.696  1.00 16.68           C  
ANISOU  939  C   LEU A  64     1988   2353   1996   -656    302   -558       C  
ATOM    940  O   LEU A  64       8.892  36.255   6.598  1.00 15.59           O  
ANISOU  940  O   LEU A  64     1853   2200   1871   -604    290   -548       O  
ATOM    941  CB  LEU A  64      10.852  38.637   5.394  1.00 13.67           C  
ANISOU  941  CB  LEU A  64     1775   1876   1542   -827    404   -596       C  
ATOM    942  CG  LEU A  64      11.999  39.605   5.747  1.00 14.96           C  
ANISOU  942  CG  LEU A  64     1989   2027   1668   -967    453   -652       C  
ATOM    943  CD1 LEU A  64      11.983  40.870   4.885  1.00 20.00           C  
ANISOU  943  CD1 LEU A  64     2771   2555   2272  -1024    514   -624       C  
ATOM    944  CD2 LEU A  64      11.950  40.017   7.225  1.00 14.79           C  
ANISOU  944  CD2 LEU A  64     1998   1987   1636   -995    455   -693       C  
ATOM    945  H   LEU A  64      12.354  36.887   4.584  1.00 15.61           H  
ATOM    946  HA  LEU A  64      11.130  37.268   6.912  1.00 15.53           H  
ATOM    947  HB2 LEU A  64      10.807  38.581   4.427  1.00 16.40           H  
ATOM    948  HB3 LEU A  64      10.030  39.025   5.733  1.00 16.40           H  
ATOM    949  HG  LEU A  64      12.844  39.154   5.594  1.00 17.95           H  
ATOM    950 HD11 LEU A  64      12.722  41.441   5.149  1.00 24.00           H  
ATOM    951 HD12 LEU A  64      12.075  40.618   3.953  1.00 24.00           H  
ATOM    952 HD13 LEU A  64      11.142  41.334   5.021  1.00 24.00           H  
ATOM    953 HD21 LEU A  64      12.685  40.624   7.407  1.00 17.75           H  
ATOM    954 HD22 LEU A  64      11.105  40.459   7.401  1.00 17.75           H  
ATOM    955 HD23 LEU A  64      12.031  39.224   7.776  1.00 17.75           H  
HETATM  956  N1  CRO A  66       9.558  35.883   4.493  1.00 15.01           N  
ANISOU  956  N1  CRO A  66     1743   2166   1795   -624    290   -536       N  
HETATM  957  CA1 CRO A  66       8.415  35.088   4.161  1.00 11.75           C  
ANISOU  957  CA1 CRO A  66     1294   1755   1414   -519    250   -494       C  
HETATM  958  CB1 CRO A  66       7.463  35.719   3.145  1.00 20.94           C  
ANISOU  958  CB1 CRO A  66     2544   2850   2563   -474    252   -435       C  
HETATM  959  CG1 CRO A  66       7.020  37.003   3.745  1.00 20.14           C  
ANISOU  959  CG1 CRO A  66     2543   2643   2466   -465    285   -420       C  
HETATM  960  OG1 CRO A  66       8.090  36.070   1.959  1.00 23.20           O  
ANISOU  960  OG1 CRO A  66     2880   3143   2792   -548    272   -430       O  
HETATM  961  C1  CRO A  66       8.935  33.796   3.598  1.00 13.40           C  
ANISOU  961  C1  CRO A  66     1390   2049   1655   -518    218   -521       C  
HETATM  962  N2  CRO A  66       9.097  33.444   2.308  1.00 13.42           N  
ANISOU  962  N2  CRO A  66     1377   2081   1642   -535    229   -531       N  
HETATM  963  N3  CRO A  66       9.410  32.737   4.460  1.00 12.57           N  
ANISOU  963  N3  CRO A  66     1174   1997   1605   -509    170   -548       N  
HETATM  964  C2  CRO A  66       9.878  31.658   3.627  1.00 11.07           C  
ANISOU  964  C2  CRO A  66      883   1858   1465   -503    155   -585       C  
HETATM  965  O2  CRO A  66      10.323  30.600   4.024  1.00 14.57           O  
ANISOU  965  O2  CRO A  66     1263   2307   1968   -451    105   -579       O  
HETATM  966  CA2 CRO A  66       9.656  32.127   2.274  1.00 16.54           C  
ANISOU  966  CA2 CRO A  66     1640   2544   2102   -526    204   -584       C  
HETATM  967  CA3 CRO A  66       9.464  32.756   5.911  1.00 11.12           C  
ANISOU  967  CA3 CRO A  66      990   1812   1423   -520    140   -542       C  
HETATM  968  C3  CRO A  66       8.291  32.084   6.521  1.00 13.28           C  
ANISOU  968  C3  CRO A  66     1257   2076   1715   -447    108   -500       C  
HETATM  969  O3  CRO A  66       8.450  31.672   7.724  1.00 15.33           O  
ANISOU  969  O3  CRO A  66     1500   2356   1970   -471     65   -492       O  
HETATM  970  CB2 CRO A  66      10.007  31.340   1.172  1.00 16.67           C  
ANISOU  970  CB2 CRO A  66     1593   2607   2132   -544    222   -635       C  
HETATM  971  CG2 CRO A  66      10.044  31.819  -0.262  1.00 17.45           C  
ANISOU  971  CG2 CRO A  66     1771   2719   2140   -615    278   -644       C  
HETATM  972  CD1 CRO A  66      10.584  30.944  -1.222  1.00 14.23           C  
ANISOU  972  CD1 CRO A  66     1287   2373   1746   -657    317   -729       C  
HETATM  973  CD2 CRO A  66       9.569  33.081  -0.639  1.00 13.27           C  
ANISOU  973  CD2 CRO A  66     1391   2134   1516   -646    291   -573       C  
HETATM  974  CE1 CRO A  66      10.643  31.305  -2.555  1.00 15.13           C  
ANISOU  974  CE1 CRO A  66     1485   2513   1751   -750    376   -744       C  
HETATM  975  CE2 CRO A  66       9.634  33.442  -2.011  1.00 19.49           C  
ANISOU  975  CE2 CRO A  66     2267   2937   2202   -732    328   -566       C  
HETATM  976  CZ  CRO A  66      10.149  32.562  -2.956  1.00 18.25           C  
ANISOU  976  CZ  CRO A  66     2047   2860   2029   -792    372   -650       C  
HETATM  977  OH  CRO A  66      10.206  32.877  -4.329  1.00 17.46           O  
ANISOU  977  OH  CRO A  66     2049   2787   1796   -904    415   -649       O  
ATOM    978  N   VAL A  68       7.075  32.229   5.948  1.00 10.19           N  
ANISOU  978  N   VAL A  68      899   1647   1326   -378    130   -470       N  
ATOM    979  CA  VAL A  68       5.863  31.742   6.599  1.00  9.98           C  
ANISOU  979  CA  VAL A  68      861   1610   1319   -320    120   -442       C  
ATOM    980  C   VAL A  68       5.145  30.766   5.656  1.00 13.64           C  
ANISOU  980  C   VAL A  68     1262   2090   1831   -253     86   -421       C  
ATOM    981  O   VAL A  68       4.012  30.963   5.226  1.00 12.40           O  
ANISOU  981  O   VAL A  68     1116   1906   1690   -195     95   -399       O  
ATOM    982  CB  VAL A  68       4.981  32.898   7.093  1.00 10.37           C  
ANISOU  982  CB  VAL A  68      993   1596   1353   -303    184   -444       C  
ATOM    983  CG1 VAL A  68       5.624  33.569   8.323  1.00 11.96           C  
ANISOU  983  CG1 VAL A  68     1251   1793   1499   -387    217   -480       C  
ATOM    984  CG2 VAL A  68       4.744  33.921   5.994  1.00 10.68           C  
ANISOU  984  CG2 VAL A  68     1090   1573   1397   -274    207   -430       C  
ATOM    985  HA  VAL A  68       6.127  31.235   7.382  1.00 11.97           H  
ATOM    986  HB  VAL A  68       4.120  32.543   7.362  1.00 12.45           H  
ATOM    987 HG11 VAL A  68       5.053  34.295   8.619  1.00 14.35           H  
ATOM    988 HG12 VAL A  68       5.716  32.911   9.029  1.00 14.35           H  
ATOM    989 HG13 VAL A  68       6.496  33.914   8.074  1.00 14.35           H  
ATOM    990 HG21 VAL A  68       4.185  34.633   6.342  1.00 12.82           H  
ATOM    991 HG22 VAL A  68       5.598  34.280   5.707  1.00 12.82           H  
ATOM    992 HG23 VAL A  68       4.300  33.486   5.249  1.00 12.82           H  
ATOM    993  N   GLN A  69       5.816  29.658   5.389  1.00 12.29           N  
ANISOU  993  N   GLN A  69     1632   1483   1554    326    -29    -93       N  
ATOM    994  CA  GLN A  69       5.346  28.717   4.388  1.00 13.14           C  
ANISOU  994  CA  GLN A  69     1715   1585   1693    266    -59    -56       C  
ATOM    995  C   GLN A  69       4.116  27.931   4.822  1.00 13.26           C  
ANISOU  995  C   GLN A  69     1695   1669   1675    206    -52     27       C  
ATOM    996  O   GLN A  69       3.524  27.214   4.013  1.00 12.64           O  
ANISOU  996  O   GLN A  69     1581   1597   1625    150    -80     57       O  
ATOM    997  CB  GLN A  69       6.489  27.803   3.976  1.00 12.19           C  
ANISOU  997  CB  GLN A  69     1621   1363   1648    235   -119   -116       C  
ATOM    998  CG  GLN A  69       7.620  28.604   3.339  1.00 11.35           C  
ANISOU  998  CG  GLN A  69     1518   1194   1601    256    -73   -238       C  
ATOM    999  CD  GLN A  69       8.851  27.775   3.024  1.00 16.17           C  
ANISOU  999  CD  GLN A  69     2095   1748   2302    199    -90   -305       C  
ATOM   1000  OE1 GLN A  69       9.346  27.034   3.859  1.00 20.76           O  
ANISOU 1000  OE1 GLN A  69     2654   2297   2936    220   -190   -309       O  
ATOM   1001  NE2 GLN A  69       9.365  27.923   1.811  1.00 24.02           N  
ANISOU 1001  NE2 GLN A  69     3101   2736   3289    131     -4   -344       N  
ATOM   1002  H   GLN A  69       6.549  29.427   5.775  1.00 14.74           H  
ATOM   1003  HA  GLN A  69       5.092  29.223   3.600  1.00 15.77           H  
ATOM   1004  HB2 GLN A  69       6.838  27.350   4.760  1.00 14.63           H  
ATOM   1005  HB3 GLN A  69       6.168  27.157   3.328  1.00 14.63           H  
ATOM   1006  HG2 GLN A  69       7.301  28.990   2.509  1.00 13.62           H  
ATOM   1007  HG3 GLN A  69       7.886  29.310   3.950  1.00 13.62           H  
ATOM   1008 HE21 GLN A  69       9.000  28.467   1.253  1.00 28.82           H  
ATOM   1009 HE22 GLN A  69      10.062  27.475   1.581  1.00 28.82           H  
ATOM   1010  N   CYS A  70       3.719  28.103   6.083  1.00 10.41           N  
ANISOU 1010  N   CYS A  70     1352   1357   1247    196      3     49       N  
ATOM   1011  CA  CYS A  70       2.432  27.630   6.570  1.00 14.00           C  
ANISOU 1011  CA  CYS A  70     1759   1891   1671    112     80     92       C  
ATOM   1012  C   CYS A  70       1.252  28.276   5.864  1.00  9.11           C  
ANISOU 1012  C   CYS A  70      971   1350   1141    147    124     64       C  
ATOM   1013  O   CYS A  70       0.135  27.801   6.019  1.00 11.91           O  
ANISOU 1013  O   CYS A  70     1226   1769   1530     70    184     67       O  
ATOM   1014  CB  CYS A  70       2.313  27.849   8.094  1.00 15.60           C  
ANISOU 1014  CB  CYS A  70     2053   2122   1754     67    173     91       C  
ATOM   1015  SG  CYS A  70       2.800  29.481   8.660  1.00 15.97           S  
ANISOU 1015  SG  CYS A  70     2107   2184   1778    186    227     11       S  
ATOM   1016  H   CYS A  70       4.189  28.500   6.683  1.00 12.50           H  
ATOM   1017  HA  CYS A  70       2.377  26.675   6.409  1.00 16.80           H  
ATOM   1018  HB2 CYS A  70       1.389  27.712   8.355  1.00 18.72           H  
ATOM   1019  HB3 CYS A  70       2.878  27.202   8.544  1.00 18.72           H  
ATOM   1020  HG  CYS A  70       2.103  30.302   8.132  1.00 19.16           H  
ATOM   1021  N   PHE A  71       1.481  29.337   5.071  1.00 10.37           N  
ANISOU 1021  N   PHE A  71     1103   1487   1350    256     79     28       N  
ATOM   1022  CA  PHE A  71       0.401  29.957   4.318  1.00 12.93           C  
ANISOU 1022  CA  PHE A  71     1296   1844   1775    313     43      7       C  
ATOM   1023  C   PHE A  71       0.272  29.449   2.880  1.00 12.62           C  
ANISOU 1023  C   PHE A  71     1272   1758   1763    286    -93     41       C  
ATOM   1024  O   PHE A  71      -0.531  29.956   2.137  1.00 12.90           O  
ANISOU 1024  O   PHE A  71     1237   1789   1874    339   -188     31       O  
ATOM   1025  CB  PHE A  71       0.511  31.479   4.346  1.00 11.83           C  
ANISOU 1025  CB  PHE A  71     1157   1678   1660    442     47    -43       C  
ATOM   1026  CG  PHE A  71       0.137  32.054   5.677  1.00 13.19           C  
ANISOU 1026  CG  PHE A  71     1265   1912   1836    467    190   -105       C  
ATOM   1027  CD1 PHE A  71      -1.195  32.151   6.045  1.00 11.82           C  
ANISOU 1027  CD1 PHE A  71      899   1815   1780    470    266   -169       C  
ATOM   1028  CD2 PHE A  71       1.113  32.459   6.573  1.00 12.90           C  
ANISOU 1028  CD2 PHE A  71     1353   1854   1695    473    257   -122       C  
ATOM   1029  CE1 PHE A  71      -1.558  32.647   7.317  1.00 16.89           C  
ANISOU 1029  CE1 PHE A  71     1490   2514   2414    461    450   -258       C  
ATOM   1030  CE2 PHE A  71       0.754  32.957   7.845  1.00 12.87           C  
ANISOU 1030  CE2 PHE A  71     1329   1903   1659    470    403   -188       C  
ATOM   1031  CZ  PHE A  71      -0.574  33.053   8.195  1.00 12.91           C  
ANISOU 1031  CZ  PHE A  71     1159   1984   1761    458    517   -259       C  
ATOM   1032  H   PHE A  71       2.249  29.707   4.959  1.00 12.44           H  
ATOM   1033  HA  PHE A  71      -0.431  29.732   4.764  1.00 15.52           H  
ATOM   1034  HB2 PHE A  71       1.427  31.734   4.154  1.00 14.20           H  
ATOM   1035  HB3 PHE A  71      -0.085  31.852   3.678  1.00 14.20           H  
ATOM   1036  HD1 PHE A  71      -1.857  31.870   5.455  1.00 14.19           H  
ATOM   1037  HD2 PHE A  71       2.011  32.388   6.342  1.00 15.48           H  
ATOM   1038  HE1 PHE A  71      -2.455  32.717   7.553  1.00 20.27           H  
ATOM   1039  HE2 PHE A  71       1.413  33.235   8.440  1.00 15.45           H  
ATOM   1040  HZ  PHE A  71      -0.810  33.393   9.028  1.00 15.49           H  
ATOM   1041  N   ALA A  72       1.037  28.433   2.529  1.00 12.02           N  
ANISOU 1041  N   ALA A  72     1297   1635   1634    203   -116     69       N  
ATOM   1042  CA  ALA A  72       0.934  27.821   1.217  1.00 13.08           C  
ANISOU 1042  CA  ALA A  72     1473   1724   1772    147   -218     86       C  
ATOM   1043  C   ALA A  72      -0.451  27.211   1.042  1.00 10.21           C  
ANISOU 1043  C   ALA A  72      966   1426   1487     95   -270    103       C  
ATOM   1044  O   ALA A  72      -1.073  26.723   1.999  1.00 10.96           O  
ANISOU 1044  O   ALA A  72      952   1592   1620     44   -182    102       O  
ATOM   1045  CB  ALA A  72       1.974  26.767   1.075  1.00 11.54           C  
ANISOU 1045  CB  ALA A  72     1378   1463   1542     70   -205     80       C  
ATOM   1046  H   ALA A  72       1.631  28.075   3.037  1.00 14.42           H  
ATOM   1047  HA  ALA A  72       1.070  28.491   0.529  1.00 15.69           H  
ATOM   1048  HB1 ALA A  72       1.897  26.365   0.196  1.00 13.84           H  
ATOM   1049  HB2 ALA A  72       2.850  27.172   1.178  1.00 13.84           H  
ATOM   1050  HB3 ALA A  72       1.838  26.095   1.760  1.00 13.84           H  
ATOM   1051  N   ARG A  73      -0.953  27.258  -0.180  1.00 10.91           N  
ANISOU 1051  N   ARG A  73     1067   1483   1596     91   -412    108       N  
ATOM   1052  CA  ARG A  73      -2.189  26.554  -0.498  1.00 11.72           C  
ANISOU 1052  CA  ARG A  73     1022   1635   1796     29   -495    105       C  
ATOM   1053  C   ARG A  73      -1.826  25.125  -0.848  1.00 16.71           C  
ANISOU 1053  C   ARG A  73     1738   2236   2375   -111   -487    130       C  
ATOM   1054  O   ARG A  73      -1.149  24.904  -1.844  1.00 13.70           O  
ANISOU 1054  O   ARG A  73     1522   1772   1910   -145   -549    132       O  
ATOM   1055  CB  ARG A  73      -2.933  27.177  -1.691  1.00 13.20           C  
ANISOU 1055  CB  ARG A  73     1205   1779   2030     86   -716     99       C  
ATOM   1056  CG  ARG A  73      -4.275  26.505  -1.910  1.00 14.78           C  
ANISOU 1056  CG  ARG A  73     1196   2037   2381     31   -821     67       C  
ATOM   1057  CD  ARG A  73      -5.063  27.138  -3.049  1.00 29.85           C  
ANISOU 1057  CD  ARG A  73     3131   3883   4329    102  -1057     53       C  
ATOM   1058  NE  ARG A  73      -4.515  26.749  -4.334  1.00 34.37           N  
ANISOU 1058  NE  ARG A  73     3977   4352   4729     20  -1174    102       N  
ATOM   1059  CZ  ARG A  73      -4.893  25.673  -5.029  1.00 37.81           C  
ANISOU 1059  CZ  ARG A  73     4434   4783   5149    -98  -1240    100       C  
ATOM   1060  NH1 ARG A  73      -5.829  24.852  -4.566  1.00 30.15           N  
ANISOU 1060  NH1 ARG A  73     3223   3906   4328   -154  -1209     56       N  
ATOM   1061  NH2 ARG A  73      -4.322  25.420  -6.201  1.00 43.91           N  
ANISOU 1061  NH2 ARG A  73     5484   5451   5747   -178  -1311    129       N  
ATOM   1062  H   ARG A  73      -0.604  27.685  -0.840  1.00 13.09           H  
ATOM   1063  HA  ARG A  73      -2.777  26.551   0.273  1.00 14.06           H  
ATOM   1064  HB2 ARG A  73      -3.087  28.118  -1.517  1.00 15.84           H  
ATOM   1065  HB3 ARG A  73      -2.401  27.065  -2.495  1.00 15.84           H  
ATOM   1066  HG2 ARG A  73      -4.131  25.571  -2.127  1.00 17.73           H  
ATOM   1067  HG3 ARG A  73      -4.804  26.582  -1.100  1.00 17.73           H  
ATOM   1068  HD2 ARG A  73      -5.985  26.841  -3.007  1.00 35.82           H  
ATOM   1069  HD3 ARG A  73      -5.015  28.104  -2.976  1.00 35.82           H  
ATOM   1070  HE  ARG A  73      -3.901  27.247  -4.673  1.00 41.24           H  
ATOM   1071 HH11 ARG A  73      -6.204  25.011  -3.808  1.00 36.19           H  
ATOM   1072 HH12 ARG A  73      -6.061  24.162  -5.024  1.00 36.19           H  
ATOM   1073 HH21 ARG A  73      -3.714  25.947  -6.506  1.00 52.69           H  
ATOM   1074 HH22 ARG A  73      -4.558  24.728  -6.653  1.00 52.69           H  
ATOM   1075  N   TYR A  74      -2.256  24.179  -0.016  1.00 13.43           N  
ANISOU 1075  N   TYR A  74     1230   1872   2001   -204   -394    138       N  
ATOM   1076  CA  TYR A  74      -2.182  22.762  -0.337  1.00 12.00           C  
ANISOU 1076  CA  TYR A  74     1110   1648   1801   -341   -410    159       C  
ATOM   1077  C   TYR A  74      -3.540  22.325  -0.915  1.00 13.66           C  
ANISOU 1077  C   TYR A  74     1163   1909   2119   -420   -504    134       C  
ATOM   1078  O   TYR A  74      -4.567  22.464  -0.255  1.00 14.95           O  
ANISOU 1078  O   TYR A  74     1123   2160   2396   -442   -443     97       O  
ATOM   1079  CB  TYR A  74      -1.790  21.940   0.912  1.00 14.73           C  
ANISOU 1079  CB  TYR A  74     1510   1979   2108   -417   -279    193       C  
ATOM   1080  CG  TYR A  74      -0.289  21.869   1.113  1.00 12.58           C  
ANISOU 1080  CG  TYR A  74     1412   1606   1762   -361   -274    201       C  
ATOM   1081  CD1 TYR A  74       0.416  22.956   1.615  1.00 12.58           C  
ANISOU 1081  CD1 TYR A  74     1437   1612   1729   -244   -234    185       C  
ATOM   1082  CD2 TYR A  74       0.416  20.719   0.805  1.00 11.06           C  
ANISOU 1082  CD2 TYR A  74     1336   1302   1566   -422   -318    203       C  
ATOM   1083  CE1 TYR A  74       1.780  22.903   1.800  1.00 11.28           C  
ANISOU 1083  CE1 TYR A  74     1389   1355   1543   -194   -242    162       C  
ATOM   1084  CE2 TYR A  74       1.804  20.642   1.009  1.00 12.46           C  
ANISOU 1084  CE2 TYR A  74     1621   1373   1739   -356   -330    171       C  
ATOM   1085  CZ  TYR A  74       2.482  21.744   1.471  1.00 10.67           C  
ANISOU 1085  CZ  TYR A  74     1395   1164   1494   -245   -296    146       C  
ATOM   1086  OH  TYR A  74       3.843  21.716   1.639  1.00 11.45           O  
ANISOU 1086  OH  TYR A  74     1558   1161   1632   -179   -320     84       O  
ATOM   1087  H   TYR A  74      -2.601  24.340   0.755  1.00 16.12           H  
ATOM   1088  HA  TYR A  74      -1.504  22.623  -1.016  1.00 14.40           H  
ATOM   1089  HB2 TYR A  74      -2.179  22.354   1.698  1.00 17.68           H  
ATOM   1090  HB3 TYR A  74      -2.124  21.035   0.813  1.00 17.68           H  
ATOM   1091  HD1 TYR A  74      -0.041  23.739   1.822  1.00 15.09           H  
ATOM   1092  HD2 TYR A  74      -0.040  19.978   0.477  1.00 13.28           H  
ATOM   1093  HE1 TYR A  74       2.235  23.648   2.121  1.00 13.54           H  
ATOM   1094  HE2 TYR A  74       2.269  19.870   0.777  1.00 14.95           H  
ATOM   1095  HH  TYR A  74       4.111  22.453   1.942  1.00 13.74           H  
ATOM   1096  N   PRO A  75      -3.561  21.845  -2.177  1.00 13.82           N  
ANISOU 1096  N   PRO A  75     1267   1871   2114   -470   -652    131       N  
ATOM   1097  CA  PRO A  75      -4.780  21.283  -2.745  1.00 15.59           C  
ANISOU 1097  CA  PRO A  75     1350   2129   2445   -561   -773    100       C  
ATOM   1098  C   PRO A  75      -5.287  20.132  -1.881  1.00 16.35           C  
ANISOU 1098  C   PRO A  75     1345   2263   2605   -714   -634     97       C  
ATOM   1099  O   PRO A  75      -4.480  19.499  -1.184  1.00 15.42           O  
ANISOU 1099  O   PRO A  75     1366   2093   2398   -764   -505    143       O  
ATOM   1100  CB  PRO A  75      -4.322  20.721  -4.087  1.00 17.02           C  
ANISOU 1100  CB  PRO A  75     1739   2211   2515   -618   -898    102       C  
ATOM   1101  CG  PRO A  75      -3.099  21.492  -4.430  1.00 21.21           C  
ANISOU 1101  CG  PRO A  75     2476   2671   2911   -537   -879    116       C  
ATOM   1102  CD  PRO A  75      -2.437  21.783  -3.133  1.00 17.27           C  
ANISOU 1102  CD  PRO A  75     1939   2201   2422   -468   -697    133       C  
ATOM   1103  HA  PRO A  75      -5.468  21.957  -2.868  1.00 18.71           H  
ATOM   1104  HB2 PRO A  75      -4.118  19.777  -3.993  1.00 20.42           H  
ATOM   1105  HB3 PRO A  75      -5.014  20.859  -4.753  1.00 20.42           H  
ATOM   1106  HG2 PRO A  75      -2.522  20.955  -4.996  1.00 25.45           H  
ATOM   1107  HG3 PRO A  75      -3.347  22.315  -4.879  1.00 25.45           H  
ATOM   1108  HD2 PRO A  75      -1.830  21.064  -2.895  1.00 20.72           H  
ATOM   1109  HD3 PRO A  75      -1.979  22.637  -3.172  1.00 20.72           H  
ATOM   1110  N   ASP A  76      -6.581  19.848  -1.980  1.00 18.34           N  
ANISOU 1110  N   ASP A  76     1393   2580   2995   -779   -662     28       N  
ATOM   1111  CA  ASP A  76      -7.213  18.840  -1.134  1.00 23.18           C  
ANISOU 1111  CA  ASP A  76     1914   3226   3666   -951   -492      2       C  
ATOM   1112  C   ASP A  76      -6.496  17.502  -1.176  1.00 21.44           C  
ANISOU 1112  C   ASP A  76     1930   2892   3324  -1065   -451     66       C  
ATOM   1113  O   ASP A  76      -6.326  16.871  -0.134  1.00 20.69           O  
ANISOU 1113  O   ASP A  76     1910   2768   3184  -1171   -292    109       O  
ATOM   1114  CB  ASP A  76      -8.662  18.620  -1.547  1.00 29.75           C  
ANISOU 1114  CB  ASP A  76     2518   4137   4647  -1004   -537   -123       C  
ATOM   1115  CG  ASP A  76      -9.559  19.796  -1.208  1.00 35.46           C  
ANISOU 1115  CG  ASP A  76     2991   4980   5503   -898   -538   -187       C  
ATOM   1116  OD1 ASP A  76      -9.146  20.700  -0.452  1.00 34.35           O  
ANISOU 1116  OD1 ASP A  76     2831   4856   5366   -800   -444   -172       O  
ATOM   1117  OD2 ASP A  76     -10.699  19.795  -1.693  1.00 37.76           O  
ANISOU 1117  OD2 ASP A  76     3110   5320   5918   -897   -635   -257       O  
ATOM   1118  H   ASP A  76      -7.119  20.227  -2.533  1.00 22.01           H  
ATOM   1119  HA  ASP A  76      -7.208  19.152  -0.216  1.00 27.81           H  
ATOM   1120  HB2 ASP A  76      -8.700  18.481  -2.506  1.00 35.70           H  
ATOM   1121  HB3 ASP A  76      -9.006  17.839  -1.085  1.00 35.70           H  
ATOM   1122  N   HIS A  77      -6.068  17.060  -2.356  1.00 18.60           N  
ANISOU 1122  N   HIS A  77     1716   2452   2898  -1038   -586     68       N  
ATOM   1123  CA  HIS A  77      -5.412  15.752  -2.459  1.00 22.42           C  
ANISOU 1123  CA  HIS A  77     2400   2817   3301  -1113   -546     98       C  
ATOM   1124  C   HIS A  77      -3.995  15.726  -1.854  1.00 23.74           C  
ANISOU 1124  C   HIS A  77     2755   2894   3371  -1057   -490    162       C  
ATOM   1125  O   HIS A  77      -3.372  14.666  -1.770  1.00 22.02           O  
ANISOU 1125  O   HIS A  77     2689   2562   3115  -1083   -468    176       O  
ATOM   1126  CB  HIS A  77      -5.370  15.242  -3.912  1.00 19.50           C  
ANISOU 1126  CB  HIS A  77     2123   2390   2894  -1108   -672     55       C  
ATOM   1127  CG  HIS A  77      -4.336  15.915  -4.756  1.00 17.38           C  
ANISOU 1127  CG  HIS A  77     2008   2073   2523  -1003   -739     58       C  
ATOM   1128  ND1 HIS A  77      -4.491  17.198  -5.245  1.00 20.69           N  
ANISOU 1128  ND1 HIS A  77     2395   2541   2925   -914   -843     55       N  
ATOM   1129  CD2 HIS A  77      -3.145  15.476  -5.228  1.00 20.53           C  
ANISOU 1129  CD2 HIS A  77     2592   2368   2839   -977   -702     42       C  
ATOM   1130  CE1 HIS A  77      -3.416  17.538  -5.934  1.00 19.97           C  
ANISOU 1130  CE1 HIS A  77     2494   2376   2718   -868   -848     49       C  
ATOM   1131  NE2 HIS A  77      -2.595  16.505  -5.960  1.00 19.57           N  
ANISOU 1131  NE2 HIS A  77     2555   2242   2639   -905   -749     26       N  
ATOM   1132  H   HIS A  77      -6.142  17.485  -3.100  1.00 22.31           H  
ATOM   1133  HA  HIS A  77      -5.943  15.116  -1.954  1.00 26.90           H  
ATOM   1134  HB2 HIS A  77      -5.174  14.292  -3.905  1.00 23.40           H  
ATOM   1135  HB3 HIS A  77      -6.235  15.396  -4.323  1.00 23.40           H  
ATOM   1136  HD1 HIS A  77      -5.161  17.713  -5.084  1.00 24.83           H  
ATOM   1137  HD2 HIS A  77      -2.763  14.643  -5.073  1.00 24.63           H  
ATOM   1138  HE1 HIS A  77      -3.283  18.349  -6.368  1.00 23.96           H  
ATOM   1139  HE2 HIS A  77      -1.834  16.482  -6.360  1.00 23.49           H  
ATOM   1140  N   MET A  78      -3.487  16.879  -1.431  1.00 16.94           N  
ANISOU 1140  N   MET A  78     1871   2072   2492   -967   -483    187       N  
ATOM   1141  CA  MET A  78      -2.146  16.955  -0.875  1.00 16.44           C  
ANISOU 1141  CA  MET A  78     1963   1917   2366   -900   -452    221       C  
ATOM   1142  C   MET A  78      -2.149  17.390   0.583  1.00 16.72           C  
ANISOU 1142  C   MET A  78     1987   1997   2367   -878   -335    270       C  
ATOM   1143  O   MET A  78      -1.101  17.614   1.153  1.00 18.09           O  
ANISOU 1143  O   MET A  78     2278   2105   2491   -788   -326    289       O  
ATOM   1144  CB  MET A  78      -1.311  17.947  -1.669  1.00 14.85           C  
ANISOU 1144  CB  MET A  78     1805   1709   2131   -757   -498    176       C  
ATOM   1145  CG  MET A  78      -0.963  17.507  -3.056  1.00 20.35           C  
ANISOU 1145  CG  MET A  78     2600   2334   2799   -773   -560    111       C  
ATOM   1146  SD  MET A  78       0.108  18.703  -3.881  1.00 15.79           S  
ANISOU 1146  SD  MET A  78     2128   1723   2150   -679   -565     49       S  
ATOM   1147  CE  MET A  78       1.585  18.658  -2.845  1.00 15.12           C  
ANISOU 1147  CE  MET A  78     2083   1552   2108   -590   -466     22       C  
ATOM   1148  H   MET A  78      -3.901  17.632  -1.456  1.00 20.32           H  
ATOM   1149  HA  MET A  78      -1.724  16.084  -0.944  1.00 19.72           H  
ATOM   1150  HB2 MET A  78      -1.806  18.779  -1.740  1.00 17.83           H  
ATOM   1151  HB3 MET A  78      -0.480  18.103  -1.193  1.00 17.83           H  
ATOM   1152  HG2 MET A  78      -0.495  16.659  -3.015  1.00 24.42           H  
ATOM   1153  HG3 MET A  78      -1.776  17.418  -3.577  1.00 24.42           H  
ATOM   1154  HE1 MET A  78       2.241  19.277  -3.204  1.00 18.14           H  
ATOM   1155  HE2 MET A  78       1.345  18.918  -1.942  1.00 18.14           H  
ATOM   1156  HE3 MET A  78       1.944  17.757  -2.846  1.00 18.14           H  
ATOM   1157  N   LYS A  79      -3.312  17.473   1.202  1.00 16.61           N  
ANISOU 1157  N   LYS A  79     1838   2086   2388   -975   -239    270       N  
ATOM   1158  CA  LYS A  79      -3.364  17.997   2.564  1.00 17.84           C  
ANISOU 1158  CA  LYS A  79     2006   2290   2484   -975    -95    294       C  
ATOM   1159  C   LYS A  79      -2.572  17.170   3.586  1.00 24.08           C  
ANISOU 1159  C   LYS A  79     3059   2944   3149  -1046    -72    378       C  
ATOM   1160  O   LYS A  79      -2.105  17.718   4.584  1.00 19.78           O  
ANISOU 1160  O   LYS A  79     2608   2396   2511   -997    -17    405       O  
ATOM   1161  CB  LYS A  79      -4.811  18.281   2.993  1.00 20.20           C  
ANISOU 1161  CB  LYS A  79     2079   2727   2871  -1085     47    231       C  
ATOM   1162  CG  LYS A  79      -5.276  19.619   2.349  1.00 28.48           C  
ANISOU 1162  CG  LYS A  79     2891   3886   4044   -917    -16    148       C  
ATOM   1163  CD  LYS A  79      -6.645  20.077   2.745  1.00 37.12           C  
ANISOU 1163  CD  LYS A  79     3698   5108   5297   -974    105     36       C  
ATOM   1164  CE  LYS A  79      -7.063  21.286   1.911  1.00 33.14           C  
ANISOU 1164  CE  LYS A  79     2985   4661   4947   -780    -50    -40       C  
ATOM   1165  NZ  LYS A  79      -6.130  22.420   2.003  1.00 36.28           N  
ANISOU 1165  NZ  LYS A  79     3497   5033   5254   -585    -84     -4       N  
ATOM   1166  H   LYS A  79      -4.071  17.240   0.871  1.00 19.94           H  
ATOM   1167  HA  LYS A  79      -2.927  18.862   2.541  1.00 21.41           H  
ATOM   1168  HB2 LYS A  79      -5.391  17.568   2.684  1.00 24.24           H  
ATOM   1169  HB3 LYS A  79      -4.856  18.368   3.959  1.00 24.24           H  
ATOM   1170  HG2 LYS A  79      -4.651  20.316   2.602  1.00 34.18           H  
ATOM   1171  HG3 LYS A  79      -5.271  19.514   1.385  1.00 34.18           H  
ATOM   1172  HD2 LYS A  79      -7.283  19.362   2.591  1.00 44.54           H  
ATOM   1173  HD3 LYS A  79      -6.642  20.335   3.680  1.00 44.54           H  
ATOM   1174  HE2 LYS A  79      -7.116  21.020   0.979  1.00 39.77           H  
ATOM   1175  HE3 LYS A  79      -7.932  21.591   2.215  1.00 39.77           H  
ATOM   1176  HZ1 LYS A  79      -5.324  22.174   1.720  1.00 43.54           H  
ATOM   1177  HZ2 LYS A  79      -6.421  23.095   1.500  1.00 43.54           H  
ATOM   1178  HZ3 LYS A  79      -6.069  22.695   2.848  1.00 43.54           H  
ATOM   1179  N  AGLN A  80      -2.390  15.877   3.324  0.62 16.50           N  
ANISOU 1179  N  AGLN A  80     2235   1849   2184  -1152   -145    416       N  
ATOM   1180  N  BGLN A  80      -2.383  15.879   3.329  0.38 16.69           N  
ANISOU 1180  N  BGLN A  80     2261   1873   2208  -1151   -145    416       N  
ATOM   1181  CA AGLN A  80      -1.595  15.040   4.225  0.62 17.11           C  
ANISOU 1181  CA AGLN A  80     2579   1765   2157  -1152   -187    481       C  
ATOM   1182  CA BGLN A  80      -1.592  15.051   4.241  0.38 17.11           C  
ANISOU 1182  CA BGLN A  80     2581   1765   2155  -1152   -186    482       C  
ATOM   1183  C  AGLN A  80      -0.083  15.347   4.194  0.62 16.76           C  
ANISOU 1183  C  AGLN A  80     2643   1603   2122   -974   -336    484       C  
ATOM   1184  C  BGLN A  80      -0.072  15.229   4.082  0.38 16.95           C  
ANISOU 1184  C  BGLN A  80     2665   1619   2156   -972   -346    479       C  
ATOM   1185  O  AGLN A  80       0.680  14.828   5.015  0.62 16.38           O  
ANISOU 1185  O  AGLN A  80     2788   1428   2009   -931   -421    520       O  
ATOM   1186  O  BGLN A  80       0.709  14.498   4.700  0.38 18.04           O  
ANISOU 1186  O  BGLN A  80     2988   1614   2250   -928   -445    506       O  
ATOM   1187  CB AGLN A  80      -1.866  13.550   3.971  0.62 24.38           C  
ANISOU 1187  CB AGLN A  80     3591   2585   3085  -1234   -223    485       C  
ATOM   1188  CB BGLN A  80      -1.980  13.576   4.105  0.38 23.30           C  
ANISOU 1188  CB BGLN A  80     3456   2458   2938  -1251   -204    489       C  
ATOM   1189  CG AGLN A  80      -1.337  12.996   2.657  0.62 22.96           C  
ANISOU 1189  CG AGLN A  80     3374   2338   3010  -1144   -348    425       C  
ATOM   1190  CG BGLN A  80      -3.416  13.267   4.514  0.38 24.73           C  
ANISOU 1190  CG BGLN A  80     3558   2732   3107  -1440    -30    476       C  
ATOM   1191  CD AGLN A  80      -2.379  12.994   1.562  0.62 29.04           C  
ANISOU 1191  CD AGLN A  80     3955   3218   3862  -1207   -312    361       C  
ATOM   1192  CD BGLN A  80      -3.749  13.712   5.931  0.38 22.49           C  
ANISOU 1192  CD BGLN A  80     3363   2492   2690  -1527    128    505       C  
ATOM   1193  OE1AGLN A  80      -2.976  14.029   1.243  0.62 17.39           O  
ANISOU 1193  OE1AGLN A  80     2299   1883   2427  -1200   -277    328       O  
ATOM   1194  OE1BGLN A  80      -3.248  13.151   6.902  0.38 23.15           O  
ANISOU 1194  OE1BGLN A  80     3715   2456   2623  -1558     96    571       O  
ATOM   1195  NE2AGLN A  80      -2.625  11.815   0.996  0.62 26.02           N  
ANISOU 1195  NE2AGLN A  80     3612   2764   3510  -1264   -342    337       N  
ATOM   1196  NE2BGLN A  80      -4.606  14.721   6.050  0.38 22.13           N  
ANISOU 1196  NE2BGLN A  80     3092   2616   2702  -1558    288    436       N  
ATOM   1197  H  AGLN A  80      -2.711  15.464   2.641  0.62 19.80           H  
ATOM   1198  H  BGLN A  80      -2.695  15.462   2.644  0.38 20.03           H  
ATOM   1199  HA AGLN A  80      -1.893  15.224   5.129  0.62 20.53           H  
ATOM   1200  HA BGLN A  80      -1.811  15.317   5.147  0.38 20.53           H  
ATOM   1201  HB2AGLN A  80      -1.457  13.039   4.687  0.62 29.25           H  
ATOM   1202  HB2BGLN A  80      -1.873  13.310   3.178  0.38 27.96           H  
ATOM   1203  HB3AGLN A  80      -2.826  13.408   3.981  0.62 29.25           H  
ATOM   1204  HB3BGLN A  80      -1.393  13.046   4.667  0.38 27.96           H  
ATOM   1205  HG2AGLN A  80      -0.592  13.542   2.361  0.62 27.55           H  
ATOM   1206  HG2BGLN A  80      -4.020  13.725   3.908  0.38 29.68           H  
ATOM   1207  HG3AGLN A  80      -1.045  12.081   2.795  0.62 27.55           H  
ATOM   1208  HG3BGLN A  80      -3.559  12.309   4.461  0.38 29.68           H  
ATOM   1209 HE21AGLN A  80      -2.200  11.115   1.259  0.62 31.22           H  
ATOM   1210 HE21BGLN A  80      -4.941  15.087   5.348  0.38 26.56           H  
ATOM   1211 HE22AGLN A  80      -3.208  11.754   0.367  0.62 31.22           H  
ATOM   1212 HE22BGLN A  80      -4.826  15.009   6.831  0.38 26.56           H  
ATOM   1213  N   HIS A  81       0.344  16.205   3.277  1.00 14.23           N  
ANISOU 1213  N   HIS A  81     2178   1343   1886   -837   -367    411       N  
ATOM   1214  CA  HIS A  81       1.766  16.519   3.098  1.00 17.52           C  
ANISOU 1214  CA  HIS A  81     2640   1663   2353   -666   -470    357       C  
ATOM   1215  C   HIS A  81       2.151  17.916   3.567  1.00 13.09           C  
ANISOU 1215  C   HIS A  81     2018   1199   1756   -538   -421    335       C  
ATOM   1216  O   HIS A  81       3.254  18.400   3.253  1.00 13.89           O  
ANISOU 1216  O   HIS A  81     2103   1253   1922   -405   -474    259       O  
ATOM   1217  CB  HIS A  81       2.139  16.368   1.625  1.00 18.27           C  
ANISOU 1217  CB  HIS A  81     2656   1733   2553   -624   -506    255       C  
ATOM   1218  CG  HIS A  81       1.805  15.017   1.094  1.00 17.56           C  
ANISOU 1218  CG  HIS A  81     2601   1589   2483   -694   -524    243       C  
ATOM   1219  ND1 HIS A  81       2.565  13.913   1.395  1.00 16.64           N  
ANISOU 1219  ND1 HIS A  81     2591   1330   2401   -650   -598    230       N  
ATOM   1220  CD2 HIS A  81       0.758  14.569   0.361  1.00 16.40           C  
ANISOU 1220  CD2 HIS A  81     2393   1508   2330   -800   -488    239       C  
ATOM   1221  CE1 HIS A  81       2.024  12.843   0.843  1.00 18.74           C  
ANISOU 1221  CE1 HIS A  81     2873   1570   2678   -733   -590    223       C  
ATOM   1222  NE2 HIS A  81       0.925  13.214   0.208  1.00 18.27           N  
ANISOU 1222  NE2 HIS A  81     2715   1637   2592   -826   -521    225       N  
ATOM   1223  H  AHIS A  81      -0.174  16.628   2.736  0.62 17.08           H  
ATOM   1224  H  BHIS A  81      -0.182  16.707   2.818  0.38 17.08           H  
ATOM   1225  HA  HIS A  81       2.292  15.881   3.605  1.00 21.02           H  
ATOM   1226  HB2 HIS A  81       1.651  17.025   1.105  1.00 21.92           H  
ATOM   1227  HB3 HIS A  81       3.094  16.504   1.524  1.00 21.92           H  
ATOM   1228  HD1 HIS A  81       3.287  13.920   1.863  1.00 19.97           H  
ATOM   1229  HD2 HIS A  81       0.065  15.084   0.015  1.00 19.68           H  
ATOM   1230  HE1 HIS A  81       2.362  11.977   0.888  1.00 22.49           H  
ATOM   1231  HE2 HIS A  81       0.403  12.693  -0.234  1.00 21.93           H  
ATOM   1232  N   ASP A  82       1.246  18.575   4.291  1.00 14.39           N  
ANISOU 1232  N   ASP A  82     2282   1323   1862    145   -529    197       N  
ATOM   1233  CA  ASP A  82       1.485  19.938   4.749  1.00 10.38           C  
ANISOU 1233  CA  ASP A  82     1704    900   1340     70   -433    162       C  
ATOM   1234  C   ASP A  82       2.092  19.909   6.152  1.00 16.82           C  
ANISOU 1234  C   ASP A  82     2500   1787   2102    104   -457    139       C  
ATOM   1235  O   ASP A  82       1.380  20.000   7.151  1.00 15.17           O  
ANISOU 1235  O   ASP A  82     2330   1549   1885     67   -445    211       O  
ATOM   1236  CB  ASP A  82       0.159  20.738   4.710  1.00 10.45           C  
ANISOU 1236  CB  ASP A  82     1737    831   1402    -36   -356    252       C  
ATOM   1237  CG  ASP A  82       0.329  22.222   5.021  1.00 11.30           C  
ANISOU 1237  CG  ASP A  82     1771   1007   1515   -119   -254    210       C  
ATOM   1238  OD1 ASP A  82       1.415  22.660   5.496  1.00 13.98           O  
ANISOU 1238  OD1 ASP A  82     2046   1458   1806   -102   -240    121       O  
ATOM   1239  OD2 ASP A  82      -0.663  22.969   4.794  1.00 13.14           O  
ANISOU 1239  OD2 ASP A  82     2008   1175   1810   -203   -191    269       O  
ATOM   1240  H   ASP A  82       0.486  18.253   4.530  1.00 17.26           H  
ATOM   1241  HA  ASP A  82       2.118  20.369   4.153  1.00 12.46           H  
ATOM   1242  HB2 ASP A  82      -0.226  20.663   3.823  1.00 12.54           H  
ATOM   1243  HB3 ASP A  82      -0.450  20.365   5.366  1.00 12.54           H  
ATOM   1244  N   PHE A  83       3.412  19.755   6.218  1.00 13.48           N  
ANISOU 1244  N   PHE A  83     2016   1463   1641    170   -494     40       N  
ATOM   1245  CA  PHE A  83       4.117  19.760   7.496  1.00 12.00           C  
ANISOU 1245  CA  PHE A  83     1804   1355   1399    199   -527     14       C  
ATOM   1246  C   PHE A  83       3.884  21.049   8.262  1.00 13.61           C  
ANISOU 1246  C   PHE A  83     1977   1612   1584    102   -430     12       C  
ATOM   1247  O   PHE A  83       3.660  21.043   9.488  1.00 16.89           O  
ANISOU 1247  O   PHE A  83     2421   2040   1958     84   -441     51       O  
ATOM   1248  CB  PHE A  83       5.609  19.596   7.264  1.00 12.68           C  
ANISOU 1248  CB  PHE A  83     1808   1546   1464    275   -568   -105       C  
ATOM   1249  CG  PHE A  83       6.435  19.981   8.445  1.00 13.23           C  
ANISOU 1249  CG  PHE A  83     1829   1719   1480    279   -582   -147       C  
ATOM   1250  CD1 PHE A  83       6.740  19.039   9.418  1.00 18.06           C  
ANISOU 1250  CD1 PHE A  83     2475   2327   2061    350   -694   -115       C  
ATOM   1251  CD2 PHE A  83       6.901  21.278   8.595  1.00 14.71           C  
ANISOU 1251  CD2 PHE A  83     1940   2003   1647    207   -492   -212       C  
ATOM   1252  CE1 PHE A  83       7.514  19.388  10.547  1.00 19.07           C  
ANISOU 1252  CE1 PHE A  83     2562   2554   2132    346   -716   -148       C  
ATOM   1253  CE2 PHE A  83       7.679  21.648   9.712  1.00 14.58           C  
ANISOU 1253  CE2 PHE A  83     1879   2084   1575    205   -509   -253       C  
ATOM   1254  CZ  PHE A  83       7.978  20.700  10.694  1.00 17.21           C  
ANISOU 1254  CZ  PHE A  83     2248   2419   1871    273   -621   -221       C  
ATOM   1255  H   PHE A  83       3.924  19.645   5.535  1.00 16.17           H  
ATOM   1256  HA  PHE A  83       3.806  19.019   8.039  1.00 14.40           H  
ATOM   1257  HB2 PHE A  83       5.795  18.666   7.060  1.00 15.22           H  
ATOM   1258  HB3 PHE A  83       5.875  20.157   6.519  1.00 15.22           H  
ATOM   1259  HD1 PHE A  83       6.428  18.168   9.327  1.00 21.68           H  
ATOM   1260  HD2 PHE A  83       6.700  21.914   7.947  1.00 17.66           H  
ATOM   1261  HE1 PHE A  83       7.711  18.749  11.192  1.00 22.89           H  
ATOM   1262  HE2 PHE A  83       7.984  22.523   9.800  1.00 17.49           H  
ATOM   1263  HZ  PHE A  83       8.493  20.936  11.432  1.00 20.65           H  
ATOM   1264  N   PHE A  84       3.964  22.161   7.536  1.00 11.19           N  
ANISOU 1264  N   PHE A  84     1610   1337   1304     34   -338    -37       N  
ATOM   1265  CA  PHE A  84       3.982  23.495   8.126  1.00 12.32           C  
ANISOU 1265  CA  PHE A  84     1703   1538   1439    -53   -246    -67       C  
ATOM   1266  C   PHE A  84       2.733  23.776   8.983  1.00 11.67           C  
ANISOU 1266  C   PHE A  84     1678   1386   1371   -118   -201     19       C  
ATOM   1267  O   PHE A  84       2.823  24.220  10.138  1.00 12.65           O  
ANISOU 1267  O   PHE A  84     1795   1562   1451   -149   -176      4       O  
ATOM   1268  CB  PHE A  84       4.053  24.575   7.024  1.00 13.11           C  
ANISOU 1268  CB  PHE A  84     1743   1652   1586   -124   -163   -109       C  
ATOM   1269  CG  PHE A  84       5.184  24.393   6.033  1.00 14.62           C  
ANISOU 1269  CG  PHE A  84     1874   1917   1763    -79   -187   -196       C  
ATOM   1270  CD1 PHE A  84       6.484  24.749   6.361  1.00 11.36           C  
ANISOU 1270  CD1 PHE A  84     1378   1632   1306    -58   -189   -296       C  
ATOM   1271  CD2 PHE A  84       4.936  23.898   4.759  1.00 12.41           C  
ANISOU 1271  CD2 PHE A  84     1617   1585   1513    -66   -202   -180       C  
ATOM   1272  CE1 PHE A  84       7.507  24.628   5.444  1.00 13.76           C  
ANISOU 1272  CE1 PHE A  84     1615   2012   1600    -24   -199   -381       C  
ATOM   1273  CE2 PHE A  84       5.982  23.754   3.834  1.00 12.11           C  
ANISOU 1273  CE2 PHE A  84     1518   1627   1456    -33   -211   -271       C  
ATOM   1274  CZ  PHE A  84       7.254  24.116   4.190  1.00 13.76           C  
ANISOU 1274  CZ  PHE A  84     1639   1964   1625    -11   -207   -372       C  
ATOM   1275  H   PHE A  84       4.009  22.167   6.677  1.00 13.42           H  
ATOM   1276  HA  PHE A  84       4.765  23.585   8.691  1.00 14.78           H  
ATOM   1277  HB2 PHE A  84       3.222  24.564   6.525  1.00 15.73           H  
ATOM   1278  HB3 PHE A  84       4.169  25.441   7.445  1.00 15.73           H  
ATOM   1279  HD1 PHE A  84       6.664  25.099   7.204  1.00 13.63           H  
ATOM   1280  HD2 PHE A  84       4.071  23.655   4.519  1.00 14.89           H  
ATOM   1281  HE1 PHE A  84       8.374  24.862   5.684  1.00 16.51           H  
ATOM   1282  HE2 PHE A  84       5.812  23.417   2.985  1.00 14.53           H  
ATOM   1283  HZ  PHE A  84       7.950  24.022   3.580  1.00 16.51           H  
ATOM   1284  N   LYS A  85       1.554  23.516   8.442  1.00 14.36           N  
ANISOU 1284  N   LYS A  85     2075   1611   1771   -142   -189    106       N  
ATOM   1285  CA  LYS A  85       0.367  23.736   9.252  1.00 15.80           C  
ANISOU 1285  CA  LYS A  85     2301   1730   1971   -201   -143    183       C  
ATOM   1286  C   LYS A  85       0.248  22.704  10.358  1.00 18.20           C  
ANISOU 1286  C   LYS A  85     2671   2034   2210   -157   -215    235       C  
ATOM   1287  O   LYS A  85      -0.261  22.998  11.423  1.00 14.90           O  
ANISOU 1287  O   LYS A  85     2271   1626   1765   -207   -174    260       O  
ATOM   1288  CB  LYS A  85      -0.879  23.718   8.393  1.00 14.63           C  
ANISOU 1288  CB  LYS A  85     2189   1458   1912   -241   -116    267       C  
ATOM   1289  CG  LYS A  85      -0.969  24.896   7.431  1.00 12.10           C  
ANISOU 1289  CG  LYS A  85     1808   1126   1662   -310    -40    236       C  
ATOM   1290  CD  LYS A  85      -2.273  24.881   6.663  1.00 12.79           C  
ANISOU 1290  CD  LYS A  85     1897   1132   1830   -314     -3    297       C  
ATOM   1291  CE  LYS A  85      -2.269  25.863   5.470  1.00 10.72           C  
ANISOU 1291  CE  LYS A  85     1568    890   1613   -332     63    246       C  
ATOM   1292  NZ  LYS A  85      -1.118  25.656   4.536  1.00 11.63           N  
ANISOU 1292  NZ  LYS A  85     1694   1015   1710   -363     -9    231       N  
ATOM   1293  H   LYS A  85       1.415  23.226   7.644  1.00 17.23           H  
ATOM   1294  HA  LYS A  85       0.429  24.610   9.668  1.00 18.96           H  
ATOM   1295  HB2 LYS A  85      -0.886  22.903   7.866  1.00 17.56           H  
ATOM   1296  HB3 LYS A  85      -1.659  23.744   8.969  1.00 17.56           H  
ATOM   1297  HG2 LYS A  85      -0.921  25.725   7.934  1.00 14.52           H  
ATOM   1298  HG3 LYS A  85      -0.239  24.847   6.794  1.00 14.52           H  
ATOM   1299  HD2 LYS A  85      -2.427  23.988   6.317  1.00 15.35           H  
ATOM   1300  HD3 LYS A  85      -2.995  25.136   7.259  1.00 15.35           H  
ATOM   1301  HE2 LYS A  85      -3.088  25.745   4.964  1.00 12.86           H  
ATOM   1302  HE3 LYS A  85      -2.218  26.770   5.810  1.00 12.86           H  
ATOM   1303  HZ1 LYS A  85      -0.350  25.767   4.972  1.00 13.96           H  
ATOM   1304  HZ2 LYS A  85      -1.144  24.833   4.200  1.00 13.96           H  
ATOM   1305  HZ3 LYS A  85      -1.160  26.243   3.869  1.00 13.96           H  
ATOM   1306  N   SER A  86       0.706  21.491  10.101  1.00 13.71           N  
ANISOU 1306  N   SER A  86     2139   1452   1619    -69   -325    251       N  
ATOM   1307  CA  SER A  86       0.522  20.417  11.064  1.00 15.14           C  
ANISOU 1307  CA  SER A  86     2391   1615   1748    -31   -412    320       C  
ATOM   1308  C   SER A  86       1.294  20.700  12.362  1.00 15.80           C  
ANISOU 1308  C   SER A  86     2451   1811   1742    -38   -421    274       C  
ATOM   1309  O   SER A  86       0.932  20.202  13.434  1.00 14.88           O  
ANISOU 1309  O   SER A  86     2392   1694   1569    -52   -457    339       O  
ATOM   1310  CB  SER A  86       0.952  19.079  10.464  1.00 17.60           C  
ANISOU 1310  CB  SER A  86     2738   1880   2067     72   -537    336       C  
ATOM   1311  OG  SER A  86       2.343  18.884  10.542  1.00 16.88           O  
ANISOU 1311  OG  SER A  86     2595   1881   1939    145   -598    246       O  
ATOM   1312  H   SER A  86       1.124  21.263   9.384  1.00 16.45           H  
ATOM   1313  HA  SER A  86      -0.420  20.354  11.286  1.00 18.17           H  
ATOM   1314  HB2 SER A  86       0.509  18.365  10.948  1.00 21.12           H  
ATOM   1315  HB3 SER A  86       0.686  19.057   9.531  1.00 21.12           H  
ATOM   1316  HG  SER A  86       2.742  19.493  10.124  1.00 20.26           H  
ATOM   1317  N   ALA A  87       2.334  21.525  12.273  1.00 15.21           N  
ANISOU 1317  N   ALA A  87     2294   1836   1650    -39   -387    167       N  
ATOM   1318  CA  ALA A  87       3.142  21.866  13.445  1.00 17.26           C  
ANISOU 1318  CA  ALA A  87     2525   2208   1825    -51   -399    115       C  
ATOM   1319  C   ALA A  87       2.511  22.947  14.323  1.00 16.43           C  
ANISOU 1319  C   ALA A  87     2416   2131   1695   -157   -287    109       C  
ATOM   1320  O   ALA A  87       2.994  23.220  15.405  1.00 18.92           O  
ANISOU 1320  O   ALA A  87     2724   2535   1930   -183   -291     75       O  
ATOM   1321  CB  ALA A  87       4.535  22.301  13.010  1.00 18.08           C  
ANISOU 1321  CB  ALA A  87     2536   2410   1924    -11   -411      0       C  
ATOM   1322  H   ALA A  87       2.594  21.902  11.545  1.00 18.25           H  
ATOM   1323  HA  ALA A  87       3.242  21.070  13.990  1.00 20.71           H  
ATOM   1324  HB1 ALA A  87       5.056  22.523  13.798  1.00 21.70           H  
ATOM   1325  HB2 ALA A  87       4.956  21.573  12.528  1.00 21.70           H  
ATOM   1326  HB3 ALA A  87       4.457  23.078  12.435  1.00 21.70           H  
ATOM   1327  N   MET A  88       1.450  23.588  13.839  1.00 15.02           N  
ANISOU 1327  N   MET A  88     2239   1878   1591   -220   -187    135       N  
ATOM   1328  CA  MET A  88       0.822  24.675  14.572  1.00 17.74           C  
ANISOU 1328  CA  MET A  88     2569   2239   1935   -317    -72    115       C  
ATOM   1329  C   MET A  88      -0.171  24.096  15.571  1.00 19.26           C  
ANISOU 1329  C   MET A  88     2838   2397   2082   -351    -72    203       C  
ATOM   1330  O   MET A  88      -0.679  23.010  15.346  1.00 18.88           O  
ANISOU 1330  O   MET A  88     2854   2277   2044   -311   -143    297       O  
ATOM   1331  CB  MET A  88       0.119  25.599  13.579  1.00 12.96           C  
ANISOU 1331  CB  MET A  88     1922   1558   1445   -365     25    107       C  
ATOM   1332  CG  MET A  88       1.090  26.249  12.621  1.00 12.21           C  
ANISOU 1332  CG  MET A  88     1751   1506   1384   -351     32     24       C  
ATOM   1333  SD  MET A  88       2.316  27.268  13.462  1.00 14.67           S  
ANISOU 1333  SD  MET A  88     1990   1960   1626   -382     64   -102       S  
ATOM   1334  CE  MET A  88       3.583  27.383  12.185  1.00 15.27           C  
ANISOU 1334  CE  MET A  88     1990   2087   1725   -333     24   -172       C  
ATOM   1335  H   MET A  88       1.075  23.409  13.086  1.00 18.03           H  
ATOM   1336  HA  MET A  88       1.500  25.185  15.043  1.00 21.29           H  
ATOM   1337  HB2 MET A  88      -0.517  25.082  13.060  1.00 15.55           H  
ATOM   1338  HB3 MET A  88      -0.339  26.300  14.067  1.00 15.55           H  
ATOM   1339  HG2 MET A  88       1.560  25.558  12.129  1.00 14.66           H  
ATOM   1340  HG3 MET A  88       0.597  26.817  12.008  1.00 14.66           H  
ATOM   1341  HE1 MET A  88       4.319  27.920  12.519  1.00 18.32           H  
ATOM   1342  HE2 MET A  88       3.895  26.490  11.970  1.00 18.32           H  
ATOM   1343  HE3 MET A  88       3.200  27.799  11.397  1.00 18.32           H  
ATOM   1344  N   PRO A  89      -0.452  24.822  16.671  1.00 19.95           N  
ANISOU 1344  N   PRO A  89     2921   2539   2119   -429      9    170       N  
ATOM   1345  CA  PRO A  89       0.019  26.195  16.943  1.00 15.03           C  
ANISOU 1345  CA  PRO A  89     2225   1989   1498   -485    102     56       C  
ATOM   1346  C   PRO A  89       1.418  26.309  17.548  1.00 16.37           C  
ANISOU 1346  C   PRO A  89     2365   2287   1568   -464     44    -25       C  
ATOM   1347  O   PRO A  89       1.982  27.391  17.533  1.00 18.93           O  
ANISOU 1347  O   PRO A  89     2621   2666   1905   -499    103   -123       O  
ATOM   1348  CB  PRO A  89      -1.035  26.726  17.915  1.00 14.73           C  
ANISOU 1348  CB  PRO A  89     2206   1943   1446   -575    209     61       C  
ATOM   1349  CG  PRO A  89      -1.444  25.471  18.697  1.00 18.28           C  
ANISOU 1349  CG  PRO A  89     2746   2393   1804   -565    134    163       C  
ATOM   1350  CD  PRO A  89      -1.371  24.336  17.721  1.00 17.91           C  
ANISOU 1350  CD  PRO A  89     2734   2271   1802   -477     22    246       C  
ATOM   1351  HA  PRO A  89      -0.013  26.721  16.129  1.00 18.04           H  
ATOM   1352  HB2 PRO A  89      -0.643  27.392  18.501  1.00 17.67           H  
ATOM   1353  HB3 PRO A  89      -1.788  27.092  17.423  1.00 17.67           H  
ATOM   1354  HG2 PRO A  89      -0.824  25.329  19.430  1.00 21.93           H  
ATOM   1355  HG3 PRO A  89      -2.348  25.576  19.031  1.00 21.93           H  
ATOM   1356  HD2 PRO A  89      -1.004  23.546  18.149  1.00 21.50           H  
ATOM   1357  HD3 PRO A  89      -2.247  24.159  17.345  1.00 21.50           H  
ATOM   1358  N  AGLU A  90       1.959  25.201  18.039  0.60 18.72           N  
ANISOU 1358  N  AGLU A  90     2710   2624   1779   -409    -77     21       N  
ATOM   1359  N  BGLU A  90       1.972  25.219  18.075  0.40 18.42           N  
ANISOU 1359  N  BGLU A  90     2672   2589   1738   -411    -76     19       N  
ATOM   1360  CA AGLU A  90       3.241  25.199  18.733  0.60 19.60           C  
ANISOU 1360  CA AGLU A  90     2796   2855   1794   -391   -147    -42       C  
ATOM   1361  CA BGLU A  90       3.274  25.278  18.750  0.40 18.76           C  
ANISOU 1361  CA BGLU A  90     2686   2754   1687   -394   -142    -49       C  
ATOM   1362  C  AGLU A  90       4.374  25.720  17.844  0.60 19.34           C  
ANISOU 1362  C  AGLU A  90     2673   2865   1810   -346   -158   -134       C  
ATOM   1363  C  BGLU A  90       4.375  25.780  17.827  0.40 19.49           C  
ANISOU 1363  C  BGLU A  90     2688   2884   1831   -349   -153   -138       C  
ATOM   1364  O  AGLU A  90       5.302  26.382  18.335  0.60 19.57           O  
ANISOU 1364  O  AGLU A  90     2650   2997   1790   -368   -155   -221       O  
ATOM   1365  O  BGLU A  90       5.296  26.475  18.277  0.40 20.43           O  
ANISOU 1365  O  BGLU A  90     2753   3104   1904   -372   -146   -227       O  
ATOM   1366  CB AGLU A  90       3.536  23.782  19.259  0.60 26.94           C  
ANISOU 1366  CB AGLU A  90     3794   3793   2647   -331   -295     43       C  
ATOM   1367  CB BGLU A  90       3.656  23.911  19.334  0.40 24.63           C  
ANISOU 1367  CB BGLU A  90     3494   3516   2348   -336   -290     29       C  
ATOM   1368  CG AGLU A  90       2.477  23.243  20.256  0.60 29.43           C  
ANISOU 1368  CG AGLU A  90     4204   4084   2894   -390   -289    141       C  
ATOM   1369  CG BGLU A  90       2.771  23.469  20.488  0.40 28.75           C  
ANISOU 1369  CG BGLU A  90     4104   4036   2783   -401   -287    112       C  
ATOM   1370  CD AGLU A  90       1.248  22.567  19.604  0.60 27.31           C  
ANISOU 1370  CD AGLU A  90     3989   3683   2704   -377   -279    246       C  
ATOM   1371  CD BGLU A  90       3.056  22.046  20.939  0.40 31.15           C  
ANISOU 1371  CD BGLU A  90     4479   4336   3021   -345   -447    210       C  
ATOM   1372  OE1AGLU A  90       1.137  22.521  18.361  0.60 17.67           O  
ANISOU 1372  OE1AGLU A  90     2740   2383   1592   -325   -274    245       O  
ATOM   1373  OE1BGLU A  90       2.857  21.105  20.140  0.40 30.34           O  
ANISOU 1373  OE1BGLU A  90     4403   4140   2987   -268   -522    279       O  
ATOM   1374  OE2AGLU A  90       0.382  22.070  20.361  0.60 29.81           O  
ANISOU 1374  OE2AGLU A  90     4378   3979   2968   -427   -277    332       O  
ATOM   1375  OE2BGLU A  90       3.482  21.872  22.096  0.40 33.36           O  
ANISOU 1375  OE2BGLU A  90     4790   4703   3182   -381   -503    220       O  
ATOM   1376  H  AGLU A  90       1.596  24.423  17.981  0.60 22.47           H  
ATOM   1377  H  BGLU A  90       1.619  24.435  18.056  0.40 22.10           H  
ATOM   1378  HA AGLU A  90       3.177  25.788  19.501  0.60 23.51           H  
ATOM   1379  HA BGLU A  90       3.207  25.902  19.490  0.40 22.51           H  
ATOM   1380  HB2AGLU A  90       3.571  23.171  18.507  0.60 32.32           H  
ATOM   1381  HB2BGLU A  90       3.588  23.242  18.634  0.40 29.55           H  
ATOM   1382  HB3AGLU A  90       4.392  23.790  19.714  0.60 32.32           H  
ATOM   1383  HB3BGLU A  90       4.568  23.954  19.659  0.40 29.55           H  
ATOM   1384  HG2AGLU A  90       2.901  22.587  20.831  0.60 35.32           H  
ATOM   1385  HG2BGLU A  90       2.919  24.058  21.243  0.40 34.50           H  
ATOM   1386  HG3AGLU A  90       2.153  23.984  20.792  0.60 35.32           H  
ATOM   1387  HG3BGLU A  90       1.843  23.514  20.209  0.40 34.50           H  
ATOM   1388  N   GLY A  91       4.283  25.421  16.548  1.00 17.41           N  
ANISOU 1388  N   GLY A  91     2411   2546   1659   -291   -171   -115       N  
ATOM   1389  CA  GLY A  91       5.156  25.989  15.527  1.00 16.09           C  
ANISOU 1389  CA  GLY A  91     2157   2409   1547   -265   -158   -197       C  
ATOM   1390  C   GLY A  91       6.378  25.177  15.161  1.00 15.56           C  
ANISOU 1390  C   GLY A  91     2057   2395   1461   -166   -275   -225       C  
ATOM   1391  O   GLY A  91       6.489  23.993  15.484  1.00 17.96           O  
ANISOU 1391  O   GLY A  91     2412   2683   1730    -99   -384   -167       O  
ATOM   1392  H  AGLY A  91       3.703  24.873  16.228  0.60 20.90           H  
ATOM   1393  H  BGLY A  91       3.719  24.847  16.246  0.40 20.90           H  
ATOM   1394  HA2 GLY A  91       4.639  26.123  14.718  1.00 19.31           H  
ATOM   1395  HA3 GLY A  91       5.462  26.859  15.830  1.00 19.31           H  
ATOM   1396  N   TYR A  92       7.306  25.819  14.463  1.00 16.76           N  
ANISOU 1396  N   TYR A  92     2119   2608   1642   -159   -253   -315       N  
ATOM   1397  CA  TYR A  92       8.523  25.146  14.030  1.00 15.25           C  
ANISOU 1397  CA  TYR A  92     1876   2474   1445    -65   -350   -361       C  
ATOM   1398  C   TYR A  92       9.691  26.102  13.986  1.00 15.44           C  
ANISOU 1398  C   TYR A  92     1796   2615   1457    -90   -321   -472       C  
ATOM   1399  O   TYR A  92       9.493  27.301  13.906  1.00 15.64           O  
ANISOU 1399  O   TYR A  92     1787   2653   1501   -177   -219   -512       O  
ATOM   1400  CB  TYR A  92       8.356  24.511  12.656  1.00 17.13           C  
ANISOU 1400  CB  TYR A  92     2114   2638   1756     -3   -367   -342       C  
ATOM   1401  CG  TYR A  92       7.838  25.423  11.553  1.00 13.26           C  
ANISOU 1401  CG  TYR A  92     1596   2105   1335    -68   -257   -357       C  
ATOM   1402  CD1 TYR A  92       8.670  26.318  10.906  1.00 13.95           C  
ANISOU 1402  CD1 TYR A  92     1590   2270   1441    -98   -207   -447       C  
ATOM   1403  CD2 TYR A  92       6.519  25.331  11.131  1.00 17.44           C  
ANISOU 1403  CD2 TYR A  92     2194   2517   1916   -102   -215   -272       C  
ATOM   1404  CE1 TYR A  92       8.182  27.151   9.880  1.00 12.51           C  
ANISOU 1404  CE1 TYR A  92     1386   2044   1321   -167   -118   -447       C  
ATOM   1405  CE2 TYR A  92       6.033  26.121  10.129  1.00 15.93           C  
ANISOU 1405  CE2 TYR A  92     1980   2281   1792   -163   -132   -274       C  
ATOM   1406  CZ  TYR A  92       6.868  27.024   9.488  1.00 13.04           C  
ANISOU 1406  CZ  TYR A  92     1525   1989   1440   -196    -86   -359       C  
ATOM   1407  OH  TYR A  92       6.329  27.817   8.488  1.00 14.86           O  
ANISOU 1407  OH  TYR A  92     1739   2168   1739   -268    -12   -346       O  
ATOM   1408  H   TYR A  92       7.255  26.645  14.227  1.00 20.11           H  
ATOM   1409  HA  TYR A  92       8.736  24.442  14.662  1.00 18.30           H  
ATOM   1410  HB2 TYR A  92       9.219  24.174  12.370  1.00 20.55           H  
ATOM   1411  HB3 TYR A  92       7.732  23.773  12.737  1.00 20.55           H  
ATOM   1412  HD1 TYR A  92       9.558  26.392  11.172  1.00 16.74           H  
ATOM   1413  HD2 TYR A  92       5.951  24.724  11.547  1.00 20.93           H  
ATOM   1414  HE1 TYR A  92       8.747  27.755   9.454  1.00 15.01           H  
ATOM   1415  HE2 TYR A  92       5.143  26.047   9.870  1.00 19.12           H  
ATOM   1416  HH  TYR A  92       6.912  28.346   8.194  1.00 17.83           H  
ATOM   1417  N   VAL A  93      10.895  25.536  14.040  1.00 15.69           N  
ANISOU 1417  N   VAL A  93     1772   2723   1465    -12   -416   -520       N  
ATOM   1418  CA  VAL A  93      12.128  26.274  13.812  1.00 16.05           C  
ANISOU 1418  CA  VAL A  93     1706   2883   1510    -21   -401   -628       C  
ATOM   1419  C   VAL A  93      12.537  26.118  12.356  1.00 16.81           C  
ANISOU 1419  C   VAL A  93     1740   2974   1673     25   -385   -671       C  
ATOM   1420  O   VAL A  93      12.549  25.003  11.835  1.00 18.29           O  
ANISOU 1420  O   VAL A  93     1948   3114   1886    117   -455   -645       O  
ATOM   1421  CB  VAL A  93      13.243  25.728  14.681  1.00 17.60           C  
ANISOU 1421  CB  VAL A  93     1866   3171   1651     39   -517   -659       C  
ATOM   1422  CG1 VAL A  93      14.556  26.429  14.388  1.00 17.82           C  
ANISOU 1422  CG1 VAL A  93     1767   3319   1685     34   -506   -771       C  
ATOM   1423  CG2 VAL A  93      12.907  25.902  16.141  1.00 17.62           C  
ANISOU 1423  CG2 VAL A  93     1932   3194   1569    -20   -535   -620       C  
ATOM   1424  H   VAL A  93      11.022  24.703  14.213  1.00 18.82           H  
ATOM   1425  HA  VAL A  93      11.999  27.215  14.010  1.00 19.26           H  
ATOM   1426  HB  VAL A  93      13.356  24.781  14.503  1.00 21.12           H  
ATOM   1427 HG11 VAL A  93      15.246  26.057  14.959  1.00 21.39           H  
ATOM   1428 HG12 VAL A  93      14.787  26.290  13.456  1.00 21.39           H  
ATOM   1429 HG13 VAL A  93      14.454  27.377  14.566  1.00 21.39           H  
ATOM   1430 HG21 VAL A  93      13.634  25.547  16.677  1.00 21.15           H  
ATOM   1431 HG22 VAL A  93      12.790  26.847  16.328  1.00 21.15           H  
ATOM   1432 HG23 VAL A  93      12.087  25.422  16.335  1.00 21.15           H  
ATOM   1433  N   GLN A  94      12.865  27.230  11.714  1.00 15.45           N  
ANISOU 1433  N   GLN A  94     1493   2850   1526    -44   -296   -736       N  
ATOM   1434  CA  GLN A  94      13.240  27.218  10.304  1.00 15.23           C  
ANISOU 1434  CA  GLN A  94     1406   2833   1548    -25   -266   -779       C  
ATOM   1435  C   GLN A  94      14.638  27.800  10.221  1.00 15.91           C  
ANISOU 1435  C   GLN A  94     1368   3057   1621    -32   -264   -887       C  
ATOM   1436  O   GLN A  94      14.889  28.945  10.609  1.00 15.93           O  
ANISOU 1436  O   GLN A  94     1329   3117   1609   -121   -208   -925       O  
ATOM   1437  CB  GLN A  94      12.229  27.986   9.437  1.00 14.26           C  
ANISOU 1437  CB  GLN A  94     1315   2630   1474   -115   -163   -739       C  
ATOM   1438  CG  GLN A  94      12.694  28.164   7.968  1.00 14.15           C  
ANISOU 1438  CG  GLN A  94     1235   2648   1495   -123   -124   -788       C  
ATOM   1439  CD  GLN A  94      11.556  28.557   7.056  1.00 13.27           C  
ANISOU 1439  CD  GLN A  94     1177   2433   1433   -193    -54   -721       C  
ATOM   1440  OE1 GLN A  94      10.517  27.896   7.031  1.00 14.82           O  
ANISOU 1440  OE1 GLN A  94     1464   2518   1648   -168    -74   -638       O  
ATOM   1441  NE2 GLN A  94      11.731  29.657   6.323  1.00 13.08           N  
ANISOU 1441  NE2 GLN A  94     1097   2442   1433   -289     21   -751       N  
ATOM   1442  H   GLN A  94      12.879  28.011  12.073  1.00 18.54           H  
ATOM   1443  HA  GLN A  94      13.273  26.301   9.990  1.00 18.28           H  
ATOM   1444  HB2 GLN A  94      11.390  27.500   9.428  1.00 17.12           H  
ATOM   1445  HB3 GLN A  94      12.095  28.868   9.817  1.00 17.12           H  
ATOM   1446  HG2 GLN A  94      13.367  28.862   7.930  1.00 16.98           H  
ATOM   1447  HG3 GLN A  94      13.063  27.326   7.648  1.00 16.98           H  
ATOM   1448 HE21 GLN A  94      12.464  30.103   6.385  1.00 15.70           H  
ATOM   1449 HE22 GLN A  94      11.112  29.921   5.789  1.00 15.70           H  
ATOM   1450  N   GLU A  95      15.561  26.956   9.778  1.00 16.58           N  
ANISOU 1450  N   GLU A  95     1392   3194   1715     66   -332   -939       N  
ATOM   1451  CA  GLU A  95      16.940  27.341   9.627  1.00 17.37           C  
ANISOU 1451  CA  GLU A  95     1361   3428   1808     73   -337  -1044       C  
ATOM   1452  C   GLU A  95      17.343  27.253   8.174  1.00 17.37           C  
ANISOU 1452  C   GLU A  95     1295   3458   1846     87   -292  -1102       C  
ATOM   1453  O   GLU A  95      16.919  26.338   7.455  1.00 18.53           O  
ANISOU 1453  O   GLU A  95     1487   3535   2020    153   -313  -1077       O  
ATOM   1454  CB  GLU A  95      17.850  26.444  10.471  1.00 18.45           C  
ANISOU 1454  CB  GLU A  95     1463   3621   1929    179   -463  -1072       C  
ATOM   1455  CG  GLU A  95      17.574  26.572  11.968  1.00 21.33           C  
ANISOU 1455  CG  GLU A  95     1890   3978   2236    150   -512  -1019       C  
ATOM   1456  CD  GLU A  95      18.336  25.567  12.810  1.00 35.83           C  
ANISOU 1456  CD  GLU A  95     3712   5844   4059    252   -652  -1017       C  
ATOM   1457  OE1 GLU A  95      17.992  24.368  12.750  1.00 43.49           O  
ANISOU 1457  OE1 GLU A  95     4738   6738   5049    346   -737   -966       O  
ATOM   1458  OE2 GLU A  95      19.246  25.987  13.559  1.00 40.30           O  
ANISOU 1458  OE2 GLU A  95     4229   6481   4605    234   -667  -1044       O  
ATOM   1459  H   GLU A  95      15.402  26.140   9.556  1.00 19.90           H  
ATOM   1460  HA  GLU A  95      17.053  28.258   9.922  1.00 20.84           H  
ATOM   1461  HB2 GLU A  95      17.708  25.519  10.216  1.00 22.15           H  
ATOM   1462  HB3 GLU A  95      18.774  26.694  10.314  1.00 22.15           H  
ATOM   1463  HG2 GLU A  95      17.830  27.460  12.260  1.00 25.59           H  
ATOM   1464  HG3 GLU A  95      16.626  26.434  12.125  1.00 25.59           H  
ATOM   1465  N   ARG A  96      18.141  28.212   7.740  1.00 17.62           N  
ANISOU 1465  N   ARG A  96     1223   3596   1876     18   -229  -1178       N  
ATOM   1466  CA  ARG A  96      18.701  28.190   6.396  1.00 17.85           C  
ANISOU 1466  CA  ARG A  96     1184   3673   1927     22   -174  -1237       C  
ATOM   1467  C   ARG A  96      20.153  28.571   6.356  1.00 19.82           C  
ANISOU 1467  C   ARG A  96     1336   4027   2166     31   -149  -1317       C  
ATOM   1468  O   ARG A  96      20.630  29.319   7.200  1.00 19.73           O  
ANISOU 1468  O   ARG A  96     1310   4051   2135    -10   -139  -1317       O  
ATOM   1469  CB  ARG A  96      18.001  29.186   5.483  1.00 17.03           C  
ANISOU 1469  CB  ARG A  96     1108   3533   1830   -105    -66  -1202       C  
ATOM   1470  CG  ARG A  96      16.559  28.922   5.191  1.00 16.05           C  
ANISOU 1470  CG  ARG A  96     1099   3274   1725   -126    -57  -1107       C  
ATOM   1471  CD  ARG A  96      16.247  29.383   3.754  1.00 15.67           C  
ANISOU 1471  CD  ARG A  96     1046   3217   1690   -209     23  -1102       C  
ATOM   1472  NE  ARG A  96      14.855  29.108   3.368  1.00 16.69           N  
ANISOU 1472  NE  ARG A  96     1294   3201   1845   -227     33   -998       N  
ATOM   1473  CZ  ARG A  96      13.840  29.955   3.525  1.00 16.33           C  
ANISOU 1473  CZ  ARG A  96     1310   3069   1826   -324     79   -917       C  
ATOM   1474  NH1 ARG A  96      14.030  31.141   4.067  1.00 16.61           N  
ANISOU 1474  NH1 ARG A  96     1306   3140   1866   -412    120   -930       N  
ATOM   1475  NH2 ARG A  96      12.629  29.626   3.128  1.00 13.37           N  
ANISOU 1475  NH2 ARG A  96     1032   2566   1480   -333     81   -827       N  
ATOM   1476  H   ARG A  96      18.378  28.894   8.207  1.00 21.14           H  
ATOM   1477  HA  ARG A  96      18.603  27.302   6.017  1.00 21.43           H  
ATOM   1478  HB2 ARG A  96      18.055  30.063   5.893  1.00 20.44           H  
ATOM   1479  HB3 ARG A  96      18.469  29.200   4.633  1.00 20.44           H  
ATOM   1480  HG2 ARG A  96      16.379  27.971   5.259  1.00 19.26           H  
ATOM   1481  HG3 ARG A  96      16.002  29.423   5.807  1.00 19.26           H  
ATOM   1482  HD2 ARG A  96      16.394  30.339   3.689  1.00 18.80           H  
ATOM   1483  HD3 ARG A  96      16.829  28.913   3.137  1.00 18.80           H  
ATOM   1484  HE  ARG A  96      14.684  28.344   3.013  1.00 20.02           H  
ATOM   1485 HH11 ARG A  96      14.817  31.374   4.326  1.00 19.93           H  
ATOM   1486 HH12 ARG A  96      13.368  31.680   4.165  1.00 19.93           H  
ATOM   1487 HH21 ARG A  96      12.487  28.855   2.774  1.00 16.04           H  
ATOM   1488 HH22 ARG A  96      11.976  30.176   3.238  1.00 16.04           H  
ATOM   1489  N   THR A  97      20.841  28.088   5.318  1.00 19.55           N  
ANISOU 1489  N   THR A  97     1243   4044   2140     78   -134  -1389       N  
ATOM   1490  CA  THR A  97      22.012  28.781   4.803  1.00 24.10           C  
ANISOU 1490  CA  THR A  97     1755   4711   2693     32    -74  -1459       C  
ATOM   1491  C   THR A  97      21.680  29.190   3.352  1.00 24.97           C  
ANISOU 1491  C   THR A  97     1887   4813   2787    -55      7  -1461       C  
ATOM   1492  O   THR A  97      21.149  28.402   2.582  1.00 21.90           O  
ANISOU 1492  O   THR A  97     1512   4394   2414    -17     -2  -1464       O  
ATOM   1493  CB  THR A  97      23.283  27.932   4.870  1.00 21.62           C  
ANISOU 1493  CB  THR A  97     1356   4467   2393    144   -135  -1550       C  
ATOM   1494  OG1 THR A  97      23.472  27.467   6.215  1.00 26.79           O  
ANISOU 1494  OG1 THR A  97     2007   5108   3063    221   -229  -1528       O  
ATOM   1495  CG2 THR A  97      24.499  28.755   4.457  1.00 26.15           C  
ANISOU 1495  CG2 THR A  97     1866   5134   2936     80    -79  -1617       C  
ATOM   1496  H   THR A  97      20.646  27.363   4.899  1.00 23.45           H  
ATOM   1497  HA  THR A  97      22.159  29.588   5.320  1.00 28.92           H  
ATOM   1498  HB  THR A  97      23.202  27.174   4.271  1.00 25.95           H  
ATOM   1499  HG1 THR A  97      24.168  26.999   6.262  1.00 32.15           H  
ATOM   1500 HG21 THR A  97      25.300  28.209   4.503  1.00 31.38           H  
ATOM   1501 HG22 THR A  97      24.388  29.076   3.548  1.00 31.38           H  
ATOM   1502 HG23 THR A  97      24.602  29.516   5.050  1.00 31.38           H  
ATOM   1503  N   ILE A  98      21.920  30.452   3.025  1.00 20.09           N  
ANISOU 1503  N   ILE A  98     1285   4210   2137   -174     76  -1445       N  
ATOM   1504  CA  ILE A  98      21.685  30.945   1.679  1.00 19.52           C  
ANISOU 1504  CA  ILE A  98     1245   4127   2045   -269    137  -1431       C  
ATOM   1505  C   ILE A  98      23.039  31.333   1.134  1.00 20.64           C  
ANISOU 1505  C   ILE A  98     1320   4369   2153   -297    155  -1508       C  
ATOM   1506  O   ILE A  98      23.702  32.231   1.675  1.00 21.63           O  
ANISOU 1506  O   ILE A  98     1428   4528   2262   -338    170  -1512       O  
ATOM   1507  CB  ILE A  98      20.734  32.162   1.667  1.00 19.30           C  
ANISOU 1507  CB  ILE A  98     1307   4009   2019   -386    189  -1328       C  
ATOM   1508  CG1 ILE A  98      19.436  31.835   2.415  1.00 17.56           C  
ANISOU 1508  CG1 ILE A  98     1144   3690   1837   -362    169  -1253       C  
ATOM   1509  CG2 ILE A  98      20.472  32.610   0.222  1.00 20.68           C  
ANISOU 1509  CG2 ILE A  98     1520   4164   2174   -476    237  -1299       C  
ATOM   1510  CD1 ILE A  98      18.517  33.037   2.614  1.00 16.73           C  
ANISOU 1510  CD1 ILE A  98     1125   3483   1749   -463    211  -1157       C  
ATOM   1511  H   ILE A  98      22.221  31.046   3.569  1.00 24.10           H  
ATOM   1512  HA  ILE A  98      21.309  30.242   1.126  1.00 23.43           H  
ATOM   1513  HB  ILE A  98      21.173  32.891   2.132  1.00 23.16           H  
ATOM   1514 HG12 ILE A  98      18.944  31.168   1.910  1.00 21.07           H  
ATOM   1515 HG13 ILE A  98      19.660  31.485   3.291  1.00 21.07           H  
ATOM   1516 HG21 ILE A  98      19.874  33.374   0.232  1.00 24.82           H  
ATOM   1517 HG22 ILE A  98      21.316  32.855  -0.190  1.00 24.82           H  
ATOM   1518 HG23 ILE A  98      20.066  31.877  -0.266  1.00 24.82           H  
ATOM   1519 HD11 ILE A  98      17.723  32.751   3.092  1.00 20.08           H  
ATOM   1520 HD12 ILE A  98      18.988  33.711   3.129  1.00 20.08           H  
ATOM   1521 HD13 ILE A  98      18.272  33.394   1.747  1.00 20.08           H  
ATOM   1522  N   PHE A  99      23.479  30.614   0.099  1.00 24.99           N  
ANISOU 1522  N   PHE A  99     1826   4972   2697   -270    152  -1574       N  
ATOM   1523  CA  PHE A  99      24.761  30.879  -0.548  1.00 23.05           C  
ANISOU 1523  CA  PHE A  99     1508   4829   2422   -300    172  -1654       C  
ATOM   1524  C   PHE A  99      24.553  31.699  -1.799  1.00 23.92           C  
ANISOU 1524  C   PHE A  99     1656   4939   2492   -429    234  -1620       C  
ATOM   1525  O   PHE A  99      24.013  31.196  -2.786  1.00 22.24           O  
ANISOU 1525  O   PHE A  99     1463   4712   2277   -445    245  -1616       O  
ATOM   1526  CB  PHE A  99      25.447  29.570  -0.954  1.00 23.55           C  
ANISOU 1526  CB  PHE A  99     1489   4952   2507   -191    131  -1755       C  
ATOM   1527  CG  PHE A  99      25.746  28.658   0.199  1.00 23.89           C  
ANISOU 1527  CG  PHE A  99     1493   4989   2594    -47     57  -1790       C  
ATOM   1528  CD1 PHE A  99      26.888  28.830   0.958  1.00 24.84           C  
ANISOU 1528  CD1 PHE A  99     1544   5175   2718    -10     34  -1841       C  
ATOM   1529  CD2 PHE A  99      24.881  27.635   0.521  1.00 27.85           C  
ANISOU 1529  CD2 PHE A  99     2030   5417   3136     50      6  -1765       C  
ATOM   1530  CE1 PHE A  99      27.162  27.989   2.016  1.00 25.25           C  
ANISOU 1530  CE1 PHE A  99     1563   5215   2814    120    -44  -1862       C  
ATOM   1531  CE2 PHE A  99      25.140  26.791   1.582  1.00 25.43           C  
ANISOU 1531  CE2 PHE A  99     1696   5094   2871    184    -75  -1784       C  
ATOM   1532  CZ  PHE A  99      26.291  26.965   2.326  1.00 30.08           C  
ANISOU 1532  CZ  PHE A  99     2218   5747   3466    217   -102  -1831       C  
ATOM   1533  H   PHE A  99      23.044  29.960  -0.251  1.00 29.99           H  
ATOM   1534  HA  PHE A  99      25.342  31.367   0.057  1.00 27.66           H  
ATOM   1535  HB2 PHE A  99      24.868  29.091  -1.568  1.00 28.26           H  
ATOM   1536  HB3 PHE A  99      26.287  29.780  -1.391  1.00 28.26           H  
ATOM   1537  HD1 PHE A  99      27.481  29.515   0.749  1.00 29.80           H  
ATOM   1538  HD2 PHE A  99      24.108  27.513   0.018  1.00 33.42           H  
ATOM   1539  HE1 PHE A  99      27.934  28.111   2.519  1.00 30.30           H  
ATOM   1540  HE2 PHE A  99      24.550  26.102   1.787  1.00 30.51           H  
ATOM   1541  HZ  PHE A  99      26.472  26.400   3.043  1.00 36.10           H  
ATOM   1542  N   PHE A 100      24.975  32.960  -1.760  1.00 24.64           N  
ANISOU 1542  N   PHE A 100     1760   5047   2554   -520    271  -1593       N  
ATOM   1543  CA  PHE A 100      24.881  33.820  -2.935  1.00 22.70           C  
ANISOU 1543  CA  PHE A 100     1551   4805   2268   -640    323  -1556       C  
ATOM   1544  C   PHE A 100      26.070  33.484  -3.858  1.00 26.60           C  
ANISOU 1544  C   PHE A 100     1954   5426   2728   -649    336  -1661       C  
ATOM   1545  O   PHE A 100      27.233  33.498  -3.443  1.00 25.11           O  
ANISOU 1545  O   PHE A 100     1683   5321   2537   -616    326  -1735       O  
ATOM   1546  CB  PHE A 100      24.855  35.304  -2.523  1.00 22.85           C  
ANISOU 1546  CB  PHE A 100     1620   4783   2280   -723    351  -1482       C  
ATOM   1547  CG  PHE A 100      23.565  35.728  -1.827  1.00 23.85           C  
ANISOU 1547  CG  PHE A 100     1841   4774   2447   -730    347  -1374       C  
ATOM   1548  CD1 PHE A 100      23.431  35.629  -0.443  1.00 23.82           C  
ANISOU 1548  CD1 PHE A 100     1834   4739   2476   -669    318  -1370       C  
ATOM   1549  CD2 PHE A 100      22.483  36.207  -2.564  1.00 20.32           C  
ANISOU 1549  CD2 PHE A 100     1483   4233   2006   -798    371  -1277       C  
ATOM   1550  CE1 PHE A 100      22.230  36.008   0.198  1.00 24.35           C  
ANISOU 1550  CE1 PHE A 100     1983   4685   2583   -680    317  -1278       C  
ATOM   1551  CE2 PHE A 100      21.276  36.588  -1.939  1.00 20.35           C  
ANISOU 1551  CE2 PHE A 100     1567   4104   2059   -799    365  -1178       C  
ATOM   1552  CZ  PHE A 100      21.147  36.482  -0.552  1.00 21.80           C  
ANISOU 1552  CZ  PHE A 100     1745   4261   2277   -742    341  -1183       C  
ATOM   1553  H   PHE A 100      25.318  33.339  -1.069  1.00 29.56           H  
ATOM   1554  HA  PHE A 100      24.060  33.622  -3.412  1.00 27.24           H  
ATOM   1555  HB2 PHE A 100      25.590  35.472  -1.913  1.00 27.42           H  
ATOM   1556  HB3 PHE A 100      24.956  35.850  -3.318  1.00 27.42           H  
ATOM   1557  HD1 PHE A 100      24.141  35.308   0.065  1.00 28.58           H  
ATOM   1558  HD2 PHE A 100      22.557  36.273  -3.488  1.00 24.39           H  
ATOM   1559  HE1 PHE A 100      22.157  35.937   1.122  1.00 29.22           H  
ATOM   1560  HE2 PHE A 100      20.567  36.906  -2.450  1.00 24.42           H  
ATOM   1561  HZ  PHE A 100      20.359  36.739  -0.130  1.00 26.16           H  
ATOM   1562  N   LYS A 101      25.784  33.125  -5.103  1.00 24.25           N  
ANISOU 1562  N   LYS A 101     1663   5144   2405   -693    357  -1670       N  
ATOM   1563  CA  LYS A 101      26.840  32.653  -5.971  1.00 25.68           C  
ANISOU 1563  CA  LYS A 101     1749   5445   2561   -695    370  -1778       C  
ATOM   1564  C   LYS A 101      27.872  33.750  -6.142  1.00 26.58           C  
ANISOU 1564  C   LYS A 101     1829   5640   2631   -777    405  -1796       C  
ATOM   1565  O   LYS A 101      27.521  34.920  -6.338  1.00 26.14           O  
ANISOU 1565  O   LYS A 101     1843   5545   2545   -876    434  -1711       O  
ATOM   1566  CB  LYS A 101      26.288  32.214  -7.327  1.00 25.76           C  
ANISOU 1566  CB  LYS A 101     1781   5461   2547   -749    395  -1777       C  
ATOM   1567  CG  LYS A 101      27.364  31.709  -8.255  1.00 27.37           C  
ANISOU 1567  CG  LYS A 101     1882   5791   2727   -754    416  -1893       C  
ATOM   1568  CD  LYS A 101      26.788  31.456  -9.633  1.00 34.20           C  
ANISOU 1568  CD  LYS A 101     2774   6664   3555   -833    450  -1883       C  
ATOM   1569  CE  LYS A 101      27.855  30.977 -10.617  1.00 41.85           C  
ANISOU 1569  CE  LYS A 101     3639   7764   4497   -846    482  -2004       C  
ATOM   1570  NZ  LYS A 101      28.256  29.563 -10.349  1.00 53.56           N  
ANISOU 1570  NZ  LYS A 101     5040   9264   6047   -694    453  -2103       N  
ATOM   1571  H   LYS A 101      25.001  33.146  -5.459  1.00 29.09           H  
ATOM   1572  HA  LYS A 101      27.274  31.889  -5.560  1.00 30.81           H  
ATOM   1573  HB2 LYS A 101      25.647  31.499  -7.191  1.00 30.92           H  
ATOM   1574  HB3 LYS A 101      25.855  32.971  -7.752  1.00 30.92           H  
ATOM   1575  HG2 LYS A 101      28.065  32.374  -8.332  1.00 32.85           H  
ATOM   1576  HG3 LYS A 101      27.722  30.875  -7.913  1.00 32.85           H  
ATOM   1577  HD2 LYS A 101      26.104  30.771  -9.572  1.00 41.04           H  
ATOM   1578  HD3 LYS A 101      26.408  32.279  -9.976  1.00 41.04           H  
ATOM   1579  HE2 LYS A 101      27.503  31.027 -11.520  1.00 50.22           H  
ATOM   1580  HE3 LYS A 101      28.642  31.537 -10.533  1.00 50.22           H  
ATOM   1581  HZ1 LYS A 101      28.877  29.307 -10.934  1.00 64.27           H  
ATOM   1582  HZ2 LYS A 101      28.587  29.492  -9.526  1.00 64.27           H  
ATOM   1583  HZ3 LYS A 101      27.549  29.027 -10.425  1.00 64.27           H  
ATOM   1584  N   ASP A 102      29.142  33.359  -6.035  0.83 27.92           N  
ANISOU 1584  N   ASP A 102     1888   5915   2803   -727    399  -1904       N  
ATOM   1585  CA  ASP A 102      30.276  34.277  -6.137  0.83 28.99           C  
ANISOU 1585  CA  ASP A 102     1970   6143   2903   -794    430  -1936       C  
ATOM   1586  C   ASP A 102      30.319  35.334  -5.037  0.83 32.15           C  
ANISOU 1586  C   ASP A 102     2406   6497   3313   -811    424  -1869       C  
ATOM   1587  O   ASP A 102      30.960  36.371  -5.184  0.83 29.03           O  
ANISOU 1587  O   ASP A 102     1997   6148   2885   -893    454  -1858       O  
ATOM   1588  CB  ASP A 102      30.290  34.959  -7.507  0.83 30.75           C  
ANISOU 1588  CB  ASP A 102     2215   6413   3058   -930    483  -1918       C  
ATOM   1589  CG  ASP A 102      30.505  33.977  -8.626  0.83 33.92           C  
ANISOU 1589  CG  ASP A 102     2557   6887   3443   -924    498  -2005       C  
ATOM   1590  OD1 ASP A 102      31.458  33.195  -8.504  0.83 31.59           O  
ANISOU 1590  OD1 ASP A 102     2155   6672   3175   -844    489  -2117       O  
ATOM   1591  OD2 ASP A 102      29.722  33.962  -9.602  0.83 30.10           O  
ANISOU 1591  OD2 ASP A 102     2132   6379   2926   -996    519  -1963       O  
ATOM   1592  H   ASP A 102      29.378  32.543  -5.900  0.83 33.50           H  
ATOM   1593  HA  ASP A 102      31.092  33.757  -6.066  0.83 34.79           H  
ATOM   1594  HB2 ASP A 102      29.438  35.399  -7.652  0.83 36.91           H  
ATOM   1595  HB3 ASP A 102      31.010  35.608  -7.533  0.83 36.91           H  
ATOM   1596  N   ASP A 103      29.649  35.083  -3.924  1.00 29.88           N  
ANISOU 1596  N   ASP A 103     2162   6120   3071   -738    385  -1824       N  
ATOM   1597  CA  ASP A 103      29.581  36.111  -2.898  1.00 27.50           C  
ANISOU 1597  CA  ASP A 103     1899   5769   2781   -762    383  -1758       C  
ATOM   1598  C   ASP A 103      29.355  35.456  -1.538  1.00 28.22           C  
ANISOU 1598  C   ASP A 103     1985   5817   2922   -651    331  -1763       C  
ATOM   1599  O   ASP A 103      29.613  34.267  -1.374  1.00 26.84           O  
ANISOU 1599  O   ASP A 103     1753   5673   2772   -548    294  -1832       O  
ATOM   1600  CB  ASP A 103      28.470  37.098  -3.245  1.00 28.44           C  
ANISOU 1600  CB  ASP A 103     2133   5783   2891   -855    410  -1637       C  
ATOM   1601  CG  ASP A 103      28.735  38.490  -2.736  1.00 28.16           C  
ANISOU 1601  CG  ASP A 103     2118   5726   2856   -923    426  -1582       C  
ATOM   1602  OD1 ASP A 103      29.450  38.632  -1.724  1.00 30.13           O  
ANISOU 1602  OD1 ASP A 103     2315   6011   3122   -885    408  -1619       O  
ATOM   1603  OD2 ASP A 103      28.210  39.453  -3.338  1.00 28.75           O  
ANISOU 1603  OD2 ASP A 103     2261   5744   2919  -1013    452  -1498       O  
ATOM   1604  H   ASP A 103      29.237  34.351  -3.740  0.83 35.86           H  
ATOM   1605  HA  ASP A 103      30.422  36.594  -2.869  1.00 33.00           H  
ATOM   1606  HB2 ASP A 103      28.381  37.144  -4.210  1.00 34.13           H  
ATOM   1607  HB3 ASP A 103      27.639  36.788  -2.851  1.00 34.13           H  
ATOM   1608  N   GLY A 104      28.890  36.227  -0.564  1.00 30.53           N  
ANISOU 1608  N   GLY A 104     2331   6037   3230   -669    326  -1691       N  
ATOM   1609  CA  GLY A 104      28.773  35.723   0.785  1.00 25.23           C  
ANISOU 1609  CA  GLY A 104     1650   5341   2596   -577    279  -1697       C  
ATOM   1610  C   GLY A 104      27.541  34.864   1.002  1.00 24.44           C  
ANISOU 1610  C   GLY A 104     1611   5152   2524   -516    253  -1655       C  
ATOM   1611  O   GLY A 104      26.833  34.479   0.049  1.00 23.67           O  
ANISOU 1611  O   GLY A 104     1555   5019   2422   -533    267  -1634       O  
ATOM   1612  H   GLY A 104      28.637  37.043  -0.662  1.00 36.63           H  
ATOM   1613  HA2 GLY A 104      29.556  35.191   0.996  1.00 30.28           H  
ATOM   1614  HA3 GLY A 104      28.736  36.470   1.403  1.00 30.28           H  
ATOM   1615  N   ASN A 105      27.279  34.539   2.265  1.00 23.77           N  
ANISOU 1615  N   ASN A 105     1529   5035   2468   -448    212  -1642       N  
ATOM   1616  CA  ASN A 105      26.134  33.716   2.600  1.00 22.81           C  
ANISOU 1616  CA  ASN A 105     1460   4834   2374   -386    183  -1600       C  
ATOM   1617  C   ASN A 105      25.394  34.251   3.800  1.00 23.90           C  
ANISOU 1617  C   ASN A 105     1654   4900   2528   -401    176  -1530       C  
ATOM   1618  O   ASN A 105      25.989  34.929   4.659  1.00 23.06           O  
ANISOU 1618  O   ASN A 105     1522   4825   2417   -420    172  -1538       O  
ATOM   1619  CB  ASN A 105      26.577  32.293   2.919  1.00 23.45           C  
ANISOU 1619  CB  ASN A 105     1472   4957   2481   -251    119  -1670       C  
ATOM   1620  CG  ASN A 105      27.494  32.235   4.129  1.00 29.41           C  
ANISOU 1620  CG  ASN A 105     2159   5765   3248   -191     72  -1706       C  
ATOM   1621  OD1 ASN A 105      27.028  32.202   5.274  1.00 26.95           O  
ANISOU 1621  OD1 ASN A 105     1874   5412   2952   -163     36  -1661       O  
ATOM   1622  ND2 ASN A 105      28.802  32.229   3.884  1.00 28.22           N  
ANISOU 1622  ND2 ASN A 105     1920   5709   3093   -178     69  -1786       N  
ATOM   1623  H   ASN A 105      27.750  34.784   2.941  1.00 28.53           H  
ATOM   1624  HA  ASN A 105      25.523  33.688   1.848  1.00 27.38           H  
ATOM   1625  HB2 ASN A 105      25.795  31.751   3.106  1.00 28.14           H  
ATOM   1626  HB3 ASN A 105      27.059  31.932   2.158  1.00 28.14           H  
ATOM   1627 HD21 ASN A 105      29.088  32.257   3.074  1.00 33.86           H  
ATOM   1628 HD22 ASN A 105      29.361  32.197   4.537  1.00 33.86           H  
ATOM   1629  N   TYR A 106      24.103  33.935   3.862  1.00 23.65           N  
ANISOU 1629  N   TYR A 106     1694   4775   2517   -394    173  -1465       N  
ATOM   1630  CA  TYR A 106      23.316  34.175   5.064  1.00 20.90           C  
ANISOU 1630  CA  TYR A 106     1390   4362   2188   -393    158  -1408       C  
ATOM   1631  C   TYR A 106      23.092  32.877   5.802  1.00 24.50           C  
ANISOU 1631  C   TYR A 106     1823   4822   2666   -279     89  -1420       C  
ATOM   1632  O   TYR A 106      22.815  31.845   5.188  1.00 20.22           O  
ANISOU 1632  O   TYR A 106     1275   4270   2138   -214     65  -1434       O  
ATOM   1633  CB  TYR A 106      21.937  34.732   4.718  1.00 19.20           C  
ANISOU 1633  CB  TYR A 106     1275   4028   1991   -466    197  -1317       C  
ATOM   1634  CG  TYR A 106      21.885  36.118   4.106  1.00 19.95           C  
ANISOU 1634  CG  TYR A 106     1417   4082   2081   -575    251  -1274       C  
ATOM   1635  CD1 TYR A 106      22.972  36.983   4.150  1.00 19.79           C  
ANISOU 1635  CD1 TYR A 106     1355   4126   2038   -616    266  -1311       C  
ATOM   1636  CD2 TYR A 106      20.720  36.563   3.488  1.00 18.11           C  
ANISOU 1636  CD2 TYR A 106     1270   3736   1875   -630    279  -1189       C  
ATOM   1637  CE1 TYR A 106      22.896  38.254   3.592  1.00 21.60           C  
ANISOU 1637  CE1 TYR A 106     1627   4310   2271   -708    305  -1264       C  
ATOM   1638  CE2 TYR A 106      20.629  37.822   2.946  1.00 18.29           C  
ANISOU 1638  CE2 TYR A 106     1336   3707   1905   -715    313  -1138       C  
ATOM   1639  CZ  TYR A 106      21.720  38.667   2.990  1.00 24.40           C  
ANISOU 1639  CZ  TYR A 106     2067   4549   2656   -753    325  -1175       C  
ATOM   1640  OH  TYR A 106      21.622  39.925   2.435  1.00 18.90           O  
ANISOU 1640  OH  TYR A 106     1409   3797   1973   -831    351  -1119       O  
ATOM   1641  H   TYR A 106      23.659  33.578   3.218  1.00 28.38           H  
ATOM   1642  HA  TYR A 106      23.776  34.799   5.647  1.00 25.08           H  
ATOM   1643  HB2 TYR A 106      21.516  34.126   4.088  1.00 23.04           H  
ATOM   1644  HB3 TYR A 106      21.411  34.761   5.533  1.00 23.04           H  
ATOM   1645  HD1 TYR A 106      23.761  36.707   4.557  1.00 23.75           H  
ATOM   1646  HD2 TYR A 106      19.979  36.001   3.458  1.00 21.73           H  
ATOM   1647  HE1 TYR A 106      23.630  38.825   3.628  1.00 25.92           H  
ATOM   1648  HE2 TYR A 106      19.841  38.097   2.536  1.00 21.95           H  
ATOM   1649  HH  TYR A 106      20.856  40.036   2.108  1.00 22.68           H  
ATOM   1650  N   LYS A 107      23.179  32.936   7.126  1.00 20.92           N  
ANISOU 1650  N   LYS A 107     1359   4375   2214   -255     48  -1411       N  
ATOM   1651  CA  LYS A 107      22.658  31.877   7.959  1.00 20.29           C  
ANISOU 1651  CA  LYS A 107     1291   4266   2153   -167    -32  -1387       C  
ATOM   1652  C   LYS A 107      21.535  32.475   8.781  1.00 19.44           C  
ANISOU 1652  C   LYS A 107     1261   4082   2044   -234    -18  -1314       C  
ATOM   1653  O   LYS A 107      21.698  33.539   9.395  1.00 19.53           O  
ANISOU 1653  O   LYS A 107     1279   4100   2040   -307     17  -1309       O  
ATOM   1654  CB  LYS A 107      23.751  31.310   8.853  1.00 22.82           C  
ANISOU 1654  CB  LYS A 107     1543   4657   2470    -84   -116  -1432       C  
ATOM   1655  CG  LYS A 107      24.807  30.526   8.092  1.00 28.41           C  
ANISOU 1655  CG  LYS A 107     2171   5429   3193      0   -140  -1512       C  
ATOM   1656  CD  LYS A 107      25.895  30.017   9.035  1.00 34.84           C  
ANISOU 1656  CD  LYS A 107     2919   6300   4017     80   -231  -1548       C  
ATOM   1657  H   LYS A 107      23.538  33.584   7.563  1.00 25.10           H  
ATOM   1658  HA  LYS A 107      22.301  31.165   7.405  1.00 24.35           H  
ATOM   1659  HB2 LYS A 107      24.194  32.042   9.309  1.00 27.38           H  
ATOM   1660  HB3 LYS A 107      23.347  30.713   9.503  1.00 27.38           H  
ATOM   1661  HG2 LYS A 107      24.393  29.761   7.662  1.00 34.09           H  
ATOM   1662  HG3 LYS A 107      25.221  31.102   7.431  1.00 34.09           H  
ATOM   1663  N   THR A 108      20.402  31.792   8.793  1.00 18.71           N  
ANISOU 1663  N   THR A 108     1227   3914   1967   -208    -46  -1261       N  
ATOM   1664  CA  THR A 108      19.228  32.303   9.464  1.00 17.92           C  
ANISOU 1664  CA  THR A 108     1208   3734   1868   -276    -27  -1197       C  
ATOM   1665  C   THR A 108      18.607  31.250  10.354  1.00 18.59           C  
ANISOU 1665  C   THR A 108     1347   3781   1935   -208   -123  -1161       C  
ATOM   1666  O   THR A 108      18.663  30.060  10.060  1.00 18.03           O  
ANISOU 1666  O   THR A 108     1276   3706   1871   -110   -195  -1163       O  
ATOM   1667  CB  THR A 108      18.177  32.788   8.482  1.00 16.96           C  
ANISOU 1667  CB  THR A 108     1140   3526   1777   -348     48  -1149       C  
ATOM   1668  OG1 THR A 108      17.698  31.667   7.726  1.00 17.26           O  
ANISOU 1668  OG1 THR A 108     1192   3535   1832   -285     11  -1136       O  
ATOM   1669  CG2 THR A 108      18.766  33.855   7.534  1.00 17.13           C  
ANISOU 1669  CG2 THR A 108     1147   3565   1798   -418    127  -1168       C  
ATOM   1670  H   THR A 108      20.289  31.027   8.416  1.00 22.45           H  
ATOM   1671  HA  THR A 108      19.486  33.053  10.022  1.00 21.51           H  
ATOM   1672  HB  THR A 108      17.439  33.186   8.971  1.00 20.35           H  
ATOM   1673  HG1 THR A 108      17.359  31.096   8.241  1.00 20.71           H  
ATOM   1674 HG21 THR A 108      18.085  34.157   6.912  1.00 20.56           H  
ATOM   1675 HG22 THR A 108      19.084  34.614   8.047  1.00 20.56           H  
ATOM   1676 HG23 THR A 108      19.507  33.480   7.033  1.00 20.56           H  
ATOM   1677  N   ARG A 109      18.016  31.715  11.452  1.00 17.68           N  
ANISOU 1677  N   ARG A 109     1289   3634   1793   -261   -122  -1128       N  
ATOM   1678  CA  ARG A 109      17.268  30.857  12.326  1.00 17.59           C  
ANISOU 1678  CA  ARG A 109     1360   3577   1746   -219   -201  -1081       C  
ATOM   1679  C   ARG A 109      16.042  31.624  12.736  1.00 16.86           C  
ANISOU 1679  C   ARG A 109     1345   3411   1649   -318   -133  -1042       C  
ATOM   1680  O   ARG A 109      16.144  32.760  13.211  1.00 20.14           O  
ANISOU 1680  O   ARG A 109     1747   3840   2066   -401    -68  -1062       O  
ATOM   1681  CB  ARG A 109      18.078  30.459  13.568  1.00 18.61           C  
ANISOU 1681  CB  ARG A 109     1479   3766   1823   -171   -290  -1090       C  
ATOM   1682  CG  ARG A 109      17.298  29.582  14.525  1.00 18.64           C  
ANISOU 1682  CG  ARG A 109     1583   3723   1774   -138   -374  -1027       C  
ATOM   1683  CD  ARG A 109      17.986  29.399  15.889  1.00 21.02           C  
ANISOU 1683  CD  ARG A 109     1891   4080   2016   -124   -456  -1022       C  
ATOM   1684  NE  ARG A 109      17.301  28.338  16.628  1.00 27.39           N  
ANISOU 1684  NE  ARG A 109     2795   4841   2771    -79   -549   -948       N  
ATOM   1685  CZ  ARG A 109      16.215  28.509  17.383  1.00 30.06           C  
ANISOU 1685  CZ  ARG A 109     3231   5140   3050   -146   -525   -901       C  
ATOM   1686  NH1 ARG A 109      15.682  29.719  17.563  1.00 25.98           N  
ANISOU 1686  NH1 ARG A 109     2727   4616   2528   -257   -408   -927       N  
ATOM   1687  NH2 ARG A 109      15.661  27.457  17.969  1.00 30.27           N  
ANISOU 1687  NH2 ARG A 109     3350   5111   3039    -99   -605   -813       N  
ATOM   1688  H   ARG A 109      18.041  32.536  11.705  1.00 21.21           H  
ATOM   1689  HA  ARG A 109      16.996  30.054  11.854  1.00 21.11           H  
ATOM   1690  HB2 ARG A 109      18.866  29.969  13.286  1.00 22.33           H  
ATOM   1691  HB3 ARG A 109      18.340  31.262  14.044  1.00 22.33           H  
ATOM   1692  HG2 ARG A 109      16.429  29.983  14.682  1.00 22.36           H  
ATOM   1693  HG3 ARG A 109      17.188  28.704  14.127  1.00 22.36           H  
ATOM   1694  HD2 ARG A 109      18.912  29.140  15.758  1.00 25.23           H  
ATOM   1695  HD3 ARG A 109      17.928  30.222  16.399  1.00 25.23           H  
ATOM   1696  HE  ARG A 109      17.623  27.542  16.571  1.00 32.87           H  
ATOM   1697 HH11 ARG A 109      16.030  30.404  17.177  1.00 31.18           H  
ATOM   1698 HH12 ARG A 109      14.985  29.812  18.059  1.00 31.18           H  
ATOM   1699 HH21 ARG A 109      16.006  26.676  17.866  1.00 36.32           H  
ATOM   1700 HH22 ARG A 109      14.972  27.559  18.474  1.00 36.32           H  
ATOM   1701  N   ALA A 110      14.897  30.976  12.572  1.00 16.22           N  
ANISOU 1701  N   ALA A 110     1357   3225   1581   -294   -135   -967       N  
ATOM   1702  CA  ALA A 110      13.615  31.587  12.832  1.00 15.82           C  
ANISOU 1702  CA  ALA A 110     1384   3074   1551   -372    -57   -913       C  
ATOM   1703  C   ALA A 110      12.700  30.649  13.617  1.00 16.32           C  
ANISOU 1703  C   ALA A 110     1557   3062   1581   -328   -102   -829       C  
ATOM   1704  O   ALA A 110      12.776  29.408  13.488  1.00 16.68           O  
ANISOU 1704  O   ALA A 110     1633   3089   1616   -231   -186   -787       O  
ATOM   1705  CB  ALA A 110      12.949  31.987  11.496  1.00 15.39           C  
ANISOU 1705  CB  ALA A 110     1331   2940   1577   -412     19   -883       C  
ATOM   1706  H   ALA A 110      14.842  30.160  12.304  1.00 19.46           H  
ATOM   1707  HA  ALA A 110      13.747  32.391  13.358  1.00 18.98           H  
ATOM   1708  HB1 ALA A 110      12.089  32.396  11.683  1.00 18.47           H  
ATOM   1709  HB2 ALA A 110      13.522  32.618  11.034  1.00 18.47           H  
ATOM   1710  HB3 ALA A 110      12.826  31.191  10.954  1.00 18.47           H  
ATOM   1711  N   GLU A 111      11.808  31.252  14.392  1.00 15.27           N  
ANISOU 1711  N   GLU A 111     1482   2883   1438   -402    -42   -805       N  
ATOM   1712  CA  GLU A 111      10.742  30.521  15.025  1.00 16.38           C  
ANISOU 1712  CA  GLU A 111     1726   2943   1554   -385    -58   -719       C  
ATOM   1713  C   GLU A 111       9.443  31.067  14.496  1.00 17.64           C  
ANISOU 1713  C   GLU A 111     1924   2986   1792   -444     40   -673       C  
ATOM   1714  O   GLU A 111       9.200  32.274  14.556  1.00 14.13           O  
ANISOU 1714  O   GLU A 111     1452   2533   1385   -532    128   -715       O  
ATOM   1715  CB  GLU A 111      10.807  30.642  16.559  1.00 16.01           C  
ANISOU 1715  CB  GLU A 111     1715   2955   1414   -422    -78   -733       C  
ATOM   1716  CG  GLU A 111      12.089  30.005  17.097  1.00 20.67           C  
ANISOU 1716  CG  GLU A 111     2268   3655   1931   -359   -196   -765       C  
ATOM   1717  CD  GLU A 111      12.095  29.863  18.607  1.00 30.32           C  
ANISOU 1717  CD  GLU A 111     3545   4931   3045   -391   -240   -755       C  
ATOM   1718  OE1 GLU A 111      11.057  30.169  19.255  1.00 30.53           O  
ANISOU 1718  OE1 GLU A 111     3642   4911   3046   -459   -172   -725       O  
ATOM   1719  OE2 GLU A 111      13.158  29.448  19.129  1.00 26.28           O  
ANISOU 1719  OE2 GLU A 111     3000   4511   2476   -352   -343   -780       O  
ATOM   1720  H   GLU A 111      11.805  32.095  14.564  1.00 18.33           H  
ATOM   1721  HA  GLU A 111      10.804  29.583  14.786  1.00 19.65           H  
ATOM   1722  HB2 GLU A 111      10.802  31.579  16.809  1.00 19.22           H  
ATOM   1723  HB3 GLU A 111      10.048  30.182  16.951  1.00 19.22           H  
ATOM   1724  HG2 GLU A 111      12.186  29.120  16.714  1.00 24.80           H  
ATOM   1725  HG3 GLU A 111      12.845  30.559  16.847  1.00 24.80           H  
ATOM   1726  N   VAL A 112       8.626  30.157  13.983  1.00 14.34           N  
ANISOU 1726  N   VAL A 112     1569   2474   1405   -395     18   -586       N  
ATOM   1727  CA  VAL A 112       7.324  30.486  13.432  1.00 13.02           C  
ANISOU 1727  CA  VAL A 112     1442   2186   1320   -441     95   -526       C  
ATOM   1728  C   VAL A 112       6.240  29.779  14.237  1.00 18.52           C  
ANISOU 1728  C   VAL A 112     2232   2814   1989   -434     86   -443       C  
ATOM   1729  O   VAL A 112       6.230  28.553  14.339  1.00 13.22           O  
ANISOU 1729  O   VAL A 112     1613   2130   1280   -360     -1   -385       O  
ATOM   1730  CB  VAL A 112       7.236  30.024  11.968  1.00 13.59           C  
ANISOU 1730  CB  VAL A 112     1506   2201   1457   -400     77   -490       C  
ATOM   1731  CG1 VAL A 112       5.906  30.427  11.353  1.00 11.69           C  
ANISOU 1731  CG1 VAL A 112     1301   1834   1308   -454    148   -423       C  
ATOM   1732  CG2 VAL A 112       8.413  30.569  11.154  1.00 16.60           C  
ANISOU 1732  CG2 VAL A 112     1792   2667   1848   -405     80   -571       C  
ATOM   1733  H   VAL A 112       8.811  29.318  13.943  1.00 17.21           H  
ATOM   1734  HA  VAL A 112       7.177  31.444  13.473  1.00 15.63           H  
ATOM   1735  HB  VAL A 112       7.288  29.056  11.945  1.00 16.31           H  
ATOM   1736 HG11 VAL A 112       5.879  30.123  10.432  1.00 14.03           H  
ATOM   1737 HG12 VAL A 112       5.187  30.015  11.859  1.00 14.03           H  
ATOM   1738 HG13 VAL A 112       5.822  31.393  11.386  1.00 14.03           H  
ATOM   1739 HG21 VAL A 112       8.331  30.263  10.237  1.00 19.92           H  
ATOM   1740 HG22 VAL A 112       8.394  31.538  11.182  1.00 19.92           H  
ATOM   1741 HG23 VAL A 112       9.241  30.242  11.540  1.00 19.92           H  
ATOM   1742  N   LYS A 113       5.318  30.537  14.817  1.00 13.85           N  
ANISOU 1742  N   LYS A 113     1662   2179   1421   -512    174   -440       N  
ATOM   1743  CA  LYS A 113       4.313  29.938  15.705  1.00 14.07           C  
ANISOU 1743  CA  LYS A 113     1773   2162   1413   -519    178   -369       C  
ATOM   1744  C   LYS A 113       3.144  30.865  15.903  1.00 14.06           C  
ANISOU 1744  C   LYS A 113     1776   2085   1483   -603    296   -369       C  
ATOM   1745  O   LYS A 113       3.235  32.054  15.587  1.00 14.87           O  
ANISOU 1745  O   LYS A 113     1816   2181   1653   -659    368   -434       O  
ATOM   1746  CB  LYS A 113       4.932  29.651  17.085  1.00 17.05           C  
ANISOU 1746  CB  LYS A 113     2173   2645   1660   -521    129   -399       C  
ATOM   1747  CG  LYS A 113       5.286  30.903  17.881  1.00 22.26           C  
ANISOU 1747  CG  LYS A 113     2788   3379   2289   -603    203   -502       C  
ATOM   1748  CD  LYS A 113       5.961  30.547  19.205  1.00 27.72           C  
ANISOU 1748  CD  LYS A 113     3508   4184   2841   -608    140   -526       C  
ATOM   1749  H   LYS A 113       5.249  31.389  14.720  1.00 16.62           H  
ATOM   1750  HA  LYS A 113       3.992  29.105  15.326  1.00 16.89           H  
ATOM   1751  HB2 LYS A 113       4.299  29.137  17.610  1.00 20.46           H  
ATOM   1752  HB3 LYS A 113       5.747  29.140  16.960  1.00 20.46           H  
ATOM   1753  HG2 LYS A 113       5.899  31.449  17.364  1.00 26.71           H  
ATOM   1754  HG3 LYS A 113       4.476  31.399  18.076  1.00 26.71           H  
ATOM   1755  N   PHE A 114       2.055  30.331  16.454  1.00 14.81           N  
ANISOU 1755  N   PHE A 114     1937   2122   1567   -614    314   -297       N  
ATOM   1756  CA  PHE A 114       0.939  31.174  16.850  1.00 14.41           C  
ANISOU 1756  CA  PHE A 114     1884   2010   1580   -692    430   -307       C  
ATOM   1757  C   PHE A 114       1.085  31.746  18.254  1.00 14.34           C  
ANISOU 1757  C   PHE A 114     1878   2089   1483   -754    484   -386       C  
ATOM   1758  O   PHE A 114       1.469  31.035  19.203  1.00 19.86           O  
ANISOU 1758  O   PHE A 114     2626   2870   2050   -742    426   -375       O  
ATOM   1759  CB  PHE A 114      -0.346  30.384  16.803  1.00 20.54           C  
ANISOU 1759  CB  PHE A 114     2723   2689   2390   -684    436   -198       C  
ATOM   1760  CG  PHE A 114      -1.011  30.407  15.464  1.00 16.46           C  
ANISOU 1760  CG  PHE A 114     2192   2052   2008   -670    444   -137       C  
ATOM   1761  CD1 PHE A 114      -0.804  29.389  14.576  1.00 18.21           C  
ANISOU 1761  CD1 PHE A 114     2445   2243   2232   -599    350    -66       C  
ATOM   1762  CD2 PHE A 114      -1.844  31.461  15.110  1.00 15.80           C  
ANISOU 1762  CD2 PHE A 114     2064   1885   2054   -730    542   -153       C  
ATOM   1763  CE1 PHE A 114      -1.434  29.404  13.330  1.00 15.22           C  
ANISOU 1763  CE1 PHE A 114     2058   1756   1967   -595    354     -9       C  
ATOM   1764  CE2 PHE A 114      -2.471  31.482  13.894  1.00 21.37           C  
ANISOU 1764  CE2 PHE A 114     2756   2500   2863   -655    489    -82       C  
ATOM   1765  CZ  PHE A 114      -2.262  30.452  12.998  1.00 16.17           C  
ANISOU 1765  CZ  PHE A 114     2132   1810   2202   -629    423    -13       C  
ATOM   1766  H   PHE A 114       1.941  29.493  16.606  1.00 17.77           H  
ATOM   1767  HA  PHE A 114       0.863  31.915  16.228  1.00 17.29           H  
ATOM   1768  HB2 PHE A 114      -0.153  29.459  17.024  1.00 24.64           H  
ATOM   1769  HB3 PHE A 114      -0.966  30.755  17.450  1.00 24.64           H  
ATOM   1770  HD1 PHE A 114      -0.248  28.679  14.805  1.00 21.85           H  
ATOM   1771  HD2 PHE A 114      -1.991  32.153  15.715  1.00 18.96           H  
ATOM   1772  HE1 PHE A 114      -1.293  28.710  12.726  1.00 18.26           H  
ATOM   1773  HE2 PHE A 114      -3.027  32.193  13.668  1.00 25.64           H  
ATOM   1774  HZ  PHE A 114      -2.679  30.468  12.167  1.00 19.41           H  
ATOM   1775  N   GLU A 115       0.745  33.022  18.370  1.00 14.32           N  
ANISOU 1775  N   GLU A 115     1824   2061   1554   -824    591   -464       N  
ATOM   1776  CA  GLU A 115       0.583  33.685  19.653  1.00 16.22           C  
ANISOU 1776  CA  GLU A 115     2068   2362   1735   -896    670   -548       C  
ATOM   1777  C   GLU A 115      -0.815  34.307  19.621  1.00 19.82           C  
ANISOU 1777  C   GLU A 115     2510   2706   2313   -947    790   -545       C  
ATOM   1778  O   GLU A 115      -1.048  35.344  19.022  1.00 16.65           O  
ANISOU 1778  O   GLU A 115     2066   2221   2039   -921    804   -581       O  
ATOM   1779  CB  GLU A 115       1.738  34.681  19.909  1.00 18.75           C  
ANISOU 1779  CB  GLU A 115     2329   2771   2025   -928    677   -670       C  
ATOM   1780  CG  GLU A 115       3.050  33.920  20.149  1.00 20.60           C  
ANISOU 1780  CG  GLU A 115     2577   3123   2126   -877    555   -667       C  
ATOM   1781  CD  GLU A 115       4.248  34.788  20.496  1.00 31.63           C  
ANISOU 1781  CD  GLU A 115     3917   4622   3479   -910    549   -783       C  
ATOM   1782  OE1 GLU A 115       4.230  36.002  20.187  1.00 20.20           O  
ANISOU 1782  OE1 GLU A 115     2409   3141   2125   -962    625   -860       O  
ATOM   1783  OE2 GLU A 115       5.207  34.230  21.103  1.00 32.45           O  
ANISOU 1783  OE2 GLU A 115     4036   4836   3456   -887    459   -792       O  
ATOM   1784  H   GLU A 115       0.599  33.538  17.698  1.00 17.18           H  
ATOM   1785  HA  GLU A 115       0.600  33.020  20.359  1.00 19.47           H  
ATOM   1786  HB2 GLU A 115       1.851  35.253  19.133  1.00 22.50           H  
ATOM   1787  HB3 GLU A 115       1.541  35.211  20.697  1.00 22.50           H  
ATOM   1788  HG2 GLU A 115       2.916  33.300  20.882  1.00 24.72           H  
ATOM   1789  HG3 GLU A 115       3.271  33.427  19.343  1.00 24.72           H  
ATOM   1790  N   GLY A 116      -1.763  33.613  20.241  1.00 19.37           N  
ANISOU 1790  N   GLY A 116     2511   2631   2216   -957    813   -483       N  
ATOM   1791  CA  GLY A 116      -3.158  33.973  20.113  1.00 18.29           C  
ANISOU 1791  CA  GLY A 116     2372   2372   2204   -931    855   -454       C  
ATOM   1792  C   GLY A 116      -3.587  33.814  18.657  1.00 14.11           C  
ANISOU 1792  C   GLY A 116     1827   1728   1807   -843    788   -362       C  
ATOM   1793  O   GLY A 116      -3.340  32.784  18.033  1.00 18.20           O  
ANISOU 1793  O   GLY A 116     2373   2239   2302   -823    727   -276       O  
ATOM   1794  H   GLY A 116      -1.619  32.929  20.741  1.00 23.24           H  
ATOM   1795  HA2 GLY A 116      -3.704  33.396  20.669  1.00 21.94           H  
ATOM   1796  HA3 GLY A 116      -3.291  34.895  20.384  1.00 21.94           H  
ATOM   1797  N   ASP A 117      -4.209  34.856  18.119  1.00 17.13           N  
ANISOU 1797  N   ASP A 117     2166   2029   2314   -791    794   -381       N  
ATOM   1798  CA  ASP A 117      -4.753  34.792  16.771  1.00 20.52           C  
ANISOU 1798  CA  ASP A 117     2578   2375   2844   -706    720   -285       C  
ATOM   1799  C   ASP A 117      -3.673  35.123  15.739  1.00 22.87           C  
ANISOU 1799  C   ASP A 117     2847   2687   3154   -683    664   -291       C  
ATOM   1800  O   ASP A 117      -3.937  35.049  14.546  1.00 18.51           O  
ANISOU 1800  O   ASP A 117     2284   2090   2658   -625    592   -213       O  
ATOM   1801  CB  ASP A 117      -5.964  35.731  16.613  1.00 24.72           C  
ANISOU 1801  CB  ASP A 117     3078   2837   3480   -666    739   -285       C  
ATOM   1802  CG  ASP A 117      -5.599  37.229  16.628  1.00 36.54           C  
ANISOU 1802  CG  ASP A 117     4533   4327   5025   -670    777   -382       C  
ATOM   1803  OD1 ASP A 117      -4.444  37.612  16.924  1.00 33.00           O  
ANISOU 1803  OD1 ASP A 117     4079   3934   4527   -711    796   -462       O  
ATOM   1804  OD2 ASP A 117      -6.502  38.055  16.356  1.00 48.96           O  
ANISOU 1804  OD2 ASP A 117     6077   5839   6686   -636    787   -379       O  
ATOM   1805  H   ASP A 117      -4.329  35.610  18.514  1.00 20.56           H  
ATOM   1806  HA  ASP A 117      -5.057  33.887  16.601  1.00 24.62           H  
ATOM   1807  HB2 ASP A 117      -6.398  35.541  15.766  1.00 29.67           H  
ATOM   1808  HB3 ASP A 117      -6.582  35.570  17.342  1.00 29.67           H  
ATOM   1809  N   THR A 118      -2.466  35.477  16.191  1.00 12.71           N  
ANISOU 1809  N   THR A 118     1547   1478   1803   -736    690   -385       N  
ATOM   1810  CA  THR A 118      -1.415  35.949  15.261  1.00 12.90           C  
ANISOU 1810  CA  THR A 118     1535   1524   1842   -718    645   -403       C  
ATOM   1811  C   THR A 118      -0.307  34.929  14.988  1.00 15.35           C  
ANISOU 1811  C   THR A 118     1849   1909   2073   -744    605   -398       C  
ATOM   1812  O   THR A 118       0.269  34.336  15.911  1.00 14.79           O  
ANISOU 1812  O   THR A 118     1788   1934   1897   -810    627   -442       O  
ATOM   1813  CB  THR A 118      -0.769  37.220  15.821  1.00 12.92           C  
ANISOU 1813  CB  THR A 118     1504   1568   1838   -754    690   -519       C  
ATOM   1814  OG1 THR A 118      -1.766  38.239  15.965  1.00 22.39           O  
ANISOU 1814  OG1 THR A 118     2694   2692   3121   -730    728   -530       O  
ATOM   1815  CG2 THR A 118       0.343  37.760  14.910  1.00 14.38           C  
ANISOU 1815  CG2 THR A 118     1650   1782   2030   -739    645   -535       C  
ATOM   1816  H   THR A 118      -2.226  35.455  17.017  1.00 15.25           H  
ATOM   1817  HA  THR A 118      -1.827  36.174  14.412  1.00 15.48           H  
ATOM   1818  HB  THR A 118      -0.382  37.026  16.689  1.00 15.51           H  
ATOM   1819  HG1 THR A 118      -2.368  37.980  16.491  1.00 26.87           H  
ATOM   1820 HG21 THR A 118       0.727  38.562  15.297  1.00 17.25           H  
ATOM   1821 HG22 THR A 118       1.041  37.094  14.809  1.00 17.25           H  
ATOM   1822 HG23 THR A 118      -0.019  37.973  14.036  1.00 17.25           H  
ATOM   1823  N   LEU A 119       0.011  34.760  13.710  1.00 14.65           N  
ANISOU 1823  N   LEU A 119     1746   1794   2024   -699    544   -346       N  
ATOM   1824  CA  LEU A 119       1.158  33.961  13.287  1.00 11.43           C  
ANISOU 1824  CA  LEU A 119     1323   1463   1556   -722    506   -362       C  
ATOM   1825  C   LEU A 119       2.394  34.852  13.329  1.00 13.68           C  
ANISOU 1825  C   LEU A 119     1547   1838   1811   -746    509   -462       C  
ATOM   1826  O   LEU A 119       2.462  35.874  12.641  1.00 14.73           O  
ANISOU 1826  O   LEU A 119     1662   1932   2002   -713    501   -459       O  
ATOM   1827  CB  LEU A 119       0.889  33.415  11.877  1.00 12.67           C  
ANISOU 1827  CB  LEU A 119     1494   1551   1768   -667    445   -271       C  
ATOM   1828  CG  LEU A 119       1.789  32.331  11.278  1.00 12.37           C  
ANISOU 1828  CG  LEU A 119     1456   1569   1675   -658    388   -270       C  
ATOM   1829  CD1 LEU A 119       3.107  32.976  10.826  1.00 14.62           C  
ANISOU 1829  CD1 LEU A 119     1668   1949   1938   -671    377   -355       C  
ATOM   1830  CD2 LEU A 119       2.023  31.196  12.295  1.00 13.83           C  
ANISOU 1830  CD2 LEU A 119     1698   1814   1743   -594    327   -256       C  
ATOM   1831  H   LEU A 119      -0.430  35.103  13.056  1.00 17.58           H  
ATOM   1832  HA  LEU A 119       1.285  33.216  13.895  1.00 13.71           H  
ATOM   1833  HB2 LEU A 119      -0.011  33.055  11.873  1.00 15.20           H  
ATOM   1834  HB3 LEU A 119       0.924  34.167  11.265  1.00 15.20           H  
ATOM   1835  HG  LEU A 119       1.354  31.953  10.497  1.00 14.85           H  
ATOM   1836 HD11 LEU A 119       3.679  32.290  10.446  1.00 17.54           H  
ATOM   1837 HD12 LEU A 119       2.914  33.654  10.160  1.00 17.54           H  
ATOM   1838 HD13 LEU A 119       3.540  33.380  11.594  1.00 17.54           H  
ATOM   1839 HD21 LEU A 119       2.594  30.524  11.891  1.00 16.60           H  
ATOM   1840 HD22 LEU A 119       2.450  31.564  13.084  1.00 16.60           H  
ATOM   1841 HD23 LEU A 119       1.168  30.805  12.533  1.00 16.60           H  
ATOM   1842  N  AVAL A 120       3.385  34.437  14.111  0.25 12.90           N  
ANISOU 1842  N  AVAL A 120     1431   1866   1604   -767    489   -529       N  
ATOM   1843  N  BVAL A 120       3.363  34.500  14.177  0.75 13.36           N  
ANISOU 1843  N  BVAL A 120     1489   1925   1663   -771    494   -533       N  
ATOM   1844  CA AVAL A 120       4.568  35.248  14.363  0.25 12.62           C  
ANISOU 1844  CA AVAL A 120     1332   1933   1531   -797    491   -632       C  
ATOM   1845  CA BVAL A 120       4.581  35.297  14.312  0.75 12.61           C  
ANISOU 1845  CA BVAL A 120     1326   1929   1534   -800    492   -633       C  
ATOM   1846  C  AVAL A 120       5.821  34.565  13.819  0.25 13.15           C  
ANISOU 1846  C  AVAL A 120     1372   2093   1531   -732    399   -640       C  
ATOM   1847  C  BVAL A 120       5.752  34.549  13.697  0.75 12.58           C  
ANISOU 1847  C  BVAL A 120     1301   2011   1469   -732    400   -633       C  
ATOM   1848  O  AVAL A 120       6.044  33.385  14.074  0.25 16.38           O  
ANISOU 1848  O  AVAL A 120     1824   2536   1863   -658    324   -602       O  
ATOM   1849  O  BVAL A 120       5.826  33.317  13.746  0.75 12.85           O  
ANISOU 1849  O  BVAL A 120     1381   2059   1441   -655    327   -581       O  
ATOM   1850  CB AVAL A 120       4.732  35.485  15.875  0.25 19.41           C  
ANISOU 1850  CB AVAL A 120     2208   2868   2299   -827    514   -700       C  
ATOM   1851  CB BVAL A 120       4.910  35.665  15.791  0.75 13.45           C  
ANISOU 1851  CB BVAL A 120     1439   2123   1550   -834    516   -714       C  
ATOM   1852  CG1AVAL A 120       5.902  36.394  16.148  0.25 13.96           C  
ANISOU 1852  CG1AVAL A 120     1451   2277   1578   -868    516   -807       C  
ATOM   1853  CG1BVAL A 120       3.717  36.351  16.440  0.75 19.28           C  
ANISOU 1853  CG1BVAL A 120     2198   2780   2348   -895    615   -727       C  
ATOM   1854  CG2AVAL A 120       3.445  36.071  16.465  0.25 17.70           C  
ANISOU 1854  CG2AVAL A 120     2015   2565   2147   -887    614   -701       C  
ATOM   1855  CG2BVAL A 120       5.314  34.427  16.586  0.75 24.61           C  
ANISOU 1855  CG2BVAL A 120     2908   3617   2827   -770    432   -686       C  
ATOM   1856  H  AVAL A 120       3.395  33.676  14.513  0.25 15.48           H  
ATOM   1857  H  BVAL A 120       3.337  33.806  14.684  0.75 16.03           H  
ATOM   1858  HA AVAL A 120       4.470  36.108  13.925  0.25 15.15           H  
ATOM   1859  HA BVAL A 120       4.468  36.125  13.819  0.75 15.13           H  
ATOM   1860  HB AVAL A 120       4.903  34.636  16.311  0.25 23.29           H  
ATOM   1861  HB BVAL A 120       5.656  36.285  15.803  0.75 16.14           H  
ATOM   1862 HG11AVAL A 120       5.981  36.526  17.105  0.25 16.76           H  
ATOM   1863 HG11BVAL A 120       3.941  36.572  17.358  0.75 23.14           H  
ATOM   1864 HG12AVAL A 120       6.709  35.982  15.802  0.25 16.76           H  
ATOM   1865 HG12BVAL A 120       3.511  37.160  15.946  0.75 23.14           H  
ATOM   1866 HG13AVAL A 120       5.749  37.245  15.707  0.25 16.76           H  
ATOM   1867 HG13BVAL A 120       2.957  35.748  16.421  0.75 23.14           H  
ATOM   1868 HG21AVAL A 120       3.571  36.212  17.416  0.25 21.24           H  
ATOM   1869 HG21BVAL A 120       5.511  34.688  17.498  0.75 29.53           H  
ATOM   1870 HG22AVAL A 120       3.254  36.915  16.027  0.25 21.24           H  
ATOM   1871 HG22BVAL A 120       4.580  33.792  16.574  0.75 29.53           H  
ATOM   1872 HG23AVAL A 120       2.718  35.448  16.315  0.25 21.24           H  
ATOM   1873 HG23BVAL A 120       6.100  34.032  16.177  0.75 29.53           H  
ATOM   1874  N   ASN A 121       6.623  35.311  13.063  1.00 13.56           N  
ANISOU 1874  N   ASN A 121     1351   2183   1620   -763    406   -691       N  
ATOM   1875  CA  ASN A 121       7.866  34.811  12.493  1.00 12.77           C  
ANISOU 1875  CA  ASN A 121     1207   2180   1467   -710    334   -717       C  
ATOM   1876  C   ASN A 121       8.984  35.699  13.047  1.00 15.74           C  
ANISOU 1876  C   ASN A 121     1511   2667   1803   -755    342   -822       C  
ATOM   1877  O   ASN A 121       9.119  36.849  12.646  1.00 17.95           O  
ANISOU 1877  O   ASN A 121     1781   2908   2130   -777    388   -830       O  
ATOM   1878  CB  ASN A 121       7.836  34.914  10.962  1.00 12.22           C  
ANISOU 1878  CB  ASN A 121     1107   2064   1472   -718    339   -683       C  
ATOM   1879  CG  ASN A 121       9.106  34.382  10.316  1.00 13.48           C  
ANISOU 1879  CG  ASN A 121     1214   2330   1580   -664    278   -721       C  
ATOM   1880  OD1 ASN A 121       9.896  33.684  10.958  1.00 13.00           O  
ANISOU 1880  OD1 ASN A 121     1145   2356   1437   -598    215   -755       O  
ATOM   1881  ND2 ASN A 121       9.326  34.734   9.045  1.00 14.37           N  
ANISOU 1881  ND2 ASN A 121     1307   2420   1732   -670    291   -701       N  
ATOM   1882  H  AASN A 121       6.461  36.132  12.863  0.25 16.28           H  
ATOM   1883  H  BASN A 121       6.513  36.156  12.945  0.75 16.28           H  
ATOM   1884  HA  ASN A 121       8.018  33.890  12.757  1.00 15.33           H  
ATOM   1885  HB2 ASN A 121       7.088  34.397  10.624  1.00 14.66           H  
ATOM   1886  HB3 ASN A 121       7.738  35.845  10.709  1.00 14.66           H  
ATOM   1887 HD21 ASN A 121       8.762  35.238   8.635  1.00 17.24           H  
ATOM   1888 HD22 ASN A 121      10.031  34.457   8.638  1.00 17.24           H  
ATOM   1889  N  AARG A 122       9.765  35.165  13.978  0.60 16.06           N  
ANISOU 1889  N  AARG A 122     1553   2808   1740   -713    282   -860       N  
ATOM   1890  N  BARG A 122       9.780  35.158  13.968  0.40 15.86           N  
ANISOU 1890  N  BARG A 122     1527   2784   1714   -712    281   -860       N  
ATOM   1891  CA AARG A 122      10.895  35.901  14.539  0.60 15.41           C  
ANISOU 1891  CA AARG A 122     1403   2840   1612   -752    275   -957       C  
ATOM   1892  CA BARG A 122      10.892  35.903  14.571  0.40 15.63           C  
ANISOU 1892  CA BARG A 122     1432   2869   1638   -753    275   -957       C  
ATOM   1893  C  AARG A 122      12.191  35.278  14.077  0.60 15.79           C  
ANISOU 1893  C  AARG A 122     1390   2995   1616   -686    194   -984       C  
ATOM   1894  C  BARG A 122      12.242  35.295  14.191  0.40 16.06           C  
ANISOU 1894  C  BARG A 122     1423   3036   1643   -687    191   -989       C  
ATOM   1895  O  AARG A 122      12.375  34.063  14.185  0.60 15.48           O  
ANISOU 1895  O  AARG A 122     1380   2974   1528   -594    115   -946       O  
ATOM   1896  O  BARG A 122      12.514  34.124  14.479  0.40 15.57           O  
ANISOU 1896  O  BARG A 122     1388   3005   1521   -599    109   -959       O  
ATOM   1897  CB AARG A 122      10.835  35.912  16.059  0.60 15.58           C  
ANISOU 1897  CB AARG A 122     1467   2906   1547   -771    268   -988       C  
ATOM   1898  CB BARG A 122      10.752  35.956  16.092  0.40 16.15           C  
ANISOU 1898  CB BARG A 122     1543   2972   1622   -775    274   -988       C  
ATOM   1899  CG AARG A 122       9.728  36.784  16.617  0.60 20.22           C  
ANISOU 1899  CG AARG A 122     2092   3411   2179   -852    366   -999       C  
ATOM   1900  CG BARG A 122       9.431  36.546  16.590  0.40 15.28           C  
ANISOU 1900  CG BARG A 122     1487   2761   1557   -839    366   -974       C  
ATOM   1901  CD AARG A 122       9.795  36.846  18.148  0.60 25.22           C  
ANISOU 1901  CD AARG A 122     2764   4112   2708   -882    364  -1048       C  
ATOM   1902  CD BARG A 122       9.659  37.514  17.771  0.40 22.43           C  
ANISOU 1902  CD BARG A 122     2382   3720   2421   -913    411  -1061       C  
ATOM   1903  NE AARG A 122       9.320  35.605  18.751  0.60 22.59           N  
ANISOU 1903  NE AARG A 122     2513   3776   2294   -825    312   -972       N  
ATOM   1904  NE BARG A 122       8.440  37.793  18.525  0.40 21.99           N  
ANISOU 1904  NE BARG A 122     2386   3593   2375   -965    489  -1065       N  
ATOM   1905  CZ AARG A 122       8.114  35.441  19.297  0.60 24.08           C  
ANISOU 1905  CZ AARG A 122     2774   3894   2482   -847    366   -930       C  
ATOM   1906  CZ BARG A 122       7.451  38.562  18.089  0.40 18.03           C  
ANISOU 1906  CZ BARG A 122     1883   2972   1995  -1001    580  -1052       C  
ATOM   1907  NH1AARG A 122       7.238  36.437  19.324  0.60 16.16           N  
ANISOU 1907  NH1AARG A 122     1765   2812   1561   -918    476   -963       N  
ATOM   1908  NH1BARG A 122       7.518  39.119  16.892  0.40 25.88           N  
ANISOU 1908  NH1BARG A 122     2865   3885   3081   -949    581  -1006       N  
ATOM   1909  NH2AARG A 122       7.787  34.271  19.825  0.60 30.34           N  
ANISOU 1909  NH2AARG A 122     3640   4693   3194   -800    306   -855       N  
ATOM   1910  NH2BARG A 122       6.386  38.761  18.836  0.40 15.94           N  
ANISOU 1910  NH2BARG A 122     1664   2652   1743  -1042    653  -1063       N  
ATOM   1911  H  AARG A 122       9.663  34.376  14.303  0.60 19.27           H  
ATOM   1912  H  BARG A 122       9.699  34.355  14.265  0.40 19.03           H  
ATOM   1913  HA AARG A 122      10.869  36.819  14.226  0.60 18.49           H  
ATOM   1914  HA BARG A 122      10.874  36.814  14.239  0.40 18.76           H  
ATOM   1915  HB2AARG A 122      10.687  35.007  16.373  0.60 18.70           H  
ATOM   1916  HB2BARG A 122      10.821  35.054  16.441  0.40 19.38           H  
ATOM   1917  HB3AARG A 122      11.679  36.246  16.403  0.60 18.70           H  
ATOM   1918  HB3BARG A 122      11.470  36.500  16.451  0.40 19.38           H  
ATOM   1919  HG2AARG A 122       9.823  37.685  16.270  0.60 24.26           H  
ATOM   1920  HG2BARG A 122       9.007  37.038  15.870  0.40 18.33           H  
ATOM   1921  HG3AARG A 122       8.868  36.414  16.363  0.60 24.26           H  
ATOM   1922  HG3BARG A 122       8.852  35.828  16.892  0.40 18.33           H  
ATOM   1923  HD2AARG A 122      10.714  36.987  18.424  0.60 30.27           H  
ATOM   1924  HD2BARG A 122      10.305  37.122  18.380  0.40 26.92           H  
ATOM   1925  HD3AARG A 122       9.234  37.572  18.464  0.60 30.27           H  
ATOM   1926  HD3BARG A 122       9.998  38.356  17.428  0.40 26.92           H  
ATOM   1927  HE AARG A 122       9.855  34.931  18.754  0.60 27.11           H  
ATOM   1928  HE BARG A 122       8.358  37.435  19.303  0.40 26.38           H  
ATOM   1929 HH11AARG A 122       7.444  37.200  18.986  0.60 19.39           H  
ATOM   1930 HH11BARG A 122       8.211  38.992  16.397  0.40 31.05           H  
ATOM   1931 HH12AARG A 122       6.464  36.319  19.679  0.60 19.39           H  
ATOM   1932 HH12BARG A 122       6.874  39.614  16.611  0.40 31.05           H  
ATOM   1933 HH21AARG A 122       8.349  33.620  19.810  0.60 36.40           H  
ATOM   1934 HH21BARG A 122       6.333  38.400  19.614  0.40 19.13           H  
ATOM   1935 HH22AARG A 122       7.009  34.160  20.176  0.60 36.40           H  
ATOM   1936 HH22BARG A 122       5.745  39.257  18.547  0.40 19.13           H  
ATOM   1937  N   ILE A 123      13.096  36.120  13.586  1.00 16.59           N  
ANISOU 1937  N   ILE A 123     1422   3137   1746   -701    224  -1016       N  
ATOM   1938  CA  ILE A 123      14.281  35.656  12.885  1.00 15.70           C  
ANISOU 1938  CA  ILE A 123     1242   3105   1616   -639    175  -1035       C  
ATOM   1939  C   ILE A 123      15.585  36.342  13.314  1.00 16.54           C  
ANISOU 1939  C   ILE A 123     1285   3305   1693   -646    175  -1092       C  
ATOM   1940  O   ILE A 123      15.600  37.531  13.593  1.00 17.07           O  
ANISOU 1940  O   ILE A 123     1357   3354   1776   -709    237  -1111       O  
ATOM   1941  CB  ILE A 123      14.156  35.991  11.370  1.00 16.33           C  
ANISOU 1941  CB  ILE A 123     1319   3126   1759   -646    223  -1002       C  
ATOM   1942  CG1 ILE A 123      12.799  35.585  10.788  1.00 18.76           C  
ANISOU 1942  CG1 ILE A 123     1691   3317   2120   -655    239   -930       C  
ATOM   1943  CG2 ILE A 123      15.228  35.325  10.608  1.00 15.48           C  
ANISOU 1943  CG2 ILE A 123     1149   3103   1632   -583    179  -1029       C  
ATOM   1944  CD1 ILE A 123      12.267  36.598   9.896  1.00 14.33           C  
ANISOU 1944  CD1 ILE A 123     1180   2643   1623   -691    299   -876       C  
ATOM   1945  H  AILE A 123      13.042  36.976  13.648  0.60 19.91           H  
ATOM   1946  H  BILE A 123      13.003  36.975  13.570  0.40 19.91           H  
ATOM   1947  HA  ILE A 123      14.377  34.696  12.991  1.00 18.83           H  
ATOM   1948  HB  ILE A 123      14.258  36.949  11.262  1.00 19.59           H  
ATOM   1949 HG12 ILE A 123      12.901  34.762  10.285  1.00 22.51           H  
ATOM   1950 HG13 ILE A 123      12.167  35.458  11.513  1.00 22.51           H  
ATOM   1951 HG21 ILE A 123      15.131  35.547   9.668  1.00 18.58           H  
ATOM   1952 HG22 ILE A 123      16.087  35.635  10.935  1.00 18.58           H  
ATOM   1953 HG23 ILE A 123      15.153  34.366  10.731  1.00 18.58           H  
ATOM   1954 HD11 ILE A 123      11.410  36.298   9.554  1.00 17.20           H  
ATOM   1955 HD12 ILE A 123      12.155  37.426  10.389  1.00 17.20           H  
ATOM   1956 HD13 ILE A 123      12.888  36.730   9.163  1.00 17.20           H  
ATOM   1957  N  AGLU A 124      16.659  35.559  13.388  0.46 17.15           N  
ANISOU 1957  N  AGLU A 124     1310   3477   1731   -574    100  -1118       N  
ATOM   1958  N  BGLU A 124      16.671  35.574  13.341  0.54 17.14           N  
ANISOU 1958  N  BGLU A 124     1307   3475   1732   -574    102  -1118       N  
ATOM   1959  CA AGLU A 124      18.022  36.067  13.474  0.46 17.97           C  
ANISOU 1959  CA AGLU A 124     1340   3670   1818   -571     96  -1170       C  
ATOM   1960  CA BGLU A 124      18.022  36.102  13.478  0.54 17.97           C  
ANISOU 1960  CA BGLU A 124     1340   3670   1818   -573     98  -1170       C  
ATOM   1961  C  AGLU A 124      18.724  35.746  12.155  0.46 19.33           C  
ANISOU 1961  C  AGLU A 124     1460   3873   2013   -527     99  -1183       C  
ATOM   1962  C  BGLU A 124      18.852  35.715  12.250  0.54 19.76           C  
ANISOU 1962  C  BGLU A 124     1508   3939   2062   -522     92  -1188       C  
ATOM   1963  O  AGLU A 124      18.578  34.647  11.633  0.46 19.29           O  
ANISOU 1963  O  AGLU A 124     1452   3866   2013   -457     53  -1169       O  
ATOM   1964  O  BGLU A 124      18.926  34.543  11.888  0.54 18.09           O  
ANISOU 1964  O  BGLU A 124     1283   3742   1849   -442     32  -1182       O  
ATOM   1965  CB AGLU A 124      18.767  35.423  14.658  0.46 18.88           C  
ANISOU 1965  CB AGLU A 124     1437   3864   1872   -521      4  -1190       C  
ATOM   1966  CB BGLU A 124      18.666  35.582  14.768  0.54 18.86           C  
ANISOU 1966  CB BGLU A 124     1441   3855   1869   -535     13  -1190       C  
ATOM   1967  CG AGLU A 124      20.283  35.510  14.574  0.46 20.82           C  
ANISOU 1967  CG AGLU A 124     1594   4208   2107   -489    -26  -1241       C  
ATOM   1968  CG BGLU A 124      17.855  35.958  16.011  0.54 23.91           C  
ANISOU 1968  CG BGLU A 124     2152   4460   2474   -594     25  -1177       C  
ATOM   1969  CD AGLU A 124      20.964  35.686  15.937  0.46 26.52           C  
ANISOU 1969  CD AGLU A 124     2306   4992   2777   -500    -81  -1264       C  
ATOM   1970  CD BGLU A 124      18.458  35.443  17.307  0.54 31.52           C  
ANISOU 1970  CD BGLU A 124     3126   5490   3360   -565    -65  -1185       C  
ATOM   1971  OE1AGLU A 124      20.778  34.830  16.835  0.46 21.51           O  
ANISOU 1971  OE1AGLU A 124     1716   4361   2096   -459   -165  -1238       O  
ATOM   1972  OE1BGLU A 124      18.940  34.283  17.306  0.54 28.93           O  
ANISOU 1972  OE1BGLU A 124     2789   5195   3007   -475   -162  -1168       O  
ATOM   1973  OE2AGLU A 124      21.703  36.685  16.101  0.46 28.48           O  
ANISOU 1973  OE2AGLU A 124     2512   5284   3026   -553    -43  -1304       O  
ATOM   1974  OE2BGLU A 124      18.449  36.206  18.315  0.54 25.93           O  
ANISOU 1974  OE2BGLU A 124     2438   4796   2618   -631    -42  -1206       O  
ATOM   1975  H  AGLU A 124      16.618  34.700  13.388  0.46 20.59           H  
ATOM   1976  H  BGLU A 124      16.647  34.716  13.281  0.54 20.57           H  
ATOM   1977  HA AGLU A 124      18.009  37.029  13.597  0.46 21.56           H  
ATOM   1978  HA BGLU A 124      17.984  37.070  13.526  0.54 21.56           H  
ATOM   1979  HB2AGLU A 124      18.492  35.867  15.475  0.46 22.66           H  
ATOM   1980  HB2BGLU A 124      18.724  34.615  14.727  0.54 22.63           H  
ATOM   1981  HB3AGLU A 124      18.529  34.484  14.700  0.46 22.66           H  
ATOM   1982  HB3BGLU A 124      19.553  35.966  14.858  0.54 22.63           H  
ATOM   1983  HG2AGLU A 124      20.622  34.694  14.176  0.46 24.98           H  
ATOM   1984  HG2BGLU A 124      17.803  36.925  16.071  0.54 28.70           H  
ATOM   1985  HG3AGLU A 124      20.523  36.271  14.022  0.46 24.98           H  
ATOM   1986  HG3BGLU A 124      16.964  35.585  15.929  0.54 28.70           H  
ATOM   1987  N   LEU A 125      19.469  36.714  11.623  1.00 18.28           N  
ANISOU 1987  N   LEU A 125     1295   3765   1885   -569    150  -1211       N  
ATOM   1988  CA  LEU A 125      20.265  36.517  10.414  1.00 18.50           C  
ANISOU 1988  CA  LEU A 125     1279   3833   1916   -541    156  -1234       C  
ATOM   1989  C   LEU A 125      21.690  37.024  10.565  1.00 19.50           C  
ANISOU 1989  C   LEU A 125     1336   4055   2018   -547    151  -1293       C  
ATOM   1990  O   LEU A 125      21.946  38.120  11.106  1.00 20.91           O  
ANISOU 1990  O   LEU A 125     1520   4236   2190   -611    179  -1304       O  
ATOM   1991  CB  LEU A 125      19.569  37.205   9.243  1.00 19.19           C  
ANISOU 1991  CB  LEU A 125     1429   3827   2035   -600    217  -1188       C  
ATOM   1992  CG  LEU A 125      20.262  37.187   7.880  1.00 18.02           C  
ANISOU 1992  CG  LEU A 125     1256   3710   1881   -598    231  -1203       C  
ATOM   1993  CD1 LEU A 125      19.214  37.377   6.792  1.00 17.19           C  
ANISOU 1993  CD1 LEU A 125     1225   3495   1810   -635    262  -1132       C  
ATOM   1994  CD2 LEU A 125      21.374  38.257   7.759  1.00 18.78           C  
ANISOU 1994  CD2 LEU A 125     1317   3860   1959   -648    253  -1239       C  
ATOM   1995  H  ALEU A 125      19.530  37.506  11.951  0.46 21.93           H  
ATOM   1996  H  BLEU A 125      19.441  37.532  11.886  0.54 21.93           H  
ATOM   1997  HA  LEU A 125      20.307  35.568  10.218  1.00 22.20           H  
ATOM   1998  HB2 LEU A 125      18.702  36.786   9.124  1.00 23.03           H  
ATOM   1999  HB3 LEU A 125      19.439  38.137   9.481  1.00 23.03           H  
ATOM   2000  HG  LEU A 125      20.672  36.318   7.749  1.00 21.63           H  
ATOM   2001 HD11 LEU A 125      19.653  37.365   5.927  1.00 20.62           H  
ATOM   2002 HD12 LEU A 125      18.569  36.654   6.846  1.00 20.62           H  
ATOM   2003 HD13 LEU A 125      18.770  38.228   6.927  1.00 20.62           H  
ATOM   2004 HD21 LEU A 125      21.775  38.197   6.878  1.00 22.54           H  
ATOM   2005 HD22 LEU A 125      20.982  39.135   7.885  1.00 22.54           H  
ATOM   2006 HD23 LEU A 125      22.045  38.093   8.440  1.00 22.54           H  
ATOM   2007  N   LYS A 126      22.622  36.200  10.100  1.00 20.33           N  
ANISOU 2007  N   LYS A 126     1373   4238   2113   -477    113  -1335       N  
ATOM   2008  CA  LYS A 126      24.027  36.541  10.104  1.00 21.48           C  
ANISOU 2008  CA  LYS A 126     1444   4478   2241   -476    105  -1394       C  
ATOM   2009  C   LYS A 126      24.577  36.320   8.707  1.00 22.94           C  
ANISOU 2009  C   LYS A 126     1599   4693   2425   -465    129  -1422       C  
ATOM   2010  O   LYS A 126      24.516  35.188   8.183  1.00 22.51           O  
ANISOU 2010  O   LYS A 126     1525   4648   2379   -389     99  -1437       O  
ATOM   2011  CB  LYS A 126      24.801  35.649  11.050  1.00 23.54           C  
ANISOU 2011  CB  LYS A 126     1640   4813   2490   -393     18  -1429       C  
ATOM   2012  CG  LYS A 126      26.295  35.931  10.991  1.00 31.80           C  
ANISOU 2012  CG  LYS A 126     2599   5956   3526   -388      7  -1492       C  
ATOM   2013  CD  LYS A 126      26.845  36.207  12.348  1.00 40.59           C  
ANISOU 2013  CD  LYS A 126     3687   7113   4622   -396    -45  -1502       C  
ATOM   2014  CE  LYS A 126      28.339  36.483  12.274  1.00 42.22           C  
ANISOU 2014  CE  LYS A 126     3801   7415   4824   -393    -59  -1562       C  
ATOM   2015  NZ  LYS A 126      28.958  36.170  13.571  1.00 41.88           N  
ANISOU 2015  NZ  LYS A 126     3722   7419   4771   -360   -150  -1571       N  
ATOM   2016  H   LYS A 126      22.456  35.423   9.771  1.00 24.40           H  
ATOM   2017  HA  LYS A 126      24.152  37.468  10.358  1.00 25.78           H  
ATOM   2018  HB2 LYS A 126      24.498  35.807  11.958  1.00 28.24           H  
ATOM   2019  HB3 LYS A 126      24.657  34.721  10.805  1.00 28.24           H  
ATOM   2020  HG2 LYS A 126      26.753  35.157  10.627  1.00 38.16           H  
ATOM   2021  HG3 LYS A 126      26.452  36.709  10.433  1.00 38.16           H  
ATOM   2022  HD2 LYS A 126      26.407  36.988  12.722  1.00 48.71           H  
ATOM   2023  HD3 LYS A 126      26.703  35.435  12.918  1.00 48.71           H  
ATOM   2024  HE2 LYS A 126      28.742  35.921  11.594  1.00 50.66           H  
ATOM   2025  HE3 LYS A 126      28.490  37.421  12.077  1.00 50.66           H  
ATOM   2026  HZ1 LYS A 126      29.833  36.328  13.537  1.00 50.26           H  
ATOM   2027  HZ2 LYS A 126      28.597  36.674  14.210  1.00 50.26           H  
ATOM   2028  HZ3 LYS A 126      28.827  35.313  13.772  1.00 50.26           H  
ATOM   2029  N   GLY A 127      25.123  37.393   8.131  1.00 21.67           N  
ANISOU 2029  N   GLY A 127     1435   4545   2253   -541    176  -1432       N  
ATOM   2030  CA  GLY A 127      25.738  37.338   6.821  1.00 22.06           C  
ANISOU 2030  CA  GLY A 127     1455   4634   2291   -551    199  -1461       C  
ATOM   2031  C   GLY A 127      27.231  37.535   6.945  1.00 23.75           C  
ANISOU 2031  C   GLY A 127     1577   4959   2487   -546    186  -1530       C  
ATOM   2032  O   GLY A 127      27.682  38.399   7.710  1.00 23.72           O  
ANISOU 2032  O   GLY A 127     1560   4975   2479   -589    188  -1534       O  
ATOM   2033  H   GLY A 127      25.145  38.173   8.491  1.00 26.00           H  
ATOM   2034  HA2 GLY A 127      25.567  36.476   6.410  1.00 26.47           H  
ATOM   2035  HA3 GLY A 127      25.374  38.035   6.254  1.00 26.47           H  
ATOM   2036  N   ILE A 128      27.999  36.746   6.195  1.00 24.50           N  
ANISOU 2036  N   ILE A 128     1607   5127   2576   -494    173  -1589       N  
ATOM   2037  CA  ILE A 128      29.466  36.827   6.254  1.00 25.85           C  
ANISOU 2037  CA  ILE A 128     1678   5406   2737   -483    158  -1661       C  
ATOM   2038  C   ILE A 128      30.066  36.621   4.872  1.00 31.52           C  
ANISOU 2038  C   ILE A 128     2357   6180   3439   -496    188  -1708       C  
ATOM   2039  O   ILE A 128      29.415  36.058   3.965  1.00 28.83           O  
ANISOU 2039  O   ILE A 128     2054   5804   3097   -485    201  -1698       O  
ATOM   2040  CB  ILE A 128      30.089  35.764   7.211  1.00 30.30           C  
ANISOU 2040  CB  ILE A 128     2166   6025   3323   -370     81  -1709       C  
ATOM   2041  CG1 ILE A 128      29.925  34.340   6.645  1.00 36.14           C  
ANISOU 2041  CG1 ILE A 128     2885   6763   4082   -266     46  -1742       C  
ATOM   2042  CG2 ILE A 128      29.456  35.850   8.613  1.00 36.84           C  
ANISOU 2042  CG2 ILE A 128     3034   6805   4159   -359     41  -1660       C  
ATOM   2043  CD1 ILE A 128      30.636  33.266   7.450  1.00 39.30           C  
ANISOU 2043  CD1 ILE A 128     3209   7207   4518   -146    -43  -1786       C  
ATOM   2044  H   ILE A 128      27.701  36.156   5.645  1.00 29.40           H  
ATOM   2045  HA  ILE A 128      29.724  37.707   6.569  1.00 31.02           H  
ATOM   2046  HB  ILE A 128      31.037  35.950   7.294  1.00 36.37           H  
ATOM   2047 HG12 ILE A 128      28.980  34.119   6.628  1.00 43.36           H  
ATOM   2048 HG13 ILE A 128      30.283  34.320   5.744  1.00 43.36           H  
ATOM   2049 HG21 ILE A 128      29.863  35.179   9.184  1.00 44.21           H  
ATOM   2050 HG22 ILE A 128      29.615  36.735   8.977  1.00 44.21           H  
ATOM   2051 HG23 ILE A 128      28.503  35.688   8.540  1.00 44.21           H  
ATOM   2052 HD11 ILE A 128      30.483  32.405   7.030  1.00 47.16           H  
ATOM   2053 HD12 ILE A 128      31.585  33.462   7.468  1.00 47.16           H  
ATOM   2054 HD13 ILE A 128      30.281  33.261   8.353  1.00 47.16           H  
ATOM   2055  N   ASP A 129      31.310  37.087   4.744  1.00 35.42           N  
ANISOU 2055  N   ASP A 129     3306   6318   3834  -2309    374  -1305       N  
ATOM   2056  CA  ASP A 129      32.134  36.916   3.539  1.00 36.40           C  
ANISOU 2056  CA  ASP A 129     3353   6555   3921  -2351    420  -1363       C  
ATOM   2057  C   ASP A 129      31.548  37.519   2.265  1.00 36.19           C  
ANISOU 2057  C   ASP A 129     3394   6516   3841  -2398    481  -1322       C  
ATOM   2058  O   ASP A 129      31.819  37.042   1.165  1.00 36.47           O  
ANISOU 2058  O   ASP A 129     3370   6632   3853  -2385    504  -1355       O  
ATOM   2059  CB  ASP A 129      32.480  35.438   3.346  1.00 36.24           C  
ANISOU 2059  CB  ASP A 129     3218   6614   3939  -2235    372  -1415       C  
ATOM   2060  CG  ASP A 129      33.578  34.983   4.283  1.00 37.18           C  
ANISOU 2060  CG  ASP A 129     3246   6786   4094  -2230    332  -1484       C  
ATOM   2061  OD1 ASP A 129      34.571  35.714   4.453  1.00 42.95           O  
ANISOU 2061  OD1 ASP A 129     3954   7563   4804  -2340    366  -1527       O  
ATOM   2062  OD2 ASP A 129      33.452  33.891   4.859  1.00 37.69           O  
ANISOU 2062  OD2 ASP A 129     3263   6844   4212  -2117    263  -1493       O  
ATOM   2063  H   ASP A 129      31.715  37.524   5.365  1.00 42.50           H  
ATOM   2064  HA  ASP A 129      32.973  37.375   3.695  1.00 43.68           H  
ATOM   2065  HB2 ASP A 129      31.691  34.901   3.522  1.00 43.49           H  
ATOM   2066  HB3 ASP A 129      32.783  35.298   2.435  1.00 43.49           H  
ATOM   2067  N   PHE A 130      30.806  38.606   2.417  1.00 35.84           N  
ANISOU 2067  N   PHE A 130     3472   6370   3774  -2456    508  -1256       N  
ATOM   2068  CA  PHE A 130      30.329  39.368   1.281  1.00 35.98           C  
ANISOU 2068  CA  PHE A 130     3566   6376   3728  -2529    574  -1224       C  
ATOM   2069  C   PHE A 130      31.372  40.338   0.738  1.00 37.78           C  
ANISOU 2069  C   PHE A 130     3786   6677   3894  -2685    644  -1268       C  
ATOM   2070  O   PHE A 130      32.174  40.912   1.472  1.00 38.75           O  
ANISOU 2070  O   PHE A 130     3896   6804   4023  -2758    647  -1294       O  
ATOM   2071  CB  PHE A 130      29.048  40.117   1.625  1.00 35.04           C  
ANISOU 2071  CB  PHE A 130     3589   6127   3596  -2535    579  -1143       C  
ATOM   2072  CG  PHE A 130      27.855  39.218   1.728  1.00 33.29           C  
ANISOU 2072  CG  PHE A 130     3385   5845   3419  -2394    526  -1092       C  
ATOM   2073  CD1 PHE A 130      27.108  38.898   0.592  1.00 32.67           C  
ANISOU 2073  CD1 PHE A 130     3327   5772   3313  -2359    545  -1065       C  
ATOM   2074  CD2 PHE A 130      27.497  38.662   2.941  1.00 32.32           C  
ANISOU 2074  CD2 PHE A 130     3254   5659   3366  -2295    454  -1069       C  
ATOM   2075  CE1 PHE A 130      26.013  38.060   0.673  1.00 31.09           C  
ANISOU 2075  CE1 PHE A 130     3141   5515   3157  -2230    494  -1017       C  
ATOM   2076  CE2 PHE A 130      26.403  37.825   3.034  1.00 30.78           C  
ANISOU 2076  CE2 PHE A 130     3074   5409   3212  -2168    403  -1020       C  
ATOM   2077  CZ  PHE A 130      25.664  37.512   1.890  1.00 30.14           C  
ANISOU 2077  CZ  PHE A 130     3011   5332   3108  -2133    423   -992       C  
ATOM   2078  H   PHE A 130      30.564  38.925   3.178  1.00 43.00           H  
ATOM   2079  HA  PHE A 130      30.116  38.746   0.567  1.00 43.17           H  
ATOM   2080  HB2 PHE A 130      29.163  40.561   2.480  1.00 42.05           H  
ATOM   2081  HB3 PHE A 130      28.870  40.772   0.932  1.00 42.05           H  
ATOM   2082  HD1 PHE A 130      27.346  39.262  -0.230  1.00 39.20           H  
ATOM   2083  HD2 PHE A 130      27.989  38.864   3.704  1.00 38.78           H  
ATOM   2084  HE1 PHE A 130      25.521  37.857  -0.090  1.00 37.31           H  
ATOM   2085  HE2 PHE A 130      26.166  37.457   3.855  1.00 36.94           H  
ATOM   2086  HZ  PHE A 130      24.925  36.951   1.952  1.00 36.17           H  
ATOM   2087  N   LYS A 131      31.330  40.515  -0.571  1.00 38.25           N  
ANISOU 2087  N   LYS A 131     3851   6789   3892  -2736    698  -1274       N  
ATOM   2088  CA  LYS A 131      32.244  41.405  -1.255  1.00 39.97           C  
ANISOU 2088  CA  LYS A 131     4064   7077   4047  -2884    766  -1309       C  
ATOM   2089  C   LYS A 131      31.687  42.820  -1.204  1.00 40.26           C  
ANISOU 2089  C   LYS A 131     4247   7010   4041  -2990    808  -1247       C  
ATOM   2090  O   LYS A 131      30.502  43.042  -1.467  1.00 39.25           O  
ANISOU 2090  O   LYS A 131     4222   6791   3902  -2958    809  -1181       O  
ATOM   2091  CB  LYS A 131      32.459  40.918  -2.697  1.00 40.39           C  
ANISOU 2091  CB  LYS A 131     4057   7236   4056  -2888    800  -1342       C  
ATOM   2092  CG  LYS A 131      32.831  39.437  -2.739  1.00 39.91           C  
ANISOU 2092  CG  LYS A 131     3863   7260   4043  -2759    750  -1397       C  
ATOM   2093  CD  LYS A 131      33.330  38.960  -4.087  1.00 40.67           C  
ANISOU 2093  CD  LYS A 131     3877   7482   4092  -2773    784  -1451       C  
ATOM   2094  CE  LYS A 131      33.635  37.468  -4.031  1.00 40.12           C  
ANISOU 2094  CE  LYS A 131     3685   7479   4078  -2630    726  -1503       C  
ATOM   2095  H   LYS A 131      30.770  40.124  -1.094  1.00 45.90           H  
ATOM   2096  HA  LYS A 131      33.101  41.397  -0.800  1.00 47.97           H  
ATOM   2097  HB2 LYS A 131      31.639  41.040  -3.201  1.00 48.47           H  
ATOM   2098  HB3 LYS A 131      33.180  41.424  -3.102  1.00 48.47           H  
ATOM   2099  HG2 LYS A 131      33.534  39.274  -2.090  1.00 47.90           H  
ATOM   2100  HG3 LYS A 131      32.048  38.912  -2.511  1.00 47.90           H  
ATOM   2101  HD2 LYS A 131      32.646  39.110  -4.759  1.00 48.80           H  
ATOM   2102  HD3 LYS A 131      34.144  39.433  -4.319  1.00 48.80           H  
ATOM   2103  N   GLU A 132      32.553  43.765  -0.843  1.00 41.80           N  
ANISOU 2103  N   GLU A 132     4450   7215   4217  -3111    838  -1268       N  
ATOM   2104  CA  GLU A 132      32.162  45.156  -0.636  1.00 43.35           C  
ANISOU 2104  CA  GLU A 132     4784   7308   4381  -3212    870  -1214       C  
ATOM   2105  C   GLU A 132      31.607  45.771  -1.924  1.00 43.47           C  
ANISOU 2105  C   GLU A 132     4884   7300   4333  -3273    924  -1171       C  
ATOM   2106  O   GLU A 132      30.773  46.679  -1.888  1.00 49.16           O  
ANISOU 2106  O   GLU A 132     5740   7902   5036  -3304    937  -1105       O  
ATOM   2107  CB  GLU A 132      33.367  45.965  -0.129  1.00 43.90           C  
ANISOU 2107  CB  GLU A 132     4825   7411   4442  -3335    892  -1253       C  
ATOM   2108  H   GLU A 132      33.390  43.621  -0.709  1.00 50.16           H  
ATOM   2109  HA  GLU A 132      31.467  45.193   0.040  1.00 52.03           H  
ATOM   2110  N   ASP A 133      32.081  45.267  -3.056  1.00 45.27           N  
ANISOU 2110  N   ASP A 133     5031   7640   4530  -3285    951  -1208       N  
ATOM   2111  CA  ASP A 133      31.644  45.738  -4.364  1.00 50.48           C  
ANISOU 2111  CA  ASP A 133     5756   8292   5134  -3338    998  -1171       C  
ATOM   2112  C   ASP A 133      30.706  44.730  -5.038  1.00 47.59           C  
ANISOU 2112  C   ASP A 133     5379   7926   4778  -3216    975  -1152       C  
ATOM   2113  O   ASP A 133      30.357  44.876  -6.210  1.00 51.91           O  
ANISOU 2113  O   ASP A 133     5959   8481   5284  -3240   1007  -1127       O  
ATOM   2114  CB  ASP A 133      32.868  45.999  -5.254  1.00 56.21           C  
ANISOU 2114  CB  ASP A 133     6401   9146   5809  -3455   1051  -1225       C  
ATOM   2115  CG  ASP A 133      33.766  44.765  -5.408  1.00 60.34           C  
ANISOU 2115  CG  ASP A 133     6756   9821   6349  -3397   1034  -1312       C  
ATOM   2116  OD1 ASP A 133      34.055  44.091  -4.394  1.00 61.41           O  
ANISOU 2116  OD1 ASP A 133     6823   9969   6541  -3321    985  -1348       O  
ATOM   2117  OD2 ASP A 133      34.181  44.465  -6.549  1.00 70.01           O  
ANISOU 2117  OD2 ASP A 133     7917  11151   7534  -3425   1066  -1345       O  
ATOM   2118  H   ASP A 133      32.668  44.639  -3.093  1.00 54.33           H  
ATOM   2119  HA  ASP A 133      31.164  46.574  -4.258  1.00 60.58           H  
ATOM   2120  HB2 ASP A 133      32.566  46.261  -6.138  1.00 67.45           H  
ATOM   2121  HB3 ASP A 133      33.399  46.709  -4.861  1.00 67.45           H  
ATOM   2122  N   GLY A 134      30.297  43.701  -4.302  1.00 40.44           N  
ANISOU 2122  N   GLY A 134     4426   7010   3929  -3083    916  -1160       N  
ATOM   2123  CA  GLY A 134      29.426  42.678  -4.858  1.00 39.06           C  
ANISOU 2123  CA  GLY A 134     4234   6836   3772  -2961    886  -1142       C  
ATOM   2124  C   GLY A 134      28.023  43.198  -5.133  1.00 38.04           C  
ANISOU 2124  C   GLY A 134     4249   6569   3635  -2939    889  -1053       C  
ATOM   2125  O   GLY A 134      27.727  44.361  -4.876  1.00 38.41           O  
ANISOU 2125  O   GLY A 134     4413   6518   3664  -3014    913  -1006       O  
ATOM   2126  H   GLY A 134      30.510  43.575  -3.479  1.00 48.53           H  
ATOM   2127  HA2 GLY A 134      29.801  42.352  -5.691  1.00 46.87           H  
ATOM   2128  HA3 GLY A 134      29.363  41.935  -4.238  1.00 46.87           H  
ATOM   2129  N   ASN A 135      27.152  42.341  -5.660  1.00 36.78           N  
ANISOU 2129  N   ASN A 135     4083   6399   3492  -2832    862  -1029       N  
ATOM   2130  CA  ASN A 135      25.799  42.757  -5.960  1.00 35.78           C  
ANISOU 2130  CA  ASN A 135     4088   6142   3364  -2801    861   -944       C  
ATOM   2131  C   ASN A 135      24.954  43.000  -4.699  1.00 34.66           C  
ANISOU 2131  C   ASN A 135     4032   5871   3266  -2744    822   -894       C  
ATOM   2132  O   ASN A 135      23.941  43.684  -4.770  1.00 34.14           O  
ANISOU 2132  O   ASN A 135     4094   5680   3196  -2741    828   -824       O  
ATOM   2133  CB  ASN A 135      25.109  41.711  -6.829  1.00 34.72           C  
ANISOU 2133  CB  ASN A 135     3916   6034   3243  -2698    839   -932       C  
ATOM   2134  CG  ASN A 135      25.691  41.641  -8.239  1.00 35.79           C  
ANISOU 2134  CG  ASN A 135     3997   6275   3328  -2757    883   -965       C  
ATOM   2135  OD1 ASN A 135      26.253  42.614  -8.746  1.00 37.19           O  
ANISOU 2135  OD1 ASN A 135     4209   6465   3456  -2881    936   -967       O  
ATOM   2136  ND2 ASN A 135      25.540  40.489  -8.879  1.00 35.16           N  
ANISOU 2136  ND2 ASN A 135     3831   6269   3260  -2667    858   -990       N  
ATOM   2137  H   ASN A 135      27.325  41.521  -5.851  1.00 44.13           H  
ATOM   2138  HA  ASN A 135      25.831  43.587  -6.461  1.00 42.93           H  
ATOM   2139  HB2 ASN A 135      25.212  40.839  -6.418  1.00 41.66           H  
ATOM   2140  HB3 ASN A 135      24.167  41.934  -6.904  1.00 41.66           H  
ATOM   2141 HD21 ASN A 135      25.133  39.834  -8.497  1.00 42.19           H  
ATOM   2142 HD22 ASN A 135      25.850  40.396  -9.676  1.00 42.19           H  
ATOM   2143  N   ILE A 136      25.355  42.438  -3.559  1.00 34.32           N  
ANISOU 2143  N   ILE A 136     3918   5856   3268  -2693    780   -929       N  
ATOM   2144  CA  ILE A 136      24.559  42.601  -2.331  1.00 33.28           C  
ANISOU 2144  CA  ILE A 136     3858   5608   3177  -2635    740   -883       C  
ATOM   2145  C   ILE A 136      24.970  43.891  -1.621  1.00 34.31           C  
ANISOU 2145  C   ILE A 136     4065   5684   3286  -2745    768   -879       C  
ATOM   2146  O   ILE A 136      24.206  44.844  -1.590  1.00 34.20           O  
ANISOU 2146  O   ILE A 136     4184   5555   3255  -2775    784   -822       O  
ATOM   2147  CB  ILE A 136      24.653  41.384  -1.390  1.00 32.32           C  
ANISOU 2147  CB  ILE A 136     3635   5524   3123  -2517    674   -909       C  
ATOM   2148  CG1 ILE A 136      23.895  40.177  -1.965  1.00 31.01           C  
ANISOU 2148  CG1 ILE A 136     3423   5373   2987  -2391    636   -890       C  
ATOM   2149  CG2 ILE A 136      23.979  41.683  -0.040  1.00 31.51           C  
ANISOU 2149  CG2 ILE A 136     3604   5309   3058  -2477    636   -866       C  
ATOM   2150  CD1 ILE A 136      24.512  39.553  -3.197  1.00 31.59           C  
ANISOU 2150  CD1 ILE A 136     3402   5567   3035  -2396    657   -940       C  
ATOM   2151  H   ILE A 136      26.069  41.967  -3.466  1.00 41.19           H  
ATOM   2152  HA  ILE A 136      23.627  42.695  -2.584  1.00 39.93           H  
ATOM   2153  HB  ILE A 136      25.584  41.150  -1.247  1.00 38.79           H  
ATOM   2154 HG12 ILE A 136      23.847  39.490  -1.283  1.00 37.21           H  
ATOM   2155 HG13 ILE A 136      22.998  40.462  -2.201  1.00 37.21           H  
ATOM   2156 HG21 ILE A 136      24.054  40.901   0.530  1.00 37.81           H  
ATOM   2157 HG22 ILE A 136      24.424  42.439   0.374  1.00 37.81           H  
ATOM   2158 HG23 ILE A 136      23.045  41.892  -0.194  1.00 37.81           H  
ATOM   2159 HD11 ILE A 136      23.963  38.805  -3.480  1.00 37.91           H  
ATOM   2160 HD12 ILE A 136      24.554  40.219  -3.901  1.00 37.91           H  
ATOM   2161 HD13 ILE A 136      25.406  39.244  -2.979  1.00 37.91           H  
ATOM   2162  N   LEU A 137      26.188  43.942  -1.096  1.00 40.34           N  
ANISOU 2162  N   LEU A 137     4747   6527   4054  -2803    771   -940       N  
ATOM   2163  CA  LEU A 137      26.645  45.146  -0.385  1.00 41.29           C  
ANISOU 2163  CA  LEU A 137     4933   6599   4158  -2908    794   -939       C  
ATOM   2164  C   LEU A 137      26.717  46.343  -1.330  1.00 38.62           C  
ANISOU 2164  C   LEU A 137     4684   6232   3758  -3030    856   -915       C  
ATOM   2165  O   LEU A 137      26.571  47.482  -0.893  1.00 38.11           O  
ANISOU 2165  O   LEU A 137     4724   6079   3679  -3098    872   -884       O  
ATOM   2166  CB  LEU A 137      27.998  44.919   0.306  1.00 39.07           C  
ANISOU 2166  CB  LEU A 137     4536   6413   3897  -2946    783  -1011       C  
ATOM   2167  CG  LEU A 137      28.030  43.936   1.490  1.00 36.46           C  
ANISOU 2167  CG  LEU A 137     4128   6089   3637  -2835    714  -1031       C  
ATOM   2168  CD1 LEU A 137      29.452  43.843   2.061  1.00 44.77           C  
ANISOU 2168  CD1 LEU A 137     5073   7230   4708  -2884    707  -1102       C  
ATOM   2169  CD2 LEU A 137      27.020  44.313   2.588  1.00 36.41           C  
ANISOU 2169  CD2 LEU A 137     4226   5952   3657  -2788    681   -974       C  
ATOM   2170  H   LEU A 137      26.767  43.307  -1.134  1.00 48.41           H  
ATOM   2171  HA  LEU A 137      25.997  45.358   0.306  1.00 49.55           H  
ATOM   2172  HB2 LEU A 137      28.622  44.585  -0.358  1.00 46.89           H  
ATOM   2173  HB3 LEU A 137      28.314  45.774   0.637  1.00 46.89           H  
ATOM   2174  HG  LEU A 137      27.789  43.054   1.164  1.00 43.76           H  
ATOM   2175 HD11 LEU A 137      29.454  43.221   2.805  1.00 53.72           H  
ATOM   2176 HD12 LEU A 137      30.051  43.530   1.365  1.00 53.72           H  
ATOM   2177 HD13 LEU A 137      29.728  44.722   2.364  1.00 53.72           H  
ATOM   2178 HD21 LEU A 137      27.079  43.665   3.307  1.00 43.69           H  
ATOM   2179 HD22 LEU A 137      27.232  45.199   2.921  1.00 43.69           H  
ATOM   2180 HD23 LEU A 137      26.126  44.307   2.210  1.00 43.69           H  
ATOM   2181  N   GLY A 138      26.909  46.077  -2.625  1.00 37.99           N  
ANISOU 2181  N   GLY A 138     4567   6224   3646  -3051    887   -926       N  
ATOM   2182  CA  GLY A 138      26.932  47.126  -3.631  1.00 39.08           C  
ANISOU 2182  CA  GLY A 138     4785   6334   3728  -3157    942   -897       C  
ATOM   2183  C   GLY A 138      25.569  47.557  -4.147  1.00 38.20           C  
ANISOU 2183  C   GLY A 138     4808   6093   3611  -3115    944   -815       C  
ATOM   2184  O   GLY A 138      25.486  48.436  -5.008  1.00 39.04           O  
ANISOU 2184  O   GLY A 138     4991   6162   3679  -3192    986   -782       O  
ATOM   2185  H   GLY A 138      27.029  45.287  -2.943  1.00 45.59           H  
ATOM   2186  HA2 GLY A 138      27.370  47.907  -3.259  1.00 46.89           H  
ATOM   2187  HA3 GLY A 138      27.455  46.822  -4.389  1.00 46.89           H  
ATOM   2188  N   HIS A 139      24.509  46.933  -3.635  1.00 36.55           N  
ANISOU 2188  N   HIS A 139     4627   5815   3444  -2991    898   -782       N  
ATOM   2189  CA  HIS A 139      23.127  47.279  -4.001  1.00 35.57           C  
ANISOU 2189  CA  HIS A 139     4630   5558   3326  -2932    893   -704       C  
ATOM   2190  C   HIS A 139      22.901  47.342  -5.520  1.00 35.89           C  
ANISOU 2190  C   HIS A 139     4689   5611   3336  -2951    926   -678       C  
ATOM   2191  O   HIS A 139      22.472  48.362  -6.057  1.00 36.39           O  
ANISOU 2191  O   HIS A 139     4864   5585   3377  -2998    955   -627       O  
ATOM   2192  CB  HIS A 139      22.728  48.610  -3.371  1.00 35.95           C  
ANISOU 2192  CB  HIS A 139     4816   5478   3367  -2982    902   -660       C  
ATOM   2193  CG  HIS A 139      22.678  48.578  -1.877  1.00 35.45           C  
ANISOU 2193  CG  HIS A 139     4755   5378   3336  -2948    865   -672       C  
ATOM   2194  ND1 HIS A 139      21.569  48.151  -1.180  1.00 33.92           N  
ANISOU 2194  ND1 HIS A 139     4604   5102   3182  -2832    821   -634       N  
ATOM   2195  CD2 HIS A 139      23.597  48.928  -0.946  1.00 36.31           C  
ANISOU 2195  CD2 HIS A 139     4828   5522   3445  -3015    865   -714       C  
ATOM   2196  CE1 HIS A 139      21.808  48.234   0.119  1.00 33.87           C  
ANISOU 2196  CE1 HIS A 139     4588   5084   3196  -2830    796   -654       C  
ATOM   2197  NE2 HIS A 139      23.031  48.708   0.287  1.00 35.29           N  
ANISOU 2197  NE2 HIS A 139     4722   5332   3356  -2939    821   -702       N  
ATOM   2198  H   HIS A 139      24.562  46.293  -3.064  1.00 43.85           H  
ATOM   2199  HA  HIS A 139      22.535  46.598  -3.645  1.00 42.68           H  
ATOM   2200  HB2 HIS A 139      23.374  49.285  -3.632  1.00 43.15           H  
ATOM   2201  HB3 HIS A 139      21.847  48.857  -3.693  1.00 43.15           H  
ATOM   2202  HD1 HIS A 139      20.837  47.871  -1.533  1.00 40.70           H  
ATOM   2203  HD2 HIS A 139      24.450  49.258  -1.110  1.00 43.57           H  
ATOM   2204  HE1 HIS A 139      21.215  48.004   0.798  1.00 40.64           H  
ATOM   2205  HE2 HIS A 139      23.413  48.848   1.045  1.00 42.35           H  
ATOM   2206  N   LYS A 140      23.182  46.239  -6.195  1.00 35.61           N  
ANISOU 2206  N   LYS A 140     4541   5685   3302  -2908    920   -714       N  
ATOM   2207  CA  LYS A 140      23.080  46.196  -7.647  1.00 35.99           C  
ANISOU 2207  CA  LYS A 140     4589   5763   3321  -2927    952   -697       C  
ATOM   2208  C   LYS A 140      21.891  45.347  -8.093  1.00 34.40           C  
ANISOU 2208  C   LYS A 140     4401   5514   3153  -2797    918   -653       C  
ATOM   2209  O   LYS A 140      21.689  45.132  -9.286  1.00 34.49           O  
ANISOU 2209  O   LYS A 140     4406   5549   3149  -2790    937   -636       O  
ATOM   2210  CB  LYS A 140      24.384  45.654  -8.223  1.00 37.12           C  
ANISOU 2210  CB  LYS A 140     4592   6079   3434  -2988    976   -776       C  
ATOM   2211  CG  LYS A 140      25.626  46.370  -7.687  1.00 38.67           C  
ANISOU 2211  CG  LYS A 140     4757   6333   3604  -3109   1005   -825       C  
ATOM   2212  CD  LYS A 140      26.911  45.853  -8.340  1.00 39.89           C  
ANISOU 2212  CD  LYS A 140     4769   6659   3727  -3168   1031   -903       C  
ATOM   2213  CE  LYS A 140      28.162  46.535  -7.761  1.00 41.44           C  
ANISOU 2213  CE  LYS A 140     4928   6912   3903  -3286   1057   -952       C  
ATOM   2214  NZ  LYS A 140      29.431  46.008  -8.389  1.00 43.28           N  
ANISOU 2214  NZ  LYS A 140     5017   7319   4107  -3337   1083  -1032       N  
ATOM   2215  H   LYS A 140      23.433  45.498  -5.837  1.00 42.73           H  
ATOM   2216  HA  LYS A 140      22.951  47.097  -7.984  1.00 43.19           H  
ATOM   2217  HB2 LYS A 140      24.461  44.714  -7.998  1.00 44.55           H  
ATOM   2218  HB3 LYS A 140      24.371  45.763  -9.187  1.00 44.55           H  
ATOM   2219  HG2 LYS A 140      25.553  47.319  -7.873  1.00 46.41           H  
ATOM   2220  HG3 LYS A 140      25.692  46.220  -6.731  1.00 46.41           H  
ATOM   2221  HD2 LYS A 140      26.986  44.899  -8.184  1.00 47.86           H  
ATOM   2222  HD3 LYS A 140      26.880  46.035  -9.292  1.00 47.86           H  
ATOM   2223  HE2 LYS A 140      28.114  47.489  -7.931  1.00 49.72           H  
ATOM   2224  HE3 LYS A 140      28.205  46.367  -6.806  1.00 49.72           H  
ATOM   2225  HZ1 LYS A 140      29.502  45.133  -8.243  1.00 51.93           H  
ATOM   2226  HZ2 LYS A 140      29.419  46.154  -9.267  1.00 51.93           H  
ATOM   2227  HZ3 LYS A 140      30.138  46.418  -8.037  1.00 51.93           H  
ATOM   2228  N   LEU A 141      21.093  44.863  -7.139  1.00 32.96           N  
ANISOU 2228  N   LEU A 141     4239   5265   3020  -2693    868   -632       N  
ATOM   2229  CA  LEU A 141      19.934  44.046  -7.493  1.00 31.42           C  
ANISOU 2229  CA  LEU A 141     4057   5020   2863  -2568    832   -586       C  
ATOM   2230  C   LEU A 141      18.756  44.945  -7.815  1.00 31.04           C  
ANISOU 2230  C   LEU A 141     4160   4812   2820  -2545    841   -499       C  
ATOM   2231  O   LEU A 141      18.532  45.940  -7.143  1.00 31.30           O  
ANISOU 2231  O   LEU A 141     4290   4750   2851  -2577    847   -474       O  
ATOM   2232  CB  LEU A 141      19.561  43.099  -6.342  1.00 30.07           C  
ANISOU 2232  CB  LEU A 141     3835   4847   2743  -2462    772   -595       C  
ATOM   2233  CG  LEU A 141      20.654  42.136  -5.865  1.00 30.32           C  
ANISOU 2233  CG  LEU A 141     3712   5024   2783  -2456    752   -678       C  
ATOM   2234  CD1 LEU A 141      20.032  41.118  -4.936  1.00 31.59           C  
ANISOU 2234  CD1 LEU A 141     3834   5166   3004  -2329    687   -667       C  
ATOM   2235  CD2 LEU A 141      21.343  41.439  -7.035  1.00 36.88           C  
ANISOU 2235  CD2 LEU A 141     4435   5990   3589  -2469    770   -727       C  
ATOM   2236  H   LEU A 141      21.198  44.991  -6.295  1.00 39.55           H  
ATOM   2237  HA  LEU A 141      20.140  43.513  -8.278  1.00 37.71           H  
ATOM   2238  HB2 LEU A 141      19.300  43.639  -5.579  1.00 36.08           H  
ATOM   2239  HB3 LEU A 141      18.806  42.560  -6.625  1.00 36.08           H  
ATOM   2240  HG  LEU A 141      21.324  42.632  -5.368  1.00 36.38           H  
ATOM   2241 HD11 LEU A 141      20.721  40.506  -4.632  1.00 37.91           H  
ATOM   2242 HD12 LEU A 141      19.641  41.580  -4.178  1.00 37.91           H  
ATOM   2243 HD13 LEU A 141      19.345  40.630  -5.417  1.00 37.91           H  
ATOM   2244 HD21 LEU A 141      22.025  40.842  -6.690  1.00 44.26           H  
ATOM   2245 HD22 LEU A 141      20.683  40.934  -7.535  1.00 44.26           H  
ATOM   2246 HD23 LEU A 141      21.750  42.110  -7.607  1.00 44.26           H  
ATOM   2247  N   GLU A 142      17.989  44.585  -8.833  1.00 30.42           N  
ANISOU 2247  N   GLU A 142     4102   4703   2753  -2482    840   -455       N  
ATOM   2248  CA  GLU A 142      16.770  45.315  -9.147  1.00 29.90           C  
ANISOU 2248  CA  GLU A 142     4173   4483   2705  -2433    841   -371       C  
ATOM   2249  C   GLU A 142      15.724  45.082  -8.057  1.00 28.44           C  
ANISOU 2249  C   GLU A 142     4037   4196   2572  -2324    790   -335       C  
ATOM   2250  O   GLU A 142      15.714  44.034  -7.431  1.00 27.52           O  
ANISOU 2250  O   GLU A 142     3839   4132   2485  -2260    750   -360       O  
ATOM   2251  CB  GLU A 142      16.206  44.854 -10.494  1.00 29.53           C  
ANISOU 2251  CB  GLU A 142     4123   4435   2664  -2379    848   -332       C  
ATOM   2252  CG  GLU A 142      17.152  45.156 -11.682  1.00 31.05           C  
ANISOU 2252  CG  GLU A 142     4276   4722   2800  -2487    902   -359       C  
ATOM   2253  CD  GLU A 142      16.544  44.876 -13.068  1.00 30.82           C  
ANISOU 2253  CD  GLU A 142     4261   4678   2771  -2439    916   -311       C  
ATOM   2254  OE1 GLU A 142      15.569  44.107 -13.189  1.00 29.43           O  
ANISOU 2254  OE1 GLU A 142     4086   4455   2640  -2317    880   -273       O  
ATOM   2255  OE2 GLU A 142      17.065  45.437 -14.059  1.00 35.08           O  
ANISOU 2255  OE2 GLU A 142     4809   5254   3265  -2525    963   -310       O  
ATOM   2256  H   GLU A 142      18.151  43.923  -9.358  1.00 36.50           H  
ATOM   2257  HA  GLU A 142      16.960  46.265  -9.197  1.00 35.88           H  
ATOM   2258  HB2 GLU A 142      16.061  43.895 -10.463  1.00 35.44           H  
ATOM   2259  HB3 GLU A 142      15.366  45.310 -10.657  1.00 35.44           H  
ATOM   2260  HG2 GLU A 142      17.397  46.094 -11.652  1.00 37.26           H  
ATOM   2261  HG3 GLU A 142      17.947  44.607 -11.592  1.00 37.26           H  
ATOM   2262  N   TYR A 143      14.837  46.056  -7.882  1.00 28.27           N  
ANISOU 2262  N   TYR A 143     4144   4035   2563  -2299    791   -275       N  
ATOM   2263  CA  TYR A 143      13.744  45.951  -6.926  1.00 26.96           C  
ANISOU 2263  CA  TYR A 143     4033   3766   2445  -2191    746   -236       C  
ATOM   2264  C   TYR A 143      12.569  45.223  -7.568  1.00 30.59           C  
ANISOU 2264  C   TYR A 143     4501   4172   2950  -2060    718   -179       C  
ATOM   2265  O   TYR A 143      11.563  45.815  -7.958  1.00 25.33           O  
ANISOU 2265  O   TYR A 143     3930   3393   2301  -2003    718   -120       O  
ATOM   2266  CB  TYR A 143      13.321  47.330  -6.422  1.00 27.44           C  
ANISOU 2266  CB  TYR A 143     4219   3707   2498  -2216    758   -206       C  
ATOM   2267  CG  TYR A 143      12.343  47.258  -5.260  1.00 26.25           C  
ANISOU 2267  CG  TYR A 143     4115   3469   2390  -2115    714   -179       C  
ATOM   2268  CD1 TYR A 143      12.765  46.870  -3.987  1.00 26.01           C  
ANISOU 2268  CD1 TYR A 143     4037   3481   2364  -2124    690   -219       C  
ATOM   2269  CD2 TYR A 143      11.017  47.594  -5.434  1.00 25.65           C  
ANISOU 2269  CD2 TYR A 143     4140   3276   2328  -2034    701   -126       C  
ATOM   2270  CE1 TYR A 143      11.881  46.813  -2.934  1.00 25.00           C  
ANISOU 2270  CE1 TYR A 143     3951   3277   2271  -2037    652   -194       C  
ATOM   2271  CE2 TYR A 143      10.112  47.522  -4.368  1.00 24.68           C  
ANISOU 2271  CE2 TYR A 143     4061   3082   2236  -1948    663   -108       C  
ATOM   2272  CZ  TYR A 143      10.559  47.136  -3.136  1.00 24.33           C  
ANISOU 2272  CZ  TYR A 143     3959   3079   2207  -1948    639   -138       C  
ATOM   2273  OH  TYR A 143       9.666  47.077  -2.094  1.00 23.45           O  
ANISOU 2273  OH  TYR A 143     3889   2899   2120  -1867    603   -119       O  
ATOM   2274  H   TYR A 143      14.848  46.800  -8.314  1.00 33.93           H  
ATOM   2275  HA  TYR A 143      14.040  45.430  -6.164  1.00 32.35           H  
ATOM   2276  HB2 TYR A 143      14.108  47.811  -6.122  1.00 32.92           H  
ATOM   2277  HB3 TYR A 143      12.892  47.813  -7.145  1.00 32.92           H  
ATOM   2278  HD1 TYR A 143      13.657  46.647  -3.849  1.00 31.21           H  
ATOM   2279  HD2 TYR A 143      10.715  47.851  -6.275  1.00 30.77           H  
ATOM   2280  HE1 TYR A 143      12.174  46.546  -2.092  1.00 30.00           H  
ATOM   2281  HE2 TYR A 143       9.218  47.746  -4.495  1.00 29.62           H  
ATOM   2282  HH  TYR A 143       8.900  47.298  -2.359  1.00 28.13           H  
ATOM   2283  N   ASN A 144      12.714  43.909  -7.640  1.00 24.88           N  
ANISOU 2283  N   ASN A 144     3671   3535   2245  -2012    691   -202       N  
ATOM   2284  CA  ASN A 144      11.673  43.040  -8.161  1.00 23.56           C  
ANISOU 2284  CA  ASN A 144     3495   3331   2125  -1886    659   -152       C  
ATOM   2285  C   ASN A 144      12.009  41.616  -7.747  1.00 22.79           C  
ANISOU 2285  C   ASN A 144     3273   3341   2047  -1847    619   -192       C  
ATOM   2286  O   ASN A 144      12.962  41.380  -6.979  1.00 23.24           O  
ANISOU 2286  O   ASN A 144     3256   3489   2085  -1906    613   -256       O  
ATOM   2287  CB  ASN A 144      11.519  43.177  -9.679  1.00 23.97           C  
ANISOU 2287  CB  ASN A 144     3564   3380   2162  -1889    692   -121       C  
ATOM   2288  CG  ASN A 144      12.828  43.033 -10.419  1.00 26.61           C  
ANISOU 2288  CG  ASN A 144     3815   3853   2442  -2003    732   -183       C  
ATOM   2289  OD1 ASN A 144      13.704  42.264 -10.015  1.00 25.37           O  
ANISOU 2289  OD1 ASN A 144     3548   3819   2274  -2036    721   -249       O  
ATOM   2290  ND2 ASN A 144      12.977  43.781 -11.519  1.00 26.24           N  
ANISOU 2290  ND2 ASN A 144     3816   3793   2362  -2061    778   -163       N  
ATOM   2291  H   ASN A 144      13.421  43.489  -7.388  1.00 29.85           H  
ATOM   2292  HA  ASN A 144      10.827  43.280  -7.752  1.00 28.27           H  
ATOM   2293  HB2 ASN A 144      10.918  42.486  -9.998  1.00 28.76           H  
ATOM   2294  HB3 ASN A 144      11.156  44.053  -9.882  1.00 28.76           H  
ATOM   2295 HD21 ASN A 144      12.346  44.308 -11.770  1.00 31.49           H  
ATOM   2296 HD22 ASN A 144      13.705  43.735 -11.975  1.00 31.49           H  
ATOM   2297  N   TYR A 145      11.214  40.669  -8.223  1.00 22.88           N  
ANISOU 2297  N   TYR A 145     3255   3340   2097  -1741    587   -153       N  
ATOM   2298  CA  TYR A 145      11.270  39.318  -7.686  1.00 25.74           C  
ANISOU 2298  CA  TYR A 145     3509   3782   2488  -1681    535   -177       C  
ATOM   2299  C   TYR A 145      10.726  38.308  -8.672  1.00 25.36           C  
ANISOU 2299  C   TYR A 145     3412   3758   2464  -1599    517   -148       C  
ATOM   2300  O   TYR A 145       9.716  38.536  -9.339  1.00 21.65           O  
ANISOU 2300  O   TYR A 145     3021   3187   2019  -1529    521    -77       O  
ATOM   2301  CB  TYR A 145      10.529  39.207  -6.337  1.00 20.25           C  
ANISOU 2301  CB  TYR A 145     2849   3009   1836  -1609    487   -148       C  
ATOM   2302  CG  TYR A 145      11.239  38.241  -5.420  1.00 19.45           C  
ANISOU 2302  CG  TYR A 145     2628   3020   1743  -1611    447   -205       C  
ATOM   2303  CD1 TYR A 145      12.363  38.638  -4.712  1.00 23.92           C  
ANISOU 2303  CD1 TYR A 145     3157   3654   2276  -1702    465   -271       C  
ATOM   2304  CD2 TYR A 145      10.822  36.921  -5.302  1.00 18.31           C  
ANISOU 2304  CD2 TYR A 145     2399   2916   1641  -1515    389   -193       C  
ATOM   2305  CE1 TYR A 145      13.047  37.751  -3.896  1.00 20.31           C  
ANISOU 2305  CE1 TYR A 145     2583   3298   1836  -1685    426   -322       C  
ATOM   2306  CE2 TYR A 145      11.500  36.035  -4.500  1.00 18.18           C  
ANISOU 2306  CE2 TYR A 145     2264   3001   1641  -1500    347   -244       C  
ATOM   2307  CZ  TYR A 145      12.612  36.449  -3.807  1.00 19.18           C  
ANISOU 2307  CZ  TYR A 145     2356   3188   1742  -1578    366   -309       C  
ATOM   2308  OH  TYR A 145      13.309  35.570  -3.007  1.00 22.30           O  
ANISOU 2308  OH  TYR A 145     2631   3671   2170  -1541    320   -357       O  
ATOM   2309  H   TYR A 145      10.638  40.781  -8.852  1.00 27.45           H  
ATOM   2310  HA  TYR A 145      12.199  39.093  -7.525  1.00 30.89           H  
ATOM   2311  HB2 TYR A 145      10.506  40.076  -5.908  1.00 24.30           H  
ATOM   2312  HB3 TYR A 145       9.629  38.880  -6.489  1.00 24.30           H  
ATOM   2313  HD1 TYR A 145      12.663  39.515  -4.786  1.00 28.70           H  
ATOM   2314  HD2 TYR A 145      10.078  36.631  -5.780  1.00 21.97           H  
ATOM   2315  HE1 TYR A 145      13.802  38.028  -3.429  1.00 24.37           H  
ATOM   2316  HE2 TYR A 145      11.211  35.154  -4.432  1.00 21.81           H  
ATOM   2317  HH  TYR A 145      12.951  34.811  -3.034  1.00 26.76           H  
ATOM   2318  N   ASN A 146      11.413  37.181  -8.741  1.00 20.94           N  
ANISOU 2318  N   ASN A 146     2717   3338   1900  -1597    492   -205       N  
ATOM   2319  CA  ASN A 146      11.089  36.143  -9.703  1.00 19.26           C  
ANISOU 2319  CA  ASN A 146     2437   3179   1702  -1529    474   -192       C  
ATOM   2320  C   ASN A 146      10.195  35.076  -9.090  1.00 20.97           C  
ANISOU 2320  C   ASN A 146     2619   3370   1977  -1408    402   -152       C  
ATOM   2321  O   ASN A 146       9.728  35.228  -7.971  1.00 23.43           O  
ANISOU 2321  O   ASN A 146     2973   3608   2320  -1377    372   -126       O  
ATOM   2322  CB  ASN A 146      12.391  35.571 -10.253  1.00 25.69           C  
ANISOU 2322  CB  ASN A 146     3115   4172   2475  -1588    487   -285       C  
ATOM   2323  CG  ASN A 146      12.911  36.379 -11.433  1.00 39.91           C  
ANISOU 2323  CG  ASN A 146     4950   5991   4221  -1679    556   -296       C  
ATOM   2324  OD1 ASN A 146      12.178  36.622 -12.391  1.00 41.81           O  
ANISOU 2324  OD1 ASN A 146     5262   6159   4466  -1649    578   -233       O  
ATOM   2325  ND2 ASN A 146      14.164  36.829 -11.354  1.00 37.65           N  
ANISOU 2325  ND2 ASN A 146     4619   5798   3888  -1788    591   -371       N  
ATOM   2326  H   ASN A 146      12.082  36.991  -8.235  1.00 25.13           H  
ATOM   2327  HA  ASN A 146      10.606  36.543 -10.442  1.00 23.11           H  
ATOM   2328  HB2 ASN A 146      13.065  35.584  -9.556  1.00 30.83           H  
ATOM   2329  HB3 ASN A 146      12.237  34.661 -10.553  1.00 30.83           H  
ATOM   2330 HD21 ASN A 146      14.639  36.658 -10.658  1.00 45.18           H  
ATOM   2331 HD22 ASN A 146      14.497  37.289 -11.999  1.00 45.18           H  
ATOM   2332  N   HIS A 147       9.947  34.005  -9.828  1.00 17.14           N  
ANISOU 2332  N   HIS A 147     2055   2950   1508  -1340    374   -146       N  
ATOM   2333  CA  HIS A 147       9.051  32.941  -9.370  1.00 15.70           C  
ANISOU 2333  CA  HIS A 147     1834   2748   1383  -1222    301   -101       C  
ATOM   2334  C   HIS A 147       9.874  31.675  -9.274  1.00 20.73           C  
ANISOU 2334  C   HIS A 147     2296   3550   2032  -1183    248   -180       C  
ATOM   2335  O   HIS A 147      10.699  31.400 -10.166  1.00 16.52           O  
ANISOU 2335  O   HIS A 147     1682   3133   1462  -1210    272   -244       O  
ATOM   2336  CB  HIS A 147       7.920  32.733 -10.367  1.00 14.93           C  
ANISOU 2336  CB  HIS A 147     1798   2570   1306  -1142    303    -16       C  
ATOM   2337  CG  HIS A 147       8.394  32.671 -11.779  1.00 21.39           C  
ANISOU 2337  CG  HIS A 147     2580   3466   2081  -1173    348    -43       C  
ATOM   2338  ND1 HIS A 147       8.623  31.482 -12.431  1.00 26.08           N  
ANISOU 2338  ND1 HIS A 147     3042   4196   2673  -1124    313    -79       N  
ATOM   2339  CD2 HIS A 147       8.709  33.650 -12.652  1.00 25.78           C  
ANISOU 2339  CD2 HIS A 147     3208   3992   2595  -1244    419    -44       C  
ATOM   2340  CE1 HIS A 147       9.054  31.731 -13.653  1.00 27.20           C  
ANISOU 2340  CE1 HIS A 147     3181   4386   2769  -1167    368   -101       C  
ATOM   2341  NE2 HIS A 147       9.104  33.041 -13.818  1.00 24.52           N  
ANISOU 2341  NE2 HIS A 147     2966   3944   2405  -1243    432    -76       N  
ATOM   2342  H   HIS A 147      10.286  33.865 -10.605  1.00 20.57           H  
ATOM   2343  HA  HIS A 147       8.682  33.156  -8.499  1.00 18.84           H  
ATOM   2344  HB2 HIS A 147       7.472  31.897 -10.164  1.00 17.92           H  
ATOM   2345  HB3 HIS A 147       7.295  33.471 -10.293  1.00 17.92           H  
ATOM   2346  HD1 HIS A 147       8.507  30.700 -12.094  1.00 31.30           H  
ATOM   2347  HD2 HIS A 147       8.655  34.566 -12.499  1.00 30.94           H  
ATOM   2348  HE1 HIS A 147       9.269  31.093 -14.295  1.00 32.65           H  
ATOM   2349  HE2 HIS A 147       9.355  33.445 -14.534  1.00 29.42           H  
ATOM   2350  N   HIS A 148       9.664  30.912  -8.202  1.00 14.83           N  
ANISOU 2350  N   HIS A 148     1626   2363   1646   -423   -347   -115       N  
ATOM   2351  CA  HIS A 148      10.576  29.830  -7.859  1.00 14.31           C  
ANISOU 2351  CA  HIS A 148     1611   2314   1513   -373   -311   -334       C  
ATOM   2352  C   HIS A 148       9.852  28.536  -7.549  1.00 16.31           C  
ANISOU 2352  C   HIS A 148     1891   2533   1772   -356   -403   -330       C  
ATOM   2353  O   HIS A 148       8.631  28.518  -7.466  1.00 14.49           O  
ANISOU 2353  O   HIS A 148     1614   2271   1620   -383   -498   -151       O  
ATOM   2354  CB  HIS A 148      11.443  30.266  -6.688  1.00 13.49           C  
ANISOU 2354  CB  HIS A 148     1450   2186   1492   -265   -213   -437       C  
ATOM   2355  CG  HIS A 148      12.221  31.515  -6.974  1.00 14.60           C  
ANISOU 2355  CG  HIS A 148     1573   2351   1622   -310   -129   -447       C  
ATOM   2356  ND1 HIS A 148      12.006  32.705  -6.308  1.00 14.17           N  
ANISOU 2356  ND1 HIS A 148     1512   2226   1646   -295    -69   -374       N  
ATOM   2357  CD2 HIS A 148      13.159  31.775  -7.918  1.00 16.74           C  
ANISOU 2357  CD2 HIS A 148     1856   2691   1814   -381    -69   -511       C  
ATOM   2358  CE1 HIS A 148      12.819  33.629  -6.793  1.00 14.21           C  
ANISOU 2358  CE1 HIS A 148     1517   2264   1617   -364     -5   -399       C  
ATOM   2359  NE2 HIS A 148      13.528  33.088  -7.770  1.00 14.66           N  
ANISOU 2359  NE2 HIS A 148     1569   2415   1588   -414     -6   -476       N  
ATOM   2360  H   HIS A 148       9.002  31.001  -7.661  1.00 17.80           H  
ATOM   2361  HA  HIS A 148      11.162  29.666  -8.614  1.00 17.17           H  
ATOM   2362  HB2 HIS A 148      10.875  30.435  -5.920  1.00 16.19           H  
ATOM   2363  HB3 HIS A 148      12.075  29.559  -6.483  1.00 16.19           H  
ATOM   2364  HD1 HIS A 148      11.454  32.819  -5.659  1.00 17.00           H  
ATOM   2365  HD2 HIS A 148      13.512  31.168  -8.528  1.00 20.09           H  
ATOM   2366  HE1 HIS A 148      12.876  34.511  -6.503  1.00 17.05           H  
ATOM   2367  HE2 HIS A 148      14.119  33.496  -8.243  1.00 17.60           H  
ATOM   2368  N   LYS A 149      10.615  27.447  -7.447  1.00 14.18           N  
ANISOU 2368  N   LYS A 149     1684   2259   1443   -316   -364   -504       N  
ATOM   2369  CA  LYS A 149      10.095  26.137  -7.073  1.00 14.16           C  
ANISOU 2369  CA  LYS A 149     1731   2205   1444   -292   -427   -529       C  
ATOM   2370  C   LYS A 149      10.863  25.695  -5.839  1.00 13.49           C  
ANISOU 2370  C   LYS A 149     1585   2088   1452   -133   -361   -640       C  
ATOM   2371  O   LYS A 149      12.085  25.585  -5.876  1.00 16.38           O  
ANISOU 2371  O   LYS A 149     1931   2475   1819    -81   -272   -756       O  
ATOM   2372  CB  LYS A 149      10.264  25.112  -8.216  1.00 16.14           C  
ANISOU 2372  CB  LYS A 149     2175   2440   1519   -413   -428   -620       C  
ATOM   2373  CG  LYS A 149       9.203  25.201  -9.244  1.00 24.50           C  
ANISOU 2373  CG  LYS A 149     3337   3514   2456   -627   -585   -471       C  
ATOM   2374  CD  LYS A 149       9.425  24.220 -10.402  1.00 27.03           C  
ANISOU 2374  CD  LYS A 149     3942   3782   2546   -786   -560   -579       C  
ATOM   2375  CE  LYS A 149       8.998  22.805 -10.098  1.00 22.45           C  
ANISOU 2375  CE  LYS A 149     3455   3102   1973   -771   -586   -621       C  
ATOM   2376  NZ  LYS A 149       8.770  22.062 -11.428  1.00 23.99           N  
ANISOU 2376  NZ  LYS A 149     3921   3220   1975   -956   -578   -615       N  
ATOM   2377  H   LYS A 149      11.463  27.445  -7.595  1.00 17.01           H  
ATOM   2378  HA  LYS A 149       9.154  26.207  -6.850  1.00 16.99           H  
ATOM   2379  HB2 LYS A 149      11.116  25.265  -8.653  1.00 19.37           H  
ATOM   2380  HB3 LYS A 149      10.241  24.217  -7.841  1.00 19.37           H  
ATOM   2381  HG2 LYS A 149       8.348  24.996  -8.835  1.00 29.39           H  
ATOM   2382  HG3 LYS A 149       9.191  26.100  -9.609  1.00 29.39           H  
ATOM   2383  HD2 LYS A 149       8.915  24.524 -11.170  1.00 32.43           H  
ATOM   2384  HD3 LYS A 149      10.370  24.204 -10.621  1.00 32.43           H  
ATOM   2385  HE2 LYS A 149       9.697  22.350  -9.601  1.00 26.94           H  
ATOM   2386  HE3 LYS A 149       8.168  22.812  -9.597  1.00 26.94           H  
ATOM   2387  HZ1 LYS A 149       9.522  22.052 -11.904  1.00 28.79           H  
ATOM   2388  HZ2 LYS A 149       8.517  21.223 -11.268  1.00 28.79           H  
ATOM   2389  HZ3 LYS A 149       8.135  22.470 -11.899  1.00 28.79           H  
ATOM   2390  N   VAL A 150      10.137  25.499  -4.741  1.00 14.31           N  
ANISOU 2390  N   VAL A 150     1651   2138   1648    -65   -406   -574       N  
ATOM   2391  CA  VAL A 150      10.699  25.175  -3.435  1.00 15.10           C  
ANISOU 2391  CA  VAL A 150     1726   2201   1811     52   -384   -638       C  
ATOM   2392  C   VAL A 150      10.536  23.669  -3.172  1.00 13.60           C  
ANISOU 2392  C   VAL A 150     1590   1954   1623     99   -421   -686       C  
ATOM   2393  O   VAL A 150       9.432  23.200  -2.998  1.00 14.69           O  
ANISOU 2393  O   VAL A 150     1759   2042   1780     76   -472   -606       O  
ATOM   2394  CB  VAL A 150       9.922  25.997  -2.383  1.00 11.69           C  
ANISOU 2394  CB  VAL A 150     1285   1707   1449     79   -362   -533       C  
ATOM   2395  CG1 VAL A 150      10.311  25.624  -0.967  1.00 11.52           C  
ANISOU 2395  CG1 VAL A 150     1312   1628   1438    151   -363   -581       C  
ATOM   2396  CG2 VAL A 150      10.115  27.493  -2.652  1.00 15.74           C  
ANISOU 2396  CG2 VAL A 150     1776   2240   1966     34   -295   -490       C  
ATOM   2397  H   VAL A 150       9.278  25.552  -4.730  1.00 17.17           H  
ATOM   2398  HA  VAL A 150      11.639  25.410  -3.402  1.00 18.12           H  
ATOM   2399  HB  VAL A 150       8.976  25.805  -2.483  1.00 14.02           H  
ATOM   2400 HG11 VAL A 150       9.798  26.165  -0.346  1.00 13.82           H  
ATOM   2401 HG12 VAL A 150      10.118  24.684  -0.824  1.00 13.82           H  
ATOM   2402 HG13 VAL A 150      11.259  25.790  -0.846  1.00 13.82           H  
ATOM   2403 HG21 VAL A 150       9.624  28.000  -1.987  1.00 18.89           H  
ATOM   2404 HG22 VAL A 150      11.061  27.704  -2.598  1.00 18.89           H  
ATOM   2405 HG23 VAL A 150       9.781  27.700  -3.539  1.00 18.89           H  
ATOM   2406  N   TYR A 151      11.628  22.912  -3.185  1.00 12.90           N  
ANISOU 2406  N   TYR A 151     1499   1862   1541    167   -380   -792       N  
ATOM   2407  CA  TYR A 151      11.538  21.460  -3.094  1.00 13.45           C  
ANISOU 2407  CA  TYR A 151     1642   1849   1617    216   -380   -839       C  
ATOM   2408  C   TYR A 151      11.532  21.014  -1.643  1.00 13.06           C  
ANISOU 2408  C   TYR A 151     1564   1753   1647    316   -438   -804       C  
ATOM   2409  O   TYR A 151      12.348  21.488  -0.854  1.00 14.08           O  
ANISOU 2409  O   TYR A 151     1613   1914   1822    364   -461   -793       O  
ATOM   2410  CB  TYR A 151      12.719  20.843  -3.831  1.00 14.74           C  
ANISOU 2410  CB  TYR A 151     1819   1992   1792    267   -250   -943       C  
ATOM   2411  CG  TYR A 151      12.603  21.056  -5.308  1.00 15.58           C  
ANISOU 2411  CG  TYR A 151     2050   2107   1762    137   -170   -992       C  
ATOM   2412  CD1 TYR A 151      11.745  20.281  -6.054  1.00 17.90           C  
ANISOU 2412  CD1 TYR A 151     2550   2328   1923     13   -193  -1012       C  
ATOM   2413  CD2 TYR A 151      13.320  22.053  -5.948  1.00 18.65           C  
ANISOU 2413  CD2 TYR A 151     2380   2574   2133    104    -91  -1006       C  
ATOM   2414  CE1 TYR A 151      11.614  20.470  -7.412  1.00 21.24           C  
ANISOU 2414  CE1 TYR A 151     3151   2752   2168   -158   -151  -1045       C  
ATOM   2415  CE2 TYR A 151      13.213  22.240  -7.315  1.00 22.24           C  
ANISOU 2415  CE2 TYR A 151     2995   3028   2428    -37    -16  -1045       C  
ATOM   2416  CZ  TYR A 151      12.350  21.442  -8.037  1.00 23.23           C  
ANISOU 2416  CZ  TYR A 151     3358   3077   2392   -177    -55  -1064       C  
ATOM   2417  OH  TYR A 151      12.193  21.616  -9.395  1.00 29.13           O  
ANISOU 2417  OH  TYR A 151     4327   3816   2927   -371    -15  -1089       O  
ATOM   2418  H   TYR A 151      12.431  23.214  -3.244  1.00 15.48           H  
ATOM   2419  HA  TYR A 151      10.718  21.157  -3.515  1.00 16.14           H  
ATOM   2420  HB2 TYR A 151      13.541  21.259  -3.526  1.00 17.69           H  
ATOM   2421  HB3 TYR A 151      12.741  19.888  -3.661  1.00 17.69           H  
ATOM   2422  HD1 TYR A 151      11.249  19.615  -5.635  1.00 21.48           H  
ATOM   2423  HD2 TYR A 151      13.907  22.582  -5.458  1.00 22.38           H  
ATOM   2424  HE1 TYR A 151      11.036  19.933  -7.904  1.00 25.49           H  
ATOM   2425  HE2 TYR A 151      13.701  22.909  -7.738  1.00 26.69           H  
ATOM   2426  HH  TYR A 151      12.693  22.235  -9.665  1.00 34.96           H  
ATOM   2427  N   ILE A 152      10.604  20.132  -1.296  1.00 14.34           N  
ANISOU 2427  N   ILE A 152     1805   1835   1807    316   -477   -773       N  
ATOM   2428  CA  ILE A 152      10.447  19.664   0.083  1.00 12.81           C  
ANISOU 2428  CA  ILE A 152     1626   1581   1661    392   -523   -730       C  
ATOM   2429  C   ILE A 152      10.557  18.153   0.169  1.00 16.03           C  
ANISOU 2429  C   ILE A 152     2100   1893   2100    458   -520   -765       C  
ATOM   2430  O   ILE A 152       9.954  17.458  -0.636  1.00 15.08           O  
ANISOU 2430  O   ILE A 152     2071   1718   1939    394   -499   -794       O  
ATOM   2431  CB  ILE A 152       9.070  20.082   0.609  1.00 16.48           C  
ANISOU 2431  CB  ILE A 152     2124   2009   2129    341   -532   -625       C  
ATOM   2432  CG1 ILE A 152       8.953  21.617   0.597  1.00 12.30           C  
ANISOU 2432  CG1 ILE A 152     1548   1531   1594    299   -488   -576       C  
ATOM   2433  CG2 ILE A 152       8.814  19.473   1.985  1.00 14.45           C  
ANISOU 2433  CG2 ILE A 152     1937   1662   1889    403   -546   -587       C  
ATOM   2434  CD1 ILE A 152       7.516  22.144   0.847  1.00 12.85           C  
ANISOU 2434  CD1 ILE A 152     1610   1542   1731    267   -429   -432       C  
ATOM   2435  H   ILE A 152      10.043  19.783  -1.846  1.00 17.20           H  
ATOM   2436  HA  ILE A 152      11.130  20.060   0.645  1.00 15.38           H  
ATOM   2437  HB  ILE A 152       8.401  19.729   0.001  1.00 19.78           H  
ATOM   2438 HG12 ILE A 152       9.525  21.978   1.292  1.00 14.76           H  
ATOM   2439 HG13 ILE A 152       9.242  21.945  -0.269  1.00 14.76           H  
ATOM   2440 HG21 ILE A 152       7.938  19.752   2.296  1.00 17.33           H  
ATOM   2441 HG22 ILE A 152       8.848  18.506   1.914  1.00 17.33           H  
ATOM   2442 HG23 ILE A 152       9.497  19.784   2.599  1.00 17.33           H  
ATOM   2443 HD11 ILE A 152       7.528  23.114   0.824  1.00 15.42           H  
ATOM   2444 HD12 ILE A 152       6.930  21.804   0.153  1.00 15.42           H  
ATOM   2445 HD13 ILE A 152       7.214  21.837   1.716  1.00 15.42           H  
ATOM   2446  N   THR A 153      11.313  17.649   1.156  1.00 14.11           N  
ANISOU 2446  N   THR A 153     1826   1614   1919    564   -554   -747       N  
ATOM   2447  CA  THR A 153      11.382  16.216   1.452  1.00 15.03           C  
ANISOU 2447  CA  THR A 153     2005   1614   2092    648   -546   -749       C  
ATOM   2448  C   THR A 153      11.326  16.034   2.966  1.00 19.03           C  
ANISOU 2448  C   THR A 153     2533   2087   2609    690   -648   -657       C  
ATOM   2449  O   THR A 153      11.638  16.964   3.732  1.00 16.88           O  
ANISOU 2449  O   THR A 153     2235   1881   2299    656   -720   -609       O  
ATOM   2450  CB  THR A 153      12.674  15.585   0.901  1.00 17.76           C  
ANISOU 2450  CB  THR A 153     2277   1923   2549    763   -450   -790       C  
ATOM   2451  OG1 THR A 153      12.606  14.149   0.965  1.00 19.90           O  
ANISOU 2451  OG1 THR A 153     2646   2037   2879    846   -389   -800       O  
ATOM   2452  CG2 THR A 153      13.916  16.107   1.646  1.00 17.19           C  
ANISOU 2452  CG2 THR A 153     2016   1929   2587    836   -531   -701       C  
ATOM   2453  H   THR A 153      11.803  18.130   1.674  1.00 16.93           H  
ATOM   2454  HA  THR A 153      10.621  15.763   1.056  1.00 18.03           H  
ATOM   2455  HB  THR A 153      12.766  15.844  -0.030  1.00 21.31           H  
ATOM   2456  HG1 THR A 153      11.957  13.871   0.510  1.00 23.89           H  
ATOM   2457 HG21 THR A 153      14.716  15.697   1.283  1.00 20.63           H  
ATOM   2458 HG22 THR A 153      13.981  17.069   1.547  1.00 20.63           H  
ATOM   2459 HG23 THR A 153      13.851  15.891   2.590  1.00 20.63           H  
ATOM   2460  N   ALA A 154      10.918  14.846   3.397  1.00 17.31           N  
ANISOU 2460  N   ALA A 154     2406   1752   2417    737   -652   -634       N  
ATOM   2461  CA  ALA A 154      10.871  14.537   4.817  1.00 19.48           C  
ANISOU 2461  CA  ALA A 154     2744   1979   2680    765   -746   -538       C  
ATOM   2462  C   ALA A 154      12.266  14.377   5.382  1.00 17.35           C  
ANISOU 2462  C   ALA A 154     2365   1733   2496    850   -849   -461       C  
ATOM   2463  O   ALA A 154      13.217  13.972   4.692  1.00 18.40           O  
ANISOU 2463  O   ALA A 154     2360   1861   2768    948   -798   -469       O  
ATOM   2464  CB  ALA A 154      10.070  13.269   5.058  1.00 19.27           C  
ANISOU 2464  CB  ALA A 154     2840   1813   2668    788   -717   -522       C  
ATOM   2465  H   ALA A 154      10.665  14.202   2.886  1.00 20.77           H  
ATOM   2466  HA  ALA A 154      10.435  15.265   5.287  1.00 23.38           H  
ATOM   2467  HB1 ALA A 154      10.052  13.084   6.010  1.00 23.12           H  
ATOM   2468  HB2 ALA A 154       9.167  13.399   4.729  1.00 23.12           H  
ATOM   2469  HB3 ALA A 154      10.493  12.535   4.585  1.00 23.12           H  
ATOM   2470  N   ASP A 155      12.349  14.666   6.675  1.00 17.77           N  
ANISOU 2470  N   ASP A 155     2493   1793   2468    799   -986   -364       N  
ATOM   2471  CA  ASP A 155      13.512  14.354   7.488  1.00 20.22           C  
ANISOU 2471  CA  ASP A 155     2721   2114   2849    837  -1164   -221       C  
ATOM   2472  C   ASP A 155      12.975  13.639   8.729  1.00 20.33           C  
ANISOU 2472  C   ASP A 155     2934   2022   2768    816  -1249   -130       C  
ATOM   2473  O   ASP A 155      12.888  14.233   9.814  1.00 21.02           O  
ANISOU 2473  O   ASP A 155     3188   2120   2680    682  -1367    -68       O  
ATOM   2474  CB  ASP A 155      14.199  15.662   7.883  1.00 21.44           C  
ANISOU 2474  CB  ASP A 155     2837   2393   2918    703  -1300   -179       C  
ATOM   2475  CG  ASP A 155      15.587  15.460   8.467  1.00 29.73           C  
ANISOU 2475  CG  ASP A 155     3717   3491   4089    708  -1532     12       C  
ATOM   2476  OD1 ASP A 155      16.016  14.300   8.691  1.00 31.92           O  
ANISOU 2476  OD1 ASP A 155     3901   3698   4528    832  -1571    136       O  
ATOM   2477  OD2 ASP A 155      16.251  16.492   8.712  1.00 28.45           O  
ANISOU 2477  OD2 ASP A 155     3508   3434   3868    566  -1666     60       O  
ATOM   2478  H   ASP A 155      11.722  15.056   7.116  1.00 21.33           H  
ATOM   2479  HA  ASP A 155      14.131  13.780   7.010  1.00 24.27           H  
ATOM   2480  HB2 ASP A 155      14.287  16.221   7.095  1.00 25.73           H  
ATOM   2481  HB3 ASP A 155      13.658  16.112   8.549  1.00 25.73           H  
ATOM   2482  N   LYS A 156      12.622  12.368   8.578  1.00 20.69           N  
ANISOU 2482  N   LYS A 156     3006   1945   2910    928  -1174   -124       N  
ATOM   2483  CA  LYS A 156      11.877  11.652   9.607  1.00 21.13           C  
ANISOU 2483  CA  LYS A 156     3272   1884   2872    905  -1204    -59       C  
ATOM   2484  C   LYS A 156      12.611  11.570  10.961  1.00 23.13           C  
ANISOU 2484  C   LYS A 156     3594   2137   3056    853  -1444    129       C  
ATOM   2485  O   LYS A 156      11.971  11.622  11.998  1.00 23.40           O  
ANISOU 2485  O   LYS A 156     3881   2111   2898    746  -1476    167       O  
ATOM   2486  CB  LYS A 156      11.490  10.230   9.151  1.00 21.52           C  
ANISOU 2486  CB  LYS A 156     3337   1787   3053   1027  -1088    -78       C  
ATOM   2487  CG  LYS A 156      12.621   9.303   8.829  1.00 23.41           C  
ANISOU 2487  CG  LYS A 156     3400   1991   3505   1163  -1072      5       C  
ATOM   2488  CD  LYS A 156      12.117   7.909   8.348  1.00 23.99           C  
ANISOU 2488  CD  LYS A 156     3549   1911   3657   1221   -879    -38       C  
ATOM   2489  CE  LYS A 156      13.278   6.939   8.228  1.00 31.53           C  
ANISOU 2489  CE  LYS A 156     4352   2787   4840   1378   -810     91       C  
ATOM   2490  NZ  LYS A 156      12.997   5.623   7.523  1.00 29.46           N  
ANISOU 2490  NZ  LYS A 156     4182   2337   4676   1446   -565     32       N  
ATOM   2491  H   LYS A 156      12.804  11.893   7.884  1.00 24.83           H  
ATOM   2492  HA  LYS A 156      11.049  12.133   9.763  1.00 25.35           H  
ATOM   2493  HB2 LYS A 156      10.970   9.816   9.857  1.00 25.82           H  
ATOM   2494  HB3 LYS A 156      10.943  10.306   8.353  1.00 25.82           H  
ATOM   2495  HG2 LYS A 156      13.158   9.691   8.121  1.00 28.09           H  
ATOM   2496  HG3 LYS A 156      13.160   9.171   9.624  1.00 28.09           H  
ATOM   2497  HD2 LYS A 156      11.485   7.554   8.991  1.00 28.79           H  
ATOM   2498  HD3 LYS A 156      11.701   7.999   7.476  1.00 28.79           H  
ATOM   2499  HE2 LYS A 156      13.991   7.380   7.740  1.00 37.83           H  
ATOM   2500  HE3 LYS A 156      13.587   6.726   9.122  1.00 37.83           H  
ATOM   2501  HZ1 LYS A 156      13.735   5.126   7.503  1.00 35.36           H  
ATOM   2502  HZ2 LYS A 156      12.359   5.178   7.955  1.00 35.36           H  
ATOM   2503  HZ3 LYS A 156      12.729   5.777   6.689  1.00 35.36           H  
ATOM   2504  N   GLN A 157      13.930  11.445  10.949  1.00 24.89           N  
ANISOU 2504  N   GLN A 157     3596   2424   3435    903  -1594    264       N  
ATOM   2505  CA  GLN A 157      14.645  11.159  12.196  1.00 27.42           C  
ANISOU 2505  CA  GLN A 157     3942   2764   3711    804  -1804    477       C  
ATOM   2506  C   GLN A 157      14.682  12.420  13.075  1.00 27.70           C  
ANISOU 2506  C   GLN A 157     4175   2880   3471    553  -1962    489       C  
ATOM   2507  O   GLN A 157      14.968  12.349  14.282  1.00 29.84           O  
ANISOU 2507  O   GLN A 157     4597   3142   3597    394  -2124    626       O  
ATOM   2508  CB  GLN A 157      16.036  10.571  11.896  1.00 29.81           C  
ANISOU 2508  CB  GLN A 157     3899   3125   4301    916  -1837    652       C  
ATOM   2509  CG  GLN A 157      16.481   9.380  12.805  1.00 35.37           C  
ANISOU 2509  CG  GLN A 157     4585   3765   5087    961  -1933    876       C  
ATOM   2510  CD  GLN A 157      15.582   8.114  12.743  1.00 38.96           C  
ANISOU 2510  CD  GLN A 157     5183   4040   5579   1098  -1762    825       C  
ATOM   2511  OE1 GLN A 157      14.855   7.884  11.766  1.00 30.15           O  
ANISOU 2511  OE1 GLN A 157     4106   2842   4508   1194  -1535    635       O  
ATOM   2512  NE2 GLN A 157      15.642   7.291  13.804  1.00 34.25           N  
ANISOU 2512  NE2 GLN A 157     4682   3383   4949   1077  -1876    997       N  
ATOM   2513  H   GLN A 157      14.430  11.517  10.253  1.00 29.86           H  
ATOM   2514  HA  GLN A 157      14.147  10.484  12.684  1.00 32.90           H  
ATOM   2515  HB2 GLN A 157      16.042  10.255  10.979  1.00 35.77           H  
ATOM   2516  HB3 GLN A 157      16.694  11.276  11.999  1.00 35.77           H  
ATOM   2517  HG2 GLN A 157      17.376   9.113  12.544  1.00 42.44           H  
ATOM   2518  HG3 GLN A 157      16.490   9.684  13.726  1.00 42.44           H  
ATOM   2519 HE21 GLN A 157      16.158   7.479  14.466  1.00 41.10           H  
ATOM   2520 HE22 GLN A 157      15.165   6.576  13.820  1.00 41.10           H  
ATOM   2521  N   LYS A 158      14.359  13.566  12.471  1.00 25.84           N  
ANISOU 2521  N   LYS A 158     3969   2702   3146    502  -1886    335       N  
ATOM   2522  CA  LYS A 158      14.257  14.842  13.197  1.00 32.05           C  
ANISOU 2522  CA  LYS A 158     4999   3524   3655    256  -1939    302       C  
ATOM   2523  C   LYS A 158      12.805  15.288  13.270  1.00 24.24           C  
ANISOU 2523  C   LYS A 158     4315   2429   2465    231  -1709    142       C  
ATOM   2524  O   LYS A 158      12.499  16.370  13.777  1.00 24.39           O  
ANISOU 2524  O   LYS A 158     4591   2424   2251     55  -1653     83       O  
ATOM   2525  CB  LYS A 158      15.092  15.936  12.515  1.00 25.92           C  
ANISOU 2525  CB  LYS A 158     4009   2891   2948    190  -1959    268       C  
ATOM   2526  CG  LYS A 158      16.570  15.857  12.886  1.00 38.55           C  
ANISOU 2526  CG  LYS A 158     5375   4597   4677    110  -2161    469       C  
ATOM   2527  CD  LYS A 158      17.384  17.023  12.348  1.00 43.26           C  
ANISOU 2527  CD  LYS A 158     5802   5324   5313     12  -2178    451       C  
ATOM   2528  CE  LYS A 158      18.882  16.809  12.585  1.00 43.69           C  
ANISOU 2528  CE  LYS A 158     5568   5478   5555    -28  -2368    678       C  
ATOM   2529  H   LYS A 158      14.191  13.635  11.631  1.00 31.00           H  
ATOM   2530  HA  LYS A 158      14.587  14.725  14.101  1.00 38.46           H  
ATOM   2531  HB2 LYS A 158      15.018  15.838  11.552  1.00 31.10           H  
ATOM   2532  HB3 LYS A 158      14.759  16.805  12.787  1.00 31.10           H  
ATOM   2533  HG2 LYS A 158      16.652  15.857  13.853  1.00 46.26           H  
ATOM   2534  HG3 LYS A 158      16.943  15.039  12.522  1.00 46.26           H  
ATOM   2535  HD2 LYS A 158      17.235  17.105  11.393  1.00 51.92           H  
ATOM   2536  HD3 LYS A 158      17.117  17.838  12.802  1.00 51.92           H  
ATOM   2537  HE2 LYS A 158      19.086  17.001  13.514  1.00 52.43           H  
ATOM   2538  HE3 LYS A 158      19.106  15.887  12.381  1.00 52.43           H  
ATOM   2539  N   ASN A 159      11.915  14.445  12.752  1.00 22.86           N  
ANISOU 2539  N   ASN A 159     4088   2179   2419    392  -1507     76       N  
ATOM   2540  CA  ASN A 159      10.483  14.723  12.752  1.00 21.48           C  
ANISOU 2540  CA  ASN A 159     4093   1908   2160    379  -1227    -32       C  
ATOM   2541  C   ASN A 159      10.153  16.042  12.025  1.00 20.02           C  
ANISOU 2541  C   ASN A 159     3855   1785   1967    337  -1065   -151       C  
ATOM   2542  O   ASN A 159       9.259  16.784  12.434  1.00 20.02           O  
ANISOU 2542  O   ASN A 159     4065   1698   1845    263   -864   -189       O  
ATOM   2543  CB  ASN A 159       9.919  14.743  14.178  1.00 28.13           C  
ANISOU 2543  CB  ASN A 159     5330   2611   2748    244  -1193     27       C  
ATOM   2544  CG  ASN A 159       8.435  14.367  14.231  1.00 22.17           C  
ANISOU 2544  CG  ASN A 159     4681   1720   2022    301   -896    -11       C  
ATOM   2545  OD1 ASN A 159       7.976  13.504  13.485  1.00 23.25           O  
ANISOU 2545  OD1 ASN A 159     4621   1852   2361    432   -836    -23       O  
ATOM   2546  ND2 ASN A 159       7.688  15.005  15.136  1.00 27.36           N  
ANISOU 2546  ND2 ASN A 159     5670   2246   2479    187   -695    -16       N  
ATOM   2547  H   ASN A 159      12.120  13.693  12.390  1.00 27.43           H  
ATOM   2548  HA  ASN A 159      10.034  14.009  12.274  1.00 25.78           H  
ATOM   2549  HB2 ASN A 159      10.410  14.107  14.721  1.00 33.76           H  
ATOM   2550  HB3 ASN A 159      10.016  15.637  14.544  1.00 33.76           H  
ATOM   2551 HD21 ASN A 159       8.046  15.593  15.652  1.00 32.83           H  
ATOM   2552 HD22 ASN A 159       6.849  14.828  15.204  1.00 32.83           H  
ATOM   2553  N   GLY A 160      10.879  16.308  10.939  1.00 20.39           N  
ANISOU 2553  N   GLY A 160     3623   1961   2162    397  -1124   -194       N  
ATOM   2554  CA  GLY A 160      10.732  17.558  10.226  1.00 20.30           C  
ANISOU 2554  CA  GLY A 160     3551   2017   2145    352  -1007   -285       C  
ATOM   2555  C   GLY A 160      10.942  17.373   8.738  1.00 16.84           C  
ANISOU 2555  C   GLY A 160     2819   1675   1905    464   -969   -349       C  
ATOM   2556  O   GLY A 160      10.723  16.286   8.203  1.00 21.45           O  
ANISOU 2556  O   GLY A 160     3310   2229   2613    571   -942   -355       O  
ATOM   2557  H   GLY A 160      11.462  15.775  10.600  1.00 24.46           H  
ATOM   2558  HA2 GLY A 160       9.842  17.915  10.372  1.00 24.36           H  
ATOM   2559  HA3 GLY A 160      11.382  18.199  10.554  1.00 24.36           H  
ATOM   2560  N   ILE A 161      11.396  18.438   8.089  1.00 17.26           N  
ANISOU 2560  N   ILE A 161     2769   1825   1964    419   -957   -399       N  
ATOM   2561  CA  ILE A 161      11.602  18.449   6.633  1.00 18.85           C  
ANISOU 2561  CA  ILE A 161     2745   2111   2307    492   -895   -467       C  
ATOM   2562  C   ILE A 161      12.911  19.154   6.292  1.00 17.99           C  
ANISOU 2562  C   ILE A 161     2483   2118   2234    457   -993   -464       C  
ATOM   2563  O   ILE A 161      13.460  19.921   7.101  1.00 19.54           O  
ANISOU 2563  O   ILE A 161     2759   2339   2327    337  -1109   -418       O  
ATOM   2564  CB  ILE A 161      10.450  19.189   5.882  1.00 14.08           C  
ANISOU 2564  CB  ILE A 161     2151   1501   1697    462   -722   -517       C  
ATOM   2565  CG1 ILE A 161      10.292  20.622   6.420  1.00 14.29           C  
ANISOU 2565  CG1 ILE A 161     2301   1517   1613    359   -658   -512       C  
ATOM   2566  CG2 ILE A 161       9.179  18.410   6.007  1.00 15.66           C  
ANISOU 2566  CG2 ILE A 161     2422   1601   1928    491   -635   -485       C  
ATOM   2567  CD1 ILE A 161       9.271  21.450   5.670  1.00 14.84           C  
ANISOU 2567  CD1 ILE A 161     2331   1574   1733    351   -487   -510       C  
ATOM   2568  H   ILE A 161      11.598  19.182   8.471  1.00 20.71           H  
ATOM   2569  HA  ILE A 161      11.648  17.537   6.305  1.00 22.62           H  
ATOM   2570  HB  ILE A 161      10.684  19.242   4.942  1.00 16.89           H  
ATOM   2571 HG12 ILE A 161      10.013  20.578   7.348  1.00 17.15           H  
ATOM   2572 HG13 ILE A 161      11.147  21.076   6.355  1.00 17.15           H  
ATOM   2573 HG21 ILE A 161       8.473  18.881   5.537  1.00 18.79           H  
ATOM   2574 HG22 ILE A 161       9.308  17.531   5.617  1.00 18.79           H  
ATOM   2575 HG23 ILE A 161       8.952  18.325   6.946  1.00 18.79           H  
ATOM   2576 HD11 ILE A 161       9.229  22.334   6.066  1.00 17.80           H  
ATOM   2577 HD12 ILE A 161       9.540  21.515   4.741  1.00 17.80           H  
ATOM   2578 HD13 ILE A 161       8.405  21.017   5.735  1.00 17.80           H  
ATOM   2579  N   LYS A 162      13.406  18.847   5.099  1.00 15.87           N  
ANISOU 2579  N   LYS A 162     2021   1905   2105    542   -937   -507       N  
ATOM   2580  CA  LYS A 162      14.515  19.520   4.481  1.00 16.41           C  
ANISOU 2580  CA  LYS A 162     1908   2079   2249    525   -959   -508       C  
ATOM   2581  C   LYS A 162      13.977  20.114   3.186  1.00 15.12           C  
ANISOU 2581  C   LYS A 162     1727   1951   2069    511   -795   -613       C  
ATOM   2582  O   LYS A 162      13.178  19.499   2.473  1.00 14.50           O  
ANISOU 2582  O   LYS A 162     1696   1821   1992    551   -693   -667       O  
ATOM   2583  CB  LYS A 162      15.678  18.559   4.183  1.00 18.07           C  
ANISOU 2583  CB  LYS A 162     1907   2293   2667    654   -985   -439       C  
ATOM   2584  CG  LYS A 162      16.609  18.319   5.397  1.00 23.15           C  
ANISOU 2584  CG  LYS A 162     2476   2950   3370    630  -1222   -260       C  
ATOM   2585  CD  LYS A 162      17.831  17.445   5.032  1.00 29.67           C  
ANISOU 2585  CD  LYS A 162     3012   3770   4492    789  -1216   -133       C  
ATOM   2586  CE  LYS A 162      18.828  17.360   6.191  1.00 40.16           C  
ANISOU 2586  CE  LYS A 162     4235   5145   5878    704  -1458    111       C  
ATOM   2587  H   LYS A 162      13.088  18.215   4.610  1.00 19.05           H  
ATOM   2588  HA  LYS A 162      14.832  20.236   5.053  1.00 19.70           H  
ATOM   2589  HB2 LYS A 162      15.314  17.701   3.913  1.00 21.69           H  
ATOM   2590  HB3 LYS A 162      16.215  18.929   3.465  1.00 21.69           H  
ATOM   2591  HG2 LYS A 162      16.934  19.173   5.721  1.00 27.78           H  
ATOM   2592  HG3 LYS A 162      16.111  17.865   6.095  1.00 27.78           H  
ATOM   2593  HD2 LYS A 162      17.531  16.546   4.823  1.00 35.61           H  
ATOM   2594  HD3 LYS A 162      18.286  17.833   4.268  1.00 35.61           H  
ATOM   2595  N   VAL A 163      14.436  21.316   2.893  1.00 15.08           N  
ANISOU 2595  N   VAL A 163     1667   2029   2036    426   -794   -625       N  
ATOM   2596  CA  VAL A 163      13.912  22.110   1.791  1.00 15.81           C  
ANISOU 2596  CA  VAL A 163     1762   2157   2090    384   -667   -692       C  
ATOM   2597  C   VAL A 163      15.110  22.700   1.035  1.00 18.80           C  
ANISOU 2597  C   VAL A 163     1973   2631   2540    365   -643   -704       C  
ATOM   2598  O   VAL A 163      16.119  23.079   1.647  1.00 17.05           O  
ANISOU 2598  O   VAL A 163     1657   2457   2364    322   -754   -640       O  
ATOM   2599  CB  VAL A 163      13.022  23.242   2.370  1.00 13.41           C  
ANISOU 2599  CB  VAL A 163     1605   1819   1671    287   -644   -674       C  
ATOM   2600  CG1 VAL A 163      12.533  24.169   1.290  1.00 13.30           C  
ANISOU 2600  CG1 VAL A 163     1565   1841   1648    244   -536   -694       C  
ATOM   2601  CG2 VAL A 163      11.845  22.629   3.196  1.00 16.39           C  
ANISOU 2601  CG2 VAL A 163     2132   2084   2011    315   -622   -639       C  
ATOM   2602  H   VAL A 163      15.067  21.706   3.328  1.00 18.10           H  
ATOM   2603  HA  VAL A 163      13.387  21.558   1.190  1.00 18.98           H  
ATOM   2604  HB  VAL A 163      13.559  23.770   2.982  1.00 16.09           H  
ATOM   2605 HG11 VAL A 163      11.983  24.859   1.691  1.00 15.96           H  
ATOM   2606 HG12 VAL A 163      13.298  24.570   0.849  1.00 15.96           H  
ATOM   2607 HG13 VAL A 163      12.011  23.660   0.650  1.00 15.96           H  
ATOM   2608 HG21 VAL A 163      11.300  23.349   3.550  1.00 19.67           H  
ATOM   2609 HG22 VAL A 163      11.312  22.066   2.614  1.00 19.67           H  
ATOM   2610 HG23 VAL A 163      12.211  22.102   3.923  1.00 19.67           H  
ATOM   2611  N   ASN A 164      15.042  22.740  -0.294  1.00 18.86           N  
ANISOU 2611  N   ASN A 164     1950   2661   2556    377   -509   -768       N  
ATOM   2612  CA  ASN A 164      16.097  23.372  -1.065  1.00 16.51           C  
ANISOU 2612  CA  ASN A 164     1513   2440   2321    354   -440   -778       C  
ATOM   2613  C   ASN A 164      15.508  24.057  -2.275  1.00 14.67           C  
ANISOU 2613  C   ASN A 164     1357   2231   1986    281   -328   -835       C  
ATOM   2614  O   ASN A 164      14.504  23.588  -2.824  1.00 14.13           O  
ANISOU 2614  O   ASN A 164     1415   2116   1838    269   -295   -864       O  
ATOM   2615  CB  ASN A 164      17.182  22.363  -1.494  1.00 17.11           C  
ANISOU 2615  CB  ASN A 164     1438   2493   2570    479   -343   -769       C  
ATOM   2616  CG  ASN A 164      16.697  21.363  -2.560  1.00 21.66           C  
ANISOU 2616  CG  ASN A 164     2147   2976   3108    538   -161   -865       C  
ATOM   2617  OD1 ASN A 164      16.042  20.362  -2.244  1.00 28.33           O  
ANISOU 2617  OD1 ASN A 164     3104   3730   3930    588   -184   -879       O  
ATOM   2618  ND2 ASN A 164      17.072  21.606  -3.811  1.00 22.96           N  
ANISOU 2618  ND2 ASN A 164     2329   3145   3251    513     25   -930       N  
ATOM   2619  H   ASN A 164      14.401  22.412  -0.765  1.00 22.63           H  
ATOM   2620  HA  ASN A 164      16.522  24.050  -0.517  1.00 19.81           H  
ATOM   2621  HB2 ASN A 164      17.936  22.849  -1.863  1.00 20.53           H  
ATOM   2622  HB3 ASN A 164      17.464  21.856  -0.717  1.00 20.53           H  
ATOM   2623 HD21 ASN A 164      17.560  22.292  -3.989  1.00 27.55           H  
ATOM   2624 HD22 ASN A 164      16.828  21.077  -4.444  1.00 27.55           H  
ATOM   2625  N   PHE A 165      16.122  25.166  -2.671  1.00 17.88           N  
ANISOU 2625  N   PHE A 165     1690   2710   2395    207   -295   -828       N  
ATOM   2626  CA  PHE A 165      15.720  25.882  -3.878  1.00 16.10           C  
ANISOU 2626  CA  PHE A 165     1530   2511   2074    128   -197   -858       C  
ATOM   2627  C   PHE A 165      16.706  26.962  -4.231  1.00 19.55           C  
ANISOU 2627  C   PHE A 165     1858   3021   2549     63   -146   -847       C  
ATOM   2628  O   PHE A 165      17.492  27.379  -3.395  1.00 17.36           O  
ANISOU 2628  O   PHE A 165     1468   2776   2352     41   -229   -802       O  
ATOM   2629  CB  PHE A 165      14.325  26.499  -3.751  1.00 14.76           C  
ANISOU 2629  CB  PHE A 165     1484   2315   1810     64   -252   -810       C  
ATOM   2630  CG  PHE A 165      14.159  27.441  -2.564  1.00 12.95           C  
ANISOU 2630  CG  PHE A 165     1273   2062   1586     33   -313   -759       C  
ATOM   2631  CD1 PHE A 165      13.940  26.949  -1.301  1.00 12.81           C  
ANISOU 2631  CD1 PHE A 165     1304   1984   1578     73   -388   -743       C  
ATOM   2632  CD2 PHE A 165      14.207  28.815  -2.745  1.00 18.49           C  
ANISOU 2632  CD2 PHE A 165     1989   2776   2261    -52   -272   -729       C  
ATOM   2633  CE1 PHE A 165      13.768  27.817  -0.221  1.00 16.33           C  
ANISOU 2633  CE1 PHE A 165     1855   2370   1979     13   -406   -712       C  
ATOM   2634  CE2 PHE A 165      14.011  29.676  -1.697  1.00 18.56           C  
ANISOU 2634  CE2 PHE A 165     2089   2715   2247    -98   -279   -699       C  
ATOM   2635  CZ  PHE A 165      13.823  29.181  -0.422  1.00 13.66           C  
ANISOU 2635  CZ  PHE A 165     1557   2024   1608    -76   -340   -698       C  
ATOM   2636  H   PHE A 165      16.781  25.529  -2.254  1.00 21.46           H  
ATOM   2637  HA  PHE A 165      15.697  25.253  -4.616  1.00 19.32           H  
ATOM   2638  HB2 PHE A 165      14.134  27.004  -4.557  1.00 17.71           H  
ATOM   2639  HB3 PHE A 165      13.676  25.784  -3.652  1.00 17.71           H  
ATOM   2640  HD1 PHE A 165      13.908  26.030  -1.163  1.00 15.37           H  
ATOM   2641  HD2 PHE A 165      14.337  29.158  -3.600  1.00 22.19           H  
ATOM   2642  HE1 PHE A 165      13.628  27.477   0.633  1.00 19.59           H  
ATOM   2643  HE2 PHE A 165      14.059  30.594  -1.835  1.00 22.27           H  
ATOM   2644  HZ  PHE A 165      13.705  29.764   0.293  1.00 16.39           H  
ATOM   2645  N   LYS A 166      16.667  27.404  -5.487  1.00 15.63           N  
ANISOU 2645  N   LYS A 166     1412   2548   1980      3    -25   -874       N  
ATOM   2646  CA  LYS A 166      17.541  28.473  -5.934  1.00 16.38           C  
ANISOU 2646  CA  LYS A 166     1415   2705   2103    -71     45   -860       C  
ATOM   2647  C   LYS A 166      16.648  29.650  -6.283  1.00 21.34           C  
ANISOU 2647  C   LYS A 166     2160   3337   2610   -177     19   -821       C  
ATOM   2648  O   LYS A 166      15.638  29.474  -6.944  1.00 25.48           O  
ANISOU 2648  O   LYS A 166     2812   3837   3031   -204     16   -805       O  
ATOM   2649  CB  LYS A 166      18.305  28.066  -7.222  1.00 21.52           C  
ANISOU 2649  CB  LYS A 166     2054   3357   2765    -56    263   -913       C  
ATOM   2650  CG  LYS A 166      18.852  26.656  -7.248  1.00 28.18           C  
ANISOU 2650  CG  LYS A 166     2852   4135   3722     81    380   -952       C  
ATOM   2651  H   LYS A 166      16.142  27.099  -6.096  1.00 18.76           H  
ATOM   2652  HA  LYS A 166      18.169  28.726  -5.239  1.00 19.66           H  
ATOM   2653  HB2 LYS A 166      17.701  28.157  -7.976  1.00 25.82           H  
ATOM   2654  HB3 LYS A 166      19.055  28.670  -7.335  1.00 25.82           H  
ATOM   2655  N   THR A 167      17.037  30.852  -5.907  1.00 20.23           N  
ANISOU 2655  N   THR A 167     1976   3218   2492   -253     -1   -784       N  
ATOM   2656  CA  THR A 167      16.329  32.032  -6.357  1.00 15.73           C  
ANISOU 2656  CA  THR A 167     1503   2628   1844   -337     22   -728       C  
ATOM   2657  C   THR A 167      17.194  32.794  -7.361  1.00 21.55           C  
ANISOU 2657  C   THR A 167     2197   3421   2569   -423    135   -732       C  
ATOM   2658  O   THR A 167      18.425  32.683  -7.354  1.00 19.14           O  
ANISOU 2658  O   THR A 167     1754   3165   2355   -428    187   -763       O  
ATOM   2659  CB  THR A 167      15.956  32.953  -5.174  1.00 16.75           C  
ANISOU 2659  CB  THR A 167     1694   2684   1986   -372    -33   -685       C  
ATOM   2660  OG1 THR A 167      17.138  33.347  -4.473  1.00 16.28           O  
ANISOU 2660  OG1 THR A 167     1565   2650   1972   -445    -77   -711       O  
ATOM   2661  CG2 THR A 167      15.030  32.243  -4.190  1.00 13.95           C  
ANISOU 2661  CG2 THR A 167     1409   2253   1636   -290   -100   -672       C  
ATOM   2662  H   THR A 167      17.707  31.013  -5.392  1.00 24.27           H  
ATOM   2663  HA  THR A 167      15.510  31.764  -6.802  1.00 18.87           H  
ATOM   2664  HB  THR A 167      15.501  33.742  -5.509  1.00 20.10           H  
ATOM   2665  HG1 THR A 167      17.654  33.761  -4.991  1.00 19.54           H  
ATOM   2666 HG21 THR A 167      14.808  32.837  -3.456  1.00 16.74           H  
ATOM   2667 HG22 THR A 167      14.213  31.976  -4.639  1.00 16.74           H  
ATOM   2668 HG23 THR A 167      15.468  31.453  -3.836  1.00 16.74           H  
ATOM   2669  N   ARG A 168      16.520  33.564  -8.215  1.00 17.54           N  
ANISOU 2669  N   ARG A 168     1790   2902   1972   -491    172   -669       N  
ATOM   2670  CA  ARG A 168      17.142  34.323  -9.301  1.00 21.59           C  
ANISOU 2670  CA  ARG A 168     2310   3455   2437   -587    288   -659       C  
ATOM   2671  C   ARG A 168      16.812  35.794  -9.118  1.00 17.23           C  
ANISOU 2671  C   ARG A 168     1799   2857   1890   -661    282   -569       C  
ATOM   2672  O   ARG A 168      15.649  36.168  -9.155  1.00 19.48           O  
ANISOU 2672  O   ARG A 168     2166   3082   2154   -652    237   -464       O  
ATOM   2673  CB  ARG A 168      16.598  33.831 -10.662  1.00 21.04           C  
ANISOU 2673  CB  ARG A 168     2384   3397   2213   -633    329   -644       C  
ATOM   2674  CG  ARG A 168      16.778  32.329 -10.885  1.00 27.96           C  
ANISOU 2674  CG  ARG A 168     3299   4267   3057   -570    374   -745       C  
ATOM   2675  CD  ARG A 168      16.142  31.813 -12.189  1.00 30.82           C  
ANISOU 2675  CD  ARG A 168     3895   4612   3202   -677    392   -739       C  
ATOM   2676  NE  ARG A 168      14.749  32.241 -12.389  1.00 41.54           N  
ANISOU 2676  NE  ARG A 168     5336   5966   4481   -763    197   -583       N  
ATOM   2677  CZ  ARG A 168      13.670  31.604 -11.913  1.00 39.82           C  
ANISOU 2677  CZ  ARG A 168     5125   5722   4284   -736     34   -520       C  
ATOM   2678  NH1 ARG A 168      13.791  30.476 -11.207  1.00 37.97           N  
ANISOU 2678  NH1 ARG A 168     4861   5458   4110   -629     38   -626       N  
ATOM   2679  NH2 ARG A 168      12.458  32.091 -12.171  1.00 34.43           N  
ANISOU 2679  NH2 ARG A 168     4461   5035   3585   -817   -130   -323       N  
ATOM   2680  H   ARG A 168      15.666  33.665  -8.184  1.00 21.05           H  
ATOM   2681  HA  ARG A 168      18.105  34.207  -9.282  1.00 25.91           H  
ATOM   2682  HB2 ARG A 168      15.650  34.027 -10.710  1.00 25.25           H  
ATOM   2683  HB3 ARG A 168      17.067  34.295 -11.374  1.00 25.25           H  
ATOM   2684  HG2 ARG A 168      17.726  32.129 -10.919  1.00 33.55           H  
ATOM   2685  HG3 ARG A 168      16.368  31.852 -10.146  1.00 33.55           H  
ATOM   2686  HD2 ARG A 168      16.662  32.139 -12.939  1.00 36.98           H  
ATOM   2687  HD3 ARG A 168      16.154  30.843 -12.178  1.00 36.98           H  
ATOM   2688  HE  ARG A 168      14.616  32.957 -12.847  1.00 49.85           H  
ATOM   2689 HH11 ARG A 168      14.571  30.155 -11.040  1.00 45.57           H  
ATOM   2690 HH12 ARG A 168      13.089  30.077 -10.910  1.00 45.57           H  
ATOM   2691 HH21 ARG A 168      12.374  32.815 -12.627  1.00 41.31           H  
ATOM   2692 HH22 ARG A 168      11.760  31.688 -11.872  1.00 41.31           H  
ATOM   2693  N   HIS A 169      17.828  36.619  -8.895  1.00 19.45           N  
ANISOU 2693  N   HIS A 169     2014   3150   2225   -737    334   -588       N  
ATOM   2694  CA  HIS A 169      17.632  38.052  -8.631  1.00 18.21           C  
ANISOU 2694  CA  HIS A 169     1933   2915   2072   -822    357   -520       C  
ATOM   2695  C   HIS A 169      18.224  38.876  -9.766  1.00 20.79           C  
ANISOU 2695  C   HIS A 169     2261   3278   2361   -928    470   -486       C  
ATOM   2696  O   HIS A 169      19.429  38.843  -9.995  1.00 26.81           O  
ANISOU 2696  O   HIS A 169     2909   4111   3168   -987    534   -537       O  
ATOM   2697  CB  HIS A 169      18.276  38.469  -7.303  1.00 18.52           C  
ANISOU 2697  CB  HIS A 169     1960   2907   2169   -885    300   -565       C  
ATOM   2698  CG  HIS A 169      17.837  37.625  -6.152  1.00 20.81           C  
ANISOU 2698  CG  HIS A 169     2275   3160   2472   -802    194   -601       C  
ATOM   2699  ND1 HIS A 169      16.619  37.800  -5.534  1.00 20.54           N  
ANISOU 2699  ND1 HIS A 169     2390   2996   2417   -738    207   -560       N  
ATOM   2700  CD2 HIS A 169      18.429  36.574  -5.534  1.00 23.63           C  
ANISOU 2700  CD2 HIS A 169     2521   3581   2876   -764     91   -653       C  
ATOM   2701  CE1 HIS A 169      16.478  36.893  -4.582  1.00 21.07           C  
ANISOU 2701  CE1 HIS A 169     2464   3054   2488   -678    118   -605       C  
ATOM   2702  NE2 HIS A 169      17.564  36.136  -4.562  1.00 22.15           N  
ANISOU 2702  NE2 HIS A 169     2446   3310   2659   -695     28   -659       N  
ATOM   2703  H   HIS A 169      18.653  36.377  -8.891  1.00 23.34           H  
ATOM   2704  HA  HIS A 169      16.682  38.242  -8.581  1.00 21.86           H  
ATOM   2705  HB2 HIS A 169      19.239  38.391  -7.381  1.00 22.22           H  
ATOM   2706  HB3 HIS A 169      18.032  39.388  -7.110  1.00 22.22           H  
ATOM   2707  HD1 HIS A 169      16.037  38.398  -5.742  1.00 24.65           H  
ATOM   2708  HD2 HIS A 169      19.261  36.212  -5.737  1.00 28.35           H  
ATOM   2709  HE1 HIS A 169      15.746  36.809  -4.014  1.00 25.29           H  
ATOM   2710  HE2 HIS A 169      17.710  35.485  -4.018  1.00 26.58           H  
ATOM   2711  N   ASN A 170      17.362  39.616 -10.456  1.00 23.54           N  
ANISOU 2711  N   ASN A 170     2722   3572   2651   -952    498   -370       N  
ATOM   2712  CA  ASN A 170      17.800  40.466 -11.558  1.00 23.89           C  
ANISOU 2712  CA  ASN A 170     2804   3636   2635  -1063    602   -316       C  
ATOM   2713  C   ASN A 170      18.814  41.469 -11.074  1.00 26.40           C  
ANISOU 2713  C   ASN A 170     3082   3925   3025  -1167    668   -349       C  
ATOM   2714  O   ASN A 170      18.625  42.085 -10.031  1.00 24.43           O  
ANISOU 2714  O   ASN A 170     2884   3569   2829  -1182    638   -347       O  
ATOM   2715  CB  ASN A 170      16.614  41.199 -12.174  1.00 33.06           C  
ANISOU 2715  CB  ASN A 170     4080   4724   3757  -1071    581   -132       C  
ATOM   2716  CG  ASN A 170      15.784  40.304 -13.066  1.00 33.14           C  
ANISOU 2716  CG  ASN A 170     4144   4792   3654  -1060    484    -59       C  
ATOM   2717  OD1 ASN A 170      15.908  39.076 -13.019  1.00 29.64           O  
ANISOU 2717  OD1 ASN A 170     3684   4413   3166  -1019    446   -170       O  
ATOM   2718  ND2 ASN A 170      14.941  40.910 -13.893  1.00 37.25           N  
ANISOU 2718  ND2 ASN A 170     4742   5283   4128  -1117    431    146       N  
ATOM   2719  H   ASN A 170      16.516  39.644 -10.306  1.00 28.25           H  
ATOM   2720  HA  ASN A 170      18.212  39.918 -12.244  1.00 28.66           H  
ATOM   2721  HB2 ASN A 170      16.043  41.531 -11.464  1.00 39.67           H  
ATOM   2722  HB3 ASN A 170      16.942  41.938 -12.711  1.00 39.67           H  
ATOM   2723 HD21 ASN A 170      14.889  41.769 -13.901  1.00 44.70           H  
ATOM   2724 HD22 ASN A 170      14.446  40.445 -14.420  1.00 44.70           H  
ATOM   2725  N   ILE A 171      19.898  41.604 -11.834  1.00 28.94           N  
ANISOU 2725  N   ILE A 171     3872   4811   2312  -1474   1250   -428       N  
ATOM   2726  CA  ILE A 171      20.938  42.582 -11.558  1.00 30.46           C  
ANISOU 2726  CA  ILE A 171     4029   4997   2548  -1641   1350   -445       C  
ATOM   2727  C   ILE A 171      20.766  43.725 -12.535  1.00 37.37           C  
ANISOU 2727  C   ILE A 171     5028   5789   3381  -1654   1468   -301       C  
ATOM   2728  O   ILE A 171      20.389  43.515 -13.693  1.00 38.00           O  
ANISOU 2728  O   ILE A 171     5154   5915   3368  -1545   1492   -223       O  
ATOM   2729  CB  ILE A 171      22.318  41.950 -11.713  1.00 31.56           C  
ANISOU 2729  CB  ILE A 171     3980   5334   2680  -1693   1379   -580       C  
ATOM   2730  CG1 ILE A 171      22.452  40.799 -10.726  1.00 34.78           C  
ANISOU 2730  CG1 ILE A 171     4254   5831   3131  -1656   1257   -715       C  
ATOM   2731  CG2 ILE A 171      23.424  42.976 -11.508  1.00 35.16           C  
ANISOU 2731  CG2 ILE A 171     4395   5786   3179  -1861   1488   -610       C  
ATOM   2732  CD1 ILE A 171      23.508  39.813 -11.098  1.00 43.98           C  
ANISOU 2732  CD1 ILE A 171     5230   7205   4277  -1630   1248   -844       C  
ATOM   2733  H   ILE A 171      20.055  41.127 -12.532  1.00 34.73           H  
ATOM   2734  HA  ILE A 171      20.845  42.921 -10.654  1.00 36.56           H  
ATOM   2735  HB  ILE A 171      22.393  41.594 -12.612  1.00 37.88           H  
ATOM   2736 HG12 ILE A 171      22.676  41.160  -9.854  1.00 41.74           H  
ATOM   2737 HG13 ILE A 171      21.607  40.326 -10.680  1.00 41.74           H  
ATOM   2738 HG21 ILE A 171      24.283  42.539 -11.614  1.00 42.19           H  
ATOM   2739 HG22 ILE A 171      23.327  43.681 -12.167  1.00 42.19           H  
ATOM   2740 HG23 ILE A 171      23.349  43.346 -10.614  1.00 42.19           H  
ATOM   2741 HD11 ILE A 171      23.535  39.113 -10.427  1.00 52.78           H  
ATOM   2742 HD12 ILE A 171      23.294  39.434 -11.964  1.00 52.78           H  
ATOM   2743 HD13 ILE A 171      24.364  40.268 -11.138  1.00 52.78           H  
ATOM   2744  N   GLU A 172      21.050  44.935 -12.060  1.00 35.72           N  
ANISOU 2744  N   GLU A 172     4868   5464   3241  -1778   1540   -267       N  
ATOM   2745  CA  GLU A 172      20.784  46.159 -12.812  1.00 35.27           C  
ANISOU 2745  CA  GLU A 172     4937   5296   3167  -1789   1649   -115       C  
ATOM   2746  C   GLU A 172      21.324  46.137 -14.249  1.00 41.80           C  
ANISOU 2746  C   GLU A 172     5746   6246   3889  -1757   1757    -54       C  
ATOM   2747  O   GLU A 172      20.802  46.833 -15.117  1.00 40.59           O  
ANISOU 2747  O   GLU A 172     5706   6036   3682  -1700   1824     99       O  
ATOM   2748  CB  GLU A 172      21.378  47.361 -12.060  1.00 37.85           C  
ANISOU 2748  CB  GLU A 172     5267   5514   3599  -1943   1724   -133       C  
ATOM   2749  H   GLU A 172      21.404  45.076 -11.289  1.00 42.87           H  
ATOM   2750  HA  GLU A 172      19.824  46.288 -12.862  1.00 42.32           H  
ATOM   2751  N   ASP A 173      22.355  45.335 -14.501  1.00 42.04           N  
ANISOU 2751  N   ASP A 173     5630   6453   3889  -1786   1771   -174       N  
ATOM   2752  CA  ASP A 173      23.005  45.326 -15.804  1.00 45.82           C  
ANISOU 2752  CA  ASP A 173     6078   7057   4273  -1772   1880   -137       C  
ATOM   2753  C   ASP A 173      22.483  44.225 -16.712  1.00 44.14           C  
ANISOU 2753  C   ASP A 173     5856   6968   3949  -1602   1818   -132       C  
ATOM   2754  O   ASP A 173      22.985  44.055 -17.806  1.00 42.15           O  
ANISOU 2754  O   ASP A 173     5570   6838   3608  -1573   1894   -118       O  
ATOM   2755  CB  ASP A 173      24.526  45.186 -15.650  1.00 51.23           C  
ANISOU 2755  CB  ASP A 173     6601   7870   4994  -1908   1944   -282       C  
ATOM   2756  CG  ASP A 173      24.953  43.805 -15.154  1.00 54.58           C  
ANISOU 2756  CG  ASP A 173     6860   8447   5430  -1877   1826   -461       C  
ATOM   2757  OD1 ASP A 173      24.083  42.961 -14.831  1.00 47.20           O  
ANISOU 2757  OD1 ASP A 173     5938   7507   4489  -1759   1699   -474       O  
ATOM   2758  OD2 ASP A 173      26.180  43.570 -15.071  1.00 55.58           O  
ANISOU 2758  OD2 ASP A 173     6838   8701   5579  -1968   1861   -591       O  
ATOM   2759  H   ASP A 173      22.695  44.787 -13.932  1.00 50.44           H  
ATOM   2760  HA  ASP A 173      22.831  46.174 -16.242  1.00 54.98           H  
ATOM   2761  HB2 ASP A 173      24.944  45.337 -16.512  1.00 61.47           H  
ATOM   2762  HB3 ASP A 173      24.839  45.844 -15.010  1.00 61.47           H  
ATOM   2763  N   GLY A 174      21.504  43.460 -16.243  1.00 41.25           N  
ANISOU 2763  N   GLY A 174     5514   6570   3591  -1490   1680   -158       N  
ATOM   2764  CA  GLY A 174      20.903  42.408 -17.048  1.00 37.22           C  
ANISOU 2764  CA  GLY A 174     4996   6159   2988  -1316   1611   -169       C  
ATOM   2765  C   GLY A 174      21.309  40.982 -16.708  1.00 41.85           C  
ANISOU 2765  C   GLY A 174     5421   6878   3601  -1276   1508   -345       C  
ATOM   2766  O   GLY A 174      20.684  40.038 -17.185  1.00 40.76           O  
ANISOU 2766  O   GLY A 174     5276   6795   3417  -1125   1428   -374       O  
ATOM   2767  H   GLY A 174      21.167  43.533 -15.455  1.00 49.51           H  
ATOM   2768  HA2 GLY A 174      19.939  42.467 -16.963  1.00 44.66           H  
ATOM   2769  HA3 GLY A 174      21.128  42.564 -17.978  1.00 44.66           H  
ATOM   2770  N   SER A 175      22.341  40.806 -15.886  1.00 38.13           N  
ANISOU 2770  N   SER A 175     4815   6463   3211  -1399   1505   -468       N  
ATOM   2771  CA  SER A 175      22.720  39.474 -15.449  1.00 35.66           C  
ANISOU 2771  CA  SER A 175     4337   6273   2937  -1350   1400   -629       C  
ATOM   2772  C   SER A 175      21.800  39.055 -14.284  1.00 32.11           C  
ANISOU 2772  C   SER A 175     3923   5719   2559  -1296   1274   -645       C  
ATOM   2773  O   SER A 175      20.874  39.788 -13.917  1.00 31.23           O  
ANISOU 2773  O   SER A 175     3961   5445   2460  -1300   1267   -538       O  
ATOM   2774  CB  SER A 175      24.203  39.434 -15.053  1.00 42.97           C  
ANISOU 2774  CB  SER A 175     5094   7320   3913  -1484   1442   -758       C  
ATOM   2775  OG  SER A 175      24.536  40.461 -14.120  1.00 43.15           O  
ANISOU 2775  OG  SER A 175     5147   7243   4004  -1636   1488   -744       O  
ATOM   2776  H   SER A 175      22.831  41.439 -15.571  1.00 45.76           H  
ATOM   2777  HA  SER A 175      22.586  38.849 -16.180  1.00 42.79           H  
ATOM   2778  HB2 SER A 175      24.394  38.572 -14.650  1.00 51.57           H  
ATOM   2779  HB3 SER A 175      24.742  39.550 -15.851  1.00 51.57           H  
ATOM   2780  HG  SER A 175      24.080  40.373 -13.420  1.00 51.78           H  
ATOM   2781  N   VAL A 176      22.051  37.874 -13.726  1.00 30.32           N  
ANISOU 2781  N   VAL A 176     3555   5584   2383  -1239   1174   -778       N  
ATOM   2782  CA  VAL A 176      21.212  37.309 -12.676  1.00 30.02           C  
ANISOU 2782  CA  VAL A 176     3537   5460   2409  -1169   1055   -799       C  
ATOM   2783  C   VAL A 176      22.087  36.785 -11.544  1.00 34.94           C  
ANISOU 2783  C   VAL A 176     3995   6170   3109  -1226   1005   -931       C  
ATOM   2784  O   VAL A 176      23.030  36.026 -11.768  1.00 30.25           O  
ANISOU 2784  O   VAL A 176     3233   5736   2524  -1205    995  -1047       O  
ATOM   2785  CB  VAL A 176      20.338  36.154 -13.208  1.00 30.14           C  
ANISOU 2785  CB  VAL A 176     3556   5483   2411   -973    961   -820       C  
ATOM   2786  CG1 VAL A 176      19.479  35.569 -12.107  1.00 34.72           C  
ANISOU 2786  CG1 VAL A 176     4163   5960   3069   -898    844   -840       C  
ATOM   2787  CG2 VAL A 176      19.468  36.637 -14.342  1.00 32.51           C  
ANISOU 2787  CG2 VAL A 176     4007   5721   2623   -901   1002   -701       C  
ATOM   2788  H   VAL A 176      22.715  37.372 -13.944  1.00 36.39           H  
ATOM   2789  HA  VAL A 176      20.629  37.999 -12.322  1.00 36.02           H  
ATOM   2790  HB  VAL A 176      20.914  35.451 -13.548  1.00 36.17           H  
ATOM   2791 HG11 VAL A 176      18.944  34.847 -12.475  1.00 41.67           H  
ATOM   2792 HG12 VAL A 176      20.054  35.229 -11.404  1.00 41.67           H  
ATOM   2793 HG13 VAL A 176      18.900  36.263 -11.755  1.00 41.67           H  
ATOM   2794 HG21 VAL A 176      18.928  35.898 -14.662  1.00 39.01           H  
ATOM   2795 HG22 VAL A 176      18.895  37.350 -14.018  1.00 39.01           H  
ATOM   2796 HG23 VAL A 176      20.035  36.966 -15.057  1.00 39.01           H  
ATOM   2797  N   GLN A 177      21.749  37.190 -10.325  1.00 27.08           N  
ANISOU 2797  N   GLN A 177     3046   5074   2168  -1289    969   -917       N  
ATOM   2798  CA  GLN A 177      22.442  36.721  -9.138  1.00 26.85           C  
ANISOU 2798  CA  GLN A 177     2869   5129   2202  -1325    912  -1033       C  
ATOM   2799  C   GLN A 177      21.693  35.503  -8.610  1.00 26.93           C  
ANISOU 2799  C   GLN A 177     2859   5123   2251  -1158    785  -1069       C  
ATOM   2800  O   GLN A 177      20.512  35.600  -8.293  1.00 28.02           O  
ANISOU 2800  O   GLN A 177     3142   5106   2401  -1105    738   -990       O  
ATOM   2801  CB  GLN A 177      22.460  37.841  -8.098  1.00 26.77           C  
ANISOU 2801  CB  GLN A 177     2924   5020   2229  -1481    942  -1001       C  
ATOM   2802  CG  GLN A 177      22.923  37.418  -6.692  1.00 31.06           C  
ANISOU 2802  CG  GLN A 177     3336   5637   2827  -1505    868  -1108       C  
ATOM   2803  CD  GLN A 177      24.395  37.064  -6.681  1.00 29.64           C  
ANISOU 2803  CD  GLN A 177     2947   5658   2656  -1541    881  -1245       C  
ATOM   2804  OE1 GLN A 177      25.231  37.900  -6.989  1.00 33.81           O  
ANISOU 2804  OE1 GLN A 177     3458   6211   3177  -1667    969  -1263       O  
ATOM   2805  NE2 GLN A 177      24.712  35.810  -6.371  1.00 31.64           N  
ANISOU 2805  NE2 GLN A 177     3047   6046   2930  -1412    792  -1344       N  
ATOM   2806  H   GLN A 177      21.113  37.744 -10.160  1.00 32.49           H  
ATOM   2807  HA  GLN A 177      23.353  36.469  -9.356  1.00 32.22           H  
ATOM   2808  HB2 GLN A 177      23.061  38.537  -8.405  1.00 32.13           H  
ATOM   2809  HB3 GLN A 177      21.563  38.199  -8.014  1.00 32.13           H  
ATOM   2810  HG2 GLN A 177      22.781  38.151  -6.074  1.00 37.27           H  
ATOM   2811  HG3 GLN A 177      22.420  36.638  -6.410  1.00 37.27           H  
ATOM   2812 HE21 GLN A 177      24.093  35.242  -6.189  1.00 37.97           H  
ATOM   2813 HE22 GLN A 177      25.537  35.567  -6.354  1.00 37.97           H  
ATOM   2814  N   LEU A 178      22.378  34.364  -8.536  1.00 25.39           N  
ANISOU 2814  N   LEU A 178     2487   5073   2086  -1066    729  -1190       N  
ATOM   2815  CA  LEU A 178      21.796  33.140  -7.995  1.00 24.21           C  
ANISOU 2815  CA  LEU A 178     2306   4897   1994   -893    608  -1233       C  
ATOM   2816  C   LEU A 178      21.982  33.075  -6.468  1.00 23.59           C  
ANISOU 2816  C   LEU A 178     2179   4825   1961   -917    543  -1276       C  
ATOM   2817  O   LEU A 178      23.007  33.515  -5.933  1.00 24.59           O  
ANISOU 2817  O   LEU A 178     2189   5071   2082  -1035    580  -1340       O  
ATOM   2818  CB  LEU A 178      22.435  31.902  -8.644  1.00 24.86           C  
ANISOU 2818  CB  LEU A 178     2223   5120   2102   -763    573  -1343       C  
ATOM   2819  H   LEU A 178      23.193  34.274  -8.796  1.00 30.46           H  
ATOM   2820  HA  LEU A 178      20.846  33.127  -8.186  1.00 29.05           H  
ATOM   2821  N   ALA A 179      20.995  32.504  -5.787  1.00 22.14           N  
ANISOU 2821  N   ALA A 179     2079   4507   1826   -800    440  -1243       N  
ATOM   2822  CA  ALA A 179      21.129  32.228  -4.365  1.00 21.69           C  
ANISOU 2822  CA  ALA A 179     1977   4442   1821   -781    343  -1272       C  
ATOM   2823  C   ALA A 179      20.602  30.829  -4.054  1.00 20.85           C  
ANISOU 2823  C   ALA A 179     1853   4273   1797   -570    222  -1291       C  
ATOM   2824  O   ALA A 179      19.417  30.552  -4.203  1.00 20.44           O  
ANISOU 2824  O   ALA A 179     1937   4051   1777   -485    188  -1222       O  
ATOM   2825  CB  ALA A 179      20.396  33.277  -3.558  1.00 28.57           C  
ANISOU 2825  CB  ALA A 179     3005   5158   2692   -896    343  -1175       C  
ATOM   2826  H   ALA A 179      20.240  32.268  -6.124  1.00 26.57           H  
ATOM   2827  HA  ALA A 179      22.067  32.259  -4.120  1.00 26.03           H  
ATOM   2828  HB1 ALA A 179      20.496  33.077  -2.614  1.00 34.28           H  
ATOM   2829  HB2 ALA A 179      20.776  34.148  -3.753  1.00 34.28           H  
ATOM   2830  HB3 ALA A 179      19.457  33.263  -3.801  1.00 34.28           H  
ATOM   2831  N   ASP A 180      21.502  29.944  -3.645  1.00 21.75           N  
ANISOU 2831  N   ASP A 180     1791   4506   1967   -479    160  -1370       N  
ATOM   2832  CA  ASP A 180      21.141  28.584  -3.285  1.00 23.64           C  
ANISOU 2832  CA  ASP A 180     1999   4683   2300   -277     55  -1386       C  
ATOM   2833  C   ASP A 180      20.672  28.554  -1.846  1.00 20.43           C  
ANISOU 2833  C   ASP A 180     1660   4161   1941   -252    -42  -1313       C  
ATOM   2834  O   ASP A 180      21.423  28.924  -0.948  1.00 21.06           O  
ANISOU 2834  O   ASP A 180     1659   4332   2012   -315    -71  -1321       O  
ATOM   2835  CB  ASP A 180      22.353  27.666  -3.383  1.00 25.35           C  
ANISOU 2835  CB  ASP A 180     1996   5074   2561   -180     29  -1494       C  
ATOM   2836  CG  ASP A 180      22.528  27.073  -4.732  1.00 27.70           C  
ANISOU 2836  CG  ASP A 180     2224   5447   2855   -115     88  -1578       C  
ATOM   2837  OD1 ASP A 180      21.567  27.054  -5.521  1.00 28.78           O  
ANISOU 2837  OD1 ASP A 180     2481   5485   2969    -92    124  -1554       O  
ATOM   2838  OD2 ASP A 180      23.647  26.606  -5.005  1.00 25.94           O  
ANISOU 2838  OD2 ASP A 180     1814   5395   2648    -81     96  -1679       O  
ATOM   2839  H   ASP A 180      22.342  30.112  -3.567  1.00 26.10           H  
ATOM   2840  HA  ASP A 180      20.436  28.254  -3.864  1.00 28.37           H  
ATOM   2841  HB2 ASP A 180      23.151  28.175  -3.174  1.00 30.42           H  
ATOM   2842  HB3 ASP A 180      22.249  26.939  -2.749  1.00 30.42           H  
ATOM   2843  N   HIS A 181      19.438  28.112  -1.643  1.00 18.99           N  
ANISOU 2843  N   HIS A 181     1619   3791   1807   -160    -87  -1252       N  
ATOM   2844  CA  HIS A 181      18.868  27.989  -0.295  1.00 18.19           C  
ANISOU 2844  CA  HIS A 181     1594   3567   1750   -126   -175  -1178       C  
ATOM   2845  C   HIS A 181      18.845  26.542   0.154  1.00 19.03           C  
ANISOU 2845  C   HIS A 181     1637   3634   1959     78   -258  -1187       C  
ATOM   2846  O   HIS A 181      18.310  25.669  -0.545  1.00 18.40           O  
ANISOU 2846  O   HIS A 181     1574   3475   1941    199   -251  -1217       O  
ATOM   2847  CB  HIS A 181      17.425  28.491  -0.272  1.00 17.71           C  
ANISOU 2847  CB  HIS A 181     1744   3300   1686   -165   -163  -1095       C  
ATOM   2848  CG  HIS A 181      17.269  29.959  -0.518  1.00 17.79           C  
ANISOU 2848  CG  HIS A 181     1849   3277   1633   -345    -79  -1028       C  
ATOM   2849  ND1 HIS A 181      17.580  30.558  -1.720  1.00 17.09           N  
ANISOU 2849  ND1 HIS A 181     1750   3265   1480   -426     18  -1052       N  
ATOM   2850  CD2 HIS A 181      16.779  30.943   0.278  1.00 15.88           C  
ANISOU 2850  CD2 HIS A 181     1720   2925   1390   -449    -75   -936       C  
ATOM   2851  CE1 HIS A 181      17.309  31.850  -1.648  1.00 16.89           C  
ANISOU 2851  CE1 HIS A 181     1826   3175   1415   -575     77   -980       C  
ATOM   2852  NE2 HIS A 181      16.811  32.106  -0.450  1.00 17.12           N  
ANISOU 2852  NE2 HIS A 181     1928   3088   1490   -588     21   -913       N  
ATOM   2853  H   HIS A 181      18.902  27.873  -2.271  1.00 22.79           H  
ATOM   2854  HA  HIS A 181      19.392  28.507   0.335  1.00 21.83           H  
ATOM   2855  HB2 HIS A 181      16.924  28.023  -0.958  1.00 21.25           H  
ATOM   2856  HB3 HIS A 181      17.045  28.297   0.599  1.00 21.25           H  
ATOM   2857  HD1 HIS A 181      17.907  30.155  -2.406  1.00 20.51           H  
ATOM   2858  HD2 HIS A 181      16.473  30.846   1.151  1.00 19.06           H  
ATOM   2859  HE1 HIS A 181      17.439  32.472  -2.327  1.00 20.27           H  
ATOM   2860  HE2 HIS A 181      16.568  32.880  -0.165  1.00 20.55           H  
ATOM   2861  N   TYR A 182      19.410  26.284   1.333  1.00 18.91           N  
ANISOU 2861  N   TYR A 182     1549   3673   1962    120   -335  -1163       N  
ATOM   2862  CA  TYR A 182      19.297  24.992   1.986  1.00 19.02           C  
ANISOU 2862  CA  TYR A 182     1531   3621   2073    314   -416  -1137       C  
ATOM   2863  C   TYR A 182      18.682  25.197   3.368  1.00 18.34           C  
ANISOU 2863  C   TYR A 182     1555   3433   1982    306   -481  -1034       C  
ATOM   2864  O   TYR A 182      19.163  26.008   4.151  1.00 18.69           O  
ANISOU 2864  O   TYR A 182     1571   3576   1953    200   -504  -1018       O  
ATOM   2865  CB  TYR A 182      20.673  24.346   2.064  1.00 20.67           C  
ANISOU 2865  CB  TYR A 182     1529   4021   2303    406   -451  -1204       C  
ATOM   2866  CG  TYR A 182      21.256  24.169   0.669  1.00 21.36           C  
ANISOU 2866  CG  TYR A 182     1507   4216   2393    403   -379  -1316       C  
ATOM   2867  CD1 TYR A 182      22.219  25.037   0.172  1.00 23.03           C  
ANISOU 2867  CD1 TYR A 182     1617   4616   2519    259   -320  -1387       C  
ATOM   2868  CD2 TYR A 182      20.798  23.163  -0.150  1.00 22.16           C  
ANISOU 2868  CD2 TYR A 182     1610   4227   2582    535   -359  -1357       C  
ATOM   2869  CE1 TYR A 182      22.727  24.870  -1.126  1.00 24.00           C  
ANISOU 2869  CE1 TYR A 182     1643   4841   2635    253   -246  -1488       C  
ATOM   2870  CE2 TYR A 182      21.286  22.999  -1.418  1.00 27.01           C  
ANISOU 2870  CE2 TYR A 182     2124   4948   3190    532   -292  -1465       C  
ATOM   2871  CZ  TYR A 182      22.242  23.852  -1.894  1.00 22.71           C  
ANISOU 2871  CZ  TYR A 182     1484   4596   2550    392   -237  -1525       C  
ATOM   2872  OH  TYR A 182      22.679  23.660  -3.162  1.00 23.42           O  
ANISOU 2872  OH  TYR A 182     1479   4792   2627    391   -165  -1630       O  
ATOM   2873  H   TYR A 182      19.872  26.856   1.779  1.00 22.69           H  
ATOM   2874  HA  TYR A 182      18.712  24.416   1.469  1.00 22.82           H  
ATOM   2875  HB2 TYR A 182      21.268  24.913   2.577  1.00 24.80           H  
ATOM   2876  HB3 TYR A 182      20.596  23.472   2.478  1.00 24.80           H  
ATOM   2877  HD1 TYR A 182      22.538  25.728   0.706  1.00 27.64           H  
ATOM   2878  HD2 TYR A 182      20.145  22.581   0.165  1.00 26.59           H  
ATOM   2879  HE1 TYR A 182      23.373  25.450  -1.461  1.00 28.80           H  
ATOM   2880  HE2 TYR A 182      20.965  22.312  -1.956  1.00 32.41           H  
ATOM   2881  HH  TYR A 182      23.254  24.240  -3.359  1.00 28.10           H  
ATOM   2882  N   GLN A 183      17.631  24.439   3.646  1.00 17.65           N  
ANISOU 2882  N   GLN A 183     1582   3151   1973    418   -505   -977       N  
ATOM   2883  CA  GLN A 183      16.696  24.771   4.706  1.00 16.67           C  
ANISOU 2883  CA  GLN A 183     1607   2889   1839    382   -539   -882       C  
ATOM   2884  C   GLN A 183      16.279  23.521   5.461  1.00 18.58           C  
ANISOU 2884  C   GLN A 183     1876   3007   2178    565   -593   -816       C  
ATOM   2885  O   GLN A 183      16.183  22.422   4.891  1.00 18.56           O  
ANISOU 2885  O   GLN A 183     1839   2936   2279    709   -579   -847       O  
ATOM   2886  CB  GLN A 183      15.486  25.452   4.067  1.00 15.23           C  
ANISOU 2886  CB  GLN A 183     1588   2555   1644    279   -479   -880       C  
ATOM   2887  CG  GLN A 183      14.302  25.699   4.972  1.00 14.08           C  
ANISOU 2887  CG  GLN A 183     1608   2233   1507    250   -503   -799       C  
ATOM   2888  CD  GLN A 183      13.079  26.210   4.220  1.00 16.93           C  
ANISOU 2888  CD  GLN A 183     2118   2442   1871    181   -447   -812       C  
ATOM   2889  OE1 GLN A 183      13.172  26.794   3.130  1.00 13.86           O  
ANISOU 2889  OE1 GLN A 183     1725   2092   1451    104   -374   -830       O  
ATOM   2890  NE2 GLN A 183      11.917  25.955   4.787  1.00 16.14           N  
ANISOU 2890  NE2 GLN A 183     2146   2157   1829    209   -451   -744       N  
ATOM   2891  H   GLN A 183      17.437  23.713   3.227  1.00 21.18           H  
ATOM   2892  HA  GLN A 183      17.110  25.389   5.329  1.00 20.01           H  
ATOM   2893  HB2 GLN A 183      15.769  26.313   3.722  1.00 18.28           H  
ATOM   2894  HB3 GLN A 183      15.178  24.897   3.334  1.00 18.28           H  
ATOM   2895  HG2 GLN A 183      14.059  24.867   5.408  1.00 16.89           H  
ATOM   2896  HG3 GLN A 183      14.545  26.363   5.636  1.00 16.89           H  
ATOM   2897 HE21 GLN A 183      11.888  25.526   5.532  1.00 19.37           H  
ATOM   2898 HE22 GLN A 183      11.189  26.217   4.413  1.00 19.37           H  
ATOM   2899  N   GLN A 184      16.062  23.695   6.759  1.00 16.95           N  
ANISOU 2899  N   GLN A 184     1726   2775   1937    557   -649   -728       N  
ATOM   2900  CA  GLN A 184      15.635  22.618   7.640  1.00 20.26           C  
ANISOU 2900  CA  GLN A 184     2192   3073   2433    719   -694   -640       C  
ATOM   2901  C   GLN A 184      14.533  23.168   8.534  1.00 19.92           C  
ANISOU 2901  C   GLN A 184     2318   2894   2357    635   -701   -562       C  
ATOM   2902  O   GLN A 184      14.667  24.289   9.049  1.00 19.79           O  
ANISOU 2902  O   GLN A 184     2317   2968   2236    486   -717   -557       O  
ATOM   2903  CB  GLN A 184      16.824  22.169   8.512  1.00 26.62           C  
ANISOU 2903  CB  GLN A 184     2854   4053   3207    826   -772   -603       C  
ATOM   2904  CG  GLN A 184      17.133  20.698   8.425  1.00 40.92           C  
ANISOU 2904  CG  GLN A 184     4594   5816   5137   1050   -788   -582       C  
ATOM   2905  H   GLN A 184      16.158  24.449   7.163  1.00 20.34           H  
ATOM   2906  HA  GLN A 184      15.299  21.866   7.128  1.00 24.31           H  
ATOM   2907  HB2 GLN A 184      17.616  22.654   8.232  1.00 31.94           H  
ATOM   2908  HB3 GLN A 184      16.625  22.375   9.439  1.00 31.94           H  
ATOM   2909  N   ASN A 185      13.464  22.402   8.743  1.00 16.43           N  
ANISOU 2909  N   ASN A 185     1996   2239   2008    724   -684   -510       N  
ATOM   2910  CA  ASN A 185      12.403  22.816   9.652  1.00 14.41           C  
ANISOU 2910  CA  ASN A 185     1896   1852   1728    656   -689   -439       C  
ATOM   2911  C   ASN A 185      12.170  21.693  10.646  1.00 15.09           C  
ANISOU 2911  C   ASN A 185     2017   1839   1877    817   -717   -333       C  
ATOM   2912  O   ASN A 185      12.118  20.522  10.256  1.00 17.31           O  
ANISOU 2912  O   ASN A 185     2276   2021   2281    971   -692   -332       O  
ATOM   2913  CB  ASN A 185      11.089  23.116   8.939  1.00 14.59           C  
ANISOU 2913  CB  ASN A 185     2057   1685   1800    581   -625   -484       C  
ATOM   2914  CG  ASN A 185      11.172  24.316   7.984  1.00 16.08           C  
ANISOU 2914  CG  ASN A 185     2241   1951   1917    420   -590   -566       C  
ATOM   2915  OD1 ASN A 185      11.934  24.309   7.035  1.00 21.86           O  
ANISOU 2915  OD1 ASN A 185     2866   2797   2642    427   -570   -633       O  
ATOM   2916  ND2 ASN A 185      10.337  25.309   8.211  1.00 12.77           N  
ANISOU 2916  ND2 ASN A 185     1943   1458   1452    282   -576   -558       N  
ATOM   2917  H   ASN A 185      13.331  21.638   8.370  1.00 19.71           H  
ATOM   2918  HA  ASN A 185      12.681  23.608  10.138  1.00 17.29           H  
ATOM   2919  HB2 ASN A 185      10.830  22.340   8.419  1.00 17.51           H  
ATOM   2920  HB3 ASN A 185      10.409  23.311   9.603  1.00 17.51           H  
ATOM   2921 HD21 ASN A 185       9.783  25.264   8.867  1.00 15.33           H  
ATOM   2922 HD22 ASN A 185      10.346  26.003   7.703  1.00 15.33           H  
ATOM   2923  N  ATHR A 186      12.056  22.031  11.928  0.48 15.15           N  
ANISOU 2923  N  ATHR A 186     2075   1877   1803    786   -764   -244       N  
ATOM   2924  N  BTHR A 186      11.996  22.067  11.908  0.52 14.91           N  
ANISOU 2924  N  BTHR A 186     2052   1839   1773    779   -761   -246       N  
ATOM   2925  CA ATHR A 186      11.800  21.038  12.982  0.48 18.76           C  
ANISOU 2925  CA ATHR A 186     2583   2245   2299    935   -786   -120       C  
ATOM   2926  CA BTHR A 186      11.801  21.119  13.000  0.52 18.44           C  
ANISOU 2926  CA BTHR A 186     2544   2212   2251    924   -787   -122       C  
ATOM   2927  C  ATHR A 186      10.709  21.525  13.925  0.48 16.50           C  
ANISOU 2927  C  ATHR A 186     2453   1846   1969    842   -779    -58       C  
ATOM   2928  C  BTHR A 186      10.604  21.578  13.827  0.52 15.85           C  
ANISOU 2928  C  BTHR A 186     2382   1749   1893    829   -771    -68       C  
ATOM   2929  O  ATHR A 186      10.709  22.684  14.318  0.48 17.50           O  
ANISOU 2929  O  ATHR A 186     2593   2073   1982    685   -804    -82       O  
ATOM   2930  O  BTHR A 186      10.411  22.772  14.018  0.52 14.48           O  
ANISOU 2930  O  BTHR A 186     2240   1639   1625    659   -782   -106       O  
ATOM   2931  CB ATHR A 186      13.059  20.716  13.829  0.48 23.81           C  
ANISOU 2931  CB ATHR A 186     3091   3095   2859   1045   -868    -49       C  
ATOM   2932  CB BTHR A 186      13.044  21.056  13.912  0.52 22.90           C  
ANISOU 2932  CB BTHR A 186     2982   3009   2712    998   -875    -59       C  
ATOM   2933  OG1ATHR A 186      13.786  21.917  14.113  0.48 17.70           O  
ANISOU 2933  OG1ATHR A 186     2236   2550   1939    903   -919   -100       O  
ATOM   2934  OG1BTHR A 186      14.229  20.922  13.114  0.52 25.55           O  
ANISOU 2934  OG1BTHR A 186     3147   3506   3054   1044   -892   -138       O  
ATOM   2935  CG2ATHR A 186      13.963  19.738  13.102  0.48 18.76           C  
ANISOU 2935  CG2ATHR A 186     2319   2499   2311   1168   -841    -78       C  
ATOM   2936  CG2BTHR A 186      12.942  19.876  14.877  0.52 26.39           C  
ANISOU 2936  CG2BTHR A 186     3455   3369   3204   1118   -841     80       C  
ATOM   2937  H  ATHR A 186      12.122  22.837  12.221  0.48 18.18           H  
ATOM   2938  H  BTHR A 186      11.987  22.888  12.164  0.52 17.89           H  
ATOM   2939  HA ATHR A 186      11.496  20.213  12.571  0.48 22.51           H  
ATOM   2940  HA BTHR A 186      11.622  20.234  12.646  0.52 22.13           H  
ATOM   2941  HB ATHR A 186      12.784  20.307  14.664  0.48 28.57           H  
ATOM   2942  HB BTHR A 186      13.100  21.872  14.434  0.52 27.48           H  
ATOM   2943  HG1ATHR A 186      13.301  22.451  14.542  0.48 21.24           H  
ATOM   2944  HG1BTHR A 186      14.303  21.580  12.597  0.52 30.66           H  
ATOM   2945 HG21ATHR A 186      14.745  19.546  13.642  0.48 22.52           H  
ATOM   2946 HG21BTHR A 186      13.727  19.845  15.446  0.52 31.67           H  
ATOM   2947 HG22ATHR A 186      13.486  18.911  12.931  0.48 22.52           H  
ATOM   2948 HG22BTHR A 186      12.153  19.971  15.433  0.52 31.67           H  
ATOM   2949 HG23ATHR A 186      14.249  20.117  12.256  0.48 22.52           H  
ATOM   2950 HG23BTHR A 186      12.880  19.046  14.379  0.52 31.67           H  
ATOM   2951  N   PRO A 187       9.777  20.639  14.303  1.00 15.07           N  
ANISOU 2951  N   PRO A 187     2354   1492   1880    855   -679      4       N  
ATOM   2952  CA  PRO A 187       8.683  21.099  15.159  1.00 14.77           C  
ANISOU 2952  CA  PRO A 187     2438   1370   1806    741   -645     39       C  
ATOM   2953  C   PRO A 187       9.185  21.584  16.544  1.00 15.07           C  
ANISOU 2953  C   PRO A 187     2478   1546   1703    750   -737    130       C  
ATOM   2954  O   PRO A 187      10.157  21.025  17.066  1.00 18.28           O  
ANISOU 2954  O   PRO A 187     2785   2086   2074    863   -778    204       O  
ATOM   2955  CB  PRO A 187       7.776  19.859  15.282  1.00 19.75           C  
ANISOU 2955  CB  PRO A 187     3061   1879   2563    736   -500     88       C  
ATOM   2956  CG  PRO A 187       8.546  18.732  14.815  1.00 24.73           C  
ANISOU 2956  CG  PRO A 187     3593   2518   3285    861   -478    116       C  
ATOM   2957  CD  PRO A 187       9.683  19.210  13.986  1.00 23.23           C  
ANISOU 2957  CD  PRO A 187     3334   2442   3048    924   -572     39       C  
ATOM   2958  HA  PRO A 187       8.193  21.814  14.725  1.00 17.73           H  
ATOM   2959  HB2 PRO A 187       7.524  19.735  16.210  1.00 23.70           H  
ATOM   2960  HB3 PRO A 187       6.987  19.981  14.731  1.00 23.70           H  
ATOM   2961  HG2 PRO A 187       8.881  18.242  15.582  1.00 29.67           H  
ATOM   2962  HG3 PRO A 187       7.971  18.158  14.284  1.00 29.67           H  
ATOM   2963  HD2 PRO A 187      10.501  18.754  14.242  1.00 27.87           H  
ATOM   2964  HD3 PRO A 187       9.489  19.086  13.044  1.00 27.87           H  
ATOM   2965  N   ILE A 188       8.538  22.615  17.071  1.00 23.61           N  
ANISOU 2965  N   ILE A 188     4691   2760   1521  -1699   -396    335       N  
ATOM   2966  CA  ILE A 188       8.810  23.107  18.431  1.00 24.90           C  
ANISOU 2966  CA  ILE A 188     4933   2947   1580  -1776   -381    323       C  
ATOM   2967  C   ILE A 188       8.140  22.237  19.475  1.00 27.65           C  
ANISOU 2967  C   ILE A 188     5394   3275   1836  -1871   -363    357       C  
ATOM   2968  O   ILE A 188       8.689  21.992  20.554  1.00 30.98           O  
ANISOU 2968  O   ILE A 188     5910   3690   2171  -1914   -428    397       O  
ATOM   2969  CB  ILE A 188       8.371  24.578  18.555  1.00 24.57           C  
ANISOU 2969  CB  ILE A 188     4848   2961   1527  -1806   -243    226       C  
ATOM   2970  CG1 ILE A 188       9.369  25.433  17.785  1.00 23.49           C  
ANISOU 2970  CG1 ILE A 188     4626   2839   1458  -1724   -292    207       C  
ATOM   2971  CG2 ILE A 188       8.321  25.037  20.031  1.00 26.11           C  
ANISOU 2971  CG2 ILE A 188     5132   3183   1604  -1900   -200    202       C  
ATOM   2972  CD1 ILE A 188       8.922  26.825  17.458  1.00 22.87           C  
ANISOU 2972  CD1 ILE A 188     4491   2793   1404  -1725   -166    114       C  
ATOM   2973  H   ILE A 188       7.926  23.058  16.660  1.00 28.34           H  
ATOM   2974  HA  ILE A 188       9.766  23.071  18.589  1.00 29.88           H  
ATOM   2975  HB  ILE A 188       7.491  24.682  18.160  1.00 29.49           H  
ATOM   2976 HG12 ILE A 188      10.180  25.505  18.312  1.00 28.18           H  
ATOM   2977 HG13 ILE A 188       9.568  24.989  16.946  1.00 28.18           H  
ATOM   2978 HG21 ILE A 188       8.041  25.965  20.063  1.00 31.33           H  
ATOM   2979 HG22 ILE A 188       7.686  24.483  20.512  1.00 31.33           H  
ATOM   2980 HG23 ILE A 188       9.204  24.943  20.421  1.00 31.33           H  
ATOM   2981 HD11 ILE A 188       9.629  27.277  16.971  1.00 27.44           H  
ATOM   2982 HD12 ILE A 188       8.121  26.780  16.914  1.00 27.44           H  
ATOM   2983 HD13 ILE A 188       8.735  27.298  18.285  1.00 27.44           H  
ATOM   2984  N   GLY A 189       6.947  21.756  19.160  1.00 26.63           N  
ANISOU 2984  N   GLY A 189     5254   3143   1722  -1904   -274    343       N  
ATOM   2985  CA  GLY A 189       6.208  20.903  20.072  1.00 33.97           C  
ANISOU 2985  CA  GLY A 189     6281   4060   2565  -2002   -243    375       C  
ATOM   2986  C   GLY A 189       6.592  19.447  19.917  1.00 33.00           C  
ANISOU 2986  C   GLY A 189     6226   3858   2457  -1979   -381    474       C  
ATOM   2987  O   GLY A 189       7.313  19.087  18.992  1.00 32.93           O  
ANISOU 2987  O   GLY A 189     6171   3806   2537  -1877   -491    507       O  
ATOM   2988  H   GLY A 189       6.542  21.910  18.417  1.00 31.96           H  
ATOM   2989  HA2 GLY A 189       6.385  21.174  20.986  1.00 40.76           H  
ATOM   2990  HA3 GLY A 189       5.257  20.992  19.902  1.00 40.76           H  
ATOM   2991  N  AASP A 190       6.114  18.605  20.824  0.58 40.93           N  
ANISOU 2991  N  AASP A 190     7341   4838   3372  -2072   -377    519       N  
ATOM   2992  N  BASP A 190       6.082  18.619  20.826  0.42 40.42           N  
ANISOU 2992  N  BASP A 190     7275   4775   3307  -2074   -372    517       N  
ATOM   2993  CA AASP A 190       6.440  17.184  20.789  0.58 42.58           C  
ANISOU 2993  CA AASP A 190     7635   4956   3586  -2058   -510    614       C  
ATOM   2994  CA BASP A 190       6.396  17.195  20.866  0.42 42.07           C  
ANISOU 2994  CA BASP A 190     7576   4895   3514  -2066   -504    613       C  
ATOM   2995  C  AASP A 190       5.380  16.397  20.015  0.58 42.32           C  
ANISOU 2995  C  AASP A 190     7566   4900   3613  -2068   -453    618       C  
ATOM   2996  C  BASP A 190       5.239  16.350  20.334  0.42 43.13           C  
ANISOU 2996  C  BASP A 190     7696   5008   3685  -2101   -437    621       C  
ATOM   2997  O  AASP A 190       5.624  15.262  19.612  0.58 43.44           O  
ANISOU 2997  O  AASP A 190     7752   4958   3797  -2031   -564    685       O  
ATOM   2998  O  BASP A 190       5.265  15.125  20.438  0.42 43.42           O  
ANISOU 2998  O  BASP A 190     7822   4965   3712  -2117   -524    697       O  
ATOM   2999  CB AASP A 190       6.572  16.627  22.215  0.58 42.84           C  
ANISOU 2999  CB AASP A 190     7828   4966   3484  -2156   -550    674       C  
ATOM   3000  CB BASP A 190       6.720  16.765  22.303  0.42 42.18           C  
ANISOU 3000  CB BASP A 190     7744   4887   3394  -2152   -557    672       C  
ATOM   3001  CG AASP A 190       7.682  17.298  23.012  0.58 41.57           C  
ANISOU 3001  CG AASP A 190     7706   4827   3263  -2139   -622    679       C  
ATOM   3002  CG BASP A 190       5.473  16.464  23.126  0.42 45.59           C  
ANISOU 3002  CG BASP A 190     8247   5349   3728  -2295   -427    666       C  
ATOM   3003  OD1AASP A 190       8.726  17.651  22.418  0.58 48.66           O  
ANISOU 3003  OD1AASP A 190     8535   5718   4235  -2027   -717    676       O  
ATOM   3004  OD1BASP A 190       4.438  17.146  22.942  0.42 36.91           O  
ANISOU 3004  OD1BASP A 190     7061   4323   2638  -2337   -263    585       O  
ATOM   3005  OD2AASP A 190       7.508  17.469  24.237  0.58 46.23           O  
ANISOU 3005  OD2AASP A 190     8391   5447   3727  -2237   -581    684       O  
ATOM   3006  OD2BASP A 190       5.536  15.540  23.969  0.42 53.18           O  
ANISOU 3006  OD2BASP A 190     9348   6258   4600  -2364   -490    744       O  
ATOM   3007  H  AASP A 190       5.597  18.831  21.473  0.58 49.11           H  
ATOM   3008  H  BASP A 190       5.539  18.867  21.446  0.42 48.50           H  
ATOM   3009  HA AASP A 190       7.291  17.065  20.339  0.58 51.09           H  
ATOM   3010  HA BASP A 190       7.175  17.024  20.314  0.42 50.48           H  
ATOM   3011  HB2AASP A 190       5.736  16.767  22.688  0.58 51.41           H  
ATOM   3012  HB2BASP A 190       7.263  15.961  22.277  0.42 50.61           H  
ATOM   3013  HB3AASP A 190       6.769  15.678  22.166  0.58 51.41           H  
ATOM   3014  HB3BASP A 190       7.205  17.479  22.744  0.42 50.61           H  
ATOM   3015  N   GLY A 191       4.218  17.012  19.795  1.00 44.03           N  
ANISOU 3015  N   GLY A 191     7699   5190   3842  -2112   -282    542       N  
ATOM   3016  CA  GLY A 191       3.080  16.326  19.203  1.00 43.26           C  
ANISOU 3016  CA  GLY A 191     7558   5085   3794  -2137   -205    539       C  
ATOM   3017  C   GLY A 191       3.362  15.877  17.771  1.00 38.74           C  
ANISOU 3017  C   GLY A 191     6901   4460   3356  -2017   -284    558       C  
ATOM   3018  O   GLY A 191       4.367  16.293  17.193  1.00 35.92           O  
ANISOU 3018  O   GLY A 191     6503   4091   3054  -1915   -376    558       O  
ATOM   3019  H  AGLY A 191       4.066  17.837  19.984  0.58 52.84           H  
ATOM   3020  H  BGLY A 191       4.163  17.870  19.761  0.42 52.84           H  
ATOM   3021  HA2 GLY A 191       2.861  15.544  19.733  1.00 51.91           H  
ATOM   3022  HA3 GLY A 191       2.312  16.918  19.195  1.00 51.91           H  
ATOM   3023  N   PRO A 192       2.496  15.010  17.209  1.00 38.02           N  
ANISOU 3023  N   PRO A 192     6786   4340   3322  -2034   -249    574       N  
ATOM   3024  CA  PRO A 192       2.686  14.452  15.853  1.00 34.12           C  
ANISOU 3024  CA  PRO A 192     6218   3787   2959  -1926   -325    593       C  
ATOM   3025  C   PRO A 192       2.602  15.511  14.764  1.00 29.08           C  
ANISOU 3025  C   PRO A 192     5421   3208   2420  -1834   -258    519       C  
ATOM   3026  O   PRO A 192       1.874  16.496  14.907  1.00 31.55           O  
ANISOU 3026  O   PRO A 192     5661   3607   2720  -1868   -110    443       O  
ATOM   3027  CB  PRO A 192       1.531  13.454  15.711  1.00 38.93           C  
ANISOU 3027  CB  PRO A 192     6831   4367   3592  -1999   -262    611       C  
ATOM   3028  CG  PRO A 192       0.504  13.895  16.713  1.00 44.73           C  
ANISOU 3028  CG  PRO A 192     7579   5185   4231  -2133   -101    566       C  
ATOM   3029  CD  PRO A 192       1.264  14.510  17.845  1.00 37.69           C  
ANISOU 3029  CD  PRO A 192     6781   4320   3221  -2165   -132    572       C  
ATOM   3030  HA  PRO A 192       3.532  13.983  15.790  1.00 40.94           H  
ATOM   3031  HB2 PRO A 192       1.172  13.497  14.811  1.00 46.71           H  
ATOM   3032  HB3 PRO A 192       1.846  12.559  15.913  1.00 46.71           H  
ATOM   3033  HG2 PRO A 192      -0.087  14.547  16.306  1.00 53.67           H  
ATOM   3034  HG3 PRO A 192       0.001  13.125  17.021  1.00 53.67           H  
ATOM   3035  HD2 PRO A 192       0.760  15.245  18.229  1.00 45.23           H  
ATOM   3036  HD3 PRO A 192       1.477  13.840  18.512  1.00 45.23           H  
ATOM   3037  N   VAL A 193       3.353  15.308  13.685  1.00 25.54           N  
ANISOU 3037  N   VAL A 193     4923   2711   2070  -1716   -369    540       N  
ATOM   3038  CA  VAL A 193       3.312  16.219  12.550  1.00 23.04           C  
ANISOU 3038  CA  VAL A 193     4463   2439   1854  -1627   -317    480       C  
ATOM   3039  C   VAL A 193       3.193  15.387  11.291  1.00 22.41           C  
ANISOU 3039  C   VAL A 193     4318   2292   1903  -1549   -378    498       C  
ATOM   3040  O   VAL A 193       3.371  14.170  11.327  1.00 23.24           O  
ANISOU 3040  O   VAL A 193     4501   2313   2015  -1551   -482    557       O  
ATOM   3041  CB  VAL A 193       4.566  17.100  12.431  1.00 25.20           C  
ANISOU 3041  CB  VAL A 193     4725   2730   2119  -1554   -395    476       C  
ATOM   3042  CG1 VAL A 193       4.759  17.945  13.693  1.00 24.45           C  
ANISOU 3042  CG1 VAL A 193     4695   2693   1904  -1630   -344    451       C  
ATOM   3043  CG2 VAL A 193       5.813  16.243  12.114  1.00 24.00           C  
ANISOU 3043  CG2 VAL A 193     4626   2495   1997  -1472   -596    546       C  
ATOM   3044  H   VAL A 193       3.895  14.648  13.587  1.00 30.65           H  
ATOM   3045  HA  VAL A 193       2.534  16.793  12.619  1.00 27.65           H  
ATOM   3046  HB  VAL A 193       4.440  17.712  11.689  1.00 30.24           H  
ATOM   3047 HG11 VAL A 193       5.556  18.489  13.589  1.00 29.35           H  
ATOM   3048 HG12 VAL A 193       3.983  18.514  13.813  1.00 29.35           H  
ATOM   3049 HG13 VAL A 193       4.859  17.355  14.456  1.00 29.35           H  
ATOM   3050 HG21 VAL A 193       6.586  16.824  12.045  1.00 28.80           H  
ATOM   3051 HG22 VAL A 193       5.945  15.601  12.830  1.00 28.80           H  
ATOM   3052 HG23 VAL A 193       5.672  15.778  11.275  1.00 28.80           H  
ATOM   3053  N   LEU A 194       2.857  16.049  10.190  1.00 20.99           N  
ANISOU 3053  N   LEU A 194     4000   2147   1828  -1483   -314    439       N  
ATOM   3054  CA  LEU A 194       2.717  15.350   8.930  1.00 20.37           C  
ANISOU 3054  CA  LEU A 194     3848   2009   1882  -1407   -370    437       C  
ATOM   3055  C   LEU A 194       4.084  15.346   8.269  1.00 19.53           C  
ANISOU 3055  C   LEU A 194     3742   1857   1820  -1292   -528    466       C  
ATOM   3056  O   LEU A 194       4.664  16.401   8.036  1.00 19.47           O  
ANISOU 3056  O   LEU A 194     3684   1898   1814  -1249   -519    440       O  
ATOM   3057  CB  LEU A 194       1.676  16.052   8.044  1.00 19.49           C  
ANISOU 3057  CB  LEU A 194     3581   1957   1868  -1391   -235    350       C  
ATOM   3058  CG  LEU A 194       0.223  15.923   8.508  1.00 20.44           C  
ANISOU 3058  CG  LEU A 194     3674   2121   1972  -1496    -86    311       C  
ATOM   3059  CD1 LEU A 194      -0.668  16.797   7.631  1.00 23.15           C  
ANISOU 3059  CD1 LEU A 194     3856   2530   2410  -1465     32    214       C  
ATOM   3060  CD2 LEU A 194      -0.270  14.482   8.472  1.00 26.39           C  
ANISOU 3060  CD2 LEU A 194     4474   2802   2752  -1545   -130    353       C  
ATOM   3061  H   LEU A 194       2.707  16.895  10.150  1.00 25.19           H  
ATOM   3062  HA  LEU A 194       2.437  14.434   9.085  1.00 24.44           H  
ATOM   3063  HB2 LEU A 194       1.888  16.998   8.013  1.00 23.39           H  
ATOM   3064  HB3 LEU A 194       1.731  15.678   7.151  1.00 23.39           H  
ATOM   3065  HG  LEU A 194       0.152  16.243   9.421  1.00 24.53           H  
ATOM   3066 HD11 LEU A 194      -1.587  16.710   7.930  1.00 27.78           H  
ATOM   3067 HD12 LEU A 194      -0.380  17.720   7.709  1.00 27.78           H  
ATOM   3068 HD13 LEU A 194      -0.590  16.502   6.710  1.00 27.78           H  
ATOM   3069 HD21 LEU A 194      -1.191  14.457   8.774  1.00 31.67           H  
ATOM   3070 HD22 LEU A 194      -0.210  14.151   7.563  1.00 31.67           H  
ATOM   3071 HD23 LEU A 194       0.286  13.944   9.058  1.00 31.67           H  
ATOM   3072  N   LEU A 195       4.613  14.162   7.989  1.00 19.99           N  
ANISOU 3072  N   LEU A 195     3860   1821   1916  -1242   -676    516       N  
ATOM   3073  CA  LEU A 195       5.886  14.057   7.279  1.00 19.35           C  
ANISOU 3073  CA  LEU A 195     3767   1695   1892  -1117   -838    534       C  
ATOM   3074  C   LEU A 195       5.608  13.790   5.804  1.00 18.46           C  
ANISOU 3074  C   LEU A 195     3517   1571   1926  -1007   -851    470       C  
ATOM   3075  O   LEU A 195       5.029  12.765   5.464  1.00 19.00           O  
ANISOU 3075  O   LEU A 195     3613   1556   2052  -1026   -879    479       O  
ATOM   3076  CB  LEU A 195       6.716  12.924   7.863  1.00 20.58           C  
ANISOU 3076  CB  LEU A 195     4050   1767   2004  -1089  -1006    600       C  
ATOM   3077  CG  LEU A 195       7.140  13.164   9.319  1.00 21.59           C  
ANISOU 3077  CG  LEU A 195     4288   1925   1991  -1170  -1010    636       C  
ATOM   3078  CD1 LEU A 195       7.839  11.927   9.843  1.00 27.32           C  
ANISOU 3078  CD1 LEU A 195     5129   2552   2698  -1141  -1172    686       C  
ATOM   3079  CD2 LEU A 195       8.039  14.399   9.439  1.00 20.78           C  
ANISOU 3079  CD2 LEU A 195     4137   1906   1853  -1131  -1012    616       C  
ATOM   3080  H   LEU A 195       4.259  13.406   8.196  1.00 23.99           H  
ATOM   3081  HA  LEU A 195       6.381  14.887   7.362  1.00 23.23           H  
ATOM   3082  HB2 LEU A 195       6.194  12.107   7.836  1.00 24.70           H  
ATOM   3083  HB3 LEU A 195       7.521  12.819   7.332  1.00 24.70           H  
ATOM   3084  HG  LEU A 195       6.348  13.314   9.859  1.00 25.91           H  
ATOM   3085 HD11 LEU A 195       8.106  12.082  10.762  1.00 32.78           H  
ATOM   3086 HD12 LEU A 195       7.228  11.176   9.797  1.00 32.78           H  
ATOM   3087 HD13 LEU A 195       8.621  11.752   9.296  1.00 32.78           H  
ATOM   3088 HD21 LEU A 195       8.287  14.519  10.369  1.00 24.94           H  
ATOM   3089 HD22 LEU A 195       8.834  14.263   8.899  1.00 24.94           H  
ATOM   3090 HD23 LEU A 195       7.552  15.176   9.122  1.00 24.94           H  
ATOM   3091  N   PRO A 196       6.018  14.707   4.932  1.00 17.21           N  
ANISOU 3091  N   PRO A 196     3209   1507   1823   -890   -827    399       N  
ATOM   3092  CA  PRO A 196       5.429  14.614   3.590  1.00 16.44           C  
ANISOU 3092  CA  PRO A 196     2973   1427   1846   -806   -795    327       C  
ATOM   3093  C   PRO A 196       6.189  13.708   2.607  1.00 16.38           C  
ANISOU 3093  C   PRO A 196     2927   1373   1922   -661   -946    311       C  
ATOM   3094  O   PRO A 196       7.369  13.471   2.797  1.00 16.64           O  
ANISOU 3094  O   PRO A 196     2996   1394   1931   -590  -1069    338       O  
ATOM   3095  CB  PRO A 196       5.516  16.043   3.098  1.00 15.29           C  
ANISOU 3095  CB  PRO A 196     2700   1399   1710   -751   -701    265       C  
ATOM   3096  CG  PRO A 196       6.772  16.579   3.748  1.00 16.59           C  
ANISOU 3096  CG  PRO A 196     2909   1597   1797   -735   -763    298       C  
ATOM   3097  CD  PRO A 196       6.809  15.938   5.114  1.00 16.54           C  
ANISOU 3097  CD  PRO A 196     3075   1519   1692   -853   -804    378       C  
ATOM   3098  HA  PRO A 196       4.499  14.341   3.640  1.00 19.73           H  
ATOM   3099  HB2 PRO A 196       5.595  16.055   2.131  1.00 18.34           H  
ATOM   3100  HB3 PRO A 196       4.736  16.541   3.389  1.00 18.34           H  
ATOM   3101  HG2 PRO A 196       7.547  16.320   3.226  1.00 19.91           H  
ATOM   3102  HG3 PRO A 196       6.715  17.545   3.823  1.00 19.91           H  
ATOM   3103  HD2 PRO A 196       7.721  15.721   5.361  1.00 19.85           H  
ATOM   3104  HD3 PRO A 196       6.390  16.516   5.770  1.00 19.85           H  
ATOM   3105  N   ASP A 197       5.511  13.219   1.572  1.00 16.14           N  
ANISOU 3105  N   ASP A 197     2819   1325   1990   -615   -937    258       N  
ATOM   3106  CA  ASP A 197       6.186  12.735   0.370  1.00 15.80           C  
ANISOU 3106  CA  ASP A 197     2689   1283   2029   -453  -1045    207       C  
ATOM   3107  C   ASP A 197       6.865  13.925  -0.307  1.00 14.67           C  
ANISOU 3107  C   ASP A 197     2414   1273   1888   -352  -1009    159       C  
ATOM   3108  O   ASP A 197       6.520  15.098  -0.050  1.00 14.09           O  
ANISOU 3108  O   ASP A 197     2304   1274   1775   -406   -888    153       O  
ATOM   3109  CB  ASP A 197       5.180  12.066  -0.599  1.00 15.82           C  
ANISOU 3109  CB  ASP A 197     2634   1250   2129   -438  -1029    150       C  
ATOM   3110  CG  ASP A 197       4.619  10.755  -0.057  1.00 20.43           C  
ANISOU 3110  CG  ASP A 197     3353   1687   2722   -537  -1084    196       C  
ATOM   3111  OD1 ASP A 197       5.125  10.243   0.960  1.00 22.36           O  
ANISOU 3111  OD1 ASP A 197     3745   1847   2903   -593  -1158    277       O  
ATOM   3112  OD2 ASP A 197       3.672  10.226  -0.658  1.00 25.23           O  
ANISOU 3112  OD2 ASP A 197     3924   2261   3401   -563  -1058    152       O  
ATOM   3113  H   ASP A 197       4.653  13.156   1.540  1.00 19.37           H  
ATOM   3114  HA  ASP A 197       6.864  12.086   0.614  1.00 18.96           H  
ATOM   3115  HB2 ASP A 197       4.436  12.671  -0.749  1.00 18.99           H  
ATOM   3116  HB3 ASP A 197       5.628  11.877  -1.438  1.00 18.99           H  
ATOM   3117  N   ASN A 198       7.831  13.641  -1.181  1.00 14.49           N  
ANISOU 3117  N   ASN A 198     2319   1278   1908   -208  -1109    121       N  
ATOM   3118  CA  ASN A 198       8.519  14.689  -1.924  1.00 13.60           C  
ANISOU 3118  CA  ASN A 198     2080   1293   1795   -121  -1076     78       C  
ATOM   3119  C   ASN A 198       7.534  15.473  -2.789  1.00 12.77           C  
ANISOU 3119  C   ASN A 198     1875   1251   1725   -119   -950     28       C  
ATOM   3120  O   ASN A 198       6.680  14.903  -3.454  1.00 12.81           O  
ANISOU 3120  O   ASN A 198     1851   1225   1791   -102   -943     -9       O  
ATOM   3121  CB  ASN A 198       9.644  14.112  -2.799  1.00 13.76           C  
ANISOU 3121  CB  ASN A 198     2026   1343   1860     30  -1160     31       C  
ATOM   3122  CG  ASN A 198      10.817  13.586  -2.001  1.00 23.00           C  
ANISOU 3122  CG  ASN A 198     3258   2481   3001     49  -1225     60       C  
ATOM   3123  OD1 ASN A 198      10.786  13.477  -0.756  1.00 15.18           O  
ANISOU 3123  OD1 ASN A 198     2392   1425   1952    -44  -1275    131       O  
ATOM   3124  ND2 ASN A 198      11.887  13.262  -2.721  1.00 18.20           N  
ANISOU 3124  ND2 ASN A 198     2562   1929   2422    162  -1219      3       N  
ATOM   3125  H   ASN A 198       8.106  12.846  -1.360  1.00 17.39           H  
ATOM   3126  HA  ASN A 198       8.920  15.308  -1.294  1.00 16.32           H  
ATOM   3127  HB2 ASN A 198       9.289  13.379  -3.325  1.00 16.51           H  
ATOM   3128  HB3 ASN A 198       9.974  14.810  -3.387  1.00 16.51           H  
ATOM   3129 HD21 ASN A 198      11.876  13.360  -3.575  1.00 21.84           H  
ATOM   3130 HD22 ASN A 198      12.590  12.956  -2.332  1.00 21.84           H  
ATOM   3131  N   HIS A 199       7.631  16.800  -2.720  1.00 12.14           N  
ANISOU 3131  N   HIS A 199     1752   1255   1605   -141   -857     28       N  
ATOM   3132  CA  HIS A 199       6.763  17.686  -3.484  1.00 11.86           C  
ANISOU 3132  CA  HIS A 199     1634   1278   1596   -129   -746    -13       C  
ATOM   3133  C   HIS A 199       7.451  19.045  -3.519  1.00 11.44           C  
ANISOU 3133  C   HIS A 199     1543   1307   1496   -121   -692     -7       C  
ATOM   3134  O   HIS A 199       8.612  19.177  -3.077  1.00 11.45           O  
ANISOU 3134  O   HIS A 199     1565   1332   1455   -121   -747     18       O  
ATOM   3135  CB  HIS A 199       5.344  17.725  -2.860  1.00 11.68           C  
ANISOU 3135  CB  HIS A 199     1655   1209   1576   -238   -651     -9       C  
ATOM   3136  CG  HIS A 199       5.288  18.384  -1.514  1.00 11.92           C  
ANISOU 3136  CG  HIS A 199     1771   1228   1530   -355   -584     34       C  
ATOM   3137  ND1 HIS A 199       5.701  17.749  -0.359  1.00 12.64           N  
ANISOU 3137  ND1 HIS A 199     1980   1258   1565   -435   -639     92       N  
ATOM   3138  CD2 HIS A 199       4.909  19.631  -1.145  1.00 11.84           C  
ANISOU 3138  CD2 HIS A 199     1754   1261   1484   -401   -474     25       C  
ATOM   3139  CE1 HIS A 199       5.569  18.575   0.666  1.00 16.61           C  
ANISOU 3139  CE1 HIS A 199     2541   1776   1995   -530   -559    114       C  
ATOM   3140  NE2 HIS A 199       5.078  19.719   0.221  1.00 14.19           N  
ANISOU 3140  NE2 HIS A 199     2158   1529   1703   -510   -456     69       N  
ATOM   3141  H   HIS A 199       8.203  17.215  -2.229  1.00 14.57           H  
ATOM   3142  HA  HIS A 199       6.688  17.358  -4.394  1.00 14.24           H  
ATOM   3143  HB2 HIS A 199       4.756  18.216  -3.455  1.00 14.02           H  
ATOM   3144  HB3 HIS A 199       5.023  16.815  -2.759  1.00 14.02           H  
ATOM   3145  HD1 HIS A 199       6.001  16.944  -0.314  1.00 15.17           H  
ATOM   3146  HD2 HIS A 199       4.581  20.297  -1.705  1.00 14.21           H  
ATOM   3147  HE1 HIS A 199       5.768  18.377   1.553  1.00 19.93           H  
ATOM   3148  HE2 HIS A 199       4.905  20.410   0.702  1.00 17.02           H  
ATOM   3149  N   TYR A 200       6.777  20.054  -4.038  1.00 10.62           N  
ANISOU 3149  N   TYR A 200     1388   1246   1402   -114   -594    -31       N  
ATOM   3150  CA  TYR A 200       7.337  21.388  -4.051  1.00 10.29           C  
ANISOU 3150  CA  TYR A 200     1330   1263   1318   -121   -539    -22       C  
ATOM   3151  C   TYR A 200       6.247  22.453  -3.960  1.00 14.27           C  
ANISOU 3151  C   TYR A 200     1837   1764   1822   -158   -421    -36       C  
ATOM   3152  O   TYR A 200       5.061  22.150  -4.073  1.00 12.70           O  
ANISOU 3152  O   TYR A 200     1624   1539   1662   -162   -383    -63       O  
ATOM   3153  CB  TYR A 200       8.195  21.594  -5.279  1.00 12.11           C  
ANISOU 3153  CB  TYR A 200     1471   1571   1559    -21   -576    -42       C  
ATOM   3154  CG  TYR A 200       7.430  21.444  -6.525  1.00 12.32           C  
ANISOU 3154  CG  TYR A 200     1426   1620   1635     62   -561    -82       C  
ATOM   3155  CD1 TYR A 200       7.400  20.249  -7.189  1.00 13.01           C  
ANISOU 3155  CD1 TYR A 200     1476   1701   1767    134   -639   -116       C  
ATOM   3156  CD2 TYR A 200       6.719  22.511  -7.037  1.00 19.75           C  
ANISOU 3156  CD2 TYR A 200     2344   2583   2577     74   -476    -91       C  
ATOM   3157  CE1 TYR A 200       6.671  20.113  -8.376  1.00 16.96           C  
ANISOU 3157  CE1 TYR A 200     1909   2228   2306    211   -631   -161       C  
ATOM   3158  CE2 TYR A 200       5.998  22.391  -8.180  1.00 28.79           C  
ANISOU 3158  CE2 TYR A 200     3427   3754   3761    155   -473   -129       C  
ATOM   3159  CZ  TYR A 200       5.973  21.189  -8.851  1.00 26.28           C  
ANISOU 3159  CZ  TYR A 200     3065   3440   3481    220   -549   -165       C  
ATOM   3160  OH  TYR A 200       5.242  21.102 -10.007  1.00 32.34           O  
ANISOU 3160  OH  TYR A 200     3769   4240   4280    300   -549   -208       O  
ATOM   3161  H   TYR A 200       5.994  19.993  -4.388  1.00 12.75           H  
ATOM   3162  HA  TYR A 200       7.910  21.489  -3.275  1.00 12.35           H  
ATOM   3163  HB2 TYR A 200       8.567  22.489  -5.260  1.00 14.53           H  
ATOM   3164  HB3 TYR A 200       8.908  20.936  -5.283  1.00 14.53           H  
ATOM   3165  HD1 TYR A 200       7.877  19.524  -6.855  1.00 15.62           H  
ATOM   3166  HD2 TYR A 200       6.730  23.325  -6.587  1.00 23.70           H  
ATOM   3167  HE1 TYR A 200       6.651  19.300  -8.828  1.00 20.35           H  
ATOM   3168  HE2 TYR A 200       5.527  23.121  -8.512  1.00 34.55           H  
ATOM   3169  HH  TYR A 200       4.872  21.838 -10.169  1.00 38.81           H  
ATOM   3170  N   LEU A 201       6.672  23.685  -3.709  1.00 10.70           N  
ANISOU 3170  N   LEU A 201     1402   1335   1328   -186   -369    -24       N  
ATOM   3171  CA  LEU A 201       5.782  24.847  -3.730  1.00 12.05           C  
ANISOU 3171  CA  LEU A 201     1576   1499   1502   -198   -267    -43       C  
ATOM   3172  C   LEU A 201       6.194  25.728  -4.902  1.00 11.30           C  
ANISOU 3172  C   LEU A 201     1429   1451   1413   -122   -258    -45       C  
ATOM   3173  O   LEU A 201       7.385  25.931  -5.108  1.00 11.86           O  
ANISOU 3173  O   LEU A 201     1492   1561   1454   -121   -296    -21       O  
ATOM   3174  CB  LEU A 201       5.949  25.666  -2.455  1.00 12.16           C  
ANISOU 3174  CB  LEU A 201     1675   1488   1458   -298   -213    -29       C  
ATOM   3175  CG  LEU A 201       5.925  24.901  -1.130  1.00 11.03           C  
ANISOU 3175  CG  LEU A 201     1609   1309   1274   -394   -230    -11       C  
ATOM   3176  CD1 LEU A 201       6.193  25.826   0.052  1.00 13.90           C  
ANISOU 3176  CD1 LEU A 201     2056   1661   1566   -487   -179     -4       C  
ATOM   3177  CD2 LEU A 201       4.593  24.123  -0.971  1.00 13.80           C  
ANISOU 3177  CD2 LEU A 201     1955   1630   1660   -413   -195    -34       C  
ATOM   3178  H   LEU A 201       7.488  23.881  -3.521  1.00 12.84           H  
ATOM   3179  HA  LEU A 201       4.857  24.574  -3.830  1.00 14.46           H  
ATOM   3180  HB2 LEU A 201       6.801  26.128  -2.503  1.00 14.59           H  
ATOM   3181  HB3 LEU A 201       5.233  26.319  -2.421  1.00 14.59           H  
ATOM   3182  HG  LEU A 201       6.639  24.245  -1.146  1.00 13.24           H  
ATOM   3183 HD11 LEU A 201       6.170  25.307   0.871  1.00 16.68           H  
ATOM   3184 HD12 LEU A 201       7.067  26.233  -0.058  1.00 16.68           H  
ATOM   3185 HD13 LEU A 201       5.509  26.513   0.076  1.00 16.68           H  
ATOM   3186 HD21 LEU A 201       4.603  23.649  -0.125  1.00 16.56           H  
ATOM   3187 HD22 LEU A 201       3.856  24.754  -0.988  1.00 16.56           H  
ATOM   3188 HD23 LEU A 201       4.507  23.493  -1.703  1.00 16.56           H  
ATOM   3189  N   HIS A 202       5.211  26.230  -5.648  1.00 10.24           N  
ANISOU 3189  N   HIS A 202     1260   1317   1315    -62   -211    -72       N  
ATOM   3190  CA  HIS A 202       5.416  27.305  -6.616  1.00 14.79           C  
ANISOU 3190  CA  HIS A 202     1818   1918   1883     -5   -188    -63       C  
ATOM   3191  C   HIS A 202       5.248  28.629  -5.884  1.00 12.69           C  
ANISOU 3191  C   HIS A 202     1626   1606   1592    -62   -114    -57       C  
ATOM   3192  O   HIS A 202       4.247  28.826  -5.183  1.00 17.13           O  
ANISOU 3192  O   HIS A 202     2212   2127   2170    -85    -61    -90       O  
ATOM   3193  CB  HIS A 202       4.320  27.311  -7.653  1.00 18.33           C  
ANISOU 3193  CB  HIS A 202     2212   2377   2377     91   -179    -95       C  
ATOM   3194  CG  HIS A 202       4.336  26.151  -8.588  1.00 21.16           C  
ANISOU 3194  CG  HIS A 202     2497   2780   2763    161   -249   -114       C  
ATOM   3195  ND1 HIS A 202       5.370  25.923  -9.467  1.00 26.58           N  
ANISOU 3195  ND1 HIS A 202     3148   3527   3424    206   -300    -97       N  
ATOM   3196  CD2 HIS A 202       3.404  25.198  -8.837  1.00 25.61           C  
ANISOU 3196  CD2 HIS A 202     3013   3340   3378    195   -273   -158       C  
ATOM   3197  CE1 HIS A 202       5.091  24.855 -10.196  1.00 26.73           C  
ANISOU 3197  CE1 HIS A 202     3107   3573   3477    272   -356   -133       C  
ATOM   3198  NE2 HIS A 202       3.904  24.399  -9.835  1.00 23.09           N  
ANISOU 3198  NE2 HIS A 202     2640   3070   3065    264   -344   -168       N  
ATOM   3199  H   HIS A 202       4.396  25.957  -5.610  1.00 12.29           H  
ATOM   3200  HA  HIS A 202       6.289  27.252  -7.037  1.00 17.75           H  
ATOM   3201  HB2 HIS A 202       3.463  27.308  -7.197  1.00 22.00           H  
ATOM   3202  HB3 HIS A 202       4.402  28.117  -8.185  1.00 22.00           H  
ATOM   3203  HD1 HIS A 202       6.088  26.392  -9.524  1.00 31.90           H  
ATOM   3204  HD2 HIS A 202       2.587  25.098  -8.405  1.00 30.74           H  
ATOM   3205  HE1 HIS A 202       5.638  24.487 -10.852  1.00 32.08           H  
ATOM   3206  HE2 HIS A 202       3.511  23.708 -10.166  1.00 27.71           H  
ATOM   3207  N   THR A 203       6.168  29.557  -6.107  1.00 13.16           N  
ANISOU 3207  N   THR A 203     1715   1674   1613    -82   -107    -24       N  
ATOM   3208  CA  THR A 203       6.048  30.887  -5.531  1.00 11.03           C  
ANISOU 3208  CA  THR A 203     1522   1346   1322   -131    -44    -23       C  
ATOM   3209  C   THR A 203       6.041  31.923  -6.619  1.00 13.10           C  
ANISOU 3209  C   THR A 203     1795   1598   1584    -73    -27     -1       C  
ATOM   3210  O   THR A 203       6.624  31.720  -7.695  1.00 15.69           O  
ANISOU 3210  O   THR A 203     2077   1983   1901    -30    -64     28       O  
ATOM   3211  CB  THR A 203       7.247  31.168  -4.632  1.00 13.66           C  
ANISOU 3211  CB  THR A 203     1906   1681   1603   -238    -53      1       C  
ATOM   3212  OG1 THR A 203       8.434  31.130  -5.444  1.00 16.94           O  
ANISOU 3212  OG1 THR A 203     2280   2161   1997   -234    -97     36       O  
ATOM   3213  CG2 THR A 203       7.328  30.128  -3.555  1.00 14.48           C  
ANISOU 3213  CG2 THR A 203     2017   1792   1694   -294    -83    -10       C  
ATOM   3214  H   THR A 203       6.871  29.442  -6.589  1.00 15.80           H  
ATOM   3215  HA  THR A 203       5.232  30.959  -5.013  1.00 13.23           H  
ATOM   3216  HB  THR A 203       7.154  32.041  -4.220  1.00 16.39           H  
ATOM   3217  HG1 THR A 203       9.111  31.282  -4.971  1.00 20.33           H  
ATOM   3218 HG21 THR A 203       8.090  30.304  -2.981  1.00 17.38           H  
ATOM   3219 HG22 THR A 203       6.520  30.142  -3.019  1.00 17.38           H  
ATOM   3220 HG23 THR A 203       7.428  29.248  -3.951  1.00 17.38           H  
ATOM   3221  N   HIS A 204       5.330  33.017  -6.385  1.00 11.53           N  
ANISOU 3221  N   HIS A 204     1658   1326   1396    -63     26    -18       N  
ATOM   3222  CA  HIS A 204       5.588  34.222  -7.155  1.00 14.57           C  
ANISOU 3222  CA  HIS A 204     2096   1675   1765    -40     39     19       C  
ATOM   3223  C   HIS A 204       5.194  35.438  -6.322  1.00 15.72           C  
ANISOU 3223  C   HIS A 204     2342   1719   1913    -76     94     -5       C  
ATOM   3224  O   HIS A 204       4.232  35.403  -5.559  1.00 14.69           O  
ANISOU 3224  O   HIS A 204     2216   1556   1811    -61    129    -64       O  
ATOM   3225  CB  HIS A 204       4.960  34.194  -8.559  1.00 22.28           C  
ANISOU 3225  CB  HIS A 204     3031   2673   2763     83     15     30       C  
ATOM   3226  CG  HIS A 204       3.470  34.210  -8.586  1.00 19.79           C  
ANISOU 3226  CG  HIS A 204     2693   2323   2503    179     29    -25       C  
ATOM   3227  ND1 HIS A 204       2.750  35.356  -8.839  1.00 17.58           N  
ANISOU 3227  ND1 HIS A 204     2473   1965   2239    245     50    -33       N  
ATOM   3228  CD2 HIS A 204       2.560  33.211  -8.464  1.00 26.60           C  
ANISOU 3228  CD2 HIS A 204     3473   3223   3410    223     19    -80       C  
ATOM   3229  CE1 HIS A 204       1.458  35.073  -8.826  1.00 23.88           C  
ANISOU 3229  CE1 HIS A 204     3215   2766   3093    331     54    -98       C  
ATOM   3230  NE2 HIS A 204       1.315  33.775  -8.614  1.00 22.65           N  
ANISOU 3230  NE2 HIS A 204     2970   2683   2954    311     39   -126       N  
ATOM   3231  H   HIS A 204       4.705  33.088  -5.798  1.00 13.84           H  
ATOM   3232  HA  HIS A 204       6.547  34.281  -7.288  1.00 17.49           H  
ATOM   3233  HB2 HIS A 204       5.270  34.971  -9.051  1.00 26.74           H  
ATOM   3234  HB3 HIS A 204       5.252  33.386  -9.011  1.00 26.74           H  
ATOM   3235  HD1 HIS A 204       3.087  36.138  -8.959  1.00 21.09           H  
ATOM   3236  HD2 HIS A 204       2.743  32.315  -8.299  1.00 31.92           H  
ATOM   3237  HE1 HIS A 204       0.767  35.681  -8.963  1.00 28.66           H  
ATOM   3238  HE2 HIS A 204       0.566  33.355  -8.563  1.00 27.18           H  
ATOM   3239  N   SER A 205       6.000  36.487  -6.455  1.00 18.19           N  
ANISOU 3239  N   SER A 205     2733   1987   2191   -133    104     37       N  
ATOM   3240  CA  SER A 205       5.965  37.627  -5.556  1.00 19.71           C  
ANISOU 3240  CA  SER A 205     3033   2079   2376   -195    148     14       C  
ATOM   3241  C   SER A 205       6.020  38.916  -6.346  1.00 19.11           C  
ANISOU 3241  C   SER A 205     3048   1917   2297   -169    155     56       C  
ATOM   3242  O   SER A 205       6.644  38.978  -7.407  1.00 18.96           O  
ANISOU 3242  O   SER A 205     3019   1932   2252   -166    130    123       O  
ATOM   3243  CB  SER A 205       7.157  37.572  -4.606  1.00 16.78           C  
ANISOU 3243  CB  SER A 205     2686   1731   1957   -338    146     22       C  
ATOM   3244  OG  SER A 205       7.159  36.388  -3.860  1.00 19.59           O  
ANISOU 3244  OG  SER A 205     2978   2158   2309   -362    129     -6       O  
ATOM   3245  H   SER A 205       6.590  36.560  -7.077  1.00 21.83           H  
ATOM   3246  HA  SER A 205       5.147  37.613  -5.035  1.00 23.65           H  
ATOM   3247  HB2 SER A 205       7.975  37.618  -5.125  1.00 20.13           H  
ATOM   3248  HB3 SER A 205       7.110  38.327  -3.998  1.00 20.13           H  
ATOM   3249  HG  SER A 205       7.201  35.725  -4.374  1.00 23.51           H  
ATOM   3250  N   LYS A 206       5.344  39.939  -5.841  1.00 17.99           N  
ANISOU 3250  N   LYS A 206     2998   1658   2178   -147    188     15       N  
ATOM   3251  CA  LYS A 206       5.445  41.284  -6.388  1.00 18.17           C  
ANISOU 3251  CA  LYS A 206     3142   1564   2197   -137    190     55       C  
ATOM   3252  C   LYS A 206       5.888  42.243  -5.296  1.00 18.74           C  
ANISOU 3252  C   LYS A 206     3327   1538   2255   -247    223     24       C  
ATOM   3253  O   LYS A 206       5.255  42.317  -4.231  1.00 19.47           O  
ANISOU 3253  O   LYS A 206     3434   1598   2368   -240    256    -61       O  
ATOM   3254  CB  LYS A 206       4.106  41.764  -6.966  1.00 25.28           C  
ANISOU 3254  CB  LYS A 206     4065   2391   3150     27    182     28       C  
ATOM   3255  CG  LYS A 206       4.235  43.119  -7.696  1.00 34.79           C  
ANISOU 3255  CG  LYS A 206     5411   3461   4344     49    167     88       C  
ATOM   3256  CD  LYS A 206       2.958  43.538  -8.389  1.00 40.99           C  
ANISOU 3256  CD  LYS A 206     6215   4180   5178    230    138     69       C  
ATOM   3257  H   LYS A 206       4.811  39.878  -5.169  1.00 21.59           H  
ATOM   3258  HA  LYS A 206       6.108  41.297  -7.096  1.00 21.80           H  
ATOM   3259  HB2 LYS A 206       3.782  41.108  -7.603  1.00 30.34           H  
ATOM   3260  HB3 LYS A 206       3.469  41.871  -6.243  1.00 30.34           H  
ATOM   3261  HG2 LYS A 206       4.464  43.806  -7.050  1.00 41.74           H  
ATOM   3262  HG3 LYS A 206       4.931  43.051  -8.368  1.00 41.74           H  
ATOM   3263  N   LEU A 207       6.960  42.981  -5.561  1.00 18.45           N  
ANISOU 3263  N   LEU A 207     3370   1460   2181   -355    219     87       N  
ATOM   3264  CA  LEU A 207       7.455  43.969  -4.607  1.00 21.13           C  
ANISOU 3264  CA  LEU A 207     3826   1697   2506   -472    244     57       C  
ATOM   3265  C   LEU A 207       6.991  45.353  -5.039  1.00 20.66           C  
ANISOU 3265  C   LEU A 207     3917   1462   2471   -421    246     71       C  
ATOM   3266  O   LEU A 207       6.962  45.653  -6.237  1.00 20.93           O  
ANISOU 3266  O   LEU A 207     3982   1470   2502   -367    222    150       O  
ATOM   3267  CB  LEU A 207       8.990  43.936  -4.518  1.00 18.51           C  
ANISOU 3267  CB  LEU A 207     3485   1428   2119   -645    235    108       C  
ATOM   3268  CG  LEU A 207       9.692  42.585  -4.427  1.00 17.05           C  
ANISOU 3268  CG  LEU A 207     3153   1420   1906   -686    212    117       C  
ATOM   3269  CD1 LEU A 207      11.185  42.763  -4.158  1.00 25.24           C  
ANISOU 3269  CD1 LEU A 207     4186   2509   2896   -857    203    144       C  
ATOM   3270  CD2 LEU A 207       9.055  41.703  -3.388  1.00 17.74           C  
ANISOU 3270  CD2 LEU A 207     3179   1554   2006   -647    216     41       C  
ATOM   3271  H   LEU A 207       7.419  42.929  -6.286  1.00 22.14           H  
ATOM   3272  HA  LEU A 207       7.091  43.782  -3.728  1.00 25.36           H  
ATOM   3273  HB2 LEU A 207       9.341  44.381  -5.305  1.00 22.21           H  
ATOM   3274  HB3 LEU A 207       9.251  44.439  -3.731  1.00 22.21           H  
ATOM   3275  HG  LEU A 207       9.603  42.136  -5.283  1.00 20.46           H  
ATOM   3276 HD11 LEU A 207      11.602  41.888  -4.106  1.00 30.29           H  
ATOM   3277 HD12 LEU A 207      11.577  43.274  -4.882  1.00 30.29           H  
ATOM   3278 HD13 LEU A 207      11.300  43.235  -3.318  1.00 30.29           H  
ATOM   3279 HD21 LEU A 207       9.527  40.856  -3.360  1.00 21.29           H  
ATOM   3280 HD22 LEU A 207       9.112  42.142  -2.524  1.00 21.29           H  
ATOM   3281 HD23 LEU A 207       8.126  41.557  -3.624  1.00 21.29           H  
ATOM   3282  N   SER A 208       6.640  46.205  -4.073  1.00 19.76           N  
ANISOU 3282  N   SER A 208     3906   1224   2377   -435    271     -5       N  
ATOM   3283  CA  SER A 208       6.198  47.567  -4.366  1.00 21.20           C  
ANISOU 3283  CA  SER A 208     4249   1215   2589   -381    265     -3       C  
ATOM   3284  C   SER A 208       6.560  48.495  -3.215  1.00 22.80           C  
ANISOU 3284  C   SER A 208     4573   1304   2788   -491    289    -72       C  
ATOM   3285  O   SER A 208       7.197  48.069  -2.255  1.00 22.70           O  
ANISOU 3285  O   SER A 208     4508   1377   2739   -610    308   -112       O  
ATOM   3286  CB  SER A 208       4.685  47.603  -4.596  1.00 23.94           C  
ANISOU 3286  CB  SER A 208     4578   1518   2998   -173    258    -63       C  
ATOM   3287  OG  SER A 208       4.015  47.027  -3.490  1.00 21.95           O  
ANISOU 3287  OG  SER A 208     4243   1331   2765   -142    297   -180       O  
ATOM   3288  H   SER A 208       6.651  46.016  -3.235  1.00 23.71           H  
ATOM   3289  HA  SER A 208       6.640  47.885  -5.169  1.00 25.43           H  
ATOM   3290  HB2 SER A 208       4.400  48.525  -4.697  1.00 28.72           H  
ATOM   3291  HB3 SER A 208       4.472  47.098  -5.396  1.00 28.72           H  
ATOM   3292  HG  SER A 208       3.185  47.047  -3.615  1.00 26.34           H  
ATOM   3293  N   LYS A 209       6.153  49.755  -3.328  1.00 25.65           N  
ANISOU 3293  N   LYS A 209     5039   1525   3180   -429    273    -83       N  
ATOM   3294  CA  LYS A 209       6.408  50.744  -2.282  1.00 26.06           C  
ANISOU 3294  CA  LYS A 209     5159   1509   3232   -500    283   -153       C  
ATOM   3295  C   LYS A 209       5.110  51.408  -1.874  1.00 30.93           C  
ANISOU 3295  C   LYS A 209     5822   2017   3912   -340    287   -255       C  
ATOM   3296  O   LYS A 209       4.189  51.522  -2.670  1.00 32.15           O  
ANISOU 3296  O   LYS A 209     5984   2119   4114   -179    262   -243       O  
ATOM   3297  CB  LYS A 209       7.404  51.801  -2.760  1.00 26.06           C  
ANISOU 3297  CB  LYS A 209     5249   1441   3212   -612    256    -69       C  
ATOM   3298  CG  LYS A 209       8.762  51.249  -3.149  1.00 28.86           C  
ANISOU 3298  CG  LYS A 209     5536   1924   3505   -774    255     18       C  
ATOM   3299  CD  LYS A 209       9.601  50.845  -1.961  1.00 26.24           C  
ANISOU 3299  CD  LYS A 209     5136   1700   3133   -910    272    -40       C  
ATOM   3300  CE  LYS A 209      10.997  50.498  -2.396  1.00 24.65           C  
ANISOU 3300  CE  LYS A 209     4862   1623   2881  -1057    262     38       C  
ATOM   3301  NZ  LYS A 209      11.882  49.995  -1.329  1.00 24.38           N  
ANISOU 3301  NZ  LYS A 209     4745   1713   2806  -1175    262    -12       N  
ATOM   3302  H   LYS A 209       5.725  50.066  -4.006  1.00 30.77           H  
ATOM   3303  HA  LYS A 209       6.782  50.301  -1.504  1.00 31.27           H  
ATOM   3304  HB2 LYS A 209       7.033  52.248  -3.537  1.00 31.27           H  
ATOM   3305  HB3 LYS A 209       7.540  52.445  -2.047  1.00 31.27           H  
ATOM   3306  HG2 LYS A 209       8.636  50.464  -3.706  1.00 34.63           H  
ATOM   3307  HG3 LYS A 209       9.249  51.928  -3.641  1.00 34.63           H  
ATOM   3308  HD2 LYS A 209       9.649  51.583  -1.333  1.00 31.48           H  
ATOM   3309  HD3 LYS A 209       9.208  50.065  -1.538  1.00 31.48           H  
ATOM   3310  HE2 LYS A 209      10.945  49.811  -3.079  1.00 29.58           H  
ATOM   3311  HE3 LYS A 209      11.410  51.294  -2.766  1.00 29.58           H  
ATOM   3312  HZ1 LYS A 209      11.966  50.608  -0.689  1.00 29.26           H  
ATOM   3313  HZ2 LYS A 209      11.541  49.253  -0.975  1.00 29.26           H  
ATOM   3314  HZ3 LYS A 209      12.687  49.813  -1.662  1.00 29.26           H  
ATOM   3315  N   ASP A 210       5.047  51.807  -0.608  1.00 27.94           N  
ANISOU 3315  N   ASP A 210     5459   1624   3532   -379    313   -361       N  
ATOM   3316  CA  ASP A 210       4.004  52.665  -0.073  1.00 27.79           C  
ANISOU 3316  CA  ASP A 210     5486   1502   3571   -252    317   -471       C  
ATOM   3317  C   ASP A 210       4.362  54.124  -0.335  1.00 29.61           C  
ANISOU 3317  C   ASP A 210     5853   1573   3825   -276    275   -437       C  
ATOM   3318  O   ASP A 210       5.365  54.622   0.184  1.00 31.07           O  
ANISOU 3318  O   ASP A 210     6091   1742   3973   -429    276   -426       O  
ATOM   3319  CB  ASP A 210       3.919  52.412   1.427  1.00 27.72           C  
ANISOU 3319  CB  ASP A 210     5437   1563   3533   -308    366   -594       C  
ATOM   3320  CG  ASP A 210       2.855  53.244   2.118  1.00 34.59           C  
ANISOU 3320  CG  ASP A 210     6336   2349   4458   -183    378   -729       C  
ATOM   3321  OD1 ASP A 210       2.306  54.196   1.519  1.00 32.29           O  
ANISOU 3321  OD1 ASP A 210     6110   1925   4234    -66    338   -729       O  
ATOM   3322  OD2 ASP A 210       2.597  52.947   3.308  1.00 36.03           O  
ANISOU 3322  OD2 ASP A 210     6473   2606   4611   -207    426   -837       O  
ATOM   3323  H   ASP A 210       5.627  51.580  -0.016  1.00 33.53           H  
ATOM   3324  HA  ASP A 210       3.150  52.460  -0.485  1.00 33.35           H  
ATOM   3325  HB2 ASP A 210       3.711  51.476   1.577  1.00 33.26           H  
ATOM   3326  HB3 ASP A 210       4.775  52.628   1.831  1.00 33.26           H  
ATOM   3327  N   PRO A 211       3.543  54.828  -1.131  1.00 38.64           N  
ANISOU 3327  N   PRO A 211     7052   2599   5032   -122    235   -423       N  
ATOM   3328  CA  PRO A 211       3.892  56.217  -1.468  1.00 43.21           C  
ANISOU 3328  CA  PRO A 211     7772   3013   5631   -148    191   -379       C  
ATOM   3329  C   PRO A 211       3.965  57.154  -0.254  1.00 43.27           C  
ANISOU 3329  C   PRO A 211     7846   2936   5658   -193    203   -492       C  
ATOM   3330  O   PRO A 211       4.613  58.203  -0.314  1.00 48.59           O  
ANISOU 3330  O   PRO A 211     8636   3492   6332   -279    176   -454       O  
ATOM   3331  CB  PRO A 211       2.766  56.644  -2.421  1.00 42.85           C  
ANISOU 3331  CB  PRO A 211     7752   2876   5653     57    142   -364       C  
ATOM   3332  CG  PRO A 211       1.656  55.653  -2.187  1.00 40.59           C  
ANISOU 3332  CG  PRO A 211     7323   2701   5397    203    169   -456       C  
ATOM   3333  CD  PRO A 211       2.311  54.382  -1.811  1.00 34.27           C  
ANISOU 3333  CD  PRO A 211     6429   2063   4530     77    220   -440       C  
ATOM   3334  HA  PRO A 211       4.738  56.244  -1.942  1.00 51.85           H  
ATOM   3335  HB2 PRO A 211       2.475  57.544  -2.202  1.00 51.42           H  
ATOM   3336  HB3 PRO A 211       3.079  56.598  -3.338  1.00 51.42           H  
ATOM   3337  HG2 PRO A 211       1.087  55.968  -1.466  1.00 48.70           H  
ATOM   3338  HG3 PRO A 211       1.142  55.543  -3.002  1.00 48.70           H  
ATOM   3339  HD2 PRO A 211       1.750  53.879  -1.201  1.00 41.13           H  
ATOM   3340  HD3 PRO A 211       2.529  53.867  -2.604  1.00 41.13           H  
ATOM   3341  N   ASN A 212       3.322  56.757   0.836  1.00 42.79           N  
ANISOU 3341  N   ASN A 212     7711   2941   5607   -143    245   -630       N  
ATOM   3342  CA  ASN A 212       3.283  57.559   2.045  1.00 43.39           C  
ANISOU 3342  CA  ASN A 212     7838   2953   5695   -171    259   -754       C  
ATOM   3343  C   ASN A 212       4.293  57.117   3.100  1.00 42.76           C  
ANISOU 3343  C   ASN A 212     7732   2982   5533   -358    296   -776       C  
ATOM   3344  O   ASN A 212       4.276  57.619   4.223  1.00 40.97           O  
ANISOU 3344  O   ASN A 212     7535   2731   5301   -387    313   -887       O  
ATOM   3345  CB  ASN A 212       1.873  57.508   2.626  1.00 47.97           C  
ANISOU 3345  CB  ASN A 212     8349   3545   6334     10    283   -908       C  
ATOM   3346  CG  ASN A 212       0.841  58.057   1.666  1.00 52.23           C  
ANISOU 3346  CG  ASN A 212     8903   3978   6964    206    238   -902       C  
ATOM   3347  OD1 ASN A 212       1.049  59.106   1.051  1.00 54.15           O  
ANISOU 3347  OD1 ASN A 212     9268   4064   7243    218    184   -839       O  
ATOM   3348  ND2 ASN A 212      -0.269  57.342   1.512  1.00 54.10           N  
ANISOU 3348  ND2 ASN A 212     9013   4307   7237    358    257   -963       N  
ATOM   3349  H   ASN A 212       2.894  56.014   0.899  1.00 51.35           H  
ATOM   3350  HA  ASN A 212       3.477  58.481   1.815  1.00 52.07           H  
ATOM   3351  HB2 ASN A 212       1.643  56.586   2.822  1.00 57.57           H  
ATOM   3352  HB3 ASN A 212       1.844  58.039   3.437  1.00 57.57           H  
ATOM   3353 HD21 ASN A 212      -0.371  56.607   1.947  1.00 64.92           H  
ATOM   3354 HD22 ASN A 212      -0.885  57.614   0.977  1.00 64.92           H  
ATOM   3355  N   GLU A 213       5.163  56.174   2.755  1.00 32.75           N  
ANISOU 3355  N   GLU A 213     6404   1840   4201   -477    306   -675       N  
ATOM   3356  CA  GLU A 213       6.132  55.664   3.727  1.00 32.07           C  
ANISOU 3356  CA  GLU A 213     6276   1875   4036   -646    331   -691       C  
ATOM   3357  C   GLU A 213       7.507  56.253   3.474  1.00 32.92           C  
ANISOU 3357  C   GLU A 213     6445   1951   4111   -815    300   -603       C  
ATOM   3358  O   GLU A 213       8.089  56.062   2.402  1.00 32.18           O  
ANISOU 3358  O   GLU A 213     6344   1875   4008   -860    280   -481       O  
ATOM   3359  CB  GLU A 213       6.204  54.140   3.695  1.00 29.99           C  
ANISOU 3359  CB  GLU A 213     5883   1791   3722   -669    361   -659       C  
ATOM   3360  CG  GLU A 213       7.178  53.558   4.704  1.00 29.39           C  
ANISOU 3360  CG  GLU A 213     5757   1847   3562   -829    376   -672       C  
ATOM   3361  CD  GLU A 213       6.838  53.924   6.146  1.00 30.34           C  
ANISOU 3361  CD  GLU A 213     5902   1966   3660   -834    404   -807       C  
ATOM   3362  OE1 GLU A 213       5.813  53.437   6.650  1.00 30.06           O  
ANISOU 3362  OE1 GLU A 213     5816   1978   3627   -736    445   -893       O  
ATOM   3363  OE2 GLU A 213       7.599  54.706   6.768  1.00 31.48           O  
ANISOU 3363  OE2 GLU A 213     6112   2068   3782   -938    386   -830       O  
ATOM   3364  H   GLU A 213       5.215  55.815   1.976  1.00 39.30           H  
ATOM   3365  HA  GLU A 213       5.853  55.930   4.617  1.00 38.49           H  
ATOM   3366  HB2 GLU A 213       5.324  53.781   3.889  1.00 35.99           H  
ATOM   3367  HB3 GLU A 213       6.488  53.859   2.811  1.00 35.99           H  
ATOM   3368  HG2 GLU A 213       7.166  52.591   4.631  1.00 35.26           H  
ATOM   3369  HG3 GLU A 213       8.068  53.893   4.512  1.00 35.26           H  
ATOM   3370  N   LYS A 214       8.019  56.956   4.482  1.00 34.65           N  
ANISOU 3370  N   LYS A 214     6719   2135   4311   -908    299   -672       N  
ATOM   3371  CA  LYS A 214       9.296  57.641   4.373  1.00 34.87           C  
ANISOU 3371  CA  LYS A 214     6805   2129   4315  -1071    271   -610       C  
ATOM   3372  C   LYS A 214      10.465  56.736   4.787  1.00 34.90           C  
ANISOU 3372  C   LYS A 214     6708   2316   4237  -1227    278   -575       C  
ATOM   3373  O   LYS A 214      11.599  56.900   4.327  1.00 35.08           O  
ANISOU 3373  O   LYS A 214     6727   2368   4235  -1356    258   -495       O  
ATOM   3374  CB  LYS A 214       9.259  58.910   5.232  1.00 36.91           C  
ANISOU 3374  CB  LYS A 214     7176   2248   4601  -1089    259   -709       C  
ATOM   3375  CG  LYS A 214       8.217  59.928   4.777  1.00 45.90           C  
ANISOU 3375  CG  LYS A 214     8419   3192   5829   -936    239   -743       C  
ATOM   3376  H   LYS A 214       7.639  57.049   5.247  1.00 41.58           H  
ATOM   3377  HA  LYS A 214       9.434  57.906   3.451  1.00 41.84           H  
ATOM   3378  HB2 LYS A 214       9.053  58.662   6.147  1.00 44.29           H  
ATOM   3379  HB3 LYS A 214      10.129  59.338   5.195  1.00 44.29           H  
ATOM   3380  N   ARG A 215      10.198  55.774   5.657  1.00 32.49           N  
ANISOU 3380  N   ARG A 215     6317   2139   3888  -1212    305   -638       N  
ATOM   3381  CA  ARG A 215      11.242  54.853   6.057  1.00 31.43           C  
ANISOU 3381  CA  ARG A 215     6085   2179   3679  -1339    300   -605       C  
ATOM   3382  C   ARG A 215      11.560  53.869   4.927  1.00 29.87           C  
ANISOU 3382  C   ARG A 215     5793   2082   3475  -1338    293   -493       C  
ATOM   3383  O   ARG A 215      10.768  53.669   4.008  1.00 29.31           O  
ANISOU 3383  O   ARG A 215     5722   1968   3448  -1225    301   -454       O  
ATOM   3384  CB  ARG A 215      10.821  54.097   7.316  1.00 30.84           C  
ANISOU 3384  CB  ARG A 215     5957   2207   3552  -1322    327   -697       C  
ATOM   3385  CG  ARG A 215      10.744  54.994   8.543  1.00 32.45           C  
ANISOU 3385  CG  ARG A 215     6242   2344   3743  -1350    332   -811       C  
ATOM   3386  CD  ARG A 215      10.058  54.263   9.674  1.00 35.38           C  
ANISOU 3386  CD  ARG A 215     6569   2810   4062  -1307    370   -902       C  
ATOM   3387  NE  ARG A 215       8.684  53.962   9.300  1.00 43.46           N  
ANISOU 3387  NE  ARG A 215     7574   3803   5134  -1149    410   -935       N  
ATOM   3388  CZ  ARG A 215       7.770  53.448  10.119  1.00 51.46           C  
ANISOU 3388  CZ  ARG A 215     8553   4879   6119  -1082    458  -1025       C  
ATOM   3389  NH1 ARG A 215       8.083  53.170  11.382  1.00 48.64           N  
ANISOU 3389  NH1 ARG A 215     8188   4616   5679  -1162    471  -1082       N  
ATOM   3390  NH2 ARG A 215       6.538  53.214   9.671  1.00 49.46           N  
ANISOU 3390  NH2 ARG A 215     8270   4604   5919   -935    492  -1057       N  
ATOM   3391  H   ARG A 215       9.433  55.635   6.023  1.00 38.99           H  
ATOM   3392  HA  ARG A 215      12.048  55.353   6.259  1.00 37.72           H  
ATOM   3393  HB2 ARG A 215       9.944  53.708   7.173  1.00 37.00           H  
ATOM   3394  HB3 ARG A 215      11.469  53.398   7.496  1.00 37.00           H  
ATOM   3395  HG2 ARG A 215      11.640  55.233   8.828  1.00 38.94           H  
ATOM   3396  HG3 ARG A 215      10.230  55.789   8.333  1.00 38.94           H  
ATOM   3397  HD2 ARG A 215      10.520  53.429   9.852  1.00 42.45           H  
ATOM   3398  HD3 ARG A 215      10.048  54.824  10.466  1.00 42.45           H  
ATOM   3399  HE  ARG A 215       8.445  54.128   8.491  1.00 52.15           H  
ATOM   3400 HH11 ARG A 215       8.878  53.322  11.671  1.00 58.37           H  
ATOM   3401 HH12 ARG A 215       7.489  52.838  11.908  1.00 58.37           H  
ATOM   3402 HH21 ARG A 215       6.336  53.394   8.854  1.00 59.35           H  
ATOM   3403 HH22 ARG A 215       5.945  52.881  10.197  1.00 59.35           H  
ATOM   3404  N   ASP A 216      12.739  53.273   5.010  1.00 29.31           N  
ANISOU 3404  N   ASP A 216     5639   2148   3349  -1460    273   -448       N  
ATOM   3405  CA  ASP A 216      13.166  52.255   4.066  1.00 27.91           C  
ANISOU 3405  CA  ASP A 216     5355   2089   3160  -1467    262   -356       C  
ATOM   3406  C   ASP A 216      12.281  51.046   4.313  1.00 26.39           C  
ANISOU 3406  C   ASP A 216     5091   1977   2960  -1368    282   -382       C  
ATOM   3407  O   ASP A 216      12.176  50.571   5.451  1.00 26.17           O  
ANISOU 3407  O   ASP A 216     5037   2017   2888  -1382    290   -449       O  
ATOM   3408  CB  ASP A 216      14.633  51.911   4.332  1.00 27.91           C  
ANISOU 3408  CB  ASP A 216     5274   2225   3106  -1612    231   -330       C  
ATOM   3409  CG  ASP A 216      15.312  51.258   3.143  1.00 27.88           C  
ANISOU 3409  CG  ASP A 216     5174   2318   3100  -1639    217   -233       C  
ATOM   3410  OD1 ASP A 216      14.648  51.085   2.097  1.00 26.50           O  
ANISOU 3410  OD1 ASP A 216     5006   2102   2962  -1550    231   -179       O  
ATOM   3411  OD2 ASP A 216      16.518  50.940   3.274  1.00 27.16           O  
ANISOU 3411  OD2 ASP A 216     5002   2348   2971  -1747    190   -216       O  
ATOM   3412  H   ASP A 216      13.322  53.445   5.618  1.00 35.17           H  
ATOM   3413  HA  ASP A 216      13.058  52.562   3.152  1.00 33.49           H  
ATOM   3414  HB2 ASP A 216      15.115  52.726   4.541  1.00 33.49           H  
ATOM   3415  HB3 ASP A 216      14.682  51.295   5.080  1.00 33.49           H  
ATOM   3416  N   HIS A 217      11.631  50.548   3.270  1.00 25.48           N  
ANISOU 3416  N   HIS A 217     4947   1851   2881  -1272    291   -330       N  
ATOM   3417  CA  HIS A 217      10.585  49.549   3.458  1.00 24.30           C  
ANISOU 3417  CA  HIS A 217     4747   1748   2739  -1167    317   -366       C  
ATOM   3418  C   HIS A 217      10.379  48.746   2.183  1.00 23.13           C  
ANISOU 3418  C   HIS A 217     4534   1637   2616  -1105    310   -284       C  
ATOM   3419  O   HIS A 217      10.942  49.050   1.113  1.00 23.31           O  
ANISOU 3419  O   HIS A 217     4562   1644   2651  -1132    290   -199       O  
ATOM   3420  CB  HIS A 217       9.265  50.239   3.812  1.00 25.08           C  
ANISOU 3420  CB  HIS A 217     4930   1718   2884  -1047    351   -452       C  
ATOM   3421  CG  HIS A 217       8.715  51.062   2.690  1.00 25.75           C  
ANISOU 3421  CG  HIS A 217     5088   1660   3036   -951    343   -412       C  
ATOM   3422  ND1 HIS A 217       9.315  52.229   2.274  1.00 27.07           N  
ANISOU 3422  ND1 HIS A 217     5344   1723   3217  -1006    317   -370       N  
ATOM   3423  CD2 HIS A 217       7.655  50.868   1.864  1.00 25.38           C  
ANISOU 3423  CD2 HIS A 217     5040   1562   3042   -804    351   -401       C  
ATOM   3424  CE1 HIS A 217       8.636  52.734   1.261  1.00 27.52           C  
ANISOU 3424  CE1 HIS A 217     5461   1666   3330   -896    307   -330       C  
ATOM   3425  NE2 HIS A 217       7.622  51.937   0.999  1.00 26.52           N  
ANISOU 3425  NE2 HIS A 217     5278   1569   3228   -766    324   -350       N  
ATOM   3426  H   HIS A 217      11.773  50.767   2.451  1.00 30.57           H  
ATOM   3427  HA  HIS A 217      10.829  48.945   4.177  1.00 29.16           H  
ATOM   3428  HB2 HIS A 217       8.606  49.563   4.037  1.00 30.10           H  
ATOM   3429  HB3 HIS A 217       9.409  50.826   4.570  1.00 30.10           H  
ATOM   3430  HD1 HIS A 217      10.016  52.580   2.627  1.00 32.48           H  
ATOM   3431  HD2 HIS A 217       7.051  50.162   1.895  1.00 30.46           H  
ATOM   3432  HE1 HIS A 217       8.835  53.524   0.813  1.00 33.03           H  
ATOM   3433  HE2 HIS A 217       7.042  52.056   0.376  1.00 31.82           H  
ATOM   3434  N   MET A 218       9.531  47.734   2.321  1.00 22.06           N  
ANISOU 3434  N   MET A 218     4342   1554   2487  -1024    331   -314       N  
ATOM   3435  CA  MET A 218       9.163  46.867   1.218  1.00 21.87           C  
ANISOU 3435  CA  MET A 218     4256   1564   2491   -951    326   -252       C  
ATOM   3436  C   MET A 218       7.739  46.420   1.444  1.00 20.57           C  
ANISOU 3436  C   MET A 218     4085   1370   2360   -821    366   -325       C  
ATOM   3437  O   MET A 218       7.392  45.914   2.510  1.00 20.37           O  
ANISOU 3437  O   MET A 218     4030   1405   2306   -832    392   -400       O  
ATOM   3438  CB  MET A 218      10.077  45.649   1.145  1.00 21.56           C  
ANISOU 3438  CB  MET A 218     4099   1684   2409  -1031    296   -201       C  
ATOM   3439  CG  MET A 218       9.615  44.597   0.122  1.00 24.36           C  
ANISOU 3439  CG  MET A 218     4370   2094   2791   -944    290   -148       C  
ATOM   3440  SD  MET A 218      10.745  43.211  -0.016  1.00 19.36           S  
ANISOU 3440  SD  MET A 218     3585   1656   2116  -1014    240    -90       S  
ATOM   3441  CE  MET A 218      10.650  42.406   1.583  1.00 20.05           C  
ANISOU 3441  CE  MET A 218     3648   1815   2156  -1059    237   -168       C  
ATOM   3442  H   MET A 218       9.149  47.527   3.063  1.00 26.48           H  
ATOM   3443  HA  MET A 218       9.225  47.355   0.382  1.00 26.25           H  
ATOM   3444  HB2 MET A 218      10.967  45.940   0.891  1.00 25.87           H  
ATOM   3445  HB3 MET A 218      10.104  45.225   2.016  1.00 25.87           H  
ATOM   3446  HG2 MET A 218       8.750  44.252   0.393  1.00 29.23           H  
ATOM   3447  HG3 MET A 218       9.546  45.015  -0.751  1.00 29.23           H  
ATOM   3448  HE1 MET A 218      11.242  41.638   1.585  1.00 24.06           H  
ATOM   3449  HE2 MET A 218      10.921  43.035   2.270  1.00 24.06           H  
ATOM   3450  HE3 MET A 218       9.736  42.121   1.738  1.00 24.06           H  
ATOM   3451  N   VAL A 219       6.910  46.636   0.435  1.00 20.62           N  
ANISOU 3451  N   VAL A 219     4115   1294   2424   -692    369   -304       N  
ATOM   3452  CA  VAL A 219       5.587  46.057   0.402  1.00 20.19           C  
ANISOU 3452  CA  VAL A 219     3981   1281   2408   -536    393   -357       C  
ATOM   3453  C   VAL A 219       5.635  44.796  -0.462  1.00 18.85           C  
ANISOU 3453  C   VAL A 219     3668   1255   2241   -493    365   -279       C  
ATOM   3454  O   VAL A 219       6.260  44.776  -1.540  1.00 18.61           O  
ANISOU 3454  O   VAL A 219     3625   1236   2208   -503    327   -182       O  
ATOM   3455  CB  VAL A 219       4.570  47.035  -0.172  1.00 21.20           C  
ANISOU 3455  CB  VAL A 219     4187   1265   2603   -385    396   -387       C  
ATOM   3456  CG1 VAL A 219       3.199  46.373  -0.303  1.00 20.81           C  
ANISOU 3456  CG1 VAL A 219     4027   1282   2600   -221    417   -446       C  
ATOM   3457  CG2 VAL A 219       4.479  48.308   0.716  1.00 22.70           C  
ANISOU 3457  CG2 VAL A 219     4497   1329   2797   -407    413   -471       C  
ATOM   3458  H   VAL A 219       7.096  47.122  -0.249  1.00 24.74           H  
ATOM   3459  HA  VAL A 219       5.313  45.811   1.299  1.00 24.22           H  
ATOM   3460  HB  VAL A 219       4.858  47.307  -1.058  1.00 25.44           H  
ATOM   3461 HG11 VAL A 219       2.572  47.016  -0.670  1.00 24.98           H  
ATOM   3462 HG12 VAL A 219       3.273  45.608  -0.894  1.00 24.98           H  
ATOM   3463 HG13 VAL A 219       2.902  46.086   0.575  1.00 24.98           H  
ATOM   3464 HG21 VAL A 219       3.827  48.915   0.332  1.00 27.24           H  
ATOM   3465 HG22 VAL A 219       4.205  48.050   1.610  1.00 27.24           H  
ATOM   3466 HG23 VAL A 219       5.350  48.734   0.747  1.00 27.24           H  
ATOM   3467  N   LEU A 220       4.956  43.755  -0.004  1.00 18.68           N  
ANISOU 3467  N   LEU A 220     3540   1337   2220   -447    385   -326       N  
ATOM   3468  CA  LEU A 220       5.095  42.444  -0.608  1.00 16.94           C  
ANISOU 3468  CA  LEU A 220     3188   1252   1996   -428    355   -265       C  
ATOM   3469  C   LEU A 220       3.740  41.780  -0.811  1.00 19.19           C  
ANISOU 3469  C   LEU A 220     3380   1583   2329   -292    375   -313       C  
ATOM   3470  O   LEU A 220       2.888  41.761   0.086  1.00 17.27           O  
ANISOU 3470  O   LEU A 220     3132   1340   2092   -271    427   -406       O  
ATOM   3471  CB  LEU A 220       5.970  41.569   0.294  1.00 19.12           C  
ANISOU 3471  CB  LEU A 220     3425   1631   2210   -559    344   -259       C  
ATOM   3472  CG  LEU A 220       6.114  40.098  -0.109  1.00 25.07           C  
ANISOU 3472  CG  LEU A 220     4049   2516   2959   -541    308   -211       C  
ATOM   3473  CD1 LEU A 220       6.821  39.979  -1.456  1.00 23.11           C  
ANISOU 3473  CD1 LEU A 220     3759   2299   2722   -520    259   -121       C  
ATOM   3474  CD2 LEU A 220       6.861  39.307   0.947  1.00 25.55           C  
ANISOU 3474  CD2 LEU A 220     4093   2656   2957   -657    290   -215       C  
ATOM   3475  H   LEU A 220       4.408  43.783   0.658  1.00 22.41           H  
ATOM   3476  HA  LEU A 220       5.529  42.529  -1.471  1.00 20.33           H  
ATOM   3477  HB2 LEU A 220       6.862  41.950   0.313  1.00 22.95           H  
ATOM   3478  HB3 LEU A 220       5.596  41.585   1.189  1.00 22.95           H  
ATOM   3479  HG  LEU A 220       5.230  39.711  -0.202  1.00 30.08           H  
ATOM   3480 HD11 LEU A 220       6.900  39.040  -1.688  1.00 27.73           H  
ATOM   3481 HD12 LEU A 220       6.299  40.444  -2.128  1.00 27.73           H  
ATOM   3482 HD13 LEU A 220       7.702  40.378  -1.386  1.00 27.73           H  
ATOM   3483 HD21 LEU A 220       6.932  38.384   0.658  1.00 30.65           H  
ATOM   3484 HD22 LEU A 220       7.745  39.688   1.060  1.00 30.65           H  
ATOM   3485 HD23 LEU A 220       6.370  39.355   1.783  1.00 30.65           H  
ATOM   3486  N   LEU A 221       3.542  41.238  -2.000  1.00 16.89           N  
ANISOU 3486  N   LEU A 221     3011   1339   2068   -207    338   -255       N  
ATOM   3487  CA  LEU A 221       2.369  40.444  -2.279  1.00 16.57           C  
ANISOU 3487  CA  LEU A 221     2862   1362   2072    -94    346   -296       C  
ATOM   3488  C   LEU A 221       2.876  39.133  -2.822  1.00 15.33           C  
ANISOU 3488  C   LEU A 221     2603   1322   1900   -118    302   -232       C  
ATOM   3489  O   LEU A 221       3.609  39.115  -3.834  1.00 20.30           O  
ANISOU 3489  O   LEU A 221     3227   1966   2519   -114    255   -152       O  
ATOM   3490  CB  LEU A 221       1.452  41.131  -3.300  1.00 16.82           C  
ANISOU 3490  CB  LEU A 221     2901   1327   2164     64    329   -303       C  
ATOM   3491  CG  LEU A 221       0.295  40.255  -3.798  1.00 16.03           C  
ANISOU 3491  CG  LEU A 221     2669   1309   2114    182    323   -341       C  
ATOM   3492  CD1 LEU A 221      -0.669  39.934  -2.684  1.00 20.35           C  
ANISOU 3492  CD1 LEU A 221     3162   1892   2679    181    389   -453       C  
ATOM   3493  CD2 LEU A 221      -0.451  40.948  -4.942  1.00 21.24           C  
ANISOU 3493  CD2 LEU A 221     3339   1907   2824    343    283   -335       C  
ATOM   3494  H   LEU A 221       4.080  41.318  -2.666  1.00 20.27           H  
ATOM   3495  HA  LEU A 221       1.872  40.281  -1.462  1.00 19.89           H  
ATOM   3496  HB2 LEU A 221       1.067  41.922  -2.890  1.00 20.19           H  
ATOM   3497  HB3 LEU A 221       1.982  41.386  -4.071  1.00 20.19           H  
ATOM   3498  HG  LEU A 221       0.653  39.420  -4.136  1.00 19.24           H  
ATOM   3499 HD11 LEU A 221      -1.385  39.381  -3.036  1.00 24.42           H  
ATOM   3500 HD12 LEU A 221      -0.196  39.458  -1.985  1.00 24.42           H  
ATOM   3501 HD13 LEU A 221      -1.033  40.762  -2.333  1.00 24.42           H  
ATOM   3502 HD21 LEU A 221      -1.175  40.376  -5.239  1.00 25.49           H  
ATOM   3503 HD22 LEU A 221      -0.805  41.792  -4.622  1.00 25.49           H  
ATOM   3504 HD23 LEU A 221       0.168  41.105  -5.673  1.00 25.49           H  
ATOM   3505  N   GLU A 222       2.466  38.028  -2.219  1.00 14.09           N  
ANISOU 3505  N   GLU A 222     2367   1247   1741   -139    318   -267       N  
ATOM   3506  CA  GLU A 222       3.056  36.741  -2.580  1.00 13.64           C  
ANISOU 3506  CA  GLU A 222     2229   1287   1668   -171    269   -212       C  
ATOM   3507  C   GLU A 222       2.023  35.631  -2.643  1.00 12.85           C  
ANISOU 3507  C   GLU A 222     2025   1251   1605   -115    275   -251       C  
ATOM   3508  O   GLU A 222       1.072  35.597  -1.834  1.00 16.00           O  
ANISOU 3508  O   GLU A 222     2414   1649   2016   -117    333   -325       O  
ATOM   3509  CB  GLU A 222       4.125  36.430  -1.526  1.00 16.73           C  
ANISOU 3509  CB  GLU A 222     2660   1702   1994   -311    263   -195       C  
ATOM   3510  CG  GLU A 222       4.888  35.141  -1.701  1.00 20.87           C  
ANISOU 3510  CG  GLU A 222     3118   2315   2499   -348    203   -144       C  
ATOM   3511  CD  GLU A 222       6.021  35.044  -0.669  1.00 35.31           C  
ANISOU 3511  CD  GLU A 222     4997   4160   4261   -477    184   -128       C  
ATOM   3512  OE1 GLU A 222       6.898  35.937  -0.670  1.00 38.09           O  
ANISOU 3512  OE1 GLU A 222     5405   4482   4588   -532    177   -108       O  
ATOM   3513  OE2 GLU A 222       6.016  34.096   0.146  1.00 32.77           O  
ANISOU 3513  OE2 GLU A 222     4663   3878   3911   -526    171   -135       O  
ATOM   3514  H   GLU A 222       1.861  37.991  -1.608  1.00 16.91           H  
ATOM   3515  HA  GLU A 222       3.486  36.812  -3.446  1.00 16.37           H  
ATOM   3516  HB2 GLU A 222       4.774  37.151  -1.531  1.00 20.08           H  
ATOM   3517  HB3 GLU A 222       3.693  36.393  -0.658  1.00 20.08           H  
ATOM   3518  HG2 GLU A 222       4.288  34.390  -1.570  1.00 25.05           H  
ATOM   3519  HG3 GLU A 222       5.278  35.113  -2.588  1.00 25.05           H  
ATOM   3520  N   PHE A 223       2.223  34.716  -3.585  1.00 12.55           N  
ANISOU 3520  N   PHE A 223     1910   1275   1583    -74    219   -207       N  
ATOM   3521  CA  PHE A 223       1.363  33.551  -3.779  1.00 11.92           C  
ANISOU 3521  CA  PHE A 223     1731   1255   1541    -33    210   -237       C  
ATOM   3522  C   PHE A 223       2.192  32.285  -3.758  1.00 17.10           C  
ANISOU 3522  C   PHE A 223     2355   1971   2173    -93    155   -191       C  
ATOM   3523  O   PHE A 223       3.220  32.192  -4.436  1.00 14.69           O  
ANISOU 3523  O   PHE A 223     2047   1687   1848    -90    102   -134       O  
ATOM   3524  CB  PHE A 223       0.629  33.612  -5.125  1.00 12.55           C  
ANISOU 3524  CB  PHE A 223     1744   1348   1675    104    180   -244       C  
ATOM   3525  CG  PHE A 223      -0.321  34.746  -5.202  1.00 12.75           C  
ANISOU 3525  CG  PHE A 223     1793   1316   1736    189    218   -296       C  
ATOM   3526  CD1 PHE A 223      -1.619  34.592  -4.787  1.00 14.75           C  
ANISOU 3526  CD1 PHE A 223     1982   1585   2035    230    262   -384       C  
ATOM   3527  CD2 PHE A 223       0.115  35.991  -5.595  1.00 14.27           C  
ANISOU 3527  CD2 PHE A 223     2076   1432   1914    219    211   -262       C  
ATOM   3528  CE1 PHE A 223      -2.501  35.670  -4.833  1.00 14.65           C  
ANISOU 3528  CE1 PHE A 223     1985   1521   2061    326    292   -446       C  
ATOM   3529  CE2 PHE A 223      -0.744  37.063  -5.616  1.00 18.35           C  
ANISOU 3529  CE2 PHE A 223     2628   1877   2466    308    236   -313       C  
ATOM   3530  CZ  PHE A 223      -2.044  36.903  -5.233  1.00 14.57           C  
ANISOU 3530  CZ  PHE A 223     2076   1420   2038    370    273   -409       C  
ATOM   3531  H   PHE A 223       2.875  34.750  -4.145  1.00 15.06           H  
ATOM   3532  HA  PHE A 223       0.706  33.507  -3.067  1.00 14.30           H  
ATOM   3533  HB2 PHE A 223       1.280  33.715  -5.836  1.00 15.05           H  
ATOM   3534  HB3 PHE A 223       0.128  32.790  -5.249  1.00 15.05           H  
ATOM   3535  HD1 PHE A 223      -1.922  33.757  -4.512  1.00 17.69           H  
ATOM   3536  HD2 PHE A 223       1.001  36.107  -5.852  1.00 17.13           H  
ATOM   3537  HE1 PHE A 223      -3.385  35.563  -4.565  1.00 17.58           H  
ATOM   3538  HE2 PHE A 223      -0.443  37.895  -5.903  1.00 22.02           H  
ATOM   3539  HZ  PHE A 223      -2.628  37.626  -5.265  1.00 17.48           H  
ATOM   3540  N   VAL A 224       1.710  31.303  -3.015  1.00 14.77           N  
ANISOU 3540  N   VAL A 224     2031   1701   1879   -143    169   -218       N  
ATOM   3541  CA  VAL A 224       2.432  30.065  -2.812  1.00 12.71           C  
ANISOU 3541  CA  VAL A 224     1757   1475   1595   -200    111   -178       C  
ATOM   3542  C   VAL A 224       1.456  28.903  -2.924  1.00 15.70           C  
ANISOU 3542  C   VAL A 224     2066   1881   2018   -184    107   -209       C  
ATOM   3543  O   VAL A 224       0.445  28.877  -2.223  1.00 15.25           O  
ANISOU 3543  O   VAL A 224     2003   1820   1971   -218    173   -260       O  
ATOM   3544  CB  VAL A 224       3.092  30.039  -1.433  1.00 16.45           C  
ANISOU 3544  CB  VAL A 224     2315   1935   2002   -322    124   -163       C  
ATOM   3545  CG1 VAL A 224       3.904  28.737  -1.253  1.00 15.33           C  
ANISOU 3545  CG1 VAL A 224     2167   1820   1837   -365     44   -117       C  
ATOM   3546  CG2 VAL A 224       3.965  31.262  -1.254  1.00 20.16           C  
ANISOU 3546  CG2 VAL A 224     2852   2375   2432   -351    134   -146       C  
ATOM   3547  H   VAL A 224       0.951  31.333  -2.610  1.00 17.72           H  
ATOM   3548  HA  VAL A 224       3.118  29.967  -3.491  1.00 15.25           H  
ATOM   3549  HB  VAL A 224       2.402  30.059  -0.752  1.00 19.75           H  
ATOM   3550 HG11 VAL A 224       4.313  28.741  -0.373  1.00 18.39           H  
ATOM   3551 HG12 VAL A 224       3.306  27.978  -1.337  1.00 18.39           H  
ATOM   3552 HG13 VAL A 224       4.590  28.696  -1.937  1.00 18.39           H  
ATOM   3553 HG21 VAL A 224       4.376  31.231  -0.376  1.00 24.19           H  
ATOM   3554 HG22 VAL A 224       4.651  31.264  -1.940  1.00 24.19           H  
ATOM   3555 HG23 VAL A 224       3.415  32.057  -1.334  1.00 24.19           H  
ATOM   3556  N   THR A 225       1.754  27.953  -3.811  1.00 12.80           N  
ANISOU 3556  N   THR A 225     1643   1544   1677   -137     33   -186       N  
ATOM   3557  CA  THR A 225       0.886  26.818  -4.074  1.00 11.08           C  
ANISOU 3557  CA  THR A 225     1358   1344   1508   -123     16   -217       C  
ATOM   3558  C   THR A 225       1.667  25.511  -4.130  1.00 14.11           C  
ANISOU 3558  C   THR A 225     1745   1732   1884   -149    -69   -178       C  
ATOM   3559  O   THR A 225       2.660  25.395  -4.873  1.00 14.43           O  
ANISOU 3559  O   THR A 225     1774   1793   1917    -98   -136   -146       O  
ATOM   3560  CB  THR A 225       0.153  26.981  -5.443  1.00 17.71           C  
ANISOU 3560  CB  THR A 225     2109   2212   2408      2     -1   -252       C  
ATOM   3561  OG1 THR A 225      -0.678  28.132  -5.386  1.00 22.39           O  
ANISOU 3561  OG1 THR A 225     2696   2793   3016     42     67   -294       O  
ATOM   3562  CG2 THR A 225      -0.720  25.767  -5.738  1.00 20.26           C  
ANISOU 3562  CG2 THR A 225     2357   2556   2785      7    -25   -292       C  
ATOM   3563  H   THR A 225       2.474  27.949  -4.282  1.00 15.36           H  
ATOM   3564  HA  THR A 225       0.219  26.749  -3.373  1.00 13.30           H  
ATOM   3565  HB  THR A 225       0.804  27.080  -6.155  1.00 21.25           H  
ATOM   3566  HG1 THR A 225      -1.080  28.233  -6.117  1.00 26.86           H  
ATOM   3567 HG21 THR A 225      -1.169  25.882  -6.590  1.00 24.31           H  
ATOM   3568 HG22 THR A 225      -0.174  24.967  -5.774  1.00 24.31           H  
ATOM   3569 HG23 THR A 225      -1.387  25.662  -5.042  1.00 24.31           H  
ATOM   3570  N   ALA A 226       1.231  24.520  -3.352  1.00 13.22           N  
ANISOU 3570  N   ALA A 226     1651   1598   1772   -229    -66   -182       N  
ATOM   3571  CA  ALA A 226       1.906  23.222  -3.357  1.00 13.95           C  
ANISOU 3571  CA  ALA A 226     1763   1674   1864   -248   -158   -147       C  
ATOM   3572  C   ALA A 226       1.543  22.404  -4.590  1.00 10.55           C  
ANISOU 3572  C   ALA A 226     1248   1259   1500   -161   -217   -177       C  
ATOM   3573  O   ALA A 226       0.413  22.459  -5.069  1.00 12.80           O  
ANISOU 3573  O   ALA A 226     1467   1562   1835   -131   -180   -228       O  
ATOM   3574  CB  ALA A 226       1.543  22.412  -2.081  1.00 11.31           C  
ANISOU 3574  CB  ALA A 226     1501   1298   1500   -374   -140   -130       C  
ATOM   3575  H   ALA A 226       0.558  24.572  -2.819  1.00 15.86           H  
ATOM   3576  HA  ALA A 226       2.866  23.363  -3.361  1.00 16.74           H  
ATOM   3577  HB1 ALA A 226       2.002  21.557  -2.109  1.00 13.57           H  
ATOM   3578  HB2 ALA A 226       1.823  22.913  -1.299  1.00 13.57           H  
ATOM   3579  HB3 ALA A 226       0.584  22.272  -2.059  1.00 13.57           H  
ATOM   3580  N   ALA A 227       2.510  21.649  -5.107  1.00 10.20           N  
ANISOU 3580  N   ALA A 227     1202   1216   1458   -115   -314   -154       N  
ATOM   3581  CA  ALA A 227       2.271  20.784  -6.240  1.00 13.12           C  
ANISOU 3581  CA  ALA A 227     1503   1598   1885    -33   -379   -190       C  
ATOM   3582  C   ALA A 227       3.296  19.659  -6.220  1.00 10.29           C  
ANISOU 3582  C   ALA A 227     1177   1211   1522    -22   -485   -166       C  
ATOM   3583  O   ALA A 227       4.043  19.504  -5.249  1.00 10.46           O  
ANISOU 3583  O   ALA A 227     1275   1199   1499    -84   -508   -119       O  
ATOM   3584  CB  ALA A 227       2.346  21.572  -7.555  1.00 17.42           C  
ANISOU 3584  CB  ALA A 227     1972   2208   2437     83   -377   -213       C  
ATOM   3585  H   ALA A 227       3.317  21.626  -4.812  1.00 12.24           H  
ATOM   3586  HA  ALA A 227       1.386  20.393  -6.166  1.00 15.75           H  
ATOM   3587  HB1 ALA A 227       2.182  20.967  -8.295  1.00 20.90           H  
ATOM   3588  HB2 ALA A 227       1.672  22.270  -7.542  1.00 20.90           H  
ATOM   3589  HB3 ALA A 227       3.229  21.965  -7.637  1.00 20.90           H  
ATOM   3590  N   GLY A 228       3.305  18.845  -7.281  1.00 10.81           N  
ANISOU 3590  N   GLY A 228     1186   1287   1634     63   -557   -205       N  
ATOM   3591  CA  GLY A 228       4.332  17.830  -7.406  1.00 15.36           C  
ANISOU 3591  CA  GLY A 228     1783   1840   2213    103   -666   -197       C  
ATOM   3592  C   GLY A 228       3.868  16.453  -6.953  1.00 23.03           C  
ANISOU 3592  C   GLY A 228     2809   2715   3224     51   -724   -202       C  
ATOM   3593  O   GLY A 228       4.639  15.494  -6.927  1.00 18.78           O  
ANISOU 3593  O   GLY A 228     2307   2132   2695     84   -826   -196       O  
ATOM   3594  H   GLY A 228       2.736  18.864  -7.925  1.00 12.97           H  
ATOM   3595  HA2 GLY A 228       4.611  17.769  -8.334  1.00 18.43           H  
ATOM   3596  HA3 GLY A 228       5.101  18.084  -6.873  1.00 18.43           H  
ATOM   3597  N   ILE A 229       2.602  16.373  -6.579  1.00 14.11           N  
ANISOU 3597  N   ILE A 229     1686   1554   2120    -33   -660   -214       N  
ATOM   3598  CA  ILE A 229       1.940  15.099  -6.291  1.00 15.34           C  
ANISOU 3598  CA  ILE A 229     1887   1620   2321   -101   -701   -223       C  
ATOM   3599  C   ILE A 229       0.692  15.059  -7.132  1.00 16.41           C  
ANISOU 3599  C   ILE A 229     1927   1788   2518    -85   -663   -296       C  
ATOM   3600  O   ILE A 229      -0.156  15.951  -7.053  1.00 21.01           O  
ANISOU 3600  O   ILE A 229     2458   2425   3099   -112   -564   -314       O  
ATOM   3601  CB  ILE A 229       1.626  14.973  -4.803  1.00 20.25           C  
ANISOU 3601  CB  ILE A 229     2617   2177   2901   -254   -652   -163       C  
ATOM   3602  CG1 ILE A 229       2.954  14.779  -4.055  1.00 23.03           C  
ANISOU 3602  CG1 ILE A 229     3068   2489   3194   -254   -727    -95       C  
ATOM   3603  CG2 ILE A 229       0.664  13.805  -4.542  1.00 22.91           C  
ANISOU 3603  CG2 ILE A 229     2994   2428   3284   -354   -665   -173       C  
ATOM   3604  CD1 ILE A 229       2.833  14.699  -2.589  1.00 21.87           C  
ANISOU 3604  CD1 ILE A 229     3042   2285   2983   -396   -692    -27       C  
ATOM   3605  H   ILE A 229       2.088  17.056  -6.480  1.00 16.93           H  
ATOM   3606  HA  ILE A 229       2.516  14.364  -6.552  1.00 18.41           H  
ATOM   3607  HB  ILE A 229       1.212  15.796  -4.499  1.00 24.30           H  
ATOM   3608 HG12 ILE A 229       3.364  13.954  -4.361  1.00 27.64           H  
ATOM   3609 HG13 ILE A 229       3.537  15.527  -4.260  1.00 27.64           H  
ATOM   3610 HG21 ILE A 229       0.485  13.751  -3.590  1.00 27.50           H  
ATOM   3611 HG22 ILE A 229      -0.161  13.962  -5.026  1.00 27.50           H  
ATOM   3612 HG23 ILE A 229       1.077  12.983  -4.848  1.00 27.50           H  
ATOM   3613 HD11 ILE A 229       3.716  14.577  -2.206  1.00 26.24           H  
ATOM   3614 HD12 ILE A 229       2.439  15.522  -2.260  1.00 26.24           H  
ATOM   3615 HD13 ILE A 229       2.266  13.946  -2.361  1.00 26.24           H  
ATOM   3616  N   THR A 230       0.612  14.027  -7.963  1.00 19.63           N  
ANISOU 3616  N   THR A 230     2311   2165   2985    -30   -750   -345       N  
ATOM   3617  CA  THR A 230      -0.365  13.952  -9.033  1.00 29.87           C  
ANISOU 3617  CA  THR A 230     3502   3508   4339     18   -743   -427       C  
ATOM   3618  C   THR A 230      -1.766  13.725  -8.525  1.00 31.95           C  
ANISOU 3618  C   THR A 230     3750   3748   4641   -108   -674   -451       C  
ATOM   3619  O   THR A 230      -1.983  12.946  -7.600  1.00 36.23           O  
ANISOU 3619  O   THR A 230     4379   4201   5188   -235   -675   -416       O  
ATOM   3620  CB  THR A 230      -0.003  12.797  -9.976  1.00 37.77           C  
ANISOU 3620  CB  THR A 230     4494   4472   5387    103   -864   -481       C  
ATOM   3621  OG1 THR A 230       1.136  13.183 -10.754  1.00 52.32           O  
ANISOU 3621  OG1 THR A 230     6313   6380   7186    239   -892   -479       O  
ATOM   3622  CG2 THR A 230      -1.168  12.430 -10.910  1.00 32.85           C  
ANISOU 3622  CG2 THR A 230     3779   3875   4830    119   -871   -572       C  
ATOM   3623  H   THR A 230       1.129  13.341  -7.924  1.00 23.56           H  
ATOM   3624  HA  THR A 230      -0.352  14.779  -9.541  1.00 35.84           H  
ATOM   3625  HB  THR A 230       0.222  12.014  -9.449  1.00 45.33           H  
ATOM   3626  HG1 THR A 230       1.786  13.350 -10.248  1.00 62.78           H  
ATOM   3627 HG21 THR A 230      -0.909  11.698 -11.492  1.00 39.43           H  
ATOM   3628 HG22 THR A 230      -1.939  12.159 -10.387  1.00 39.43           H  
ATOM   3629 HG23 THR A 230      -1.410  13.195 -11.454  1.00 39.43           H  
ATOM   3630  N   LEU A 231      -2.708  14.403  -9.167  1.00 39.25           N  
ANISOU 3630  N   LEU A 231     4564   4759   5592    -71   -618   -512       N  
ATOM   3631  CA  LEU A 231      -4.122  14.281  -8.869  1.00 40.15           C  
ANISOU 3631  CA  LEU A 231     4621   4882   5751   -173   -549   -559       C  
ATOM   3632  C   LEU A 231      -4.776  13.248  -9.789  1.00 46.12           C  
ANISOU 3632  C   LEU A 231     5315   5624   6584   -159   -622   -641       C  
ATOM   3633  O   LEU A 231      -4.788  12.052  -9.492  1.00 52.60           O  
ANISOU 3633  O   LEU A 231     6203   6347   7437   -244   -675   -636       O  
ATOM   3634  CB  LEU A 231      -4.779  15.650  -9.051  1.00 37.22           C  
ANISOU 3634  CB  LEU A 231     4156   4616   5369   -123   -457   -589       C  
ATOM   3635  CG  LEU A 231      -6.294  15.754  -8.871  1.00 46.02           C  
ANISOU 3635  CG  LEU A 231     5174   5779   6534   -198   -378   -660       C  
ATOM   3636  CD1 LEU A 231      -6.819  14.891  -7.702  1.00 46.37           C  
ANISOU 3636  CD1 LEU A 231     5275   5756   6586   -392   -329   -642       C  
ATOM   3637  CD2 LEU A 231      -6.668  17.234  -8.695  1.00 46.85           C  
ANISOU 3637  CD2 LEU A 231     5225   5964   6613   -146   -285   -670       C  
ATOM   3638  H   LEU A 231      -2.543  14.960  -9.802  1.00 47.10           H  
ATOM   3639  HA  LEU A 231      -4.240  13.998  -7.949  1.00 48.18           H  
ATOM   3640  HB2 LEU A 231      -4.377  16.260  -8.413  1.00 44.66           H  
ATOM   3641  HB3 LEU A 231      -4.581  15.958  -9.950  1.00 44.66           H  
ATOM   3642  HG  LEU A 231      -6.724  15.439  -9.681  1.00 55.23           H  
ATOM   3643 HD11 LEU A 231      -7.781  14.998  -7.638  1.00 55.64           H  
ATOM   3644 HD12 LEU A 231      -6.599  13.962  -7.874  1.00 55.64           H  
ATOM   3645 HD13 LEU A 231      -6.397  15.184  -6.879  1.00 55.64           H  
ATOM   3646 HD21 LEU A 231      -7.628  17.305  -8.580  1.00 56.22           H  
ATOM   3647 HD22 LEU A 231      -6.214  17.583  -7.913  1.00 56.22           H  
ATOM   3648 HD23 LEU A 231      -6.392  17.724  -9.485  1.00 56.22           H  
TER    3649      LEU A 231                                                      
HETATM 3650  O   HOH A 301      16.109  35.961   2.353  1.00 13.96           O  
HETATM 3651  O   HOH A 302       8.126  29.114   7.029  1.00 13.38           O  
HETATM 3652  O   HOH A 303       8.473  34.452  -5.601  1.00 13.09           O  
HETATM 3653  O   HOH A 304      10.775  31.631   9.097  1.00 12.25           O  
HETATM 3654  O   HOH A 305      -4.928  31.430   6.331  1.00 14.29           O  
HETATM 3655  O   HOH A 306      16.385  32.304   5.352  1.00 11.56           O  
HETATM 3656  O   HOH A 307       5.189  20.177   3.855  1.00 11.63           O  
HETATM 3657  O   HOH A 308       6.194  32.265   3.178  1.00 16.11           O  
HETATM 3658  O   HOH A 309      16.356  47.181  -2.364  1.00 14.97           O  
HETATM 3659  O   HOH A 310      15.116  36.430  -1.081  1.00 13.91           O  
HETATM 3660  O   HOH A 311       5.272  21.705  16.943  1.00 20.08           O  
HETATM 3661  O   HOH A 312      13.116  10.994   6.040  1.00 14.86           O  
HETATM 3662  O   HOH A 313       8.353  42.688  -8.098  1.00 18.49           O  
HETATM 3663  O   HOH A 314      15.261  30.973   8.676  1.00 19.18           O  
HETATM 3664  O   HOH A 315      13.035  32.228   7.646  1.00 12.84           O  
HETATM 3665  O   HOH A 316      13.731  36.867  -7.210  1.00 14.30           O  
HETATM 3666  O   HOH A 317       9.761  12.825   1.621  1.00 15.51           O  
HETATM 3667  O   HOH A 318      14.554  39.598  -9.940  1.00 21.63           O  
HETATM 3668  O   HOH A 319      -1.402  20.425   7.929  1.00 16.37           O  
HETATM 3669  O   HOH A 320      -3.182  19.467   6.309  1.00 19.89           O  
HETATM 3670  O   HOH A 321      20.034  46.500  -4.849  1.00 23.37           O  
HETATM 3671  O   HOH A 322      -6.081  31.119  13.643  1.00 18.53           O  
HETATM 3672  O   HOH A 323      -3.734  24.895   2.364  1.00 21.28           O  
HETATM 3673  O   HOH A 324      17.429  35.329  -1.519  1.00 18.08           O  
HETATM 3674  O   HOH A 325      -7.962  31.194  10.238  1.00 21.36           O  
HETATM 3675  O   HOH A 326      28.129  31.653  -0.902  1.00 23.47           O  
HETATM 3676  O   HOH A 327      -7.528  30.794   4.420  1.00 24.02           O  
HETATM 3677  O   HOH A 328      16.826  41.559  -7.913  1.00 19.08           O  
HETATM 3678  O   HOH A 329       3.451  44.516  -3.793  1.00 19.13           O  
HETATM 3679  O   HOH A 330      -1.697  19.478  13.713  1.00 27.39           O  
HETATM 3680  O   HOH A 331      -6.980  18.334  -4.978  1.00 21.76           O  
HETATM 3681  O   HOH A 332      14.568  25.915  -7.101  1.00 17.77           O  
HETATM 3682  O   HOH A 333      16.066  32.620  16.324  1.00 30.32           O  
HETATM 3683  O   HOH A 334      15.078  39.755  -6.899  1.00 17.53           O  
HETATM 3684  O   HOH A 335      19.809  49.945   9.481  1.00 26.78           O  
HETATM 3685  O   HOH A 336       8.254  10.773  -1.468  1.00 19.25           O  
HETATM 3686  O   HOH A 337       9.946  15.880  -6.140  1.00 22.36           O  
HETATM 3687  O   HOH A 338      -2.166  42.553  10.542  1.00 27.35           O  
HETATM 3688  O   HOH A 339      15.806  11.381   8.626  1.00 21.45           O  
HETATM 3689  O   HOH A 340      28.145  41.892  -1.918  1.00 26.80           O  
HETATM 3690  O   HOH A 341      14.343  49.709  -2.321  1.00 25.75           O  
HETATM 3691  O   HOH A 342      18.439  21.394   3.165  1.00 31.79           O  
HETATM 3692  O   HOH A 343      -3.208  38.130   2.149  1.00 23.03           O  
HETATM 3693  O   HOH A 344       9.387  11.263  13.317  1.00 25.71           O  
HETATM 3694  O   HOH A 345      26.574  33.505   7.666  1.00 21.15           O  
HETATM 3695  O   HOH A 346      17.754  38.720  18.381  1.00 22.94           O  
HETATM 3696  O   HOH A 347       0.024  43.393  -7.655  1.00 26.29           O  
HETATM 3697  O   HOH A 348      -5.901  33.644  13.486  1.00 20.15           O  
HETATM 3698  O   HOH A 349      -2.185  43.430   4.962  1.00 39.40           O  
HETATM 3699  O   HOH A 350       6.368  12.437  -4.573  1.00 20.74           O  
HETATM 3700  O   HOH A 351      10.918  17.254  -3.526  1.00 26.35           O  
HETATM 3701  O   HOH A 352      19.200  48.199  -2.583  1.00 28.85           O  
HETATM 3702  O   HOH A 353      18.096  19.870   0.908  1.00 24.42           O  
HETATM 3703  O   HOH A 354      11.822  21.911 -12.343  1.00 21.57           O  
HETATM 3704  O   HOH A 355       6.183  38.366  21.683  1.00 24.62           O  
HETATM 3705  O   HOH A 356       1.840  48.539  -3.217  1.00 33.22           O  
HETATM 3706  O   HOH A 357      12.557  51.987   0.715  1.00 23.55           O  
HETATM 3707  O   HOH A 358      15.204  23.368  12.131  1.00 24.06           O  
HETATM 3708  O   HOH A 359       6.952  28.357  -9.664  1.00 28.42           O  
HETATM 3709  O   HOH A 360      26.394  48.010  12.417  1.00 24.10           O  
HETATM 3710  O   HOH A 361      16.204  50.200  -0.046  1.00 35.65           O  
HETATM 3711  O   HOH A 362       6.351  43.539  13.415  1.00 26.40           O  
HETATM 3712  O   HOH A 363      34.420  33.610   7.504  1.00 28.90           O  
HETATM 3713  O   HOH A 364       1.162  20.368  16.159  1.00 32.01           O  
HETATM 3714  O   HOH A 365      -0.347  41.843  12.397  1.00 22.41           O  
HETATM 3715  O   HOH A 366     -11.179  35.345   7.805  1.00 41.19           O  
HETATM 3716  O   HOH A 367      29.751  32.155   0.982  1.00 29.74           O  
HETATM 3717  O   HOH A 368      24.840  24.486  -3.800  1.00 33.28           O  
HETATM 3718  O   HOH A 369       7.440  36.621  -9.220  1.00 21.44           O  
HETATM 3719  O   HOH A 370       1.262  44.542  -5.359  1.00 29.09           O  
HETATM 3720  O   HOH A 371      -5.633  38.385   2.912  1.00 31.46           O  
HETATM 3721  O   HOH A 372      15.160  48.400  -9.468  1.00 29.82           O  
HETATM 3722  O   HOH A 373       3.086  37.544  -9.336  1.00 32.88           O  
HETATM 3723  O   HOH A 374       6.664  31.514   0.715  1.00 32.87           O  
HETATM 3724  O   HOH A 375      27.662  29.031  -5.063  1.00 36.45           O  
HETATM 3725  O   HOH A 376       0.787  43.761   0.099  1.00 27.97           O  
HETATM 3726  O   HOH A 377       4.255  10.789  -3.890  1.00 37.06           O  
HETATM 3727  O   HOH A 378      -8.039  21.684  -3.447  1.00 31.45           O  
HETATM 3728  O   HOH A 379      12.864  22.403  17.020  1.00 34.28           O  
HETATM 3729  O   HOH A 380       0.094  44.963   4.974  1.00 44.64           O  
HETATM 3730  O   HOH A 381       6.407  57.591   6.894  1.00 33.26           O  
HETATM 3731  O   HOH A 382      -1.343  31.071  21.675  1.00 25.33           O  
HETATM 3732  O   HOH A 383      13.269  27.770  -8.581  1.00 27.74           O  
HETATM 3733  O   HOH A 384      -9.527  29.409  11.897  1.00 36.57           O  
HETATM 3734  O   HOH A 385      -0.123  18.683  -7.960  1.00 29.69           O  
HETATM 3735  O   HOH A 386       6.667  10.370   5.043  1.00 33.14           O  
HETATM 3736  O   HOH A 387      14.493  19.053  -0.296  1.00 25.20           O  
HETATM 3737  O   HOH A 388      -0.548  23.398  -9.136  1.00 30.45           O  
HETATM 3738  O   HOH A 389     -12.154  30.512   9.216  1.00 37.19           O  
HETATM 3739  O   HOH A 390       7.532  16.484  -6.776  1.00 28.87           O  
HETATM 3740  O   HOH A 391       9.186  47.189  15.746  1.00 38.04           O  
HETATM 3741  O   HOH A 392      22.462  38.624  13.975  1.00 38.23           O  
HETATM 3742  O   HOH A 393       5.680  50.632  -6.054  1.00 30.69           O  
HETATM 3743  O   HOH A 394      18.439  25.897  16.308  1.00 40.17           O  
HETATM 3744  O   HOH A 395      24.313  25.339  -7.068  1.00 35.20           O  
HETATM 3745  O   HOH A 396      -3.927  41.742  14.869  1.00 34.70           O  
HETATM 3746  O   HOH A 397      -1.464  40.838  15.209  1.00 32.29           O  
HETATM 3747  O   HOH A 398      27.759  32.412  10.159  1.00 27.67           O  
HETATM 3748  O   HOH A 399      25.229  29.863  -4.938  1.00 28.08           O  
HETATM 3749  O   HOH A 400      -6.386  25.297   5.957  1.00 38.93           O  
HETATM 3750  O   HOH A 401      -7.747  37.462   1.609  1.00 28.26           O  
HETATM 3751  O   HOH A 402       8.854  45.740  -8.376  1.00 34.24           O  
HETATM 3752  O   HOH A 403       5.993  47.615  -8.104  1.00 39.84           O  
HETATM 3753  O   HOH A 404      27.691  39.476  -5.757  1.00 32.46           O  
HETATM 3754  O   HOH A 405       0.165  17.948  16.582  1.00 36.20           O  
HETATM 3755  O   HOH A 406      12.705  45.977  13.791  1.00 32.30           O  
HETATM 3756  O   HOH A 407      -0.114  44.362  13.169  1.00 43.09           O  
HETATM 3757  O   HOH A 408      29.720  44.977  13.838  1.00 41.32           O  
HETATM 3758  O   HOH A 409      28.408  48.735  10.643  1.00 45.07           O  
HETATM 3759  O   HOH A 410      13.678  23.643 -10.704  1.00 45.45           O  
HETATM 3760  O   HOH A 411      21.298  53.935   8.502  1.00 35.33           O  
HETATM 3761  O   HOH A 412      -1.625  45.000   9.292  1.00 42.19           O  
HETATM 3762  O   HOH A 413      11.217   9.504   4.949  1.00 19.36           O  
HETATM 3763  O   HOH A 414       7.902  29.167  -0.335  1.00 26.22           O  
HETATM 3764  O   HOH A 415      -0.278  11.239  -1.719  1.00 30.85           O  
HETATM 3765  O   HOH A 416       7.245   9.828   3.001  1.00 45.11           O  
HETATM 3766  O   HOH A 417      15.727  28.570 -10.388  1.00 34.32           O  
HETATM 3767  O   HOH A 418       0.847  30.405  23.734  1.00 29.68           O  
HETATM 3768  O   HOH A 419       3.676  31.012   2.267  1.00 33.06           O  
HETATM 3769  O   HOH A 420      -0.110  44.634  -2.494  1.00 45.59           O  
HETATM 3770  O   HOH A 421      31.744  32.367   4.664  1.00 39.39           O  
HETATM 3771  O   HOH A 422       1.422  32.365   0.959  1.00 30.44           O  
HETATM 3772  O   HOH A 423      28.363  39.239  10.231  1.00 32.15           O  
HETATM 3773  O   HOH A 424      29.057  30.871  -2.866  1.00 29.47           O  
HETATM 3774  O   HOH A 425      -2.308  43.006  -7.624  1.00 39.20           O  
HETATM 3775  O   HOH A 426       5.042  30.278  -9.625  1.00 30.24           O  
HETATM 3776  O   HOH A 427       2.185  10.699  -2.621  1.00 39.82           O  
HETATM 3777  O   HOH A 428      -7.760  26.201  -1.115  1.00 37.98           O  
HETATM 3778  O   HOH A 429      19.045  50.552   1.456  1.00 43.46           O  
HETATM 3779  O   HOH A 430      14.323  50.642  -4.704  1.00 35.86           O  
HETATM 3780  O   HOH A 431      28.704  45.684  16.238  1.00 34.46           O  
HETATM 3781  O   HOH A 432       0.702  45.430   2.504  1.00 34.56           O  
HETATM 3782  O   HOH A 433       8.142  49.709  -6.614  1.00 43.16           O  
HETATM 3783  O   HOH A 434      -3.013  43.345   7.334  1.00 44.70           O  
HETATM 3784  O   HOH A 435       3.746  19.774  17.171  1.00 43.44           O  
HETATM 3785  O   HOH A 436      -8.811  33.658  10.524  1.00 40.11           O  
HETATM 3786  O   HOH A 437      16.609   7.093   9.753  1.00 42.27           O  
HETATM 3787  O   HOH A 438       7.442  40.199  -9.683  1.00 38.41           O  
HETATM 3788  O   HOH A 439      29.709  33.450  11.711  1.00 44.23           O  
HETATM 3789  O   HOH A 440      -6.104  40.261   9.578  1.00 39.15           O  
HETATM 3790  O   HOH A 441       8.970   9.884   6.468  1.00 35.58           O  
HETATM 3791  O   HOH A 442      12.809  23.910  19.458  1.00 33.02           O  
HETATM 3792  O   HOH A 443      -5.715  14.500   1.201  1.00 37.85           O  
HETATM 3793  O   HOH A 444      -5.053  26.481  18.956  1.00 37.39           O  
HETATM 3794  O   HOH A 445       2.662  48.531   8.325  1.00 38.48           O  
HETATM 3795  O   HOH A 446      25.999  32.120  12.039  1.00 33.19           O  
HETATM 3796  O   HOH A 447      20.142  21.276   4.645  1.00 37.33           O  
HETATM 3797  O   HOH A 448      35.563  37.367   2.666  1.00 47.47           O  
HETATM 3798  O   HOH A 449      13.149  26.400  20.051  1.00 40.56           O  
HETATM 3799  O   HOH A 450      -8.579  30.063  14.213  1.00 38.58           O  
HETATM 3800  O   HOH A 451      29.282  41.435  13.988  1.00 36.18           O  
HETATM 3801  O   HOH A 452      16.560  24.044  -7.285  1.00 40.05           O  
HETATM 3802  O   HOH A 453      16.585  46.492  -5.045  1.00 33.85           O  
HETATM 3803  O   HOH A 454      27.181  35.373  -9.596  1.00 36.07           O  
HETATM 3804  O   HOH A 455      14.475  53.336   7.412  1.00 37.57           O  
HETATM 3805  O   HOH A 456       5.335  47.415   8.745  1.00 31.30           O  
HETATM 3806  O   HOH A 457      18.036  48.440   0.218  1.00 36.95           O  
HETATM 3807  O   HOH A 458      16.540  18.043   1.035  1.00 33.95           O  
HETATM 3808  O   HOH A 459      -4.273  28.891  18.404  1.00 41.53           O  
HETATM 3809  O   HOH A 460      27.326  43.262 -10.939  1.00 38.78           O  
HETATM 3810  O   HOH A 461      -8.429  37.713  13.414  1.00 45.86           O  
HETATM 3811  O   HOH A 462      11.282  22.621  21.115  1.00 33.00           O  
HETATM 3812  O   HOH A 463       0.878  48.196   2.454  1.00 42.75           O  
HETATM 3813  O   HOH A 464      -7.974  35.118  13.194  1.00 47.30           O  
HETATM 3814  O   HOH A 465      22.028  40.861  15.063  1.00 43.96           O  
HETATM 3815  O   HOH A 466      -5.123  30.954  16.408  1.00 38.64           O  
HETATM 3816  O   HOH A 467      -4.589  31.758  -5.520  1.00 27.92           O  
HETATM 3817  O   HOH A 468      33.013  35.996  -0.988  1.00 43.74           O  
HETATM 3818  O   HOH A 469      16.656  24.496  17.243  1.00 54.22           O  
HETATM 3819  O   HOH A 470      12.897  43.078  15.244  1.00 30.73           O  
HETATM 3820  O   HOH A 471      15.055  18.939   9.562  1.00 30.85           O  
HETATM 3821  O   HOH A 472      13.339   4.058   9.695  1.00 50.77           O  
HETATM 3822  O   HOH A 473       7.747  29.054  21.177  1.00 42.97           O  
HETATM 3823  O   HOH A 474       3.337  11.721   8.580  1.00 41.98           O  
HETATM 3824  O   HOH A 475      18.126  23.704  -4.842  1.00 36.02           O  
HETATM 3825  O   HOH A 476      -2.652  12.194  -2.717  1.00 42.79           O  
HETATM 3826  O   HOH A 477      17.372  22.834  14.986  1.00 49.56           O  
HETATM 3827  O   HOH A 478       2.498  30.631  22.031  1.00 43.08           O  
HETATM 3828  O   HOH A 479       1.568  25.233   4.387  1.00 10.65           O  
HETATM 3829  O   HOH A 480      24.934  34.540  -9.973  1.00 24.30           O  
HETATM 3830  O   HOH A 481      14.211  33.673  16.999  1.00 31.69           O  
HETATM 3831  O   HOH A 482      -3.570  32.017  23.499  1.00 31.91           O  
HETATM 3832  O   HOH A 483       1.608  12.152   5.566  1.00 31.76           O  
HETATM 3833  O   HOH A 484       5.048  51.662  12.029  1.00 40.34           O  
HETATM 3834  O   HOH A 485      12.626  25.843 -11.726  1.00 43.88           O  
HETATM 3835  O   HOH A 486       8.565  28.920 -11.766  1.00 33.04           O  
HETATM 3836  O   HOH A 487      14.228  25.869  -9.907  1.00 35.68           O  
HETATM 3837  O   HOH A 488      23.836  48.512   8.838  1.00 26.41           O  
HETATM 3838  O   HOH A 489      26.076  49.952   8.665  1.00 38.32           O  
HETATM 3839  O   HOH A 490      22.701  50.585   7.446  1.00 43.53           O  
HETATM 3840  O   HOH A 491       8.973  19.330 -10.968  1.00 36.49           O  
HETATM 3841  O   HOH A 492      22.071  24.844   6.276  1.00 51.24           O  
HETATM 3842  O   HOH A 493       7.054  48.311  14.125  1.00 37.90           O  
HETATM 3843  O   HOH A 494      15.637  34.724 -14.264  1.00 38.56           O  
HETATM 3844  O   HOH A 495      -1.756  11.378   6.941  1.00 42.29           O  
HETATM 3845  O   HOH A 496      11.605  19.437 -11.301  1.00 45.19           O  
HETATM 3846  O   HOH A 497      17.811  33.485 -14.890  1.00 42.95           O  
HETATM 3847  O   HOH A 498      15.339  17.301  -1.997  1.00 41.79           O  
HETATM 3848  O   HOH A 499      26.846  39.917 -11.448  1.00 46.47           O  
HETATM 3849  O   HOH A 500      18.981  50.358  -3.698  1.00 42.85           O  
HETATM 3850  O   HOH A 501      17.309  43.480 -16.097  1.00 38.52           O  
HETATM 3851  O   HOH A 502       2.641  51.104   7.991  1.00 38.65           O  
HETATM 3852  O   HOH A 503      23.878  50.492   2.587  1.00 37.75           O  
HETATM 3853  O   HOH A 504      -6.358  29.766  -5.180  1.00 47.79           O  
HETATM 3854  O   HOH A 505      13.610  18.426 -10.147  1.00 45.15           O  
HETATM 3855  O   HOH A 506       4.578  19.976  23.046  1.00 46.91           O  
HETATM 3856  O   HOH A 507      26.054  48.060   2.002  1.00 48.69           O  
HETATM 3857  O   HOH A 508      19.552  31.538 -14.059  1.00 46.01           O  
HETATM 3858  O   HOH A 509      -7.322  26.995   4.404  1.00 43.96           O  
HETATM 3859  O   HOH A 510      -0.513  13.625  12.477  1.00 42.96           O  
HETATM 3860  O   HOH A 511      -9.175  16.778  -5.052  1.00 43.93           O  
HETATM 3861  O   HOH A 512       6.542  36.976 -11.686  1.00 40.78           O  
HETATM 3862  O   HOH A 513      -0.589  16.199  12.501  1.00 48.92           O  
HETATM 3863  O   HOH A 514      -2.407  21.376  16.433  1.00 33.94           O  
HETATM 3864  O   HOH A 515      30.608  48.809  11.596  1.00 49.83           O  
HETATM 3865  O   HOH A 516      23.826  49.580  12.514  1.00 39.87           O  
HETATM 3866  O   HOH A 517      17.982  27.980 -11.547  1.00 47.77           O  
HETATM 3867  O   HOH A 518      21.263  28.050  12.694  1.00 50.42           O  
HETATM 3868  O   HOH A 519      34.100  35.787   8.464  1.00 48.88           O  
HETATM 3869  O   HOH A 520      23.761  36.033 -15.365  1.00 40.05           O  
HETATM 3870  O   HOH A 521      15.805   3.602  10.499  1.00 54.00           O  
HETATM 3871  O   HOH A 522       6.760  59.548   1.417  1.00 46.91           O  
HETATM 3872  O   HOH A 523      -1.121  21.688  -7.220  1.00 22.96           O  
HETATM 3873  O   HOH A 524       2.338  12.003  -7.509  1.00 33.26           O  
HETATM 3874  O   HOH A 525      20.559  28.296 -12.813  1.00 39.76           O  
HETATM 3875  O   HOH A 526      -3.429  27.888  -6.783  1.00 50.39           O  
HETATM 3876  O   HOH A 527      -7.001  24.112  -2.013  1.00 50.30           O  
HETATM 3877  O   HOH A 528      24.425  50.815   5.072  1.00 37.94           O  
HETATM 3878  O   HOH A 529      18.557  40.957 -15.020  1.00 45.61           O  
HETATM 3879  O   HOH A 530      -8.133  38.007  10.648  1.00 38.65           O  
HETATM 3880  O   HOH A 531      34.514  40.013   2.980  1.00 50.69           O  
HETATM 3881  O   HOH A 532       7.679  55.825  -0.462  1.00 49.44           O  
HETATM 3882  O   HOH A 533       0.636  41.062  -8.721  1.00 26.58           O  
HETATM 3883  O   HOH A 534      -2.556  24.892  -9.377  1.00 28.17           O  
HETATM 3884  O   HOH A 535      21.193  28.586  10.425  1.00 32.20           O  
HETATM 3885  O   HOH A 536      19.758  25.191  -3.944  1.00 45.88           O  
HETATM 3886  O   HOH A 537      31.375  46.337   3.991  1.00 40.06           O  
HETATM 3887  O   HOH A 538      32.515  45.285  10.510  1.00 50.15           O  
HETATM 3888  O   HOH A 539      -2.803  29.844  19.714  1.00 45.26           O  
HETATM 3889  O   HOH A 540      29.936  31.030  -5.205  1.00 45.67           O  
HETATM 3890  O   HOH A 541       5.688  46.370  11.507  1.00 46.50           O  
HETATM 3891  O   HOH A 542     -10.578  35.243   2.061  1.00 47.98           O  
HETATM 3892  O   HOH A 543       2.778  61.195   1.595  1.00 55.00           O  
HETATM 3893  O   HOH A 544       3.350  39.778 -10.200  1.00 46.61           O  
HETATM 3894  O   HOH A 545       3.304  51.568  10.036  1.00 54.60           O  
HETATM 3895  O   HOH A 546      18.688  16.789   9.357  1.00 43.85           O  
HETATM 3896  O   HOH A 547      23.323  34.026 -14.220  1.00 53.49           O  
HETATM 3897  O   HOH A 548       1.988   8.015   0.572  1.00 49.21           O  
HETATM 3898  O   HOH A 549      16.368  20.154  11.125  1.00 58.56           O  
HETATM 3899  O   HOH A 550     -11.758  18.437  -3.562  1.00 48.47           O  
HETATM 3900  O   HOH A 551      -6.461  14.114   3.347  1.00 60.09           O  
HETATM 3901  O   HOH A 552       4.239  10.569   3.630  1.00 50.88           O  
HETATM 3902  O   HOH A 553      10.271  50.981  -6.588  1.00 47.68           O  
HETATM 3903  O   HOH A 554      12.428  50.948  -5.939  1.00 47.14           O  
HETATM 3904  O   HOH A 555      15.044  37.058 -14.884  1.00 45.17           O  
HETATM 3905  O   HOH A 556      -1.742  28.501  21.171  1.00 43.82           O  
HETATM 3906  O   HOH A 557       1.343  12.448  11.831  1.00 47.02           O  
HETATM 3907  O   HOH A 558       1.558  28.611  20.295  1.00 47.38           O  
HETATM 3908  O   HOH A 559       1.204  38.903  -8.294  1.00 47.86           O  
HETATM 3909  O   HOH A 560       3.060  27.722  22.147  1.00 48.45           O  
HETATM 3910  O   HOH A 561       0.607  47.486   6.778  1.00 45.73           O  
HETATM 3911  O   HOH A 562      13.736  43.909 -15.190  1.00 50.29           O  
HETATM 3912  O   HOH A 563      21.774  31.665 -14.651  1.00 48.62           O  
HETATM 3913  O   HOH A 564      27.540  41.354 -13.553  1.00 50.28           O  
HETATM 3914  O   HOH A 565       1.577  10.345   3.360  1.00 57.14           O  
HETATM 3915  O   HOH A 566       0.545  26.888  21.447  1.00 44.79           O  
HETATM 3916  O   HOH A 567      22.179  27.124   9.013  1.00 44.39           O  
HETATM 3917  O   HOH A 568      30.933  46.601   9.105  1.00 58.26           O  
HETATM 3918  O   HOH A 569      14.098  55.247   1.519  1.00 52.33           O  
HETATM 3919  O   HOH A 570       7.256  51.538  13.671  1.00 41.33           O  
HETATM 3920  O   HOH A 571      10.472  40.470 -12.056  1.00 40.56           O  
HETATM 3921  O   HOH A 572       6.308   9.148  -3.016  1.00 43.86           O  
HETATM 3922  O   HOH A 573      31.432  49.249   9.583  1.00 56.70           O  
HETATM 3923  O   HOH A 574      -4.531  42.021  10.626  1.00 50.52           O  
HETATM 3924  O   HOH A 575      17.088  48.547  -5.947  1.00 53.23           O  
HETATM 3925  O   HOH A 576      12.334  39.277 -12.017  1.00 43.21           O  
HETATM 3926  O   HOH A 577      14.046  53.779  -0.512  1.00 57.31           O  
HETATM 3927  O   HOH A 578      32.611  44.353   4.536  1.00 56.03           O  
HETATM 3928  O   HOH A 579      -7.077  24.854   1.028  1.00 48.13           O  
HETATM 3929  O   HOH A 580      -2.041  11.113  -5.885  1.00 48.03           O  
HETATM 3930  O   HOH A 581     -11.017  27.276  13.176  1.00 53.67           O  
HETATM 3931  O   HOH A 582     -11.744  37.885   7.361  1.00 55.43           O  
HETATM 3932  O   HOH A 583     -10.006  38.479   2.477  1.00 47.42           O  
HETATM 3933  O   HOH A 584      32.540  38.308   6.847  1.00 49.77           O  
HETATM 3934  O   HOH A 585       5.306  12.623  13.526  1.00 29.43           O  
HETATM 3935  O   HOH A 586      -3.803  20.861  -8.119  1.00 35.40           O  
HETATM 3936  O   HOH A 587      -7.852  21.113  -5.674  1.00 38.38           O  
HETATM 3937  O   HOH A 588       5.467  24.511  22.351  1.00 38.44           O  
HETATM 3938  O   HOH A 589      -5.292  23.368   4.498  1.00 35.79           O  
HETATM 3939  O   HOH A 590       5.525  27.164  20.864  1.00 28.83           O  
HETATM 3940  O   HOH A 591       9.673  10.153   2.623  1.00 29.24           O  
HETATM 3941  O   HOH A 592       1.758  22.449 -11.067  1.00 32.43           O  
HETATM 3942  O   HOH A 593       9.352  51.695  14.799  1.00 48.40           O  
HETATM 3943  O   HOH A 594      13.924  30.699  21.391  1.00 36.69           O  
HETATM 3944  O   HOH A 595      -6.572  19.374   7.255  1.00 41.16           O  
HETATM 3945  O   HOH A 596       7.010  16.779  17.469  1.00 38.67           O  
HETATM 3946  O   HOH A 597      16.943  38.935 -16.242  1.00 51.85           O  
HETATM 3947  O   HOH A 598      -6.979  41.259  13.536  1.00 48.11           O  
HETATM 3948  O   HOH A 599      11.541  49.998  -9.050  1.00 49.26           O  
HETATM 3949  O   HOH A 600     -11.878  33.990  10.136  1.00 46.44           O  
HETATM 3950  O   HOH A 601      -6.822  17.137   7.018  1.00 53.44           O  
HETATM 3951  O   HOH A 602      19.274  37.480 -18.007  1.00 47.85           O  
HETATM 3952  O   HOH A 603      34.798  38.614   5.740  1.00 52.75           O  
CONECT  939  956                                                                
CONECT  956  939  957                                                           
CONECT  957  956  958  961                                                      
CONECT  958  957  959  960                                                      
CONECT  959  958                                                                
CONECT  960  958                                                                
CONECT  961  957  962  963                                                      
CONECT  962  961  966                                                           
CONECT  963  961  964  967                                                      
CONECT  964  963  965  966                                                      
CONECT  965  964                                                                
CONECT  966  962  964  970                                                      
CONECT  967  963  968                                                           
CONECT  968  967  969  978                                                      
CONECT  969  968                                                                
CONECT  970  966  971                                                           
CONECT  971  970  972  973                                                      
CONECT  972  971  974                                                           
CONECT  973  971  975                                                           
CONECT  974  972  976                                                           
CONECT  975  973  976                                                           
CONECT  976  974  975  977                                                      
CONECT  977  976                                                                
CONECT  978  968                                                                
MASTER      419    0    1    6   12    0    0    6 2098    1   24   19          
END



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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.