CNRS Nantes University UFIP UFIP
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***  6pvg  ***

elNémo ID: 2001272159519472

Job options:

ID        	=	 2001272159519472
JOBID     	=	 6pvg
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER 6pvg

HEADER    BIOSYNTHETIC PROTEIN                    20-JUL-19   6PVG              
TITLE     CRYSTAL STRUCTURE OF LIGAND FREE PHQK                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: FAD MONOOXYGENASE;                                         
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PENICILLIUM FELLUTANUM;                         
SOURCE   3 ORGANISM_TAXID: 70095;                                               
SOURCE   4 GENE: PHQK;                                                          
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PKLD116                                   
KEYWDS    MONOOXYGENASE, FLAVIN, BIOSYNTHETIC PROTEIN                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.E.FRALEY,J.L.SMITH,D.H.SHERMAN                                      
REVDAT   1   22-JAN-20 6PVG    0                                                
JRNL        AUTH   A.FRALEY,K.CADDELL HAATVEIT,Y.YE,S.P.KELLY,S.A.NEWMISTER,    
JRNL        AUTH 2 F.YU,R.M.WILLIAMS,J.L.SMITH,K.N.HOUK,D.H.SHERMAN             
JRNL        TITL   MOLECULAR BASIS FOR SPIROCYCLE FORMATION IN THE              
JRNL        TITL 2 PARAHERQUAMIDE BIOSYNTHETIC PATHWAY.                         
JRNL        REF    J.AM.CHEM.SOC.                             2020              
JRNL        REFN                   ESSN 1520-5126                               
JRNL        PMID   31904957                                                     
JRNL        DOI    10.1021/JACS.9B09070                                         
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.71 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX                                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.71                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.88                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 96541                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.164                           
REMARK   3   R VALUE            (WORKING SET) : 0.162                           
REMARK   3   FREE R VALUE                     : 0.192                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.960                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3820                            
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 47.8750 -  5.1264    1.00     3474   149  0.1344 0.1442        
REMARK   3     2  5.1264 -  4.0697    1.00     3479   150  0.1181 0.1377        
REMARK   3     3  4.0697 -  3.5554    1.00     3498   139  0.1310 0.1527        
REMARK   3     4  3.5554 -  3.2304    1.00     3480   144  0.1453 0.1555        
REMARK   3     5  3.2304 -  2.9989    1.00     3468   147  0.1639 0.1930        
REMARK   3     6  2.9989 -  2.8221    1.00     3508   140  0.1659 0.1641        
REMARK   3     7  2.8221 -  2.6808    1.00     3492   144  0.1793 0.2401        
REMARK   3     8  2.6808 -  2.5641    1.00     3482   150  0.1786 0.2332        
REMARK   3     9  2.5641 -  2.4654    1.00     3476   145  0.1808 0.2188        
REMARK   3    10  2.4654 -  2.3803    1.00     3477   141  0.1731 0.2782        
REMARK   3    11  2.3803 -  2.3059    1.00     3483   136  0.1712 0.2483        
REMARK   3    12  2.3059 -  2.2400    1.00     3496   145  0.1728 0.2155        
REMARK   3    13  2.2400 -  2.1810    1.00     3484   144  0.1711 0.2499        
REMARK   3    14  2.1810 -  2.1278    1.00     3491   143  0.1685 0.1795        
REMARK   3    15  2.1278 -  2.0794    1.00     3440   144  0.1682 0.1877        
REMARK   3    16  2.0794 -  2.0352    1.00     3530   143  0.1720 0.2234        
REMARK   3    17  2.0352 -  1.9945    1.00     3433   145  0.1744 0.2129        
REMARK   3    18  1.9945 -  1.9568    1.00     3519   147  0.2048 0.2319        
REMARK   3    19  1.9568 -  1.9219    1.00     3449   139  0.2082 0.2260        
REMARK   3    20  1.9219 -  1.8893    0.99     3472   143  0.2049 0.2565        
REMARK   3    21  1.8893 -  1.8588    0.99     3447   143  0.2077 0.2364        
REMARK   3    22  1.8588 -  1.8302    0.99     3421   143  0.2228 0.2574        
REMARK   3    23  1.8302 -  1.8033    0.97     3467   138  0.2374 0.2768        
REMARK   3    24  1.8033 -  1.7779    0.96     3324   136  0.2653 0.3132        
REMARK   3    25  1.7779 -  1.7539    0.96     3349   133  0.2974 0.3230        
REMARK   3    26  1.7539 -  1.7311    0.93     3259   137  0.3348 0.3336        
REMARK   3    27  1.7311 -  1.7095    0.82     2823   112  0.4063 0.4246        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.230            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.710           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 37.52                          
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      :   NULL           NULL                                  
REMARK   3   ANGLE     :   NULL           NULL                                  
REMARK   3   CHIRALITY :   NULL           NULL                                  
REMARK   3   PLANARITY :   NULL           NULL                                  
REMARK   3   DIHEDRAL  :   NULL           NULL                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 7                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 4 THROUGH 37 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  20.0753  29.7237  15.5092              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2431 T22:   0.2214                                     
REMARK   3      T33:   0.2628 T12:  -0.0373                                     
REMARK   3      T13:   0.0221 T23:   0.0098                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.5080 L22:   2.4938                                     
REMARK   3      L33:   3.2966 L12:  -0.7070                                     
REMARK   3      L13:   0.4748 L23:   1.2289                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0469 S12:   0.2433 S13:   0.5588                       
REMARK   3      S21:  -0.2130 S22:   0.1408 S23:  -0.2729                       
REMARK   3      S31:  -0.4183 S32:   0.2072 S33:  -0.1118                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 38 THROUGH 149 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  14.9877  19.9132  29.1433              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2099 T22:   0.2220                                     
REMARK   3      T33:   0.2108 T12:  -0.0077                                     
REMARK   3      T13:  -0.0058 T23:  -0.0234                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5658 L22:   1.1798                                     
REMARK   3      L33:   1.1372 L12:   0.0284                                     
REMARK   3      L13:  -0.1860 L23:  -0.9646                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0256 S12:  -0.0305 S13:   0.0089                       
REMARK   3      S21:   0.1537 S22:  -0.0966 S23:  -0.0542                       
REMARK   3      S31:  -0.0866 S32:   0.0917 S33:   0.1024                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 150 THROUGH 187 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  11.7428  17.2625   8.0472              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2838 T22:   0.2924                                     
REMARK   3      T33:   0.2055 T12:   0.0044                                     
REMARK   3      T13:   0.0118 T23:  -0.0549                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2712 L22:   1.8128                                     
REMARK   3      L33:   2.3145 L12:   0.9498                                     
REMARK   3      L13:  -0.8661 L23:  -1.6023                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0000 S12:   0.1390 S13:  -0.1569                       
REMARK   3      S21:  -0.3791 S22:  -0.1935 S23:  -0.0876                       
REMARK   3      S31:   0.3491 S32:  -0.0773 S33:   0.1898                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 188 THROUGH 309 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   2.4691   7.5493  34.2932              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2496 T22:   0.2160                                     
REMARK   3      T33:   0.2527 T12:   0.0124                                     
REMARK   3      T13:   0.0258 T23:  -0.0046                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0826 L22:   0.8641                                     
REMARK   3      L33:   1.0958 L12:   0.4751                                     
REMARK   3      L13:  -0.5667 L23:  -0.9652                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0396 S12:  -0.0384 S13:   0.0055                       
REMARK   3      S21:   0.0625 S22:   0.0685 S23:   0.1190                       
REMARK   3      S31:  -0.0893 S32:  -0.1435 S33:  -0.1132                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 310 THROUGH 350 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  23.9301  18.1818  17.3856              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1746 T22:   0.1723                                     
REMARK   3      T33:   0.1849 T12:   0.0290                                     
REMARK   3      T13:  -0.0078 T23:   0.0157                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.2054 L22:   1.2915                                     
REMARK   3      L33:   3.2127 L12:  -0.2254                                     
REMARK   3      L13:   0.5892 L23:   1.2202                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0837 S12:  -0.1050 S13:   0.0572                       
REMARK   3      S21:   0.0078 S22:  -0.0151 S23:  -0.0373                       
REMARK   3      S31:  -0.0127 S32:   0.0285 S33:   0.0845                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 351 THROUGH 408 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  20.5005   2.7411  26.2307              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2830 T22:   0.2780                                     
REMARK   3      T33:   0.3271 T12:   0.0506                                     
REMARK   3      T13:   0.0659 T23:   0.0233                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6077 L22:   2.2577                                     
REMARK   3      L33:   1.4830 L12:   2.3551                                     
REMARK   3      L13:  -1.5690 L23:  -2.2129                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0555 S12:  -0.0635 S13:  -0.1588                       
REMARK   3      S21:  -0.0884 S22:  -0.0587 S23:  -0.1125                       
REMARK   3      S31:   0.1546 S32:   0.0610 S33:   0.1192                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 409 THROUGH 448 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  35.1215   8.8056  16.4243              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3087 T22:   0.2420                                     
REMARK   3      T33:   0.3194 T12:   0.0568                                     
REMARK   3      T13:   0.0529 T23:   0.0459                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1983 L22:   1.5197                                     
REMARK   3      L33:   5.3088 L12:  -0.5794                                     
REMARK   3      L13:  -0.9869 L23:  -2.2351                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2645 S12:  -0.0206 S13:  -0.5556                       
REMARK   3      S21:  -0.3850 S22:  -0.0656 S23:   0.0104                       
REMARK   3      S31:   0.9326 S32:   0.4617 S33:   0.2959                       
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 6PVG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-JUL-19.                  
REMARK 100 THE DEPOSITION ID IS D_1000243117.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 13-DEC-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 23-ID-D                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.033                              
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL                     
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 6M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 630819                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 47.880                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY                : 12.40                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 1.3400                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.71                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.77                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.99                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.28                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG 3350, 200 MM AMMONIUM ACETATE,   
REMARK 280  100 MM BIS-TRIS PH 5.5, 2% 2,2,2-TRIFLUOROETHANOL, VAPOR            
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 293K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       23.86200            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       58.19450            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       42.10500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       58.19450            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       23.86200            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       42.10500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 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     MET A     1                                                      
REMARK 465     GLY A     2                                                      
REMARK 465     SER A     3                                                      
REMARK 465     ASP A   449                                                      
REMARK 465     VAL A   450                                                      
REMARK 465     LYS A   451                                                      
REMARK 465     GLU A   452                                                      
REMARK 465     PRO A   453                                                      
REMARK 465     LEU A   454                                                      
REMARK 465     GLN A   455                                                      
REMARK 465     ASN A   456                                                      
REMARK 465     LYS A   457                                                      
REMARK 465     SER A   458                                                      
REMARK 465     PRO A   459                                                      
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   O    HOH A   870     O    HOH A   906              1.91            
REMARK 500   O    ARG A   440     O    HOH A   601              1.94            
REMARK 500   O    HOH A   713     O    HOH A   941              2.12            
REMARK 500   O    HOH A   657     O    HOH A   946              2.12            
REMARK 500   NH2  ARG A   154     O    HOH A   602              2.13            
REMARK 500   O    HOH A   743     O    HOH A   938              2.15            
REMARK 500   O    HOH A   650     O    HOH A   835              2.16            
REMARK 500   O    HOH A   609     O    HOH A   617              2.17            
REMARK 500   O    PRO A   287     O    HOH A   603              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LEU A  15       60.58   -116.89                                   
REMARK 500    ASP A  47     -127.18   -129.56                                   
REMARK 500    ILE A 176      -60.53    -97.90                                   
REMARK 500    PHE A 219       84.31   -150.93                                   
REMARK 500    PRO A 323       92.01    -61.35                                   
REMARK 500    ALA A 325     -134.41     48.81                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FAD A 501                 
DBREF  6PVG A    1   459  UNP    L0E4H0   L0E4H0_9EURO     1    459             
SEQRES   1 A  459  MET GLY SER LEU GLY GLU GLU VAL GLN VAL ILE ILE VAL          
SEQRES   2 A  459  GLY LEU GLY ILE VAL GLY LEU ALA ALA ALA ILE GLU CYS          
SEQRES   3 A  459  ARG GLU LYS GLY HIS SER VAL HIS ALA PHE GLU LYS SER          
SEQRES   4 A  459  ASN ILE LEU LYS SER ILE GLY ASP CYS ILE GLY LEU GLN          
SEQRES   5 A  459  SER ASN ALA THR ARG ILE ILE LYS ARG TRP GLY ASP GLY          
SEQRES   6 A  459  ALA VAL HIS GLU ALA LEU ARG PRO TRP ILE VAL SER SER          
SEQRES   7 A  459  LYS GLU ILE ARG ILE HIS ASN SER SER GLY ARG LEU ILE          
SEQRES   8 A  459  ILE ARG GLN ASP LEU SER GLU VAL CYS GLU GLN PRO ASN          
SEQRES   9 A  459  TYR LEU LEU PRO ARG SER GLU LEU ILE ARG VAL MET TYR          
SEQRES  10 A  459  GLU HIS ALA LEU LYS ILE GLY VAL GLU ILE SER LEU GLY          
SEQRES  11 A  459  VAL GLU VAL CYS GLU PRO SER GLU ASP GLU GLU GLY ALA          
SEQRES  12 A  459  SER VAL VAL ALA LEU THR ARG ASP GLY GLU ARG GLN ILE          
SEQRES  13 A  459  VAL ARG GLY ASP PHE ILE ILE CYS SER ASP GLY VAL HIS          
SEQRES  14 A  459  SER LYS MET ARG LYS ALA ILE MET PRO GLN PRO VAL GLU          
SEQRES  15 A  459  PRO ARG PRO SER GLY TYR ALA ALA PHE ARG ALA LEU VAL          
SEQRES  16 A  459  ASP THR GLU THR LEU LYS GLY ASP PRO GLU ALA SER TRP          
SEQRES  17 A  459  VAL PHE GLU GLY VAL GLU GLU ASN ASP ARG PHE ASP VAL          
SEQRES  18 A  459  PHE PHE LEU SER GLY ALA GLN ILE ALA LEU GLN SER CYS          
SEQRES  19 A  459  ASN LYS GLY LYS VAL PHE SER TRP PHE CYS ILE HIS GLN          
SEQRES  20 A  459  ASP THR ARG ASN LEU LEU ASP VAL TRP THR SER PRO ALA          
SEQRES  21 A  459  ASP PRO ASN GLU MET LEU ASP LEU ILE LYS VAL TRP PRO          
SEQRES  22 A  459  ILE GLY GLN ARG LEU TRP SER VAL ILE ARG HIS THR GLN          
SEQRES  23 A  459  PRO GLN LYS PHE ILE ASN TYR PRO LEU LEU ASN HIS LYS          
SEQRES  24 A  459  PRO LEU ASP HIS TRP VAL SER SER HIS GLY ARG LEU ILE          
SEQRES  25 A  459  LEU ILE GLY ASP ALA ALA HIS PRO LEU SER PRO ALA ALA          
SEQRES  26 A  459  GLY GLN GLY ALA SER GLN GLY ILE GLU ASP ALA ASN VAL          
SEQRES  27 A  459  LEU ALA THR SER LEU SER LEU ALA GLY ARG GLN ARG VAL          
SEQRES  28 A  459  SER LEU ALA LEU HIS VAL ALA GLU ARG ILE ARG TYR ALA          
SEQRES  29 A  459  ARG ALA SER ALA VAL GLN LEU ILE SER HIS ARG VAL ASN          
SEQRES  30 A  459  GLU GLY TRP ARG ASN GLN ASP TRP ASP ALA TYR GLU PRO          
SEQRES  31 A  459  ASN GLU GLN ASN ILE ALA SER LEU PRO LEU GLU THR TRP          
SEQRES  32 A  459  ILE TYR GLY HIS ASP SER GLN ALA TYR THR GLU GLN GLU          
SEQRES  33 A  459  PHE GLU MET VAL VAL ARG ALA VAL GLN GLU GLY GLU GLU          
SEQRES  34 A  459  TYR HIS ALA THR ASN LEU PRO ASP LYS LEU ARG VAL GLN          
SEQRES  35 A  459  LEU GLY ILE ARG ASN VAL ASP VAL LYS GLU PRO LEU GLN          
SEQRES  36 A  459  ASN LYS SER PRO                                              
HET    FAD  A 501      53                                                       
HETNAM     FAD FLAVIN-ADENINE DINUCLEOTIDE                                      
FORMUL   2  FAD    C27 H33 N9 O15 P2                                            
FORMUL   3  HOH   *400(H2 O)                                                    
HELIX    1 AA1 GLY A   16  GLU A   28  1                                  13    
HELIX    2 AA2 GLN A   52  LYS A   60  1                                   9    
HELIX    3 AA3 ARG A   61  ASP A   64  5                                   4    
HELIX    4 AA4 GLY A   65  ARG A   72  1                                   8    
HELIX    5 AA5 PRO A   73  ILE A   75  5                                   3    
HELIX    6 AA6 ARG A  109  ILE A  123  1                                  15    
HELIX    7 AA7 MET A  172  MET A  177  1                                   6    
HELIX    8 AA8 ASP A  196  LYS A  201  1                                   6    
HELIX    9 AA9 ASP A  203  GLU A  211  5                                   9    
HELIX   10 AB1 ASP A  261  VAL A  271  1                                  11    
HELIX   11 AB2 ILE A  274  ARG A  283  1                                  10    
HELIX   12 AB3 GLY A  315  ALA A  318  5                                   4    
HELIX   13 AB4 GLY A  326  GLY A  347  1                                  22    
HELIX   14 AB5 ARG A  350  ARG A  381  1                                  32    
HELIX   15 AB6 ASN A  391  ILE A  395  5                                   5    
HELIX   16 AB7 GLU A  401  GLY A  406  1                                   6    
HELIX   17 AB8 ASP A  408  GLY A  427  1                                  20    
HELIX   18 AB9 LYS A  438  LEU A  443  1                                   6    
SHEET    1 AA1 5 GLU A 126  LEU A 129  0                                        
SHEET    2 AA1 5 SER A  32  GLU A  37  1  N  ALA A  35   O  GLU A 126           
SHEET    3 AA1 5 GLN A   9  VAL A  13  1  N  VAL A  10   O  SER A  32           
SHEET    4 AA1 5 PHE A 161  CYS A 164  1  O  ILE A 163   N  ILE A  11           
SHEET    5 AA1 5 LEU A 311  LEU A 313  1  O  ILE A 312   N  CYS A 164           
SHEET    1 AA2 2 CYS A  48  LEU A  51  0                                        
SHEET    2 AA2 2 TYR A 105  PRO A 108 -1  O  LEU A 107   N  ILE A  49           
SHEET    1 AA3 7 LEU A  90  ASP A  95  0                                        
SHEET    2 AA3 7 GLU A  80  HIS A  84 -1  N  ILE A  83   O  ILE A  92           
SHEET    3 AA3 7 PHE A 219  LEU A 224  1  O  VAL A 221   N  ARG A  82           
SHEET    4 AA3 7 ALA A 227  CYS A 234 -1  O  ALA A 227   N  LEU A 224           
SHEET    5 AA3 7 VAL A 239  GLN A 247 -1  O  SER A 241   N  GLN A 232           
SHEET    6 AA3 7 ARG A 184  LEU A 194 -1  N  PHE A 191   O  CYS A 244           
SHEET    7 AA3 7 ILE A 291  ASN A 297 -1  O  ASN A 297   N  ARG A 184           
SHEET    1 AA4 3 VAL A 131  GLU A 138  0                                        
SHEET    2 AA4 3 ALA A 143  THR A 149 -1  O  SER A 144   N  SER A 137           
SHEET    3 AA4 3 ARG A 154  GLY A 159 -1  O  GLN A 155   N  ALA A 147           
CISPEP   1 LEU A  398    PRO A  399          0         4.95                     
SITE     1 AC1 33 GLY A  14  GLY A  16  ILE A  17  VAL A  18                    
SITE     2 AC1 33 GLU A  37  LYS A  38  ILE A  45  GLY A  46                    
SITE     3 AC1 33 ASP A  47  CYS A  48  ILE A  49  ARG A 109                    
SITE     4 AC1 33 VAL A 131  GLU A 132  VAL A 133  ASP A 166                    
SITE     5 AC1 33 GLY A 167  ARG A 192  TRP A 256  GLY A 315                    
SITE     6 AC1 33 ASP A 316  PRO A 323  ALA A 329  HOH A 621                    
SITE     7 AC1 33 HOH A 639  HOH A 649  HOH A 658  HOH A 686                    
SITE     8 AC1 33 HOH A 721  HOH A 730  HOH A 759  HOH A 807                    
SITE     9 AC1 33 HOH A 812                                                     
CRYST1   47.724   84.210  116.389  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.020954  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011875  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008592        0.00000                         
ATOM      1  N   LEU A   4      34.399  38.972   3.739  1.00 92.37           N  
ANISOU    1  N   LEU A   4    10630  11920  12546  -3148   2747   2250       N  
ATOM      2  CA  LEU A   4      33.155  39.717   3.566  1.00 96.38           C  
ANISOU    2  CA  LEU A   4    11476  12120  13025  -3051   2637   2501       C  
ATOM      3  C   LEU A   4      32.549  40.117   4.912  1.00 92.93           C  
ANISOU    3  C   LEU A   4    11126  11413  12772  -3114   2290   2355       C  
ATOM      4  O   LEU A   4      32.314  41.297   5.155  1.00107.91           O  
ANISOU    4  O   LEU A   4    13220  13009  14772  -3319   2152   2477       O  
ATOM      5  CB  LEU A   4      32.151  38.903   2.747  1.00 99.43           C  
ANISOU    5  CB  LEU A   4    12122  12633  13023  -2777   2740   2504       C  
ATOM      6  CG  LEU A   4      32.544  38.693   1.279  1.00104.34           C  
ANISOU    6  CG  LEU A   4    12811  13518  13315  -2788   3042   2644       C  
ATOM      7  CD1 LEU A   4      31.414  38.020   0.506  1.00102.07           C  
ANISOU    7  CD1 LEU A   4    12808  13397  12577  -2575   3004   2678       C  
ATOM      8  CD2 LEU A   4      32.962  40.010   0.616  1.00102.01           C  
ANISOU    8  CD2 LEU A   4    12649  12977  13133  -2983   3257   2933       C  
ATOM      9  N   GLY A   5      32.284  39.142   5.778  1.00 79.22           N  
ANISOU    9  N   GLY A   5     9319   9756  11025  -2971   2184   2033       N  
ATOM     10  CA  GLY A   5      31.984  39.423   7.168  1.00 73.11           C  
ANISOU   10  CA  GLY A   5     8596   8709  10472  -2991   1956   1768       C  
ATOM     11  C   GLY A   5      30.529  39.382   7.583  1.00 77.72           C  
ANISOU   11  C   GLY A   5     9458   9085  10986  -2798   1785   1769       C  
ATOM     12  O   GLY A   5      30.217  39.769   8.718  1.00 75.10           O  
ANISOU   12  O   GLY A   5     9183   8474  10880  -2772   1630   1564       O  
ATOM     13  N   GLU A   6      29.631  38.920   6.721  1.00 80.26           N  
ANISOU   13  N   GLU A   6     9939   9541  11015  -2629   1812   1971       N  
ATOM     14  CA  GLU A   6      28.224  38.870   7.082  1.00 79.71           C  
ANISOU   14  CA  GLU A   6    10138   9281  10868  -2441   1656   1962       C  
ATOM     15  C   GLU A   6      27.971  37.737   8.071  1.00 68.48           C  
ANISOU   15  C   GLU A   6     8589   7949   9481  -2256   1582   1627       C  
ATOM     16  O   GLU A   6      28.614  36.684   8.020  1.00 63.63           O  
ANISOU   16  O   GLU A   6     7776   7651   8750  -2239   1658   1436       O  
ATOM     17  CB  GLU A   6      27.363  38.702   5.832  1.00 86.75           C  
ANISOU   17  CB  GLU A   6    11311  10271  11379  -2303   1748   2161       C  
ATOM     18  CG  GLU A   6      27.813  39.615   4.701  1.00100.21           C  
ANISOU   18  CG  GLU A   6    13173  11909  12992  -2455   1948   2402       C  
ATOM     19  CD  GLU A   6      26.676  40.065   3.811  1.00107.40           C  
ANISOU   19  CD  GLU A   6    14402  12713  13693  -2289   1913   2709       C  
ATOM     20  OE1 GLU A   6      26.422  39.397   2.786  1.00108.23           O  
ANISOU   20  OE1 GLU A   6    14542  13110  13472  -2143   2004   2809       O  
ATOM     21  OE2 GLU A   6      26.037  41.089   4.141  1.00110.58           O  
ANISOU   21  OE2 GLU A   6    15005  12754  14257  -2282   1760   2841       O  
ATOM     22  N   GLU A   7      27.035  37.976   8.991  1.00 66.94           N  
ANISOU   22  N   GLU A   7     8523   7473   9437  -2119   1423   1533       N  
ATOM     23  CA  GLU A   7      26.736  37.014  10.045  1.00 63.41           C  
ANISOU   23  CA  GLU A   7     7978   7138   8978  -1919   1256   1198       C  
ATOM     24  C   GLU A   7      26.331  35.662   9.466  1.00 49.91           C  
ANISOU   24  C   GLU A   7     6250   5786   6927  -1730   1243   1165       C  
ATOM     25  O   GLU A   7      25.707  35.575   8.407  1.00 57.35           O  
ANISOU   25  O   GLU A   7     7327   6827   7635  -1660   1284   1395       O  
ATOM     26  CB  GLU A   7      25.619  37.539  10.945  1.00 79.17           C  
ANISOU   26  CB  GLU A   7    10124   8844  11114  -1746   1051   1140       C  
ATOM     27  CG  GLU A   7      26.102  38.331  12.137  1.00 94.59           C  
ANISOU   27  CG  GLU A   7    11999  10529  13411  -1849    980    927       C  
ATOM     28  CD  GLU A   7      24.983  38.639  13.107  1.00105.16           C  
ANISOU   28  CD  GLU A   7    13453  11667  14837  -1634    775    803       C  
ATOM     29  OE1 GLU A   7      24.005  39.302  12.699  1.00110.24           O  
ANISOU   29  OE1 GLU A   7    14296  12106  15485  -1539    729   1008       O  
ATOM     30  OE2 GLU A   7      25.073  38.202  14.275  1.00107.08           O  
ANISOU   30  OE2 GLU A   7    13581  11978  15126  -1545    659    499       O  
ATOM     31  N   VAL A   8      26.702  34.594  10.178  1.00 42.51           N  
ANISOU   31  N   VAL A   8     5146   5038   5967  -1640   1172    869       N  
ATOM     32  CA  VAL A   8      26.221  33.255   9.847  1.00 40.86           C  
ANISOU   32  CA  VAL A   8     4928   5102   5497  -1443   1119    789       C  
ATOM     33  C   VAL A   8      24.713  33.197  10.057  1.00 41.45           C  
ANISOU   33  C   VAL A   8     5186   5064   5500  -1235    957    845       C  
ATOM     34  O   VAL A   8      24.200  33.617  11.104  1.00 42.25           O  
ANISOU   34  O   VAL A   8     5333   4954   5765  -1171    829    759       O  
ATOM     35  CB  VAL A   8      26.924  32.196  10.709  1.00 41.47           C  
ANISOU   35  CB  VAL A   8     4810   5335   5612  -1380   1055    474       C  
ATOM     36  CG1 VAL A   8      26.390  30.806  10.381  1.00 39.65           C  
ANISOU   36  CG1 VAL A   8     4587   5325   5153  -1182    991    392       C  
ATOM     37  CG2 VAL A   8      28.425  32.258  10.519  1.00 47.31           C  
ANISOU   37  CG2 VAL A   8     5329   6213   6435  -1571   1204    384       C  
ATOM     38  N   GLN A   9      23.992  32.658   9.071  1.00 35.58           N  
ANISOU   38  N   GLN A   9     4528   4487   4505  -1124    960    963       N  
ATOM     39  CA  GLN A   9      22.533  32.566   9.119  1.00 30.29           C  
ANISOU   39  CA  GLN A   9     4000   3753   3756   -932    813   1012       C  
ATOM     40  C   GLN A   9      22.139  31.114   9.356  1.00 27.44           C  
ANISOU   40  C   GLN A   9     3566   3589   3271   -783    725    806       C  
ATOM     41  O   GLN A   9      22.260  30.280   8.455  1.00 35.44           O  
ANISOU   41  O   GLN A   9     4541   4841   4085   -752    773    791       O  
ATOM     42  CB  GLN A   9      21.920  33.101   7.824  1.00 35.04           C  
ANISOU   42  CB  GLN A   9     4754   4387   4173   -907    854   1299       C  
ATOM     43  CG  GLN A   9      22.372  34.517   7.440  1.00 54.05           C  
ANISOU   43  CG  GLN A   9     7259   6579   6699  -1074    962   1562       C  
ATOM     44  CD  GLN A   9      21.705  35.606   8.268  1.00 65.56           C  
ANISOU   44  CD  GLN A   9     8833   7667   8408  -1031    842   1602       C  
ATOM     45  OE1 GLN A   9      20.561  35.457   8.701  1.00 75.09           O  
ANISOU   45  OE1 GLN A   9    10098   8825   9607   -836    682   1532       O  
ATOM     46  NE2 GLN A   9      22.422  36.709   8.492  1.00 60.35           N  
ANISOU   46  NE2 GLN A   9     8194   6749   7987  -1218    921   1695       N  
ATOM     47  N   VAL A  10      21.666  30.816  10.564  1.00 24.65           N  
ANISOU   47  N   VAL A  10     3196   3132   3036   -693    601    646       N  
ATOM     48  CA  VAL A  10      21.232  29.473  10.936  1.00 23.04           C  
ANISOU   48  CA  VAL A  10     2942   3058   2756   -568    517    477       C  
ATOM     49  C   VAL A  10      19.712  29.418  10.878  1.00 29.48           C  
ANISOU   49  C   VAL A  10     3854   3841   3507   -434    410    529       C  
ATOM     50  O   VAL A  10      19.037  30.305  11.410  1.00 25.82           O  
ANISOU   50  O   VAL A  10     3460   3207   3144   -398    353    584       O  
ATOM     51  CB  VAL A  10      21.733  29.102  12.341  1.00 26.11           C  
ANISOU   51  CB  VAL A  10     3245   3387   3290   -560    460    286       C  
ATOM     52  CG1 VAL A  10      21.286  27.691  12.710  1.00 26.35           C  
ANISOU   52  CG1 VAL A  10     3246   3516   3250   -442    381    156       C  
ATOM     53  CG2 VAL A  10      23.265  29.265  12.412  1.00 32.30           C  
ANISOU   53  CG2 VAL A  10     3900   4212   4158   -690    550    212       C  
ATOM     54  N   ILE A  11      19.168  28.381  10.237  1.00 21.93           N  
ANISOU   54  N   ILE A  11     2884   3053   2397   -355    378    484       N  
ATOM     55  CA  ILE A  11      17.730  28.106  10.233  1.00 20.98           C  
ANISOU   55  CA  ILE A  11     2806   2939   2228   -236    270    481       C  
ATOM     56  C   ILE A  11      17.484  26.882  11.099  1.00 20.25           C  
ANISOU   56  C   ILE A  11     2643   2867   2185   -197    214    303       C  
ATOM     57  O   ILE A  11      18.148  25.858  10.921  1.00 26.16           O  
ANISOU   57  O   ILE A  11     3330   3710   2901   -213    237    195       O  
ATOM     58  CB  ILE A  11      17.217  27.864   8.803  1.00 22.86           C  
ANISOU   58  CB  ILE A  11     3074   3353   2259   -183    262    555       C  
ATOM     59  CG1 ILE A  11      17.453  29.110   7.954  1.00 26.29           C  
ANISOU   59  CG1 ILE A  11     3605   3761   2623   -219    324    787       C  
ATOM     60  CG2 ILE A  11      15.766  27.475   8.822  1.00 25.77           C  
ANISOU   60  CG2 ILE A  11     3443   3752   2597    -67    139    507       C  
ATOM     61  CD1 ILE A  11      17.150  28.941   6.497  1.00 34.90           C  
ANISOU   61  CD1 ILE A  11     4734   5069   3457   -166    328    881       C  
ATOM     62  N   ILE A  12      16.528  26.972  12.019  1.00 19.57           N  
ANISOU   62  N   ILE A  12     2567   2693   2177   -140    144    276       N  
ATOM     63  CA  ILE A  12      16.182  25.841  12.877  1.00 18.84           C  
ANISOU   63  CA  ILE A  12     2424   2611   2125   -118    105    152       C  
ATOM     64  C   ILE A  12      14.724  25.482  12.629  1.00 24.24           C  
ANISOU   64  C   ILE A  12     3095   3346   2771    -58     40    143       C  
ATOM     65  O   ILE A  12      13.849  26.356  12.662  1.00 22.99           O  
ANISOU   65  O   ILE A  12     2957   3157   2621     -3      5    203       O  
ATOM     66  CB  ILE A  12      16.442  26.158  14.356  1.00 21.72           C  
ANISOU   66  CB  ILE A  12     2784   2869   2599   -122    101    112       C  
ATOM     67  CG1 ILE A  12      17.943  26.352  14.564  1.00 23.80           C  
ANISOU   67  CG1 ILE A  12     3025   3111   2908   -184    148     80       C  
ATOM     68  CG2 ILE A  12      15.886  25.034  15.276  1.00 23.97           C  
ANISOU   68  CG2 ILE A  12     3040   3168   2898    -97     70     39       C  
ATOM     69  CD1 ILE A  12      18.308  26.680  15.974  1.00 26.58           C  
ANISOU   69  CD1 ILE A  12     3364   3390   3347   -177    124     13       C  
ATOM     70  N   VAL A  13      14.469  24.201  12.365  1.00 22.13           N  
ANISOU   70  N   VAL A  13     2781   3147   2480    -65     18     51       N  
ATOM     71  CA  VAL A  13      13.128  23.690  12.107  1.00 20.56           C  
ANISOU   71  CA  VAL A  13     2535   3007   2269    -37    -44      6       C  
ATOM     72  C   VAL A  13      12.693  22.887  13.330  1.00 25.12           C  
ANISOU   72  C   VAL A  13     3075   3517   2951    -73    -38    -47       C  
ATOM     73  O   VAL A  13      13.187  21.777  13.569  1.00 25.17           O  
ANISOU   73  O   VAL A  13     3078   3485   3001   -115    -29   -107       O  
ATOM     74  CB  VAL A  13      13.076  22.834  10.838  1.00 21.04           C  
ANISOU   74  CB  VAL A  13     2564   3191   2239    -34    -79    -78       C  
ATOM     75  CG1 VAL A  13      11.636  22.391  10.570  1.00 20.70           C  
ANISOU   75  CG1 VAL A  13     2446   3216   2204    -14   -158   -150       C  
ATOM     76  CG2 VAL A  13      13.638  23.619   9.644  1.00 23.36           C  
ANISOU   76  CG2 VAL A  13     2905   3588   2382     -2    -59      3       C  
ATOM     77  N   GLY A  14      11.767  23.449  14.106  1.00 19.78           N  
ANISOU   77  N   GLY A  14     2373   2828   2312    -48    -41    -20       N  
ATOM     78  CA  GLY A  14      11.242  22.788  15.283  1.00 21.96           C  
ANISOU   78  CA  GLY A  14     2612   3078   2656    -90    -12    -42       C  
ATOM     79  C   GLY A  14      11.847  23.294  16.576  1.00 21.37           C  
ANISOU   79  C   GLY A  14     2581   2943   2594    -76     32     -6       C  
ATOM     80  O   GLY A  14      13.069  23.285  16.740  1.00 23.21           O  
ANISOU   80  O   GLY A  14     2869   3124   2824    -82     41      1       O  
ATOM     81  N   LEU A  15      10.993  23.751  17.493  1.00 20.01           N  
ANISOU   81  N   LEU A  15     2370   2805   2430    -50     54     -6       N  
ATOM     82  CA  LEU A  15      11.419  24.217  18.811  1.00 19.99           C  
ANISOU   82  CA  LEU A  15     2398   2785   2414    -22     88     -3       C  
ATOM     83  C   LEU A  15      10.826  23.340  19.906  1.00 23.18           C  
ANISOU   83  C   LEU A  15     2768   3243   2795    -67    147     15       C  
ATOM     84  O   LEU A  15      10.076  23.816  20.766  1.00 24.97           O  
ANISOU   84  O   LEU A  15     2943   3553   2990    -32    188     -5       O  
ATOM     85  CB  LEU A  15      11.023  25.685  19.024  1.00 23.20           C  
ANISOU   85  CB  LEU A  15     2792   3194   2830     69     70    -36       C  
ATOM     86  CG  LEU A  15      11.816  26.651  18.133  1.00 21.82           C  
ANISOU   86  CG  LEU A  15     2682   2923   2687     94     27    -11       C  
ATOM     87  CD1 LEU A  15      11.353  28.083  18.345  1.00 25.94           C  
ANISOU   87  CD1 LEU A  15     3208   3392   3258    190     -4    -38       C  
ATOM     88  CD2 LEU A  15      13.320  26.526  18.435  1.00 23.95           C  
ANISOU   88  CD2 LEU A  15     3006   3132   2963     46     41    -15       C  
ATOM     89  N   GLY A  16      11.157  22.052  19.878  1.00 23.35           N  
ANISOU   89  N   GLY A  16     2819   3217   2836   -142    158     57       N  
ATOM     90  CA  GLY A  16      11.122  21.253  21.086  1.00 23.24           C  
ANISOU   90  CA  GLY A  16     2832   3211   2786   -180    215    127       C  
ATOM     91  C   GLY A  16      12.376  21.533  21.889  1.00 26.25           C  
ANISOU   91  C   GLY A  16     3298   3574   3103   -111    189    136       C  
ATOM     92  O   GLY A  16      13.048  22.552  21.709  1.00 20.81           O  
ANISOU   92  O   GLY A  16     2616   2880   2410    -48    147     69       O  
ATOM     93  N   ILE A  17      12.710  20.601  22.779  1.00 23.06           N  
ANISOU   93  N   ILE A  17     2955   3152   2654   -124    207    224       N  
ATOM     94  CA  ILE A  17      13.867  20.810  23.641  1.00 23.90           C  
ANISOU   94  CA  ILE A  17     3127   3275   2680    -38    162    221       C  
ATOM     95  C   ILE A  17      15.130  20.999  22.813  1.00 23.50           C  
ANISOU   95  C   ILE A  17     3086   3144   2698     -3     81    142       C  
ATOM     96  O   ILE A  17      15.969  21.853  23.116  1.00 22.92           O  
ANISOU   96  O   ILE A  17     3005   3104   2599     57     39     64       O  
ATOM     97  CB  ILE A  17      14.003  19.630  24.613  1.00 27.03           C  
ANISOU   97  CB  ILE A  17     3606   3655   3010    -43    179    362       C  
ATOM     98  CG1 ILE A  17      12.760  19.556  25.494  1.00 28.52           C  
ANISOU   98  CG1 ILE A  17     3768   3964   3104    -97    293    451       C  
ATOM     99  CG2 ILE A  17      15.293  19.729  25.429  1.00 26.52           C  
ANISOU   99  CG2 ILE A  17     3603   3620   2851     74     98    350       C  
ATOM    100  CD1 ILE A  17      12.757  18.344  26.344  1.00 35.96           C  
ANISOU  100  CD1 ILE A  17     4807   4872   3983   -131    332    642       C  
ATOM    101  N   VAL A  18      15.290  20.205  21.755  1.00 20.89           N  
ANISOU  101  N   VAL A  18     2758   2720   2461    -46     63    142       N  
ATOM    102  CA  VAL A  18      16.577  20.170  21.064  1.00 21.92           C  
ANISOU  102  CA  VAL A  18     2886   2806   2636     -9      3     67       C  
ATOM    103  C   VAL A  18      16.744  21.391  20.168  1.00 23.28           C  
ANISOU  103  C   VAL A  18     3004   3015   2827    -22     12     -8       C  
ATOM    104  O   VAL A  18      17.830  21.984  20.108  1.00 22.53           O  
ANISOU  104  O   VAL A  18     2887   2931   2740      2    -11    -70       O  
ATOM    105  CB  VAL A  18      16.721  18.853  20.285  1.00 20.87           C  
ANISOU  105  CB  VAL A  18     2771   2572   2587    -31    -21     66       C  
ATOM    106  CG1 VAL A  18      18.028  18.835  19.498  1.00 20.17           C  
ANISOU  106  CG1 VAL A  18     2649   2480   2534     18    -66    -39       C  
ATOM    107  CG2 VAL A  18      16.705  17.697  21.266  1.00 20.77           C  
ANISOU  107  CG2 VAL A  18     2839   2476   2578    -12    -38    173       C  
ATOM    108  N   GLY A  19      15.673  21.802  19.484  1.00 19.94           N  
ANISOU  108  N   GLY A  19     2555   2610   2413    -62     44      3       N  
ATOM    109  CA  GLY A  19      15.753  22.998  18.662  1.00 20.73           C  
ANISOU  109  CA  GLY A  19     2631   2725   2521    -63     48    -25       C  
ATOM    110  C   GLY A  19      16.010  24.249  19.482  1.00 22.58           C  
ANISOU  110  C   GLY A  19     2867   2959   2754    -29     46    -51       C  
ATOM    111  O   GLY A  19      16.740  25.145  19.048  1.00 20.01           O  
ANISOU  111  O   GLY A  19     2537   2600   2466    -42     43    -76       O  
ATOM    112  N   LEU A  20      15.412  24.330  20.671  1.00 18.77           N  
ANISOU  112  N   LEU A  20     2386   2516   2228      6     53    -54       N  
ATOM    113  CA  LEU A  20      15.711  25.452  21.565  1.00 18.91           C  
ANISOU  113  CA  LEU A  20     2400   2543   2243     54     35   -127       C  
ATOM    114  C   LEU A  20      17.159  25.401  22.043  1.00 22.73           C  
ANISOU  114  C   LEU A  20     2885   3022   2730     64     -8   -188       C  
ATOM    115  O   LEU A  20      17.832  26.435  22.124  1.00 20.56           O  
ANISOU  115  O   LEU A  20     2587   2709   2516     60    -33   -272       O  
ATOM    116  CB  LEU A  20      14.739  25.465  22.750  1.00 21.13           C  
ANISOU  116  CB  LEU A  20     2670   2919   2441    103     62   -137       C  
ATOM    117  CG  LEU A  20      13.338  25.999  22.406  1.00 24.80           C  
ANISOU  117  CG  LEU A  20     3089   3406   2926    119     94   -137       C  
ATOM    118  CD1 LEU A  20      12.294  25.682  23.491  1.00 23.55           C  
ANISOU  118  CD1 LEU A  20     2889   3388   2671    145    154   -138       C  
ATOM    119  CD2 LEU A  20      13.433  27.512  22.144  1.00 25.87           C  
ANISOU  119  CD2 LEU A  20     3223   3460   3145    170     54   -218       C  
ATOM    120  N   ALA A  21      17.657  24.209  22.372  1.00 22.48           N  
ANISOU  120  N   ALA A  21     2871   3018   2651     79    -27   -153       N  
ATOM    121  CA  ALA A  21      19.059  24.087  22.765  1.00 20.31           C  
ANISOU  121  CA  ALA A  21     2575   2760   2382    112    -89   -225       C  
ATOM    122  C   ALA A  21      19.989  24.506  21.626  1.00 22.15           C  
ANISOU  122  C   ALA A  21     2752   2945   2720     50    -81   -276       C  
ATOM    123  O   ALA A  21      20.959  25.245  21.840  1.00 22.21           O  
ANISOU  123  O   ALA A  21     2701   2959   2780     38   -109   -377       O  
ATOM    124  CB  ALA A  21      19.357  22.653  23.203  1.00 21.78           C  
ANISOU  124  CB  ALA A  21     2803   2960   2511    164   -124   -158       C  
ATOM    125  N   ALA A  22      19.707  24.031  20.407  1.00 21.40           N  
ANISOU  125  N   ALA A  22     2664   2819   2650      4    -38   -217       N  
ATOM    126  CA  ALA A  22      20.495  24.431  19.246  1.00 22.34           C  
ANISOU  126  CA  ALA A  22     2731   2931   2828    -60     -3   -244       C  
ATOM    127  C   ALA A  22      20.434  25.934  19.019  1.00 24.71           C  
ANISOU  127  C   ALA A  22     3024   3179   3186   -121     30   -242       C  
ATOM    128  O   ALA A  22      21.452  26.558  18.688  1.00 22.22           O  
ANISOU  128  O   ALA A  22     2650   2853   2940   -187     53   -287       O  
ATOM    129  CB  ALA A  22      20.013  23.685  18.002  1.00 23.80           C  
ANISOU  129  CB  ALA A  22     2930   3124   2987    -81     33   -191       C  
ATOM    130  N   ALA A  23      19.254  26.536  19.192  1.00 23.20           N  
ANISOU  130  N   ALA A  23     2886   2945   2986   -102     33   -194       N  
ATOM    131  CA  ALA A  23      19.134  27.979  18.993  1.00 22.79           C  
ANISOU  131  CA  ALA A  23     2847   2797   3016   -138     46   -187       C  
ATOM    132  C   ALA A  23      19.990  28.740  19.995  1.00 25.66           C  
ANISOU  132  C   ALA A  23     3168   3122   3460   -149      8   -316       C  
ATOM    133  O   ALA A  23      20.688  29.692  19.629  1.00 23.00           O  
ANISOU  133  O   ALA A  23     2806   2693   3239   -236     29   -335       O  
ATOM    134  CB  ALA A  23      17.670  28.415  19.104  1.00 20.64           C  
ANISOU  134  CB  ALA A  23     2622   2494   2724    -75     35   -143       C  
ATOM    135  N   ILE A  24      19.953  28.331  21.264  1.00 20.80           N  
ANISOU  135  N   ILE A  24     2539   2582   2781    -70    -48   -405       N  
ATOM    136  CA  ILE A  24      20.750  28.999  22.287  1.00 20.62           C  
ANISOU  136  CA  ILE A  24     2463   2561   2811    -60   -109   -566       C  
ATOM    137  C   ILE A  24      22.241  28.795  22.020  1.00 22.88           C  
ANISOU  137  C   ILE A  24     2656   2875   3161   -129   -119   -633       C  
ATOM    138  O   ILE A  24      23.029  29.748  22.051  1.00 24.84           O  
ANISOU  138  O   ILE A  24     2836   3055   3545   -211   -127   -736       O  
ATOM    139  CB  ILE A  24      20.339  28.486  23.684  1.00 20.35           C  
ANISOU  139  CB  ILE A  24     2444   2654   2635     61   -166   -629       C  
ATOM    140  CG1 ILE A  24      18.909  28.949  24.001  1.00 21.73           C  
ANISOU  140  CG1 ILE A  24     2669   2820   2768    118   -141   -607       C  
ATOM    141  CG2 ILE A  24      21.359  28.945  24.756  1.00 22.87           C  
ANISOU  141  CG2 ILE A  24     2691   3030   2967     93   -257   -823       C  
ATOM    142  CD1 ILE A  24      18.268  28.214  25.181  1.00 25.56           C  
ANISOU  142  CD1 ILE A  24     3173   3469   3069    218   -148   -605       C  
ATOM    143  N   GLU A  25      22.653  27.550  21.739  1.00 21.16           N  
ANISOU  143  N   GLU A  25     2420   2751   2867    -98   -118   -589       N  
ATOM    144  CA  GLU A  25      24.072  27.271  21.499  1.00 24.66           C  
ANISOU  144  CA  GLU A  25     2747   3255   3369   -136   -131   -677       C  
ATOM    145  C   GLU A  25      24.604  28.073  20.316  1.00 24.90           C  
ANISOU  145  C   GLU A  25     2719   3218   3523   -292    -33   -651       C  
ATOM    146  O   GLU A  25      25.691  28.650  20.392  1.00 26.51           O  
ANISOU  146  O   GLU A  25     2802   3429   3842   -377    -33   -767       O  
ATOM    147  CB  GLU A  25      24.295  25.769  21.264  1.00 23.22           C  
ANISOU  147  CB  GLU A  25     2568   3157   3100    -53   -149   -634       C  
ATOM    148  CG  GLU A  25      24.244  24.915  22.545  1.00 25.79           C  
ANISOU  148  CG  GLU A  25     2931   3552   3315     96   -257   -655       C  
ATOM    149  CD  GLU A  25      25.587  24.820  23.269  1.00 35.82           C  
ANISOU  149  CD  GLU A  25     4083   4923   4603    162   -363   -815       C  
ATOM    150  OE1 GLU A  25      26.619  25.210  22.682  1.00 33.56           O  
ANISOU  150  OE1 GLU A  25     3659   4661   4431     84   -341   -920       O  
ATOM    151  OE2 GLU A  25      25.620  24.355  24.429  1.00 32.94           O  
ANISOU  151  OE2 GLU A  25     3754   4633   4128    295   -467   -834       O  
ATOM    152  N   CYS A  26      23.842  28.130  19.224  1.00 24.83           N  
ANISOU  152  N   CYS A  26     2791   3157   3488   -335     52   -496       N  
ATOM    153  CA  CYS A  26      24.286  28.847  18.032  1.00 24.60           C  
ANISOU  153  CA  CYS A  26     2732   3083   3532   -479    160   -421       C  
ATOM    154  C   CYS A  26      24.304  30.350  18.257  1.00 25.23           C  
ANISOU  154  C   CYS A  26     2826   2996   3766   -579    170   -428       C  
ATOM    155  O   CYS A  26      25.244  31.037  17.829  1.00 27.39           O  
ANISOU  155  O   CYS A  26     3016   3228   4163   -729    239   -442       O  
ATOM    156  CB  CYS A  26      23.385  28.504  16.851  1.00 25.32           C  
ANISOU  156  CB  CYS A  26     2919   3186   3517   -468    223   -254       C  
ATOM    157  SG  CYS A  26      23.697  26.853  16.210  1.00 29.65           S  
ANISOU  157  SG  CYS A  26     3419   3906   3940   -399    233   -282       S  
ATOM    158  N   ARG A  27      23.273  30.882  18.918  1.00 23.41           N  
ANISOU  158  N   ARG A  27     2692   2659   3544   -502    108   -426       N  
ATOM    159  CA  ARG A  27      23.229  32.323  19.157  1.00 26.23           C  
ANISOU  159  CA  ARG A  27     3073   2818   4075   -575     99   -456       C  
ATOM    160  C   ARG A  27      24.362  32.767  20.075  1.00 30.38           C  
ANISOU  160  C   ARG A  27     3468   3335   4738   -639     45   -676       C  
ATOM    161  O   ARG A  27      24.953  33.839  19.875  1.00 30.13           O  
ANISOU  161  O   ARG A  27     3398   3145   4906   -790     78   -705       O  
ATOM    162  CB  ARG A  27      21.874  32.714  19.748  1.00 26.93           C  
ANISOU  162  CB  ARG A  27     3269   2826   4139   -442     33   -457       C  
ATOM    163  CG  ARG A  27      21.687  34.210  19.941  1.00 24.14           C  
ANISOU  163  CG  ARG A  27     2959   2229   3984   -482      8   -497       C  
ATOM    164  CD  ARG A  27      21.835  34.983  18.632  1.00 31.05           C  
ANISOU  164  CD  ARG A  27     3900   2929   4969   -617     98   -291       C  
ATOM    165  NE  ARG A  27      21.599  36.415  18.842  1.00 32.55           N  
ANISOU  165  NE  ARG A  27     4154   2830   5382   -644     61   -316       N  
ATOM    166  CZ  ARG A  27      22.123  37.372  18.085  1.00 42.62           C  
ANISOU  166  CZ  ARG A  27     5469   3884   6841   -809    129   -187       C  
ATOM    167  NH1 ARG A  27      22.918  37.050  17.075  1.00 46.98           N  
ANISOU  167  NH1 ARG A  27     5986   4519   7347   -965    254    -27       N  
ATOM    168  NH2 ARG A  27      21.859  38.652  18.336  1.00 40.83           N  
ANISOU  168  NH2 ARG A  27     5317   3350   6848   -821     77   -218       N  
ATOM    169  N   GLU A  28      24.699  31.953  21.081  1.00 25.44           N  
ANISOU  169  N   GLU A  28     2772   2879   4016   -531    -45   -831       N  
ATOM    170  CA  GLU A  28      25.791  32.343  21.962  1.00 30.68           C  
ANISOU  170  CA  GLU A  28     3292   3573   4791   -572   -123  -1066       C  
ATOM    171  C   GLU A  28      27.157  32.179  21.298  1.00 30.51           C  
ANISOU  171  C   GLU A  28     3109   3621   4862   -717    -57  -1098       C  
ATOM    172  O   GLU A  28      28.156  32.634  21.857  1.00 31.07           O  
ANISOU  172  O   GLU A  28     3027   3710   5069   -791   -111  -1303       O  
ATOM    173  CB  GLU A  28      25.684  31.571  23.289  1.00 31.71           C  
ANISOU  173  CB  GLU A  28     3411   3882   4756   -384   -254  -1206       C  
ATOM    174  CG  GLU A  28      24.369  31.931  24.000  1.00 31.59           C  
ANISOU  174  CG  GLU A  28     3523   3818   4661   -264   -294  -1203       C  
ATOM    175  CD  GLU A  28      24.323  31.654  25.497  1.00 39.38           C  
ANISOU  175  CD  GLU A  28     4490   4970   5502   -106   -419  -1380       C  
ATOM    176  OE1 GLU A  28      25.163  30.884  26.006  1.00 41.06           O  
ANISOU  176  OE1 GLU A  28     4624   5353   5624    -47   -492  -1455       O  
ATOM    177  OE2 GLU A  28      23.418  32.224  26.166  1.00 33.55           O  
ANISOU  177  OE2 GLU A  28     3815   4205   4727    -26   -447  -1444       O  
ATOM    178  N   LYS A  29      27.216  31.577  20.108  1.00 30.50           N  
ANISOU  178  N   LYS A  29     3121   3677   4792   -763     60   -923       N  
ATOM    179  CA  LYS A  29      28.408  31.636  19.268  1.00 29.90           C  
ANISOU  179  CA  LYS A  29     2888   3665   4808   -929    169   -931       C  
ATOM    180  C   LYS A  29      28.386  32.838  18.336  1.00 34.76           C  
ANISOU  180  C   LYS A  29     3545   4087   5574  -1142    306   -778       C  
ATOM    181  O   LYS A  29      29.286  32.980  17.503  1.00 36.43           O  
ANISOU  181  O   LYS A  29     3636   4354   5850  -1312    439   -738       O  
ATOM    182  CB  LYS A  29      28.549  30.346  18.452  1.00 37.93           C  
ANISOU  182  CB  LYS A  29     3884   4870   5656   -856    227   -849       C  
ATOM    183  CG  LYS A  29      28.785  29.120  19.309  1.00 34.04           C  
ANISOU  183  CG  LYS A  29     3344   4539   5052   -658     92   -986       C  
ATOM    184  CD  LYS A  29      30.073  29.252  20.084  1.00 43.10           C  
ANISOU  184  CD  LYS A  29     4279   5787   6311   -675     10  -1227       C  
ATOM    185  CE  LYS A  29      30.319  28.020  20.928  1.00 54.19           C  
ANISOU  185  CE  LYS A  29     5655   7346   7588   -449   -141  -1333       C  
ATOM    186  NZ  LYS A  29      31.541  28.185  21.758  1.00 63.32           N  
ANISOU  186  NZ  LYS A  29     6596   8624   8838   -434   -256  -1586       N  
ATOM    187  N   GLY A  30      27.373  33.695  18.452  1.00 34.23           N  
ANISOU  187  N   GLY A  30     3645   3800   5561  -1128    282   -683       N  
ATOM    188  CA  GLY A  30      27.282  34.908  17.675  1.00 40.76           C  
ANISOU  188  CA  GLY A  30     4548   4391   6550  -1306    387   -516       C  
ATOM    189  C   GLY A  30      26.526  34.796  16.369  1.00 40.44           C  
ANISOU  189  C   GLY A  30     4661   4341   6364  -1299    495   -215       C  
ATOM    190  O   GLY A  30      26.420  35.798  15.648  1.00 47.14           O  
ANISOU  190  O   GLY A  30     5599   4990   7323  -1434    583    -25       O  
ATOM    191  N   HIS A  31      25.994  33.623  16.042  1.00 33.70           N  
ANISOU  191  N   HIS A  31     3844   3688   5272  -1145    484   -163       N  
ATOM    192  CA  HIS A  31      25.282  33.452  14.787  1.00 35.73           C  
ANISOU  192  CA  HIS A  31     4229   3978   5368  -1123    567     86       C  
ATOM    193  C   HIS A  31      23.929  34.137  14.823  1.00 39.68           C  
ANISOU  193  C   HIS A  31     4916   4282   5878  -1020    495    211       C  
ATOM    194  O   HIS A  31      23.339  34.349  15.885  1.00 33.70           O  
ANISOU  194  O   HIS A  31     4187   3430   5187   -910    375     80       O  
ATOM    195  CB  HIS A  31      25.079  31.975  14.487  1.00 37.56           C  
ANISOU  195  CB  HIS A  31     4432   4464   5373   -987    553     54       C  
ATOM    196  CG  HIS A  31      26.340  31.186  14.545  1.00 39.21           C  
ANISOU  196  CG  HIS A  31     4452   4870   5575  -1029    592   -103       C  
ATOM    197  ND1 HIS A  31      27.501  31.617  13.946  1.00 46.09           N  
ANISOU  197  ND1 HIS A  31     5192   5796   6525  -1218    729    -93       N  
ATOM    198  CD2 HIS A  31      26.631  30.007  15.138  1.00 42.99           C  
ANISOU  198  CD2 HIS A  31     4845   5502   5986   -902    510   -273       C  
ATOM    199  CE1 HIS A  31      28.455  30.731  14.159  1.00 39.68           C  
ANISOU  199  CE1 HIS A  31     4199   5184   5693  -1191    724   -278       C  
ATOM    200  NE2 HIS A  31      27.958  29.753  14.892  1.00 43.19           N  
ANISOU  200  NE2 HIS A  31     4680   5675   6054   -989    582   -384       N  
ATOM    201  N   SER A  32      23.453  34.498  13.639  1.00 33.44           N  
ANISOU  201  N   SER A  32     4245   3453   5006  -1044    569    462       N  
ATOM    202  CA  SER A  32      22.073  34.910  13.467  1.00 33.75           C  
ANISOU  202  CA  SER A  32     4450   3369   5003   -899    489    590       C  
ATOM    203  C   SER A  32      21.231  33.647  13.368  1.00 30.78           C  
ANISOU  203  C   SER A  32     4073   3221   4403   -726    430    549       C  
ATOM    204  O   SER A  32      21.541  32.758  12.572  1.00 36.44           O  
ANISOU  204  O   SER A  32     4745   4150   4950   -741    496    584       O  
ATOM    205  CB  SER A  32      21.946  35.771  12.211  1.00 42.48           C  
ANISOU  205  CB  SER A  32     5687   4360   6092   -978    577    891       C  
ATOM    206  OG  SER A  32      20.705  36.440  12.161  1.00 56.86           O  
ANISOU  206  OG  SER A  32     7663   6004   7935   -830    474   1002       O  
ATOM    207  N   VAL A  33      20.201  33.534  14.205  1.00 24.27           N  
ANISOU  207  N   VAL A  33     3280   2357   3585   -572    312    451       N  
ATOM    208  CA  VAL A  33      19.408  32.312  14.295  1.00 22.24           C  
ANISOU  208  CA  VAL A  33     3001   2291   3157   -439    260    391       C  
ATOM    209  C   VAL A  33      17.950  32.646  14.038  1.00 28.21           C  
ANISOU  209  C   VAL A  33     3849   2999   3869   -299    186    479       C  
ATOM    210  O   VAL A  33      17.374  33.489  14.732  1.00 27.67           O  
ANISOU  210  O   VAL A  33     3819   2771   3923   -230    120    438       O  
ATOM    211  CB  VAL A  33      19.542  31.638  15.671  1.00 22.78           C  
ANISOU  211  CB  VAL A  33     2985   2417   3251   -388    200    179       C  
ATOM    212  CG1 VAL A  33      18.691  30.377  15.709  1.00 24.39           C  
ANISOU  212  CG1 VAL A  33     3180   2782   3305   -281    163    154       C  
ATOM    213  CG2 VAL A  33      21.018  31.344  15.988  1.00 28.23           C  
ANISOU  213  CG2 VAL A  33     3566   3164   3996   -497    244     69       C  
ATOM    214  N   HIS A  34      17.347  31.975  13.062  1.00 25.91           N  
ANISOU  214  N   HIS A  34     3578   2861   3407   -244    186    569       N  
ATOM    215  CA  HIS A  34      15.911  32.107  12.831  1.00 22.06           C  
ANISOU  215  CA  HIS A  34     3137   2380   2863    -95     97    616       C  
ATOM    216  C   HIS A  34      15.290  30.728  12.999  1.00 24.72           C  
ANISOU  216  C   HIS A  34     3392   2913   3086    -39     66    498       C  
ATOM    217  O   HIS A  34      15.511  29.836  12.164  1.00 24.11           O  
ANISOU  217  O   HIS A  34     3290   2992   2877    -67     95    510       O  
ATOM    218  CB  HIS A  34      15.599  32.684  11.457  1.00 25.44           C  
ANISOU  218  CB  HIS A  34     3666   2807   3194    -67     98    834       C  
ATOM    219  CG  HIS A  34      14.185  33.179  11.330  1.00 31.85           C  
ANISOU  219  CG  HIS A  34     4525   3578   4000    108    -20    880       C  
ATOM    220  ND1 HIS A  34      13.766  33.997  10.299  1.00 31.52           N  
ANISOU  220  ND1 HIS A  34     4599   3478   3898    182    -59   1093       N  
ATOM    221  CD2 HIS A  34      13.099  32.977  12.116  1.00 33.11           C  
ANISOU  221  CD2 HIS A  34     4619   3761   4201    233   -106    739       C  
ATOM    222  CE1 HIS A  34      12.480  34.270  10.453  1.00 36.36           C  
ANISOU  222  CE1 HIS A  34     5208   4077   4529    364   -185   1062       C  
ATOM    223  NE2 HIS A  34      12.051  33.663  11.548  1.00 33.72           N  
ANISOU  223  NE2 HIS A  34     4753   3801   4259    388   -205    840       N  
ATOM    224  N   ALA A  35      14.515  30.562  14.066  1.00 22.10           N  
ANISOU  224  N   ALA A  35     3015   2573   2809     35     13    379       N  
ATOM    225  CA  ALA A  35      13.887  29.289  14.400  1.00 23.42           C  
ANISOU  225  CA  ALA A  35     3105   2889   2906     60     -3    281       C  
ATOM    226  C   ALA A  35      12.401  29.339  14.081  1.00 25.41           C  
ANISOU  226  C   ALA A  35     3330   3204   3121    171    -73    288       C  
ATOM    227  O   ALA A  35      11.745  30.363  14.296  1.00 25.12           O  
ANISOU  227  O   ALA A  35     3315   3082   3149    266   -121    306       O  
ATOM    228  CB  ALA A  35      14.075  28.942  15.880  1.00 22.59           C  
ANISOU  228  CB  ALA A  35     2952   2772   2860     50      8    155       C  
ATOM    229  N   PHE A  36      11.874  28.223  13.586  1.00 20.03           N  
ANISOU  229  N   PHE A  36     2588   2668   2353    165    -88    250       N  
ATOM    230  CA  PHE A  36      10.487  28.140  13.141  1.00 20.30           C  
ANISOU  230  CA  PHE A  36     2561   2802   2350    257   -163    232       C  
ATOM    231  C   PHE A  36       9.821  26.982  13.861  1.00 24.40           C  
ANISOU  231  C   PHE A  36     2968   3410   2893    214   -148    111       C  
ATOM    232  O   PHE A  36      10.445  25.940  14.060  1.00 25.45           O  
ANISOU  232  O   PHE A  36     3096   3551   3022    118   -101     73       O  
ATOM    233  CB  PHE A  36      10.401  27.907  11.624  1.00 22.82           C  
ANISOU  233  CB  PHE A  36     2901   3234   2536    279   -208    293       C  
ATOM    234  CG  PHE A  36      10.953  29.031  10.813  1.00 24.78           C  
ANISOU  234  CG  PHE A  36     3271   3411   2734    313   -209    461       C  
ATOM    235  CD1 PHE A  36      12.297  29.063  10.477  1.00 23.66           C  
ANISOU  235  CD1 PHE A  36     3194   3234   2560    208   -120    530       C  
ATOM    236  CD2 PHE A  36      10.139  30.074  10.411  1.00 24.99           C  
ANISOU  236  CD2 PHE A  36     3342   3398   2755    451   -297    558       C  
ATOM    237  CE1 PHE A  36      12.815  30.102   9.709  1.00 23.84           C  
ANISOU  237  CE1 PHE A  36     3330   3190   2540    208    -95    715       C  
ATOM    238  CE2 PHE A  36      10.657  31.121   9.670  1.00 28.39           C  
ANISOU  238  CE2 PHE A  36     3909   3729   3148    472   -292    755       C  
ATOM    239  CZ  PHE A  36      12.007  31.134   9.320  1.00 27.99           C  
ANISOU  239  CZ  PHE A  36     3928   3646   3062    333   -178    844       C  
ATOM    240  N   GLU A  37       8.552  27.156  14.219  1.00 20.67           N  
ANISOU  240  N   GLU A  37     2402   2999   2453    286   -186     55       N  
ATOM    241  CA  GLU A  37       7.837  26.167  15.022  1.00 21.54           C  
ANISOU  241  CA  GLU A  37     2394   3190   2598    221   -144    -38       C  
ATOM    242  C   GLU A  37       6.363  26.231  14.663  1.00 24.01           C  
ANISOU  242  C   GLU A  37     2567   3636   2921    295   -210   -106       C  
ATOM    243  O   GLU A  37       5.772  27.314  14.662  1.00 22.46           O  
ANISOU  243  O   GLU A  37     2352   3442   2739    434   -266   -106       O  
ATOM    244  CB  GLU A  37       8.041  26.432  16.522  1.00 24.45           C  
ANISOU  244  CB  GLU A  37     2767   3512   3010    212    -69    -60       C  
ATOM    245  CG  GLU A  37       6.991  25.761  17.434  1.00 23.87           C  
ANISOU  245  CG  GLU A  37     2560   3555   2956    171    -10   -129       C  
ATOM    246  CD  GLU A  37       7.037  24.233  17.371  1.00 23.40           C  
ANISOU  246  CD  GLU A  37     2472   3513   2905     21     34   -123       C  
ATOM    247  OE1 GLU A  37       8.136  23.648  17.536  1.00 26.37           O  
ANISOU  247  OE1 GLU A  37     2950   3799   3271    -43     60    -76       O  
ATOM    248  OE2 GLU A  37       5.954  23.610  17.165  1.00 25.86           O  
ANISOU  248  OE2 GLU A  37     2650   3923   3254    -30     36   -177       O  
ATOM    249  N   LYS A  38       5.755  25.076  14.372  1.00 20.82           N  
ANISOU  249  N   LYS A  38     2263   2965   2681     83    -52    -88       N  
ATOM    250  CA  LYS A  38       4.402  25.116  13.846  1.00 23.27           C  
ANISOU  250  CA  LYS A  38     2523   3314   3003     66    -82    -36       C  
ATOM    251  C   LYS A  38       3.343  25.235  14.926  1.00 30.98           C  
ANISOU  251  C   LYS A  38     3458   4283   4032     70    -56     -3       C  
ATOM    252  O   LYS A  38       2.229  25.677  14.625  1.00 29.66           O  
ANISOU  252  O   LYS A  38     3229   4148   3893     73    -62     65       O  
ATOM    253  CB  LYS A  38       4.124  23.878  12.990  1.00 29.51           C  
ANISOU  253  CB  LYS A  38     3339   4129   3744     15   -145    -51       C  
ATOM    254  CG  LYS A  38       4.235  22.583  13.750  1.00 36.47           C  
ANISOU  254  CG  LYS A  38     4260   4980   4617    -13   -155    -98       C  
ATOM    255  CD  LYS A  38       4.018  21.396  12.818  1.00 45.98           C  
ANISOU  255  CD  LYS A  38     5511   6194   5764    -66   -217   -118       C  
ATOM    256  CE  LYS A  38       4.024  20.079  13.580  1.00 55.58           C  
ANISOU  256  CE  LYS A  38     6768   7374   6977    -97   -226   -158       C  
ATOM    257  NZ  LYS A  38       3.782  18.924  12.665  1.00 60.82           N  
ANISOU  257  NZ  LYS A  38     7495   8034   7579   -154   -287   -181       N  
ATOM    258  N   SER A  39       3.650  24.866  16.168  1.00 25.15           N  
ANISOU  258  N   SER A  39     2747   3504   3305     76    -25    -39       N  
ATOM    259  CA  SER A  39       2.643  24.813  17.212  1.00 24.03           C  
ANISOU  259  CA  SER A  39     2573   3353   3204     83      5     -7       C  
ATOM    260  C   SER A  39       2.828  25.947  18.214  1.00 27.31           C  
ANISOU  260  C   SER A  39     3006   3726   3646    134     77     -4       C  
ATOM    261  O   SER A  39       3.862  26.619  18.274  1.00 28.17           O  
ANISOU  261  O   SER A  39     3158   3805   3741    150     95    -37       O  
ATOM    262  CB  SER A  39       2.678  23.449  17.917  1.00 31.22           C  
ANISOU  262  CB  SER A  39     3510   4249   4103     48    -14    -45       C  
ATOM    263  OG  SER A  39       3.791  23.347  18.780  1.00 43.25           O  
ANISOU  263  OG  SER A  39     5092   5730   5612     61     13   -102       O  
ATOM    264  N   ASN A  40       1.784  26.153  19.012  1.00 25.35           N  
ANISOU  264  N   ASN A  40     2725   3471   3434    158    121     41       N  
ATOM    265  CA  ASN A  40       1.823  27.099  20.121  1.00 26.22           C  
ANISOU  265  CA  ASN A  40     2873   3529   3560    208    199     41       C  
ATOM    266  C   ASN A  40       2.513  26.406  21.298  1.00 27.69           C  
ANISOU  266  C   ASN A  40     3125   3676   3720    191    206    -22       C  
ATOM    267  O   ASN A  40       1.875  25.787  22.152  1.00 31.05           O  
ANISOU  267  O   ASN A  40     3544   4098   4157    193    227    -11       O  
ATOM    268  CB  ASN A  40       0.408  27.558  20.458  1.00 28.19           C  
ANISOU  268  CB  ASN A  40     3066   3789   3858    251    255    125       C  
ATOM    269  CG  ASN A  40       0.357  28.431  21.696  1.00 39.68           C  
ANISOU  269  CG  ASN A  40     4580   5178   5318    309    348    122       C  
ATOM    270  OD1 ASN A  40       1.395  28.862  22.215  1.00 39.17           O  
ANISOU  270  OD1 ASN A  40     4602   5060   5220    308    361     58       O  
ATOM    271  ND2 ASN A  40      -0.855  28.698  22.179  1.00 38.21           N  
ANISOU  271  ND2 ASN A  40     4351   4995   5173    359    415    198       N  
ATOM    272  N   ILE A  41       3.844  26.504  21.345  1.00 23.99           N  
ANISOU  272  N   ILE A  41     2715   3182   3219    175    187    -81       N  
ATOM    273  CA  ILE A  41       4.606  25.712  22.308  1.00 26.14           C  
ANISOU  273  CA  ILE A  41     3039   3429   3465    151    177   -133       C  
ATOM    274  C   ILE A  41       4.530  26.254  23.726  1.00 23.89           C  
ANISOU  274  C   ILE A  41     2813   3092   3173    175    235   -143       C  
ATOM    275  O   ILE A  41       5.040  25.615  24.655  1.00 29.17           O  
ANISOU  275  O   ILE A  41     3525   3741   3818    156    229   -178       O  
ATOM    276  CB  ILE A  41       6.099  25.590  21.926  1.00 27.72           C  
ANISOU  276  CB  ILE A  41     3272   3625   3636    125    137   -176       C  
ATOM    277  CG1 ILE A  41       6.744  26.964  21.728  1.00 28.72           C  
ANISOU  277  CG1 ILE A  41     3425   3725   3762    139    153   -174       C  
ATOM    278  CG2 ILE A  41       6.290  24.687  20.703  1.00 26.39           C  
ANISOU  278  CG2 ILE A  41     3070   3501   3457    103     85   -179       C  
ATOM    279  CD1 ILE A  41       8.237  26.888  21.470  1.00 26.54           C  
ANISOU  279  CD1 ILE A  41     3171   3447   3464    113    116   -200       C  
ATOM    280  N   LEU A  42       3.916  27.409  23.930  1.00 21.97           N  
ANISOU  280  N   LEU A  42     2581   2820   2946    219    294   -110       N  
ATOM    281  CA  LEU A  42       3.778  27.923  25.282  1.00 33.21           C  
ANISOU  281  CA  LEU A  42     4082   4184   4352    246    358   -122       C  
ATOM    282  C   LEU A  42       2.547  27.367  25.985  1.00 40.11           C  
ANISOU  282  C   LEU A  42     4927   5069   5246    277    408    -82       C  
ATOM    283  O   LEU A  42       2.309  27.706  27.146  1.00 45.15           O  
ANISOU  283  O   LEU A  42     5634   5658   5864    309    472    -86       O  
ATOM    284  CB  LEU A  42       3.736  29.454  25.256  1.00 39.44           C  
ANISOU  284  CB  LEU A  42     4920   4922   5144    286    412   -108       C  
ATOM    285  CG  LEU A  42       4.992  30.065  24.629  1.00 42.42           C  
ANISOU  285  CG  LEU A  42     5325   5285   5505    251    363   -140       C  
ATOM    286  CD1 LEU A  42       4.871  31.576  24.519  1.00 45.08           C  
ANISOU  286  CD1 LEU A  42     5711   5568   5851    288    416   -121       C  
ATOM    287  CD2 LEU A  42       6.227  29.672  25.434  1.00 42.37           C  
ANISOU  287  CD2 LEU A  42     5389   5254   5454    198    321   -198       C  
ATOM    288  N   LYS A  43       1.767  26.524  25.311  1.00 32.91           N  
ANISOU  288  N   LYS A  43     3920   4216   4368    266    378    -39       N  
ATOM    289  CA  LYS A  43       0.617  25.867  25.925  1.00 33.10           C  
ANISOU  289  CA  LYS A  43     3900   4257   4418    284    415     11       C  
ATOM    290  C   LYS A  43       1.060  24.572  26.597  1.00 37.30           C  
ANISOU  290  C   LYS A  43     4454   4792   4926    240    378    -32       C  
ATOM    291  O   LYS A  43       1.781  23.772  25.993  1.00 35.76           O  
ANISOU  291  O   LYS A  43     4250   4620   4718    188    304    -70       O  
ATOM    292  CB  LYS A  43      -0.454  25.584  24.872  1.00 41.23           C  
ANISOU  292  CB  LYS A  43     4815   5352   5500    278    389     88       C  
ATOM    293  CG  LYS A  43      -1.793  25.155  25.443  1.00 48.55           C  
ANISOU  293  CG  LYS A  43     5677   6301   6469    304    435    169       C  
ATOM    294  CD  LYS A  43      -2.897  25.344  24.407  1.00 59.48           C  
ANISOU  294  CD  LYS A  43     6946   7745   7908    307    419    268       C  
ATOM    295  CE  LYS A  43      -4.262  25.010  24.981  1.00 65.61           C  
ANISOU  295  CE  LYS A  43     7642   8549   8737    336    471    370       C  
ATOM    296  NZ  LYS A  43      -4.355  23.573  25.349  1.00 66.23           N  
ANISOU  296  NZ  LYS A  43     7704   8646   8814    274    419    356       N  
ATOM    297  N   SER A  44       0.624  24.369  27.843  1.00 31.25           N  
ANISOU  297  N   SER A  44     3721   4001   4153    266    436    -22       N  
ATOM    298  CA  SER A  44       1.028  23.196  28.612  1.00 35.52           C  
ANISOU  298  CA  SER A  44     4286   4540   4669    231    410    -57       C  
ATOM    299  C   SER A  44       0.554  21.907  27.960  1.00 32.87           C  
ANISOU  299  C   SER A  44     3867   4256   4368    185    350    -31       C  
ATOM    300  O   SER A  44      -0.623  21.762  27.628  1.00 34.33           O  
ANISOU  300  O   SER A  44     3972   4474   4599    193    362     41       O  
ATOM    301  CB  SER A  44       0.467  23.286  30.028  1.00 37.66           C  
ANISOU  301  CB  SER A  44     4604   4778   4925    275    494    -37       C  
ATOM    302  OG  SER A  44       1.098  24.339  30.731  1.00 55.42           O  
ANISOU  302  OG  SER A  44     6964   6968   7124    302    537    -79       O  
ATOM    303  N   ILE A  45       1.466  20.946  27.821  1.00 26.34           N  
ANISOU  303  N   ILE A  45     3061   3430   3517    135    287    -84       N  
ATOM    304  CA  ILE A  45       1.127  19.660  27.231  1.00 27.54           C  
ANISOU  304  CA  ILE A  45     3161   3614   3691     87    229    -71       C  
ATOM    305  C   ILE A  45       2.178  18.667  27.695  1.00 28.14           C  
ANISOU  305  C   ILE A  45     3289   3669   3733     56    197   -128       C  
ATOM    306  O   ILE A  45       3.307  19.047  28.017  1.00 26.98           O  
ANISOU  306  O   ILE A  45     3202   3501   3550     63    197   -175       O  
ATOM    307  CB  ILE A  45       1.051  19.757  25.685  1.00 29.06           C  
ANISOU  307  CB  ILE A  45     3308   3838   3894     59    171    -63       C  
ATOM    308  CG1 ILE A  45       0.503  18.456  25.093  1.00 34.12           C  
ANISOU  308  CG1 ILE A  45     3907   4504   4552      1    110    -44       C  
ATOM    309  CG2 ILE A  45       2.411  20.148  25.092  1.00 34.25           C  
ANISOU  309  CG2 ILE A  45     4016   4483   4514     55    142   -125       C  
ATOM    310  CD1 ILE A  45       0.062  18.572  23.654  1.00 38.71           C  
ANISOU  310  CD1 ILE A  45     4444   5122   5143    -30     54    -17       C  
ATOM    311  N   GLY A  46       1.797  17.396  27.763  1.00 29.77           N  
ANISOU  311  N   GLY A  46     3473   3885   3955     21    170   -117       N  
ATOM    312  CA  GLY A  46       2.746  16.378  28.187  1.00 28.59           C  
ANISOU  312  CA  GLY A  46     3369   3714   3780     -1    146   -161       C  
ATOM    313  C   GLY A  46       2.885  16.309  29.699  1.00 29.08           C  
ANISOU  313  C   GLY A  46     3470   3755   3824     21    193   -161       C  
ATOM    314  O   GLY A  46       2.059  16.836  30.462  1.00 28.40           O  
ANISOU  314  O   GLY A  46     3375   3667   3747     54    250   -124       O  
ATOM    315  N   ASP A  47       3.935  15.615  30.145  1.00 25.53           N  
ANISOU  315  N   ASP A  47     3064   3289   3347      8    174   -198       N  
ATOM    316  CA  ASP A  47       4.176  15.572  31.581  1.00 28.35           C  
ANISOU  316  CA  ASP A  47     3466   3629   3677     24    210   -198       C  
ATOM    317  C   ASP A  47       5.629  15.937  31.869  1.00 29.46           C  
ANISOU  317  C   ASP A  47     3663   3757   3774     21    189   -238       C  
ATOM    318  O   ASP A  47       6.081  17.001  31.427  1.00 27.47           O  
ANISOU  318  O   ASP A  47     3426   3503   3509     29    184   -255       O  
ATOM    319  CB  ASP A  47       3.738  14.215  32.185  1.00 27.20           C  
ANISOU  319  CB  ASP A  47     3306   3481   3549      7    212   -175       C  
ATOM    320  CG  ASP A  47       4.416  13.014  31.553  1.00 31.38           C  
ANISOU  320  CG  ASP A  47     3835   4003   4084    -27    160   -197       C  
ATOM    321  OD1 ASP A  47       5.505  12.633  32.046  1.00 32.65           O  
ANISOU  321  OD1 ASP A  47     4034   4152   4218    -26    151   -218       O  
ATOM    322  OD2 ASP A  47       3.849  12.424  30.599  1.00 30.96           O  
ANISOU  322  OD2 ASP A  47     3748   3954   4061    -55    131   -188       O  
ATOM    323  N   CYS A  48       6.368  15.117  32.613  1.00 26.11           N  
ANISOU  323  N   CYS A  48     3266   3326   3330      9    176   -245       N  
ATOM    324  CA  CYS A  48       7.708  15.500  33.041  1.00 25.55           C  
ANISOU  324  CA  CYS A  48     3239   3250   3218      1    153   -265       C  
ATOM    325  C   CYS A  48       8.796  14.962  32.115  1.00 29.74           C  
ANISOU  325  C   CYS A  48     3749   3791   3760    -12    108   -275       C  
ATOM    326  O   CYS A  48       8.675  13.881  31.527  1.00 27.20           O  
ANISOU  326  O   CYS A  48     3402   3470   3465    -16     98   -272       O  
ATOM    327  CB  CYS A  48       7.989  15.021  34.470  1.00 26.46           C  
ANISOU  327  CB  CYS A  48     3397   3358   3300     -4    163   -255       C  
ATOM    328  SG  CYS A  48       7.239  16.075  35.689  1.00 33.72           S  
ANISOU  328  SG  CYS A  48     4381   4256   4175     18    220   -252       S  
ATOM    329  N   ILE A  49       9.876  15.736  32.011  1.00 24.13           N  
ANISOU  329  N   ILE A  49     3056   3085   3028    -19     84   -282       N  
ATOM    330  CA  ILE A  49      11.094  15.349  31.308  1.00 25.00           C  
ANISOU  330  CA  ILE A  49     3145   3207   3145    -23     51   -277       C  
ATOM    331  C   ILE A  49      12.235  15.373  32.312  1.00 24.17           C  
ANISOU  331  C   ILE A  49     3064   3109   3012    -41     27   -256       C  
ATOM    332  O   ILE A  49      12.297  16.273  33.155  1.00 27.33           O  
ANISOU  332  O   ILE A  49     3506   3502   3377    -59     22   -260       O  
ATOM    333  CB  ILE A  49      11.404  16.313  30.138  1.00 31.10           C  
ANISOU  333  CB  ILE A  49     3902   3989   3926    -19     39   -285       C  
ATOM    334  CG1 ILE A  49      10.504  16.041  28.939  1.00 46.77           C  
ANISOU  334  CG1 ILE A  49     5858   5976   5936     -6     49   -297       C  
ATOM    335  CG2 ILE A  49      12.865  16.197  29.706  1.00 42.96           C  
ANISOU  335  CG2 ILE A  49     5387   5507   5429    -20     12   -265       C  
ATOM    336  CD1 ILE A  49      11.267  15.580  27.705  1.00 55.84           C  
ANISOU  336  CD1 ILE A  49     6990   7134   7093      4     35   -297       C  
ATOM    337  N   GLY A  50      13.150  14.405  32.210  1.00 25.25           N  
ANISOU  337  N   GLY A  50     3177   3256   3159    -36     12   -231       N  
ATOM    338  CA  GLY A  50      14.369  14.397  33.001  1.00 24.67           C  
ANISOU  338  CA  GLY A  50     3107   3200   3066    -56    -20   -193       C  
ATOM    339  C   GLY A  50      15.574  14.778  32.159  1.00 27.99           C  
ANISOU  339  C   GLY A  50     3491   3642   3502    -55    -45   -165       C  
ATOM    340  O   GLY A  50      15.634  14.483  30.961  1.00 29.75           O  
ANISOU  340  O   GLY A  50     3685   3866   3753    -25    -27   -169       O  
ATOM    341  N   LEU A  51      16.541  15.431  32.797  1.00 31.06           N  
ANISOU  341  N   LEU A  51     3883   4049   3870    -91    -88   -131       N  
ATOM    342  CA  LEU A  51      17.818  15.746  32.168  1.00 25.40           C  
ANISOU  342  CA  LEU A  51     3118   3360   3173    -96   -117    -82       C  
ATOM    343  C   LEU A  51      18.932  15.277  33.094  1.00 24.11           C  
ANISOU  343  C   LEU A  51     2933   3226   3003   -120   -156    -12       C  
ATOM    344  O   LEU A  51      18.946  15.615  34.289  1.00 28.61           O  
ANISOU  344  O   LEU A  51     3545   3795   3531   -169   -193     -8       O  
ATOM    345  CB  LEU A  51      17.947  17.247  31.893  1.00 27.59           C  
ANISOU  345  CB  LEU A  51     3411   3633   3437   -131   -145    -94       C  
ATOM    346  CG  LEU A  51      16.943  17.786  30.871  1.00 31.80           C  
ANISOU  346  CG  LEU A  51     3955   4146   3983   -103   -107   -148       C  
ATOM    347  CD1 LEU A  51      17.142  19.263  30.646  1.00 34.87           C  
ANISOU  347  CD1 LEU A  51     4361   4527   4362   -136   -132   -154       C  
ATOM    348  CD2 LEU A  51      17.085  17.030  29.573  1.00 35.22           C  
ANISOU  348  CD2 LEU A  51     4339   4590   4452    -53    -76   -140       C  
ATOM    349  N   GLN A  52      19.843  14.476  32.555  1.00 26.09           N  
ANISOU  349  N   GLN A  52     3120   3500   3291    -84   -144     49       N  
ATOM    350  CA  GLN A  52      20.947  13.948  33.335  1.00 27.80           C  
ANISOU  350  CA  GLN A  52     3298   3752   3512    -99   -177    135       C  
ATOM    351  C   GLN A  52      22.138  14.898  33.252  1.00 27.43           C  
ANISOU  351  C   GLN A  52     3206   3744   3472   -145   -236    204       C  
ATOM    352  O   GLN A  52      22.097  15.925  32.568  1.00 25.16           O  
ANISOU  352  O   GLN A  52     2922   3450   3187   -161   -246    180       O  
ATOM    353  CB  GLN A  52      21.286  12.534  32.865  1.00 24.78           C  
ANISOU  353  CB  GLN A  52     2874   3370   3170    -27   -123    175       C  
ATOM    354  CG  GLN A  52      20.122  11.576  33.066  1.00 36.79           C  
ANISOU  354  CG  GLN A  52     4444   4850   4684      1    -77    114       C  
ATOM    355  CD  GLN A  52      20.563  10.136  33.074  1.00 65.52           C  
ANISOU  355  CD  GLN A  52     8058   8483   8352     56    -35    165       C  
ATOM    356  OE1 GLN A  52      21.558   9.779  32.447  1.00 74.82           O  
ANISOU  356  OE1 GLN A  52     9188   9678   9564    100    -12    231       O  
ATOM    357  NE2 GLN A  52      19.835   9.297  33.796  1.00 79.33           N  
ANISOU  357  NE2 GLN A  52     9844  10207  10092     58    -18    142       N  
ATOM    358  N   SER A  53      23.207  14.559  33.983  1.00 23.65           N  
ANISOU  358  N   SER A  53     2681   3307   2999   -171   -281    298       N  
ATOM    359  CA  SER A  53      24.324  15.483  34.170  1.00 29.45           C  
ANISOU  359  CA  SER A  53     3372   4081   3735   -239   -359    376       C  
ATOM    360  C   SER A  53      25.021  15.839  32.858  1.00 26.95           C  
ANISOU  360  C   SER A  53     2983   3786   3473   -204   -336    423       C  
ATOM    361  O   SER A  53      25.588  16.933  32.739  1.00 30.76           O  
ANISOU  361  O   SER A  53     3448   4285   3956   -264   -393    456       O  
ATOM    362  CB  SER A  53      25.351  14.887  35.148  1.00 34.16           C  
ANISOU  362  CB  SER A  53     3917   4728   4335   -270   -412    488       C  
ATOM    363  OG  SER A  53      24.826  14.777  36.459  1.00 42.91           O  
ANISOU  363  OG  SER A  53     5100   5823   5381   -320   -449    453       O  
ATOM    364  N   ASN A  54      25.035  14.927  31.881  1.00 26.96           N  
ANISOU  364  N   ASN A  54     2946   3783   3515   -108   -252    432       N  
ATOM    365  CA  ASN A  54      25.650  15.275  30.600  1.00 31.02           C  
ANISOU  365  CA  ASN A  54     3401   4314   4071    -66   -220    475       C  
ATOM    366  C   ASN A  54      24.901  16.426  29.941  1.00 32.84           C  
ANISOU  366  C   ASN A  54     3681   4513   4282    -90   -224    387       C  
ATOM    367  O   ASN A  54      25.509  17.251  29.243  1.00 29.72           O  
ANISOU  367  O   ASN A  54     3243   4139   3910   -102   -237    429       O  
ATOM    368  CB  ASN A  54      25.725  14.053  29.663  1.00 27.92           C  
ANISOU  368  CB  ASN A  54     2987   3911   3712     46   -120    490       C  
ATOM    369  CG  ASN A  54      24.389  13.332  29.497  1.00 28.02           C  
ANISOU  369  CG  ASN A  54     3084   3864   3697     84    -67    374       C  
ATOM    370  OD1 ASN A  54      23.719  12.989  30.481  1.00 28.49           O  
ANISOU  370  OD1 ASN A  54     3190   3905   3729     53    -88    331       O  
ATOM    371  ND2 ASN A  54      24.010  13.065  28.241  1.00 25.79           N  
ANISOU  371  ND2 ASN A  54     2825   3554   3422    150      1    330       N  
ATOM    372  N   ALA A  55      23.589  16.520  30.180  1.00 27.63           N  
ANISOU  372  N   ALA A  55     3108   3808   3584    -98   -211    274       N  
ATOM    373  CA  ALA A  55      22.836  17.655  29.667  1.00 26.26           C  
ANISOU  373  CA  ALA A  55     2980   3605   3392   -121   -215    200       C  
ATOM    374  C   ALA A  55      22.967  18.877  30.571  1.00 28.38           C  
ANISOU  374  C   ALA A  55     3286   3868   3628   -216   -293    197       C  
ATOM    375  O   ALA A  55      23.124  20.001  30.073  1.00 24.86           O  
ANISOU  375  O   ALA A  55     2842   3417   3187   -246   -315    196       O  
ATOM    376  CB  ALA A  55      21.368  17.270  29.482  1.00 26.23           C  
ANISOU  376  CB  ALA A  55     3042   3557   3367    -86   -165     97       C  
ATOM    377  N   THR A  56      22.914  18.698  31.900  1.00 23.91           N  
ANISOU  377  N   THR A  56     2763   3299   3024   -266   -336    197       N  
ATOM    378  CA  THR A  56      22.961  19.885  32.753  1.00 26.03           C  
ANISOU  378  CA  THR A  56     3096   3547   3245   -359   -408    183       C  
ATOM    379  C   THR A  56      24.324  20.564  32.681  1.00 24.20           C  
ANISOU  379  C   THR A  56     2805   3355   3036   -425   -483    281       C  
ATOM    380  O   THR A  56      24.407  21.783  32.828  1.00 28.92           O  
ANISOU  380  O   THR A  56     3451   3927   3610   -496   -534    267       O  
ATOM    381  CB  THR A  56      22.605  19.551  34.216  1.00 27.66           C  
ANISOU  381  CB  THR A  56     3375   3740   3393   -400   -438    161       C  
ATOM    382  OG1 THR A  56      23.611  18.719  34.790  1.00 31.73           O  
ANISOU  382  OG1 THR A  56     3828   4307   3921   -415   -478    255       O  
ATOM    383  CG2 THR A  56      21.260  18.848  34.307  1.00 30.57           C  
ANISOU  383  CG2 THR A  56     3792   4076   3748   -336   -363     78       C  
ATOM    384  N   ARG A  57      25.404  19.816  32.441  1.00 27.81           N  
ANISOU  384  N   ARG A  57     3156   3868   3541   -402   -488    388       N  
ATOM    385  CA  ARG A  57      26.688  20.496  32.337  1.00 27.21           C  
ANISOU  385  CA  ARG A  57     3009   3835   3495   -467   -560    498       C  
ATOM    386  C   ARG A  57      26.744  21.377  31.091  1.00 28.31           C  
ANISOU  386  C   ARG A  57     3122   3966   3669   -449   -534    492       C  
ATOM    387  O   ARG A  57      27.433  22.407  31.096  1.00 29.13           O  
ANISOU  387  O   ARG A  57     3210   4077   3781   -529   -604    544       O  
ATOM    388  CB  ARG A  57      27.853  19.501  32.375  1.00 39.53           C  
ANISOU  388  CB  ARG A  57     4449   5464   5105   -438   -564    634       C  
ATOM    389  CG  ARG A  57      28.055  18.604  31.174  1.00 48.26           C  
ANISOU  389  CG  ARG A  57     5474   6590   6272   -315   -461    670       C  
ATOM    390  CD  ARG A  57      29.269  17.711  31.430  1.00 49.05           C  
ANISOU  390  CD  ARG A  57     5463   6756   6420   -291   -468    820       C  
ATOM    391  NE  ARG A  57      30.322  18.495  32.055  1.00 55.16           N  
ANISOU  391  NE  ARG A  57     6180   7577   7201   -403   -581    931       N  
ATOM    392  CZ  ARG A  57      31.238  18.009  32.885  1.00 58.29           C  
ANISOU  392  CZ  ARG A  57     6505   8031   7613   -441   -640   1056       C  
ATOM    393  NH1 ARG A  57      31.243  16.718  33.205  1.00 56.34           N  
ANISOU  393  NH1 ARG A  57     6233   7797   7376   -367   -587   1085       N  
ATOM    394  NH2 ARG A  57      32.150  18.824  33.401  1.00 53.30           N  
ANISOU  394  NH2 ARG A  57     5827   7440   6984   -559   -757   1157       N  
ATOM    395  N   ILE A  58      25.995  21.023  30.043  1.00 25.35           N  
ANISOU  395  N   ILE A  58     2750   3571   3311   -353   -441    428       N  
ATOM    396  CA  ILE A  58      25.870  21.895  28.876  1.00 23.84           C  
ANISOU  396  CA  ILE A  58     2550   3367   3143   -334   -413    410       C  
ATOM    397  C   ILE A  58      25.022  23.115  29.214  1.00 25.27           C  
ANISOU  397  C   ILE A  58     2834   3489   3279   -395   -444    319       C  
ATOM    398  O   ILE A  58      25.398  24.257  28.923  1.00 27.24           O  
ANISOU  398  O   ILE A  58     3084   3730   3538   -449   -483    341       O  
ATOM    399  CB  ILE A  58      25.269  21.100  27.701  1.00 23.96           C  
ANISOU  399  CB  ILE A  58     2550   3378   3177   -219   -311    367       C  
ATOM    400  CG1 ILE A  58      26.308  20.093  27.178  1.00 25.32           C  
ANISOU  400  CG1 ILE A  58     2624   3601   3396   -151   -270    473       C  
ATOM    401  CG2 ILE A  58      24.748  22.041  26.598  1.00 29.06           C  
ANISOU  401  CG2 ILE A  58     3215   4000   3827   -201   -282    319       C  
ATOM    402  CD1 ILE A  58      25.704  19.048  26.237  1.00 24.42           C  
ANISOU  402  CD1 ILE A  58     2525   3470   3284    -42   -171    424       C  
ATOM    403  N   ILE A  59      23.860  22.890  29.828  1.00 25.46           N  
ANISOU  403  N   ILE A  59     2948   3470   3256   -384   -420    221       N  
ATOM    404  CA  ILE A  59      22.936  23.979  30.138  1.00 30.21           C  
ANISOU  404  CA  ILE A  59     3654   4009   3815   -421   -426    136       C  
ATOM    405  C   ILE A  59      23.584  24.993  31.069  1.00 28.65           C  
ANISOU  405  C   ILE A  59     3510   3791   3583   -535   -519    164       C  
ATOM    406  O   ILE A  59      23.333  26.201  30.956  1.00 28.02           O  
ANISOU  406  O   ILE A  59     3495   3663   3487   -576   -534    130       O  
ATOM    407  CB  ILE A  59      21.644  23.390  30.734  1.00 26.44           C  
ANISOU  407  CB  ILE A  59     3250   3497   3298   -382   -377     48       C  
ATOM    408  CG1 ILE A  59      20.895  22.606  29.650  1.00 24.34           C  
ANISOU  408  CG1 ILE A  59     2943   3241   3065   -285   -295     15       C  
ATOM    409  CG2 ILE A  59      20.774  24.487  31.348  1.00 27.94           C  
ANISOU  409  CG2 ILE A  59     3558   3621   3437   -420   -381    -26       C  
ATOM    410  CD1 ILE A  59      19.767  21.742  30.161  1.00 26.78           C  
ANISOU  410  CD1 ILE A  59     3295   3530   3350   -246   -251    -47       C  
ATOM    411  N   LYS A  60      24.447  24.528  31.980  1.00 26.06           N  
ANISOU  411  N   LYS A  60     3161   3498   3242   -593   -586    231       N  
ATOM    412  CA  LYS A  60      25.089  25.420  32.948  1.00 29.97           C  
ANISOU  412  CA  LYS A  60     3719   3975   3695   -718   -691    261       C  
ATOM    413  C   LYS A  60      25.934  26.500  32.286  1.00 30.06           C  
ANISOU  413  C   LYS A  60     3689   3990   3744   -779   -742    324       C  
ATOM    414  O   LYS A  60      26.135  27.565  32.878  1.00 30.66           O  
ANISOU  414  O   LYS A  60     3852   4019   3776   -883   -817    316       O  
ATOM    415  CB  LYS A  60      25.949  24.597  33.905  1.00 34.04           C  
ANISOU  415  CB  LYS A  60     4192   4543   4198   -765   -758    344       C  
ATOM    416  CG  LYS A  60      26.443  25.373  35.122  1.00 56.27           C  
ANISOU  416  CG  LYS A  60     7099   7335   6944   -905   -875    362       C  
ATOM    417  CD  LYS A  60      27.277  24.503  36.062  1.00 67.05           C  
ANISOU  417  CD  LYS A  60     8415   8764   8299   -952   -946    454       C  
ATOM    418  CE  LYS A  60      27.380  25.132  37.457  1.00 75.30           C  
ANISOU  418  CE  LYS A  60     9597   9770   9243  -1083  -1051    436       C  
ATOM    419  NZ  LYS A  60      27.890  26.536  37.421  1.00 75.40           N  
ANISOU  419  NZ  LYS A  60     9669   9742   9237  -1202  -1140    450       N  
ATOM    420  N   ARG A  61      26.440  26.257  31.075  1.00 28.96           N  
ANISOU  420  N   ARG A  61     3425   3899   3678   -717   -702    389       N  
ATOM    421  CA  ARG A  61      27.254  27.262  30.403  1.00 29.89           C  
ANISOU  421  CA  ARG A  61     3494   4026   3839   -770   -746    460       C  
ATOM    422  C   ARG A  61      26.424  28.381  29.799  1.00 34.65           C  
ANISOU  422  C   ARG A  61     4176   4559   4431   -760   -708    374       C  
ATOM    423  O   ARG A  61      26.961  29.468  29.550  1.00 34.90           O  
ANISOU  423  O   ARG A  61     4211   4572   4479   -833   -760    414       O  
ATOM    424  CB  ARG A  61      28.091  26.627  29.287  1.00 34.98           C  
ANISOU  424  CB  ARG A  61     3980   4747   4565   -697   -703    566       C  
ATOM    425  CG  ARG A  61      28.934  25.454  29.718  1.00 34.81           C  
ANISOU  425  CG  ARG A  61     3864   4796   4568   -682   -719    666       C  
ATOM    426  CD  ARG A  61      29.956  25.078  28.644  1.00 38.60           C  
ANISOU  426  CD  ARG A  61     4191   5347   5130   -620   -681    795       C  
ATOM    427  NE  ARG A  61      30.749  23.934  29.077  1.00 37.55           N  
ANISOU  427  NE  ARG A  61     3967   5279   5024   -595   -685    899       N  
ATOM    428  CZ  ARG A  61      30.499  22.676  28.725  1.00 35.51           C  
ANISOU  428  CZ  ARG A  61     3677   5036   4777   -476   -590    889       C  
ATOM    429  NH1 ARG A  61      29.491  22.403  27.902  1.00 31.07           N  
ANISOU  429  NH1 ARG A  61     3168   4434   4202   -380   -493    780       N  
ATOM    430  NH2 ARG A  61      31.273  21.700  29.178  1.00 42.05           N  
ANISOU  430  NH2 ARG A  61     4425   5920   5634   -455   -595    995       N  
ATOM    431  N   TRP A  62      25.145  28.134  29.538  1.00 30.05           N  
ANISOU  431  N   TRP A  62     3650   3940   3826   -674   -620    269       N  
ATOM    432  CA  TRP A  62      24.323  29.087  28.803  1.00 28.11           C  
ANISOU  432  CA  TRP A  62     3458   3640   3583   -644   -570    203       C  
ATOM    433  C   TRP A  62      24.077  30.350  29.612  1.00 32.34           C  
ANISOU  433  C   TRP A  62     4131   4092   4065   -736   -620    156       C  
ATOM    434  O   TRP A  62      23.814  30.297  30.820  1.00 35.15           O  
ANISOU  434  O   TRP A  62     4588   4412   4356   -784   -652    114       O  
ATOM    435  CB  TRP A  62      22.974  28.472  28.440  1.00 27.68           C  
ANISOU  435  CB  TRP A  62     3428   3572   3517   -537   -473    113       C  
ATOM    436  CG  TRP A  62      23.041  27.300  27.549  1.00 24.61           C  
ANISOU  436  CG  TRP A  62     2935   3245   3169   -445   -416    140       C  
ATOM    437  CD1 TRP A  62      24.119  26.864  26.824  1.00 29.02           C  
ANISOU  437  CD1 TRP A  62     3382   3867   3779   -426   -420    234       C  
ATOM    438  CD2 TRP A  62      21.977  26.387  27.283  1.00 25.57           C  
ANISOU  438  CD2 TRP A  62     3065   3368   3283   -359   -342     76       C  
ATOM    439  NE1 TRP A  62      23.784  25.730  26.117  1.00 28.59           N  
ANISOU  439  NE1 TRP A  62     3279   3843   3740   -329   -348    223       N  
ATOM    440  CE2 TRP A  62      22.471  25.421  26.374  1.00 28.24           C  
ANISOU  440  CE2 TRP A  62     3308   3762   3661   -293   -306    125       C  
ATOM    441  CE3 TRP A  62      20.650  26.300  27.712  1.00 28.77           C  
ANISOU  441  CE3 TRP A  62     3548   3730   3652   -331   -301    -12       C  
ATOM    442  CZ2 TRP A  62      21.687  24.376  25.896  1.00 29.42           C  
ANISOU  442  CZ2 TRP A  62     3450   3918   3808   -213   -242     81       C  
ATOM    443  CZ3 TRP A  62      19.864  25.257  27.233  1.00 29.14           C  
ANISOU  443  CZ3 TRP A  62     3570   3794   3707   -253   -240    -46       C  
ATOM    444  CH2 TRP A  62      20.390  24.304  26.336  1.00 26.60           C  
ANISOU  444  CH2 TRP A  62     3165   3522   3419   -201   -216     -3       C  
ATOM    445  N   GLY A  63      24.149  31.486  28.926  1.00 32.27           N  
ANISOU  445  N   GLY A  63     4134   4048   4079   -756   -622    163       N  
ATOM    446  CA  GLY A  63      23.844  32.762  29.561  1.00 34.02           C  
ANISOU  446  CA  GLY A  63     4503   4173   4251   -834   -654    112       C  
ATOM    447  C   GLY A  63      24.556  32.974  30.875  1.00 36.17           C  
ANISOU  447  C   GLY A  63     4856   4421   4465   -963   -762    134       C  
ATOM    448  O   GLY A  63      23.959  33.485  31.831  1.00 36.84           O  
ANISOU  448  O   GLY A  63     5101   4423   4474  -1001   -768     58       O  
ATOM    449  N   ASP A  64      25.822  32.566  30.954  1.00 35.92           N  
ANISOU  449  N   ASP A  64     4720   4462   4467  -1028   -846    242       N  
ATOM    450  CA  ASP A  64      26.638  32.755  32.150  1.00 35.90           C  
ANISOU  450  CA  ASP A  64     4778   4450   4413  -1167   -969    284       C  
ATOM    451  C   ASP A  64      26.000  32.123  33.378  1.00 35.43           C  
ANISOU  451  C   ASP A  64     4825   4367   4269  -1163   -963    211       C  
ATOM    452  O   ASP A  64      26.140  32.630  34.492  1.00 34.82           O  
ANISOU  452  O   ASP A  64     4885   4234   4111  -1271  -1042    189       O  
ATOM    453  CB  ASP A  64      26.911  34.239  32.401  1.00 44.64           C  
ANISOU  453  CB  ASP A  64     6006   5467   5489  -1290  -1043    277       C  
ATOM    454  CG  ASP A  64      27.383  34.951  31.158  1.00 50.83           C  
ANISOU  454  CG  ASP A  64     6695   6263   6356  -1285  -1035    341       C  
ATOM    455  OD1 ASP A  64      28.482  34.614  30.670  1.00 49.87           O  
ANISOU  455  OD1 ASP A  64     6417   6229   6304  -1310  -1083    465       O  
ATOM    456  OD2 ASP A  64      26.641  35.819  30.648  1.00 54.79           O  
ANISOU  456  OD2 ASP A  64     7272   6690   6856  -1247   -972    273       O  
ATOM    457  N   GLY A  65      25.298  31.004  33.188  1.00 32.01           N  
ANISOU  457  N   GLY A  65     4338   3975   3850  -1042   -872    175       N  
ATOM    458  CA  GLY A  65      24.676  30.303  34.290  1.00 34.14           C  
ANISOU  458  CA  GLY A  65     4691   4231   4048  -1028   -858    116       C  
ATOM    459  C   GLY A  65      23.227  30.659  34.551  1.00 35.32           C  
ANISOU  459  C   GLY A  65     4979   4296   4143   -962   -765     -6       C  
ATOM    460  O   GLY A  65      22.620  30.076  35.464  1.00 36.13           O  
ANISOU  460  O   GLY A  65     5153   4386   4187   -940   -740    -54       O  
ATOM    461  N   ALA A  66      22.647  31.573  33.764  1.00 35.52           N  
ANISOU  461  N   ALA A  66     5037   4268   4192   -924   -707    -48       N  
ATOM    462  CA  ALA A  66      21.320  32.104  34.072  1.00 36.44           C  
ANISOU  462  CA  ALA A  66     5293   4297   4258   -869   -620   -149       C  
ATOM    463  C   ALA A  66      20.230  31.053  33.895  1.00 32.51           C  
ANISOU  463  C   ALA A  66     4744   3832   3775   -744   -518   -189       C  
ATOM    464  O   ALA A  66      19.274  31.012  34.675  1.00 34.66           O  
ANISOU  464  O   ALA A  66     5124   4055   3989   -710   -463   -254       O  
ATOM    465  CB  ALA A  66      21.025  33.320  33.195  1.00 39.13           C  
ANISOU  465  CB  ALA A  66     5661   4577   4629   -854   -583   -166       C  
ATOM    466  N   VAL A  67      20.349  30.210  32.869  1.00 27.24           N  
ANISOU  466  N   VAL A  67     3920   3245   3185   -675   -489   -150       N  
ATOM    467  CA  VAL A  67      19.341  29.176  32.643  1.00 26.47           C  
ANISOU  467  CA  VAL A  67     3775   3177   3104   -570   -403   -184       C  
ATOM    468  C   VAL A  67      19.369  28.146  33.766  1.00 28.21           C  
ANISOU  468  C   VAL A  67     4017   3422   3281   -582   -421   -185       C  
ATOM    469  O   VAL A  67      18.319  27.704  34.253  1.00 29.08           O  
ANISOU  469  O   VAL A  67     4175   3512   3363   -526   -357   -236       O  
ATOM    470  CB  VAL A  67      19.557  28.525  31.268  1.00 26.03           C  
ANISOU  470  CB  VAL A  67     3567   3193   3130   -505   -375   -142       C  
ATOM    471  CG1 VAL A  67      18.510  27.443  31.010  1.00 24.10           C  
ANISOU  471  CG1 VAL A  67     3283   2974   2901   -410   -298   -177       C  
ATOM    472  CG2 VAL A  67      19.510  29.589  30.179  1.00 32.22           C  
ANISOU  472  CG2 VAL A  67     4335   3955   3952   -494   -357   -137       C  
ATOM    473  N   HIS A  68      20.566  27.735  34.185  1.00 26.60           N  
ANISOU  473  N   HIS A  68     3768   3263   3074   -653   -508   -120       N  
ATOM    474  CA  HIS A  68      20.667  26.822  35.321  1.00 28.62           C  
ANISOU  474  CA  HIS A  68     4049   3542   3285   -672   -534   -113       C  
ATOM    475  C   HIS A  68      20.059  27.431  36.580  1.00 32.54           C  
ANISOU  475  C   HIS A  68     4721   3961   3683   -712   -534   -177       C  
ATOM    476  O   HIS A  68      19.400  26.734  37.361  1.00 34.96           O  
ANISOU  476  O   HIS A  68     5070   4265   3948   -677   -495   -208       O  
ATOM    477  CB  HIS A  68      22.130  26.452  35.568  1.00 35.80           C  
ANISOU  477  CB  HIS A  68     4881   4513   4208   -751   -636    -15       C  
ATOM    478  CG  HIS A  68      22.339  25.649  36.812  1.00 38.19           C  
ANISOU  478  CG  HIS A  68     5215   4837   4456   -786   -677      2       C  
ATOM    479  ND1 HIS A  68      21.835  24.375  36.967  1.00 43.62           N  
ANISOU  479  ND1 HIS A  68     5857   5560   5158   -707   -619     -5       N  
ATOM    480  CD2 HIS A  68      22.982  25.944  37.967  1.00 40.32           C  
ANISOU  480  CD2 HIS A  68     5566   5098   4655   -894   -773     28       C  
ATOM    481  CE1 HIS A  68      22.168  23.916  38.161  1.00 43.86           C  
ANISOU  481  CE1 HIS A  68     5931   5605   5131   -760   -672     19       C  
ATOM    482  NE2 HIS A  68      22.865  24.848  38.786  1.00 42.50           N  
ANISOU  482  NE2 HIS A  68     5837   5409   4903   -874   -769     40       N  
ATOM    483  N   GLU A  69      20.274  28.728  36.803  1.00 32.23           N  
ANISOU  483  N   GLU A  69     4792   3854   3601   -785   -574   -196       N  
ATOM    484  CA  GLU A  69      19.671  29.364  37.973  1.00 37.46           C  
ANISOU  484  CA  GLU A  69     5646   4428   4158   -817   -562   -262       C  
ATOM    485  C   GLU A  69      18.149  29.308  37.903  1.00 33.30           C  
ANISOU  485  C   GLU A  69     5166   3861   3627   -700   -429   -333       C  
ATOM    486  O   GLU A  69      17.482  29.027  38.905  1.00 34.56           O  
ANISOU  486  O   GLU A  69     5424   3990   3717   -678   -389   -371       O  
ATOM    487  CB  GLU A  69      20.157  30.807  38.108  1.00 39.14           C  
ANISOU  487  CB  GLU A  69     5981   4563   4328   -915   -624   -273       C  
ATOM    488  CG  GLU A  69      21.565  30.914  38.658  1.00 51.33           C  
ANISOU  488  CG  GLU A  69     7527   6134   5843  -1057   -771   -204       C  
ATOM    489  CD  GLU A  69      21.766  30.080  39.919  1.00 59.68           C  
ANISOU  489  CD  GLU A  69     8630   7221   6826  -1098   -819   -194       C  
ATOM    490  OE1 GLU A  69      20.940  30.193  40.856  1.00 58.43           O  
ANISOU  490  OE1 GLU A  69     8629   6998   6575  -1079   -770   -265       O  
ATOM    491  OE2 GLU A  69      22.749  29.301  39.967  1.00 52.67           O  
ANISOU  491  OE2 GLU A  69     7619   6422   5971  -1143   -900   -106       O  
ATOM    492  N   ALA A  70      17.586  29.552  36.721  1.00 32.07           N  
ANISOU  492  N   ALA A  70     4933   3707   3545   -623   -361   -340       N  
ATOM    493  CA  ALA A  70      16.144  29.445  36.548  1.00 26.13           C  
ANISOU  493  CA  ALA A  70     4195   2929   2803   -513   -240   -386       C  
ATOM    494  C   ALA A  70      15.650  28.026  36.804  1.00 31.36           C  
ANISOU  494  C   ALA A  70     4781   3653   3481   -454   -203   -379       C  
ATOM    495  O   ALA A  70      14.517  27.839  37.257  1.00 34.28           O  
ANISOU  495  O   ALA A  70     5201   3996   3828   -388   -119   -411       O  
ATOM    496  CB  ALA A  70      15.751  29.899  35.140  1.00 31.60           C  
ANISOU  496  CB  ALA A  70     4800   3629   3577   -453   -191   -380       C  
ATOM    497  N   LEU A  71      16.468  27.016  36.510  1.00 30.30           N  
ANISOU  497  N   LEU A  71     4524   3598   3389   -473   -260   -329       N  
ATOM    498  CA  LEU A  71      16.037  25.631  36.653  1.00 30.03           C  
ANISOU  498  CA  LEU A  71     4416   3616   3377   -418   -226   -319       C  
ATOM    499  C   LEU A  71      16.373  25.049  38.019  1.00 31.69           C  
ANISOU  499  C   LEU A  71     4690   3833   3518   -463   -266   -311       C  
ATOM    500  O   LEU A  71      16.022  23.892  38.287  1.00 29.93           O  
ANISOU  500  O   LEU A  71     4417   3648   3308   -422   -237   -301       O  
ATOM    501  CB  LEU A  71      16.661  24.770  35.548  1.00 27.42           C  
ANISOU  501  CB  LEU A  71     3927   3360   3130   -398   -248   -270       C  
ATOM    502  CG  LEU A  71      16.165  25.184  34.158  1.00 28.49           C  
ANISOU  502  CG  LEU A  71     4000   3497   3329   -342   -200   -280       C  
ATOM    503  CD1 LEU A  71      16.883  24.436  33.050  1.00 25.57           C  
ANISOU  503  CD1 LEU A  71     3497   3191   3026   -324   -220   -233       C  
ATOM    504  CD2 LEU A  71      14.649  24.990  34.043  1.00 31.74           C  
ANISOU  504  CD2 LEU A  71     4423   3888   3749   -263   -107   -321       C  
ATOM    505  N   ARG A  72      17.005  25.831  38.891  1.00 30.66           N  
ANISOU  505  N   ARG A  72     4676   3662   3311   -550   -332   -315       N  
ATOM    506  CA  ARG A  72      17.429  25.325  40.192  1.00 30.58           C  
ANISOU  506  CA  ARG A  72     4732   3663   3226   -606   -384   -300       C  
ATOM    507  C   ARG A  72      16.310  24.684  41.009  1.00 31.19           C  
ANISOU  507  C   ARG A  72     4866   3724   3261   -539   -300   -334       C  
ATOM    508  O   ARG A  72      16.582  23.668  41.673  1.00 30.28           O  
ANISOU  508  O   ARG A  72     4722   3654   3129   -548   -326   -303       O  
ATOM    509  CB  ARG A  72      18.098  26.464  40.979  1.00 33.14           C  
ANISOU  509  CB  ARG A  72     5206   3929   3459   -716   -466   -310       C  
ATOM    510  CG  ARG A  72      18.669  26.004  42.301  1.00 41.82           C  
ANISOU  510  CG  ARG A  72     6376   5044   4470   -791   -541   -286       C  
ATOM    511  CD  ARG A  72      19.508  27.089  42.981  1.00 52.42           C  
ANISOU  511  CD  ARG A  72     7860   6335   5724   -925   -649   -286       C  
ATOM    512  NE  ARG A  72      20.750  27.384  42.265  1.00 53.72           N  
ANISOU  512  NE  ARG A  72     7919   6543   5950  -1006   -754   -215       N  
ATOM    513  CZ  ARG A  72      21.832  26.606  42.281  1.00 58.63           C  
ANISOU  513  CZ  ARG A  72     8412   7254   6609  -1056   -843   -122       C  
ATOM    514  NH1 ARG A  72      21.828  25.467  42.965  1.00 63.67           N  
ANISOU  514  NH1 ARG A  72     9015   7947   7231  -1034   -843    -94       N  
ATOM    515  NH2 ARG A  72      22.919  26.960  41.605  1.00 59.20           N  
ANISOU  515  NH2 ARG A  72     8387   7365   6742  -1123   -928    -49       N  
ATOM    516  N   PRO A  73      15.066  25.190  41.017  1.00 32.93           N  
ANISOU  516  N   PRO A  73     5160   3886   3466   -468   -197   -387       N  
ATOM    517  CA  PRO A  73      14.008  24.507  41.788  1.00 32.81           C  
ANISOU  517  CA  PRO A  73     5182   3865   3421   -400   -113   -403       C  
ATOM    518  C   PRO A  73      13.761  23.083  41.357  1.00 31.12           C  
ANISOU  518  C   PRO A  73     4816   3723   3285   -347    -91   -368       C  
ATOM    519  O   PRO A  73      13.166  22.313  42.123  1.00 29.68           O  
ANISOU  519  O   PRO A  73     4650   3549   3077   -313    -47   -364       O  
ATOM    520  CB  PRO A  73      12.768  25.370  41.523  1.00 36.54           C  
ANISOU  520  CB  PRO A  73     5719   4271   3893   -324     -1   -445       C  
ATOM    521  CG  PRO A  73      13.309  26.715  41.201  1.00 39.65           C  
ANISOU  521  CG  PRO A  73     6193   4609   4265   -378    -41   -467       C  
ATOM    522  CD  PRO A  73      14.551  26.435  40.411  1.00 35.60           C  
ANISOU  522  CD  PRO A  73     5555   4159   3813   -444   -148   -424       C  
ATOM    523  N   TRP A  74      14.183  22.712  40.154  1.00 27.99           N  
ANISOU  523  N   TRP A  74     4280   3375   2979   -339   -117   -341       N  
ATOM    524  CA  TRP A  74      13.882  21.412  39.579  1.00 26.38           C  
ANISOU  524  CA  TRP A  74     3946   3226   2851   -286    -90   -314       C  
ATOM    525  C   TRP A  74      15.048  20.431  39.686  1.00 28.17           C  
ANISOU  525  C   TRP A  74     4097   3511   3096   -326   -165   -261       C  
ATOM    526  O   TRP A  74      14.976  19.335  39.117  1.00 28.50           O  
ANISOU  526  O   TRP A  74     4036   3592   3201   -286   -147   -237       O  
ATOM    527  CB  TRP A  74      13.456  21.585  38.119  1.00 27.59           C  
ANISOU  527  CB  TRP A  74     4008   3387   3087   -239    -55   -321       C  
ATOM    528  CG  TRP A  74      12.357  22.611  37.954  1.00 27.97           C  
ANISOU  528  CG  TRP A  74     4119   3383   3126   -196     19   -358       C  
ATOM    529  CD1 TRP A  74      12.500  23.914  37.549  1.00 27.99           C  
ANISOU  529  CD1 TRP A  74     4172   3344   3119   -212     14   -377       C  
ATOM    530  CD2 TRP A  74      10.955  22.418  38.197  1.00 27.76           C  
ANISOU  530  CD2 TRP A  74     4105   3338   3105   -127    111   -368       C  
ATOM    531  NE1 TRP A  74      11.269  24.540  37.523  1.00 30.07           N  
ANISOU  531  NE1 TRP A  74     4482   3563   3380   -151    104   -400       N  
ATOM    532  CE2 TRP A  74      10.307  23.641  37.911  1.00 29.85           C  
ANISOU  532  CE2 TRP A  74     4426   3553   3364    -97    165   -390       C  
ATOM    533  CE3 TRP A  74      10.182  21.322  38.610  1.00 27.41           C  
ANISOU  533  CE3 TRP A  74     4023   3317   3076    -87    156   -352       C  
ATOM    534  CZ2 TRP A  74       8.926  23.805  38.040  1.00 28.94           C  
ANISOU  534  CZ2 TRP A  74     4325   3414   3258    -24    265   -389       C  
ATOM    535  CZ3 TRP A  74       8.795  21.490  38.741  1.00 26.85           C  
ANISOU  535  CZ3 TRP A  74     3964   3222   3013    -22    250   -352       C  
ATOM    536  CH2 TRP A  74       8.192  22.722  38.462  1.00 28.06           C  
ANISOU  536  CH2 TRP A  74     4169   3332   3163     12    305   -367       C  
ATOM    537  N   ILE A  75      16.104  20.784  40.421  1.00 27.59           N  
ANISOU  537  N   ILE A  75     4076   3442   2966   -406   -248   -237       N  
ATOM    538  CA  ILE A  75      17.211  19.857  40.630  1.00 25.56           C  
ANISOU  538  CA  ILE A  75     3741   3244   2725   -441   -317   -169       C  
ATOM    539  C   ILE A  75      16.715  18.669  41.444  1.00 30.02           C  
ANISOU  539  C   ILE A  75     4305   3826   3275   -405   -281   -158       C  
ATOM    540  O   ILE A  75      16.057  18.839  42.481  1.00 30.73           O  
ANISOU  540  O   ILE A  75     4502   3884   3291   -406   -253   -188       O  
ATOM    541  CB  ILE A  75      18.386  20.565  41.326  1.00 29.42           C  
ANISOU  541  CB  ILE A  75     4290   3737   3152   -546   -424   -135       C  
ATOM    542  CG1 ILE A  75      18.966  21.647  40.419  1.00 33.26           C  
ANISOU  542  CG1 ILE A  75     4757   4211   3668   -583   -463   -132       C  
ATOM    543  CG2 ILE A  75      19.479  19.566  41.721  1.00 31.72           C  
ANISOU  543  CG2 ILE A  75     4499   4097   3457   -580   -493    -48       C  
ATOM    544  CD1 ILE A  75      19.972  22.566  41.110  1.00 32.36           C  
ANISOU  544  CD1 ILE A  75     4723   4084   3486   -702   -572   -105       C  
ATOM    545  N   VAL A  76      17.039  17.464  40.974  1.00 26.37           N  
ANISOU  545  N   VAL A  76     3728   3411   2881   -371   -277   -113       N  
ATOM    546  CA  VAL A  76      16.560  16.226  41.581  1.00 25.60           C  
ANISOU  546  CA  VAL A  76     3615   3327   2786   -332   -238    -97       C  
ATOM    547  C   VAL A  76      17.210  16.040  42.943  1.00 27.81           C  
ANISOU  547  C   VAL A  76     3952   3626   2990   -390   -298    -56       C  
ATOM    548  O   VAL A  76      18.443  16.067  43.069  1.00 29.87           O  
ANISOU  548  O   VAL A  76     4178   3924   3246   -447   -382      5       O  
ATOM    549  CB  VAL A  76      16.876  15.032  40.667  1.00 26.31           C  
ANISOU  549  CB  VAL A  76     3580   3450   2965   -285   -221    -57       C  
ATOM    550  CG1 VAL A  76      16.578  13.702  41.383  1.00 31.69           C  
ANISOU  550  CG1 VAL A  76     4247   4145   3650   -256   -193    -28       C  
ATOM    551  CG2 VAL A  76      16.102  15.139  39.349  1.00 28.63           C  
ANISOU  551  CG2 VAL A  76     3832   3725   3322   -232   -163   -101       C  
ATOM    552  N   SER A  77      16.386  15.824  43.971  1.00 28.43           N  
ANISOU  552  N   SER A  77     4112   3682   3008   -375   -257    -80       N  
ATOM    553  CA  SER A  77      16.891  15.586  45.318  1.00 27.14           C  
ANISOU  553  CA  SER A  77     4015   3537   2762   -427   -310    -42       C  
ATOM    554  C   SER A  77      16.677  14.155  45.790  1.00 27.22           C  
ANISOU  554  C   SER A  77     3971   3576   2796   -384   -277      1       C  
ATOM    555  O   SER A  77      17.027  13.839  46.937  1.00 31.45           O  
ANISOU  555  O   SER A  77     4555   4131   3263   -420   -315     39       O  
ATOM    556  CB  SER A  77      16.238  16.550  46.312  1.00 27.55           C  
ANISOU  556  CB  SER A  77     4232   3535   2701   -450   -291    -98       C  
ATOM    557  OG  SER A  77      14.845  16.302  46.391  1.00 28.85           O  
ANISOU  557  OG  SER A  77     4422   3667   2874   -370   -179   -139       O  
ATOM    558  N   SER A  78      16.096  13.283  44.956  1.00 27.65           N  
ANISOU  558  N   SER A  78     3934   3631   2942   -314   -210     -1       N  
ATOM    559  CA  SER A  78      16.035  11.866  45.301  1.00 30.34           C  
ANISOU  559  CA  SER A  78     4217   3994   3315   -278   -186     48       C  
ATOM    560  C   SER A  78      17.449  11.328  45.463  1.00 33.02           C  
ANISOU  560  C   SER A  78     4492   4386   3668   -314   -263    133       C  
ATOM    561  O   SER A  78      18.337  11.618  44.656  1.00 36.71           O  
ANISOU  561  O   SER A  78     4896   4874   4178   -330   -306    159       O  
ATOM    562  CB  SER A  78      15.318  11.065  44.212  1.00 29.32           C  
ANISOU  562  CB  SER A  78     4005   3850   3284   -211   -116     31       C  
ATOM    563  OG  SER A  78      14.161  11.728  43.769  1.00 41.36           O  
ANISOU  563  OG  SER A  78     5564   5337   4814   -184    -58    -34       O  
ATOM    564  N   LYS A  79      17.659  10.536  46.503  1.00 32.60           N  
ANISOU  564  N   LYS A  79     4449   4358   3582   -321   -277    186       N  
ATOM    565  CA  LYS A  79      18.946   9.886  46.663  1.00 48.10           C  
ANISOU  565  CA  LYS A  79     6333   6374   5567   -344   -341    285       C  
ATOM    566  C   LYS A  79      18.900   8.413  46.283  1.00 45.15           C  
ANISOU  566  C   LYS A  79     5869   6006   5279   -273   -285    331       C  
ATOM    567  O   LYS A  79      19.957   7.773  46.196  1.00 38.22           O  
ANISOU  567  O   LYS A  79     4911   5169   4442   -270   -318    420       O  
ATOM    568  CB  LYS A  79      19.447  10.076  48.103  1.00 58.92           C  
ANISOU  568  CB  LYS A  79     7776   7775   6834   -414   -415    331       C  
ATOM    569  CG  LYS A  79      19.963  11.505  48.343  1.00 71.55           C  
ANISOU  569  CG  LYS A  79     9457   9374   8355   -504   -501    309       C  
ATOM    570  CD  LYS A  79      19.769  11.987  49.783  1.00 80.42           C  
ANISOU  570  CD  LYS A  79    10725  10490   9342   -566   -541    295       C  
ATOM    571  CE  LYS A  79      20.266  13.426  49.961  1.00 81.83           C  
ANISOU  571  CE  LYS A  79    11002  10651   9439   -663   -627    266       C  
ATOM    572  NZ  LYS A  79      19.987  13.978  51.319  1.00 79.56           N  
ANISOU  572  NZ  LYS A  79    10888  10339   9003   -722   -658    236       N  
ATOM    573  N   GLU A  80      17.715   7.880  46.002  1.00 37.22           N  
ANISOU  573  N   GLU A  80     4875   4959   4309   -217   -200    277       N  
ATOM    574  CA  GLU A  80      17.584   6.471  45.673  1.00 32.56           C  
ANISOU  574  CA  GLU A  80     4218   4359   3794   -157   -146    314       C  
ATOM    575  C   GLU A  80      16.268   6.255  44.942  1.00 31.58           C  
ANISOU  575  C   GLU A  80     4102   4182   3714   -113    -68    240       C  
ATOM    576  O   GLU A  80      15.352   7.086  44.997  1.00 29.76           O  
ANISOU  576  O   GLU A  80     3929   3930   3449   -123    -48    174       O  
ATOM    577  CB  GLU A  80      17.642   5.595  46.932  1.00 29.97           C  
ANISOU  577  CB  GLU A  80     3904   4051   3432   -158   -148    377       C  
ATOM    578  CG  GLU A  80      16.520   5.898  47.920  1.00 29.83           C  
ANISOU  578  CG  GLU A  80     3980   4014   3340   -168   -118    331       C  
ATOM    579  CD  GLU A  80      16.744   5.262  49.278  1.00 42.13           C  
ANISOU  579  CD  GLU A  80     5565   5602   4843   -182   -135    399       C  
ATOM    580  OE1 GLU A  80      17.849   4.726  49.506  1.00 49.98           O  
ANISOU  580  OE1 GLU A  80     6504   6638   5849   -193   -185    485       O  
ATOM    581  OE2 GLU A  80      15.819   5.300  50.118  1.00 43.16           O  
ANISOU  581  OE2 GLU A  80     5767   5716   4916   -177    -96    374       O  
ATOM    582  N   ILE A  81      16.198   5.129  44.237  1.00 27.33           N  
ANISOU  582  N   ILE A  81     3510   3622   3253    -66    -25    257       N  
ATOM    583  CA  ILE A  81      14.951   4.616  43.691  1.00 27.27           C  
ANISOU  583  CA  ILE A  81     3507   3565   3290    -35     40    207       C  
ATOM    584  C   ILE A  81      14.465   3.537  44.642  1.00 27.40           C  
ANISOU  584  C   ILE A  81     3533   3571   3306    -21     73    246       C  
ATOM    585  O   ILE A  81      15.220   2.612  44.977  1.00 31.36           O  
ANISOU  585  O   ILE A  81     4005   4085   3827     -5     67    315       O  
ATOM    586  CB  ILE A  81      15.144   4.045  42.277  1.00 27.28           C  
ANISOU  586  CB  ILE A  81     3462   3535   3366      0     64    195       C  
ATOM    587  CG1 ILE A  81      15.860   5.051  41.380  1.00 28.18           C  
ANISOU  587  CG1 ILE A  81     3558   3668   3481    -10     30    175       C  
ATOM    588  CG2 ILE A  81      13.801   3.654  41.707  1.00 29.81           C  
ANISOU  588  CG2 ILE A  81     3795   3807   3723     12    113    142       C  
ATOM    589  CD1 ILE A  81      16.166   4.537  39.977  1.00 34.38           C  
ANISOU  589  CD1 ILE A  81     4308   4425   4328     29     57    168       C  
ATOM    590  N   ARG A  82      13.230   3.663  45.107  1.00 24.13           N  
ANISOU  590  N   ARG A  82     3157   3139   2873    -23    111    213       N  
ATOM    591  CA  ARG A  82      12.659   2.690  46.030  1.00 26.18           C  
ANISOU  591  CA  ARG A  82     3426   3390   3133    -10    147    254       C  
ATOM    592  C   ARG A  82      11.779   1.745  45.219  1.00 26.41           C  
ANISOU  592  C   ARG A  82     3424   3367   3243     12    196    240       C  
ATOM    593  O   ARG A  82      10.747   2.157  44.677  1.00 27.61           O  
ANISOU  593  O   ARG A  82     3579   3498   3412      8    220    192       O  
ATOM    594  CB  ARG A  82      11.883   3.393  47.143  1.00 26.70           C  
ANISOU  594  CB  ARG A  82     3554   3468   3121    -23    165    242       C  
ATOM    595  CG  ARG A  82      12.818   4.185  48.075  1.00 26.35           C  
ANISOU  595  CG  ARG A  82     3561   3467   2982    -56    107    261       C  
ATOM    596  CD  ARG A  82      12.081   5.040  49.103  1.00 33.84           C  
ANISOU  596  CD  ARG A  82     4602   4418   3839    -67    130    236       C  
ATOM    597  NE  ARG A  82      11.444   4.238  50.138  1.00 40.30           N  
ANISOU  597  NE  ARG A  82     5440   5236   4638    -46    177    279       N  
ATOM    598  CZ  ARG A  82      12.031   3.897  51.283  1.00 45.33           C  
ANISOU  598  CZ  ARG A  82     6110   5903   5208    -62    149    334       C  
ATOM    599  NH1 ARG A  82      13.274   4.291  51.535  1.00 45.81           N  
ANISOU  599  NH1 ARG A  82     6185   6000   5219   -104     67    357       N  
ATOM    600  NH2 ARG A  82      11.376   3.162  52.173  1.00 48.44           N  
ANISOU  600  NH2 ARG A  82     6521   6296   5589    -38    200    375       N  
ATOM    601  N   ILE A  83      12.185   0.475  45.131  1.00 25.64           N  
ANISOU  601  N   ILE A  83     3301   3248   3195     32    208    286       N  
ATOM    602  CA  ILE A  83      11.544  -0.486  44.230  1.00 27.11           C  
ANISOU  602  CA  ILE A  83     3471   3374   3456     43    243    271       C  
ATOM    603  C   ILE A  83      10.740  -1.485  45.052  1.00 25.84           C  
ANISOU  603  C   ILE A  83     3314   3189   3313     45    281    313       C  
ATOM    604  O   ILE A  83      11.283  -2.128  45.958  1.00 25.11           O  
ANISOU  604  O   ILE A  83     3221   3111   3208     59    284    376       O  
ATOM    605  CB  ILE A  83      12.575  -1.204  43.348  1.00 23.78           C  
ANISOU  605  CB  ILE A  83     3031   2924   3078     71    240    288       C  
ATOM    606  CG1 ILE A  83      13.396  -0.160  42.574  1.00 28.17           C  
ANISOU  606  CG1 ILE A  83     3575   3511   3616     71    204    257       C  
ATOM    607  CG2 ILE A  83      11.869  -2.134  42.361  1.00 27.20           C  
ANISOU  607  CG2 ILE A  83     3475   3283   3575     74    271    260       C  
ATOM    608  CD1 ILE A  83      14.638  -0.721  41.967  1.00 33.24           C  
ANISOU  608  CD1 ILE A  83     4194   4145   4290    109    207    297       C  
ATOM    609  N   HIS A  84       9.457  -1.632  44.712  1.00 21.72           N  
ANISOU  609  N   HIS A  84     2791   2635   2825     28    307    287       N  
ATOM    610  CA  HIS A  84       8.487  -2.376  45.512  1.00 24.51           C  
ANISOU  610  CA  HIS A  84     3142   2973   3198     23    345    330       C  
ATOM    611  C   HIS A  84       7.861  -3.502  44.702  1.00 24.92           C  
ANISOU  611  C   HIS A  84     3185   2956   3329      7    359    331       C  
ATOM    612  O   HIS A  84       7.823  -3.448  43.469  1.00 25.93           O  
ANISOU  612  O   HIS A  84     3314   3051   3488     -7    341    282       O  
ATOM    613  CB  HIS A  84       7.344  -1.478  46.000  1.00 25.92           C  
ANISOU  613  CB  HIS A  84     3323   3180   3346     13    368    319       C  
ATOM    614  CG  HIS A  84       7.786  -0.223  46.689  1.00 27.70           C  
ANISOU  614  CG  HIS A  84     3582   3459   3485     22    356    303       C  
ATOM    615  ND1 HIS A  84       8.245   0.884  46.004  1.00 31.00           N  
ANISOU  615  ND1 HIS A  84     4009   3893   3877     16    323    248       N  
ATOM    616  CD2 HIS A  84       7.807   0.110  48.004  1.00 28.21           C  
ANISOU  616  CD2 HIS A  84     3683   3558   3476     32    372    335       C  
ATOM    617  CE1 HIS A  84       8.544   1.839  46.871  1.00 27.56           C  
ANISOU  617  CE1 HIS A  84     3618   3495   3358     18    316    244       C  
ATOM    618  NE2 HIS A  84       8.290   1.394  48.090  1.00 28.56           N  
ANISOU  618  NE2 HIS A  84     3768   3634   3451     27    345    294       N  
ATOM    619  N   ASN A  85       7.290  -4.486  45.415  1.00 23.05           N  
ANISOU  619  N   ASN A  85     2942   2694   3120      2    389    386       N  
ATOM    620  CA  ASN A  85       6.526  -5.553  44.777  1.00 24.13           C  
ANISOU  620  CA  ASN A  85     3077   2760   3331    -29    398    393       C  
ATOM    621  C   ASN A  85       5.041  -5.184  44.712  1.00 26.50           C  
ANISOU  621  C   ASN A  85     3347   3067   3654    -67    406    393       C  
ATOM    622  O   ASN A  85       4.642  -4.037  44.951  1.00 27.40           O  
ANISOU  622  O   ASN A  85     3446   3236   3730    -60    411    379       O  
ATOM    623  CB  ASN A  85       6.741  -6.895  45.494  1.00 24.34           C  
ANISOU  623  CB  ASN A  85     3114   2748   3387    -17    425    460       C  
ATOM    624  CG  ASN A  85       6.135  -6.941  46.898  1.00 30.14           C  
ANISOU  624  CG  ASN A  85     3829   3523   4101    -11    458    526       C  
ATOM    625  OD1 ASN A  85       5.417  -6.033  47.336  1.00 25.94           O  
ANISOU  625  OD1 ASN A  85     3281   3041   3535    -15    469    523       O  
ATOM    626  ND2 ASN A  85       6.426  -8.031  47.612  1.00 28.42           N  
ANISOU  626  ND2 ASN A  85     3617   3279   3901      4    481    591       N  
ATOM    627  N   SER A  86       4.200  -6.167  44.388  1.00 24.34           N  
ANISOU  627  N   SER A  86     3066   2737   3447   -108    409    419       N  
ATOM    628  CA  SER A  86       2.788  -5.907  44.131  1.00 25.77           C  
ANISOU  628  CA  SER A  86     3204   2924   3665   -153    408    433       C  
ATOM    629  C   SER A  86       1.972  -5.718  45.406  1.00 29.52           C  
ANISOU  629  C   SER A  86     3639   3446   4131   -138    457    505       C  
ATOM    630  O   SER A  86       0.775  -5.419  45.323  1.00 27.92           O  
ANISOU  630  O   SER A  86     3388   3260   3961   -164    467    536       O  
ATOM    631  CB  SER A  86       2.199  -7.043  43.293  1.00 25.35           C  
ANISOU  631  CB  SER A  86     3159   2789   3683   -218    381    440       C  
ATOM    632  OG  SER A  86       2.144  -8.250  44.040  1.00 27.54           O  
ANISOU  632  OG  SER A  86     3445   3024   3993   -222    406    503       O  
ATOM    633  N   SER A  87       2.586  -5.879  46.579  1.00 24.53           N  
ANISOU  633  N   SER A  87     3026   2838   3454    -93    489    540       N  
ATOM    634  CA  SER A  87       1.968  -5.504  47.842  1.00 26.32           C  
ANISOU  634  CA  SER A  87     3236   3117   3648    -64    543    600       C  
ATOM    635  C   SER A  87       2.496  -4.179  48.352  1.00 27.04           C  
ANISOU  635  C   SER A  87     3359   3270   3646    -20    553    564       C  
ATOM    636  O   SER A  87       2.109  -3.746  49.444  1.00 30.36           O  
ANISOU  636  O   SER A  87     3788   3730   4016     12    602    603       O  
ATOM    637  CB  SER A  87       2.205  -6.592  48.882  1.00 32.50           C  
ANISOU  637  CB  SER A  87     4028   3885   4435    -50    572    670       C  
ATOM    638  OG  SER A  87       1.447  -7.738  48.554  1.00 37.43           O  
ANISOU  638  OG  SER A  87     4623   4450   5147    -97    572    716       O  
ATOM    639  N   GLY A  88       3.351  -3.520  47.579  1.00 25.15           N  
ANISOU  639  N   GLY A  88     3142   3034   3378    -18    509    491       N  
ATOM    640  CA  GLY A  88       3.991  -2.303  48.032  1.00 27.15           C  
ANISOU  640  CA  GLY A  88     3436   3337   3543     13    506    455       C  
ATOM    641  C   GLY A  88       5.100  -2.496  49.038  1.00 31.50           C  
ANISOU  641  C   GLY A  88     4028   3911   4027     35    498    478       C  
ATOM    642  O   GLY A  88       5.513  -1.516  49.671  1.00 32.31           O  
ANISOU  642  O   GLY A  88     4176   4056   4044     52    496    461       O  
ATOM    643  N   ARG A  89       5.593  -3.721  49.226  1.00 27.74           N  
ANISOU  643  N   ARG A  89     3545   3408   3586     34    492    521       N  
ATOM    644  CA  ARG A  89       6.727  -3.920  50.118  1.00 30.79           C  
ANISOU  644  CA  ARG A  89     3960   3823   3913     54    476    554       C  
ATOM    645  C   ARG A  89       8.010  -3.453  49.446  1.00 28.94           C  
ANISOU  645  C   ARG A  89     3736   3601   3660     54    420    510       C  
ATOM    646  O   ARG A  89       8.237  -3.710  48.258  1.00 25.53           O  
ANISOU  646  O   ARG A  89     3284   3130   3286     46    401    475       O  
ATOM    647  CB  ARG A  89       6.860  -5.386  50.525  1.00 33.66           C  
ANISOU  647  CB  ARG A  89     4309   4154   4327     60    494    624       C  
ATOM    648  CG  ARG A  89       8.070  -5.671  51.431  1.00 36.26           C  
ANISOU  648  CG  ARG A  89     4658   4519   4602     81    475    675       C  
ATOM    649  CD  ARG A  89       7.909  -6.999  52.179  1.00 38.57           C  
ANISOU  649  CD  ARG A  89     4938   4786   4929     94    510    760       C  
ATOM    650  NE  ARG A  89       7.766  -8.132  51.266  1.00 34.76           N  
ANISOU  650  NE  ARG A  89     4432   4225   4549     86    519    763       N  
ATOM    651  CZ  ARG A  89       8.784  -8.807  50.742  1.00 41.90           C  
ANISOU  651  CZ  ARG A  89     5336   5096   5489    103    503    773       C  
ATOM    652  NH1 ARG A  89      10.036  -8.466  51.029  1.00 38.59           N  
ANISOU  652  NH1 ARG A  89     4919   4725   5020    127    471    791       N  
ATOM    653  NH2 ARG A  89       8.552  -9.826  49.921  1.00 41.49           N  
ANISOU  653  NH2 ARG A  89     5286   4959   5521     95    519    770       N  
ATOM    654  N   LEU A  90       8.856  -2.765  50.216  1.00 27.36           N  
ANISOU  654  N   LEU A  90     3568   3452   3374     59    392    518       N  
ATOM    655  CA  LEU A  90      10.137  -2.305  49.689  1.00 29.79           C  
ANISOU  655  CA  LEU A  90     3874   3780   3664     55    335    496       C  
ATOM    656  C   LEU A  90      11.095  -3.484  49.533  1.00 28.50           C  
ANISOU  656  C   LEU A  90     3680   3599   3551     73    325    553       C  
ATOM    657  O   LEU A  90      11.386  -4.195  50.507  1.00 32.40           O  
ANISOU  657  O   LEU A  90     4174   4108   4029     85    333    625       O  
ATOM    658  CB  LEU A  90      10.738  -1.248  50.611  1.00 32.37           C  
ANISOU  658  CB  LEU A  90     4249   4166   3883     42    298    498       C  
ATOM    659  CG  LEU A  90      12.112  -0.700  50.205  1.00 30.72           C  
ANISOU  659  CG  LEU A  90     4032   3988   3653     27    230    492       C  
ATOM    660  CD1 LEU A  90      11.989   0.104  48.931  1.00 28.04           C  
ANISOU  660  CD1 LEU A  90     3681   3630   3344     20    219    416       C  
ATOM    661  CD2 LEU A  90      12.700   0.159  51.319  1.00 32.65           C  
ANISOU  661  CD2 LEU A  90     4333   4288   3784     -1    183    510       C  
ATOM    662  N   ILE A  91      11.574  -3.699  48.312  1.00 27.03           N  
ANISOU  662  N   ILE A  91     3469   3378   3422     81    314    525       N  
ATOM    663  CA  ILE A  91      12.501  -4.788  48.016  1.00 27.51           C  
ANISOU  663  CA  ILE A  91     3507   3412   3535    112    319    578       C  
ATOM    664  C   ILE A  91      13.933  -4.287  47.858  1.00 31.74           C  
ANISOU  664  C   ILE A  91     4021   3994   4045    123    273    602       C  
ATOM    665  O   ILE A  91      14.853  -4.807  48.488  1.00 35.24           O  
ANISOU  665  O   ILE A  91     4442   4465   4482    142    263    685       O  
ATOM    666  CB  ILE A  91      12.038  -5.544  46.753  1.00 31.52           C  
ANISOU  666  CB  ILE A  91     4015   3835   4125    119    350    539       C  
ATOM    667  CG1 ILE A  91      10.564  -5.960  46.886  1.00 27.17           C  
ANISOU  667  CG1 ILE A  91     3476   3244   3603     92    383    524       C  
ATOM    668  CG2 ILE A  91      12.965  -6.729  46.473  1.00 32.28           C  
ANISOU  668  CG2 ILE A  91     4105   3889   4272    162    373    596       C  
ATOM    669  CD1 ILE A  91      10.292  -6.909  48.034  1.00 28.92           C  
ANISOU  669  CD1 ILE A  91     3696   3460   3831    101    414    601       C  
ATOM    670  N   ILE A  92      14.133  -3.277  47.017  1.00 27.30           N  
ANISOU  670  N   ILE A  92     3458   3445   3471    109    245    540       N  
ATOM    671  CA  ILE A  92      15.447  -2.758  46.659  1.00 30.96           C  
ANISOU  671  CA  ILE A  92     3892   3949   3923    116    202    564       C  
ATOM    672  C   ILE A  92      15.434  -1.248  46.814  1.00 34.35           C  
ANISOU  672  C   ILE A  92     4341   4428   4283     72    151    515       C  
ATOM    673  O   ILE A  92      14.476  -0.585  46.401  1.00 30.54           O  
ANISOU  673  O   ILE A  92     3886   3926   3792     55    163    437       O  
ATOM    674  CB  ILE A  92      15.837  -3.099  45.203  1.00 39.98           C  
ANISOU  674  CB  ILE A  92     5015   5042   5132    150    226    539       C  
ATOM    675  CG1 ILE A  92      15.711  -4.594  44.928  1.00 51.10           C  
ANISOU  675  CG1 ILE A  92     6430   6378   6608    193    285    572       C  
ATOM    676  CG2 ILE A  92      17.249  -2.618  44.900  1.00 42.93           C  
ANISOU  676  CG2 ILE A  92     5346   5465   5501    165    189    586       C  
ATOM    677  CD1 ILE A  92      16.799  -5.399  45.567  1.00 59.41           C  
ANISOU  677  CD1 ILE A  92     7448   7450   7675    234    293    682       C  
ATOM    678  N   ARG A  93      16.513  -0.704  47.373  1.00 30.79           N  
ANISOU  678  N   ARG A  93     3876   4039   3783     52     93    566       N  
ATOM    679  CA  ARG A  93      16.816   0.719  47.298  1.00 29.16           C  
ANISOU  679  CA  ARG A  93     3689   3872   3519      8     35    526       C  
ATOM    680  C   ARG A  93      18.038   0.853  46.395  1.00 37.93           C  
ANISOU  680  C   ARG A  93     4739   5002   4671     21      7    561       C  
ATOM    681  O   ARG A  93      19.135   0.410  46.759  1.00 41.91           O  
ANISOU  681  O   ARG A  93     5195   5545   5184     30    -21    658       O  
ATOM    682  CB  ARG A  93      17.076   1.315  48.686  1.00 32.55           C  
ANISOU  682  CB  ARG A  93     4161   4356   3850    -41    -20    560       C  
ATOM    683  CG  ARG A  93      15.914   1.185  49.684  1.00 33.87           C  
ANISOU  683  CG  ARG A  93     4394   4509   3966    -44     19    538       C  
ATOM    684  CD  ARG A  93      16.191   1.860  51.053  1.00 48.87           C  
ANISOU  684  CD  ARG A  93     6362   6458   5749    -94    -35    563       C  
ATOM    685  NE  ARG A  93      17.603   1.861  51.440  1.00 62.92           N  
ANISOU  685  NE  ARG A  93     8108   8296   7504   -126   -117    649       N  
ATOM    686  CZ  ARG A  93      18.155   1.010  52.302  1.00 75.82           C  
ANISOU  686  CZ  ARG A  93     9717   9965   9126   -123   -136    747       C  
ATOM    687  NH1 ARG A  93      17.417   0.075  52.883  1.00 78.15           N  
ANISOU  687  NH1 ARG A  93    10024  10238   9430    -87    -74    767       N  
ATOM    688  NH2 ARG A  93      19.450   1.093  52.587  1.00 78.34           N  
ANISOU  688  NH2 ARG A  93     9994  10344   9427   -158   -217    835       N  
ATOM    689  N   GLN A  94      17.857   1.434  45.209  1.00 28.45           N  
ANISOU  689  N   GLN A  94     3535   3776   3500     27     17    493       N  
ATOM    690  CA  GLN A  94      18.968   1.609  44.278  1.00 32.50           C  
ANISOU  690  CA  GLN A  94     3992   4305   4052     45      0    526       C  
ATOM    691  C   GLN A  94      19.576   2.994  44.478  1.00 37.15           C  
ANISOU  691  C   GLN A  94     4582   4948   4585    -14    -77    525       C  
ATOM    692  O   GLN A  94      18.928   4.010  44.207  1.00 30.91           O  
ANISOU  692  O   GLN A  94     3836   4145   3762    -45    -87    441       O  
ATOM    693  CB  GLN A  94      18.534   1.417  42.831  1.00 35.55           C  
ANISOU  693  CB  GLN A  94     4377   4633   4496     85     54    461       C  
ATOM    694  CG  GLN A  94      19.742   1.250  41.938  1.00 52.52           C  
ANISOU  694  CG  GLN A  94     6468   6793   6692    126     60    518       C  
ATOM    695  CD  GLN A  94      19.566   1.887  40.593  1.00 75.00           C  
ANISOU  695  CD  GLN A  94     9322   9616   9558    135     74    446       C  
ATOM    696  OE1 GLN A  94      18.445   2.138  40.154  1.00 84.52           O  
ANISOU  696  OE1 GLN A  94    10574  10783  10758    122     92    355       O  
ATOM    697  NE2 GLN A  94      20.678   2.159  39.921  1.00 82.00           N  
ANISOU  697  NE2 GLN A  94    10156  10530  10468    159     66    497       N  
ATOM    698  N   ASP A  95      20.830   3.032  44.923  1.00 36.55           N  
ANISOU  698  N   ASP A  95     4456   4931   4501    -32   -133    625       N  
ATOM    699  CA  ASP A  95      21.450   4.299  45.283  1.00 33.17           C  
ANISOU  699  CA  ASP A  95     4036   4555   4013   -106   -222    636       C  
ATOM    700  C   ASP A  95      21.661   5.165  44.044  1.00 37.69           C  
ANISOU  700  C   ASP A  95     4588   5118   4616   -106   -225    590       C  
ATOM    701  O   ASP A  95      22.150   4.688  43.015  1.00 45.49           O  
ANISOU  701  O   ASP A  95     5513   6096   5676    -49   -184    620       O  
ATOM    702  CB  ASP A  95      22.772   4.036  46.007  1.00 40.83           C  
ANISOU  702  CB  ASP A  95     4942   5594   4976   -131   -290    772       C  
ATOM    703  CG  ASP A  95      23.562   5.301  46.268  1.00 45.77           C  
ANISOU  703  CG  ASP A  95     5568   6273   5548   -219   -395    798       C  
ATOM    704  OD1 ASP A  95      22.953   6.340  46.593  1.00 50.65           O  
ANISOU  704  OD1 ASP A  95     6278   6876   6093   -279   -427    712       O  
ATOM    705  OD2 ASP A  95      24.804   5.246  46.171  1.00 56.71           O  
ANISOU  705  OD2 ASP A  95     6865   7715   6967   -230   -444    914       O  
ATOM    706  N   LEU A  96      21.278   6.439  44.139  1.00 39.00           N  
ANISOU  706  N   LEU A  96     4813   5280   4722   -165   -266    519       N  
ATOM    707  CA  LEU A  96      21.459   7.406  43.060  1.00 37.32           C  
ANISOU  707  CA  LEU A  96     4587   5061   4530   -174   -276    476       C  
ATOM    708  C   LEU A  96      22.585   8.398  43.330  1.00 38.43           C  
ANISOU  708  C   LEU A  96     4707   5256   4639   -249   -374    537       C  
ATOM    709  O   LEU A  96      22.735   9.365  42.572  1.00 38.30           O  
ANISOU  709  O   LEU A  96     4688   5234   4630   -270   -392    503       O  
ATOM    710  CB  LEU A  96      20.169   8.191  42.815  1.00 34.98           C  
ANISOU  710  CB  LEU A  96     4373   4716   4203   -183   -246    354       C  
ATOM    711  CG  LEU A  96      18.973   7.419  42.275  1.00 34.84           C  
ANISOU  711  CG  LEU A  96     4368   4645   4225   -121   -158    290       C  
ATOM    712  CD1 LEU A  96      17.780   8.351  42.066  1.00 38.20           C  
ANISOU  712  CD1 LEU A  96     4860   5035   4621   -134   -135    191       C  
ATOM    713  CD2 LEU A  96      19.372   6.739  40.987  1.00 33.79           C  
ANISOU  713  CD2 LEU A  96     4169   4498   4173    -62   -115    308       C  
ATOM    714  N   SER A  97      23.375   8.194  44.387  1.00 36.44           N  
ANISOU  714  N   SER A  97     4438   5055   4352   -296   -443    631       N  
ATOM    715  CA  SER A  97      24.321   9.231  44.791  1.00 41.68           C  
ANISOU  715  CA  SER A  97     5100   5766   4970   -391   -553    684       C  
ATOM    716  C   SER A  97      25.341   9.537  43.698  1.00 41.94           C  
ANISOU  716  C   SER A  97     5028   5829   5076   -382   -569    750       C  
ATOM    717  O   SER A  97      25.778  10.685  43.570  1.00 45.33           O  
ANISOU  717  O   SER A  97     5470   6273   5482   -455   -641    749       O  
ATOM    718  CB  SER A  97      25.024   8.829  46.088  1.00 48.75           C  
ANISOU  718  CB  SER A  97     5987   6719   5817   -446   -631    789       C  
ATOM    719  OG  SER A  97      25.770   7.639  45.911  1.00 54.34           O  
ANISOU  719  OG  SER A  97     6579   7465   6603   -382   -602    907       O  
ATOM    720  N   GLU A  98      25.727   8.545  42.894  1.00 36.57           N  
ANISOU  720  N   GLU A  98     4253   5155   4486   -290   -498    809       N  
ATOM    721  CA  GLU A  98      26.653   8.834  41.803  1.00 48.47           C  
ANISOU  721  CA  GLU A  98     5665   6689   6063   -267   -496    874       C  
ATOM    722  C   GLU A  98      25.943   9.485  40.620  1.00 46.63           C  
ANISOU  722  C   GLU A  98     5470   6402   5845   -238   -443    758       C  
ATOM    723  O   GLU A  98      26.456  10.448  40.037  1.00 43.03           O  
ANISOU  723  O   GLU A  98     4987   5964   5400   -274   -482    771       O  
ATOM    724  CB  GLU A  98      27.372   7.560  41.364  1.00 58.02           C  
ANISOU  724  CB  GLU A  98     6770   7918   7356   -170   -429    985       C  
ATOM    725  CG  GLU A  98      28.396   7.064  42.373  1.00 74.74           C  
ANISOU  725  CG  GLU A  98     8815  10108   9475   -200   -493   1140       C  
ATOM    726  CD  GLU A  98      29.175   5.875  41.861  1.00 84.85           C  
ANISOU  726  CD  GLU A  98     9988  11406  10846    -91   -415   1263       C  
ATOM    727  OE1 GLU A  98      28.859   5.408  40.745  1.00 85.58           O  
ANISOU  727  OE1 GLU A  98    10082  11444  10990      6   -307   1214       O  
ATOM    728  OE2 GLU A  98      30.099   5.412  42.567  1.00 87.83           O  
ANISOU  728  OE2 GLU A  98    10282  11848  11240   -102   -458   1412       O  
ATOM    729  N   VAL A  99      24.759   8.981  40.260  1.00 37.40           N  
ANISOU  729  N   VAL A  99     4361   5170   4678   -178   -358    652       N  
ATOM    730  CA  VAL A  99      23.991   9.570  39.163  1.00 34.47           C  
ANISOU  730  CA  VAL A  99     4027   4752   4319   -154   -311    546       C  
ATOM    731  C   VAL A  99      23.711  11.047  39.428  1.00 43.97           C  
ANISOU  731  C   VAL A  99     5294   5951   5462   -240   -377    484       C  
ATOM    732  O   VAL A  99      23.740  11.876  38.505  1.00 40.45           O  
ANISOU  732  O   VAL A  99     4840   5495   5033   -243   -375    451       O  
ATOM    733  CB  VAL A  99      22.687   8.775  38.949  1.00 38.37           C  
ANISOU  733  CB  VAL A  99     4578   5184   4817    -96   -228    452       C  
ATOM    734  CG1 VAL A  99      21.775   9.482  37.946  1.00 43.42           C  
ANISOU  734  CG1 VAL A  99     5260   5780   5457    -86   -194    345       C  
ATOM    735  CG2 VAL A  99      22.995   7.360  38.493  1.00 39.09           C  
ANISOU  735  CG2 VAL A  99     4620   5263   4969    -10   -156    506       C  
ATOM    736  N   CYS A 100      23.459  11.402  40.693  1.00 40.93           N  
ANISOU  736  N   CYS A 100     4980   5570   5003   -309   -434    470       N  
ATOM    737  CA  CYS A 100      23.108  12.761  41.094  1.00 37.52           C  
ANISOU  737  CA  CYS A 100     4638   5118   4501   -388   -489    405       C  
ATOM    738  C   CYS A 100      24.256  13.488  41.791  1.00 40.59           C  
ANISOU  738  C   CYS A 100     5019   5553   4849   -490   -605    487       C  
ATOM    739  O   CYS A 100      24.013  14.444  42.538  1.00 45.42           O  
ANISOU  739  O   CYS A 100     5735   6145   5379   -570   -662    442       O  
ATOM    740  CB  CYS A 100      21.875  12.746  41.999  1.00 42.07           C  
ANISOU  740  CB  CYS A 100     5326   5651   5008   -392   -460    319       C  
ATOM    741  SG  CYS A 100      20.363  12.218  41.164  1.00 51.13           S  
ANISOU  741  SG  CYS A 100     6490   6741   6197   -298   -340    218       S  
ATOM    742  N   GLU A 101      25.501  13.057  41.559  1.00 40.21           N  
ANISOU  742  N   GLU A 101     4854   5566   4856   -490   -641    614       N  
ATOM    743  CA  GLU A 101      26.656  13.788  42.082  1.00 49.52           C  
ANISOU  743  CA  GLU A 101     6009   6798   6011   -597   -763    709       C  
ATOM    744  C   GLU A 101      26.657  15.226  41.575  1.00 42.51           C  
ANISOU  744  C   GLU A 101     5166   5882   5104   -661   -805    656       C  
ATOM    745  O   GLU A 101      26.888  16.172  42.337  1.00 42.53           O  
ANISOU  745  O   GLU A 101     5248   5880   5032   -773   -902    653       O  
ATOM    746  CB  GLU A 101      27.945  13.077  41.672  1.00 55.81           C  
ANISOU  746  CB  GLU A 101     6648   7665   6892   -566   -774    867       C  
ATOM    747  CG  GLU A 101      28.930  12.865  42.792  1.00 69.20           C  
ANISOU  747  CG  GLU A 101     8303   9430   8560   -647   -880    999       C  
ATOM    748  CD  GLU A 101      30.129  12.067  42.333  1.00 86.32           C  
ANISOU  748  CD  GLU A 101    10303  11669  10824   -594   -869   1166       C  
ATOM    749  OE1 GLU A 101      30.775  12.492  41.351  1.00 93.05           O  
ANISOU  749  OE1 GLU A 101    11072  12542  11743   -580   -863   1219       O  
ATOM    750  OE2 GLU A 101      30.410  11.010  42.938  1.00 90.52           O  
ANISOU  750  OE2 GLU A 101    10788  12235  11369   -559   -858   1249       O  
ATOM    751  N   GLN A 102      26.403  15.398  40.287  1.00 34.77           N  
ANISOU  751  N   GLN A 102     4146   4878   4186   -593   -732    616       N  
ATOM    752  CA  GLN A 102      26.170  16.670  39.634  1.00 35.08           C  
ANISOU  752  CA  GLN A 102     4230   4880   4217   -627   -743    550       C  
ATOM    753  C   GLN A 102      24.680  16.821  39.336  1.00 32.81           C  
ANISOU  753  C   GLN A 102     4039   4521   3906   -569   -654    405       C  
ATOM    754  O   GLN A 102      23.941  15.831  39.314  1.00 32.10           O  
ANISOU  754  O   GLN A 102     3949   4417   3830   -491   -576    369       O  
ATOM    755  CB  GLN A 102      26.994  16.755  38.340  1.00 40.23           C  
ANISOU  755  CB  GLN A 102     4758   5566   4960   -588   -724    624       C  
ATOM    756  CG  GLN A 102      28.490  16.825  38.594  1.00 43.06           C  
ANISOU  756  CG  GLN A 102     5011   5999   5349   -655   -818    783       C  
ATOM    757  CD  GLN A 102      28.861  18.023  39.449  1.00 57.15           C  
ANISOU  757  CD  GLN A 102     6870   7782   7063   -804   -949    792       C  
ATOM    758  OE1 GLN A 102      28.472  19.155  39.148  1.00 57.42           O  
ANISOU  758  OE1 GLN A 102     6982   7765   7069   -848   -963    713       O  
ATOM    759  NE2 GLN A 102      29.603  17.780  40.532  1.00 61.49           N  
ANISOU  759  NE2 GLN A 102     7404   8381   7579   -886  -1047    888       N  
ATOM    760  N   PRO A 103      24.196  18.045  39.135  1.00 30.28           N  
ANISOU  760  N   PRO A 103     3801   4153   3552   -609   -664    328       N  
ATOM    761  CA  PRO A 103      22.744  18.262  39.065  1.00 32.29           C  
ANISOU  761  CA  PRO A 103     4151   4342   3776   -561   -585    205       C  
ATOM    762  C   PRO A 103      22.083  17.460  37.952  1.00 33.32           C  
ANISOU  762  C   PRO A 103     4217   4467   3975   -451   -484    173       C  
ATOM    763  O   PRO A 103      22.614  17.342  36.843  1.00 30.71           O  
ANISOU  763  O   PRO A 103     3797   4159   3711   -414   -466    211       O  
ATOM    764  CB  PRO A 103      22.625  19.766  38.801  1.00 34.53           C  
ANISOU  764  CB  PRO A 103     4507   4582   4030   -617   -615    156       C  
ATOM    765  CG  PRO A 103      23.873  20.339  39.367  1.00 39.13           C  
ANISOU  765  CG  PRO A 103     5086   5194   4585   -728   -733    237       C  
ATOM    766  CD  PRO A 103      24.942  19.317  39.151  1.00 37.07           C  
ANISOU  766  CD  PRO A 103     4682   5012   4390   -709   -756    358       C  
ATOM    767  N   ASN A 104      20.923  16.889  38.280  1.00 24.99           N  
ANISOU  767  N   ASN A 104     3213   3381   2902   -402   -419    107       N  
ATOM    768  CA  ASN A 104      19.959  16.379  37.315  1.00 24.95           C  
ANISOU  768  CA  ASN A 104     3183   3352   2943   -318   -330     53       C  
ATOM    769  C   ASN A 104      18.686  17.190  37.481  1.00 28.80           C  
ANISOU  769  C   ASN A 104     3764   3787   3391   -316   -293    -37       C  
ATOM    770  O   ASN A 104      18.423  17.716  38.566  1.00 28.51           O  
ANISOU  770  O   ASN A 104     3819   3728   3285   -360   -315    -59       O  
ATOM    771  CB  ASN A 104      19.617  14.897  37.543  1.00 26.33           C  
ANISOU  771  CB  ASN A 104     3328   3534   3141   -262   -283     67       C  
ATOM    772  CG  ASN A 104      20.794  13.990  37.358  1.00 36.26           C  
ANISOU  772  CG  ASN A 104     4495   4838   4444   -245   -299    161       C  
ATOM    773  OD1 ASN A 104      21.898  14.283  37.817  1.00 44.73           O  
ANISOU  773  OD1 ASN A 104     5540   5949   5507   -297   -368    236       O  
ATOM    774  ND2 ASN A 104      20.568  12.870  36.694  1.00 28.06           N  
ANISOU  774  ND2 ASN A 104     3414   3792   3454   -172   -236    164       N  
ATOM    775  N   TYR A 105      17.882  17.281  36.422  1.00 24.87           N  
ANISOU  775  N   TYR A 105     3246   3269   2933   -263   -234    -83       N  
ATOM    776  CA  TYR A 105      16.594  17.950  36.526  1.00 24.05           C  
ANISOU  776  CA  TYR A 105     3214   3121   2803   -248   -188   -153       C  
ATOM    777  C   TYR A 105      15.462  16.958  36.318  1.00 28.53           C  
ANISOU  777  C   TYR A 105     3760   3680   3399   -188   -120   -178       C  
ATOM    778  O   TYR A 105      15.603  15.971  35.591  1.00 28.16           O  
ANISOU  778  O   TYR A 105     3645   3652   3401   -153   -105   -159       O  
ATOM    779  CB  TYR A 105      16.407  19.063  35.491  1.00 22.21           C  
ANISOU  779  CB  TYR A 105     2979   2870   2591   -243   -178   -182       C  
ATOM    780  CG  TYR A 105      17.483  20.131  35.429  1.00 25.55           C  
ANISOU  780  CG  TYR A 105     3414   3296   2999   -305   -244   -155       C  
ATOM    781  CD1 TYR A 105      18.043  20.689  36.575  1.00 28.09           C  
ANISOU  781  CD1 TYR A 105     3810   3605   3257   -377   -304   -143       C  
ATOM    782  CD2 TYR A 105      17.902  20.614  34.194  1.00 34.18           C  
ANISOU  782  CD2 TYR A 105     4448   4400   4139   -295   -248   -142       C  
ATOM    783  CE1 TYR A 105      19.014  21.685  36.486  1.00 32.90           C  
ANISOU  783  CE1 TYR A 105     4432   4214   3856   -447   -373   -114       C  
ATOM    784  CE2 TYR A 105      18.865  21.599  34.101  1.00 35.20           C  
ANISOU  784  CE2 TYR A 105     4582   4532   4263   -355   -308   -110       C  
ATOM    785  CZ  TYR A 105      19.416  22.125  35.239  1.00 34.97           C  
ANISOU  785  CZ  TYR A 105     4622   4489   4175   -434   -374    -95       C  
ATOM    786  OH  TYR A 105      20.369  23.112  35.093  1.00 39.52           O  
ANISOU  786  OH  TYR A 105     5201   5065   4750   -504   -442    -58       O  
ATOM    787  N   LEU A 106      14.325  17.252  36.948  1.00 27.30           N  
ANISOU  787  N   LEU A 106     3669   3493   3210   -176    -77   -216       N  
ATOM    788  CA  LEU A 106      13.047  16.638  36.598  1.00 22.90           C  
ANISOU  788  CA  LEU A 106     3089   2926   2688   -125    -13   -237       C  
ATOM    789  C   LEU A 106      12.004  17.736  36.662  1.00 24.61           C  
ANISOU  789  C   LEU A 106     3359   3107   2883   -110     31   -273       C  
ATOM    790  O   LEU A 106      11.868  18.386  37.704  1.00 24.50           O  
ANISOU  790  O   LEU A 106     3432   3067   2808   -125     39   -285       O  
ATOM    791  CB  LEU A 106      12.682  15.503  37.551  1.00 24.41           C  
ANISOU  791  CB  LEU A 106     3287   3121   2868   -115      7   -219       C  
ATOM    792  CG  LEU A 106      11.414  14.758  37.114  1.00 26.96           C  
ANISOU  792  CG  LEU A 106     3573   3436   3236    -73     63   -228       C  
ATOM    793  CD1 LEU A 106      11.650  13.917  35.850  1.00 26.82           C  
ANISOU  793  CD1 LEU A 106     3481   3429   3278    -59     54   -222       C  
ATOM    794  CD2 LEU A 106      10.874  13.916  38.258  1.00 27.95           C  
ANISOU  794  CD2 LEU A 106     3721   3557   3342    -65     92   -210       C  
ATOM    795  N   LEU A 107      11.283  17.967  35.567  1.00 24.97           N  
ANISOU  795  N   LEU A 107     3362   3151   2975    -79     62   -287       N  
ATOM    796  CA  LEU A 107      10.331  19.071  35.556  1.00 25.59           C  
ANISOU  796  CA  LEU A 107     3482   3198   3042    -56    109   -308       C  
ATOM    797  C   LEU A 107       9.340  18.864  34.417  1.00 22.59           C  
ANISOU  797  C   LEU A 107     3031   2830   2723    -20    142   -305       C  
ATOM    798  O   LEU A 107       9.633  18.145  33.456  1.00 23.16           O  
ANISOU  798  O   LEU A 107     3037   2927   2835    -22    115   -298       O  
ATOM    799  CB  LEU A 107      11.048  20.426  35.411  1.00 22.91           C  
ANISOU  799  CB  LEU A 107     3194   2836   2673    -85     80   -323       C  
ATOM    800  CG  LEU A 107      11.623  20.797  34.041  1.00 24.59           C  
ANISOU  800  CG  LEU A 107     3344   3068   2931    -91     48   -319       C  
ATOM    801  CD1 LEU A 107      12.064  22.255  34.108  1.00 26.70           C  
ANISOU  801  CD1 LEU A 107     3677   3300   3166   -119     32   -332       C  
ATOM    802  CD2 LEU A 107      12.791  19.891  33.672  1.00 25.24           C  
ANISOU  802  CD2 LEU A 107     3366   3191   3035   -113     -6   -292       C  
ATOM    803  N   PRO A 108       8.159  19.476  34.500  1.00 22.67           N  
ANISOU  803  N   PRO A 108     3055   2820   2737     15    201   -304       N  
ATOM    804  CA  PRO A 108       7.234  19.456  33.358  1.00 24.40           C  
ANISOU  804  CA  PRO A 108     3202   3056   3013     41    221   -290       C  
ATOM    805  C   PRO A 108       7.925  19.948  32.091  1.00 25.05           C  
ANISOU  805  C   PRO A 108     3252   3152   3115     27    179   -301       C  
ATOM    806  O   PRO A 108       8.648  20.950  32.101  1.00 25.24           O  
ANISOU  806  O   PRO A 108     3318   3158   3115     14    164   -315       O  
ATOM    807  CB  PRO A 108       6.107  20.399  33.797  1.00 24.97           C  
ANISOU  807  CB  PRO A 108     3308   3102   3079     83    294   -277       C  
ATOM    808  CG  PRO A 108       6.142  20.324  35.341  1.00 23.87           C  
ANISOU  808  CG  PRO A 108     3254   2934   2880     87    326   -282       C  
ATOM    809  CD  PRO A 108       7.613  20.215  35.660  1.00 22.96           C  
ANISOU  809  CD  PRO A 108     3180   2819   2723     35    256   -308       C  
ATOM    810  N   ARG A 109       7.748  19.200  31.003  1.00 23.34           N  
ANISOU  810  N   ARG A 109     2965   2962   2939     26    158   -293       N  
ATOM    811  CA  ARG A 109       8.370  19.598  29.736  1.00 25.62           C  
ANISOU  811  CA  ARG A 109     3226   3266   3243     20    125   -300       C  
ATOM    812  C   ARG A 109       7.996  21.025  29.360  1.00 26.94           C  
ANISOU  812  C   ARG A 109     3404   3420   3412     37    148   -298       C  
ATOM    813  O   ARG A 109       8.844  21.794  28.892  1.00 26.24           O  
ANISOU  813  O   ARG A 109     3326   3328   3315     27    125   -305       O  
ATOM    814  CB  ARG A 109       7.951  18.649  28.619  1.00 24.99           C  
ANISOU  814  CB  ARG A 109     3089   3211   3195     19    108   -293       C  
ATOM    815  CG  ARG A 109       8.544  19.018  27.258  1.00 26.87           C  
ANISOU  815  CG  ARG A 109     3304   3466   3441     18     80   -298       C  
ATOM    816  CD  ARG A 109       8.064  18.049  26.211  1.00 26.08           C  
ANISOU  816  CD  ARG A 109     3170   3381   3357     12     62   -297       C  
ATOM    817  NE  ARG A 109       8.576  18.310  24.863  1.00 23.04           N  
ANISOU  817  NE  ARG A 109     2773   3012   2969     15     41   -301       N  
ATOM    818  CZ  ARG A 109       8.063  19.228  24.045  1.00 27.51           C  
ANISOU  818  CZ  ARG A 109     3317   3592   3544     23     42   -290       C  
ATOM    819  NH1 ARG A 109       7.050  19.989  24.445  1.00 25.33           N  
ANISOU  819  NH1 ARG A 109     3026   3314   3284     33     67   -270       N  
ATOM    820  NH2 ARG A 109       8.569  19.380  22.818  1.00 27.74           N  
ANISOU  820  NH2 ARG A 109     3339   3637   3564     27     23   -293       N  
ATOM    821  N   SER A 110       6.731  21.401  29.570  1.00 25.09           N  
ANISOU  821  N   SER A 110     3164   3178   3192     67    198   -279       N  
ATOM    822  CA  SER A 110       6.290  22.745  29.211  1.00 26.03           C  
ANISOU  822  CA  SER A 110     3292   3279   3317     94    232   -268       C  
ATOM    823  C   SER A 110       7.033  23.819  29.996  1.00 26.39           C  
ANISOU  823  C   SER A 110     3429   3278   3319     88    241   -292       C  
ATOM    824  O   SER A 110       7.225  24.930  29.492  1.00 26.84           O  
ANISOU  824  O   SER A 110     3503   3317   3379     94    246   -293       O  
ATOM    825  CB  SER A 110       4.786  22.873  29.430  1.00 39.66           C  
ANISOU  825  CB  SER A 110     4993   5007   5071    136    294   -228       C  
ATOM    826  OG  SER A 110       4.098  22.074  28.483  1.00 50.96           O  
ANISOU  826  OG  SER A 110     6336   6482   6544    128    270   -198       O  
ATOM    827  N   GLU A 111       7.429  23.529  31.230  1.00 25.37           N  
ANISOU  827  N   GLU A 111     3365   3127   3148     71    242   -309       N  
ATOM    828  CA  GLU A 111       8.210  24.511  31.974  1.00 23.31           C  
ANISOU  828  CA  GLU A 111     3202   2818   2835     48    235   -333       C  
ATOM    829  C   GLU A 111       9.652  24.565  31.486  1.00 26.88           C  
ANISOU  829  C   GLU A 111     3642   3286   3283     -5    158   -341       C  
ATOM    830  O   GLU A 111      10.250  25.649  31.455  1.00 26.55           O  
ANISOU  830  O   GLU A 111     3652   3213   3223    -28    141   -350       O  
ATOM    831  CB  GLU A 111       8.145  24.197  33.470  1.00 26.61           C  
ANISOU  831  CB  GLU A 111     3702   3210   3198     42    256   -344       C  
ATOM    832  CG  GLU A 111       8.968  25.135  34.352  1.00 33.28           C  
ANISOU  832  CG  GLU A 111     4670   4001   3974      2    236   -372       C  
ATOM    833  CD  GLU A 111       8.419  26.562  34.430  1.00 40.41           C  
ANISOU  833  CD  GLU A 111     5658   4839   4857     34    297   -382       C  
ATOM    834  OE1 GLU A 111       7.360  26.868  33.831  1.00 39.74           O  
ANISOU  834  OE1 GLU A 111     5529   4755   4817     95    362   -360       O  
ATOM    835  OE2 GLU A 111       9.070  27.389  35.099  1.00 41.29           O  
ANISOU  835  OE2 GLU A 111     5886   4895   4907     -6    278   -408       O  
ATOM    836  N   LEU A 112      10.225  23.427  31.080  1.00 23.14           N  
ANISOU  836  N   LEU A 112     3102   2859   2830    -22    114   -332       N  
ATOM    837  CA  LEU A 112      11.551  23.474  30.478  1.00 22.00           C  
ANISOU  837  CA  LEU A 112     2930   2736   2693    -58     54   -323       C  
ATOM    838  C   LEU A 112      11.509  24.264  29.181  1.00 25.97           C  
ANISOU  838  C   LEU A 112     3393   3245   3228    -42     57   -316       C  
ATOM    839  O   LEU A 112      12.385  25.102  28.924  1.00 23.87           O  
ANISOU  839  O   LEU A 112     3142   2970   2959    -71     26   -308       O  
ATOM    840  CB  LEU A 112      12.078  22.063  30.236  1.00 22.62           C  
ANISOU  840  CB  LEU A 112     2948   2858   2790    -61     26   -309       C  
ATOM    841  CG  LEU A 112      13.453  21.960  29.562  1.00 23.21           C  
ANISOU  841  CG  LEU A 112     2981   2960   2878    -83    -23   -284       C  
ATOM    842  CD1 LEU A 112      14.564  22.627  30.380  1.00 22.44           C  
ANISOU  842  CD1 LEU A 112     2926   2850   2750   -137    -70   -268       C  
ATOM    843  CD2 LEU A 112      13.771  20.492  29.295  1.00 23.27           C  
ANISOU  843  CD2 LEU A 112     2938   3000   2904    -68    -28   -269       C  
ATOM    844  N   ILE A 113      10.470  24.035  28.369  1.00 18.95           N  
ANISOU  844  N   ILE A 113     2456   2374   2372     -2     90   -311       N  
ATOM    845  CA  ILE A 113      10.308  24.777  27.117  1.00 22.96           C  
ANISOU  845  CA  ILE A 113     2925   2891   2907     15     94   -299       C  
ATOM    846  C   ILE A 113      10.227  26.268  27.401  1.00 24.02           C  
ANISOU  846  C   ILE A 113     3119   2978   3029     17    117   -301       C  
ATOM    847  O   ILE A 113      10.878  27.078  26.729  1.00 26.12           O  
ANISOU  847  O   ILE A 113     3381   3240   3304      4     97   -292       O  
ATOM    848  CB  ILE A 113       9.059  24.296  26.355  1.00 24.56           C  
ANISOU  848  CB  ILE A 113     3072   3122   3140     49    120   -286       C  
ATOM    849  CG1 ILE A 113       9.245  22.866  25.820  1.00 26.17           C  
ANISOU  849  CG1 ILE A 113     3230   3363   3352     40     90   -288       C  
ATOM    850  CG2 ILE A 113       8.709  25.276  25.222  1.00 23.23           C  
ANISOU  850  CG2 ILE A 113     2873   2959   2993     70    130   -267       C  
ATOM    851  CD1 ILE A 113      10.247  22.719  24.705  1.00 28.81           C  
ANISOU  851  CD1 ILE A 113     3536   3723   3689     34     56   -284       C  
ATOM    852  N   ARG A 114       9.421  26.654  28.400  1.00 23.52           N  
ANISOU  852  N   ARG A 114     3119   2873   2946     35    166   -311       N  
ATOM    853  CA  ARG A 114       9.225  28.076  28.677  1.00 25.09           C  
ANISOU  853  CA  ARG A 114     3393   3012   3129     46    203   -315       C  
ATOM    854  C   ARG A 114      10.537  28.738  29.060  1.00 20.98           C  
ANISOU  854  C   ARG A 114     2938   2457   2575    -14    151   -330       C  
ATOM    855  O   ARG A 114      10.870  29.816  28.559  1.00 23.23           O  
ANISOU  855  O   ARG A 114     3244   2714   2868    -24    146   -324       O  
ATOM    856  CB  ARG A 114       8.192  28.276  29.790  1.00 27.18           C  
ANISOU  856  CB  ARG A 114     3728   3231   3367     85    275   -320       C  
ATOM    857  CG  ARG A 114       7.862  29.751  30.044  1.00 29.69           C  
ANISOU  857  CG  ARG A 114     4138   3474   3667    110    332   -323       C  
ATOM    858  CD  ARG A 114       6.986  29.973  31.288  1.00 33.21           C  
ANISOU  858  CD  ARG A 114     4679   3865   4073    154    415   -330       C  
ATOM    859  NE  ARG A 114       7.672  29.578  32.518  1.00 33.49           N  
ANISOU  859  NE  ARG A 114     4806   3877   4043    105    383   -366       N  
ATOM    860  CZ  ARG A 114       8.534  30.351  33.176  1.00 38.52           C  
ANISOU  860  CZ  ARG A 114     5566   4452   4619     52    352   -399       C  
ATOM    861  NH1 ARG A 114       8.815  31.569  32.730  1.00 39.58           N  
ANISOU  861  NH1 ARG A 114     5751   4534   4755     42    353   -404       N  
ATOM    862  NH2 ARG A 114       9.114  29.908  34.285  1.00 40.52           N  
ANISOU  862  NH2 ARG A 114     5895   4692   4808      3    314   -424       N  
ATOM    863  N   VAL A 115      11.300  28.099  29.946  1.00 21.98           N  
ANISOU  863  N   VAL A 115     3096   2589   2666    -60    107   -342       N  
ATOM    864  CA  VAL A 115      12.554  28.699  30.406  1.00 22.07           C  
ANISOU  864  CA  VAL A 115     3168   2573   2644   -131     45   -344       C  
ATOM    865  C   VAL A 115      13.522  28.861  29.239  1.00 19.96           C  
ANISOU  865  C   VAL A 115     2821   2345   2419   -155     -5   -313       C  
ATOM    866  O   VAL A 115      14.158  29.911  29.082  1.00 23.58           O  
ANISOU  866  O   VAL A 115     3315   2770   2874   -195    -33   -304       O  
ATOM    867  CB  VAL A 115      13.165  27.873  31.556  1.00 26.28           C  
ANISOU  867  CB  VAL A 115     3734   3116   3133   -177      1   -349       C  
ATOM    868  CG1 VAL A 115      14.597  28.339  31.869  1.00 23.74           C  
ANISOU  868  CG1 VAL A 115     3445   2786   2788   -264    -84   -332       C  
ATOM    869  CG2 VAL A 115      12.299  28.014  32.798  1.00 27.56           C  
ANISOU  869  CG2 VAL A 115     4005   3225   3240   -158     55   -380       C  
ATOM    870  N   MET A 116      13.648  27.824  28.404  1.00 22.41           N  
ANISOU  870  N   MET A 116     3026   2721   2766   -131    -15   -293       N  
ATOM    871  CA  MET A 116      14.576  27.898  27.279  1.00 24.08           C  
ANISOU  871  CA  MET A 116     3164   2973   3014   -142    -50   -258       C  
ATOM    872  C   MET A 116      14.110  28.913  26.245  1.00 23.89           C  
ANISOU  872  C   MET A 116     3126   2934   3016   -112    -20   -252       C  
ATOM    873  O   MET A 116      14.928  29.648  25.671  1.00 24.07           O  
ANISOU  873  O   MET A 116     3134   2956   3054   -139    -48   -224       O  
ATOM    874  CB  MET A 116      14.735  26.520  26.642  1.00 23.40           C  
ANISOU  874  CB  MET A 116     2992   2948   2950   -113    -53   -243       C  
ATOM    875  CG  MET A 116      15.320  25.486  27.595  1.00 23.88           C  
ANISOU  875  CG  MET A 116     3057   3025   2992   -139    -83   -238       C  
ATOM    876  SD  MET A 116      15.348  23.872  26.781  1.00 31.25           S  
ANISOU  876  SD  MET A 116     3909   4013   3952    -93    -69   -226       S  
ATOM    877  CE  MET A 116      16.801  24.096  25.790  1.00 24.88           C  
ANISOU  877  CE  MET A 116     3040   3242   3171   -102    -99   -169       C  
ATOM    878  N   TYR A 117      12.799  28.964  26.006  1.00 21.19           N  
ANISOU  878  N   TYR A 117     2783   2585   2683    -58     37   -267       N  
ATOM    879  CA  TYR A 117      12.223  29.914  25.064  1.00 21.96           C  
ANISOU  879  CA  TYR A 117     2865   2673   2808    -24     70   -253       C  
ATOM    880  C   TYR A 117      12.491  31.344  25.500  1.00 22.02           C  
ANISOU  880  C   TYR A 117     2958   2609   2801    -50     75   -256       C  
ATOM    881  O   TYR A 117      12.889  32.189  24.691  1.00 22.57           O  
ANISOU  881  O   TYR A 117     3010   2673   2893    -56     67   -232       O  
ATOM    882  CB  TYR A 117      10.724  29.652  24.973  1.00 22.24           C  
ANISOU  882  CB  TYR A 117     2882   2713   2853     33    128   -256       C  
ATOM    883  CG  TYR A 117       9.922  30.628  24.164  1.00 21.44           C  
ANISOU  883  CG  TYR A 117     2764   2600   2780     76    170   -232       C  
ATOM    884  CD1 TYR A 117       9.319  31.725  24.760  1.00 26.60           C  
ANISOU  884  CD1 TYR A 117     3492   3188   3428     99    225   -233       C  
ATOM    885  CD2 TYR A 117       9.705  30.418  22.805  1.00 23.94           C  
ANISOU  885  CD2 TYR A 117     2997   2973   3126     98    161   -204       C  
ATOM    886  CE1 TYR A 117       8.541  32.610  24.019  1.00 27.37           C  
ANISOU  886  CE1 TYR A 117     3568   3276   3556    147    271   -199       C  
ATOM    887  CE2 TYR A 117       8.919  31.293  22.059  1.00 26.56           C  
ANISOU  887  CE2 TYR A 117     3306   3301   3483    138    197   -171       C  
ATOM    888  CZ  TYR A 117       8.348  32.389  22.674  1.00 28.55           C  
ANISOU  888  CZ  TYR A 117     3621   3489   3738    164    253   -166       C  
ATOM    889  OH  TYR A 117       7.574  33.278  21.942  1.00 28.05           O  
ANISOU  889  OH  TYR A 117     3531   3421   3706    211    296   -123       O  
ATOM    890  N   GLU A 118      12.249  31.643  26.778  1.00 23.19           N  
ANISOU  890  N   GLU A 118     3207   2697   2908    -66     92   -285       N  
ATOM    891  CA  GLU A 118      12.485  33.001  27.255  1.00 20.87           C  
ANISOU  891  CA  GLU A 118     3020   2319   2590    -95     98   -294       C  
ATOM    892  C   GLU A 118      13.953  33.376  27.132  1.00 27.75           C  
ANISOU  892  C   GLU A 118     3893   3190   3460   -177     17   -275       C  
ATOM    893  O   GLU A 118      14.282  34.506  26.742  1.00 24.39           O  
ANISOU  893  O   GLU A 118     3499   2721   3045   -199     10   -261       O  
ATOM    894  CB  GLU A 118      11.987  33.150  28.693  1.00 24.99           C  
ANISOU  894  CB  GLU A 118     3668   2773   3054    -97    133   -333       C  
ATOM    895  CG  GLU A 118      10.458  33.094  28.746  1.00 31.52           C  
ANISOU  895  CG  GLU A 118     4493   3590   3892     -7    230   -333       C  
ATOM    896  CD  GLU A 118       9.875  33.295  30.139  1.00 39.22           C  
ANISOU  896  CD  GLU A 118     5600   4494   4807      9    286   -365       C  
ATOM    897  OE1 GLU A 118      10.619  33.687  31.066  1.00 39.63           O  
ANISOU  897  OE1 GLU A 118     5770   4489   4799    -55    249   -395       O  
ATOM    898  OE2 GLU A 118       8.657  33.052  30.294  1.00 37.86           O  
ANISOU  898  OE2 GLU A 118     5412   4325   4647     84    367   -353       O  
ATOM    899  N   HIS A 119      14.858  32.438  27.428  1.00 24.71           N  
ANISOU  899  N   HIS A 119     3465   2855   3067   -222    -46   -264       N  
ATOM    900  CA  HIS A 119      16.273  32.750  27.247  1.00 25.55           C  
ANISOU  900  CA  HIS A 119     3551   2975   3183   -298   -124   -225       C  
ATOM    901  C   HIS A 119      16.600  32.997  25.780  1.00 25.27           C  
ANISOU  901  C   HIS A 119     3415   2984   3205   -273   -122   -181       C  
ATOM    902  O   HIS A 119      17.314  33.954  25.448  1.00 22.94           O  
ANISOU  902  O   HIS A 119     3128   2663   2924   -318   -154   -149       O  
ATOM    903  CB  HIS A 119      17.157  31.635  27.802  1.00 22.10           C  
ANISOU  903  CB  HIS A 119     3071   2591   2734   -340   -184   -205       C  
ATOM    904  CG  HIS A 119      18.615  31.966  27.749  1.00 24.32           C  
ANISOU  904  CG  HIS A 119     3324   2889   3028   -423   -266   -148       C  
ATOM    905  ND1 HIS A 119      19.176  32.971  28.515  1.00 24.38           N  
ANISOU  905  ND1 HIS A 119     3430   2833   3001   -513   -323   -146       N  
ATOM    906  CD2 HIS A 119      19.622  31.462  26.993  1.00 26.49           C  
ANISOU  906  CD2 HIS A 119     3484   3235   3347   -429   -301    -82       C  
ATOM    907  CE1 HIS A 119      20.468  33.055  28.249  1.00 30.64           C  
ANISOU  907  CE1 HIS A 119     4157   3663   3822   -580   -397    -76       C  
ATOM    908  NE2 HIS A 119      20.763  32.151  27.328  1.00 26.32           N  
ANISOU  908  NE2 HIS A 119     3475   3199   3325   -524   -379    -33       N  
ATOM    909  N   ALA A 120      16.093  32.141  24.891  1.00 21.24           N  
ANISOU  909  N   ALA A 120     2813   2535   2721   -204    -86   -176       N  
ATOM    910  CA  ALA A 120      16.361  32.315  23.468  1.00 22.01           C  
ANISOU  910  CA  ALA A 120     2824   2677   2861   -174    -80   -135       C  
ATOM    911  C   ALA A 120      15.899  33.681  22.982  1.00 22.32           C  
ANISOU  911  C   ALA A 120     2900   2666   2916   -162    -49   -131       C  
ATOM    912  O   ALA A 120      16.634  34.357  22.251  1.00 23.35           O  
ANISOU  912  O   ALA A 120     2998   2802   3073   -183    -70    -87       O  
ATOM    913  CB  ALA A 120      15.691  31.203  22.662  1.00 24.32           C  
ANISOU  913  CB  ALA A 120     3044   3032   3166   -107    -45   -141       C  
ATOM    914  N   LEU A 121      14.705  34.124  23.403  1.00 24.60           N  
ANISOU  914  N   LEU A 121     3254   2903   3190   -126      5   -166       N  
ATOM    915  CA  LEU A 121      14.251  35.465  23.014  1.00 24.04           C  
ANISOU  915  CA  LEU A 121     3224   2774   3134   -107     43   -157       C  
ATOM    916  C   LEU A 121      15.168  36.541  23.571  1.00 26.38           C  
ANISOU  916  C   LEU A 121     3606   2998   3418   -185      2   -151       C  
ATOM    917  O   LEU A 121      15.498  37.514  22.881  1.00 25.82           O  
ANISOU  917  O   LEU A 121     3532   2905   3376   -196      0   -118       O  
ATOM    918  CB  LEU A 121      12.825  35.722  23.506  1.00 25.39           C  
ANISOU  918  CB  LEU A 121     3454   2899   3293    -47    119   -185       C  
ATOM    919  CG  LEU A 121      11.693  35.099  22.694  1.00 32.83           C  
ANISOU  919  CG  LEU A 121     4309   3903   4261     30    165   -171       C  
ATOM    920  CD1 LEU A 121      10.356  35.543  23.274  1.00 30.35           C  
ANISOU  920  CD1 LEU A 121     4051   3538   3943     88    244   -179       C  
ATOM    921  CD2 LEU A 121      11.827  35.474  21.203  1.00 31.96           C  
ANISOU  921  CD2 LEU A 121     4115   3838   4190     52    160   -125       C  
ATOM    922  N   LYS A 122      15.567  36.395  24.828  1.00 23.46           N  
ANISOU  922  N   LYS A 122     3321   2589   3003   -245    -34   -181       N  
ATOM    923  CA  LYS A 122      16.359  37.432  25.483  1.00 22.09           C  
ANISOU  923  CA  LYS A 122     3253   2335   2806   -334    -83   -180       C  
ATOM    924  C   LYS A 122      17.682  37.666  24.761  1.00 31.06           C  
ANISOU  924  C   LYS A 122     4310   3510   3980   -397   -155   -116       C  
ATOM    925  O   LYS A 122      18.138  38.810  24.643  1.00 27.07           O  
ANISOU  925  O   LYS A 122     3857   2944   3484   -450   -178    -95       O  
ATOM    926  CB  LYS A 122      16.618  37.030  26.931  1.00 23.67           C  
ANISOU  926  CB  LYS A 122     3549   2503   2942   -394   -122   -218       C  
ATOM    927  CG  LYS A 122      17.381  38.075  27.714  1.00 31.82           C  
ANISOU  927  CG  LYS A 122     4713   3445   3935   -500   -183   -222       C  
ATOM    928  CD  LYS A 122      18.026  37.455  28.939  1.00 43.39           C  
ANISOU  928  CD  LYS A 122     6231   4914   5342   -580   -256   -236       C  
ATOM    929  CE  LYS A 122      19.494  37.153  28.684  1.00 49.38           C  
ANISOU  929  CE  LYS A 122     6892   5740   6130   -670   -364   -165       C  
ATOM    930  NZ  LYS A 122      20.334  38.387  28.701  1.00 53.10           N  
ANISOU  930  NZ  LYS A 122     7430   6145   6602   -775   -432   -134       N  
ATOM    931  N   ILE A 123      18.317  36.592  24.272  1.00 25.02           N  
ANISOU  931  N   ILE A 123     3421   2844   3240   -391   -187    -79       N  
ATOM    932  CA  ILE A 123      19.610  36.709  23.604  1.00 26.73           C  
ANISOU  932  CA  ILE A 123     3551   3108   3498   -441   -246     -3       C  
ATOM    933  C   ILE A 123      19.491  36.985  22.106  1.00 30.43           C  
ANISOU  933  C   ILE A 123     3927   3617   4016   -378   -204     38       C  
ATOM    934  O   ILE A 123      20.515  37.057  21.416  1.00 28.68           O  
ANISOU  934  O   ILE A 123     3623   3441   3831   -403   -238    109       O  
ATOM    935  CB  ILE A 123      20.466  35.448  23.859  1.00 25.02           C  
ANISOU  935  CB  ILE A 123     3253   2972   3282   -462   -294     30       C  
ATOM    936  CG1 ILE A 123      19.837  34.211  23.214  1.00 25.82           C  
ANISOU  936  CG1 ILE A 123     3273   3146   3393   -364   -237     14       C  
ATOM    937  CG2 ILE A 123      20.659  35.195  25.361  1.00 28.67           C  
ANISOU  937  CG2 ILE A 123     3804   3398   3690   -533   -345     -1       C  
ATOM    938  CD1 ILE A 123      20.759  32.992  23.275  1.00 27.77           C  
ANISOU  938  CD1 ILE A 123     3435   3469   3649   -370   -270     58       C  
ATOM    939  N   GLY A 124      18.287  37.152  21.582  1.00 25.86           N  
ANISOU  939  N   GLY A 124     3358   3028   3440   -297   -131      4       N  
ATOM    940  CA  GLY A 124      18.110  37.600  20.221  1.00 24.06           C  
ANISOU  940  CA  GLY A 124     3062   2829   3251   -244    -95     43       C  
ATOM    941  C   GLY A 124      17.878  36.530  19.184  1.00 25.38           C  
ANISOU  941  C   GLY A 124     3124   3090   3428   -171    -68     57       C  
ATOM    942  O   GLY A 124      18.035  36.811  17.989  1.00 26.64           O  
ANISOU  942  O   GLY A 124     3220   3287   3614   -138    -51    102       O  
ATOM    943  N   VAL A 125      17.516  35.317  19.588  1.00 23.78           N  
ANISOU  943  N   VAL A 125     2910   2925   3202   -147    -63     21       N  
ATOM    944  CA  VAL A 125      17.022  34.350  18.614  1.00 24.63           C  
ANISOU  944  CA  VAL A 125     2946   3103   3309    -77    -31     20       C  
ATOM    945  C   VAL A 125      15.753  34.902  17.987  1.00 25.01           C  
ANISOU  945  C   VAL A 125     3003   3139   3362    -21     19      8       C  
ATOM    946  O   VAL A 125      14.861  35.401  18.689  1.00 26.71           O  
ANISOU  946  O   VAL A 125     3281   3297   3569    -15     45    -24       O  
ATOM    947  CB  VAL A 125      16.769  32.988  19.281  1.00 23.67           C  
ANISOU  947  CB  VAL A 125     2826   3007   3160    -68    -35    -20       C  
ATOM    948  CG1 VAL A 125      16.163  32.022  18.270  1.00 21.71           C  
ANISOU  948  CG1 VAL A 125     2523   2819   2905     -4     -6    -26       C  
ATOM    949  CG2 VAL A 125      18.072  32.429  19.848  1.00 23.23           C  
ANISOU  949  CG2 VAL A 125     2750   2971   3105   -117    -83      8       C  
ATOM    950  N   GLU A 126      15.692  34.871  16.651  1.00 22.74           N  
ANISOU  950  N   GLU A 126     2651   2903   3086     21     35     43       N  
ATOM    951  CA  GLU A 126      14.472  35.225  15.942  1.00 24.54           C  
ANISOU  951  CA  GLU A 126     2869   3137   3317     74     74     44       C  
ATOM    952  C   GLU A 126      13.575  33.994  15.912  1.00 27.82           C  
ANISOU  952  C   GLU A 126     3267   3595   3708    105     82     10       C  
ATOM    953  O   GLU A 126      14.002  32.929  15.450  1.00 27.06           O  
ANISOU  953  O   GLU A 126     3137   3550   3593    111     65      7       O  
ATOM    954  CB  GLU A 126      14.812  35.701  14.534  1.00 24.94           C  
ANISOU  954  CB  GLU A 126     2865   3228   3381     99     81     98       C  
ATOM    955  CG  GLU A 126      13.640  36.226  13.761  1.00 33.19           C  
ANISOU  955  CG  GLU A 126     3895   4282   4433    147    114    115       C  
ATOM    956  CD  GLU A 126      14.076  36.848  12.449  1.00 45.76           C  
ANISOU  956  CD  GLU A 126     5443   5907   6037    166    120    174       C  
ATOM    957  OE1 GLU A 126      15.298  36.840  12.164  1.00 49.81           O  
ANISOU  957  OE1 GLU A 126     5935   6436   6555    144    102    203       O  
ATOM    958  OE2 GLU A 126      13.199  37.342  11.713  1.00 50.46           O  
ANISOU  958  OE2 GLU A 126     6018   6516   6637    205    143    201       O  
ATOM    959  N   ILE A 127      12.364  34.114  16.440  1.00 23.88           N  
ANISOU  959  N   ILE A 127     2794   3070   3210    125    109    -12       N  
ATOM    960  CA  ILE A 127      11.453  32.974  16.564  1.00 24.77           C  
ANISOU  960  CA  ILE A 127     2890   3217   3305    144    111    -38       C  
ATOM    961  C   ILE A 127      10.154  33.289  15.834  1.00 27.88           C  
ANISOU  961  C   ILE A 127     3250   3633   3711    186    137     -9       C  
ATOM    962  O   ILE A 127       9.567  34.367  16.018  1.00 24.79           O  
ANISOU  962  O   ILE A 127     2874   3200   3343    208    174     14       O  
ATOM    963  CB  ILE A 127      11.182  32.623  18.041  1.00 24.10           C  
ANISOU  963  CB  ILE A 127     2859   3088   3212    126    119    -79       C  
ATOM    964  CG1 ILE A 127      12.457  32.079  18.706  1.00 25.72           C  
ANISOU  964  CG1 ILE A 127     3085   3288   3401     80     81   -100       C  
ATOM    965  CG2 ILE A 127      10.035  31.612  18.173  1.00 24.17           C  
ANISOU  965  CG2 ILE A 127     2844   3127   3212    148    128    -94       C  
ATOM    966  CD1 ILE A 127      12.268  31.738  20.169  1.00 26.54           C  
ANISOU  966  CD1 ILE A 127     3246   3350   3487     59     84   -138       C  
ATOM    967  N   SER A 128       9.678  32.333  15.033  1.00 21.71           N  
ANISOU  967  N   SER A 128     2425   2913   2911    196    117     -5       N  
ATOM    968  CA  SER A 128       8.414  32.476  14.313  1.00 21.86           C  
ANISOU  968  CA  SER A 128     2400   2966   2939    223    125     33       C  
ATOM    969  C   SER A 128       7.562  31.262  14.628  1.00 25.95           C  
ANISOU  969  C   SER A 128     2906   3511   3444    213    108     14       C  
ATOM    970  O   SER A 128       7.875  30.154  14.176  1.00 24.61           O  
ANISOU  970  O   SER A 128     2734   3376   3241    193     72    -10       O  
ATOM    971  CB  SER A 128       8.643  32.596  12.806  1.00 27.91           C  
ANISOU  971  CB  SER A 128     3130   3785   3688    233    104     68       C  
ATOM    972  OG  SER A 128       9.364  33.784  12.507  1.00 28.17           O  
ANISOU  972  OG  SER A 128     3168   3793   3741    243    123     96       O  
ATOM    973  N   LEU A 129       6.509  31.466  15.412  1.00 22.78           N  
ANISOU  973  N   LEU A 129     2499   3088   3068    230    140     28       N  
ATOM    974  CA  LEU A 129       5.566  30.416  15.753  1.00 21.00           C  
ANISOU  974  CA  LEU A 129     2251   2888   2841    219    127     25       C  
ATOM    975  C   LEU A 129       4.435  30.376  14.737  1.00 25.84           C  
ANISOU  975  C   LEU A 129     2796   3559   3463    225    106     86       C  
ATOM    976  O   LEU A 129       4.215  31.330  13.986  1.00 27.25           O  
ANISOU  976  O   LEU A 129     2946   3752   3657    251    118    136       O  
ATOM    977  CB  LEU A 129       4.987  30.649  17.149  1.00 24.79           C  
ANISOU  977  CB  LEU A 129     2756   3319   3344    238    178     22       C  
ATOM    978  CG  LEU A 129       6.003  30.778  18.286  1.00 24.46           C  
ANISOU  978  CG  LEU A 129     2790   3216   3287    224    193    -34       C  
ATOM    979  CD1 LEU A 129       5.246  30.886  19.601  1.00 27.02           C  
ANISOU  979  CD1 LEU A 129     3147   3497   3624    247    246    -35       C  
ATOM    980  CD2 LEU A 129       6.953  29.591  18.329  1.00 26.99           C  
ANISOU  980  CD2 LEU A 129     3124   3555   3576    183    144    -82       C  
ATOM    981  N   GLY A 130       3.691  29.269  14.747  1.00 22.78           N  
ANISOU  981  N   GLY A 130     2382   3205   3067    197     72     89       N  
ATOM    982  CA  GLY A 130       2.632  29.089  13.768  1.00 26.16           C  
ANISOU  982  CA  GLY A 130     2747   3695   3499    185     33    152       C  
ATOM    983  C   GLY A 130       3.145  28.976  12.347  1.00 27.55           C  
ANISOU  983  C   GLY A 130     2928   3912   3628    164    -19    150       C  
ATOM    984  O   GLY A 130       2.440  29.351  11.403  1.00 26.46           O  
ANISOU  984  O   GLY A 130     2741   3822   3492    164    -44    213       O  
ATOM    985  N   VAL A 131       4.357  28.462  12.168  1.00 25.00           N  
ANISOU  985  N   VAL A 131     2664   3573   3263    151    -32     85       N  
ATOM    986  CA  VAL A 131       4.955  28.309  10.844  1.00 22.37           C  
ANISOU  986  CA  VAL A 131     2350   3273   2876    141    -67     80       C  
ATOM    987  C   VAL A 131       5.391  26.860  10.669  1.00 23.12           C  
ANISOU  987  C   VAL A 131     2500   3367   2916    104   -105     22       C  
ATOM    988  O   VAL A 131       6.153  26.331  11.491  1.00 24.21           O  
ANISOU  988  O   VAL A 131     2676   3466   3055    106    -85    -29       O  
ATOM    989  CB  VAL A 131       6.146  29.252  10.640  1.00 23.96           C  
ANISOU  989  CB  VAL A 131     2572   3452   3081    175    -30     74       C  
ATOM    990  CG1 VAL A 131       6.841  28.945   9.313  1.00 27.64           C  
ANISOU  990  CG1 VAL A 131     3064   3952   3486    172    -56     69       C  
ATOM    991  CG2 VAL A 131       5.681  30.703  10.684  1.00 25.95           C  
ANISOU  991  CG2 VAL A 131     2781   3697   3383    211      8    134       C  
ATOM    992  N   GLU A 132       4.891  26.219   9.610  1.00 27.82           N  
ANISOU  992  N   GLU A 132     3106   4003   3462     69   -162     32       N  
ATOM    993  CA  GLU A 132       5.315  24.880   9.225  1.00 26.89           C  
ANISOU  993  CA  GLU A 132     3062   3877   3279     36   -195    -23       C  
ATOM    994  C   GLU A 132       6.366  25.020   8.132  1.00 28.66           C  
ANISOU  994  C   GLU A 132     3337   4108   3444     62   -184    -37       C  
ATOM    995  O   GLU A 132       6.112  25.645   7.098  1.00 29.31           O  
ANISOU  995  O   GLU A 132     3404   4230   3503     66   -202      5       O  
ATOM    996  CB  GLU A 132       4.130  24.055   8.726  1.00 31.70           C  
ANISOU  996  CB  GLU A 132     3672   4515   3858    -28   -268     -5       C  
ATOM    997  CG  GLU A 132       4.520  22.745   8.056  1.00 34.63           C  
ANISOU  997  CG  GLU A 132     4142   4870   4145    -65   -306    -62       C  
ATOM    998  CD  GLU A 132       3.358  22.118   7.285  1.00 55.90           C  
ANISOU  998  CD  GLU A 132     6846   7598   6796   -143   -396    -35       C  
ATOM    999  OE1 GLU A 132       2.219  22.625   7.399  1.00 59.49           O  
ANISOU  999  OE1 GLU A 132     7211   8093   7298   -167   -428     36       O  
ATOM   1000  OE2 GLU A 132       3.590  21.123   6.561  1.00 62.16           O  
ANISOU 1000  OE2 GLU A 132     7739   8374   7506   -180   -434    -80       O  
ATOM   1001  N   VAL A 133       7.540  24.465   8.370  1.00 22.30           N  
ANISOU 1001  N   VAL A 133     2585   3268   2618     85   -150    -86       N  
ATOM   1002  CA  VAL A 133       8.634  24.510   7.407  1.00 24.18           C  
ANISOU 1002  CA  VAL A 133     2871   3512   2804    120   -125    -92       C  
ATOM   1003  C   VAL A 133       8.527  23.294   6.506  1.00 29.70           C  
ANISOU 1003  C   VAL A 133     3662   4209   3413     94   -158   -127       C  
ATOM   1004  O   VAL A 133       8.277  22.177   6.981  1.00 29.67           O  
ANISOU 1004  O   VAL A 133     3702   4176   3397     62   -177   -168       O  
ATOM   1005  CB  VAL A 133       9.992  24.527   8.122  1.00 25.72           C  
ANISOU 1005  CB  VAL A 133     3072   3673   3027    161    -67   -110       C  
ATOM   1006  CG1 VAL A 133      11.138  24.458   7.113  1.00 28.00           C  
ANISOU 1006  CG1 VAL A 133     3405   3970   3264    204    -32   -104       C  
ATOM   1007  CG2 VAL A 133      10.102  25.758   8.989  1.00 28.54           C  
ANISOU 1007  CG2 VAL A 133     3360   4023   3463    174    -43    -79       C  
ATOM   1008  N   CYS A 134       8.728  23.495   5.206  1.00 24.79           N  
ANISOU 1008  N   CYS A 134     3079   3615   2724    107   -164   -111       N  
ATOM   1009  CA  CYS A 134       8.738  22.370   4.277  1.00 27.14           C  
ANISOU 1009  CA  CYS A 134     3492   3901   2919     86   -189   -149       C  
ATOM   1010  C   CYS A 134       9.737  22.642   3.158  1.00 26.47           C  
ANISOU 1010  C   CYS A 134     3461   3828   2770    143   -142   -139       C  
ATOM   1011  O   CYS A 134      10.371  23.700   3.098  1.00 27.11           O  
ANISOU 1011  O   CYS A 134     3479   3930   2892    192    -98    -96       O  
ATOM   1012  CB  CYS A 134       7.347  22.113   3.708  1.00 33.06           C  
ANISOU 1012  CB  CYS A 134     4252   4680   3629      8   -280   -136       C  
ATOM   1013  SG  CYS A 134       6.726  23.527   2.823  1.00 45.40           S  
ANISOU 1013  SG  CYS A 134     5736   6316   5200     10   -310    -54       S  
ATOM   1014  N   GLU A 135       9.860  21.660   2.265  1.00 25.68           N  
ANISOU 1014  N   GLU A 135     3487   3708   2564    136   -151   -177       N  
ATOM   1015  CA  GLU A 135      10.606  21.793   1.018  1.00 28.22           C  
ANISOU 1015  CA  GLU A 135     3883   4042   2799    187   -110   -166       C  
ATOM   1016  C   GLU A 135      12.015  22.364   1.227  1.00 27.34           C  
ANISOU 1016  C   GLU A 135     3727   3928   2735    277    -12   -136       C  
ATOM   1017  O   GLU A 135      12.346  23.426   0.691  1.00 28.40           O  
ANISOU 1017  O   GLU A 135     3808   4102   2881    311     10    -82       O  
ATOM   1018  CB  GLU A 135       9.827  22.630   0.017  1.00 29.79           C  
ANISOU 1018  CB  GLU A 135     4059   4301   2961    157   -167   -119       C  
ATOM   1019  CG  GLU A 135       8.475  22.004  -0.356  1.00 37.53           C  
ANISOU 1019  CG  GLU A 135     5087   5290   3881     59   -273   -135       C  
ATOM   1020  CD  GLU A 135       7.560  22.947  -1.136  1.00 43.32           C  
ANISOU 1020  CD  GLU A 135     5761   6094   4603     22   -341    -68       C  
ATOM   1021  OE1 GLU A 135       8.043  23.584  -2.096  1.00 40.21           O  
ANISOU 1021  OE1 GLU A 135     5386   5732   4161     67   -312    -36       O  
ATOM   1022  OE2 GLU A 135       6.359  23.046  -0.783  1.00 48.74           O  
ANISOU 1022  OE2 GLU A 135     6379   6809   5333    -48   -419    -39       O  
ATOM   1023  N   PRO A 136      12.863  21.684   1.984  1.00 29.57           N  
ANISOU 1023  N   PRO A 136     4025   4166   3046    313     44   -161       N  
ATOM   1024  CA  PRO A 136      14.253  22.135   2.087  1.00 30.46           C  
ANISOU 1024  CA  PRO A 136     4096   4281   3198    393    132   -118       C  
ATOM   1025  C   PRO A 136      14.999  21.892   0.786  1.00 31.06           C  
ANISOU 1025  C   PRO A 136     4267   4360   3177    459    193   -104       C  
ATOM   1026  O   PRO A 136      14.735  20.933   0.052  1.00 29.22           O  
ANISOU 1026  O   PRO A 136     4168   4097   2836    454    189   -150       O  
ATOM   1027  CB  PRO A 136      14.818  21.273   3.219  1.00 32.37           C  
ANISOU 1027  CB  PRO A 136     4337   4476   3486    406    164   -145       C  
ATOM   1028  CG  PRO A 136      14.058  19.991   3.094  1.00 32.83           C  
ANISOU 1028  CG  PRO A 136     4509   4492   3472    363    126   -213       C  
ATOM   1029  CD  PRO A 136      12.645  20.418   2.714  1.00 30.39           C  
ANISOU 1029  CD  PRO A 136     4188   4215   3144    283     31   -219       C  
ATOM   1030  N   SER A 137      15.934  22.787   0.489  1.00 29.17           N  
ANISOU 1030  N   SER A 137     3963   4152   2971    519    253    -37       N  
ATOM   1031  CA  SER A 137      16.875  22.553  -0.594  1.00 30.23           C  
ANISOU 1031  CA  SER A 137     4174   4287   3026    602    337     -9       C  
ATOM   1032  C   SER A 137      18.226  23.144  -0.215  1.00 24.55           C  
ANISOU 1032  C   SER A 137     3355   3583   2391    670    417     69       C  
ATOM   1033  O   SER A 137      18.343  23.954   0.719  1.00 25.56           O  
ANISOU 1033  O   SER A 137     3359   3726   2628    642    392    101       O  
ATOM   1034  CB  SER A 137      16.372  23.123  -1.927  1.00 40.62           C  
ANISOU 1034  CB  SER A 137     5535   5642   4255    597    313      8       C  
ATOM   1035  OG  SER A 137      16.134  24.502  -1.810  1.00 39.25           O  
ANISOU 1035  OG  SER A 137     5234   5518   4160    576    280     65       O  
ATOM   1036  N   GLU A 138      19.252  22.721  -0.947  1.00 26.66           N  
ANISOU 1036  N   GLU A 138     3683   3843   2603    760    514    103       N  
ATOM   1037  CA  GLU A 138      20.617  23.130  -0.644  1.00 31.44           C  
ANISOU 1037  CA  GLU A 138     4193   4465   3286    829    595    193       C  
ATOM   1038  C   GLU A 138      21.457  23.052  -1.908  1.00 36.83           C  
ANISOU 1038  C   GLU A 138     4940   5162   3890    929    697    248       C  
ATOM   1039  O   GLU A 138      21.145  22.299  -2.838  1.00 33.66           O  
ANISOU 1039  O   GLU A 138     4690   4736   3363    956    722    200       O  
ATOM   1040  CB  GLU A 138      21.231  22.241   0.452  1.00 29.97           C  
ANISOU 1040  CB  GLU A 138     3990   4241   3156    846    626    186       C  
ATOM   1041  CG  GLU A 138      21.131  20.766   0.123  1.00 35.80           C  
ANISOU 1041  CG  GLU A 138     4885   4922   3796    882    669    121       C  
ATOM   1042  CD  GLU A 138      22.041  19.895   0.962  1.00 44.13           C  
ANISOU 1042  CD  GLU A 138     5924   5942   4901    933    735    144       C  
ATOM   1043  OE1 GLU A 138      22.646  20.413   1.920  1.00 33.47           O  
ANISOU 1043  OE1 GLU A 138     4435   4617   3663    922    728    205       O  
ATOM   1044  OE2 GLU A 138      22.162  18.690   0.642  1.00 37.60           O  
ANISOU 1044  OE2 GLU A 138     5229   5060   3996    983    794    104       O  
ATOM   1045  N   ASP A 139      22.523  23.843  -1.936  1.00 30.35           N  
ANISOU 1045  N   ASP A 139     4011   4380   3142    980    756    353       N  
ATOM   1046  CA  ASP A 139      23.558  23.670  -2.946  1.00 31.05           C  
ANISOU 1046  CA  ASP A 139     4142   4481   3175   1093    878    427       C  
ATOM   1047  C   ASP A 139      24.904  23.859  -2.256  1.00 35.40           C  
ANISOU 1047  C   ASP A 139     4561   5048   3839   1143    945    536       C  
ATOM   1048  O   ASP A 139      25.014  23.798  -1.026  1.00 32.52           O  
ANISOU 1048  O   ASP A 139     4112   4674   3570   1094    899    534       O  
ATOM   1049  CB  ASP A 139      23.319  24.594  -4.159  1.00 38.98           C  
ANISOU 1049  CB  ASP A 139     5160   5531   4121   1105    879    462       C  
ATOM   1050  CG  ASP A 139      23.521  26.075  -3.850  1.00 45.71           C  
ANISOU 1050  CG  ASP A 139     5846   6434   5089   1065    838    544       C  
ATOM   1051  OD1 ASP A 139      23.981  26.432  -2.751  1.00 37.31           O  
ANISOU 1051  OD1 ASP A 139     4660   5371   4146   1032    816    581       O  
ATOM   1052  OD2 ASP A 139      23.214  26.897  -4.741  1.00 51.89           O  
ANISOU 1052  OD2 ASP A 139     6629   7253   5835   1064    827    571       O  
ATOM   1053  N   GLU A 140      25.953  24.087  -3.048  1.00 36.59           N  
ANISOU 1053  N   GLU A 140     4692   5230   3982   1242   1052    642       N  
ATOM   1054  CA  GLU A 140      27.285  24.179  -2.473  1.00 38.47           C  
ANISOU 1054  CA  GLU A 140     4801   5490   4326   1293   1120    765       C  
ATOM   1055  C   GLU A 140      27.484  25.453  -1.653  1.00 38.93           C  
ANISOU 1055  C   GLU A 140     4683   5589   4520   1207   1037    830       C  
ATOM   1056  O   GLU A 140      28.407  25.505  -0.831  1.00 41.37           O  
ANISOU 1056  O   GLU A 140     4876   5911   4931   1209   1050    915       O  
ATOM   1057  CB  GLU A 140      28.318  24.077  -3.596  1.00 48.02           C  
ANISOU 1057  CB  GLU A 140     6035   6723   5488   1427   1265    872       C  
ATOM   1058  CG  GLU A 140      29.744  23.958  -3.128  1.00 67.84           C  
ANISOU 1058  CG  GLU A 140     8421   9257   8099   1499   1354   1015       C  
ATOM   1059  CD  GLU A 140      30.512  25.256  -3.296  1.00 88.29           C  
ANISOU 1059  CD  GLU A 140    10848  11915  10785   1494   1358   1157       C  
ATOM   1060  OE1 GLU A 140      29.870  26.326  -3.410  1.00 93.36           O  
ANISOU 1060  OE1 GLU A 140    11453  12578  11443   1409   1266   1131       O  
ATOM   1061  OE2 GLU A 140      31.760  25.203  -3.325  1.00 93.96           O  
ANISOU 1061  OE2 GLU A 140    11471  12664  11564   1576   1455   1303       O  
ATOM   1062  N   GLU A 141      26.632  26.469  -1.832  1.00 39.13           N  
ANISOU 1062  N   GLU A 141     4691   5629   4548   1130    950    793       N  
ATOM   1063  CA  GLU A 141      26.823  27.759  -1.179  1.00 41.71           C  
ANISOU 1063  CA  GLU A 141     4872   5982   4993   1053    881    855       C  
ATOM   1064  C   GLU A 141      25.809  28.083  -0.091  1.00 37.43           C  
ANISOU 1064  C   GLU A 141     4313   5412   4495    936    759    762       C  
ATOM   1065  O   GLU A 141      26.084  28.954   0.742  1.00 36.21           O  
ANISOU 1065  O   GLU A 141     4052   5263   4442    870    704    806       O  
ATOM   1066  CB  GLU A 141      26.800  28.891  -2.216  1.00 44.71           C  
ANISOU 1066  CB  GLU A 141     5226   6402   5361   1065    892    915       C  
ATOM   1067  CG  GLU A 141      28.184  29.446  -2.501  1.00 68.07           C  
ANISOU 1067  CG  GLU A 141     8071   9403   8389   1121    969   1074       C  
ATOM   1068  CD  GLU A 141      28.258  30.219  -3.800  1.00 88.75           C  
ANISOU 1068  CD  GLU A 141    10697  12061  10964   1169   1017   1137       C  
ATOM   1069  OE1 GLU A 141      27.280  30.922  -4.143  1.00 95.60           O  
ANISOU 1069  OE1 GLU A 141    11593  12927  11802   1116    950   1081       O  
ATOM   1070  OE2 GLU A 141      29.299  30.114  -4.483  1.00 91.08           O  
ANISOU 1070  OE2 GLU A 141    10965  12387  11254   1265   1126   1250       O  
ATOM   1071  N   GLY A 142      24.651  27.435  -0.078  1.00 31.95           N  
ANISOU 1071  N   GLY A 142     3725   4687   3729    908    715    641       N  
ATOM   1072  CA  GLY A 142      23.683  27.744   0.952  1.00 33.27           C  
ANISOU 1072  CA  GLY A 142     3872   4830   3940    808    611    565       C  
ATOM   1073  C   GLY A 142      22.514  26.788   0.895  1.00 32.00           C  
ANISOU 1073  C   GLY A 142     3827   4637   3694    788    576    446       C  
ATOM   1074  O   GLY A 142      22.522  25.806   0.147  1.00 29.47           O  
ANISOU 1074  O   GLY A 142     3613   4304   3279    845    628    417       O  
ATOM   1075  N   ALA A 143      21.502  27.105   1.699  1.00 28.41           N  
ANISOU 1075  N   ALA A 143     3357   4166   3274    704    488    383       N  
ATOM   1076  CA  ALA A 143      20.329  26.261   1.850  1.00 24.14           C  
ANISOU 1076  CA  ALA A 143     2903   3596   2672    667    439    281       C  
ATOM   1077  C   ALA A 143      19.098  27.151   1.916  1.00 31.23           C  
ANISOU 1077  C   ALA A 143     3777   4503   3586    599    360    252       C  
ATOM   1078  O   ALA A 143      19.191  28.364   2.146  1.00 28.56           O  
ANISOU 1078  O   ALA A 143     3355   4179   3317    576    343    300       O  
ATOM   1079  CB  ALA A 143      20.431  25.381   3.100  1.00 28.17           C  
ANISOU 1079  CB  ALA A 143     3413   4070   3222    644    426    239       C  
ATOM   1080  N   SER A 144      17.929  26.544   1.723  1.00 25.57           N  
ANISOU 1080  N   SER A 144     3133   3775   2806    564    312    179       N  
ATOM   1081  CA  SER A 144      16.694  27.302   1.831  1.00 25.80           C  
ANISOU 1081  CA  SER A 144     3130   3816   2855    504    241    164       C  
ATOM   1082  C   SER A 144      15.559  26.372   2.236  1.00 28.18           C  
ANISOU 1082  C   SER A 144     3488   4095   3123    453    184     87       C  
ATOM   1083  O   SER A 144      15.629  25.147   2.076  1.00 27.93           O  
ANISOU 1083  O   SER A 144     3544   4041   3028    463    196     40       O  
ATOM   1084  CB  SER A 144      16.355  28.023   0.523  1.00 33.72           C  
ANISOU 1084  CB  SER A 144     4145   4861   3805    520    238    203       C  
ATOM   1085  OG  SER A 144      15.813  27.118  -0.415  1.00 41.57           O  
ANISOU 1085  OG  SER A 144     5248   5862   4686    521    224    161       O  
ATOM   1086  N   VAL A 145      14.508  26.980   2.773  1.00 27.64           N  
ANISOU 1086  N   VAL A 145     3368   4031   3101    399    126     80       N  
ATOM   1087  CA  VAL A 145      13.282  26.290   3.141  1.00 22.58           C  
ANISOU 1087  CA  VAL A 145     2758   3379   2443    344     65     26       C  
ATOM   1088  C   VAL A 145      12.112  27.184   2.756  1.00 26.91           C  
ANISOU 1088  C   VAL A 145     3261   3962   3000    311     14     57       C  
ATOM   1089  O   VAL A 145      12.266  28.383   2.524  1.00 30.37           O  
ANISOU 1089  O   VAL A 145     3640   4421   3480    329     29    112       O  
ATOM   1090  CB  VAL A 145      13.204  25.958   4.647  1.00 25.91           C  
ANISOU 1090  CB  VAL A 145     3147   3763   2936    316     57     -6       C  
ATOM   1091  CG1 VAL A 145      14.304  25.007   5.065  1.00 28.73           C  
ANISOU 1091  CG1 VAL A 145     3541   4089   3285    348    104    -28       C  
ATOM   1092  CG2 VAL A 145      13.243  27.237   5.480  1.00 27.91           C  
ANISOU 1092  CG2 VAL A 145     3309   4014   3282    309     60     31       C  
ATOM   1093  N   VAL A 146      10.929  26.581   2.726  1.00 25.63           N  
ANISOU 1093  N   VAL A 146     3125   3805   2807    259    -47     29       N  
ATOM   1094  CA  VAL A 146       9.674  27.300   2.558  1.00 24.00           C  
ANISOU 1094  CA  VAL A 146     2861   3634   2623    223   -100     68       C  
ATOM   1095  C   VAL A 146       9.005  27.369   3.919  1.00 28.51           C  
ANISOU 1095  C   VAL A 146     3373   4180   3278    194   -113     58       C  
ATOM   1096  O   VAL A 146       8.802  26.334   4.567  1.00 26.70           O  
ANISOU 1096  O   VAL A 146     3179   3924   3044    166   -130      9       O  
ATOM   1097  CB  VAL A 146       8.756  26.601   1.541  1.00 27.73           C  
ANISOU 1097  CB  VAL A 146     3397   4138   3003    176   -168     61       C  
ATOM   1098  CG1 VAL A 146       7.412  27.314   1.476  1.00 29.61           C  
ANISOU 1098  CG1 VAL A 146     3556   4419   3278    137   -226    119       C  
ATOM   1099  CG2 VAL A 146       9.429  26.527   0.155  1.00 31.46           C  
ANISOU 1099  CG2 VAL A 146     3948   4631   3375    209   -149     69       C  
ATOM   1100  N   ALA A 147       8.662  28.580   4.357  1.00 26.57           N  
ANISOU 1100  N   ALA A 147     3048   3940   3109    206   -100    105       N  
ATOM   1101  CA  ALA A 147       7.932  28.784   5.601  1.00 26.14           C  
ANISOU 1101  CA  ALA A 147     2943   3861   3129    189   -102    105       C  
ATOM   1102  C   ALA A 147       6.463  29.039   5.278  1.00 26.40           C  
ANISOU 1102  C   ALA A 147     2927   3934   3170    160   -149    155       C  
ATOM   1103  O   ALA A 147       6.140  29.976   4.535  1.00 29.23           O  
ANISOU 1103  O   ALA A 147     3245   4327   3533    177   -152    218       O  
ATOM   1104  CB  ALA A 147       8.532  29.946   6.393  1.00 26.79           C  
ANISOU 1104  CB  ALA A 147     2983   3908   3286    222    -49    124       C  
ATOM   1105  N   LEU A 148       5.581  28.193   5.818  1.00 23.39           N  
ANISOU 1105  N   LEU A 148     2543   3551   2793    117   -187    139       N  
ATOM   1106  CA  LEU A 148       4.137  28.248   5.594  1.00 25.88           C  
ANISOU 1106  CA  LEU A 148     2802   3910   3121     81   -240    198       C  
ATOM   1107  C   LEU A 148       3.421  28.699   6.862  1.00 25.78           C  
ANISOU 1107  C   LEU A 148     2721   3875   3198     95   -207    226       C  
ATOM   1108  O   LEU A 148       3.487  28.009   7.881  1.00 28.60           O  
ANISOU 1108  O   LEU A 148     3097   4194   3574     83   -195    178       O  
ATOM   1109  CB  LEU A 148       3.607  26.865   5.214  1.00 30.36           C  
ANISOU 1109  CB  LEU A 148     3420   4492   3623     12   -314    169       C  
ATOM   1110  CG  LEU A 148       2.776  26.662   3.979  1.00 51.14           C  
ANISOU 1110  CG  LEU A 148     6055   7184   6193    -40   -396    216       C  
ATOM   1111  CD1 LEU A 148       3.579  27.243   2.898  1.00 49.59           C  
ANISOU 1111  CD1 LEU A 148     5896   7005   5942     -3   -378    221       C  
ATOM   1112  CD2 LEU A 148       2.605  25.184   3.744  1.00 52.02           C  
ANISOU 1112  CD2 LEU A 148     6253   7282   6229   -111   -461    160       C  
ATOM   1113  N   THR A 149       2.681  29.803   6.790  1.00 27.39           N  
ANISOU 1113  N   THR A 149     2850   4102   3455    123   -189    307       N  
ATOM   1114  CA  THR A 149       1.775  30.059   7.907  1.00 30.84           C  
ANISOU 1114  CA  THR A 149     3229   4522   3968    136   -157    343       C  
ATOM   1115  C   THR A 149       0.475  29.273   7.740  1.00 34.51           C  
ANISOU 1115  C   THR A 149     3644   5037   4432     81   -225    393       C  
ATOM   1116  O   THR A 149       0.183  28.714   6.681  1.00 33.40           O  
ANISOU 1116  O   THR A 149     3513   4946   4232     27   -303    408       O  
ATOM   1117  CB  THR A 149       1.444  31.543   8.036  1.00 31.17           C  
ANISOU 1117  CB  THR A 149     3212   4556   4074    198    -96    416       C  
ATOM   1118  OG1 THR A 149       0.541  31.927   6.982  1.00 37.91           O  
ANISOU 1118  OG1 THR A 149     3999   5480   4926    190   -137    512       O  
ATOM   1119  CG2 THR A 149       2.707  32.380   8.000  1.00 31.43           C  
ANISOU 1119  CG2 THR A 149     3293   4545   4106    238    -45    380       C  
ATOM   1120  N   ARG A 150      -0.341  29.279   8.801  1.00 41.57           N  
ANISOU 1120  N   ARG A 150     4377   6191   5227    487     67    -19       N  
ATOM   1121  CA  ARG A 150      -1.619  28.577   8.766  1.00 39.06           C  
ANISOU 1121  CA  ARG A 150     3899   6010   4934    448     -7     54       C  
ATOM   1122  C   ARG A 150      -2.605  29.203   7.798  1.00 42.21           C  
ANISOU 1122  C   ARG A 150     4129   6531   5380    538    -47    243       C  
ATOM   1123  O   ARG A 150      -3.539  28.522   7.364  1.00 45.29           O  
ANISOU 1123  O   ARG A 150     4381   7077   5751    469   -169    327       O  
ATOM   1124  CB  ARG A 150      -2.245  28.533  10.155  1.00 45.73           C  
ANISOU 1124  CB  ARG A 150     4705   6807   5862    453    116     31       C  
ATOM   1125  CG  ARG A 150      -1.441  27.778  11.175  1.00 44.00           C  
ANISOU 1125  CG  ARG A 150     4624   6501   5594    341    134   -131       C  
ATOM   1126  CD  ARG A 150      -1.949  28.115  12.558  1.00 56.86           C  
ANISOU 1126  CD  ARG A 150     6246   8057   7301    365    295   -148       C  
ATOM   1127  NE  ARG A 150      -1.032  27.700  13.610  1.00 67.55           N  
ANISOU 1127  NE  ARG A 150     7752   9310   8604    263    334   -289       N  
ATOM   1128  CZ  ARG A 150      -1.167  28.060  14.881  1.00 69.56           C  
ANISOU 1128  CZ  ARG A 150     8062   9475   8892    256    483   -332       C  
ATOM   1129  NH1 ARG A 150      -2.178  28.843  15.229  1.00 67.51           N  
ANISOU 1129  NH1 ARG A 150     7727   9198   8726    366    629   -252       N  
ATOM   1130  NH2 ARG A 150      -0.296  27.645  15.796  1.00 64.95           N  
ANISOU 1130  NH2 ARG A 150     7611   8822   8247    140    495   -442       N  
ATOM   1131  N   ASP A 151      -2.443  30.480   7.465  1.00 36.42           N  
ANISOU 1131  N   ASP A 151     3399   5735   4706    679     50    328       N  
ATOM   1132  CA  ASP A 151      -3.298  31.109   6.475  1.00 39.75           C  
ANISOU 1132  CA  ASP A 151     3652   6276   5175    771      8    534       C  
ATOM   1133  C   ASP A 151      -2.775  30.926   5.061  1.00 41.35           C  
ANISOU 1133  C   ASP A 151     3891   6566   5253    714   -155    556       C  
ATOM   1134  O   ASP A 151      -3.341  31.493   4.121  1.00 45.40           O  
ANISOU 1134  O   ASP A 151     4278   7185   5785    777   -207    734       O  
ATOM   1135  CB  ASP A 151      -3.478  32.595   6.781  1.00 49.53           C  
ANISOU 1135  CB  ASP A 151     4873   7397   6550    965    209    638       C  
ATOM   1136  CG  ASP A 151      -4.703  32.864   7.638  1.00 46.87           C  
ANISOU 1136  CG  ASP A 151     4384   7069   6357   1059    348    749       C  
ATOM   1137  OD1 ASP A 151      -5.011  34.047   7.870  1.00 48.87           O  
ANISOU 1137  OD1 ASP A 151     4614   7221   6733   1232    536    854       O  
ATOM   1138  OD2 ASP A 151      -5.361  31.895   8.082  1.00 41.80           O  
ANISOU 1138  OD2 ASP A 151     3648   6527   5707    965    283    736       O  
ATOM   1139  N   GLY A 152      -1.719  30.142   4.891  1.00 39.02           N  
ANISOU 1139  N   GLY A 152     3763   6230   4834    598   -228    390       N  
ATOM   1140  CA  GLY A 152      -1.266  29.759   3.571  1.00 41.60           C  
ANISOU 1140  CA  GLY A 152     4142   6640   5023    523   -374    393       C  
ATOM   1141  C   GLY A 152      -0.297  30.700   2.894  1.00 41.96           C  
ANISOU 1141  C   GLY A 152     4285   6611   5047    610   -331    405       C  
ATOM   1142  O   GLY A 152      -0.052  30.543   1.694  1.00 45.62           O  
ANISOU 1142  O   GLY A 152     4776   7157   5399    564   -442    438       O  
ATOM   1143  N   GLU A 153       0.263  31.670   3.608  1.00 34.95           N  
ANISOU 1143  N   GLU A 153     3462   5568   4249    718   -172    378       N  
ATOM   1144  CA  GLU A 153       1.306  32.500   3.023  1.00 36.23           C  
ANISOU 1144  CA  GLU A 153     3734   5651   4382    778   -133    378       C  
ATOM   1145  C   GLU A 153       2.607  31.710   2.994  1.00 33.01           C  
ANISOU 1145  C   GLU A 153     3489   5190   3861    677   -168    218       C  
ATOM   1146  O   GLU A 153       2.976  31.078   3.989  1.00 32.29           O  
ANISOU 1146  O   GLU A 153     3461   5032   3776    614   -131     98       O  
ATOM   1147  CB  GLU A 153       1.482  33.802   3.807  1.00 46.58           C  
ANISOU 1147  CB  GLU A 153     5081   6802   5813    903     52    402       C  
ATOM   1148  CG  GLU A 153       0.299  34.781   3.710  1.00 69.62           C  
ANISOU 1148  CG  GLU A 153     7846   9744   8861   1047    130    590       C  
ATOM   1149  CD  GLU A 153      -0.188  35.013   2.278  1.00 79.79           C  
ANISOU 1149  CD  GLU A 153     9011  11189  10118   1083      6    767       C  
ATOM   1150  OE1 GLU A 153      -1.379  34.741   2.004  1.00 81.28           O  
ANISOU 1150  OE1 GLU A 153     9015  11528  10341   1088    -66    907       O  
ATOM   1151  OE2 GLU A 153       0.614  35.465   1.429  1.00 80.90           O  
ANISOU 1151  OE2 GLU A 153     9233  11312  10193   1095    -24    778       O  
ATOM   1152  N   ARG A 154       3.283  31.740   1.843  1.00 29.38           N  
ANISOU 1152  N   ARG A 154     3092   4768   3304    667   -235    233       N  
ATOM   1153  CA  ARG A 154       4.555  31.065   1.607  1.00 32.19           C  
ANISOU 1153  CA  ARG A 154     3593   5080   3558    598   -251    116       C  
ATOM   1154  C   ARG A 154       5.675  32.089   1.582  1.00 32.85           C  
ANISOU 1154  C   ARG A 154     3760   5059   3662    668   -160    126       C  
ATOM   1155  O   ARG A 154       5.536  33.154   0.972  1.00 34.67           O  
ANISOU 1155  O   ARG A 154     3959   5294   3919    752   -141    234       O  
ATOM   1156  CB  ARG A 154       4.579  30.340   0.254  1.00 39.81           C  
ANISOU 1156  CB  ARG A 154     4591   6156   4377    529   -373    125       C  
ATOM   1157  CG  ARG A 154       3.964  28.986   0.216  1.00 46.31           C  
ANISOU 1157  CG  ARG A 154     5413   7055   5126    403   -467     63       C  
ATOM   1158  CD  ARG A 154       3.966  28.394  -1.179  1.00 45.19           C  
ANISOU 1158  CD  ARG A 154     5339   7012   4819    317   -575     72       C  
ATOM   1159  NE  ARG A 154       5.300  28.230  -1.744  1.00 37.13           N  
ANISOU 1159  NE  ARG A 154     4476   5920   3712    327   -526      1       N  
ATOM   1160  CZ  ARG A 154       5.952  27.073  -1.829  1.00 42.42           C  
ANISOU 1160  CZ  ARG A 154     5286   6541   4293    252   -510   -118       C  
ATOM   1161  NH1 ARG A 154       5.409  25.944  -1.372  1.00 41.22           N  
ANISOU 1161  NH1 ARG A 154     5150   6394   4118    149   -549   -194       N  
ATOM   1162  NH2 ARG A 154       7.153  27.043  -2.382  1.00 51.81           N  
ANISOU 1162  NH2 ARG A 154     6597   7669   5418    286   -445   -153       N  
ATOM   1163  N   GLN A 155       6.804  31.741   2.179  1.00 28.92           N  
ANISOU 1163  N   GLN A 155     3364   4476   3147    624   -112     28       N  
ATOM   1164  CA  GLN A 155       7.969  32.607   2.130  1.00 30.72           C  
ANISOU 1164  CA  GLN A 155     3672   4621   3379    659    -42     45       C  
ATOM   1165  C   GLN A 155       9.207  31.738   2.028  1.00 30.46           C  
ANISOU 1165  C   GLN A 155     3724   4578   3272    598    -51    -24       C  
ATOM   1166  O   GLN A 155       9.355  30.779   2.788  1.00 35.16           O  
ANISOU 1166  O   GLN A 155     4334   5157   3868    533    -52   -102       O  
ATOM   1167  CB  GLN A 155       8.064  33.508   3.369  1.00 33.79           C  
ANISOU 1167  CB  GLN A 155     4085   4890   3864    672     70     36       C  
ATOM   1168  CG  GLN A 155       9.124  34.592   3.230  1.00 52.42           C  
ANISOU 1168  CG  GLN A 155     6527   7166   6223    693    136     76       C  
ATOM   1169  CD  GLN A 155       9.270  35.439   4.477  1.00 66.73           C  
ANISOU 1169  CD  GLN A 155     8406   8847   8102    668    250     52       C  
ATOM   1170  OE1 GLN A 155       9.219  34.933   5.599  1.00 68.76           O  
ANISOU 1170  OE1 GLN A 155     8680   9071   8373    593    274    -24       O  
ATOM   1171  NE2 GLN A 155       9.457  36.740   4.285  1.00 74.51           N  
ANISOU 1171  NE2 GLN A 155     9443   9748   9118    719    325    118       N  
ATOM   1172  N   ILE A 156      10.081  32.064   1.093  1.00 26.91           N  
ANISOU 1172  N   ILE A 156     3324   4137   2763    626    -49     18       N  
ATOM   1173  CA  ILE A 156      11.371  31.392   1.021  1.00 28.48           C  
ANISOU 1173  CA  ILE A 156     3594   4318   2912    593    -26    -17       C  
ATOM   1174  C   ILE A 156      12.277  31.989   2.086  1.00 29.20           C  
ANISOU 1174  C   ILE A 156     3704   4325   3065    566     44     -8       C  
ATOM   1175  O   ILE A 156      12.364  33.214   2.229  1.00 33.76           O  
ANISOU 1175  O   ILE A 156     4290   4856   3682    589     84     45       O  
ATOM   1176  CB  ILE A 156      11.986  31.534  -0.377  1.00 31.67           C  
ANISOU 1176  CB  ILE A 156     4042   4765   3225    634    -35     34       C  
ATOM   1177  CG1 ILE A 156      11.048  30.948  -1.428  1.00 39.20           C  
ANISOU 1177  CG1 ILE A 156     4995   5809   4089    624   -116     25       C  
ATOM   1178  CG2 ILE A 156      13.338  30.841  -0.427  1.00 33.15           C  
ANISOU 1178  CG2 ILE A 156     4290   4930   3376    620     17     18       C  
ATOM   1179  CD1 ILE A 156      10.964  29.455  -1.376  1.00 45.55           C  
ANISOU 1179  CD1 ILE A 156     5851   6624   4833    557   -136    -70       C  
ATOM   1180  N   VAL A 157      12.931  31.128   2.861  1.00 25.46           N  
ANISOU 1180  N   VAL A 157     3244   3833   2597    505     60    -50       N  
ATOM   1181  CA  VAL A 157      13.880  31.549   3.883  1.00 28.17           C  
ANISOU 1181  CA  VAL A 157     3603   4122   2979    443    107    -26       C  
ATOM   1182  C   VAL A 157      15.229  30.946   3.529  1.00 30.55           C  
ANISOU 1182  C   VAL A 157     3915   4448   3246    439    125     22       C  
ATOM   1183  O   VAL A 157      15.331  29.732   3.318  1.00 29.79           O  
ANISOU 1183  O   VAL A 157     3818   4375   3127    449    121    -10       O  
ATOM   1184  CB  VAL A 157      13.443  31.104   5.291  1.00 28.39           C  
ANISOU 1184  CB  VAL A 157     3617   4118   3052    363    111    -88       C  
ATOM   1185  CG1 VAL A 157      14.443  31.595   6.340  1.00 32.67           C  
ANISOU 1185  CG1 VAL A 157     4187   4616   3609    266    146    -51       C  
ATOM   1186  CG2 VAL A 157      12.033  31.607   5.592  1.00 31.40           C  
ANISOU 1186  CG2 VAL A 157     3977   4478   3474    388    115   -125       C  
ATOM   1187  N   ARG A 158      16.260  31.783   3.452  1.00 28.13           N  
ANISOU 1187  N   ARG A 158     3619   4132   2939    424    154    107       N  
ATOM   1188  CA  ARG A 158      17.586  31.325   3.061  1.00 25.02           C  
ANISOU 1188  CA  ARG A 158     3212   3772   2524    434    184    187       C  
ATOM   1189  C   ARG A 158      18.532  31.378   4.251  1.00 28.69           C  
ANISOU 1189  C   ARG A 158     3645   4233   3025    326    194    253       C  
ATOM   1190  O   ARG A 158      18.378  32.200   5.159  1.00 30.05           O  
ANISOU 1190  O   ARG A 158     3837   4366   3213    232    182    247       O  
ATOM   1191  CB  ARG A 158      18.152  32.170   1.912  1.00 28.93           C  
ANISOU 1191  CB  ARG A 158     3725   4287   2980    494    205    266       C  
ATOM   1192  CG  ARG A 158      17.342  32.068   0.618  1.00 36.52           C  
ANISOU 1192  CG  ARG A 158     4719   5274   3884    585    187    225       C  
ATOM   1193  CD  ARG A 158      17.881  33.000  -0.463  1.00 46.05           C  
ANISOU 1193  CD  ARG A 158     5946   6503   5050    636    206    311       C  
ATOM   1194  NE  ARG A 158      19.160  32.549  -1.012  1.00 57.43           N  
ANISOU 1194  NE  ARG A 158     7385   7977   6460    665    264    386       N  
ATOM   1195  CZ  ARG A 158      19.824  33.191  -1.971  1.00 62.70           C  
ANISOU 1195  CZ  ARG A 158     8065   8671   7086    708    294    472       C  
ATOM   1196  NH1 ARG A 158      19.326  34.310  -2.485  1.00 69.04           N  
ANISOU 1196  NH1 ARG A 158     8889   9470   7875    723    262    492       N  
ATOM   1197  NH2 ARG A 158      20.982  32.721  -2.416  1.00 58.15           N  
ANISOU 1197  NH2 ARG A 158     7477   8127   6490    744    366    550       N  
ATOM   1198  N   GLY A 159      19.501  30.471   4.253  1.00 27.51           N  
ANISOU 1198  N   GLY A 159     3449   4122   2883    335    221    324       N  
ATOM   1199  CA  GLY A 159      20.474  30.448   5.328  1.00 27.35           C  
ANISOU 1199  CA  GLY A 159     3372   4125   2893    223    216    425       C  
ATOM   1200  C   GLY A 159      21.707  29.688   4.896  1.00 27.00           C  
ANISOU 1200  C   GLY A 159     3258   4137   2866    280    269    558       C  
ATOM   1201  O   GLY A 159      21.777  29.140   3.794  1.00 30.68           O  
ANISOU 1201  O   GLY A 159     3742   4602   3312    409    326    550       O  
ATOM   1202  N   ASP A 160      22.687  29.658   5.789  1.00 24.39           N  
ANISOU 1202  N   ASP A 160     2848   3855   2566    178    257    693       N  
ATOM   1203  CA  ASP A 160      23.905  28.916   5.497  1.00 27.59           C  
ANISOU 1203  CA  ASP A 160     3155   4320   3008    240    320    859       C  
ATOM   1204  C   ASP A 160      23.727  27.414   5.714  1.00 27.20           C  
ANISOU 1204  C   ASP A 160     3084   4249   3003    316    368    834       C  
ATOM   1205  O   ASP A 160      24.381  26.616   5.024  1.00 28.59           O  
ANISOU 1205  O   ASP A 160     3228   4429   3206    444    467    915       O  
ATOM   1206  CB  ASP A 160      25.047  29.484   6.337  1.00 30.89           C  
ANISOU 1206  CB  ASP A 160     3474   4822   3442     89    277   1049       C  
ATOM   1207  CG  ASP A 160      25.414  30.903   5.913  1.00 42.19           C  
ANISOU 1207  CG  ASP A 160     4938   6267   4827     25    252   1095       C  
ATOM   1208  OD1 ASP A 160      25.654  31.111   4.707  1.00 47.08           O  
ANISOU 1208  OD1 ASP A 160     5569   6888   5434    150    310   1116       O  
ATOM   1209  OD2 ASP A 160      25.435  31.815   6.760  1.00 45.19           O  
ANISOU 1209  OD2 ASP A 160     5349   6647   5175   -156    181   1105       O  
ATOM   1210  N   PHE A 161      22.860  27.013   6.648  1.00 28.82           N  
ANISOU 1210  N   PHE A 161     3314   4420   3216    243    314    725       N  
ATOM   1211  CA  PHE A 161      22.519  25.608   6.848  1.00 28.01           C  
ANISOU 1211  CA  PHE A 161     3212   4279   3150    305    355    679       C  
ATOM   1212  C   PHE A 161      21.235  25.514   7.659  1.00 27.62           C  
ANISOU 1212  C   PHE A 161     3218   4188   3087    221    282    516       C  
ATOM   1213  O   PHE A 161      20.792  26.489   8.281  1.00 22.36           O  
ANISOU 1213  O   PHE A 161     2574   3527   2395    107    213    470       O  
ATOM   1214  CB  PHE A 161      23.654  24.820   7.528  1.00 23.19           C  
ANISOU 1214  CB  PHE A 161     2476   3721   2615    295    393    877       C  
ATOM   1215  CG  PHE A 161      24.020  25.309   8.900  1.00 28.29           C  
ANISOU 1215  CG  PHE A 161     3040   4440   3270    104    296    978       C  
ATOM   1216  CD1 PHE A 161      24.884  26.382   9.053  1.00 34.87           C  
ANISOU 1216  CD1 PHE A 161     3816   5353   4081     -2    252   1117       C  
ATOM   1217  CD2 PHE A 161      23.536  24.662  10.038  1.00 33.17           C  
ANISOU 1217  CD2 PHE A 161     3646   5050   3908     15    249    941       C  
ATOM   1218  CE1 PHE A 161      25.236  26.832  10.312  1.00 32.47           C  
ANISOU 1218  CE1 PHE A 161     3461   5118   3760   -212    158   1209       C  
ATOM   1219  CE2 PHE A 161      23.894  25.104  11.308  1.00 34.44           C  
ANISOU 1219  CE2 PHE A 161     3747   5283   4054   -183    160   1036       C  
ATOM   1220  CZ  PHE A 161      24.756  26.194  11.430  1.00 29.18           C  
ANISOU 1220  CZ  PHE A 161     3039   4696   3353   -304    113   1169       C  
ATOM   1221  N  AILE A 162      20.647  24.318   7.658  0.39 22.47           N  
ANISOU 1221  N  AILE A 162     2598   3488   2452    276    311    435       N  
ATOM   1222  N  BILE A 162      20.633  24.324   7.640  0.61 22.88           N  
ANISOU 1222  N  BILE A 162     2651   3538   2503    277    311    432       N  
ATOM   1223  CA AILE A 162      19.360  24.065   8.303  0.39 22.08           C  
ANISOU 1223  CA AILE A 162     2595   3402   2392    212    252    283       C  
ATOM   1224  CA BILE A 162      19.364  24.073   8.315  0.61 21.72           C  
ANISOU 1224  CA BILE A 162     2549   3357   2347    211    251    284       C  
ATOM   1225  C  AILE A 162      19.568  23.022   9.387  0.39 23.84           C  
ANISOU 1225  C  AILE A 162     2762   3627   2670    159    253    336       C  
ATOM   1226  C  BILE A 162      19.589  23.034   9.394  0.61 24.49           C  
ANISOU 1226  C  BILE A 162     2843   3709   2752    158    253    339       C  
ATOM   1227  O  AILE A 162      20.063  21.922   9.109  0.39 25.11           O  
ANISOU 1227  O  AILE A 162     2910   3760   2869    246    328    397       O  
ATOM   1228  O  BILE A 162      20.104  21.946   9.114  0.61 26.23           O  
ANISOU 1228  O  BILE A 162     3049   3905   3013    245    329    403       O  
ATOM   1229  CB AILE A 162      18.302  23.570   7.308  0.39 20.49           C  
ANISOU 1229  CB AILE A 162     2490   3148   2148    297    266    132       C  
ATOM   1230  CB BILE A 162      18.278  23.566   7.356  0.61 20.37           C  
ANISOU 1230  CB BILE A 162     2474   3133   2134    293    264    130       C  
ATOM   1231  CG1AILE A 162      18.476  24.242   5.945  0.39 21.20           C  
ANISOU 1231  CG1AILE A 162     2627   3243   2183    383    295    131       C  
ATOM   1232  CG1BILE A 162      18.024  24.563   6.229  0.61 24.22           C  
ANISOU 1232  CG1BILE A 162     3010   3630   2564    345    256     92       C  
ATOM   1233  CG2AILE A 162      16.915  23.808   7.883  0.39 23.49           C  
ANISOU 1233  CG2AILE A 162     2895   3518   2514    222    191     -3       C  
ATOM   1234  CG2BILE A 162      17.014  23.280   8.157  0.61 20.66           C  
ANISOU 1234  CG2BILE A 162     2527   3151   2173    215    201      7       C  
ATOM   1235  CD1AILE A 162      18.105  25.690   5.943  0.39 21.91           C  
ANISOU 1235  CD1AILE A 162     2715   3360   2250    338    235    113       C  
ATOM   1236  CD1BILE A 162      17.594  23.899   4.940  0.61 21.04           C  
ANISOU 1236  CD1BILE A 162     2698   3195   2101    437    296     14       C  
ATOM   1237  N   ILE A 163      19.185  23.357  10.613  1.00 21.88           N  
ANISOU 1237  N   ILE A 163     2491   3400   2422     20    182    317       N  
ATOM   1238  CA  ILE A 163      19.158  22.392  11.700  1.00 22.02           C  
ANISOU 1238  CA  ILE A 163     2465   3422   2480    -46    168    350       C  
ATOM   1239  C   ILE A 163      17.743  21.823  11.757  1.00 26.04           C  
ANISOU 1239  C   ILE A 163     3046   3873   2977    -40    152    171       C  
ATOM   1240  O   ILE A 163      16.771  22.555  11.987  1.00 24.24           O  
ANISOU 1240  O   ILE A 163     2857   3639   2713    -95    107     57       O  
ATOM   1241  CB  ILE A 163      19.556  23.040  13.032  1.00 22.22           C  
ANISOU 1241  CB  ILE A 163     2438   3513   2493   -226    100    435       C  
ATOM   1242  CG1 ILE A 163      20.949  23.657  12.945  1.00 25.61           C  
ANISOU 1242  CG1 ILE A 163     2789   4018   2924   -261     98    630       C  
ATOM   1243  CG2 ILE A 163      19.413  22.011  14.168  1.00 24.56           C  
ANISOU 1243  CG2 ILE A 163     2690   3819   2823   -302     78    466       C  
ATOM   1244  CD1 ILE A 163      21.389  24.346  14.243  1.00 29.84           C  
ANISOU 1244  CD1 ILE A 163     3292   4627   3419   -482     18    721       C  
ATOM   1245  N   CYS A 164      17.616  20.519  11.507  1.00 22.36           N  
ANISOU 1245  N   CYS A 164     2597   3357   2541     31    199    154       N  
ATOM   1246  CA  CYS A 164      16.314  19.856  11.453  1.00 21.28           C  
ANISOU 1246  CA  CYS A 164     2529   3170   2386     26    180     -3       C  
ATOM   1247  C   CYS A 164      16.090  19.212  12.810  1.00 24.70           C  
ANISOU 1247  C   CYS A 164     2918   3611   2857    -76    148     16       C  
ATOM   1248  O   CYS A 164      16.570  18.112  13.084  1.00 23.17           O  
ANISOU 1248  O   CYS A 164     2703   3388   2712    -52    192     92       O  
ATOM   1249  CB  CYS A 164      16.269  18.834  10.325  1.00 26.64           C  
ANISOU 1249  CB  CYS A 164     3291   3776   3055    140    255    -46       C  
ATOM   1250  SG  CYS A 164      16.660  19.564   8.729  1.00 30.13           S  
ANISOU 1250  SG  CYS A 164     3793   4218   3439    250    300    -51       S  
ATOM   1251  N   SER A 165      15.401  19.941  13.687  1.00 21.70           N  
ANISOU 1251  N   SER A 165     2526   3265   2453   -189     84    -42       N  
ATOM   1252  CA  SER A 165      15.117  19.443  15.027  1.00 24.35           C  
ANISOU 1252  CA  SER A 165     2828   3616   2806   -304     51    -32       C  
ATOM   1253  C   SER A 165      13.612  19.247  15.173  1.00 22.89           C  
ANISOU 1253  C   SER A 165     2686   3406   2604   -331     25   -189       C  
ATOM   1254  O   SER A 165      13.002  19.675  16.163  1.00 22.68           O  
ANISOU 1254  O   SER A 165     2652   3403   2562   -434     -4   -230       O  
ATOM   1255  CB  SER A 165      15.663  20.406  16.086  1.00 25.92           C  
ANISOU 1255  CB  SER A 165     2990   3878   2980   -440     13     48       C  
ATOM   1256  OG  SER A 165      15.367  21.752  15.750  1.00 28.04           O  
ANISOU 1256  OG  SER A 165     3304   4148   3203   -448      8    -16       O  
ATOM   1257  N   ASP A 166      13.002  18.582  14.195  1.00 20.57           N  
ANISOU 1257  N   ASP A 166     2442   3068   2306   -249     40   -269       N  
ATOM   1258  CA  ASP A 166      11.554  18.536  14.113  1.00 23.41           C  
ANISOU 1258  CA  ASP A 166     2825   3427   2643   -274      4   -397       C  
ATOM   1259  C   ASP A 166      10.964  17.224  14.639  1.00 25.62           C  
ANISOU 1259  C   ASP A 166     3115   3677   2944   -326     -6   -433       C  
ATOM   1260  O   ASP A 166       9.814  16.890  14.319  1.00 25.53           O  
ANISOU 1260  O   ASP A 166     3125   3663   2911   -344    -36   -527       O  
ATOM   1261  CB  ASP A 166      11.088  18.846  12.682  1.00 25.47           C  
ANISOU 1261  CB  ASP A 166     3134   3681   2861   -190      0   -460       C  
ATOM   1262  CG  ASP A 166      11.816  18.049  11.595  1.00 28.29           C  
ANISOU 1262  CG  ASP A 166     3560   3986   3203   -106     50   -438       C  
ATOM   1263  OD1 ASP A 166      12.941  17.535  11.810  1.00 29.03           O  
ANISOU 1263  OD1 ASP A 166     3647   4049   3335    -74    107   -343       O  
ATOM   1264  OD2 ASP A 166      11.234  17.971  10.488  1.00 30.48           O  
ANISOU 1264  OD2 ASP A 166     3900   4256   3425    -73     38   -508       O  
ATOM   1265  N   GLY A 167      11.718  16.491  15.461  1.00 21.72           N  
ANISOU 1265  N   GLY A 167     2594   3168   2491   -361     15   -345       N  
ATOM   1266  CA  GLY A 167      11.113  15.451  16.284  1.00 21.80           C  
ANISOU 1266  CA  GLY A 167     2600   3159   2523   -436      0   -369       C  
ATOM   1267  C   GLY A 167      10.945  14.115  15.588  1.00 21.36           C  
ANISOU 1267  C   GLY A 167     2622   3018   2477   -392     35   -402       C  
ATOM   1268  O   GLY A 167      11.341  13.906  14.443  1.00 20.91           O  
ANISOU 1268  O   GLY A 167     2635   2909   2402   -300     82   -410       O  
ATOM   1269  N   VAL A 168      10.290  13.196  16.307  1.00 23.87           N  
ANISOU 1269  N   VAL A 168     2943   3315   2813   -470     17   -430       N  
ATOM   1270  CA  VAL A 168      10.264  11.810  15.849  1.00 23.82           C  
ANISOU 1270  CA  VAL A 168     3029   3204   2818   -447     65   -447       C  
ATOM   1271  C   VAL A 168       9.502  11.671  14.532  1.00 26.57           C  
ANISOU 1271  C   VAL A 168     3485   3516   3095   -430     56   -569       C  
ATOM   1272  O   VAL A 168       9.771  10.747  13.755  1.00 27.14           O  
ANISOU 1272  O   VAL A 168     3680   3482   3151   -388    124   -588       O  
ATOM   1273  CB  VAL A 168       9.685  10.903  16.957  1.00 26.11           C  
ANISOU 1273  CB  VAL A 168     3298   3482   3139   -551     41   -446       C  
ATOM   1274  CG1 VAL A 168       8.229  11.261  17.241  1.00 30.11           C  
ANISOU 1274  CG1 VAL A 168     3777   4059   3605   -651    -41   -556       C  
ATOM   1275  CG2 VAL A 168       9.827   9.430  16.573  1.00 28.79           C  
ANISOU 1275  CG2 VAL A 168     3750   3687   3501   -526    111   -446       C  
ATOM   1276  N   HIS A 169       8.558  12.573  14.240  1.00 22.79           N  
ANISOU 1276  N   HIS A 169     2970   3122   2567   -465    -19   -643       N  
ATOM   1277  CA  HIS A 169       7.819  12.529  12.984  1.00 26.37           C  
ANISOU 1277  CA  HIS A 169     3507   3573   2941   -471    -49   -733       C  
ATOM   1278  C   HIS A 169       8.391  13.467  11.924  1.00 29.66           C  
ANISOU 1278  C   HIS A 169     3942   4009   3319   -373    -30   -721       C  
ATOM   1279  O   HIS A 169       7.669  13.864  10.999  1.00 28.05           O  
ANISOU 1279  O   HIS A 169     3764   3849   3044   -387    -82   -778       O  
ATOM   1280  CB  HIS A 169       6.350  12.855  13.236  1.00 31.19           C  
ANISOU 1280  CB  HIS A 169     4047   4276   3527   -567   -146   -792       C  
ATOM   1281  CG  HIS A 169       5.686  11.884  14.156  1.00 32.54           C  
ANISOU 1281  CG  HIS A 169     4207   4432   3724   -674   -168   -808       C  
ATOM   1282  ND1 HIS A 169       5.620  10.535  13.884  1.00 41.34           N  
ANISOU 1282  ND1 HIS A 169     5443   5448   4815   -727   -147   -843       N  
ATOM   1283  CD2 HIS A 169       5.083  12.058  15.354  1.00 37.74           C  
ANISOU 1283  CD2 HIS A 169     4761   5153   4427   -739   -198   -794       C  
ATOM   1284  CE1 HIS A 169       4.989   9.920  14.869  1.00 40.92           C  
ANISOU 1284  CE1 HIS A 169     5348   5404   4794   -824   -175   -844       C  
ATOM   1285  NE2 HIS A 169       4.650  10.822  15.770  1.00 38.08           N  
ANISOU 1285  NE2 HIS A 169     4847   5147   4475   -832   -207   -814       N  
ATOM   1286  N   SER A 170       9.672  13.810  12.038  1.00 25.50           N  
ANISOU 1286  N   SER A 170     3394   3461   2836   -283     39   -632       N  
ATOM   1287  CA  SER A 170      10.360  14.736  11.148  1.00 24.96           C  
ANISOU 1287  CA  SER A 170     3331   3413   2740   -190     65   -601       C  
ATOM   1288  C   SER A 170      10.002  14.527   9.682  1.00 25.95           C  
ANISOU 1288  C   SER A 170     3579   3509   2771   -169     70   -677       C  
ATOM   1289  O   SER A 170      10.236  13.450   9.115  1.00 27.89           O  
ANISOU 1289  O   SER A 170     3959   3654   2983   -160    138   -707       O  
ATOM   1290  CB  SER A 170      11.871  14.560  11.348  1.00 26.21           C  
ANISOU 1290  CB  SER A 170     3475   3525   2958   -103    160   -479       C  
ATOM   1291  OG  SER A 170      12.617  15.200  10.321  1.00 24.43           O  
ANISOU 1291  OG  SER A 170     3278   3303   2703     -7    206   -446       O  
ATOM   1292  N   LYS A 171       9.442  15.571   9.053  1.00 24.96           N  
ANISOU 1292  N   LYS A 171     3421   3467   2597   -167      4   -703       N  
ATOM   1293  CA  LYS A 171       9.326  15.570   7.599  1.00 29.57           C  
ANISOU 1293  CA  LYS A 171     4115   4042   3077   -147      6   -748       C  
ATOM   1294  C   LYS A 171      10.611  16.014   6.918  1.00 29.47           C  
ANISOU 1294  C   LYS A 171     4139   3997   3062    -27     97   -686       C  
ATOM   1295  O   LYS A 171      10.798  15.718   5.733  1.00 27.90           O  
ANISOU 1295  O   LYS A 171     4071   3758   2774     -2    141   -721       O  
ATOM   1296  CB  LYS A 171       8.176  16.475   7.147  1.00 32.87           C  
ANISOU 1296  CB  LYS A 171     4468   4574   3446   -193   -105   -773       C  
ATOM   1297  CG  LYS A 171       6.839  16.079   7.717  1.00 38.93           C  
ANISOU 1297  CG  LYS A 171     5182   5393   4217   -309   -194   -813       C  
ATOM   1298  CD  LYS A 171       6.422  14.704   7.242  1.00 51.98           C  
ANISOU 1298  CD  LYS A 171     6979   6984   5789   -411   -202   -886       C  
ATOM   1299  CE  LYS A 171       5.036  14.364   7.757  1.00 64.32           C  
ANISOU 1299  CE  LYS A 171     8470   8620   7350   -543   -304   -910       C  
ATOM   1300  NZ  LYS A 171       4.097  15.496   7.520  1.00 70.00           N  
ANISOU 1300  NZ  LYS A 171     9047   9482   8067   -546   -397   -865       N  
ATOM   1301  N   MET A 172      11.493  16.724   7.631  1.00 27.68           N  
ANISOU 1301  N   MET A 172     3804   3793   2918     33    126   -591       N  
ATOM   1302  CA  MET A 172      12.798  17.042   7.065  1.00 25.30           C  
ANISOU 1302  CA  MET A 172     3520   3467   2626    142    218   -508       C  
ATOM   1303  C   MET A 172      13.596  15.777   6.776  1.00 28.15           C  
ANISOU 1303  C   MET A 172     3988   3712   2995    201    348   -485       C  
ATOM   1304  O   MET A 172      14.415  15.756   5.853  1.00 33.59           O  
ANISOU 1304  O   MET A 172     4749   4359   3653    295    447   -450       O  
ATOM   1305  CB  MET A 172      13.600  17.955   8.002  1.00 27.53           C  
ANISOU 1305  CB  MET A 172     3666   3803   2991    160    214   -395       C  
ATOM   1306  CG  MET A 172      12.993  19.348   8.247  1.00 27.95           C  
ANISOU 1306  CG  MET A 172     3640   3941   3038    121    126   -409       C  
ATOM   1307  SD  MET A 172      12.818  20.381   6.746  1.00 37.94           S  
ANISOU 1307  SD  MET A 172     4948   5245   4222    185    109   -428       S  
ATOM   1308  CE  MET A 172      11.038  20.396   6.546  1.00 42.13           C  
ANISOU 1308  CE  MET A 172     5480   5824   4706    111      6   -532       C  
ATOM   1309  N   ARG A 173      13.357  14.710   7.538  1.00 26.33           N  
ANISOU 1309  N   ARG A 173     3776   3420   2808    154    364   -500       N  
ATOM   1310  CA  ARG A 173      14.178  13.507   7.425  1.00 23.43           C  
ANISOU 1310  CA  ARG A 173     3502   2924   2476    228    512   -453       C  
ATOM   1311  C   ARG A 173      14.190  12.931   6.011  1.00 34.39           C  
ANISOU 1311  C   ARG A 173     5098   4211   3756    268    612   -536       C  
ATOM   1312  O   ARG A 173      15.184  12.320   5.604  1.00 40.13           O  
ANISOU 1312  O   ARG A 173     5907   4832   4510    382    779   -472       O  
ATOM   1313  CB  ARG A 173      13.688  12.480   8.454  1.00 30.64           C  
ANISOU 1313  CB  ARG A 173     4413   3786   3443    151    498   -470       C  
ATOM   1314  CG  ARG A 173      14.561  11.246   8.613  1.00 34.24           C  
ANISOU 1314  CG  ARG A 173     4936   4103   3970    236    659   -388       C  
ATOM   1315  CD  ARG A 173      14.282  10.600   9.959  1.00 40.80           C  
ANISOU 1315  CD  ARG A 173     5687   4929   4885    163    618   -348       C  
ATOM   1316  NE  ARG A 173      12.878  10.249  10.087  1.00 49.04           N  
ANISOU 1316  NE  ARG A 173     6797   5976   5862     21    513   -498       N  
ATOM   1317  CZ  ARG A 173      12.187  10.301  11.219  1.00 45.14           C  
ANISOU 1317  CZ  ARG A 173     6195   5552   5403    -85    405   -503       C  
ATOM   1318  NH1 ARG A 173      12.763  10.712  12.340  1.00 42.63           N  
ANISOU 1318  NH1 ARG A 173     5716   5308   5174    -80    381   -377       N  
ATOM   1319  NH2 ARG A 173      10.907   9.953  11.225  1.00 40.45           N  
ANISOU 1319  NH2 ARG A 173     5657   4965   4748   -211    320   -627       N  
ATOM   1320  N   LYS A 174      13.130  13.142   5.229  1.00 45.83           N  
ANISOU 1320  N   LYS A 174     6637   5694   5080    174    520   -664       N  
ATOM   1321  CA  LYS A 174      13.154  12.612   3.865  1.00 53.84           C  
ANISOU 1321  CA  LYS A 174     7875   6617   5964    182    610   -747       C  
ATOM   1322  C   LYS A 174      14.100  13.373   2.938  1.00 51.04           C  
ANISOU 1322  C   LYS A 174     7530   6283   5581    304    692   -685       C  
ATOM   1323  O   LYS A 174      14.376  12.891   1.835  1.00 55.36           O  
ANISOU 1323  O   LYS A 174     8274   6736   6023    333    810   -736       O  
ATOM   1324  CB  LYS A 174      11.752  12.603   3.268  1.00 46.02           C  
ANISOU 1324  CB  LYS A 174     6971   5681   4832     19    471   -879       C  
ATOM   1325  CG  LYS A 174      11.157  13.971   3.056  1.00 53.00           C  
ANISOU 1325  CG  LYS A 174     7713   6736   5690    -10    317   -864       C  
ATOM   1326  CD  LYS A 174       9.676  13.841   2.705  1.00 63.12           C  
ANISOU 1326  CD  LYS A 174     9033   8090   6860   -182    167   -955       C  
ATOM   1327  CE  LYS A 174       9.280  14.746   1.552  1.00 67.46           C  
ANISOU 1327  CE  LYS A 174     9592   8747   7291   -207     85   -958       C  
ATOM   1328  NZ  LYS A 174       7.806  14.711   1.298  1.00 72.40           N  
ANISOU 1328  NZ  LYS A 174    10204   9480   7824   -380    -82  -1002       N  
ATOM   1329  N   ALA A 175      14.602  14.537   3.348  1.00 39.15           N  
ANISOU 1329  N   ALA A 175     5833   4890   4154    363    640   -579       N  
ATOM   1330  CA  ALA A 175      15.624  15.219   2.562  1.00 42.69           C  
ANISOU 1330  CA  ALA A 175     6276   5355   4590    482    727   -497       C  
ATOM   1331  C   ALA A 175      16.982  14.538   2.691  1.00 48.61           C  
ANISOU 1331  C   ALA A 175     7035   6003   5431    624    925   -374       C  
ATOM   1332  O   ALA A 175      17.825  14.660   1.794  1.00 50.81           O  
ANISOU 1332  O   ALA A 175     7378   6248   5679    732   1056   -323       O  
ATOM   1333  CB  ALA A 175      15.731  16.686   2.991  1.00 41.14           C  
ANISOU 1333  CB  ALA A 175     5884   5302   4447    483    611   -418       C  
ATOM   1334  N   ILE A 176      17.222  13.837   3.795  1.00 44.00           N  
ANISOU 1334  N   ILE A 176     6377   5376   4965    631    955   -306       N  
ATOM   1335  CA  ILE A 176      18.517  13.211   4.028  1.00 46.41           C  
ANISOU 1335  CA  ILE A 176     6649   5601   5383    775   1139   -145       C  
ATOM   1336  C   ILE A 176      18.416  11.752   3.623  1.00 52.07           C  
ANISOU 1336  C   ILE A 176     7588   6125   6070    808   1306   -219       C  
ATOM   1337  O   ILE A 176      19.131  11.287   2.725  1.00 51.60           O  
ANISOU 1337  O   ILE A 176     7670   5951   5985    931   1509   -195       O  
ATOM   1338  CB  ILE A 176      18.963  13.348   5.497  1.00 47.90           C  
ANISOU 1338  CB  ILE A 176     6612   5867   5720    762   1076     11       C  
ATOM   1339  CG1 ILE A 176      19.457  14.771   5.784  1.00 50.97           C  
ANISOU 1339  CG1 ILE A 176     6813   6418   6137    748    970    118       C  
ATOM   1340  CG2 ILE A 176      20.041  12.332   5.814  1.00 40.07           C  
ANISOU 1340  CG2 ILE A 176     5600   4775   4850    894   1266    178       C  
ATOM   1341  CD1 ILE A 176      18.360  15.754   6.136  1.00 50.08           C  
ANISOU 1341  CD1 ILE A 176     6655   6410   5965    606    769      1       C  
ATOM   1342  N   MET A 177      17.520  11.028   4.286  1.00 59.36           N  
ANISOU 1342  N   MET A 177     8555   7005   6996    696   1235   -309       N  
ATOM   1343  CA  MET A 177      17.280   9.635   3.961  1.00 72.63           C  
ANISOU 1343  CA  MET A 177    10469   8489   8636    694   1379   -397       C  
ATOM   1344  C   MET A 177      16.165   9.553   2.931  1.00 68.46           C  
ANISOU 1344  C   MET A 177    10166   7936   7911    553   1312   -610       C  
ATOM   1345  O   MET A 177      15.046  10.004   3.209  1.00 60.91           O  
ANISOU 1345  O   MET A 177     9149   7096   6900    398   1102   -700       O  
ATOM   1346  CB  MET A 177      16.913   8.841   5.207  1.00 83.74           C  
ANISOU 1346  CB  MET A 177    11813   9860  10144    634   1338   -372       C  
ATOM   1347  CG  MET A 177      17.962   8.880   6.326  1.00 88.72           C  
ANISOU 1347  CG  MET A 177    12210  10538  10962    741   1380   -140       C  
ATOM   1348  SD  MET A 177      19.655   8.442   5.840  1.00 92.21           S  
ANISOU 1348  SD  MET A 177    12654  10869  11514    994   1672     74       S  
ATOM   1349  CE  MET A 177      19.411   6.920   4.918  1.00 96.42           C  
ANISOU 1349  CE  MET A 177    13553  11111  11970   1040   1918    -66       C  
ATOM   1350  N   PRO A 178      16.419   9.012   1.740  1.00 77.34           N  
ANISOU 1350  N   PRO A 178    11548   8919   8920    595   1484   -685       N  
ATOM   1351  CA  PRO A 178      15.343   8.953   0.741  1.00 86.36           C  
ANISOU 1351  CA  PRO A 178    12907  10056   9848    423   1398   -877       C  
ATOM   1352  C   PRO A 178      14.220   8.016   1.144  1.00 87.42           C  
ANISOU 1352  C   PRO A 178    13162  10125   9930    242   1316  -1002       C  
ATOM   1353  O   PRO A 178      13.048   8.307   0.874  1.00 85.99           O  
ANISOU 1353  O   PRO A 178    13004  10047   9622     55   1123  -1111       O  
ATOM   1354  CB  PRO A 178      16.071   8.472  -0.521  1.00 88.39           C  
ANISOU 1354  CB  PRO A 178    13434  10150   9998    517   1645   -912       C  
ATOM   1355  CG  PRO A 178      17.221   7.666   0.008  1.00 86.76           C  
ANISOU 1355  CG  PRO A 178    13218   9784   9962    715   1893   -773       C  
ATOM   1356  CD  PRO A 178      17.650   8.345   1.282  1.00 81.11           C  
ANISOU 1356  CD  PRO A 178    12142   9225   9450    787   1776   -592       C  
ATOM   1357  N   GLN A 179      14.543   6.901   1.807  1.00 84.33           N  
ANISOU 1357  N   GLN A 179    12833   9570   9640    293   1457   -968       N  
ATOM   1358  CA  GLN A 179      13.536   5.924   2.165  1.00 86.31           C  
ANISOU 1358  CA  GLN A 179    13221   9736   9839    118   1399  -1084       C  
ATOM   1359  C   GLN A 179      13.368   5.847   3.676  1.00 78.03           C  
ANISOU 1359  C   GLN A 179    11927   8756   8966    116   1296   -988       C  
ATOM   1360  O   GLN A 179      14.361   5.839   4.415  1.00 77.22           O  
ANISOU 1360  O   GLN A 179    11667   8637   9036    282   1396   -825       O  
ATOM   1361  CB  GLN A 179      13.903   4.534   1.636  1.00 96.78           C  
ANISOU 1361  CB  GLN A 179    14882  10779  11113    148   1662  -1147       C  
ATOM   1362  CG  GLN A 179      14.466   4.544   0.229  1.00101.38           C  
ANISOU 1362  CG  GLN A 179    15610  11308  11600    196   1780  -1143       C  
ATOM   1363  CD  GLN A 179      14.207   3.246  -0.502  1.00106.25           C  
ANISOU 1363  CD  GLN A 179    16510  11736  12126     85   1886  -1212       C  
ATOM   1364  OE1 GLN A 179      15.119   2.446  -0.719  1.00107.64           O  
ANISOU 1364  OE1 GLN A 179    16807  11722  12369    225   2135  -1136       O  
ATOM   1365  NE2 GLN A 179      12.953   3.027  -0.887  1.00108.79           N  
ANISOU 1365  NE2 GLN A 179    16931  12113  12292   -170   1701  -1340       N  
ATOM   1366  N   PRO A 180      12.133   5.804   4.161  1.00 72.01           N  
ANISOU 1366  N   PRO A 180    11120   8082   8158    -77   1096  -1072       N  
ATOM   1367  CA  PRO A 180      11.907   5.615   5.596  1.00 75.26           C  
ANISOU 1367  CA  PRO A 180    11333   8543   8718    -97   1012   -994       C  
ATOM   1368  C   PRO A 180      12.038   4.153   5.992  1.00 82.20           C  
ANISOU 1368  C   PRO A 180    12381   9205   9646    -98   1165   -999       C  
ATOM   1369  O   PRO A 180      11.768   3.242   5.206  1.00 91.84           O  
ANISOU 1369  O   PRO A 180    13899  10250  10745   -173   1273  -1119       O  
ATOM   1370  CB  PRO A 180      10.467   6.110   5.797  1.00 66.99           C  
ANISOU 1370  CB  PRO A 180    10197   7667   7588   -303    760  -1086       C  
ATOM   1371  CG  PRO A 180      10.064   6.765   4.475  1.00 62.27           C  
ANISOU 1371  CG  PRO A 180     9701   7142   6817   -368    696  -1176       C  
ATOM   1372  CD  PRO A 180      10.890   6.098   3.434  1.00 64.16           C  
ANISOU 1372  CD  PRO A 180    10214   7186   6979   -286    919  -1214       C  
ATOM   1373  N   VAL A 181      12.470   3.939   7.230  1.00 77.96           N  
ANISOU 1373  N   VAL A 181    11661   8677   9283    -23   1179   -862       N  
ATOM   1374  CA  VAL A 181      12.471   2.617   7.848  1.00 79.26           C  
ANISOU 1374  CA  VAL A 181    11934   8661   9519    -34   1291   -842       C  
ATOM   1375  C   VAL A 181      11.471   2.661   8.994  1.00 75.66           C  
ANISOU 1375  C   VAL A 181    11313   8336   9098   -194   1083   -853       C  
ATOM   1376  O   VAL A 181      11.596   3.492   9.903  1.00 75.95           O  
ANISOU 1376  O   VAL A 181    11078   8551   9229   -168    963   -750       O  
ATOM   1377  CB  VAL A 181      13.869   2.210   8.338  1.00 77.96           C  
ANISOU 1377  CB  VAL A 181    11693   8392   9536    195   1501   -638       C  
ATOM   1378  CG1 VAL A 181      13.875   0.744   8.778  1.00 72.74           C  
ANISOU 1378  CG1 VAL A 181    11193   7504   8941    198   1654   -620       C  
ATOM   1379  CG2 VAL A 181      14.911   2.464   7.251  1.00 79.26           C  
ANISOU 1379  CG2 VAL A 181    11953   8482   9682    375   1694   -596       C  
ATOM   1380  N   GLU A 182      10.471   1.784   8.947  1.00 70.05           N  
ANISOU 1380  N   GLU A 182    10777   7538   8301   -371   1045   -980       N  
ATOM   1381  CA  GLU A 182       9.383   1.850   9.920  1.00 66.60           C  
ANISOU 1381  CA  GLU A 182    10191   7237   7878   -540    844  -1001       C  
ATOM   1382  C   GLU A 182       9.848   1.324  11.272  1.00 52.55           C  
ANISOU 1382  C   GLU A 182     8271   5423   6270   -473    890   -856       C  
ATOM   1383  O   GLU A 182      10.476   0.259  11.335  1.00 51.01           O  
ANISOU 1383  O   GLU A 182     8218   5021   6143   -389   1077   -802       O  
ATOM   1384  CB  GLU A 182       8.180   1.047   9.448  1.00 81.61           C  
ANISOU 1384  CB  GLU A 182    12313   9064   9630   -768    782  -1162       C  
ATOM   1385  CG  GLU A 182       7.472   1.643   8.254  1.00101.57           C  
ANISOU 1385  CG  GLU A 182    14935  11686  11972   -891    674  -1288       C  
ATOM   1386  CD  GLU A 182       6.370   0.742   7.729  1.00121.46           C  
ANISOU 1386  CD  GLU A 182    17697  14125  14326  -1143    618  -1430       C  
ATOM   1387  OE1 GLU A 182       6.185  -0.361   8.289  1.00127.86           O  
ANISOU 1387  OE1 GLU A 182    18618  14789  15173  -1213    678  -1441       O  
ATOM   1388  OE2 GLU A 182       5.692   1.135   6.756  1.00128.50           O  
ANISOU 1388  OE2 GLU A 182    18623  15129  15071  -1260    501  -1488       O  
ATOM   1389  N   PRO A 183       9.554   2.023  12.365  1.00 45.17           N  
ANISOU 1389  N   PRO A 183     7073   4681   5407   -510    734   -786       N  
ATOM   1390  CA  PRO A 183       9.928   1.508  13.683  1.00 39.67           C  
ANISOU 1390  CA  PRO A 183     6249   3970   4855   -478    759   -645       C  
ATOM   1391  C   PRO A 183       9.153   0.246  14.023  1.00 43.08           C  
ANISOU 1391  C   PRO A 183     6827   4268   5272   -615    770   -708       C  
ATOM   1392  O   PRO A 183       8.039   0.018  13.540  1.00 50.35           O  
ANISOU 1392  O   PRO A 183     7875   5187   6068   -788    683   -861       O  
ATOM   1393  CB  PRO A 183       9.565   2.657  14.630  1.00 38.93           C  
ANISOU 1393  CB  PRO A 183     5883   4121   4788   -534    575   -601       C  
ATOM   1394  CG  PRO A 183       8.499   3.405  13.914  1.00 44.18           C  
ANISOU 1394  CG  PRO A 183     6566   4900   5322   -647    439   -751       C  
ATOM   1395  CD  PRO A 183       8.859   3.320  12.458  1.00 43.92           C  
ANISOU 1395  CD  PRO A 183     6732   4756   5198   -584    540   -826       C  
ATOM   1396  N   ARG A 184       9.771  -0.585  14.855  1.00 36.19           N  
ANISOU 1396  N   ARG A 184     5933   3288   4529   -543    878   -571       N  
ATOM   1397  CA  ARG A 184       9.184  -1.831  15.326  1.00 39.08           C  
ANISOU 1397  CA  ARG A 184     6428   3513   4908   -655    907   -599       C  
ATOM   1398  C   ARG A 184       8.468  -1.588  16.652  1.00 32.48           C  
ANISOU 1398  C   ARG A 184     5374   2856   4112   -784    729   -556       C  
ATOM   1399  O   ARG A 184       9.064  -1.018  17.575  1.00 31.46           O  
ANISOU 1399  O   ARG A 184     5017   2857   4080   -711    692   -406       O  
ATOM   1400  CB  ARG A 184      10.255  -2.896  15.507  1.00 44.76           C  
ANISOU 1400  CB  ARG A 184     7243   4006   5757   -492   1138   -453       C  
ATOM   1401  CG  ARG A 184       9.819  -4.295  15.102  1.00 69.61           C  
ANISOU 1401  CG  ARG A 184    10703   6886   8862   -571   1270   -551       C  
ATOM   1402  CD  ARG A 184      10.881  -5.346  15.430  1.00 85.78           C  
ANISOU 1402  CD  ARG A 184    12822   8702  11068   -386   1518   -374       C  
ATOM   1403  NE  ARG A 184      12.227  -4.923  15.047  1.00 95.45           N  
ANISOU 1403  NE  ARG A 184    13970   9911  12384   -135   1676   -223       N  
ATOM   1404  CZ  ARG A 184      12.731  -5.035  13.821  1.00100.91           C  
ANISOU 1404  CZ  ARG A 184    14880  10440  13021    -20   1864   -288       C  
ATOM   1405  NH1 ARG A 184      11.999  -5.553  12.843  1.00102.59           N  
ANISOU 1405  NH1 ARG A 184    15421  10489  13070   -153   1911   -511       N  
ATOM   1406  NH2 ARG A 184      13.968  -4.623  13.571  1.00101.23           N  
ANISOU 1406  NH2 ARG A 184    14814  10488  13160    212   2004   -122       N  
ATOM   1407  N   PRO A 185       7.197  -1.957  16.773  1.00 40.76           N  
ANISOU 1407  N   PRO A 185     6483   3925   5078   -987    615   -679       N  
ATOM   1408  CA  PRO A 185       6.535  -1.869  18.078  1.00 38.24           C  
ANISOU 1408  CA  PRO A 185     5973   3752   4803  -1102    479   -629       C  
ATOM   1409  C   PRO A 185       7.210  -2.803  19.067  1.00 37.68           C  
ANISOU 1409  C   PRO A 185     5880   3568   4867  -1040    582   -469       C  
ATOM   1410  O   PRO A 185       7.514  -3.952  18.751  1.00 37.56           O  
ANISOU 1410  O   PRO A 185     6067   3321   4881  -1005    734   -458       O  
ATOM   1411  CB  PRO A 185       5.096  -2.302  17.779  1.00 45.81           C  
ANISOU 1411  CB  PRO A 185     7045   4716   5645  -1326    372   -784       C  
ATOM   1412  CG  PRO A 185       4.947  -2.179  16.289  1.00 48.97           C  
ANISOU 1412  CG  PRO A 185     7642   5050   5916  -1342    397   -919       C  
ATOM   1413  CD  PRO A 185       6.295  -2.464  15.723  1.00 45.52           C  
ANISOU 1413  CD  PRO A 185     7333   4431   5534  -1137    602   -859       C  
ATOM   1414  N   SER A 186       7.473  -2.289  20.266  1.00 34.32           N  
ANISOU 1414  N   SER A 186     5217   3303   4519  -1028    507   -335       N  
ATOM   1415  CA  SER A 186       8.005  -3.144  21.317  1.00 33.04           C  
ANISOU 1415  CA  SER A 186     5005   3070   4478   -997    574   -162       C  
ATOM   1416  C   SER A 186       6.962  -4.109  21.859  1.00 33.38           C  
ANISOU 1416  C   SER A 186     5126   3054   4503  -1173    529   -219       C  
ATOM   1417  O   SER A 186       7.328  -5.096  22.509  1.00 34.03           O  
ANISOU 1417  O   SER A 186     5235   3015   4680  -1151    614    -92       O  
ATOM   1418  CB  SER A 186       8.530  -2.297  22.468  1.00 34.41           C  
ANISOU 1418  CB  SER A 186     4912   3452   4710   -977    488     -3       C  
ATOM   1419  OG  SER A 186       7.432  -1.644  23.092  1.00 29.29           O  
ANISOU 1419  OG  SER A 186     4156   2987   3985  -1144    322    -98       O  
ATOM   1420  N   GLY A 187       5.675  -3.851  21.613  1.00 32.44           N  
ANISOU 1420  N   GLY A 187     5035   3023   4270  -1346    399   -387       N  
ATOM   1421  CA  GLY A 187       4.611  -4.571  22.275  1.00 34.79           C  
ANISOU 1421  CA  GLY A 187     5350   3321   4547  -1534    325   -425       C  
ATOM   1422  C   GLY A 187       4.205  -3.965  23.596  1.00 31.23           C  
ANISOU 1422  C   GLY A 187     4657   3091   4120  -1611    199   -354       C  
ATOM   1423  O   GLY A 187       3.333  -4.519  24.277  1.00 31.61           O  
ANISOU 1423  O   GLY A 187     4693   3161   4158  -1765    138   -366       O  
ATOM   1424  N   TYR A 188       4.808  -2.844  23.968  1.00 22.81           N  
ANISOU 1424  N   TYR A 188     3355   2326   2987   -412    227   -369       N  
ATOM   1425  CA  TYR A 188       4.530  -2.160  25.215  1.00 26.07           C  
ANISOU 1425  CA  TYR A 188     3679   2790   3436   -347    195   -307       C  
ATOM   1426  C   TYR A 188       4.163  -0.710  24.938  1.00 26.27           C  
ANISOU 1426  C   TYR A 188     3656   2902   3423   -323    144   -279       C  
ATOM   1427  O   TYR A 188       4.488  -0.142  23.885  1.00 24.83           O  
ANISOU 1427  O   TYR A 188     3501   2736   3198   -334    140   -302       O  
ATOM   1428  CB  TYR A 188       5.737  -2.230  26.174  1.00 23.52           C  
ANISOU 1428  CB  TYR A 188     3343   2418   3178   -261    245   -287       C  
ATOM   1429  CG  TYR A 188       5.980  -3.633  26.653  1.00 24.99           C  
ANISOU 1429  CG  TYR A 188     3555   2523   3419   -271    298   -289       C  
ATOM   1430  CD1 TYR A 188       6.719  -4.529  25.884  1.00 30.30           C  
ANISOU 1430  CD1 TYR A 188     4305   3103   4104   -288    369   -333       C  
ATOM   1431  CD2 TYR A 188       5.444  -4.079  27.855  1.00 28.00           C  
ANISOU 1431  CD2 TYR A 188     3884   2915   3841   -264    286   -243       C  
ATOM   1432  CE1 TYR A 188       6.922  -5.830  26.307  1.00 33.03           C  
ANISOU 1432  CE1 TYR A 188     4677   3362   4510   -294    431   -329       C  
ATOM   1433  CE2 TYR A 188       5.646  -5.376  28.280  1.00 32.18           C  
ANISOU 1433  CE2 TYR A 188     4432   3367   4427   -273    337   -235       C  
ATOM   1434  CZ  TYR A 188       6.386  -6.243  27.500  1.00 32.61           C  
ANISOU 1434  CZ  TYR A 188     4566   3324   4502   -287    411   -277       C  
ATOM   1435  OH  TYR A 188       6.596  -7.536  27.920  1.00 38.69           O  
ANISOU 1435  OH  TYR A 188     5356   4005   5340   -290    476   -264       O  
ATOM   1436  N   ALA A 189       3.478  -0.125  25.917  1.00 23.62           N  
ANISOU 1436  N   ALA A 189     3249   2618   3106   -288    115   -226       N  
ATOM   1437  CA  ALA A 189       3.113   1.285  25.913  1.00 24.12           C  
ANISOU 1437  CA  ALA A 189     3264   2751   3152   -248     85   -189       C  
ATOM   1438  C   ALA A 189       3.220   1.794  27.349  1.00 30.91           C  
ANISOU 1438  C   ALA A 189     4080   3614   4050   -176     98   -154       C  
ATOM   1439  O   ALA A 189       3.330   1.015  28.301  1.00 25.37           O  
ANISOU 1439  O   ALA A 189     3373   2884   3382   -169    116   -148       O  
ATOM   1440  CB  ALA A 189       1.703   1.509  25.349  1.00 25.40           C  
ANISOU 1440  CB  ALA A 189     3384   2989   3277   -305     34   -148       C  
ATOM   1441  N   ALA A 190       3.209   3.115  27.508  1.00 27.54           N  
ANISOU 1441  N   ALA A 190     3627   3221   3617   -126     95   -132       N  
ATOM   1442  CA  ALA A 190       3.298   3.735  28.827  1.00 26.53           C  
ANISOU 1442  CA  ALA A 190     3474   3097   3511    -67    113   -109       C  
ATOM   1443  C   ALA A 190       2.095   4.651  29.021  1.00 26.15           C  
ANISOU 1443  C   ALA A 190     3377   3103   3458    -45    106    -59       C  
ATOM   1444  O   ALA A 190       1.958   5.651  28.309  1.00 24.10           O  
ANISOU 1444  O   ALA A 190     3108   2864   3184    -30    102    -46       O  
ATOM   1445  CB  ALA A 190       4.603   4.519  28.975  1.00 27.31           C  
ANISOU 1445  CB  ALA A 190     3601   3166   3609    -26    134   -131       C  
ATOM   1446  N   PHE A 191       1.220   4.312  29.969  1.00 23.28           N  
ANISOU 1446  N   PHE A 191     2977   2760   3110    -40    110    -22       N  
ATOM   1447  CA  PHE A 191       0.332   5.327  30.525  1.00 23.08           C  
ANISOU 1447  CA  PHE A 191     2911   2769   3089      8    131     28       C  
ATOM   1448  C   PHE A 191       1.187   6.331  31.287  1.00 23.23           C  
ANISOU 1448  C   PHE A 191     2965   2755   3105     62    171      0       C  
ATOM   1449  O   PHE A 191       2.088   5.939  32.029  1.00 27.06           O  
ANISOU 1449  O   PHE A 191     3482   3211   3589     60    179    -33       O  
ATOM   1450  CB  PHE A 191      -0.696   4.727  31.497  1.00 25.08           C  
ANISOU 1450  CB  PHE A 191     3120   3050   3359      8    137     74       C  
ATOM   1451  CG  PHE A 191      -1.679   3.775  30.875  1.00 28.19           C  
ANISOU 1451  CG  PHE A 191     3474   3483   3755    -56     95    112       C  
ATOM   1452  CD1 PHE A 191      -2.594   4.214  29.922  1.00 32.30           C  
ANISOU 1452  CD1 PHE A 191     3949   4059   4266    -77     69    167       C  
ATOM   1453  CD2 PHE A 191      -1.736   2.446  31.290  1.00 29.21           C  
ANISOU 1453  CD2 PHE A 191     3606   3597   3896   -102     80    103       C  
ATOM   1454  CE1 PHE A 191      -3.529   3.339  29.371  1.00 34.16           C  
ANISOU 1454  CE1 PHE A 191     4146   4340   4492   -155     21    208       C  
ATOM   1455  CE2 PHE A 191      -2.666   1.567  30.741  1.00 30.81           C  
ANISOU 1455  CE2 PHE A 191     3779   3831   4097   -175     40    137       C  
ATOM   1456  CZ  PHE A 191      -3.560   2.014  29.777  1.00 31.28           C  
ANISOU 1456  CZ  PHE A 191     3797   3953   4136   -208      6    188       C  
ATOM   1457  N   ARG A 192       0.914   7.628  31.119  1.00 22.46           N  
ANISOU 1457  N   ARG A 192     2864   2663   3008    106    198     20       N  
ATOM   1458  CA  ARG A 192       1.723   8.590  31.866  1.00 22.42           C  
ANISOU 1458  CA  ARG A 192     2906   2619   2994    142    238    -14       C  
ATOM   1459  C   ARG A 192       1.046   9.950  31.888  1.00 24.68           C  
ANISOU 1459  C   ARG A 192     3184   2901   3290    197    288     20       C  
ATOM   1460  O   ARG A 192       0.324  10.317  30.956  1.00 24.75           O  
ANISOU 1460  O   ARG A 192     3150   2939   3316    208    282     69       O  
ATOM   1461  CB  ARG A 192       3.134   8.725  31.291  1.00 26.94           C  
ANISOU 1461  CB  ARG A 192     3523   3159   3553    124    219    -63       C  
ATOM   1462  CG  ARG A 192       3.188   8.987  29.788  1.00 23.61           C  
ANISOU 1462  CG  ARG A 192     3092   2748   3132    114    193    -57       C  
ATOM   1463  CD  ARG A 192       4.636   8.913  29.301  1.00 24.55           C  
ANISOU 1463  CD  ARG A 192     3251   2835   3240     97    179   -102       C  
ATOM   1464  NE  ARG A 192       5.416  10.004  29.886  1.00 25.31           N  
ANISOU 1464  NE  ARG A 192     3384   2902   3332    122    205   -119       N  
ATOM   1465  CZ  ARG A 192       6.716   9.953  30.159  1.00 29.08           C  
ANISOU 1465  CZ  ARG A 192     3893   3355   3799    107    199   -146       C  
ATOM   1466  NH1 ARG A 192       7.408   8.850  29.920  1.00 32.10           N  
ANISOU 1466  NH1 ARG A 192     4275   3735   4187     82    179   -155       N  
ATOM   1467  NH2 ARG A 192       7.324  11.012  30.675  1.00 30.62           N  
ANISOU 1467  NH2 ARG A 192     4124   3528   3983    115    218   -159       N  
ATOM   1468  N   ALA A 193       1.299  10.696  32.964  1.00 23.58           N  
ANISOU 1468  N   ALA A 193     3090   2728   3140    227    342     -3       N  
ATOM   1469  CA  ALA A 193       0.681  12.009  33.124  1.00 22.99           C  
ANISOU 1469  CA  ALA A 193     3023   2630   3081    285    413     24       C  
ATOM   1470  C   ALA A 193       1.250  12.693  34.362  1.00 25.57           C  
ANISOU 1470  C   ALA A 193     3429   2908   3378    293    470    -29       C  
ATOM   1471  O   ALA A 193       1.894  12.065  35.207  1.00 25.58           O  
ANISOU 1471  O   ALA A 193     3462   2913   3346    252    450    -68       O  
ATOM   1472  CB  ALA A 193      -0.838  11.897  33.252  1.00 24.97           C  
ANISOU 1472  CB  ALA A 193     3205   2921   3363    323    444    105       C  
ATOM   1473  N   LEU A 194       1.004  14.001  34.442  1.00 21.52           N  
ANISOU 1473  N   LEU A 194     2952   2348   2877    340    545    -25       N  
ATOM   1474  CA  LEU A 194       1.112  14.751  35.682  1.00 28.91           C  
ANISOU 1474  CA  LEU A 194     3968   3233   3782    351    625    -67       C  
ATOM   1475  C   LEU A 194      -0.178  14.617  36.473  1.00 26.67           C  
ANISOU 1475  C   LEU A 194     3658   2965   3512    399    693    -20       C  
ATOM   1476  O   LEU A 194      -1.265  14.479  35.902  1.00 27.90           O  
ANISOU 1476  O   LEU A 194     3731   3154   3716    445    702     61       O  
ATOM   1477  CB  LEU A 194       1.327  16.237  35.408  1.00 31.62           C  
ANISOU 1477  CB  LEU A 194     4370   3503   4139    383    694    -83       C  
ATOM   1478  CG  LEU A 194       2.507  16.647  34.558  1.00 33.94           C  
ANISOU 1478  CG  LEU A 194     4690   3776   4429    347    643   -117       C  
ATOM   1479  CD1 LEU A 194       2.416  18.124  34.311  1.00 32.00           C  
ANISOU 1479  CD1 LEU A 194     4492   3454   4211    391    726   -115       C  
ATOM   1480  CD2 LEU A 194       3.777  16.294  35.299  1.00 39.01           C  
ANISOU 1480  CD2 LEU A 194     5396   4417   5009    269    598   -188       C  
ATOM   1481  N   VAL A 195      -0.054  14.711  37.790  1.00 25.46           N  
ANISOU 1481  N   VAL A 195     3573   2791   3311    386    744    -65       N  
ATOM   1482  CA  VAL A 195      -1.198  14.737  38.695  1.00 28.94           C  
ANISOU 1482  CA  VAL A 195     4005   3235   3755    436    830    -28       C  
ATOM   1483  C   VAL A 195      -1.579  16.189  38.948  1.00 33.78           C  
ANISOU 1483  C   VAL A 195     4689   3765   4382    498    961    -35       C  
ATOM   1484  O   VAL A 195      -0.730  17.087  38.909  1.00 37.76           O  
ANISOU 1484  O   VAL A 195     5281   4204   4862    474    984   -100       O  
ATOM   1485  CB  VAL A 195      -0.851  13.994  40.000  1.00 28.95           C  
ANISOU 1485  CB  VAL A 195     4046   3265   3689    382    816    -72       C  
ATOM   1486  CG1 VAL A 195      -2.013  13.995  40.966  1.00 39.60           C  
ANISOU 1486  CG1 VAL A 195     5388   4621   5036    435    909    -34       C  
ATOM   1487  CG2 VAL A 195      -0.434  12.559  39.664  1.00 27.91           C  
ANISOU 1487  CG2 VAL A 195     3843   3203   3560    328    696    -57       C  
ATOM   1488  N   ASP A 196      -2.873  16.434  39.176  1.00 29.76           N  
ANISOU 1488  N   ASP A 196     4138   3254   3916    580   1054     39       N  
ATOM   1489  CA  ASP A 196      -3.333  17.743  39.649  1.00 36.85           C  
ANISOU 1489  CA  ASP A 196     5112   4060   4828    650   1209     35       C  
ATOM   1490  C   ASP A 196      -2.976  17.886  41.123  1.00 36.53           C  
ANISOU 1490  C   ASP A 196     5197   3983   4701    610   1276    -56       C  
ATOM   1491  O   ASP A 196      -3.581  17.234  41.978  1.00 35.70           O  
ANISOU 1491  O   ASP A 196     5072   3922   4572    618   1297    -36       O  
ATOM   1492  CB  ASP A 196      -4.837  17.879  39.430  1.00 40.95           C  
ANISOU 1492  CB  ASP A 196     5534   4597   5428    755   1292    163       C  
ATOM   1493  CG  ASP A 196      -5.379  19.261  39.796  1.00 56.28           C  
ANISOU 1493  CG  ASP A 196     7547   6432   7405    846   1474    177       C  
ATOM   1494  OD1 ASP A 196      -4.956  19.853  40.815  1.00 58.11           O  
ANISOU 1494  OD1 ASP A 196     7919   6584   7576    828   1565     79       O  
ATOM   1495  OD2 ASP A 196      -6.258  19.751  39.062  1.00 61.02           O  
ANISOU 1495  OD2 ASP A 196     8062   7029   8095    934   1531    292       O  
ATOM   1496  N   THR A 197      -1.996  18.746  41.432  1.00 38.48           N  
ANISOU 1496  N   THR A 197     5573   4154   4895    559   1307   -155       N  
ATOM   1497  CA  THR A 197      -1.511  18.862  42.813  1.00 38.54           C  
ANISOU 1497  CA  THR A 197     5708   4137   4797    491   1352   -250       C  
ATOM   1498  C   THR A 197      -2.579  19.422  43.754  1.00 39.61           C  
ANISOU 1498  C   THR A 197     5903   4218   4928    565   1523   -240       C  
ATOM   1499  O   THR A 197      -2.642  19.026  44.925  1.00 38.44           O  
ANISOU 1499  O   THR A 197     5807   4097   4700    526   1550   -279       O  
ATOM   1500  CB  THR A 197      -0.244  19.733  42.848  1.00 42.61           C  
ANISOU 1500  CB  THR A 197     6351   4584   5256    407   1345   -351       C  
ATOM   1501  OG1 THR A 197       0.731  19.187  41.951  1.00 42.29           O  
ANISOU 1501  OG1 THR A 197     6246   4597   5224    349   1193   -347       O  
ATOM   1502  CG2 THR A 197       0.353  19.769  44.265  1.00 37.40           C  
ANISOU 1502  CG2 THR A 197     5822   3920   4468    307   1369   -447       C  
ATOM   1503  N   GLU A 198      -3.426  20.334  43.271  1.00 42.65           N  
ANISOU 1503  N   GLU A 198     6277   4529   5399    674   1647   -181       N  
ATOM   1504  CA  GLU A 198      -4.413  20.933  44.161  1.00 48.33           C  
ANISOU 1504  CA  GLU A 198     7060   5182   6121    754   1833   -169       C  
ATOM   1505  C   GLU A 198      -5.429  19.904  44.649  1.00 46.29           C  
ANISOU 1505  C   GLU A 198     6696   5019   5874    799   1828    -84       C  
ATOM   1506  O   GLU A 198      -5.720  19.842  45.849  1.00 49.08           O  
ANISOU 1506  O   GLU A 198     7124   5364   6158    794   1916   -121       O  
ATOM   1507  CB  GLU A 198      -5.105  22.104  43.465  1.00 56.96           C  
ANISOU 1507  CB  GLU A 198     8146   6174   7321    873   1972   -101       C  
ATOM   1508  CG  GLU A 198      -4.202  23.323  43.313  1.00 68.14           C  
ANISOU 1508  CG  GLU A 198     9707   7465   8718    833   2028   -198       C  
ATOM   1509  CD  GLU A 198      -3.509  23.700  44.612  1.00 80.76           C  
ANISOU 1509  CD  GLU A 198    11500   8999  10184    735   2092   -347       C  
ATOM   1510  OE1 GLU A 198      -4.192  23.793  45.656  1.00 86.54           O  
ANISOU 1510  OE1 GLU A 198    12300   9702  10879    770   2225   -361       O  
ATOM   1511  OE2 GLU A 198      -2.273  23.895  44.591  1.00 84.61           O  
ANISOU 1511  OE2 GLU A 198    12073   9473  10602    617   2006   -445       O  
ATOM   1512  N   THR A 199      -5.977  19.081  43.744  1.00 43.42           N  
ANISOU 1512  N   THR A 199     6162   4747   5588    834   1727     31       N  
ATOM   1513  CA  THR A 199      -6.924  18.064  44.194  1.00 44.35           C  
ANISOU 1513  CA  THR A 199     6177   4958   5718    865   1714    116       C  
ATOM   1514  C   THR A 199      -6.219  16.936  44.936  1.00 38.15           C  
ANISOU 1514  C   THR A 199     5408   4251   4838    756   1596     48       C  
ATOM   1515  O   THR A 199      -6.817  16.315  45.822  1.00 38.36           O  
ANISOU 1515  O   THR A 199     5412   4327   4836    766   1625     76       O  
ATOM   1516  CB  THR A 199      -7.736  17.508  43.020  1.00 44.75           C  
ANISOU 1516  CB  THR A 199     6045   5085   5871    917   1637    260       C  
ATOM   1517  OG1 THR A 199      -6.884  16.775  42.134  1.00 46.85           O  
ANISOU 1517  OG1 THR A 199     6262   5411   6130    830   1459    235       O  
ATOM   1518  CG2 THR A 199      -8.414  18.638  42.253  1.00 48.02           C  
ANISOU 1518  CG2 THR A 199     6428   5434   6384   1025   1751    348       C  
ATOM   1519  N   LEU A 200      -4.958  16.653  44.588  1.00 38.70           N  
ANISOU 1519  N   LEU A 200     5506   4335   4862    655   1466    -29       N  
ATOM   1520  CA  LEU A 200      -4.169  15.689  45.352  1.00 37.43           C  
ANISOU 1520  CA  LEU A 200     5368   4242   4613    551   1367    -87       C  
ATOM   1521  C   LEU A 200      -4.078  16.106  46.815  1.00 37.65           C  
ANISOU 1521  C   LEU A 200     5529   4238   4537    520   1472   -163       C  
ATOM   1522  O   LEU A 200      -4.335  15.305  47.724  1.00 41.53           O  
ANISOU 1522  O   LEU A 200     6002   4798   4981    496   1461   -150       O  
ATOM   1523  CB  LEU A 200      -2.775  15.555  44.735  1.00 38.51           C  
ANISOU 1523  CB  LEU A 200     5525   4384   4724    458   1238   -150       C  
ATOM   1524  CG  LEU A 200      -1.870  14.461  45.284  1.00 35.66           C  
ANISOU 1524  CG  LEU A 200     5155   4101   4294    354   1118   -182       C  
ATOM   1525  CD1 LEU A 200      -2.486  13.092  44.990  1.00 32.72           C  
ANISOU 1525  CD1 LEU A 200     4642   3815   3976    374   1036    -93       C  
ATOM   1526  CD2 LEU A 200      -0.464  14.569  44.688  1.00 35.01           C  
ANISOU 1526  CD2 LEU A 200     5102   4008   4190    274   1018   -237       C  
ATOM   1527  N   LYS A 201      -3.689  17.357  47.060  1.00 41.62           N  
ANISOU 1527  N   LYS A 201     6174   4640   5001    511   1575   -245       N  
ATOM   1528  CA  LYS A 201      -3.794  17.917  48.395  1.00 42.89           C  
ANISOU 1528  CA  LYS A 201     6479   4754   5063    489   1707   -318       C  
ATOM   1529  C   LYS A 201      -5.253  17.886  48.821  1.00 45.96           C  
ANISOU 1529  C   LYS A 201     6822   5140   5499    608   1842   -236       C  
ATOM   1530  O   LYS A 201      -6.158  18.090  48.010  1.00 60.78           O  
ANISOU 1530  O   LYS A 201     8603   6999   7493    721   1888   -136       O  
ATOM   1531  CB  LYS A 201      -3.264  19.351  48.420  1.00 42.69           C  
ANISOU 1531  CB  LYS A 201     6618   4599   5004    467   1812   -415       C  
ATOM   1532  CG  LYS A 201      -1.800  19.487  48.066  1.00 53.51           C  
ANISOU 1532  CG  LYS A 201     8039   5970   6321    344   1687   -493       C  
ATOM   1533  CD  LYS A 201      -1.252  20.859  48.456  1.00 63.78           C  
ANISOU 1533  CD  LYS A 201     9532   7146   7555    291   1799   -606       C  
ATOM   1534  CE  LYS A 201      -1.993  21.976  47.752  1.00 67.99           C  
ANISOU 1534  CE  LYS A 201    10084   7552   8197    417   1946   -576       C  
ATOM   1535  NZ  LYS A 201      -1.053  22.918  47.084  1.00 72.16           N  
ANISOU 1535  NZ  LYS A 201    10690   7994   8732    365   1928   -636       N  
ATOM   1536  N   GLY A 202      -5.498  17.610  50.090  1.00 49.30           N  
ANISOU 1536  N   GLY A 202     7306   5593   5832    582   1904   -264       N  
ATOM   1537  CA  GLY A 202      -6.898  17.583  50.466  1.00 54.70           C  
ANISOU 1537  CA  GLY A 202     7938   6276   6568    703   2038   -174       C  
ATOM   1538  C   GLY A 202      -7.649  16.333  50.072  1.00 53.26           C  
ANISOU 1538  C   GLY A 202     7562   6210   6465    748   1938    -42       C  
ATOM   1539  O   GLY A 202      -8.855  16.259  50.310  1.00 49.61           O  
ANISOU 1539  O   GLY A 202     7034   5758   6056    850   2039     54       O  
ATOM   1540  N   ASP A 203      -6.987  15.357  49.447  1.00 43.12           N  
ANISOU 1540  N   ASP A 203     6183   5007   5194    675   1748    -28       N  
ATOM   1541  CA  ASP A 203      -7.499  13.995  49.477  1.00 34.96           C  
ANISOU 1541  CA  ASP A 203     5004   4087   4193    674   1649     65       C  
ATOM   1542  C   ASP A 203      -6.737  13.267  50.572  1.00 39.04           C  
ANISOU 1542  C   ASP A 203     5573   4668   4593    565   1584      0       C  
ATOM   1543  O   ASP A 203      -5.574  12.893  50.361  1.00 36.43           O  
ANISOU 1543  O   ASP A 203     5257   4363   4224    466   1457    -55       O  
ATOM   1544  CB  ASP A 203      -7.312  13.291  48.128  1.00 33.04           C  
ANISOU 1544  CB  ASP A 203     4628   3889   4038    661   1493    124       C  
ATOM   1545  CG  ASP A 203      -7.773  11.834  48.160  1.00 41.98           C  
ANISOU 1545  CG  ASP A 203     5624   5128   5200    644   1389    211       C  
ATOM   1546  OD1 ASP A 203      -8.264  11.380  49.223  1.00 40.32           O  
ANISOU 1546  OD1 ASP A 203     5410   4961   4948    650   1435    234       O  
ATOM   1547  OD2 ASP A 203      -7.649  11.137  47.127  1.00 37.60           O  
ANISOU 1547  OD2 ASP A 203     4970   4610   4706    621   1265    254       O  
ATOM   1548  N   PRO A 204      -7.336  13.034  51.750  1.00 41.59           N  
ANISOU 1548  N   PRO A 204     5919   5025   4858    579   1668     15       N  
ATOM   1549  CA  PRO A 204      -6.570  12.425  52.849  1.00 38.30           C  
ANISOU 1549  CA  PRO A 204     5557   4677   4319    466   1611    -43       C  
ATOM   1550  C   PRO A 204      -6.062  11.040  52.527  1.00 37.90           C  
ANISOU 1550  C   PRO A 204     5382   4723   4295    402   1430      7       C  
ATOM   1551  O   PRO A 204      -5.035  10.626  53.077  1.00 41.43           O  
ANISOU 1551  O   PRO A 204     5868   5218   4657    294   1348    -42       O  
ATOM   1552  CB  PRO A 204      -7.576  12.388  54.014  1.00 43.53           C  
ANISOU 1552  CB  PRO A 204     6240   5362   4936    518   1745     -8       C  
ATOM   1553  CG  PRO A 204      -8.669  13.328  53.623  1.00 44.77           C  
ANISOU 1553  CG  PRO A 204     6403   5433   5177    654   1905     36       C  
ATOM   1554  CD  PRO A 204      -8.735  13.283  52.130  1.00 40.98           C  
ANISOU 1554  CD  PRO A 204     5810   4935   4825    697   1818     97       C  
ATOM   1555  N   GLU A 205      -6.754  10.304  51.654  1.00 34.75           N  
ANISOU 1555  N   GLU A 205     4835   4354   4012    461   1368    108       N  
ATOM   1556  CA  GLU A 205      -6.288   8.974  51.281  1.00 37.02           C  
ANISOU 1556  CA  GLU A 205     5015   4716   4334    401   1210    150       C  
ATOM   1557  C   GLU A 205      -5.031   9.018  50.423  1.00 36.05           C  
ANISOU 1557  C   GLU A 205     4913   4568   4217    334   1101     91       C  
ATOM   1558  O   GLU A 205      -4.407   7.971  50.224  1.00 32.28           O  
ANISOU 1558  O   GLU A 205     4371   4141   3753    275    981    111       O  
ATOM   1559  CB  GLU A 205      -7.391   8.211  50.547  1.00 37.62           C  
ANISOU 1559  CB  GLU A 205     4943   4825   4525    468   1177    268       C  
ATOM   1560  CG  GLU A 205      -8.670   8.059  51.356  1.00 40.27           C  
ANISOU 1560  CG  GLU A 205     5236   5198   4868    538   1277    349       C  
ATOM   1561  CD  GLU A 205      -9.652   7.088  50.721  1.00 54.83           C  
ANISOU 1561  CD  GLU A 205     6922   7095   6816    574   1216    474       C  
ATOM   1562  OE1 GLU A 205      -9.534   6.825  49.505  1.00 53.38           O  
ANISOU 1562  OE1 GLU A 205     6675   6902   6704    562   1126    495       O  
ATOM   1563  OE2 GLU A 205     -10.544   6.582  51.440  1.00 60.49           O  
ANISOU 1563  OE2 GLU A 205     7580   7866   7539    606   1259    553       O  
ATOM   1564  N   ALA A 206      -4.644  10.191  49.924  1.00 32.55           N  
ANISOU 1564  N   ALA A 206     4556   4044   3766    345   1148     25       N  
ATOM   1565  CA  ALA A 206      -3.427  10.342  49.139  1.00 31.83           C  
ANISOU 1565  CA  ALA A 206     4490   3928   3675    282   1055    -30       C  
ATOM   1566  C   ALA A 206      -2.326  11.082  49.890  1.00 36.02           C  
ANISOU 1566  C   ALA A 206     5159   4436   4090    195   1073   -130       C  
ATOM   1567  O   ALA A 206      -1.246  11.298  49.320  1.00 36.64           O  
ANISOU 1567  O   ALA A 206     5264   4496   4162    138   1001   -173       O  
ATOM   1568  CB  ALA A 206      -3.737  11.070  47.825  1.00 33.30           C  
ANISOU 1568  CB  ALA A 206     4657   4047   3950    350   1073    -19       C  
ATOM   1569  N   SER A 207      -2.560  11.455  51.156  1.00 36.14           N  
ANISOU 1569  N   SER A 207     5264   4458   4008    175   1166   -165       N  
ATOM   1570  CA  SER A 207      -1.614  12.294  51.890  1.00 37.84           C  
ANISOU 1570  CA  SER A 207     5629   4648   4099     79   1196   -266       C  
ATOM   1571  C   SER A 207      -0.254  11.631  52.050  1.00 33.88           C  
ANISOU 1571  C   SER A 207     5110   4219   3542    -44   1055   -274       C  
ATOM   1572  O   SER A 207       0.764  12.325  52.160  1.00 35.78           O  
ANISOU 1572  O   SER A 207     5448   4437   3709   -132   1038   -345       O  
ATOM   1573  CB  SER A 207      -2.186  12.637  53.268  1.00 42.26           C  
ANISOU 1573  CB  SER A 207     6285   5217   4556     71   1320   -296       C  
ATOM   1574  OG  SER A 207      -3.308  13.482  53.130  1.00 56.78           O  
ANISOU 1574  OG  SER A 207     8162   6969   6443    186   1475   -294       O  
ATOM   1575  N   TRP A 208      -0.215  10.296  52.062  1.00 34.76           N  
ANISOU 1575  N   TRP A 208     5097   4417   3693    -52    958   -195       N  
ATOM   1576  CA  TRP A 208       1.051   9.586  52.220  1.00 35.17           C  
ANISOU 1576  CA  TRP A 208     5115   4540   3707   -156    833   -179       C  
ATOM   1577  C   TRP A 208       2.079   9.990  51.169  1.00 36.69           C  
ANISOU 1577  C   TRP A 208     5317   4687   3935   -184    765   -210       C  
ATOM   1578  O   TRP A 208       3.283   9.953  51.442  1.00 33.00           O  
ANISOU 1578  O   TRP A 208     4873   4261   3405   -286    694   -221       O  
ATOM   1579  CB  TRP A 208       0.815   8.083  52.142  1.00 38.82           C  
ANISOU 1579  CB  TRP A 208     5433   5075   4243   -135    755    -80       C  
ATOM   1580  CG  TRP A 208       0.200   7.663  50.844  1.00 34.74           C  
ANISOU 1580  CG  TRP A 208     4821   4514   3864    -43    731    -38       C  
ATOM   1581  CD1 TRP A 208      -1.135   7.612  50.545  1.00 36.25           C  
ANISOU 1581  CD1 TRP A 208     4966   4682   4124     53    793      0       C  
ATOM   1582  CD2 TRP A 208       0.894   7.256  49.661  1.00 35.30           C  
ANISOU 1582  CD2 TRP A 208     4834   4565   4014    -46    642    -24       C  
ATOM   1583  NE1 TRP A 208      -1.309   7.186  49.248  1.00 30.29           N  
ANISOU 1583  NE1 TRP A 208     4129   3901   3478     96    737     34       N  
ATOM   1584  CE2 TRP A 208      -0.080   6.955  48.688  1.00 31.59           C  
ANISOU 1584  CE2 TRP A 208     4291   4062   3649     39    650     14       C  
ATOM   1585  CE3 TRP A 208       2.246   7.092  49.339  1.00 34.63           C  
ANISOU 1585  CE3 TRP A 208     4749   4491   3919   -114    560    -33       C  
ATOM   1586  CZ2 TRP A 208       0.256   6.506  47.409  1.00 32.25           C  
ANISOU 1586  CZ2 TRP A 208     4316   4120   3817     51    579     30       C  
ATOM   1587  CZ3 TRP A 208       2.580   6.650  48.066  1.00 32.07           C  
ANISOU 1587  CZ3 TRP A 208     4362   4134   3688    -88    499    -13       C  
ATOM   1588  CH2 TRP A 208       1.589   6.366  47.116  1.00 30.20           C  
ANISOU 1588  CH2 TRP A 208     4067   3861   3545     -9    510     11       C  
ATOM   1589  N   VAL A 209       1.631  10.369  49.967  1.00 33.06           N  
ANISOU 1589  N   VAL A 209     4832   4153   3576    -99    784   -213       N  
ATOM   1590  CA  VAL A 209       2.562  10.587  48.869  1.00 32.61           C  
ANISOU 1590  CA  VAL A 209     4765   4061   3564   -117    713   -228       C  
ATOM   1591  C   VAL A 209       3.417  11.826  49.108  1.00 28.21           C  
ANISOU 1591  C   VAL A 209     4338   3460   2921   -191    740   -311       C  
ATOM   1592  O   VAL A 209       4.464  11.990  48.465  1.00 31.39           O  
ANISOU 1592  O   VAL A 209     4740   3855   3334   -236    669   -321       O  
ATOM   1593  CB  VAL A 209       1.793  10.685  47.533  1.00 28.93           C  
ANISOU 1593  CB  VAL A 209     4238   3536   3218    -12    728   -204       C  
ATOM   1594  CG1 VAL A 209       1.214  12.067  47.345  1.00 26.62           C  
ANISOU 1594  CG1 VAL A 209     4033   3156   2924     41    839   -254       C  
ATOM   1595  CG2 VAL A 209       2.695  10.310  46.358  1.00 24.44           C  
ANISOU 1595  CG2 VAL A 209     3613   2963   2709    -28    629   -190       C  
ATOM   1596  N   PHE A 210       3.002  12.707  50.026  1.00 32.55           N  
ANISOU 1596  N   PHE A 210     5006   3978   3383   -208    845   -372       N  
ATOM   1597  CA  PHE A 210       3.774  13.898  50.350  1.00 32.48           C  
ANISOU 1597  CA  PHE A 210     5139   3920   3281   -295    878   -459       C  
ATOM   1598  C   PHE A 210       4.882  13.646  51.361  1.00 37.44           C  
ANISOU 1598  C   PHE A 210     5808   4636   3780   -446    806   -470       C  
ATOM   1599  O   PHE A 210       5.670  14.563  51.619  1.00 34.44           O  
ANISOU 1599  O   PHE A 210     5544   4229   3314   -545    812   -538       O  
ATOM   1600  CB  PHE A 210       2.852  14.997  50.889  1.00 34.77           C  
ANISOU 1600  CB  PHE A 210     5558   4124   3531   -252   1040   -527       C  
ATOM   1601  CG  PHE A 210       1.918  15.557  49.863  1.00 36.90           C  
ANISOU 1601  CG  PHE A 210     5802   4298   3922   -114   1120   -513       C  
ATOM   1602  CD1 PHE A 210       2.311  16.617  49.050  1.00 37.33           C  
ANISOU 1602  CD1 PHE A 210     5918   4258   4009   -107   1146   -558       C  
ATOM   1603  CD2 PHE A 210       0.655  15.014  49.691  1.00 37.81           C  
ANISOU 1603  CD2 PHE A 210     5822   4425   4120      3   1166   -441       C  
ATOM   1604  CE1 PHE A 210       1.449  17.127  48.090  1.00 39.34           C  
ANISOU 1604  CE1 PHE A 210     6136   4435   4378     20   1218   -528       C  
ATOM   1605  CE2 PHE A 210      -0.210  15.521  48.732  1.00 39.67           C  
ANISOU 1605  CE2 PHE A 210     6019   4587   4465    123   1233   -408       C  
ATOM   1606  CZ  PHE A 210       0.187  16.576  47.933  1.00 36.96           C  
ANISOU 1606  CZ  PHE A 210     5734   4154   4155    133   1260   -449       C  
ATOM   1607  N   GLU A 211       4.967  12.446  51.936  1.00 34.55           N  
ANISOU 1607  N   GLU A 211     5349   4379   3401   -473    738   -397       N  
ATOM   1608  CA  GLU A 211       5.936  12.212  53.004  1.00 37.42           C  
ANISOU 1608  CA  GLU A 211     5743   4841   3635   -621    674   -389       C  
ATOM   1609  C   GLU A 211       7.347  12.479  52.502  1.00 33.78           C  
ANISOU 1609  C   GLU A 211     5282   4392   3160   -713    577   -386       C  
ATOM   1610  O   GLU A 211       7.792  11.866  51.524  1.00 35.05           O  
ANISOU 1610  O   GLU A 211     5331   4558   3427   -668    500   -325       O  
ATOM   1611  CB  GLU A 211       5.825  10.781  53.530  1.00 40.03           C  
ANISOU 1611  CB  GLU A 211     5945   5285   3981   -619    610   -287       C  
ATOM   1612  CG  GLU A 211       4.732  10.559  54.554  1.00 64.21           C  
ANISOU 1612  CG  GLU A 211     9030   8376   6991   -591    695   -287       C  
ATOM   1613  CD  GLU A 211       4.783   9.161  55.147  1.00 79.99           C  
ANISOU 1613  CD  GLU A 211    10903  10493   8997   -608    622   -180       C  
ATOM   1614  OE1 GLU A 211       5.834   8.498  54.999  1.00 82.92           O  
ANISOU 1614  OE1 GLU A 211    11193  10930   9382   -670    513   -112       O  
ATOM   1615  OE2 GLU A 211       3.777   8.728  55.753  1.00 83.95           O  
ANISOU 1615  OE2 GLU A 211    11382  11019   9495   -556    680   -155       O  
ATOM   1616  N   GLY A 212       8.026  13.428  53.146  1.00 33.09           N  
ANISOU 1616  N   GLY A 212     5327   4304   2942   -843    588   -454       N  
ATOM   1617  CA  GLY A 212       9.423  13.723  52.895  1.00 37.99           C  
ANISOU 1617  CA  GLY A 212     5953   4955   3524   -959    493   -443       C  
ATOM   1618  C   GLY A 212       9.750  14.431  51.593  1.00 36.66           C  
ANISOU 1618  C   GLY A 212     5794   4686   3448   -906    490   -474       C  
ATOM   1619  O   GLY A 212      10.938  14.677  51.330  1.00 34.97           O  
ANISOU 1619  O   GLY A 212     5577   4498   3210   -999    409   -456       O  
ATOM   1620  N   VAL A 213       8.752  14.779  50.770  1.00 31.43           N  
ANISOU 1620  N   VAL A 213     5136   3916   2891   -764    574   -509       N  
ATOM   1621  CA  VAL A 213       9.065  15.310  49.446  1.00 27.80           C  
ANISOU 1621  CA  VAL A 213     4660   3375   2528   -708    561   -520       C  
ATOM   1622  C   VAL A 213       9.703  16.692  49.493  1.00 27.90           C  
ANISOU 1622  C   VAL A 213     4817   3318   2467   -801    592   -604       C  
ATOM   1623  O   VAL A 213      10.283  17.126  48.489  1.00 32.23           O  
ANISOU 1623  O   VAL A 213     5349   3819   3076   -789    557   -602       O  
ATOM   1624  CB  VAL A 213       7.810  15.336  48.550  1.00 31.26           C  
ANISOU 1624  CB  VAL A 213     5057   3729   3092   -541    639   -520       C  
ATOM   1625  CG1 VAL A 213       7.269  13.915  48.355  1.00 31.76           C  
ANISOU 1625  CG1 VAL A 213     4973   3860   3236   -462    594   -433       C  
ATOM   1626  CG2 VAL A 213       6.753  16.269  49.125  1.00 33.30           C  
ANISOU 1626  CG2 VAL A 213     5438   3903   3310   -503    785   -596       C  
ATOM   1627  N   GLU A 214       9.617  17.414  50.617  1.00 32.28           N  
ANISOU 1627  N   GLU A 214     5519   3859   2887   -900    660   -682       N  
ATOM   1628  CA  GLU A 214      10.294  18.707  50.666  1.00 40.22           C  
ANISOU 1628  CA  GLU A 214     6672   4793   3818  -1007    686   -766       C  
ATOM   1629  C   GLU A 214      11.801  18.555  50.820  1.00 41.82           C  
ANISOU 1629  C   GLU A 214     6848   5094   3948  -1168    547   -721       C  
ATOM   1630  O   GLU A 214      12.555  19.468  50.467  1.00 43.89           O  
ANISOU 1630  O   GLU A 214     7185   5305   4188  -1245    532   -761       O  
ATOM   1631  CB  GLU A 214       9.733  19.559  51.799  1.00 44.04           C  
ANISOU 1631  CB  GLU A 214     7340   5220   4174  -1072    814   -872       C  
ATOM   1632  CG  GLU A 214       8.274  19.905  51.619  1.00 53.79           C  
ANISOU 1632  CG  GLU A 214     8609   6342   5485   -909    971   -910       C  
ATOM   1633  CD  GLU A 214       7.905  21.194  52.311  1.00 73.71           C  
ANISOU 1633  CD  GLU A 214    11346   8746   7914   -958   1126  -1033       C  
ATOM   1634  OE1 GLU A 214       8.652  22.184  52.148  1.00 83.21           O  
ANISOU 1634  OE1 GLU A 214    12663   9880   9074  -1055   1130  -1098       O  
ATOM   1635  OE2 GLU A 214       6.876  21.216  53.020  1.00 81.25           O  
ANISOU 1635  OE2 GLU A 214    12358   9673   8839   -901   1249  -1063       O  
ATOM   1636  N   GLU A 215      12.255  17.428  51.359  1.00 37.22           N  
ANISOU 1636  N   GLU A 215     6157   4653   3331  -1221    449   -630       N  
ATOM   1637  CA  GLU A 215      13.678  17.155  51.509  1.00 41.22           C  
ANISOU 1637  CA  GLU A 215     6609   5270   3781  -1364    315   -555       C  
ATOM   1638  C   GLU A 215      14.224  16.260  50.410  1.00 37.67           C  
ANISOU 1638  C   GLU A 215     5981   4859   3473  -1277    223   -442       C  
ATOM   1639  O   GLU A 215      15.358  16.463  49.959  1.00 33.82           O  
ANISOU 1639  O   GLU A 215     5461   4398   2989  -1348    142   -397       O  
ATOM   1640  CB  GLU A 215      13.962  16.506  52.866  1.00 44.31           C  
ANISOU 1640  CB  GLU A 215     6991   5805   4038  -1495    264   -507       C  
ATOM   1641  CG  GLU A 215      13.711  17.421  54.055  1.00 58.39           C  
ANISOU 1641  CG  GLU A 215     8968   7571   5645  -1630    339   -620       C  
ATOM   1642  CD  GLU A 215      12.238  17.549  54.407  1.00 70.44           C  
ANISOU 1642  CD  GLU A 215    10570   9013   7180  -1513    486   -701       C  
ATOM   1643  OE1 GLU A 215      11.499  16.551  54.271  1.00 71.59           O  
ANISOU 1643  OE1 GLU A 215    10594   9189   7419  -1380    492   -637       O  
ATOM   1644  OE2 GLU A 215      11.817  18.653  54.819  1.00 78.96           O  
ANISOU 1644  OE2 GLU A 215    11832   9992   8178  -1554    601   -825       O  
ATOM   1645  N   ASN A 216      13.447  15.271  49.971  1.00 31.22           N  
ANISOU 1645  N   ASN A 216     5051   4042   2769  -1128    239   -394       N  
ATOM   1646  CA  ASN A 216      13.900  14.322  48.958  1.00 31.50           C  
ANISOU 1646  CA  ASN A 216     4928   4106   2935  -1045    166   -292       C  
ATOM   1647  C   ASN A 216      12.742  13.984  48.030  1.00 28.52           C  
ANISOU 1647  C   ASN A 216     4504   3644   2688   -867    230   -310       C  
ATOM   1648  O   ASN A 216      11.703  13.493  48.490  1.00 31.30           O  
ANISOU 1648  O   ASN A 216     4846   4000   3047   -805    282   -317       O  
ATOM   1649  CB  ASN A 216      14.454  13.048  49.602  1.00 41.08           C  
ANISOU 1649  CB  ASN A 216     6019   5456   4132  -1092     84   -171       C  
ATOM   1650  CG  ASN A 216      15.618  13.328  50.532  1.00 44.09           C  
ANISOU 1650  CG  ASN A 216     6430   5945   4379  -1279      9   -129       C  
ATOM   1651  OD1 ASN A 216      16.758  13.502  50.089  1.00 44.63           O  
ANISOU 1651  OD1 ASN A 216     6458   6043   4457  -1341    -64    -72       O  
ATOM   1652  ND2 ASN A 216      15.335  13.389  51.823  1.00 40.24           N  
ANISOU 1652  ND2 ASN A 216     6010   5520   3760  -1377     24   -153       N  
ATOM   1653  N   ASP A 217      12.933  14.234  46.729  1.00 27.57           N  
ANISOU 1653  N   ASP A 217     4351   3457   2668   -792    223   -310       N  
ATOM   1654  CA  ASP A 217      11.916  13.912  45.736  1.00 27.53           C  
ANISOU 1654  CA  ASP A 217     4293   3384   2783   -640    270   -316       C  
ATOM   1655  C   ASP A 217      11.526  12.444  45.842  1.00 28.68           C  
ANISOU 1655  C   ASP A 217     4321   3593   2984   -582    243   -240       C  
ATOM   1656  O   ASP A 217      12.382  11.565  45.989  1.00 28.47           O  
ANISOU 1656  O   ASP A 217     4211   3644   2964   -624    170   -157       O  
ATOM   1657  CB  ASP A 217      12.427  14.193  44.316  1.00 27.48           C  
ANISOU 1657  CB  ASP A 217     4249   3326   2865   -589    244   -305       C  
ATOM   1658  CG  ASP A 217      12.664  15.679  44.031  1.00 31.79           C  
ANISOU 1658  CG  ASP A 217     4907   3792   3380   -625    282   -379       C  
ATOM   1659  OD1 ASP A 217      11.924  16.542  44.568  1.00 32.12           O  
ANISOU 1659  OD1 ASP A 217     5058   3772   3374   -628    368   -456       O  
ATOM   1660  OD2 ASP A 217      13.587  15.983  43.227  1.00 28.11           O  
ANISOU 1660  OD2 ASP A 217     4419   3316   2945   -644    234   -357       O  
ATOM   1661  N   ARG A 218      10.228  12.179  45.749  1.00 27.30           N  
ANISOU 1661  N   ARG A 218     4136   3382   2855   -486    305   -259       N  
ATOM   1662  CA  ARG A 218       9.764  10.797  45.701  1.00 27.34           C  
ANISOU 1662  CA  ARG A 218     4031   3431   2926   -427    282   -190       C  
ATOM   1663  C   ARG A 218      10.205  10.145  44.393  1.00 26.40           C  
ANISOU 1663  C   ARG A 218     3823   3294   2913   -370    235   -144       C  
ATOM   1664  O   ARG A 218      10.162  10.761  43.325  1.00 25.42           O  
ANISOU 1664  O   ARG A 218     3717   3106   2836   -325    248   -177       O  
ATOM   1665  CB  ARG A 218       8.240  10.733  45.835  1.00 25.96           C  
ANISOU 1665  CB  ARG A 218     3864   3222   2778   -341    358   -215       C  
ATOM   1666  CG  ARG A 218       7.661   9.311  45.745  1.00 25.05           C  
ANISOU 1666  CG  ARG A 218     3639   3145   2733   -285    336   -146       C  
ATOM   1667  CD  ARG A 218       6.187   9.242  46.194  1.00 25.41           C  
ANISOU 1667  CD  ARG A 218     3690   3180   2784   -222    407   -156       C  
ATOM   1668  NE  ARG A 218       6.008   9.744  47.559  1.00 27.65           N  
ANISOU 1668  NE  ARG A 218     4053   3493   2959   -278    455   -187       N  
ATOM   1669  CZ  ARG A 218       6.350   9.075  48.655  1.00 33.28           C  
ANISOU 1669  CZ  ARG A 218     4746   4290   3608   -346    425   -147       C  
ATOM   1670  NH1 ARG A 218       6.876   7.864  48.562  1.00 36.16           N  
ANISOU 1670  NH1 ARG A 218     5007   4711   4019   -357    351    -67       N  
ATOM   1671  NH2 ARG A 218       6.172   9.621  49.847  1.00 36.13           N  
ANISOU 1671  NH2 ARG A 218     5193   4678   3858   -404    474   -185       N  
ATOM   1672  N   PHE A 219      10.649   8.882  44.481  1.00 23.67           N  
ANISOU 1672  N   PHE A 219     3384   3005   2605   -374    186    -63       N  
ATOM   1673  CA  PHE A 219      11.025   8.093  43.302  1.00 23.85           C  
ANISOU 1673  CA  PHE A 219     3329   3006   2729   -318    157    -20       C  
ATOM   1674  C   PHE A 219      10.752   6.635  43.681  1.00 24.08           C  
ANISOU 1674  C   PHE A 219     3273   3075   2803   -297    145     51       C  
ATOM   1675  O   PHE A 219      11.638   5.911  44.150  1.00 28.25           O  
ANISOU 1675  O   PHE A 219     3743   3659   3330   -339    108    130       O  
ATOM   1676  CB  PHE A 219      12.480   8.326  42.900  1.00 23.97           C  
ANISOU 1676  CB  PHE A 219     3330   3036   2742   -367    108     16       C  
ATOM   1677  CG  PHE A 219      12.821   7.861  41.501  1.00 27.31           C  
ANISOU 1677  CG  PHE A 219     3703   3414   3260   -302    100     36       C  
ATOM   1678  CD1 PHE A 219      11.965   7.037  40.790  1.00 25.52           C  
ANISOU 1678  CD1 PHE A 219     3439   3149   3109   -225    123     32       C  
ATOM   1679  CD2 PHE A 219      14.030   8.239  40.917  1.00 29.21           C  
ANISOU 1679  CD2 PHE A 219     3935   3654   3508   -329     69     61       C  
ATOM   1680  CE1 PHE A 219      12.303   6.593  39.504  1.00 30.43           C  
ANISOU 1680  CE1 PHE A 219     4028   3729   3804   -177    121     43       C  
ATOM   1681  CE2 PHE A 219      14.368   7.809  39.637  1.00 29.32           C  
ANISOU 1681  CE2 PHE A 219     3910   3627   3603   -269     71     78       C  
ATOM   1682  CZ  PHE A 219      13.506   6.986  38.936  1.00 27.76           C  
ANISOU 1682  CZ  PHE A 219     3687   3389   3473   -195     99     65       C  
ATOM   1683  N   ASP A 220       9.493   6.235  43.504  1.00 24.77           N  
ANISOU 1683  N   ASP A 220     3348   3133   2929   -233    181     32       N  
ATOM   1684  CA  ASP A 220       8.997   4.900  43.820  1.00 25.48           C  
ANISOU 1684  CA  ASP A 220     3367   3248   3068   -209    179     90       C  
ATOM   1685  C   ASP A 220       8.735   4.134  42.530  1.00 31.46           C  
ANISOU 1685  C   ASP A 220     4080   3948   3923   -148    179     96       C  
ATOM   1686  O   ASP A 220       8.155   4.679  41.586  1.00 28.45           O  
ANISOU 1686  O   ASP A 220     3728   3517   3563   -108    196     43       O  
ATOM   1687  CB  ASP A 220       7.679   4.953  44.606  1.00 24.65           C  
ANISOU 1687  CB  ASP A 220     3278   3156   2931   -191    219     70       C  
ATOM   1688  CG  ASP A 220       7.837   5.464  46.032  1.00 31.06           C  
ANISOU 1688  CG  ASP A 220     4134   4030   3637   -258    228     67       C  
ATOM   1689  OD1 ASP A 220       8.946   5.374  46.612  1.00 31.07           O  
ANISOU 1689  OD1 ASP A 220     4125   4087   3592   -330    188    108       O  
ATOM   1690  OD2 ASP A 220       6.821   5.949  46.592  1.00 34.41           O  
ANISOU 1690  OD2 ASP A 220     4603   4451   4019   -241    280     29       O  
ATOM   1691  N   VAL A 221       9.112   2.856  42.504  1.00 23.84           N  
ANISOU 1691  N   VAL A 221     3049   2991   3017   -143    165    162       N  
ATOM   1692  CA  VAL A 221       8.745   1.966  41.410  1.00 21.90           C  
ANISOU 1692  CA  VAL A 221     2775   2688   2858    -97    175    163       C  
ATOM   1693  C   VAL A 221       8.017   0.769  42.010  1.00 23.95           C  
ANISOU 1693  C   VAL A 221     2985   2961   3154    -90    184    211       C  
ATOM   1694  O   VAL A 221       8.352   0.320  43.112  1.00 25.14           O  
ANISOU 1694  O   VAL A 221     3099   3166   3287   -117    177    273       O  
ATOM   1695  CB  VAL A 221       9.980   1.520  40.601  1.00 24.57           C  
ANISOU 1695  CB  VAL A 221     3093   2996   3248    -92    167    195       C  
ATOM   1696  CG1 VAL A 221       9.579   0.503  39.530  1.00 24.44           C  
ANISOU 1696  CG1 VAL A 221     3062   2912   3311    -55    189    188       C  
ATOM   1697  CG2 VAL A 221      10.679   2.735  39.968  1.00 25.71           C  
ANISOU 1697  CG2 VAL A 221     3283   3128   3356   -100    156    151       C  
ATOM   1698  N   PHE A 222       6.991   0.284  41.305  1.00 22.53           N  
ANISOU 1698  N   PHE A 222     2801   2739   3020    -60    197    187       N  
ATOM   1699  CA  PHE A 222       6.204  -0.864  41.740  1.00 21.94           C  
ANISOU 1699  CA  PHE A 222     2681   2669   2988    -56    205    230       C  
ATOM   1700  C   PHE A 222       6.116  -1.857  40.598  1.00 28.64           C  
ANISOU 1700  C   PHE A 222     3521   3446   3913    -45    214    226       C  
ATOM   1701  O   PHE A 222       5.789  -1.475  39.473  1.00 25.99           O  
ANISOU 1701  O   PHE A 222     3221   3073   3582    -36    212    170       O  
ATOM   1702  CB  PHE A 222       4.791  -0.453  42.154  1.00 22.58           C  
ANISOU 1702  CB  PHE A 222     2766   2775   3036    -45    215    210       C  
ATOM   1703  CG  PHE A 222       4.754   0.558  43.262  1.00 21.95           C  
ANISOU 1703  CG  PHE A 222     2714   2753   2874    -57    225    201       C  
ATOM   1704  CD1 PHE A 222       4.904   1.910  42.985  1.00 26.74           C  
ANISOU 1704  CD1 PHE A 222     3381   3350   3429    -53    235    142       C  
ATOM   1705  CD2 PHE A 222       4.569   0.160  44.572  1.00 25.67           C  
ANISOU 1705  CD2 PHE A 222     3156   3282   3314    -75    231    250       C  
ATOM   1706  CE1 PHE A 222       4.866   2.852  44.019  1.00 26.91           C  
ANISOU 1706  CE1 PHE A 222     3445   3411   3368    -71    256    123       C  
ATOM   1707  CE2 PHE A 222       4.528   1.084  45.600  1.00 27.19           C  
ANISOU 1707  CE2 PHE A 222     3388   3525   3417    -96    248    233       C  
ATOM   1708  CZ  PHE A 222       4.682   2.431  45.321  1.00 27.25           C  
ANISOU 1708  CZ  PHE A 222     3468   3514   3373    -96    263    165       C  
ATOM   1709  N   PHE A 223       6.400  -3.125  40.882  1.00 26.90           N  
ANISOU 1709  N   PHE A 223     3261   3208   3754    -49    226    285       N  
ATOM   1710  CA  PHE A 223       6.282  -4.182  39.886  1.00 22.07           C  
ANISOU 1710  CA  PHE A 223     2655   2516   3215    -46    248    277       C  
ATOM   1711  C   PHE A 223       5.053  -5.030  40.183  1.00 26.83           C  
ANISOU 1711  C   PHE A 223     3233   3115   3846    -60    249    295       C  
ATOM   1712  O   PHE A 223       4.960  -5.651  41.249  1.00 26.82           O  
ANISOU 1712  O   PHE A 223     3182   3145   3861    -63    254    362       O  
ATOM   1713  CB  PHE A 223       7.531  -5.058  39.851  1.00 21.73           C  
ANISOU 1713  CB  PHE A 223     2590   2431   3235    -36    279    334       C  
ATOM   1714  CG  PHE A 223       8.663  -4.459  39.070  1.00 26.34           C  
ANISOU 1714  CG  PHE A 223     3203   2992   3812    -22    286    312       C  
ATOM   1715  CD1 PHE A 223       8.735  -4.629  37.691  1.00 27.48           C  
ANISOU 1715  CD1 PHE A 223     3398   3060   3982    -15    310    253       C  
ATOM   1716  CD2 PHE A 223       9.655  -3.724  39.705  1.00 26.81           C  
ANISOU 1716  CD2 PHE A 223     3242   3112   3833    -24    268    352       C  
ATOM   1717  CE1 PHE A 223       9.789  -4.081  36.957  1.00 30.76           C  
ANISOU 1717  CE1 PHE A 223     3838   3457   4393      2    321    238       C  
ATOM   1718  CE2 PHE A 223      10.694  -3.168  38.981  1.00 27.23           C  
ANISOU 1718  CE2 PHE A 223     3316   3148   3882    -13    272    340       C  
ATOM   1719  CZ  PHE A 223      10.764  -3.348  37.605  1.00 33.99           C  
ANISOU 1719  CZ  PHE A 223     4218   3925   4772      6    301    285       C  
ATOM   1720  N   LEU A 224       4.129  -5.053  39.228  1.00 23.56           N  
ANISOU 1720  N   LEU A 224     2848   2670   3435    -75    241    244       N  
ATOM   1721  CA  LEU A 224       2.921  -5.861  39.241  1.00 25.48           C  
ANISOU 1721  CA  LEU A 224     3072   2904   3705   -101    236    258       C  
ATOM   1722  C   LEU A 224       2.925  -6.725  37.986  1.00 26.89           C  
ANISOU 1722  C   LEU A 224     3294   2995   3929   -134    251    220       C  
ATOM   1723  O   LEU A 224       3.649  -6.442  37.027  1.00 29.57           O  
ANISOU 1723  O   LEU A 224     3682   3292   4263   -130    263    172       O  
ATOM   1724  CB  LEU A 224       1.661  -4.968  39.270  1.00 23.78           C  
ANISOU 1724  CB  LEU A 224     2849   2750   3438   -102    208    242       C  
ATOM   1725  CG  LEU A 224       1.271  -4.233  40.564  1.00 29.44           C  
ANISOU 1725  CG  LEU A 224     3531   3546   4108    -75    208    276       C  
ATOM   1726  CD1 LEU A 224       2.345  -3.262  41.089  1.00 30.84           C  
ANISOU 1726  CD1 LEU A 224     3730   3750   4236    -53    215    263       C  
ATOM   1727  CD2 LEU A 224      -0.063  -3.494  40.376  1.00 29.75           C  
ANISOU 1727  CD2 LEU A 224     3562   3626   4117    -68    199    270       C  
ATOM   1728  N   SER A 225       2.123  -7.778  37.986  1.00 25.59           N  
ANISOU 1728  N   SER A 225     3119   2800   3805   -172    254    240       N  
ATOM   1729  CA  SER A 225       1.991  -8.566  36.765  1.00 23.90           C  
ANISOU 1729  CA  SER A 225     2963   2500   3617   -222    270    191       C  
ATOM   1730  C   SER A 225       1.579  -7.660  35.609  1.00 25.79           C  
ANISOU 1730  C   SER A 225     3243   2760   3794   -246    236    125       C  
ATOM   1731  O   SER A 225       0.547  -6.996  35.672  1.00 27.81           O  
ANISOU 1731  O   SER A 225     3469   3088   4009   -257    193    134       O  
ATOM   1732  CB  SER A 225       0.963  -9.676  36.959  1.00 28.87           C  
ANISOU 1732  CB  SER A 225     3576   3108   4286   -276    265    221       C  
ATOM   1733  OG  SER A 225       0.941 -10.521  35.818  1.00 35.83           O  
ANISOU 1733  OG  SER A 225     4530   3895   5189   -338    289    167       O  
ATOM   1734  N   GLY A 226       2.416  -7.580  34.583  1.00 32.42           N  
ANISOU 1734  N   GLY A 226     4146   3543   4629   -248    261     70       N  
ATOM   1735  CA  GLY A 226       2.072  -6.782  33.420  1.00 31.00           C  
ANISOU 1735  CA  GLY A 226     4005   3385   4391   -276    229     13       C  
ATOM   1736  C   GLY A 226       2.049  -5.280  33.619  1.00 33.21           C  
ANISOU 1736  C   GLY A 226     4254   3746   4618   -229    198     17       C  
ATOM   1737  O   GLY A 226       1.526  -4.567  32.752  1.00 29.12           O  
ANISOU 1737  O   GLY A 226     3748   3260   4054   -251    167    -11       O  
ATOM   1738  N   ALA A 227       2.595  -4.762  34.722  1.00 28.02           N  
ANISOU 1738  N   ALA A 227     3559   3122   3965   -170    206     52       N  
ATOM   1739  CA  ALA A 227       2.509  -3.325  34.991  1.00 27.90           C  
ANISOU 1739  CA  ALA A 227     3528   3173   3900   -132    186     51       C  
ATOM   1740  C   ALA A 227       3.721  -2.892  35.803  1.00 28.95           C  
ANISOU 1740  C   ALA A 227     3656   3312   4032    -87    205     66       C  
ATOM   1741  O   ALA A 227       3.937  -3.386  36.916  1.00 29.71           O  
ANISOU 1741  O   ALA A 227     3718   3422   4149    -78    216    114       O  
ATOM   1742  CB  ALA A 227       1.215  -2.973  35.736  1.00 28.90           C  
ANISOU 1742  CB  ALA A 227     3604   3367   4009   -128    165     91       C  
ATOM   1743  N   GLN A 228       4.506  -1.965  35.265  1.00 24.11           N  
ANISOU 1743  N   GLN A 228     3073   2697   3392    -68    205     33       N  
ATOM   1744  CA  GLN A 228       5.619  -1.381  36.006  1.00 20.72           C  
ANISOU 1744  CA  GLN A 228     2638   2286   2949    -40    213     51       C  
ATOM   1745  C   GLN A 228       5.311   0.098  36.195  1.00 25.08           C  
ANISOU 1745  C   GLN A 228     3200   2884   3444    -23    197     29       C  
ATOM   1746  O   GLN A 228       5.269   0.855  35.216  1.00 27.94           O  
ANISOU 1746  O   GLN A 228     3590   3237   3788    -18    190     -9       O  
ATOM   1747  CB  GLN A 228       6.939  -1.592  35.272  1.00 25.30           C  
ANISOU 1747  CB  GLN A 228     3244   2817   3553    -32    233     42       C  
ATOM   1748  CG  GLN A 228       8.066  -0.789  35.891  1.00 30.43           C  
ANISOU 1748  CG  GLN A 228     3885   3498   4179    -15    229     65       C  
ATOM   1749  CD  GLN A 228       9.353  -0.830  35.082  1.00 32.34           C  
ANISOU 1749  CD  GLN A 228     4144   3699   4443     -2    250     66       C  
ATOM   1750  OE1 GLN A 228      10.183   0.060  35.204  1.00 31.89           O  
ANISOU 1750  OE1 GLN A 228     4089   3668   4358      3    238     73       O  
ATOM   1751  NE2 GLN A 228       9.528  -1.871  34.260  1.00 30.71           N  
ANISOU 1751  NE2 GLN A 228     3955   3427   4288      0    287     59       N  
ATOM   1752  N   ILE A 229       5.087   0.507  37.443  1.00 24.34           N  
ANISOU 1752  N   ILE A 229     3088   2837   3322    -16    199     54       N  
ATOM   1753  CA  ILE A 229       4.596   1.844  37.757  1.00 22.24           C  
ANISOU 1753  CA  ILE A 229     2841   2603   3005      1    203     33       C  
ATOM   1754  C   ILE A 229       5.695   2.630  38.447  1.00 26.90           C  
ANISOU 1754  C   ILE A 229     3458   3210   3555     -5    206     28       C  
ATOM   1755  O   ILE A 229       6.310   2.144  39.401  1.00 27.55           O  
ANISOU 1755  O   ILE A 229     3521   3317   3631    -24    202     65       O  
ATOM   1756  CB  ILE A 229       3.340   1.794  38.641  1.00 25.15           C  
ANISOU 1756  CB  ILE A 229     3182   3010   3363     10    216     60       C  
ATOM   1757  CG1 ILE A 229       2.212   1.078  37.904  1.00 26.89           C  
ANISOU 1757  CG1 ILE A 229     3372   3224   3622      3    205     75       C  
ATOM   1758  CG2 ILE A 229       2.904   3.208  39.031  1.00 20.78           C  
ANISOU 1758  CG2 ILE A 229     2658   2476   2761     36    242     40       C  
ATOM   1759  CD1 ILE A 229       1.698  -0.139  38.627  1.00 34.80           C  
ANISOU 1759  CD1 ILE A 229     4331   4238   4653    -14    203    122       C  
ATOM   1760  N   ALA A 230       5.926   3.850  37.977  1.00 24.88           N  
ANISOU 1760  N   ALA A 230     3240   2943   3268      5    209    -11       N  
ATOM   1761  CA  ALA A 230       6.853   4.766  38.620  1.00 25.28           C  
ANISOU 1761  CA  ALA A 230     3327   3009   3270    -14    210    -22       C  
ATOM   1762  C   ALA A 230       6.082   5.985  39.103  1.00 31.79           C  
ANISOU 1762  C   ALA A 230     4193   3839   4048      0    242    -54       C  
ATOM   1763  O   ALA A 230       5.170   6.464  38.423  1.00 27.73           O  
ANISOU 1763  O   ALA A 230     3680   3304   3550     36    261    -69       O  
ATOM   1764  CB  ALA A 230       7.975   5.193  37.670  1.00 27.04           C  
ANISOU 1764  CB  ALA A 230     3569   3203   3500    -18    194    -39       C  
ATOM   1765  N   LEU A 231       6.439   6.470  40.288  1.00 26.43           N  
ANISOU 1765  N   LEU A 231     3545   3186   3309    -31    254    -58       N  
ATOM   1766  CA  LEU A 231       5.774   7.608  40.900  1.00 28.81           C  
ANISOU 1766  CA  LEU A 231     3903   3483   3562    -21    303    -93       C  
ATOM   1767  C   LEU A 231       6.855   8.563  41.385  1.00 27.81           C  
ANISOU 1767  C   LEU A 231     3843   3355   3370    -75    301   -125       C  
ATOM   1768  O   LEU A 231       7.713   8.181  42.193  1.00 27.68           O  
ANISOU 1768  O   LEU A 231     3822   3383   3314   -134    270   -101       O  
ATOM   1769  CB  LEU A 231       4.872   7.148  42.047  1.00 27.10           C  
ANISOU 1769  CB  LEU A 231     3671   3303   3323    -18    332    -69       C  
ATOM   1770  CG  LEU A 231       4.131   8.211  42.827  1.00 33.19           C  
ANISOU 1770  CG  LEU A 231     4505   4065   4040     -3    402   -102       C  
ATOM   1771  CD1 LEU A 231       3.347   9.120  41.880  1.00 37.68           C  
ANISOU 1771  CD1 LEU A 231     5088   4581   4648     60    446   -121       C  
ATOM   1772  CD2 LEU A 231       3.207   7.551  43.862  1.00 34.49           C  
ANISOU 1772  CD2 LEU A 231     4639   4273   4191      7    430    -66       C  
ATOM   1773  N   GLN A 232       6.834   9.791  40.878  1.00 24.61           N  
ANISOU 1773  N   GLN A 232     3493   2901   2954    -60    330   -170       N  
ATOM   1774  CA  GLN A 232       7.891  10.741  41.182  1.00 24.18           C  
ANISOU 1774  CA  GLN A 232     3508   2838   2842   -120    324   -203       C  
ATOM   1775  C   GLN A 232       7.302  12.091  41.558  1.00 26.23           C  
ANISOU 1775  C   GLN A 232     3858   3048   3061   -111    399   -260       C  
ATOM   1776  O   GLN A 232       6.195  12.447  41.140  1.00 29.07           O  
ANISOU 1776  O   GLN A 232     4214   3370   3460    -39    455   -265       O  
ATOM   1777  CB  GLN A 232       8.851  10.904  39.996  1.00 28.69           C  
ANISOU 1777  CB  GLN A 232     4062   3387   3453   -121    281   -198       C  
ATOM   1778  CG  GLN A 232       9.724   9.669  39.784  1.00 27.25           C  
ANISOU 1778  CG  GLN A 232     3808   3246   3302   -141    222   -142       C  
ATOM   1779  CD  GLN A 232      10.618   9.790  38.577  1.00 33.18           C  
ANISOU 1779  CD  GLN A 232     4542   3973   4092   -132    193   -134       C  
ATOM   1780  OE1 GLN A 232      11.777  10.192  38.688  1.00 37.58           O  
ANISOU 1780  OE1 GLN A 232     5114   4544   4623   -183    164   -122       O  
ATOM   1781  NE2 GLN A 232      10.085   9.449  37.414  1.00 31.55           N  
ANISOU 1781  NE2 GLN A 232     4305   3737   3946    -74    198   -136       N  
ATOM   1782  N   SER A 233       8.056  12.832  42.366  1.00 24.76           N  
ANISOU 1782  N   SER A 233     3751   2862   2793   -189    405   -296       N  
ATOM   1783  CA  SER A 233       7.748  14.225  42.639  1.00 23.55           C  
ANISOU 1783  CA  SER A 233     3706   2642   2599   -193    484   -360       C  
ATOM   1784  C   SER A 233       8.954  15.080  42.268  1.00 29.12           C  
ANISOU 1784  C   SER A 233     4464   3320   3278   -259    452   -388       C  
ATOM   1785  O   SER A 233      10.063  14.577  42.058  1.00 25.90           O  
ANISOU 1785  O   SER A 233     4012   2961   2868   -312    369   -352       O  
ATOM   1786  CB  SER A 233       7.363  14.438  44.120  1.00 26.56           C  
ANISOU 1786  CB  SER A 233     4165   3040   2888   -241    540   -394       C  
ATOM   1787  OG  SER A 233       8.495  14.428  44.961  1.00 25.92           O  
ANISOU 1787  OG  SER A 233     4124   3011   2713   -363    488   -402       O  
ATOM   1788  N   CYS A 234       8.732  16.385  42.152  1.00 27.43           N  
ANISOU 1788  N   CYS A 234     4343   3025   3053   -251    524   -444       N  
ATOM   1789  CA  CYS A 234       9.843  17.300  41.927  1.00 26.45           C  
ANISOU 1789  CA  CYS A 234     4284   2870   2897   -327    500   -474       C  
ATOM   1790  C   CYS A 234       9.459  18.680  42.439  1.00 30.39           C  
ANISOU 1790  C   CYS A 234     4921   3276   3349   -345    604   -551       C  
ATOM   1791  O   CYS A 234       8.281  18.976  42.656  1.00 28.97           O  
ANISOU 1791  O   CYS A 234     4772   3047   3190   -269    703   -570       O  
ATOM   1792  CB  CYS A 234      10.260  17.348  40.451  1.00 29.55           C  
ANISOU 1792  CB  CYS A 234     4609   3244   3376   -276    456   -441       C  
ATOM   1793  SG  CYS A 234       8.935  17.680  39.247  1.00 29.72           S  
ANISOU 1793  SG  CYS A 234     4589   3200   3504   -133    524   -427       S  
ATOM   1794  N   ASN A 235      10.482  19.512  42.644  1.00 25.56           N  
ANISOU 1794  N   ASN A 235     4395   2641   2676   -449    586   -591       N  
ATOM   1795  CA  ASN A 235      10.330  20.878  43.141  1.00 28.58           C  
ANISOU 1795  CA  ASN A 235     4930   2922   3005   -491    686   -674       C  
ATOM   1796  C   ASN A 235       9.528  20.892  44.445  1.00 30.39           C  
ANISOU 1796  C   ASN A 235     5245   3146   3155   -509    773   -722       C  
ATOM   1797  O   ASN A 235       8.470  21.519  44.562  1.00 31.04           O  
ANISOU 1797  O   ASN A 235     5391   3141   3263   -429    902   -757       O  
ATOM   1798  CB  ASN A 235       9.691  21.768  42.074  1.00 27.91           C  
ANISOU 1798  CB  ASN A 235     4853   2729   3021   -380    767   -679       C  
ATOM   1799  CG  ASN A 235       9.760  23.235  42.418  1.00 32.48           C  
ANISOU 1799  CG  ASN A 235     5592   3188   3560   -427    868   -760       C  
ATOM   1800  OD1 ASN A 235      10.160  23.616  43.514  1.00 34.18           O  
ANISOU 1800  OD1 ASN A 235     5929   3395   3662   -547    890   -825       O  
ATOM   1801  ND2 ASN A 235       9.354  24.075  41.475  1.00 37.72           N  
ANISOU 1801  ND2 ASN A 235     6260   3757   4316   -338    936   -753       N  
ATOM   1802  N   LYS A 236      10.061  20.169  45.434  1.00 30.78           N  
ANISOU 1802  N   LYS A 236     5290   3295   3108   -613    706   -713       N  
ATOM   1803  CA  LYS A 236       9.520  20.156  46.795  1.00 29.78           C  
ANISOU 1803  CA  LYS A 236     5254   3183   2879   -661    775   -759       C  
ATOM   1804  C   LYS A 236       8.027  19.830  46.818  1.00 32.93           C  
ANISOU 1804  C   LYS A 236     5615   3553   3343   -517    873   -745       C  
ATOM   1805  O   LYS A 236       7.242  20.446  47.538  1.00 31.69           O  
ANISOU 1805  O   LYS A 236     5567   3330   3143   -501   1000   -804       O  
ATOM   1806  CB  LYS A 236       9.811  21.477  47.501  1.00 32.52           C  
ANISOU 1806  CB  LYS A 236     5791   3444   3119   -771    856   -863       C  
ATOM   1807  CG  LYS A 236      11.288  21.706  47.781  1.00 37.08           C  
ANISOU 1807  CG  LYS A 236     6410   4077   3600   -950    749   -870       C  
ATOM   1808  CD  LYS A 236      11.511  23.059  48.465  1.00 44.50           C  
ANISOU 1808  CD  LYS A 236     7558   4920   4430  -1072    837   -984       C  
ATOM   1809  CE  LYS A 236      12.981  23.326  48.755  1.00 55.22           C  
ANISOU 1809  CE  LYS A 236     8958   6342   5684  -1269    722   -984       C  
ATOM   1810  NZ  LYS A 236      13.489  22.461  49.853  1.00 58.09           N  
ANISOU 1810  NZ  LYS A 236     9291   6859   5922  -1399    630   -944       N  
ATOM   1811  N   GLY A 237       7.631  18.841  46.022  1.00 31.08           N  
ANISOU 1811  N   GLY A 237     5227   3367   3213   -415    817   -664       N  
ATOM   1812  CA  GLY A 237       6.260  18.390  46.023  1.00 35.10           C  
ANISOU 1812  CA  GLY A 237     5680   3871   3785   -291    889   -631       C  
ATOM   1813  C   GLY A 237       5.299  19.268  45.262  1.00 34.69           C  
ANISOU 1813  C   GLY A 237     5646   3710   3824   -169   1001   -635       C  
ATOM   1814  O   GLY A 237       4.083  19.073  45.372  1.00 34.43           O  
ANISOU 1814  O   GLY A 237     5578   3667   3837    -69   1080   -603       O  
ATOM   1815  N   LYS A 238       5.795  20.230  44.489  1.00 30.82           N  
ANISOU 1815  N   LYS A 238     5201   3143   3367   -173   1012   -661       N  
ATOM   1816  CA  LYS A 238       4.893  21.042  43.688  1.00 32.33           C  
ANISOU 1816  CA  LYS A 238     5390   3237   3657    -51   1116   -645       C  
ATOM   1817  C   LYS A 238       4.343  20.279  42.496  1.00 31.23           C  
ANISOU 1817  C   LYS A 238     5088   3147   3632     52   1056   -550       C  
ATOM   1818  O   LYS A 238       3.254  20.609  42.015  1.00 33.64           O  
ANISOU 1818  O   LYS A 238     5355   3408   4018    165   1141   -505       O  
ATOM   1819  CB  LYS A 238       5.599  22.316  43.221  1.00 36.24           C  
ANISOU 1819  CB  LYS A 238     5982   3633   4155    -89   1148   -695       C  
ATOM   1820  CG  LYS A 238       5.836  23.304  44.371  1.00 38.70           C  
ANISOU 1820  CG  LYS A 238     6483   3862   4358   -181   1250   -798       C  
ATOM   1821  CD  LYS A 238       6.443  24.609  43.895  1.00 47.19           C  
ANISOU 1821  CD  LYS A 238     7660   4824   5446   -217   1293   -848       C  
ATOM   1822  CE  LYS A 238       7.088  25.359  45.054  1.00 51.35           C  
ANISOU 1822  CE  LYS A 238     8377   5298   5834   -367   1342   -958       C  
ATOM   1823  NZ  LYS A 238       8.294  24.633  45.562  1.00 46.52           N  
ANISOU 1823  NZ  LYS A 238     7748   4811   5115   -523   1186   -963       N  
ATOM   1824  N   VAL A 239       5.058  19.262  42.027  1.00 25.25           N  
ANISOU 1824  N   VAL A 239     4235   2479   2881     13    918   -514       N  
ATOM   1825  CA  VAL A 239       4.664  18.490  40.856  1.00 24.84           C  
ANISOU 1825  CA  VAL A 239     4043   2474   2923     88    854   -437       C  
ATOM   1826  C   VAL A 239       4.819  17.014  41.176  1.00 27.67           C  
ANISOU 1826  C   VAL A 239     4318   2935   3263     56    760   -402       C  
ATOM   1827  O   VAL A 239       5.834  16.601  41.748  1.00 29.36           O  
ANISOU 1827  O   VAL A 239     4552   3194   3411    -37    693   -423       O  
ATOM   1828  CB  VAL A 239       5.506  18.873  39.620  1.00 28.50           C  
ANISOU 1828  CB  VAL A 239     4482   2918   3429     80    792   -428       C  
ATOM   1829  CG1 VAL A 239       5.252  17.909  38.455  1.00 28.26           C  
ANISOU 1829  CG1 VAL A 239     4317   2949   3472    131    713   -358       C  
ATOM   1830  CG2 VAL A 239       5.205  20.306  39.206  1.00 29.33           C  
ANISOU 1830  CG2 VAL A 239     4654   2918   3571    126    893   -446       C  
ATOM   1831  N   PHE A 240       3.815  16.219  40.808  1.00 26.11           N  
ANISOU 1831  N   PHE A 240     4021   2774   3125    129    756   -340       N  
ATOM   1832  CA  PHE A 240       3.892  14.765  40.860  1.00 25.49           C  
ANISOU 1832  CA  PHE A 240     3853   2780   3052    110    668   -299       C  
ATOM   1833  C   PHE A 240       3.615  14.204  39.476  1.00 27.57           C  
ANISOU 1833  C   PHE A 240     4016   3063   3397    158    613   -245       C  
ATOM   1834  O   PHE A 240       2.705  14.665  38.779  1.00 28.37           O  
ANISOU 1834  O   PHE A 240     4086   3139   3553    228    658   -212       O  
ATOM   1835  CB  PHE A 240       2.887  14.174  41.853  1.00 24.82           C  
ANISOU 1835  CB  PHE A 240     3749   2731   2950    134    713   -275       C  
ATOM   1836  CG  PHE A 240       3.206  14.472  43.283  1.00 31.39           C  
ANISOU 1836  CG  PHE A 240     4677   3565   3685     70    755   -327       C  
ATOM   1837  CD1 PHE A 240       2.922  15.718  43.831  1.00 30.69           C  
ANISOU 1837  CD1 PHE A 240     4702   3403   3556     78    867   -380       C  
ATOM   1838  CD2 PHE A 240       3.784  13.508  44.091  1.00 29.62           C  
ANISOU 1838  CD2 PHE A 240     4433   3415   3406     -2    689   -318       C  
ATOM   1839  CE1 PHE A 240       3.220  15.999  45.155  1.00 32.31           C  
ANISOU 1839  CE1 PHE A 240     5009   3611   3655      4    909   -436       C  
ATOM   1840  CE2 PHE A 240       4.068  13.782  45.420  1.00 26.97           C  
ANISOU 1840  CE2 PHE A 240     4185   3096   2967    -73    723   -360       C  
ATOM   1841  CZ  PHE A 240       3.795  15.024  45.948  1.00 30.43           C  
ANISOU 1841  CZ  PHE A 240     4745   3463   3352    -76    831   -425       C  
ATOM   1842  N   SER A 241       4.399  13.204  39.080  1.00 23.13           N  
ANISOU 1842  N   SER A 241     3402   2546   2840    116    520   -232       N  
ATOM   1843  CA  SER A 241       4.187  12.564  37.794  1.00 27.73           C  
ANISOU 1843  CA  SER A 241     3903   3146   3486    146    469   -191       C  
ATOM   1844  C   SER A 241       4.280  11.059  37.977  1.00 28.91           C  
ANISOU 1844  C   SER A 241     3992   3351   3643    119    409   -163       C  
ATOM   1845  O   SER A 241       4.814  10.565  38.972  1.00 27.35           O  
ANISOU 1845  O   SER A 241     3808   3178   3404     75    394   -170       O  
ATOM   1846  CB  SER A 241       5.203  13.052  36.751  1.00 30.34           C  
ANISOU 1846  CB  SER A 241     4247   3453   3829    129    431   -208       C  
ATOM   1847  OG  SER A 241       6.517  12.730  37.169  1.00 32.05           O  
ANISOU 1847  OG  SER A 241     4486   3685   4007     63    383   -229       O  
ATOM   1848  N   TRP A 242       3.765  10.328  36.993  1.00 23.91           N  
ANISOU 1848  N   TRP A 242     3292   2734   3060    141    376   -128       N  
ATOM   1849  CA  TRP A 242       3.768   8.879  37.079  1.00 24.04           C  
ANISOU 1849  CA  TRP A 242     3257   2786   3091    117    330   -103       C  
ATOM   1850  C   TRP A 242       3.797   8.303  35.675  1.00 26.50           C  
ANISOU 1850  C   TRP A 242     3529   3097   3444    116    286    -91       C  
ATOM   1851  O   TRP A 242       3.417   8.962  34.702  1.00 24.35           O  
ANISOU 1851  O   TRP A 242     3251   2814   3187    140    292    -86       O  
ATOM   1852  CB  TRP A 242       2.539   8.366  37.852  1.00 21.91           C  
ANISOU 1852  CB  TRP A 242     2952   2546   2828    137    356    -66       C  
ATOM   1853  CG  TRP A 242       1.238   8.763  37.192  1.00 23.84           C  
ANISOU 1853  CG  TRP A 242     3157   2793   3106    185    384    -29       C  
ATOM   1854  CD1 TRP A 242       0.519   9.904  37.409  1.00 26.89           C  
ANISOU 1854  CD1 TRP A 242     3563   3161   3493    235    454    -19       C  
ATOM   1855  CD2 TRP A 242       0.530   8.022  36.198  1.00 24.15           C  
ANISOU 1855  CD2 TRP A 242     3132   2859   3186    183    345     13       C  
ATOM   1856  NE1 TRP A 242      -0.598   9.920  36.607  1.00 25.05           N  
ANISOU 1856  NE1 TRP A 242     3266   2950   3304    271    458     42       N  
ATOM   1857  CE2 TRP A 242      -0.613   8.774  35.849  1.00 24.36           C  
ANISOU 1857  CE2 TRP A 242     3127   2895   3235    230    384     61       C  
ATOM   1858  CE3 TRP A 242       0.759   6.797  35.556  1.00 24.55           C  
ANISOU 1858  CE3 TRP A 242     3153   2922   3255    139    285     17       C  
ATOM   1859  CZ2 TRP A 242      -1.530   8.344  34.886  1.00 25.89           C  
ANISOU 1859  CZ2 TRP A 242     3251   3126   3460    225    352    119       C  
ATOM   1860  CZ3 TRP A 242      -0.169   6.362  34.599  1.00 26.68           C  
ANISOU 1860  CZ3 TRP A 242     3370   3218   3549    129    257     58       C  
ATOM   1861  CH2 TRP A 242      -1.298   7.137  34.281  1.00 27.24           C  
ANISOU 1861  CH2 TRP A 242     3401   3313   3634    167    284    112       C  
ATOM   1862  N   PHE A 243       4.270   7.061  35.570  1.00 23.46           N  
ANISOU 1862  N   PHE A 243     3119   2720   3073     85    248    -83       N  
ATOM   1863  CA  PHE A 243       4.047   6.306  34.348  1.00 22.08           C  
ANISOU 1863  CA  PHE A 243     2916   2543   2930     75    218    -75       C  
ATOM   1864  C   PHE A 243       3.804   4.848  34.694  1.00 26.33           C  
ANISOU 1864  C   PHE A 243     3423   3091   3490     50    202    -54       C  
ATOM   1865  O   PHE A 243       4.070   4.396  35.807  1.00 25.68           O  
ANISOU 1865  O   PHE A 243     3336   3019   3403     42    209    -40       O  
ATOM   1866  CB  PHE A 243       5.195   6.457  33.316  1.00 25.52           C  
ANISOU 1866  CB  PHE A 243     3376   2952   3367     64    199   -102       C  
ATOM   1867  CG  PHE A 243       6.541   5.935  33.765  1.00 28.36           C  
ANISOU 1867  CG  PHE A 243     3750   3299   3727     44    191   -106       C  
ATOM   1868  CD1 PHE A 243       6.821   4.577  33.777  1.00 32.21           C  
ANISOU 1868  CD1 PHE A 243     4218   3778   4244     26    184    -90       C  
ATOM   1869  CD2 PHE A 243       7.559   6.827  34.079  1.00 31.71           C  
ANISOU 1869  CD2 PHE A 243     4204   3717   4127     41    194   -118       C  
ATOM   1870  CE1 PHE A 243       8.072   4.116  34.154  1.00 34.51           C  
ANISOU 1870  CE1 PHE A 243     4508   4060   4545     16    185    -73       C  
ATOM   1871  CE2 PHE A 243       8.807   6.372  34.450  1.00 34.58           C  
ANISOU 1871  CE2 PHE A 243     4565   4080   4492     19    183   -101       C  
ATOM   1872  CZ  PHE A 243       9.065   5.016  34.478  1.00 34.24           C  
ANISOU 1872  CZ  PHE A 243     4492   4034   4485     12    181    -73       C  
ATOM   1873  N   CYS A 244       3.251   4.127  33.728  1.00 24.87           N  
ANISOU 1873  N   CYS A 244     3218   2904   3326     30    181    -47       N  
ATOM   1874  CA  CYS A 244       2.922   2.721  33.923  1.00 23.41           C  
ANISOU 1874  CA  CYS A 244     3010   2717   3167     -1    170    -29       C  
ATOM   1875  C   CYS A 244       3.180   1.995  32.614  1.00 23.38           C  
ANISOU 1875  C   CYS A 244     3026   2683   3176    -38    153    -53       C  
ATOM   1876  O   CYS A 244       2.436   2.175  31.646  1.00 26.07           O  
ANISOU 1876  O   CYS A 244     3360   3040   3504    -59    134    -54       O  
ATOM   1877  CB  CYS A 244       1.472   2.547  34.370  1.00 25.94           C  
ANISOU 1877  CB  CYS A 244     3286   3076   3492     -1    169     14       C  
ATOM   1878  SG  CYS A 244       0.953   0.794  34.438  1.00 29.10           S  
ANISOU 1878  SG  CYS A 244     3660   3470   3929    -53    151     38       S  
ATOM   1879  N   ILE A 245       4.231   1.186  32.589  1.00 22.57           N  
ANISOU 1879  N   ILE A 245     2945   2537   3094    -48    166    -68       N  
ATOM   1880  CA  ILE A 245       4.555   0.384  31.418  1.00 22.99           C  
ANISOU 1880  CA  ILE A 245     3032   2546   3159    -83    169    -98       C  
ATOM   1881  C   ILE A 245       3.678  -0.857  31.427  1.00 26.13           C  
ANISOU 1881  C   ILE A 245     3420   2930   3577   -129    164    -87       C  
ATOM   1882  O   ILE A 245       3.561  -1.535  32.455  1.00 26.75           O  
ANISOU 1882  O   ILE A 245     3472   3005   3685   -125    174    -54       O  
ATOM   1883  CB  ILE A 245       6.037  -0.001  31.419  1.00 24.55           C  
ANISOU 1883  CB  ILE A 245     3254   2693   3380    -65    200   -105       C  
ATOM   1884  CG1 ILE A 245       6.914   1.245  31.316  1.00 31.07           C  
ANISOU 1884  CG1 ILE A 245     4089   3535   4183    -31    198   -113       C  
ATOM   1885  CG2 ILE A 245       6.346  -0.941  30.267  1.00 26.59           C  
ANISOU 1885  CG2 ILE A 245     3558   2892   3653    -96    225   -139       C  
ATOM   1886  CD1 ILE A 245       7.884   1.279  32.404  1.00 51.75           C  
ANISOU 1886  CD1 ILE A 245     6690   6158   6815     -9    210    -78       C  
ATOM   1887  N   HIS A 246       3.073  -1.169  30.280  1.00 23.17           N  
ANISOU 1887  N   HIS A 246     3069   2552   3182   -183    147   -111       N  
ATOM   1888  CA  HIS A 246       2.142  -2.288  30.186  1.00 22.90           C  
ANISOU 1888  CA  HIS A 246     3032   2509   3159   -247    135   -103       C  
ATOM   1889  C   HIS A 246       2.134  -2.820  28.757  1.00 24.53           C  
ANISOU 1889  C   HIS A 246     3300   2681   3337   -319    133   -153       C  
ATOM   1890  O   HIS A 246       2.522  -2.128  27.811  1.00 25.11           O  
ANISOU 1890  O   HIS A 246     3402   2765   3374   -318    128   -183       O  
ATOM   1891  CB  HIS A 246       0.730  -1.854  30.604  1.00 22.88           C  
ANISOU 1891  CB  HIS A 246     2967   2584   3143   -256     95    -50       C  
ATOM   1892  CG  HIS A 246       0.111  -0.862  29.668  1.00 28.63           C  
ANISOU 1892  CG  HIS A 246     3681   3370   3827   -270     62    -43       C  
ATOM   1893  ND1 HIS A 246      -0.921  -1.187  28.814  1.00 28.46           N  
ANISOU 1893  ND1 HIS A 246     3649   3387   3777   -349     21    -26       N  
ATOM   1894  CD2 HIS A 246       0.391   0.445  29.443  1.00 27.39           C  
ANISOU 1894  CD2 HIS A 246     3516   3240   3649   -219     64    -42       C  
ATOM   1895  CE1 HIS A 246      -1.252  -0.123  28.103  1.00 28.81           C  
ANISOU 1895  CE1 HIS A 246     3671   3488   3787   -342     -2     -6       C  
ATOM   1896  NE2 HIS A 246      -0.470   0.879  28.463  1.00 26.52           N  
ANISOU 1896  NE2 HIS A 246     3385   3186   3506   -259     27    -17       N  
ATOM   1897  N   GLN A 247       1.698  -4.065  28.602  1.00 24.14           N  
ANISOU 1897  N   GLN A 247     3278   2590   3302   -387    139   -164       N  
ATOM   1898  CA  GLN A 247       1.583  -4.628  27.265  1.00 23.31           C  
ANISOU 1898  CA  GLN A 247     3247   2453   3156   -476    139   -220       C  
ATOM   1899  C   GLN A 247       0.414  -3.995  26.528  1.00 28.40           C  
ANISOU 1899  C   GLN A 247     3862   3191   3737   -540     69   -199       C  
ATOM   1900  O   GLN A 247      -0.660  -3.777  27.099  1.00 28.65           O  
ANISOU 1900  O   GLN A 247     3821   3293   3773   -547     26   -135       O  
ATOM   1901  CB  GLN A 247       1.384  -6.138  27.326  1.00 28.11           C  
ANISOU 1901  CB  GLN A 247     3903   2982   3795   -544    170   -240       C  
ATOM   1902  CG  GLN A 247       2.556  -6.909  27.884  1.00 38.79           C  
ANISOU 1902  CG  GLN A 247     5286   4233   5219   -485    251   -250       C  
ATOM   1903  CD  GLN A 247       2.320  -8.396  27.816  1.00 47.70           C  
ANISOU 1903  CD  GLN A 247     6472   5270   6382   -556    292   -272       C  
ATOM   1904  OE1 GLN A 247       1.350  -8.847  27.209  1.00 49.84           O  
ANISOU 1904  OE1 GLN A 247     6776   5551   6612   -663    257   -294       O  
ATOM   1905  NE2 GLN A 247       3.198  -9.168  28.438  1.00 50.90           N  
ANISOU 1905  NE2 GLN A 247     6887   5586   6864   -501    368   -257       N  
ATOM   1906  N   ASP A 248       0.630  -3.693  25.253  1.00 25.76           N  
ANISOU 1906  N   ASP A 248     3579   2865   3344   -586     61   -242       N  
ATOM   1907  CA  ASP A 248      -0.435  -3.121  24.437  1.00 32.31           C  
ANISOU 1907  CA  ASP A 248     4376   3793   4108   -657     -8   -210       C  
ATOM   1908  C   ASP A 248      -0.087  -3.406  22.993  1.00 33.55           C  
ANISOU 1908  C   ASP A 248     4623   3929   4195   -744     -4   -279       C  
ATOM   1909  O   ASP A 248       0.950  -2.948  22.507  1.00 35.10           O  
ANISOU 1909  O   ASP A 248     4861   4094   4382   -695     34   -320       O  
ATOM   1910  CB  ASP A 248      -0.571  -1.623  24.673  1.00 28.67           C  
ANISOU 1910  CB  ASP A 248     3835   3411   3648   -572    -31   -151       C  
ATOM   1911  CG  ASP A 248      -1.966  -1.096  24.351  1.00 35.77           C  
ANISOU 1911  CG  ASP A 248     4656   4423   4513   -623    -99    -70       C  
ATOM   1912  OD1 ASP A 248      -2.613  -1.592  23.390  1.00 34.78           O  
ANISOU 1912  OD1 ASP A 248     4550   4337   4329   -743   -143    -70       O  
ATOM   1913  OD2 ASP A 248      -2.413  -0.176  25.075  1.00 34.90           O  
ANISOU 1913  OD2 ASP A 248     4464   4364   4433   -544   -103      0       O  
ATOM   1914  N   THR A 249      -0.934  -4.168  22.320  1.00 34.99           N  
ANISOU 1914  N   THR A 249     4840   4132   4324   -879    -40   -290       N  
ATOM   1915  CA  THR A 249      -0.714  -4.511  20.927  1.00 39.77           C  
ANISOU 1915  CA  THR A 249     5545   4722   4844   -986    -37   -361       C  
ATOM   1916  C   THR A 249      -1.584  -3.697  19.983  1.00 43.55           C  
ANISOU 1916  C   THR A 249     5975   5336   5236  -1064   -121   -309       C  
ATOM   1917  O   THR A 249      -1.581  -3.958  18.777  1.00 39.15           O  
ANISOU 1917  O   THR A 249     5495   4791   4589  -1176   -133   -359       O  
ATOM   1918  CB  THR A 249      -0.956  -6.004  20.716  1.00 44.21           C  
ANISOU 1918  CB  THR A 249     6203   5203   5391  -1107    -12   -422       C  
ATOM   1919  OG1 THR A 249      -2.277  -6.335  21.152  1.00 42.79           O  
ANISOU 1919  OG1 THR A 249     5957   5091   5211  -1184    -83   -353       O  
ATOM   1920  CG2 THR A 249       0.056  -6.815  21.521  1.00 54.03           C  
ANISOU 1920  CG2 THR A 249     7498   6305   6727  -1022     87   -466       C  
ATOM   1921  N   ARG A 250      -2.338  -2.733  20.502  1.00 34.55           N  
ANISOU 1921  N   ARG A 250     4710   4297   4121  -1008   -173   -205       N  
ATOM   1922  CA  ARG A 250      -3.129  -1.871  19.640  1.00 31.74           C  
ANISOU 1922  CA  ARG A 250     4290   4073   3698  -1065   -246   -132       C  
ATOM   1923  C   ARG A 250      -2.217  -0.994  18.793  1.00 37.96           C  
ANISOU 1923  C   ARG A 250     5108   4865   4450  -1019   -225   -166       C  
ATOM   1924  O   ARG A 250      -1.063  -0.732  19.133  1.00 35.41           O  
ANISOU 1924  O   ARG A 250     4821   4459   4174   -909   -159   -217       O  
ATOM   1925  CB  ARG A 250      -4.078  -0.995  20.461  1.00 29.37           C  
ANISOU 1925  CB  ARG A 250     3845   3864   3449   -992   -284     -3       C  
ATOM   1926  CG  ARG A 250      -5.210  -1.775  21.116  1.00 37.84           C  
ANISOU 1926  CG  ARG A 250     4868   4967   4544  -1056   -322     57       C  
ATOM   1927  CD  ARG A 250      -6.036  -0.903  22.044  1.00 38.16           C  
ANISOU 1927  CD  ARG A 250     4771   5081   4646   -959   -334    183       C  
ATOM   1928  NE  ARG A 250      -5.286  -0.502  23.231  1.00 36.04           N  
ANISOU 1928  NE  ARG A 250     4500   4735   4459   -804   -264    157       N  
ATOM   1929  CZ  ARG A 250      -5.807   0.186  24.247  1.00 36.42           C  
ANISOU 1929  CZ  ARG A 250     4456   4815   4567   -704   -248    241       C  
ATOM   1930  NH1 ARG A 250      -7.089   0.554  24.221  1.00 37.16           N  
ANISOU 1930  NH1 ARG A 250     4443   5015   4659   -728   -291    365       N  
ATOM   1931  NH2 ARG A 250      -5.052   0.511  25.285  1.00 37.69           N  
ANISOU 1931  NH2 ARG A 250     4632   4906   4785   -583   -185    206       N  
ATOM   1932  N   ASN A 251      -2.761  -0.534  17.670  1.00 37.81           N  
ANISOU 1932  N   ASN A 251     5068   4952   4344  -1110   -285   -124       N  
ATOM   1933  CA  ASN A 251      -2.021   0.313  16.740  1.00 42.51           C  
ANISOU 1933  CA  ASN A 251     5685   5570   4897  -1081   -273   -144       C  
ATOM   1934  C   ASN A 251      -2.114   1.773  17.193  1.00 47.40           C  
ANISOU 1934  C   ASN A 251     6187   6247   5577   -948   -280    -46       C  
ATOM   1935  O   ASN A 251      -2.835   2.599  16.630  1.00 55.51           O  
ANISOU 1935  O   ASN A 251     7129   7390   6572   -972   -334     52       O  
ATOM   1936  CB  ASN A 251      -2.555   0.122  15.329  1.00 47.72           C  
ANISOU 1936  CB  ASN A 251     6378   6324   5430  -1248   -334   -140       C  
ATOM   1937  CG  ASN A 251      -1.825   0.970  14.323  1.00 60.00           C  
ANISOU 1937  CG  ASN A 251     7953   7911   6933  -1225   -324   -154       C  
ATOM   1938  OD1 ASN A 251      -0.612   1.166  14.427  1.00 58.52           O  
ANISOU 1938  OD1 ASN A 251     7822   7630   6783  -1124   -251   -225       O  
ATOM   1939  ND2 ASN A 251      -2.561   1.503  13.354  1.00 66.30           N  
ANISOU 1939  ND2 ASN A 251     8695   8848   7647  -1319   -398    -74       N  
ATOM   1940  N   LEU A 252      -1.356   2.085  18.242  1.00 38.84           N  
ANISOU 1940  N   LEU A 252     5099   5076   4582   -809   -219    -70       N  
ATOM   1941  CA  LEU A 252      -1.383   3.417  18.827  1.00 38.05           C  
ANISOU 1941  CA  LEU A 252     4908   5005   4544   -682   -210      7       C  
ATOM   1942  C   LEU A 252      -0.407   4.343  18.111  1.00 35.64           C  
ANISOU 1942  C   LEU A 252     4626   4693   4223   -629   -186    -16       C  
ATOM   1943  O   LEU A 252       0.669   3.927  17.680  1.00 33.51           O  
ANISOU 1943  O   LEU A 252     4447   4354   3930   -636   -149   -107       O  
ATOM   1944  CB  LEU A 252      -1.033   3.355  20.315  1.00 34.64           C  
ANISOU 1944  CB  LEU A 252     4468   4492   4202   -574   -159     -8       C  
ATOM   1945  CG  LEU A 252      -1.858   2.379  21.156  1.00 34.90           C  
ANISOU 1945  CG  LEU A 252     4481   4519   4260   -613   -172      9       C  
ATOM   1946  CD1 LEU A 252      -1.186   2.145  22.502  1.00 44.00           C  
ANISOU 1946  CD1 LEU A 252     5652   5580   5486   -518   -115    -28       C  
ATOM   1947  CD2 LEU A 252      -3.269   2.892  21.348  1.00 37.46           C  
ANISOU 1947  CD2 LEU A 252     4692   4948   4593   -623   -218    134       C  
ATOM   1948  N   LEU A 253      -0.783   5.612  18.011  1.00 33.89           N  
ANISOU 1948  N   LEU A 253     4317   4538   4021   -571   -201     76       N  
ATOM   1949  CA  LEU A 253       0.096   6.624  17.441  1.00 33.31           C  
ANISOU 1949  CA  LEU A 253     4252   4457   3946   -510   -178     69       C  
ATOM   1950  C   LEU A 253       1.011   7.188  18.521  1.00 32.76           C  
ANISOU 1950  C   LEU A 253     4195   4294   3957   -381   -117     36       C  
ATOM   1951  O   LEU A 253       0.567   7.475  19.639  1.00 28.54           O  
ANISOU 1951  O   LEU A 253     3615   3744   3484   -317   -100     74       O  
ATOM   1952  CB  LEU A 253      -0.726   7.741  16.804  1.00 40.39           C  
ANISOU 1952  CB  LEU A 253     5049   5465   4833   -509   -216    191       C  
ATOM   1953  CG  LEU A 253       0.069   8.779  16.021  1.00 51.43           C  
ANISOU 1953  CG  LEU A 253     6451   6870   6221   -464   -200    197       C  
ATOM   1954  CD1 LEU A 253       0.919   8.105  14.944  1.00 51.43           C  
ANISOU 1954  CD1 LEU A 253     6548   6858   6136   -544   -204    104       C  
ATOM   1955  CD2 LEU A 253      -0.877   9.809  15.422  1.00 55.51           C  
ANISOU 1955  CD2 LEU A 253     6855   7501   6735   -465   -236    338       C  
ATOM   1956  N   ASP A 254       2.301   7.342  18.189  1.00 32.58           N  
ANISOU 1956  N   ASP A 254     4236   4213   3929   -349    -82    -31       N  
ATOM   1957  CA  ASP A 254       3.265   7.890  19.142  1.00 31.83           C  
ANISOU 1957  CA  ASP A 254     4154   4038   3900   -245    -33    -57       C  
ATOM   1958  C   ASP A 254       3.201   9.417  19.112  1.00 34.68           C  
ANISOU 1958  C   ASP A 254     4458   4426   4293   -174    -27     10       C  
ATOM   1959  O   ASP A 254       4.067  10.109  18.570  1.00 29.20           O  
ANISOU 1959  O   ASP A 254     3781   3719   3595   -144    -13     -1       O  
ATOM   1960  CB  ASP A 254       4.679   7.369  18.878  1.00 29.65           C  
ANISOU 1960  CB  ASP A 254     3961   3690   3614   -240      4   -142       C  
ATOM   1961  CG  ASP A 254       5.129   7.510  17.425  1.00 37.94           C  
ANISOU 1961  CG  ASP A 254     5044   4771   4599   -284     -3   -158       C  
ATOM   1962  OD1 ASP A 254       4.267   7.514  16.503  1.00 34.68           O  
ANISOU 1962  OD1 ASP A 254     4609   4441   4126   -360    -47   -123       O  
ATOM   1963  OD2 ASP A 254       6.371   7.582  17.215  1.00 33.26           O  
ANISOU 1963  OD2 ASP A 254     4498   4127   4014   -248     36   -200       O  
ATOM   1964  N   VAL A 255       2.132   9.938  19.717  1.00 28.14           N  
ANISOU 1964  N   VAL A 255     3559   3632   3500   -144    -31     86       N  
ATOM   1965  CA  VAL A 255       1.935  11.371  19.900  1.00 25.96           C  
ANISOU 1965  CA  VAL A 255     3231   3363   3271    -65     -5    155       C  
ATOM   1966  C   VAL A 255       1.500  11.636  21.338  1.00 25.57           C  
ANISOU 1966  C   VAL A 255     3163   3271   3280      1     36    171       C  
ATOM   1967  O   VAL A 255       1.144  10.725  22.088  1.00 25.89           O  
ANISOU 1967  O   VAL A 255     3213   3302   3324    -20     32    149       O  
ATOM   1968  CB  VAL A 255       0.900  11.949  18.912  1.00 26.92           C  
ANISOU 1968  CB  VAL A 255     3270   3587   3374    -93    -39    265       C  
ATOM   1969  CG1 VAL A 255       1.392  11.778  17.492  1.00 28.74           C  
ANISOU 1969  CG1 VAL A 255     3523   3863   3532   -162    -77    247       C  
ATOM   1970  CG2 VAL A 255      -0.467  11.287  19.111  1.00 26.33           C  
ANISOU 1970  CG2 VAL A 255     3134   3579   3290   -143    -72    330       C  
ATOM   1971  N   TRP A 256       1.521  12.914  21.714  1.00 23.90           N  
ANISOU 1971  N   TRP A 256     2932   3032   3116     79     81    210       N  
ATOM   1972  CA  TRP A 256       1.291  13.335  23.090  1.00 25.65           C  
ANISOU 1972  CA  TRP A 256     3160   3200   3388    145    136    211       C  
ATOM   1973  C   TRP A 256      -0.050  14.037  23.272  1.00 30.39           C  
ANISOU 1973  C   TRP A 256     3680   3838   4029    191    168    322       C  
ATOM   1974  O   TRP A 256      -0.248  14.733  24.271  1.00 29.60           O  
ANISOU 1974  O   TRP A 256     3588   3685   3973    260    235    331       O  
ATOM   1975  CB  TRP A 256       2.432  14.251  23.543  1.00 25.99           C  
ANISOU 1975  CB  TRP A 256     3262   3162   3452    195    181    159       C  
ATOM   1976  CG  TRP A 256       3.743  13.549  23.586  1.00 25.32           C  
ANISOU 1976  CG  TRP A 256     3244   3040   3337    160    159     68       C  
ATOM   1977  CD1 TRP A 256       4.656  13.429  22.572  1.00 26.41           C  
ANISOU 1977  CD1 TRP A 256     3405   3183   3446    130    132     40       C  
ATOM   1978  CD2 TRP A 256       4.278  12.827  24.694  1.00 26.45           C  
ANISOU 1978  CD2 TRP A 256     3432   3139   3478    153    167      7       C  
ATOM   1979  NE1 TRP A 256       5.739  12.685  22.992  1.00 27.61           N  
ANISOU 1979  NE1 TRP A 256     3612   3293   3587    112    129    -30       N  
ATOM   1980  CE2 TRP A 256       5.532  12.308  24.293  1.00 29.83           C  
ANISOU 1980  CE2 TRP A 256     3904   3546   3885    124    147    -48       C  
ATOM   1981  CE3 TRP A 256       3.826  12.581  25.995  1.00 29.30           C  
ANISOU 1981  CE3 TRP A 256     3797   3480   3854    170    193      1       C  
ATOM   1982  CZ2 TRP A 256       6.333  11.556  25.142  1.00 27.51           C  
ANISOU 1982  CZ2 TRP A 256     3648   3216   3590    112    151    -96       C  
ATOM   1983  CZ3 TRP A 256       4.627  11.836  26.845  1.00 28.84           C  
ANISOU 1983  CZ3 TRP A 256     3782   3390   3787    151    191    -54       C  
ATOM   1984  CH2 TRP A 256       5.870  11.334  26.420  1.00 29.00           C  
ANISOU 1984  CH2 TRP A 256     3835   3392   3791    123    169    -97       C  
ATOM   1985  N   THR A 257      -0.985  13.854  22.339  1.00 29.90           N  
ANISOU 1985  N   THR A 257     3540   3869   3951    150    125    411       N  
ATOM   1986  CA  THR A 257      -2.164  14.700  22.261  1.00 30.33           C  
ANISOU 1986  CA  THR A 257     3500   3970   4052    200    157    545       C  
ATOM   1987  C   THR A 257      -3.481  13.991  22.543  1.00 33.16           C  
ANISOU 1987  C   THR A 257     3784   4401   4414    172    136    627       C  
ATOM   1988  O   THR A 257      -4.485  14.679  22.758  1.00 34.96           O  
ANISOU 1988  O   THR A 257     3930   4657   4695    232    181    747       O  
ATOM   1989  CB  THR A 257      -2.259  15.351  20.869  1.00 33.24           C  
ANISOU 1989  CB  THR A 257     3812   4409   4409    182    127    627       C  
ATOM   1990  OG1 THR A 257      -2.164  14.333  19.862  1.00 30.23           O  
ANISOU 1990  OG1 THR A 257     3435   4104   3948     69     38    602       O  
ATOM   1991  CG2 THR A 257      -1.145  16.374  20.661  1.00 39.24           C  
ANISOU 1991  CG2 THR A 257     4626   5096   5189    233    166    581       C  
ATOM   1992  N   SER A 258      -3.517  12.654  22.543  1.00 27.01           N  
ANISOU 1992  N   SER A 258     3027   3651   3585     85     74    573       N  
ATOM   1993  CA  SER A 258      -4.821  11.989  22.613  1.00 30.62           C  
ANISOU 1993  CA  SER A 258     3403   4193   4040     40     39    667       C  
ATOM   1994  C   SER A 258      -5.117  11.481  24.013  1.00 36.36           C  
ANISOU 1994  C   SER A 258     4146   4872   4798     76     79    638       C  
ATOM   1995  O   SER A 258      -4.234  10.921  24.672  1.00 34.40           O  
ANISOU 1995  O   SER A 258     3985   4547   4536     72     87    519       O  
ATOM   1996  CB  SER A 258      -4.893  10.811  21.643  1.00 34.40           C  
ANISOU 1996  CB  SER A 258     3889   4743   4440    -98    -56    643       C  
ATOM   1997  OG  SER A 258      -4.850  11.271  20.308  1.00 52.64           O  
ANISOU 1997  OG  SER A 258     6168   7122   6710   -143    -98    692       O  
ATOM   1998  N   PRO A 259      -6.357  11.655  24.468  1.00 28.21           N  
ANISOU 1998  N   PRO A 259     3023   3888   3808    111    105    758       N  
ATOM   1999  CA  PRO A 259      -6.718  11.199  25.817  1.00 29.23           C  
ANISOU 1999  CA  PRO A 259     3163   3980   3965    148    148    742       C  
ATOM   2000  C   PRO A 259      -6.934   9.692  25.815  1.00 37.94           C  
ANISOU 2000  C   PRO A 259     4271   5120   5023     41     71    708       C  
ATOM   2001  O   PRO A 259      -7.621   9.151  24.947  1.00 46.72           O  
ANISOU 2001  O   PRO A 259     5324   6325   6104    -50     -3    776       O  
ATOM   2002  CB  PRO A 259      -8.016  11.956  26.117  1.00 34.36           C  
ANISOU 2002  CB  PRO A 259     3702   4676   4676    224    208    901       C  
ATOM   2003  CG  PRO A 259      -8.628  12.161  24.757  1.00 34.82           C  
ANISOU 2003  CG  PRO A 259     3664   4845   4720    168    145   1023       C  
ATOM   2004  CD  PRO A 259      -7.483  12.314  23.778  1.00 32.76           C  
ANISOU 2004  CD  PRO A 259     3475   4561   4410    122    102    929       C  
ATOM   2005  N   ALA A 260      -6.307   9.012  26.767  1.00 30.89           N  
ANISOU 2005  N   ALA A 260     3455   4156   4127     45     87    602       N  
ATOM   2006  CA  ALA A 260      -6.488   7.582  26.936  1.00 33.45           C  
ANISOU 2006  CA  ALA A 260     3790   4496   4424    -44     31    570       C  
ATOM   2007  C   ALA A 260      -7.567   7.333  27.979  1.00 35.61           C  
ANISOU 2007  C   ALA A 260     3998   4798   4736    -11     59    651       C  
ATOM   2008  O   ALA A 260      -7.963   8.234  28.718  1.00 31.76           O  
ANISOU 2008  O   ALA A 260     3479   4296   4292     90    137    705       O  
ATOM   2009  CB  ALA A 260      -5.175   6.918  27.355  1.00 29.03           C  
ANISOU 2009  CB  ALA A 260     3339   3847   3845    -57     34    426       C  
ATOM   2010  N   ASP A 261      -8.049   6.092  28.027  1.00 30.98           N  
ANISOU 2010  N   ASP A 261     3395   4245   4131    -98      3    658       N  
ATOM   2011  CA  ASP A 261      -9.094   5.701  28.967  1.00 33.04           C  
ANISOU 2011  CA  ASP A 261     3587   4541   4426    -80     21    741       C  
ATOM   2012  C   ASP A 261      -8.496   5.404  30.336  1.00 33.19           C  
ANISOU 2012  C   ASP A 261     3669   4479   4462    -22     77    658       C  
ATOM   2013  O   ASP A 261      -7.817   4.385  30.493  1.00 29.41           O  
ANISOU 2013  O   ASP A 261     3254   3957   3962    -79     46    568       O  
ATOM   2014  CB  ASP A 261      -9.834   4.473  28.440  1.00 34.13           C  
ANISOU 2014  CB  ASP A 261     3684   4749   4537   -210    -67    784       C  
ATOM   2015  CG  ASP A 261     -10.956   4.016  29.362  1.00 36.45           C  
ANISOU 2015  CG  ASP A 261     3897   5087   4867   -198    -56    883       C  
ATOM   2016  OD1 ASP A 261     -11.175   4.646  30.422  1.00 33.23           O  
ANISOU 2016  OD1 ASP A 261     3467   4656   4503    -84     27    916       O  
ATOM   2017  OD2 ASP A 261     -11.635   3.019  29.013  1.00 39.91           O  
ANISOU 2017  OD2 ASP A 261     4296   5582   5284   -310   -129    928       O  
ATOM   2018  N   PRO A 262      -8.753   6.234  31.355  1.00 31.92           N  
ANISOU 2018  N   PRO A 262     3494   4297   4337     86    164    691       N  
ATOM   2019  CA  PRO A 262      -8.177   5.951  32.682  1.00 28.77           C  
ANISOU 2019  CA  PRO A 262     3157   3833   3939    126    212    615       C  
ATOM   2020  C   PRO A 262      -8.621   4.620  33.258  1.00 30.96           C  
ANISOU 2020  C   PRO A 262     3410   4134   4219     69    175    629       C  
ATOM   2021  O   PRO A 262      -7.877   4.020  34.047  1.00 31.56           O  
ANISOU 2021  O   PRO A 262     3546   4159   4286     65    183    549       O  
ATOM   2022  CB  PRO A 262      -8.669   7.119  33.553  1.00 37.35           C  
ANISOU 2022  CB  PRO A 262     4226   4908   5058    241    318    668       C  
ATOM   2023  CG  PRO A 262      -9.183   8.156  32.590  1.00 38.39           C  
ANISOU 2023  CG  PRO A 262     4301   5073   5212    275    333    754       C  
ATOM   2024  CD  PRO A 262      -9.649   7.405  31.380  1.00 35.57           C  
ANISOU 2024  CD  PRO A 262     3881   4795   4839    172    228    810       C  
ATOM   2025  N  AASN A 263      -9.805   4.124  32.888  0.53 27.79           N  
ANISOU 2025  N  AASN A 263     2918   3811   3830     20    132    736       N  
ATOM   2026  N  BASN A 263      -9.808   4.132  32.894  0.47 27.56           N  
ANISOU 2026  N  BASN A 263     2888   3781   3801     21    133    737       N  
ATOM   2027  CA AASN A 263     -10.263   2.861  33.461  0.53 28.48           C  
ANISOU 2027  CA AASN A 263     2980   3917   3924    -37     99    755       C  
ATOM   2028  CA BASN A 263     -10.268   2.870  33.460  0.47 28.47           C  
ANISOU 2028  CA BASN A 263     2979   3916   3923    -37     99    756       C  
ATOM   2029  C  AASN A 263      -9.425   1.675  32.994  0.53 27.86           C  
ANISOU 2029  C  AASN A 263     2973   3794   3818   -139     34    654       C  
ATOM   2030  C  BASN A 263      -9.424   1.683  32.998  0.47 28.08           C  
ANISOU 2030  C  BASN A 263     3002   3822   3846   -138     34    654       C  
ATOM   2031  O  AASN A 263      -9.415   0.639  33.666  0.53 31.38           O  
ANISOU 2031  O  AASN A 263     3428   4220   4274   -171     24    637       O  
ATOM   2032  O  BASN A 263      -9.392   0.658  33.687  0.47 31.53           O  
ANISOU 2032  O  BASN A 263     3449   4238   4294   -169     26    636       O  
ATOM   2033  CB AASN A 263     -11.734   2.624  33.127  0.53 32.23           C  
ANISOU 2033  CB AASN A 263     3337   4492   4418    -78     62    903       C  
ATOM   2034  CB BASN A 263     -11.745   2.661  33.119  0.47 32.55           C  
ANISOU 2034  CB BASN A 263     3376   4534   4459    -76     64    906       C  
ATOM   2035  CG AASN A 263     -12.351   1.530  33.979  0.53 32.63           C  
ANISOU 2035  CG AASN A 263     3349   4562   4486   -112     48    944       C  
ATOM   2036  CG BASN A 263     -12.654   3.625  33.867  0.47 36.99           C  
ANISOU 2036  CG BASN A 263     3860   5131   5062     39    150   1021       C  
ATOM   2037  OD1AASN A 263     -12.520   1.694  35.186  0.53 29.95           O  
ANISOU 2037  OD1AASN A 263     2999   4209   4169    -30    118    962       O  
ATOM   2038  OD1BASN A 263     -12.354   4.035  34.989  0.47 44.05           O  
ANISOU 2038  OD1BASN A 263     4794   5975   5968    130    235    983       O  
ATOM   2039  ND2AASN A 263     -12.695   0.410  33.353  0.53 32.24           N  
ANISOU 2039  ND2AASN A 263     3283   4545   4421   -239    -39    958       N  
ATOM   2040  ND2BASN A 263     -13.775   3.987  33.249  0.47 49.37           N  
ANISOU 2040  ND2BASN A 263     5317   6790   6651     32    134   1168       N  
ATOM   2041  N   GLU A 264      -8.735   1.797  31.859  1.00 27.84           N  
ANISOU 2041  N   GLU A 264     3022   3771   3784   -186     -3    592       N  
ATOM   2042  CA  GLU A 264      -7.824   0.735  31.445  1.00 25.93           C  
ANISOU 2042  CA  GLU A 264     2862   3469   3521   -266    -40    489       C  
ATOM   2043  C   GLU A 264      -6.679   0.612  32.437  1.00 31.75           C  
ANISOU 2043  C   GLU A 264     3667   4125   4271   -206     11    403       C  
ATOM   2044  O   GLU A 264      -6.264  -0.498  32.788  1.00 32.19           O  
ANISOU 2044  O   GLU A 264     3757   4136   4337   -247      2    361       O  
ATOM   2045  CB  GLU A 264      -7.292   1.000  30.037  1.00 26.46           C  
ANISOU 2045  CB  GLU A 264     2974   3533   3547   -319    -76    441       C  
ATOM   2046  CG  GLU A 264      -8.302   0.696  28.921  1.00 30.82           C  
ANISOU 2046  CG  GLU A 264     3474   4169   4068   -429   -148    513       C  
ATOM   2047  CD  GLU A 264      -7.771   1.102  27.543  1.00 37.60           C  
ANISOU 2047  CD  GLU A 264     4375   5034   4875   -477   -178    470       C  
ATOM   2048  OE1 GLU A 264      -6.563   1.410  27.444  1.00 35.76           O  
ANISOU 2048  OE1 GLU A 264     4220   4729   4637   -431   -144    375       O  
ATOM   2049  OE2 GLU A 264      -8.558   1.120  26.571  1.00 40.20           O  
ANISOU 2049  OE2 GLU A 264     4657   5448   5167   -563   -237    539       O  
ATOM   2050  N   MET A 265      -6.181   1.748  32.923  1.00 28.62           N  
ANISOU 2050  N   MET A 265     3288   3710   3877   -112     65    385       N  
ATOM   2051  CA  MET A 265      -5.138   1.748  33.942  1.00 31.63           C  
ANISOU 2051  CA  MET A 265     3726   4032   4261    -63    108    319       C  
ATOM   2052  C   MET A 265      -5.666   1.205  35.267  1.00 24.60           C  
ANISOU 2052  C   MET A 265     2800   3157   3390    -43    133    361       C  
ATOM   2053  O   MET A 265      -5.031   0.353  35.905  1.00 26.38           O  
ANISOU 2053  O   MET A 265     3053   3347   3622    -60    133    325       O  
ATOM   2054  CB  MET A 265      -4.612   3.173  34.098  1.00 32.61           C  
ANISOU 2054  CB  MET A 265     3879   4138   4373     15    158    295       C  
ATOM   2055  CG  MET A 265      -3.750   3.399  35.304  1.00 44.96           C  
ANISOU 2055  CG  MET A 265     5491   5663   5928     60    204    247       C  
ATOM   2056  SD  MET A 265      -2.088   2.810  35.026  1.00 46.55           S  
ANISOU 2056  SD  MET A 265     5766   5803   6119     23    180    156       S  
ATOM   2057  CE  MET A 265      -1.309   3.459  36.499  1.00 47.81           C  
ANISOU 2057  CE  MET A 265     5965   5946   6257     73    232    129       C  
ATOM   2058  N   LEU A 266      -6.837   1.677  35.689  1.00 30.49           N  
ANISOU 2058  N   LEU A 266     3479   3958   4149     -4    158    447       N  
ATOM   2059  CA  LEU A 266      -7.426   1.189  36.932  1.00 25.89           C  
ANISOU 2059  CA  LEU A 266     2857   3398   3582     18    186    496       C  
ATOM   2060  C   LEU A 266      -7.602  -0.326  36.906  1.00 28.91           C  
ANISOU 2060  C   LEU A 266     3222   3780   3982    -65    132    506       C  
ATOM   2061  O   LEU A 266      -7.251  -1.020  37.870  1.00 27.55           O  
ANISOU 2061  O   LEU A 266     3061   3588   3820    -63    146    492       O  
ATOM   2062  CB  LEU A 266      -8.764   1.892  37.175  1.00 28.71           C  
ANISOU 2062  CB  LEU A 266     3135   3817   3956     71    224    604       C  
ATOM   2063  CG  LEU A 266      -9.565   1.503  38.423  1.00 29.37           C  
ANISOU 2063  CG  LEU A 266     3167   3935   4056    103    263    672       C  
ATOM   2064  CD1 LEU A 266      -8.651   1.519  39.637  1.00 29.37           C  
ANISOU 2064  CD1 LEU A 266     3235   3893   4032    138    310    600       C  
ATOM   2065  CD2 LEU A 266     -10.767   2.429  38.605  1.00 35.92           C  
ANISOU 2065  CD2 LEU A 266     3924   4817   4906    177    324    781       C  
ATOM   2066  N   ASP A 267      -8.139  -0.862  35.802  1.00 27.65           N  
ANISOU 2066  N   ASP A 267     3038   3643   3826   -146     71    532       N  
ATOM   2067  CA  ASP A 267      -8.363  -2.307  35.723  1.00 29.97           C  
ANISOU 2067  CA  ASP A 267     3325   3925   4137   -236     26    537       C  
ATOM   2068  C   ASP A 267      -7.061  -3.084  35.816  1.00 29.30           C  
ANISOU 2068  C   ASP A 267     3322   3754   4057   -257     31    442       C  
ATOM   2069  O   ASP A 267      -7.038  -4.210  36.337  1.00 28.20           O  
ANISOU 2069  O   ASP A 267     3181   3587   3945   -293     27    448       O  
ATOM   2070  CB  ASP A 267      -9.055  -2.675  34.415  1.00 33.45           C  
ANISOU 2070  CB  ASP A 267     3745   4400   4563   -339    -42    567       C  
ATOM   2071  CG  ASP A 267     -10.542  -2.381  34.423  1.00 42.22           C  
ANISOU 2071  CG  ASP A 267     4749   5611   5683   -345    -61    698       C  
ATOM   2072  OD1 ASP A 267     -11.120  -2.111  35.501  1.00 38.16           O  
ANISOU 2072  OD1 ASP A 267     4176   5129   5195   -272    -17    768       O  
ATOM   2073  OD2 ASP A 267     -11.128  -2.417  33.321  1.00 46.31           O  
ANISOU 2073  OD2 ASP A 267     5240   6178   6179   -428   -119    738       O  
ATOM   2074  N   LEU A 268      -5.985  -2.517  35.276  1.00 27.62           N  
ANISOU 2074  N   LEU A 268     3174   3497   3823   -235     43    365       N  
ATOM   2075  CA  LEU A 268      -4.690  -3.182  35.283  1.00 29.14           C  
ANISOU 2075  CA  LEU A 268     3437   3611   4026   -247     56    289       C  
ATOM   2076  C   LEU A 268      -4.166  -3.366  36.699  1.00 29.15           C  
ANISOU 2076  C   LEU A 268     3431   3600   4045   -192     95    297       C  
ATOM   2077  O   LEU A 268      -3.615  -4.424  37.033  1.00 30.33           O  
ANISOU 2077  O   LEU A 268     3597   3701   4226   -216    102    286       O  
ATOM   2078  CB  LEU A 268      -3.712  -2.365  34.444  1.00 29.58           C  
ANISOU 2078  CB  LEU A 268     3550   3636   4053   -227     62    221       C  
ATOM   2079  CG  LEU A 268      -2.326  -2.934  34.183  1.00 34.94           C  
ANISOU 2079  CG  LEU A 268     4299   4236   4742   -236     80    150       C  
ATOM   2080  CD1 LEU A 268      -2.442  -4.227  33.398  1.00 32.58           C  
ANISOU 2080  CD1 LEU A 268     4032   3888   4458   -324     62    128       C  
ATOM   2081  CD2 LEU A 268      -1.498  -1.896  33.426  1.00 35.84           C  
ANISOU 2081  CD2 LEU A 268     4455   4338   4825   -206     86    100       C  
ATOM   2082  N   ILE A 269      -4.351  -2.360  37.557  1.00 25.08           N  
ANISOU 2082  N   ILE A 269     2893   3127   3511   -121    127    322       N  
ATOM   2083  CA  ILE A 269      -3.708  -2.373  38.863  1.00 28.25           C  
ANISOU 2083  CA  ILE A 269     3300   3526   3909    -79    163    322       C  
ATOM   2084  C   ILE A 269      -4.649  -2.728  40.012  1.00 27.47           C  
ANISOU 2084  C   ILE A 269     3140   3476   3820    -64    178    394       C  
ATOM   2085  O   ILE A 269      -4.170  -3.211  41.048  1.00 26.67           O  
ANISOU 2085  O   ILE A 269     3036   3374   3722    -55    196    405       O  
ATOM   2086  CB  ILE A 269      -3.015  -1.024  39.143  1.00 30.19           C  
ANISOU 2086  CB  ILE A 269     3585   3773   4112    -22    196    282       C  
ATOM   2087  CG1 ILE A 269      -4.044   0.096  39.322  1.00 28.69           C  
ANISOU 2087  CG1 ILE A 269     3370   3630   3902     27    226    317       C  
ATOM   2088  CG2 ILE A 269      -2.055  -0.678  38.012  1.00 29.05           C  
ANISOU 2088  CG2 ILE A 269     3494   3583   3960    -35    180    218       C  
ATOM   2089  CD1 ILE A 269      -3.419   1.384  39.851  1.00 31.90           C  
ANISOU 2089  CD1 ILE A 269     3826   4028   4266     79    274    276       C  
ATOM   2090  N   LYS A 270      -5.962  -2.531  39.858  1.00 24.87           N  
ANISOU 2090  N   LYS A 270     2756   3196   3496    -63    173    456       N  
ATOM   2091  CA  LYS A 270      -6.844  -2.648  41.017  1.00 22.69           C  
ANISOU 2091  CA  LYS A 270     2422   2973   3225    -32    202    530       C  
ATOM   2092  C   LYS A 270      -6.971  -4.086  41.512  1.00 27.60           C  
ANISOU 2092  C   LYS A 270     3011   3589   3885    -81    179    567       C  
ATOM   2093  O   LYS A 270      -7.354  -4.295  42.666  1.00 28.51           O  
ANISOU 2093  O   LYS A 270     3088   3742   4001    -54    206    619       O  
ATOM   2094  CB  LYS A 270      -8.221  -2.076  40.704  1.00 25.48           C  
ANISOU 2094  CB  LYS A 270     2713   3384   3584    -13    208    605       C  
ATOM   2095  CG  LYS A 270      -9.124  -2.959  39.851  1.00 30.01           C  
ANISOU 2095  CG  LYS A 270     3232   3979   4190    -92    146    661       C  
ATOM   2096  CD  LYS A 270     -10.484  -2.310  39.679  1.00 28.61           C  
ANISOU 2096  CD  LYS A 270     2975   3876   4019    -65    156    761       C  
ATOM   2097  CE  LYS A 270     -11.409  -3.175  38.861  1.00 29.44           C  
ANISOU 2097  CE  LYS A 270     3021   4018   4147   -161     84    829       C  
ATOM   2098  NZ  LYS A 270     -12.757  -2.539  38.759  1.00 35.55           N  
ANISOU 2098  NZ  LYS A 270     3697   4878   4932   -133     94    953       N  
ATOM   2099  N   VAL A 271      -6.640  -5.076  40.676  1.00 26.10           N  
ANISOU 2099  N   VAL A 271     2842   3347   3727   -151    138    540       N  
ATOM   2100  CA  VAL A 271      -6.759  -6.476  41.082  1.00 23.28           C  
ANISOU 2100  CA  VAL A 271     2460   2968   3417   -199    124    576       C  
ATOM   2101  C   VAL A 271      -5.567  -6.972  41.888  1.00 27.90           C  
ANISOU 2101  C   VAL A 271     3071   3514   4016   -179    151    556       C  
ATOM   2102  O   VAL A 271      -5.577  -8.129  42.331  1.00 27.95           O  
ANISOU 2102  O   VAL A 271     3054   3498   4069   -210    149    594       O  
ATOM   2103  CB  VAL A 271      -6.952  -7.366  39.838  1.00 23.47           C  
ANISOU 2103  CB  VAL A 271     2507   2941   3468   -292     80    555       C  
ATOM   2104  CG1 VAL A 271      -8.156  -6.892  39.029  1.00 23.78           C  
ANISOU 2104  CG1 VAL A 271     2508   3038   3487   -327     42    594       C  
ATOM   2105  CG2 VAL A 271      -5.671  -7.349  38.970  1.00 25.92           C  
ANISOU 2105  CG2 VAL A 271     2903   3173   3773   -303     85    461       C  
ATOM   2106  N   TRP A 272      -4.540  -6.145  42.092  1.00 24.39           N  
ANISOU 2106  N   TRP A 272     2670   3064   3535   -134    174    506       N  
ATOM   2107  CA  TRP A 272      -3.381  -6.521  42.888  1.00 25.15           C  
ANISOU 2107  CA  TRP A 272     2778   3142   3637   -119    194    505       C  
ATOM   2108  C   TRP A 272      -3.372  -5.720  44.185  1.00 25.71           C  
ANISOU 2108  C   TRP A 272     2834   3284   3652    -71    223    529       C  
ATOM   2109  O   TRP A 272      -3.998  -4.658  44.272  1.00 26.04           O  
ANISOU 2109  O   TRP A 272     2880   3366   3649    -38    239    521       O  
ATOM   2110  CB  TRP A 272      -2.068  -6.311  42.108  1.00 28.65           C  
ANISOU 2110  CB  TRP A 272     3283   3523   4078   -120    195    437       C  
ATOM   2111  CG  TRP A 272      -2.014  -7.168  40.882  1.00 25.36           C  
ANISOU 2111  CG  TRP A 272     2896   3029   3710   -170    181    407       C  
ATOM   2112  CD1 TRP A 272      -2.243  -6.766  39.588  1.00 27.42           C  
ANISOU 2112  CD1 TRP A 272     3197   3267   3954   -196    161    353       C  
ATOM   2113  CD2 TRP A 272      -1.791  -8.582  40.834  1.00 27.55           C  
ANISOU 2113  CD2 TRP A 272     3171   3241   4055   -208    192    430       C  
ATOM   2114  NE1 TRP A 272      -2.164  -7.848  38.742  1.00 25.54           N  
ANISOU 2114  NE1 TRP A 272     2990   2954   3758   -255    158    332       N  
ATOM   2115  CE2 TRP A 272      -1.884  -8.974  39.480  1.00 27.16           C  
ANISOU 2115  CE2 TRP A 272     3175   3124   4021   -261    182    375       C  
ATOM   2116  CE3 TRP A 272      -1.516  -9.553  41.801  1.00 27.91           C  
ANISOU 2116  CE3 TRP A 272     3177   3277   4150   -204    214    493       C  
ATOM   2117  CZ2 TRP A 272      -1.708 -10.297  39.069  1.00 27.64           C  
ANISOU 2117  CZ2 TRP A 272     3263   3095   4144   -310    202    373       C  
ATOM   2118  CZ3 TRP A 272      -1.342 -10.870  41.392  1.00 25.67           C  
ANISOU 2118  CZ3 TRP A 272     2910   2904   3941   -244    233    502       C  
ATOM   2119  CH2 TRP A 272      -1.437 -11.230  40.037  1.00 27.65           C  
ANISOU 2119  CH2 TRP A 272     3225   3075   4204   -297    231    436       C  
ATOM   2120  N   PRO A 273      -2.712  -6.221  45.234  1.00 24.58           N  
ANISOU 2120  N   PRO A 273     2671   3158   3509    -70    235    566       N  
ATOM   2121  CA  PRO A 273      -2.933  -5.628  46.571  1.00 26.37           C  
ANISOU 2121  CA  PRO A 273     2882   3465   3674    -41    263    598       C  
ATOM   2122  C   PRO A 273      -2.641  -4.133  46.671  1.00 27.59           C  
ANISOU 2122  C   PRO A 273     3095   3640   3747    -12    287    537       C  
ATOM   2123  O   PRO A 273      -3.409  -3.408  47.317  1.00 29.55           O  
ANISOU 2123  O   PRO A 273     3344   3936   3948     18    323    546       O  
ATOM   2124  CB  PRO A 273      -1.996  -6.458  47.460  1.00 27.50           C  
ANISOU 2124  CB  PRO A 273     2999   3621   3830    -59    261    647       C  
ATOM   2125  CG  PRO A 273      -2.028  -7.835  46.793  1.00 29.71           C  
ANISOU 2125  CG  PRO A 273     3249   3831   4208    -88    244    677       C  
ATOM   2126  CD  PRO A 273      -2.008  -7.522  45.313  1.00 26.81           C  
ANISOU 2126  CD  PRO A 273     2934   3395   3857    -97    230    601       C  
ATOM   2127  N   ILE A 274      -1.565  -3.645  46.040  1.00 25.26           N  
ANISOU 2127  N   ILE A 274     2853   3306   3440    -18    275    477       N  
ATOM   2128  CA  ILE A 274      -1.178  -2.238  46.158  1.00 27.43           C  
ANISOU 2128  CA  ILE A 274     3190   3594   3640      0    298    418       C  
ATOM   2129  C   ILE A 274      -1.949  -1.333  45.208  1.00 27.10           C  
ANISOU 2129  C   ILE A 274     3172   3527   3599     31    311    379       C  
ATOM   2130  O   ILE A 274      -1.804  -0.102  45.283  1.00 24.32           O  
ANISOU 2130  O   ILE A 274     2872   3174   3193     54    342    333       O  
ATOM   2131  CB  ILE A 274       0.337  -2.111  45.892  1.00 24.85           C  
ANISOU 2131  CB  ILE A 274     2899   3240   3302    -24    276    385       C  
ATOM   2132  CG1 ILE A 274       0.910  -0.765  46.379  1.00 27.45           C  
ANISOU 2132  CG1 ILE A 274     3294   3594   3542    -25    297    335       C  
ATOM   2133  CG2 ILE A 274       0.631  -2.282  44.402  1.00 23.57           C  
ANISOU 2133  CG2 ILE A 274     2753   3007   3195    -25    253    346       C  
ATOM   2134  CD1 ILE A 274       0.741  -0.525  47.889  1.00 26.99           C  
ANISOU 2134  CD1 ILE A 274     3240   3608   3406    -38    325    361       C  
ATOM   2135  N   GLY A 275      -2.778  -1.903  44.326  1.00 27.09           N  
ANISOU 2135  N   GLY A 275     3131   3505   3656     27    289    401       N  
ATOM   2136  CA  GLY A 275      -3.406  -1.097  43.282  1.00 28.41           C  
ANISOU 2136  CA  GLY A 275     3310   3656   3827     47    292    378       C  
ATOM   2137  C   GLY A 275      -4.203   0.080  43.813  1.00 33.15           C  
ANISOU 2137  C   GLY A 275     3918   4290   4387    101    350    388       C  
ATOM   2138  O   GLY A 275      -4.086   1.200  43.304  1.00 29.75           O  
ANISOU 2138  O   GLY A 275     3529   3839   3935    129    373    348       O  
ATOM   2139  N   GLN A 276      -5.029  -0.156  44.839  1.00 30.53           N  
ANISOU 2139  N   GLN A 276     3547   4006   4048    120    383    446       N  
ATOM   2140  CA  GLN A 276      -5.857   0.914  45.409  1.00 35.05           C  
ANISOU 2140  CA  GLN A 276     4128   4603   4585    180    459    462       C  
ATOM   2141  C   GLN A 276      -5.006   2.065  45.923  1.00 32.70           C  
ANISOU 2141  C   GLN A 276     3923   4285   4217    195    507    388       C  
ATOM   2142  O   GLN A 276      -5.326   3.240  45.688  1.00 32.79           O  
ANISOU 2142  O   GLN A 276     3972   4274   4213    241    564    366       O  
ATOM   2143  CB  GLN A 276      -6.718   0.394  46.562  1.00 40.52           C  
ANISOU 2143  CB  GLN A 276     4770   5352   5274    196    493    535       C  
ATOM   2144  CG  GLN A 276      -8.022  -0.260  46.194  1.00 68.39           C  
ANISOU 2144  CG  GLN A 276     8206   8912   8866    201    477    626       C  
ATOM   2145  CD  GLN A 276      -8.807  -0.710  47.426  1.00 87.88           C  
ANISOU 2145  CD  GLN A 276    10625  11438  11326    221    517    701       C  
ATOM   2146  OE1 GLN A 276      -8.768  -0.062  48.477  1.00 89.10           O  
ANISOU 2146  OE1 GLN A 276    10821  11613  11420    258    590    687       O  
ATOM   2147  NE2 GLN A 276      -9.516  -1.832  47.301  1.00 93.67           N  
ANISOU 2147  NE2 GLN A 276    11275  12200  12116    190    472    779       N  
ATOM   2148  N   ARG A 277      -3.949   1.749  46.678  1.00 28.62           N  
ANISOU 2148  N   ARG A 277     3440   3778   3655    153    489    358       N  
ATOM   2149  CA  ARG A 277      -3.074   2.799  47.186  1.00 25.40           C  
ANISOU 2149  CA  ARG A 277     3124   3356   3169    144    525    288       C  
ATOM   2150  C   ARG A 277      -2.456   3.593  46.046  1.00 24.60           C  
ANISOU 2150  C   ARG A 277     3069   3198   3080    146    508    228       C  
ATOM   2151  O   ARG A 277      -2.335   4.821  46.126  1.00 29.78           O  
ANISOU 2151  O   ARG A 277     3796   3825   3692    167    563    178       O  
ATOM   2152  CB  ARG A 277      -1.975   2.204  48.072  1.00 30.41           C  
ANISOU 2152  CB  ARG A 277     3770   4026   3757     82    489    285       C  
ATOM   2153  CG  ARG A 277      -1.083   3.247  48.749  1.00 39.42           C  
ANISOU 2153  CG  ARG A 277     5008   5170   4800     49    518    220       C  
ATOM   2154  CD  ARG A 277      -0.297   2.605  49.883  1.00 56.50           C  
ANISOU 2154  CD  ARG A 277     7162   7398   6906    -16    488    248       C  
ATOM   2155  NE  ARG A 277       0.918   3.318  50.288  1.00 60.06           N  
ANISOU 2155  NE  ARG A 277     7690   7860   7271    -79    477    198       N  
ATOM   2156  CZ  ARG A 277       1.005   4.125  51.345  1.00 56.24           C  
ANISOU 2156  CZ  ARG A 277     7288   7407   6676   -116    526    160       C  
ATOM   2157  NH1 ARG A 277      -0.060   4.351  52.111  1.00 41.94           N  
ANISOU 2157  NH1 ARG A 277     5495   5613   4828    -82    603    164       N  
ATOM   2158  NH2 ARG A 277       2.161   4.708  51.638  1.00 56.44           N  
ANISOU 2158  NH2 ARG A 277     7378   7445   6622   -192    502    119       N  
ATOM   2159  N   LEU A 278      -2.030   2.912  44.982  1.00 23.62           N  
ANISOU 2159  N   LEU A 278     2910   3051   3013    124    440    231       N  
ATOM   2160  CA  LEU A 278      -1.478   3.649  43.851  1.00 24.61           C  
ANISOU 2160  CA  LEU A 278     3074   3127   3149    128    425    180       C  
ATOM   2161  C   LEU A 278      -2.542   4.528  43.205  1.00 25.74           C  
ANISOU 2161  C   LEU A 278     3210   3255   3315    184    469    192       C  
ATOM   2162  O   LEU A 278      -2.272   5.677  42.833  1.00 26.61           O  
ANISOU 2162  O   LEU A 278     3376   3329   3407    205    502    149       O  
ATOM   2163  CB  LEU A 278      -0.886   2.683  42.827  1.00 23.19           C  
ANISOU 2163  CB  LEU A 278     2863   2927   3023     93    354    182       C  
ATOM   2164  CG  LEU A 278       0.325   1.877  43.299  1.00 24.41           C  
ANISOU 2164  CG  LEU A 278     3018   3086   3170     48    319    183       C  
ATOM   2165  CD1 LEU A 278       0.891   1.051  42.137  1.00 28.19           C  
ANISOU 2165  CD1 LEU A 278     3479   3524   3707     26    272    178       C  
ATOM   2166  CD2 LEU A 278       1.402   2.794  43.876  1.00 26.50           C  
ANISOU 2166  CD2 LEU A 278     3348   3355   3367     29    331    140       C  
ATOM   2167  N   TRP A 279      -3.761   4.007  43.065  1.00 24.58           N  
ANISOU 2167  N   TRP A 279     2992   3137   3212    206    472    261       N  
ATOM   2168  CA  TRP A 279      -4.826   4.773  42.427  1.00 26.73           C  
ANISOU 2168  CA  TRP A 279     3236   3407   3514    259    512    300       C  
ATOM   2169  C   TRP A 279      -5.219   5.994  43.252  1.00 25.68           C  
ANISOU 2169  C   TRP A 279     3152   3261   3344    321    618    292       C  
ATOM   2170  O   TRP A 279      -5.670   6.999  42.684  1.00 30.01           O  
ANISOU 2170  O   TRP A 279     3708   3784   3913    371    667    304       O  
ATOM   2171  CB  TRP A 279      -6.033   3.869  42.184  1.00 28.01           C  
ANISOU 2171  CB  TRP A 279     3301   3615   3727    257    485    390       C  
ATOM   2172  CG  TRP A 279      -7.069   4.459  41.269  1.00 33.82           C  
ANISOU 2172  CG  TRP A 279     3984   4364   4502    294    501    453       C  
ATOM   2173  CD1 TRP A 279      -8.360   4.770  41.588  1.00 39.54           C  
ANISOU 2173  CD1 TRP A 279     4647   5126   5250    350    559    545       C  
ATOM   2174  CD2 TRP A 279      -6.894   4.825  39.891  1.00 28.00           C  
ANISOU 2174  CD2 TRP A 279     3243   3611   3785    280    460    444       C  
ATOM   2175  NE1 TRP A 279      -9.008   5.289  40.486  1.00 31.43           N  
ANISOU 2175  NE1 TRP A 279     3569   4111   4261    368    553    603       N  
ATOM   2176  CE2 TRP A 279      -8.132   5.338  39.437  1.00 31.70           C  
ANISOU 2176  CE2 TRP A 279     3640   4116   4289    323    490    539       C  
ATOM   2177  CE3 TRP A 279      -5.820   4.766  38.997  1.00 30.66           C  
ANISOU 2177  CE3 TRP A 279     3625   3912   4112    235    403    373       C  
ATOM   2178  CZ2 TRP A 279      -8.322   5.789  38.131  1.00 34.84           C  
ANISOU 2178  CZ2 TRP A 279     4008   4520   4708    316    459    567       C  
ATOM   2179  CZ3 TRP A 279      -6.016   5.206  37.686  1.00 37.05           C  
ANISOU 2179  CZ3 TRP A 279     4413   4723   4939    230    376    390       C  
ATOM   2180  CH2 TRP A 279      -7.260   5.711  37.272  1.00 35.42           C  
ANISOU 2180  CH2 TRP A 279     4134   4560   4764    267    400    487       C  
ATOM   2181  N   SER A 280      -5.038   5.945  44.575  1.00 27.02           N  
ANISOU 2181  N   SER A 280     3362   3445   3459    315    660    274       N  
ATOM   2182  CA  SER A 280      -5.443   7.078  45.412  1.00 29.01           C  
ANISOU 2182  CA  SER A 280     3678   3676   3668    368    776    258       C  
ATOM   2183  C   SER A 280      -4.740   8.360  44.989  1.00 26.96           C  
ANISOU 2183  C   SER A 280     3510   3350   3385    376    813    183       C  
ATOM   2184  O   SER A 280      -5.288   9.458  45.170  1.00 31.29           O  
ANISOU 2184  O   SER A 280     4102   3857   3930    438    919    182       O  
ATOM   2185  CB  SER A 280      -5.166   6.780  46.890  1.00 28.38           C  
ANISOU 2185  CB  SER A 280     3642   3629   3513    338    806    237       C  
ATOM   2186  OG  SER A 280      -3.777   6.847  47.191  1.00 30.11           O  
ANISOU 2186  OG  SER A 280     3933   3838   3668    266    763    159       O  
ATOM   2187  N   VAL A 281      -3.533   8.237  44.439  1.00 27.87           N  
ANISOU 2187  N   VAL A 281     3654   3447   3488    318    735    127       N  
ATOM   2188  CA  VAL A 281      -2.789   9.363  43.875  1.00 28.14           C  
ANISOU 2188  CA  VAL A 281     3765   3421   3508    317    752     62       C  
ATOM   2189  C   VAL A 281      -3.093   9.543  42.391  1.00 31.74           C  
ANISOU 2189  C   VAL A 281     4164   3859   4037    348    719     96       C  
ATOM   2190  O   VAL A 281      -3.413  10.645  41.935  1.00 29.47           O  
ANISOU 2190  O   VAL A 281     3901   3526   3769    399    783     97       O  
ATOM   2191  CB  VAL A 281      -1.276   9.151  44.114  1.00 27.68           C  
ANISOU 2191  CB  VAL A 281     3760   3362   3394    233    686     -4       C  
ATOM   2192  CG1 VAL A 281      -0.431  10.148  43.293  1.00 27.77           C  
ANISOU 2192  CG1 VAL A 281     3831   3315   3403    224    680    -60       C  
ATOM   2193  CG2 VAL A 281      -0.952   9.247  45.611  1.00 31.95           C  
ANISOU 2193  CG2 VAL A 281     4370   3925   3844    192    726    -38       C  
ATOM   2194  N   ILE A 282      -2.984   8.465  41.610  1.00 26.51           N  
ANISOU 2194  N   ILE A 282     3429   3231   3412    314    624    125       N  
ATOM   2195  CA  ILE A 282      -3.088   8.582  40.157  1.00 26.62           C  
ANISOU 2195  CA  ILE A 282     3402   3237   3477    321    580    146       C  
ATOM   2196  C   ILE A 282      -4.484   9.019  39.703  1.00 30.13           C  
ANISOU 2196  C   ILE A 282     3779   3697   3971    385    628    232       C  
ATOM   2197  O   ILE A 282      -4.623   9.639  38.639  1.00 31.86           O  
ANISOU 2197  O   ILE A 282     3980   3904   4222    406    625    253       O  
ATOM   2198  CB  ILE A 282      -2.645   7.240  39.542  1.00 28.26           C  
ANISOU 2198  CB  ILE A 282     3563   3471   3702    259    478    149       C  
ATOM   2199  CG1 ILE A 282      -1.169   6.990  39.869  1.00 27.88           C  
ANISOU 2199  CG1 ILE A 282     3574   3403   3616    208    442     81       C  
ATOM   2200  CG2 ILE A 282      -2.860   7.207  38.032  1.00 29.48           C  
ANISOU 2200  CG2 ILE A 282     3676   3628   3897    252    430    173       C  
ATOM   2201  CD1 ILE A 282      -0.661   5.667  39.359  1.00 29.16           C  
ANISOU 2201  CD1 ILE A 282     3700   3576   3802    157    365     85       C  
ATOM   2202  N   ARG A 283      -5.524   8.755  40.497  1.00 28.87           N  
ANISOU 2202  N   ARG A 283     3578   3571   3821    419    677    294       N  
ATOM   2203  CA  ARG A 283      -6.870   9.211  40.142  1.00 29.30           C  
ANISOU 2203  CA  ARG A 283     3557   3647   3927    487    732    397       C  
ATOM   2204  C   ARG A 283      -6.996  10.730  40.105  1.00 33.87           C  
ANISOU 2204  C   ARG A 283     4187   4166   4516    562    841    394       C  
ATOM   2205  O   ARG A 283      -7.997  11.239  39.587  1.00 33.24           O  
ANISOU 2205  O   ARG A 283     4038   4099   4491    624    888    491       O  
ATOM   2206  CB  ARG A 283      -7.900   8.653  41.121  1.00 28.51           C  
ANISOU 2206  CB  ARG A 283     3405   3593   3834    514    774    468       C  
ATOM   2207  CG  ARG A 283      -7.783   9.214  42.527  1.00 31.00           C  
ANISOU 2207  CG  ARG A 283     3805   3875   4100    550    881    422       C  
ATOM   2208  CD  ARG A 283      -8.708   8.468  43.477  1.00 31.53           C  
ANISOU 2208  CD  ARG A 283     3814   3998   4169    567    908    492       C  
ATOM   2209  NE  ARG A 283      -8.425   8.774  44.876  1.00 37.05           N  
ANISOU 2209  NE  ARG A 283     4602   4676   4799    577    992    434       N  
ATOM   2210  CZ  ARG A 283      -9.037   8.187  45.903  1.00 41.25           C  
ANISOU 2210  CZ  ARG A 283     5106   5254   5314    587   1025    478       C  
ATOM   2211  NH1 ARG A 283      -8.715   8.515  47.148  1.00 38.21           N  
ANISOU 2211  NH1 ARG A 283     4813   4853   4852    586   1101    417       N  
ATOM   2212  NH2 ARG A 283      -9.973   7.269  45.681  1.00 36.12           N  
ANISOU 2212  NH2 ARG A 283     4336   4669   4719    591    981    583       N  
ATOM   2213  N   HIS A 284      -6.026  11.468  40.634  1.00 31.95           N  
ANISOU 2213  N   HIS A 284     4059   3857   4223    555    885    293       N  
ATOM   2214  CA  HIS A 284      -6.069  12.922  40.557  1.00 29.17           C  
ANISOU 2214  CA  HIS A 284     3769   3431   3883    619    994    280       C  
ATOM   2215  C   HIS A 284      -5.420  13.458  39.289  1.00 29.14           C  
ANISOU 2215  C   HIS A 284     3769   3400   3904    604    944    262       C  
ATOM   2216  O   HIS A 284      -5.286  14.678  39.133  1.00 32.87           O  
ANISOU 2216  O   HIS A 284     4299   3802   4389    649   1026    245       O  
ATOM   2217  CB  HIS A 284      -5.430  13.523  41.808  1.00 31.53           C  
ANISOU 2217  CB  HIS A 284     4202   3670   4109    607   1076    181       C  
ATOM   2218  CG  HIS A 284      -6.181  13.194  43.058  1.00 34.73           C  
ANISOU 2218  CG  HIS A 284     4610   4099   4487    634   1149    206       C  
ATOM   2219  ND1 HIS A 284      -7.371  13.805  43.392  1.00 39.08           N  
ANISOU 2219  ND1 HIS A 284     5140   4629   5077    731   1282    280       N  
ATOM   2220  CD2 HIS A 284      -5.939  12.281  44.029  1.00 33.27           C  
ANISOU 2220  CD2 HIS A 284     4435   3961   4244    579   1112    178       C  
ATOM   2221  CE1 HIS A 284      -7.817  13.299  44.529  1.00 41.05           C  
ANISOU 2221  CE1 HIS A 284     5396   4913   5290    734   1324    290       C  
ATOM   2222  NE2 HIS A 284      -6.965  12.375  44.937  1.00 35.02           N  
ANISOU 2222  NE2 HIS A 284     4650   4193   4465    640   1219    228       N  
ATOM   2223  N   THR A 285      -5.029  12.579  38.379  1.00 28.88           N  
ANISOU 2223  N   THR A 285     3680   3416   3878    544    819    266       N  
ATOM   2224  CA  THR A 285      -4.695  13.005  37.032  1.00 26.27           C  
ANISOU 2224  CA  THR A 285     3327   3078   3576    538    773    276       C  
ATOM   2225  C   THR A 285      -5.932  13.585  36.367  1.00 33.07           C  
ANISOU 2225  C   THR A 285     4099   3961   4503    609    824    399       C  
ATOM   2226  O   THR A 285      -7.010  12.990  36.430  1.00 34.13           O  
ANISOU 2226  O   THR A 285     4142   4159   4665    624    819    493       O  
ATOM   2227  CB  THR A 285      -4.179  11.812  36.231  1.00 27.47           C  
ANISOU 2227  CB  THR A 285     3439   3282   3718    457    641    262       C  
ATOM   2228  OG1 THR A 285      -2.982  11.317  36.842  1.00 28.31           O  
ANISOU 2228  OG1 THR A 285     3617   3367   3773    400    603    165       O  
ATOM   2229  CG2 THR A 285      -3.907  12.211  34.787  1.00 30.13           C  
ANISOU 2229  CG2 THR A 285     3750   3622   4077    447    594    278       C  
ATOM   2230  N   GLN A 286      -5.787  14.748  35.742  1.00 32.32           N  
ANISOU 2230  N   GLN A 286     4023   3817   4438    653    874    410       N  
ATOM   2231  CA  GLN A 286      -6.930  15.337  35.052  1.00 40.62           C  
ANISOU 2231  CA  GLN A 286     4978   4896   5560    723    924    547       C  
ATOM   2232  C   GLN A 286      -7.409  14.388  33.957  1.00 40.68           C  
ANISOU 2232  C   GLN A 286     4868   5011   5580    667    802    629       C  
ATOM   2233  O   GLN A 286      -6.590  13.828  33.218  1.00 35.23           O  
ANISOU 2233  O   GLN A 286     4192   4340   4855    588    696    568       O  
ATOM   2234  CB  GLN A 286      -6.576  16.698  34.452  1.00 45.76           C  
ANISOU 2234  CB  GLN A 286     5666   5477   6245    773    989    548       C  
ATOM   2235  CG  GLN A 286      -6.207  17.754  35.477  1.00 60.36           C  
ANISOU 2235  CG  GLN A 286     7640   7209   8083    823   1125    471       C  
ATOM   2236  CD  GLN A 286      -7.266  18.826  35.621  1.00 75.71           C  
ANISOU 2236  CD  GLN A 286     9557   9106  10103    941   1280    577       C  
ATOM   2237  OE1 GLN A 286      -8.376  18.563  36.090  1.00 85.04           O  
ANISOU 2237  OE1 GLN A 286    10670  10325  11316    995   1338    671       O  
ATOM   2238  NE2 GLN A 286      -6.929  20.045  35.214  1.00 78.74           N  
ANISOU 2238  NE2 GLN A 286     9991   9405  10523    984   1356    571       N  
ATOM   2239  N   PRO A 287      -8.720  14.187  33.821  1.00 48.50           N  
ANISOU 2239  N   PRO A 287     5742   6070   6614    700    817    769       N  
ATOM   2240  CA  PRO A 287      -9.213  13.118  32.934  1.00 46.57           C  
ANISOU 2240  CA  PRO A 287     5395   5934   6364    619    693    840       C  
ATOM   2241  C   PRO A 287      -8.790  13.267  31.479  1.00 44.24           C  
ANISOU 2241  C   PRO A 287     5076   5672   6061    566    609    848       C  
ATOM   2242  O   PRO A 287      -8.749  12.260  30.763  1.00 84.18           O  
ANISOU 2242  O   PRO A 287    10100  10798  11085    470    494    845       O  
ATOM   2243  CB  PRO A 287     -10.740  13.206  33.093  1.00 46.38           C  
ANISOU 2243  CB  PRO A 287     5247   5977   6398    678    746   1012       C  
ATOM   2244  CG  PRO A 287     -10.996  14.584  33.650  1.00 48.82           C  
ANISOU 2244  CG  PRO A 287     5585   6206   6758    805    907   1047       C  
ATOM   2245  CD  PRO A 287      -9.812  14.904  34.503  1.00 51.56           C  
ANISOU 2245  CD  PRO A 287     6090   6443   7058    807    954    874       C  
ATOM   2246  N   GLN A 288      -8.453  14.470  31.019  1.00 35.03           N  
ANISOU 2246  N   GLN A 288     3932   4457   4921    622    665    855       N  
ATOM   2247  CA  GLN A 288      -7.983  14.674  29.653  1.00 36.41           C  
ANISOU 2247  CA  GLN A 288     4088   4663   5085    574    590    862       C  
ATOM   2248  C   GLN A 288      -6.478  14.500  29.512  1.00 39.14           C  
ANISOU 2248  C   GLN A 288     4548   4947   5375    519    541    702       C  
ATOM   2249  O   GLN A 288      -5.963  14.545  28.388  1.00 34.39           O  
ANISOU 2249  O   GLN A 288     3941   4371   4754    472    475    692       O  
ATOM   2250  CB  GLN A 288      -8.377  16.071  29.162  1.00 39.09           C  
ANISOU 2250  CB  GLN A 288     4382   4983   5488    663    677    966       C  
ATOM   2251  CG  GLN A 288      -9.794  16.477  29.540  1.00 60.45           C  
ANISOU 2251  CG  GLN A 288     6982   7723   8264    749    768   1132       C  
ATOM   2252  CD  GLN A 288     -10.857  15.571  28.925  1.00 74.27           C  
ANISOU 2252  CD  GLN A 288     8593   9616  10011    685    673   1269       C  
ATOM   2253  OE1 GLN A 288     -11.928  15.371  29.503  1.00 76.62           O  
ANISOU 2253  OE1 GLN A 288     8812   9955  10346    725    718   1377       O  
ATOM   2254  NE2 GLN A 288     -10.570  15.032  27.739  1.00 76.44           N  
ANISOU 2254  NE2 GLN A 288     8837   9969  10237    578    545   1266       N  
ATOM   2255  N   LYS A 289      -5.757  14.312  30.617  1.00 30.89           N  
ANISOU 2255  N   LYS A 289     3602   3831   4305    523    573    587       N  
ATOM   2256  CA  LYS A 289      -4.301  14.300  30.595  1.00 29.46           C  
ANISOU 2256  CA  LYS A 289     3523   3589   4080    482    540    453       C  
ATOM   2257  C   LYS A 289      -3.704  12.896  30.560  1.00 28.59           C  
ANISOU 2257  C   LYS A 289     3433   3509   3921    392    442    380       C  
ATOM   2258  O   LYS A 289      -2.475  12.769  30.463  1.00 29.04           O  
ANISOU 2258  O   LYS A 289     3562   3526   3946    356    411    285       O  
ATOM   2259  CB  LYS A 289      -3.751  15.058  31.813  1.00 34.39           C  
ANISOU 2259  CB  LYS A 289     4248   4118   4700    530    635    376       C  
ATOM   2260  CG  LYS A 289      -4.082  16.546  31.813  1.00 40.93           C  
ANISOU 2260  CG  LYS A 289     5088   4885   5578    617    748    423       C  
ATOM   2261  CD  LYS A 289      -3.572  17.211  30.541  1.00 45.80           C  
ANISOU 2261  CD  LYS A 289     5691   5499   6210    611    716    440       C  
ATOM   2262  CE  LYS A 289      -2.681  18.404  30.839  1.00 52.60           C  
ANISOU 2262  CE  LYS A 289     6656   6254   7075    640    789    367       C  
ATOM   2263  NZ  LYS A 289      -2.146  19.008  29.578  1.00 51.07           N  
ANISOU 2263  NZ  LYS A 289     6444   6062   6898    633    752    388       N  
ATOM   2264  N   PHE A 290      -4.530  11.843  30.661  1.00 31.63           N  
ANISOU 2264  N   PHE A 290     3756   3958   4304    356    400    429       N  
ATOM   2265  CA  PHE A 290      -4.023  10.477  30.555  1.00 28.13           C  
ANISOU 2265  CA  PHE A 290     3334   3532   3824    270    317    366       C  
ATOM   2266  C   PHE A 290      -3.511  10.229  29.142  1.00 30.40           C  
ANISOU 2266  C   PHE A 290     3620   3844   4085    207    244    348       C  
ATOM   2267  O   PHE A 290      -4.280  10.281  28.176  1.00 34.67           O  
ANISOU 2267  O   PHE A 290     4092   4453   4629    181    209    430       O  
ATOM   2268  CB  PHE A 290      -5.113   9.452  30.874  1.00 28.06           C  
ANISOU 2268  CB  PHE A 290     3256   3585   3822    239    290    431       C  
ATOM   2269  CG  PHE A 290      -5.325   9.205  32.332  1.00 32.50           C  
ANISOU 2269  CG  PHE A 290     3836   4123   4391    275    343    419       C  
ATOM   2270  CD1 PHE A 290      -6.158  10.039  33.067  1.00 42.18           C  
ANISOU 2270  CD1 PHE A 290     5033   5344   5648    358    432    486       C  
ATOM   2271  CD2 PHE A 290      -4.737   8.120  32.960  1.00 34.50           C  
ANISOU 2271  CD2 PHE A 290     4130   4359   4621    228    310    350       C  
ATOM   2272  CE1 PHE A 290      -6.384   9.806  34.409  1.00 46.76           C  
ANISOU 2272  CE1 PHE A 290     5632   5908   6225    388    486    474       C  
ATOM   2273  CE2 PHE A 290      -4.949   7.885  34.304  1.00 37.71           C  
ANISOU 2273  CE2 PHE A 290     4547   4755   5028    257    355    346       C  
ATOM   2274  CZ  PHE A 290      -5.773   8.733  35.032  1.00 48.22           C  
ANISOU 2274  CZ  PHE A 290     5856   6086   6379    334    442    404       C  
ATOM   2275  N   ILE A 291      -2.227   9.930  29.031  1.00 23.68           N  
ANISOU 2275  N   ILE A 291     2845   2946   3207    176    221    249       N  
ATOM   2276  CA  ILE A 291      -1.577   9.604  27.770  1.00 28.52           C  
ANISOU 2276  CA  ILE A 291     3475   3571   3790    117    162    216       C  
ATOM   2277  C   ILE A 291      -1.251   8.118  27.783  1.00 29.93           C  
ANISOU 2277  C   ILE A 291     3681   3747   3945     44    116    163       C  
ATOM   2278  O   ILE A 291      -0.768   7.604  28.794  1.00 30.50           O  
ANISOU 2278  O   ILE A 291     3789   3778   4023     53    134    117       O  
ATOM   2279  CB  ILE A 291      -0.307  10.462  27.593  1.00 29.67           C  
ANISOU 2279  CB  ILE A 291     3684   3658   3931    147    185    154       C  
ATOM   2280  CG1 ILE A 291      -0.691  11.907  27.262  1.00 35.55           C  
ANISOU 2280  CG1 ILE A 291     4399   4404   4703    209    229    215       C  
ATOM   2281  CG2 ILE A 291       0.613   9.891  26.549  1.00 29.76           C  
ANISOU 2281  CG2 ILE A 291     3730   3668   3909     89    136    101       C  
ATOM   2282  CD1 ILE A 291      -1.484  12.027  25.986  1.00 45.96           C  
ANISOU 2282  CD1 ILE A 291     5644   5799   6018    183    190    301       C  
ATOM   2283  N   ASN A 292      -1.521   7.424  26.672  1.00 25.39           N  
ANISOU 2283  N   ASN A 292     3091   3214   3340    -32     60    172       N  
ATOM   2284  CA  ASN A 292      -1.048   6.042  26.496  1.00 24.37           C  
ANISOU 2284  CA  ASN A 292     3009   3061   3189   -105     29    108       C  
ATOM   2285  C   ASN A 292      -0.086   6.047  25.308  1.00 26.43           C  
ANISOU 2285  C   ASN A 292     3323   3305   3415   -140     12     53       C  
ATOM   2286  O   ASN A 292      -0.518   6.029  24.149  1.00 26.57           O  
ANISOU 2286  O   ASN A 292     3325   3376   3395   -199    -26     77       O  
ATOM   2287  CB  ASN A 292      -2.203   5.062  26.278  1.00 26.16           C  
ANISOU 2287  CB  ASN A 292     3193   3343   3403   -182    -15    155       C  
ATOM   2288  CG  ASN A 292      -1.754   3.603  26.330  1.00 26.58           C  
ANISOU 2288  CG  ASN A 292     3303   3349   3445   -250    -28     87       C  
ATOM   2289  OD1 ASN A 292      -0.767   3.267  26.994  1.00 27.85           O  
ANISOU 2289  OD1 ASN A 292     3514   3442   3627   -217      5     27       O  
ATOM   2290  ND2 ASN A 292      -2.482   2.729  25.628  1.00 30.35           N  
ANISOU 2290  ND2 ASN A 292     3774   3865   3892   -350    -75    102       N  
ATOM   2291  N   TYR A 293       1.218   6.080  25.601  1.00 23.66           N  
ANISOU 2291  N   TYR A 293     3031   2887   3072   -107     41    -14       N  
ATOM   2292  CA  TYR A 293       2.234   6.340  24.583  1.00 22.64           C  
ANISOU 2292  CA  TYR A 293     2946   2738   2916   -116     40    -57       C  
ATOM   2293  C   TYR A 293       2.907   5.034  24.203  1.00 24.49           C  
ANISOU 2293  C   TYR A 293     3241   2929   3134   -171     41   -121       C  
ATOM   2294  O   TYR A 293       3.560   4.410  25.062  1.00 24.77           O  
ANISOU 2294  O   TYR A 293     3302   2909   3199   -151     69   -151       O  
ATOM   2295  CB  TYR A 293       3.273   7.330  25.105  1.00 25.37           C  
ANISOU 2295  CB  TYR A 293     3313   3041   3286    -44     75    -76       C  
ATOM   2296  CG  TYR A 293       4.182   7.912  24.049  1.00 23.48           C  
ANISOU 2296  CG  TYR A 293     3101   2794   3025    -41     75    -97       C  
ATOM   2297  CD1 TYR A 293       3.786   9.012  23.297  1.00 27.02           C  
ANISOU 2297  CD1 TYR A 293     3517   3285   3465    -27     66    -52       C  
ATOM   2298  CD2 TYR A 293       5.451   7.379  23.812  1.00 26.92           C  
ANISOU 2298  CD2 TYR A 293     3590   3183   3457    -48     90   -151       C  
ATOM   2299  CE1 TYR A 293       4.612   9.563  22.340  1.00 28.31           C  
ANISOU 2299  CE1 TYR A 293     3701   3445   3610    -24     65    -66       C  
ATOM   2300  CE2 TYR A 293       6.288   7.928  22.842  1.00 30.29           C  
ANISOU 2300  CE2 TYR A 293     4038   3605   3864    -42     93   -164       C  
ATOM   2301  CZ  TYR A 293       5.859   9.019  22.110  1.00 32.37           C  
ANISOU 2301  CZ  TYR A 293     4271   3914   4115    -33     78   -124       C  
ATOM   2302  OH  TYR A 293       6.676   9.589  21.150  1.00 35.41           O  
ANISOU 2302  OH  TYR A 293     4673   4300   4481    -27     80   -131       O  
ATOM   2303  N   PRO A 294       2.785   4.584  22.957  1.00 26.31           N  
ANISOU 2303  N   PRO A 294     3499   3181   3318   -243     18   -139       N  
ATOM   2304  CA  PRO A 294       3.429   3.329  22.567  1.00 27.58           C  
ANISOU 2304  CA  PRO A 294     3732   3283   3463   -294     39   -206       C  
ATOM   2305  C   PRO A 294       4.939   3.492  22.546  1.00 29.76           C  
ANISOU 2305  C   PRO A 294     4054   3496   3758   -239     85   -248       C  
ATOM   2306  O   PRO A 294       5.470   4.551  22.205  1.00 26.13           O  
ANISOU 2306  O   PRO A 294     3583   3051   3293   -196     87   -237       O  
ATOM   2307  CB  PRO A 294       2.879   3.077  21.161  1.00 33.48           C  
ANISOU 2307  CB  PRO A 294     4502   4080   4139   -390      4   -214       C  
ATOM   2308  CG  PRO A 294       2.678   4.454  20.616  1.00 31.53           C  
ANISOU 2308  CG  PRO A 294     4203   3902   3875   -359    -21   -161       C  
ATOM   2309  CD  PRO A 294       2.278   5.329  21.793  1.00 28.02           C  
ANISOU 2309  CD  PRO A 294     3688   3469   3489   -274    -16   -102       C  
ATOM   2310  N   LEU A 295       5.636   2.425  22.918  1.00 25.58           N  
ANISOU 2310  N   LEU A 295     3569   2895   3256   -239    127   -285       N  
ATOM   2311  CA  LEU A 295       7.094   2.428  22.944  1.00 28.34           C  
ANISOU 2311  CA  LEU A 295     3951   3185   3631   -187    177   -307       C  
ATOM   2312  C   LEU A 295       7.573   1.707  21.691  1.00 32.33           C  
ANISOU 2312  C   LEU A 295     4532   3652   4099   -234    212   -360       C  
ATOM   2313  O   LEU A 295       7.516   0.476  21.606  1.00 30.96           O  
ANISOU 2313  O   LEU A 295     4409   3424   3932   -276    247   -394       O  
ATOM   2314  CB  LEU A 295       7.609   1.777  24.223  1.00 28.85           C  
ANISOU 2314  CB  LEU A 295     4005   3200   3757   -147    209   -294       C  
ATOM   2315  CG  LEU A 295       7.067   2.452  25.497  1.00 35.07           C  
ANISOU 2315  CG  LEU A 295     4730   4028   4566   -112    179   -249       C  
ATOM   2316  CD1 LEU A 295       7.451   1.676  26.739  1.00 36.42           C  
ANISOU 2316  CD1 LEU A 295     4887   4163   4786    -90    204   -230       C  
ATOM   2317  CD2 LEU A 295       7.541   3.899  25.605  1.00 36.44           C  
ANISOU 2317  CD2 LEU A 295     4881   4231   4734    -63    167   -230       C  
ATOM   2318  N   LEU A 296       8.012   2.480  20.701  1.00 25.39           N  
ANISOU 2318  N   LEU A 296     3666   2799   3181   -229    209   -367       N  
ATOM   2319  CA  LEU A 296       8.468   1.925  19.434  1.00 28.67           C  
ANISOU 2319  CA  LEU A 296     4160   3185   3549   -274    248   -420       C  
ATOM   2320  C   LEU A 296       9.989   1.979  19.378  1.00 30.94           C  
ANISOU 2320  C   LEU A 296     4470   3414   3872   -204    315   -424       C  
ATOM   2321  O   LEU A 296      10.614   2.884  19.931  1.00 33.82           O  
ANISOU 2321  O   LEU A 296     4784   3794   4273   -136    305   -382       O  
ATOM   2322  CB  LEU A 296       7.872   2.697  18.254  1.00 33.24           C  
ANISOU 2322  CB  LEU A 296     4733   3846   4049   -327    199   -416       C  
ATOM   2323  CG  LEU A 296       6.366   2.995  18.333  1.00 37.24           C  
ANISOU 2323  CG  LEU A 296     5184   4437   4527   -383    123   -375       C  
ATOM   2324  CD1 LEU A 296       5.955   3.969  17.239  1.00 38.14           C  
ANISOU 2324  CD1 LEU A 296     5271   4643   4577   -416     77   -343       C  
ATOM   2325  CD2 LEU A 296       5.542   1.721  18.249  1.00 33.94           C  
ANISOU 2325  CD2 LEU A 296     4809   4005   4081   -480    117   -407       C  
ATOM   2326  N   ASN A 297      10.592   1.002  18.711  1.00 29.23           N  
ANISOU 2326  N   ASN A 297     4334   3128   3646   -223    388   -472       N  
ATOM   2327  CA  ASN A 297      12.044   0.943  18.599  1.00 28.77           C  
ANISOU 2327  CA  ASN A 297     4294   3012   3627   -152    464   -463       C  
ATOM   2328  C   ASN A 297      12.457   1.375  17.197  1.00 30.45           C  
ANISOU 2328  C   ASN A 297     4553   3243   3773   -170    484   -492       C  
ATOM   2329  O   ASN A 297      12.091   0.726  16.208  1.00 30.12           O  
ANISOU 2329  O   ASN A 297     4593   3185   3664   -244    511   -553       O  
ATOM   2330  CB  ASN A 297      12.553  -0.461  18.918  1.00 29.00           C  
ANISOU 2330  CB  ASN A 297     4374   2935   3708   -141    556   -481       C  
ATOM   2331  CG  ASN A 297      12.395  -0.800  20.394  1.00 34.22           C  
ANISOU 2331  CG  ASN A 297     4974   3584   4446   -108    541   -432       C  
ATOM   2332  OD1 ASN A 297      12.416   0.091  21.244  1.00 36.83           O  
ANISOU 2332  OD1 ASN A 297     5225   3970   4798    -69    483   -380       O  
ATOM   2333  ND2 ASN A 297      12.210  -2.077  20.699  1.00 34.71           N  
ANISOU 2333  ND2 ASN A 297     5077   3571   4543   -129    595   -451       N  
ATOM   2334  N   HIS A 298      13.231   2.455  17.119  1.00 26.65           N  
ANISOU 2334  N   HIS A 298     4025   2797   3304   -110    471   -448       N  
ATOM   2335  CA  HIS A 298      13.701   2.992  15.850  1.00 29.41           C  
ANISOU 2335  CA  HIS A 298     4406   3173   3596   -116    488   -462       C  
ATOM   2336  C   HIS A 298      15.137   2.547  15.598  1.00 26.74           C  
ANISOU 2336  C   HIS A 298     4102   2762   3297    -53    591   -455       C  
ATOM   2337  O   HIS A 298      15.992   2.663  16.482  1.00 31.50           O  
ANISOU 2337  O   HIS A 298     4652   3339   3977     20    610   -397       O  
ATOM   2338  CB  HIS A 298      13.621   4.520  15.852  1.00 29.11           C  
ANISOU 2338  CB  HIS A 298     4291   3218   3551    -90    412   -410       C  
ATOM   2339  CG  HIS A 298      12.247   5.055  16.137  1.00 33.19           C  
ANISOU 2339  CG  HIS A 298     4762   3805   4044   -134    325   -397       C  
ATOM   2340  ND1 HIS A 298      11.436   5.586  15.154  1.00 38.13           N  
ANISOU 2340  ND1 HIS A 298     5384   4507   4595   -193    276   -397       N  
ATOM   2341  CD2 HIS A 298      11.541   5.137  17.291  1.00 34.62           C  
ANISOU 2341  CD2 HIS A 298     4893   3995   4267   -126    283   -372       C  
ATOM   2342  CE1 HIS A 298      10.291   5.976  15.693  1.00 29.47           C  
ANISOU 2342  CE1 HIS A 298     4231   3461   3503   -214    211   -365       C  
ATOM   2343  NE2 HIS A 298      10.330   5.714  16.988  1.00 35.76           N  
ANISOU 2343  NE2 HIS A 298     5003   4214   4368   -172    218   -355       N  
ATOM   2344  N   LYS A 299      15.408   2.069  14.390  1.00 30.24           N  
ANISOU 2344  N   LYS A 299     4631   3177   3680    -83    658   -507       N  
ATOM   2345  CA  LYS A 299      16.801   1.746  14.115  1.00 33.96           C  
ANISOU 2345  CA  LYS A 299     5128   3582   4194    -10    766   -487       C  
ATOM   2346  C   LYS A 299      17.597   3.023  13.842  1.00 33.90           C  
ANISOU 2346  C   LYS A 299     5055   3636   4191     45    736   -425       C  
ATOM   2347  O   LYS A 299      17.037   4.023  13.374  1.00 29.63           O  
ANISOU 2347  O   LYS A 299     4486   3179   3593     10    655   -423       O  
ATOM   2348  CB  LYS A 299      16.906   0.803  12.923  1.00 47.58           C  
ANISOU 2348  CB  LYS A 299     6979   5244   5853    -55    868   -567       C  
ATOM   2349  CG  LYS A 299      16.483  -0.622  13.250  1.00 58.86           C  
ANISOU 2349  CG  LYS A 299     8485   6577   7302    -94    934   -622       C  
ATOM   2350  CD  LYS A 299      16.728  -1.528  12.069  1.00 68.01           C  
ANISOU 2350  CD  LYS A 299     9787   7659   8397   -137   1055   -706       C  
ATOM   2351  CE  LYS A 299      16.639  -2.988  12.459  1.00 70.92           C  
ANISOU 2351  CE  LYS A 299    10237   7899   8812   -150   1156   -750       C  
ATOM   2352  NZ  LYS A 299      17.167  -3.841  11.354  1.00 76.87           N  
ANISOU 2352  NZ  LYS A 299    11138   8552   9519   -169   1309   -826       N  
ATOM   2353  N   PRO A 300      18.898   3.027  14.144  1.00 36.49           N  
ANISOU 2353  N   PRO A 300     5350   3925   4590    129    800   -361       N  
ATOM   2354  CA  PRO A 300      19.733   4.164  13.736  1.00 31.30           C  
ANISOU 2354  CA  PRO A 300     4640   3320   3933    173    782   -302       C  
ATOM   2355  C   PRO A 300      19.586   4.435  12.250  1.00 28.40           C  
ANISOU 2355  C   PRO A 300     4335   2987   3470    133    799   -351       C  
ATOM   2356  O   PRO A 300      19.413   3.516  11.449  1.00 27.26           O  
ANISOU 2356  O   PRO A 300     4290   2796   3271     95    876   -422       O  
ATOM   2357  CB  PRO A 300      21.152   3.707  14.090  1.00 33.73           C  
ANISOU 2357  CB  PRO A 300     4922   3568   4325    259    878   -229       C  
ATOM   2358  CG  PRO A 300      20.951   2.750  15.218  1.00 35.43           C  
ANISOU 2358  CG  PRO A 300     5128   3726   4607    267    897   -220       C  
ATOM   2359  CD  PRO A 300      19.667   2.031  14.914  1.00 35.08           C  
ANISOU 2359  CD  PRO A 300     5167   3660   4502    188    889   -322       C  
ATOM   2360  N   LEU A 301      19.635   5.716  11.895  1.00 24.45           N  
ANISOU 2360  N   LEU A 301     3779   2566   2944    136    728   -313       N  
ATOM   2361  CA  LEU A 301      19.668   6.128  10.500  1.00 27.20           C  
ANISOU 2361  CA  LEU A 301     4169   2961   3207    107    741   -336       C  
ATOM   2362  C   LEU A 301      21.047   5.859   9.908  1.00 27.08           C  
ANISOU 2362  C   LEU A 301     4178   2901   3210    174    855   -307       C  
ATOM   2363  O   LEU A 301      22.049   5.774  10.622  1.00 32.79           O  
ANISOU 2363  O   LEU A 301     4851   3583   4025    250    895   -237       O  
ATOM   2364  CB  LEU A 301      19.348   7.616  10.372  1.00 23.55           C  
ANISOU 2364  CB  LEU A 301     3628   2593   2728    100    636   -287       C  
ATOM   2365  CG  LEU A 301      18.010   8.098  10.921  1.00 29.03           C  
ANISOU 2365  CG  LEU A 301     4282   3337   3410     49    530   -295       C  
ATOM   2366  CD1 LEU A 301      17.835   9.574  10.598  1.00 31.64           C  
ANISOU 2366  CD1 LEU A 301     4544   3747   3730     52    455   -239       C  
ATOM   2367  CD2 LEU A 301      16.873   7.284  10.326  1.00 33.70           C  
ANISOU 2367  CD2 LEU A 301     4945   3943   3917    -43    525   -369       C  
ATOM   2368  N   ASP A 302      21.099   5.725   8.584  1.00 27.34           N  
ANISOU 2368  N   ASP A 302     4287   2948   3155    142    908   -352       N  
ATOM   2369  CA  ASP A 302      22.395   5.526   7.949  1.00 28.57           C  
ANISOU 2369  CA  ASP A 302     4466   3064   3325    211   1026   -320       C  
ATOM   2370  C   ASP A 302      23.285   6.745   8.139  1.00 34.49           C  
ANISOU 2370  C   ASP A 302     5106   3868   4131    278    981   -212       C  
ATOM   2371  O   ASP A 302      24.503   6.611   8.310  1.00 32.39           O  
ANISOU 2371  O   ASP A 302     4808   3563   3935    359   1058   -140       O  
ATOM   2372  CB  ASP A 302      22.243   5.211   6.468  1.00 31.64           C  
ANISOU 2372  CB  ASP A 302     4964   3464   3592    156   1092   -395       C  
ATOM   2373  CG  ASP A 302      23.580   4.971   5.804  1.00 61.09           C  
ANISOU 2373  CG  ASP A 302     8724   7148   7338    235   1230   -361       C  
ATOM   2374  OD1 ASP A 302      24.050   3.813   5.815  1.00 64.46           O  
ANISOU 2374  OD1 ASP A 302     9229   7468   7793    269   1368   -391       O  
ATOM   2375  OD2 ASP A 302      24.181   5.950   5.309  1.00 62.93           O  
ANISOU 2375  OD2 ASP A 302     8899   7447   7565    270   1208   -295       O  
ATOM   2376  N   HIS A 303      22.697   7.938   8.122  1.00 30.88           N  
ANISOU 2376  N   HIS A 303     4586   3498   3648    243    860   -190       N  
ATOM   2377  CA  HIS A 303      23.437   9.164   8.397  1.00 28.09           C  
ANISOU 2377  CA  HIS A 303     4132   3190   3350    292    807    -92       C  
ATOM   2378  C   HIS A 303      22.441  10.282   8.686  1.00 26.48           C  
ANISOU 2378  C   HIS A 303     3874   3056   3132    245    676    -87       C  
ATOM   2379  O   HIS A 303      21.227  10.126   8.510  1.00 28.01           O  
ANISOU 2379  O   HIS A 303     4100   3277   3266    179    630   -147       O  
ATOM   2380  CB  HIS A 303      24.378   9.522   7.245  1.00 33.28           C  
ANISOU 2380  CB  HIS A 303     4796   3872   3976    327    870    -54       C  
ATOM   2381  CG  HIS A 303      23.691   9.694   5.927  1.00 34.10           C  
ANISOU 2381  CG  HIS A 303     4961   4037   3960    262    863   -113       C  
ATOM   2382  ND1 HIS A 303      23.451   8.640   5.067  1.00 39.06           N  
ANISOU 2382  ND1 HIS A 303     5704   4634   4502    222    953   -200       N  
ATOM   2383  CD2 HIS A 303      23.218  10.800   5.306  1.00 38.04           C  
ANISOU 2383  CD2 HIS A 303     5420   4626   4407    226    780    -90       C  
ATOM   2384  CE1 HIS A 303      22.841   9.088   3.984  1.00 39.51           C  
ANISOU 2384  CE1 HIS A 303     5791   4773   4450    154    916   -229       C  
ATOM   2385  NE2 HIS A 303      22.693  10.395   4.101  1.00 41.14           N  
ANISOU 2385  NE2 HIS A 303     5897   5055   4679    160    811   -157       N  
ATOM   2386  N   TRP A 304      22.972  11.418   9.170  1.00 25.27           N  
ANISOU 2386  N   TRP A 304     3635   2929   3036    279    620     -6       N  
ATOM   2387  CA  TRP A 304      22.155  12.550   9.583  1.00 22.64           C  
ANISOU 2387  CA  TRP A 304     3250   2643   2710    249    514     10       C  
ATOM   2388  C   TRP A 304      22.344  13.799   8.743  1.00 25.46           C  
ANISOU 2388  C   TRP A 304     3565   3062   3045    251    479     62       C  
ATOM   2389  O   TRP A 304      21.537  14.729   8.887  1.00 24.63           O  
ANISOU 2389  O   TRP A 304     3425   2995   2940    226    405     75       O  
ATOM   2390  CB  TRP A 304      22.451  12.966  11.034  1.00 22.06           C  
ANISOU 2390  CB  TRP A 304     3119   2540   2723    271    470     54       C  
ATOM   2391  CG  TRP A 304      22.342  11.893  12.071  1.00 24.59           C  
ANISOU 2391  CG  TRP A 304     3459   2806   3080    273    493     25       C  
ATOM   2392  CD1 TRP A 304      21.826  10.636  11.921  1.00 25.84           C  
ANISOU 2392  CD1 TRP A 304     3681   2930   3208    255    542    -43       C  
ATOM   2393  CD2 TRP A 304      22.760  11.999  13.431  1.00 25.32           C  
ANISOU 2393  CD2 TRP A 304     3506   2872   3241    287    467     67       C  
ATOM   2394  NE1 TRP A 304      21.902   9.951  13.121  1.00 24.27           N  
ANISOU 2394  NE1 TRP A 304     3472   2684   3065    267    550    -39       N  
ATOM   2395  CE2 TRP A 304      22.479  10.768  14.056  1.00 24.30           C  
ANISOU 2395  CE2 TRP A 304     3407   2698   3126    286    502     30       C  
ATOM   2396  CE3 TRP A 304      23.344  13.022  14.181  1.00 23.20           C  
ANISOU 2396  CE3 TRP A 304     3178   2617   3019    292    415    132       C  
ATOM   2397  CZ2 TRP A 304      22.772  10.528  15.400  1.00 24.08           C  
ANISOU 2397  CZ2 TRP A 304     3343   2647   3157    293    487     64       C  
ATOM   2398  CZ3 TRP A 304      23.635  12.785  15.514  1.00 24.82           C  
ANISOU 2398  CZ3 TRP A 304     3357   2800   3273    288    397    159       C  
ATOM   2399  CH2 TRP A 304      23.338  11.553  16.111  1.00 24.98           C  
ANISOU 2399  CH2 TRP A 304     3400   2785   3306    291    431    128       C  
ATOM   2400  N   VAL A 305      23.385  13.869   7.913  1.00 22.77           N  
ANISOU 2400  N   VAL A 305     3225   2732   2694    285    536    101       N  
ATOM   2401  CA  VAL A 305      23.758  15.086   7.199  1.00 22.28           C  
ANISOU 2401  CA  VAL A 305     3114   2726   2626    295    506    167       C  
ATOM   2402  C   VAL A 305      23.457  14.906   5.717  1.00 28.03           C  
ANISOU 2402  C   VAL A 305     3888   3511   3253    266    539    139       C  
ATOM   2403  O   VAL A 305      23.649  13.822   5.151  1.00 26.04           O  
ANISOU 2403  O   VAL A 305     3709   3237   2947    262    621     86       O  
ATOM   2404  CB  VAL A 305      25.247  15.423   7.419  1.00 21.91           C  
ANISOU 2404  CB  VAL A 305     3019   2659   2648    352    539    252       C  
ATOM   2405  CG1 VAL A 305      25.671  16.653   6.603  1.00 23.53           C  
ANISOU 2405  CG1 VAL A 305     3174   2919   2846    360    513    324       C  
ATOM   2406  CG2 VAL A 305      25.515  15.642   8.903  1.00 26.09           C  
ANISOU 2406  CG2 VAL A 305     3505   3147   3263    359    495    284       C  
ATOM   2407  N   SER A 306      22.982  15.976   5.092  1.00 24.09           N  
ANISOU 2407  N   SER A 306     3347   3081   2724    243    480    176       N  
ATOM   2408  CA  SER A 306      22.549  15.931   3.703  1.00 25.14           C  
ANISOU 2408  CA  SER A 306     3514   3290   2750    199    492    159       C  
ATOM   2409  C   SER A 306      23.744  15.895   2.747  1.00 29.02           C  
ANISOU 2409  C   SER A 306     4019   3794   3214    237    570    193       C  
ATOM   2410  O   SER A 306      24.914  16.077   3.132  1.00 26.90           O  
ANISOU 2410  O   SER A 306     3715   3484   3021    301    605    249       O  
ATOM   2411  CB  SER A 306      21.679  17.142   3.407  1.00 27.96           C  
ANISOU 2411  CB  SER A 306     3805   3721   3097    169    404    212       C  
ATOM   2412  OG  SER A 306      22.469  18.310   3.511  1.00 29.34           O  
ANISOU 2412  OG  SER A 306     3908   3895   3344    219    386    301       O  
ATOM   2413  N   SER A 307      23.416  15.708   1.461  1.00 31.76           N  
ANISOU 2413  N   SER A 307     4412   4209   3446    190    593    168       N  
ATOM   2414  CA  SER A 307      24.423  15.515   0.416  1.00 31.26           C  
ANISOU 2414  CA  SER A 307     4382   4163   3333    218    683    185       C  
ATOM   2415  C   SER A 307      25.417  16.669   0.355  1.00 33.00           C  
ANISOU 2415  C   SER A 307     4509   4402   3626    282    668    298       C  
ATOM   2416  O   SER A 307      26.635  16.452   0.290  1.00 34.08           O  
ANISOU 2416  O   SER A 307     4644   4503   3801    346    747    336       O  
ATOM   2417  CB  SER A 307      23.743  15.362  -0.949  1.00 36.73           C  
ANISOU 2417  CB  SER A 307     5132   4947   3877    138    687    146       C  
ATOM   2418  OG  SER A 307      22.752  14.352  -0.936  1.00 46.88           O  
ANISOU 2418  OG  SER A 307     6503   6223   5086     58    689     44       O  
ATOM   2419  N   HIS A 308      24.915  17.907   0.321  1.00 28.54           N  
ANISOU 2419  N   HIS A 308     3865   3896   3082    265    574    362       N  
ATOM   2420  CA  HIS A 308      25.790  19.072   0.285  1.00 28.76           C  
ANISOU 2420  CA  HIS A 308     3807   3938   3183    315    554    470       C  
ATOM   2421  C   HIS A 308      26.230  19.538   1.668  1.00 31.51           C  
ANISOU 2421  C   HIS A 308     4100   4211   3660    352    515    508       C  
ATOM   2422  O   HIS A 308      26.952  20.539   1.760  1.00 30.03           O  
ANISOU 2422  O   HIS A 308     3844   4028   3538    382    491    597       O  
ATOM   2423  CB  HIS A 308      25.118  20.237  -0.447  1.00 29.88           C  
ANISOU 2423  CB  HIS A 308     3890   4170   3295    282    483    531       C  
ATOM   2424  CG  HIS A 308      24.938  20.016  -1.917  1.00 39.91           C  
ANISOU 2424  CG  HIS A 308     5195   5534   4434    242    515    524       C  
ATOM   2425  ND1 HIS A 308      25.890  20.380  -2.847  1.00 47.13           N  
ANISOU 2425  ND1 HIS A 308     6091   6493   5323    274    563    588       N  
ATOM   2426  CD2 HIS A 308      23.912  19.479  -2.618  1.00 47.17           C  
ANISOU 2426  CD2 HIS A 308     6169   6521   5233    164    505    465       C  
ATOM   2427  CE1 HIS A 308      25.456  20.076  -4.058  1.00 46.73           C  
ANISOU 2427  CE1 HIS A 308     6086   6531   5138    217    583    563       C  
ATOM   2428  NE2 HIS A 308      24.261  19.523  -3.946  1.00 47.59           N  
ANISOU 2428  NE2 HIS A 308     6241   6657   5184    144    546    488       N  
ATOM   2429  N   GLY A 309      25.832  18.845   2.733  1.00 27.85           N  
ANISOU 2429  N   GLY A 309     3668   3685   3229    344    508    446       N  
ATOM   2430  CA  GLY A 309      26.352  19.173   4.042  1.00 27.08           C  
ANISOU 2430  CA  GLY A 309     3527   3522   3238    370    479    480       C  
ATOM   2431  C   GLY A 309      25.781  20.448   4.620  1.00 28.17           C  
ANISOU 2431  C   GLY A 309     3610   3661   3430    350    390    517       C  
ATOM   2432  O   GLY A 309      26.426  21.082   5.455  1.00 25.51           O  
ANISOU 2432  O   GLY A 309     3234   3286   3174    363    363    567       O  
ATOM   2433  N   ARG A 310      24.585  20.846   4.195  1.00 26.87           N  
ANISOU 2433  N   ARG A 310     3389   4163   2658    125    -26    711       N  
ATOM   2434  CA  ARG A 310      23.967  22.050   4.734  1.00 25.71           C  
ANISOU 2434  CA  ARG A 310     3359   3802   2609    138   -110    841       C  
ATOM   2435  C   ARG A 310      22.627  21.783   5.413  1.00 26.72           C  
ANISOU 2435  C   ARG A 310     3498   3826   2828    257   -186    712       C  
ATOM   2436  O   ARG A 310      21.900  22.731   5.724  1.00 25.95           O  
ANISOU 2436  O   ARG A 310     3479   3586   2795    309   -273    782       O  
ATOM   2437  CB  ARG A 310      23.838  23.092   3.627  1.00 26.33           C  
ANISOU 2437  CB  ARG A 310     3513   3938   2554    119   -148   1067       C  
ATOM   2438  CG  ARG A 310      25.234  23.582   3.183  1.00 28.15           C  
ANISOU 2438  CG  ARG A 310     3737   4239   2721    -47    -60   1228       C  
ATOM   2439  CD  ARG A 310      25.142  24.739   2.215  1.00 33.20           C  
ANISOU 2439  CD  ARG A 310     4480   4889   3245    -93    -97   1509       C  
ATOM   2440  NE  ARG A 310      26.468  25.185   1.782  1.00 36.34           N  
ANISOU 2440  NE  ARG A 310     4858   5374   3574   -287      6   1670       N  
ATOM   2441  CZ  ARG A 310      27.219  26.071   2.430  1.00 37.91           C  
ANISOU 2441  CZ  ARG A 310     5113   5362   3932   -430     23   1779       C  
ATOM   2442  NH1 ARG A 310      26.783  26.626   3.556  1.00 31.83           N  
ANISOU 2442  NH1 ARG A 310     4425   4277   3394   -384    -64   1734       N  
ATOM   2443  NH2 ARG A 310      28.409  26.408   1.948  1.00 36.18           N  
ANISOU 2443  NH2 ARG A 310     4849   5264   3633   -627    129   1916       N  
ATOM   2444  N   LEU A 311      22.280  20.522   5.648  1.00 24.28           N  
ANISOU 2444  N   LEU A 311     3108   3583   2534    297   -155    520       N  
ATOM   2445  CA  LEU A 311      21.157  20.168   6.507  1.00 23.36           C  
ANISOU 2445  CA  LEU A 311     2983   3373   2519    365   -198    392       C  
ATOM   2446  C   LEU A 311      21.620  19.063   7.431  1.00 24.20           C  
ANISOU 2446  C   LEU A 311     3042   3431   2721    329   -132    268       C  
ATOM   2447  O   LEU A 311      22.342  18.163   7.001  1.00 24.68           O  
ANISOU 2447  O   LEU A 311     3049   3582   2747    305    -73    207       O  
ATOM   2448  CB  LEU A 311      19.935  19.683   5.734  1.00 28.47           C  
ANISOU 2448  CB  LEU A 311     3579   4157   3083    446   -242    289       C  
ATOM   2449  CG  LEU A 311      19.160  20.675   4.885  1.00 39.90           C  
ANISOU 2449  CG  LEU A 311     5068   5665   4427    528   -338    394       C  
ATOM   2450  CD1 LEU A 311      19.726  20.720   3.488  1.00 46.69           C  
ANISOU 2450  CD1 LEU A 311     5918   6723   5097    511   -320    493       C  
ATOM   2451  CD2 LEU A 311      17.704  20.243   4.878  1.00 41.16           C  
ANISOU 2451  CD2 LEU A 311     5158   5895   4587    620   -398    230       C  
ATOM   2452  N   ILE A 312      21.217  19.124   8.697  1.00 20.65           N  
ANISOU 2452  N   ILE A 312     2610   2850   2387    337   -146    230       N  
ATOM   2453  CA  ILE A 312      21.579  18.055   9.632  1.00 18.29           C  
ANISOU 2453  CA  ILE A 312     2281   2502   2166    311    -92    145       C  
ATOM   2454  C   ILE A 312      20.380  17.740  10.521  1.00 23.19           C  
ANISOU 2454  C   ILE A 312     2889   3075   2848    331   -107     64       C  
ATOM   2455  O   ILE A 312      19.701  18.649  11.015  1.00 22.64           O  
ANISOU 2455  O   ILE A 312     2837   2969   2797    363   -157     78       O  
ATOM   2456  CB  ILE A 312      22.825  18.407  10.474  1.00 21.23           C  
ANISOU 2456  CB  ILE A 312     2675   2802   2591    270    -69    210       C  
ATOM   2457  CG1 ILE A 312      23.188  17.218  11.372  1.00 20.90           C  
ANISOU 2457  CG1 ILE A 312     2608   2723   2610    269    -28    142       C  
ATOM   2458  CG2 ILE A 312      22.584  19.655  11.329  1.00 22.79           C  
ANISOU 2458  CG2 ILE A 312     2918   2897   2844    272   -121    263       C  
ATOM   2459  CD1 ILE A 312      24.537  17.349  12.095  1.00 22.46           C  
ANISOU 2459  CD1 ILE A 312     2799   2896   2838    250    -11    181       C  
ATOM   2460  N   LEU A 313      20.085  16.446  10.668  1.00 20.02           N  
ANISOU 2460  N   LEU A 313     2450   2678   2480    310    -64    -30       N  
ATOM   2461  CA  LEU A 313      19.070  15.984  11.604  1.00 24.93           C  
ANISOU 2461  CA  LEU A 313     3049   3266   3156    288    -52    -92       C  
ATOM   2462  C   LEU A 313      19.691  15.843  12.984  1.00 22.15           C  
ANISOU 2462  C   LEU A 313     2731   2831   2855    263    -23    -34       C  
ATOM   2463  O   LEU A 313      20.755  15.227  13.118  1.00 21.62           O  
ANISOU 2463  O   LEU A 313     2684   2718   2813    255      5      0       O  
ATOM   2464  CB  LEU A 313      18.531  14.627  11.161  1.00 23.35           C  
ANISOU 2464  CB  LEU A 313     2803   3081   2989    249    -16   -203       C  
ATOM   2465  CG  LEU A 313      17.993  14.512   9.741  1.00 24.40           C  
ANISOU 2465  CG  LEU A 313     2880   3333   3058    276    -44   -299       C  
ATOM   2466  CD1 LEU A 313      17.738  13.034   9.436  1.00 25.66           C  
ANISOU 2466  CD1 LEU A 313     2993   3467   3288    222     -5   -435       C  
ATOM   2467  CD2 LEU A 313      16.725  15.303   9.592  1.00 26.82           C  
ANISOU 2467  CD2 LEU A 313     3144   3729   3316    315   -100   -337       C  
ATOM   2468  N   ILE A 314      19.037  16.403  14.015  1.00 20.18           N  
ANISOU 2468  N   ILE A 314     2473   2585   2610    264    -35    -35       N  
ATOM   2469  CA  ILE A 314      19.464  16.188  15.392  1.00 19.74           C  
ANISOU 2469  CA  ILE A 314     2433   2497   2570    242     -7     10       C  
ATOM   2470  C   ILE A 314      18.234  15.903  16.246  1.00 20.63           C  
ANISOU 2470  C   ILE A 314     2500   2667   2673    203     21    -38       C  
ATOM   2471  O   ILE A 314      17.090  16.033  15.803  1.00 22.45           O  
ANISOU 2471  O   ILE A 314     2675   2962   2894    201     11   -122       O  
ATOM   2472  CB  ILE A 314      20.260  17.384  15.974  1.00 21.61           C  
ANISOU 2472  CB  ILE A 314     2691   2721   2798    279    -50     50       C  
ATOM   2473  CG1 ILE A 314      19.397  18.649  15.995  1.00 21.80           C  
ANISOU 2473  CG1 ILE A 314     2696   2768   2818    326   -110     -3       C  
ATOM   2474  CG2 ILE A 314      21.592  17.580  15.199  1.00 21.40           C  
ANISOU 2474  CG2 ILE A 314     2693   2659   2778    283    -58    106       C  
ATOM   2475  CD1 ILE A 314      20.038  19.823  16.765  1.00 23.61           C  
ANISOU 2475  CD1 ILE A 314     2941   2960   3071    353   -158      0       C  
ATOM   2476  N   GLY A 315      18.488  15.493  17.489  1.00 20.65           N  
ANISOU 2476  N   GLY A 315     2513   2671   2660    171     58     18       N  
ATOM   2477  CA  GLY A 315      17.393  15.208  18.408  1.00 21.33           C  
ANISOU 2477  CA  GLY A 315     2546   2848   2710    112    104     -9       C  
ATOM   2478  C   GLY A 315      16.613  13.977  17.974  1.00 22.09           C  
ANISOU 2478  C   GLY A 315     2624   2918   2852     13    163    -26       C  
ATOM   2479  O   GLY A 315      17.158  13.033  17.383  1.00 23.15           O  
ANISOU 2479  O   GLY A 315     2810   2932   3054    -10    177      9       O  
ATOM   2480  N   ASP A 316      15.305  14.004  18.244  1.00 21.24           N  
ANISOU 2480  N   ASP A 316     2426   2929   2715    -46    195   -107       N  
ATOM   2481  CA  ASP A 316      14.459  12.858  17.917  1.00 22.20           C  
ANISOU 2481  CA  ASP A 316     2509   3034   2891   -173    259   -142       C  
ATOM   2482  C   ASP A 316      14.256  12.697  16.418  1.00 24.78           C  
ANISOU 2482  C   ASP A 316     2814   3323   3277   -147    219   -252       C  
ATOM   2483  O   ASP A 316      13.810  11.634  15.967  1.00 24.24           O  
ANISOU 2483  O   ASP A 316     2725   3201   3283   -249    260   -300       O  
ATOM   2484  CB  ASP A 316      13.093  12.977  18.594  1.00 20.95           C  
ANISOU 2484  CB  ASP A 316     2227   3058   2674   -256    311   -220       C  
ATOM   2485  CG  ASP A 316      13.100  12.506  20.046  1.00 25.94           C  
ANISOU 2485  CG  ASP A 316     2872   3743   3242   -357    394    -93       C  
ATOM   2486  OD1 ASP A 316      14.212  12.351  20.634  1.00 28.14           O  
ANISOU 2486  OD1 ASP A 316     3257   3931   3504   -319    386     54       O  
ATOM   2487  OD2 ASP A 316      11.991  12.268  20.581  1.00 28.34           O  
ANISOU 2487  OD2 ASP A 316     3069   4201   3499   -475    468   -138       O  
ATOM   2488  N   ALA A 317      14.556  13.724  15.625  1.00 21.06           N  
ANISOU 2488  N   ALA A 317     2346   2882   2772    -19    137   -293       N  
ATOM   2489  CA  ALA A 317      14.527  13.509  14.178  1.00 22.67           C  
ANISOU 2489  CA  ALA A 317     2537   3079   2999     12    100   -374       C  
ATOM   2490  C   ALA A 317      15.593  12.513  13.753  1.00 24.46           C  
ANISOU 2490  C   ALA A 317     2839   3163   3293    -11    122   -326       C  
ATOM   2491  O   ALA A 317      15.411  11.791  12.763  1.00 26.81           O  
ANISOU 2491  O   ALA A 317     3106   3448   3631    -33    121   -426       O  
ATOM   2492  CB  ALA A 317      14.719  14.831  13.431  1.00 23.85           C  
ANISOU 2492  CB  ALA A 317     2694   3287   3083    148      9   -379       C  
ATOM   2493  N   ALA A 318      16.682  12.429  14.513  1.00 21.76           N  
ANISOU 2493  N   ALA A 318     2580   2725   2962      5    136   -199       N  
ATOM   2494  CA  ALA A 318      17.817  11.570  14.197  1.00 23.73           C  
ANISOU 2494  CA  ALA A 318     2895   2847   3276     20    142   -161       C  
ATOM   2495  C   ALA A 318      17.864  10.290  15.021  1.00 27.59           C  
ANISOU 2495  C   ALA A 318     3433   3192   3857    -63    194    -95       C  
ATOM   2496  O   ALA A 318      18.177   9.221  14.477  1.00 28.24           O  
ANISOU 2496  O   ALA A 318     3540   3148   4042    -77    198   -140       O  
ATOM   2497  CB  ALA A 318      19.131  12.339  14.403  1.00 22.80           C  
ANISOU 2497  CB  ALA A 318     2825   2728   3111    110    109    -69       C  
ATOM   2498  N   HIS A 319      17.601  10.348  16.327  1.00 24.00           N  
ANISOU 2498  N   HIS A 319     2999   2751   3369   -114    229     15       N  
ATOM   2499  CA  HIS A 319      17.833   9.189  17.195  1.00 24.19           C  
ANISOU 2499  CA  HIS A 319     3098   2630   3462   -183    271    140       C  
ATOM   2500  C   HIS A 319      16.752   9.080  18.264  1.00 27.57           C  
ANISOU 2500  C   HIS A 319     3497   3136   3843   -315    340    205       C  
ATOM   2501  O   HIS A 319      17.034   9.122  19.465  1.00 27.89           O  
ANISOU 2501  O   HIS A 319     3578   3209   3809   -320    361    352       O  
ATOM   2502  CB  HIS A 319      19.227   9.262  17.820  1.00 24.50           C  
ANISOU 2502  CB  HIS A 319     3215   2618   3474    -75    233    267       C  
ATOM   2503  CG  HIS A 319      19.551  10.597  18.416  1.00 25.63           C  
ANISOU 2503  CG  HIS A 319     3329   2923   3487     -5    206    291       C  
ATOM   2504  ND1 HIS A 319      19.003  11.031  19.605  1.00 27.13           N  
ANISOU 2504  ND1 HIS A 319     3496   3233   3579    -47    235    352       N  
ATOM   2505  CD2 HIS A 319      20.354  11.596  17.981  1.00 24.39           C  
ANISOU 2505  CD2 HIS A 319     3152   2825   3288     93    153    247       C  
ATOM   2506  CE1 HIS A 319      19.450  12.246  19.872  1.00 24.12           C  
ANISOU 2506  CE1 HIS A 319     3083   2963   3117     36    190    322       C  
ATOM   2507  NE2 HIS A 319      20.271  12.613  18.903  1.00 24.94           N  
ANISOU 2507  NE2 HIS A 319     3196   3018   3264    111    142    270       N  
ATOM   2508  N   PRO A 320      15.498   8.901  17.860  1.00 28.62           N  
ANISOU 2508  N   PRO A 320     3542   3329   4004   -428    381     91       N  
ATOM   2509  CA  PRO A 320      14.424   8.839  18.858  1.00 31.20           C  
ANISOU 2509  CA  PRO A 320     3808   3779   4269   -569    461    134       C  
ATOM   2510  C   PRO A 320      14.545   7.608  19.744  1.00 32.40           C  
ANISOU 2510  C   PRO A 320     4055   3777   4479   -702    529    326       C  
ATOM   2511  O   PRO A 320      14.807   6.499  19.269  1.00 30.01           O  
ANISOU 2511  O   PRO A 320     3828   3239   4335   -753    528    347       O  
ATOM   2512  CB  PRO A 320      13.147   8.811  18.011  1.00 31.51           C  
ANISOU 2512  CB  PRO A 320     3715   3911   4348   -656    480    -63       C  
ATOM   2513  CG  PRO A 320      13.572   8.278  16.690  1.00 32.06           C  
ANISOU 2513  CG  PRO A 320     3814   3828   4539   -610    428   -168       C  
ATOM   2514  CD  PRO A 320      15.011   8.676  16.487  1.00 28.16           C  
ANISOU 2514  CD  PRO A 320     3419   3255   4024   -438    358    -95       C  
ATOM   2515  N   LEU A 321      14.340   7.830  21.042  1.00 27.77           N  
ANISOU 2515  N   LEU A 321     3463   3329   3758   -754    582    465       N  
ATOM   2516  CA  LEU A 321      14.343   6.820  22.088  1.00 30.96           C  
ANISOU 2516  CA  LEU A 321     3956   3646   4163   -890    654    697       C  
ATOM   2517  C   LEU A 321      13.021   6.872  22.838  1.00 31.71           C  
ANISOU 2517  C   LEU A 321     3930   3966   4150  -1083    767    703       C  
ATOM   2518  O   LEU A 321      12.311   7.880  22.809  1.00 36.55           O  
ANISOU 2518  O   LEU A 321     4392   4838   4655  -1054    771    533       O  
ATOM   2519  CB  LEU A 321      15.441   7.074  23.126  1.00 40.51           C  
ANISOU 2519  CB  LEU A 321     5259   4887   5246   -763    615    887       C  
ATOM   2520  CG  LEU A 321      16.859   6.565  23.108  1.00 52.43           C  
ANISOU 2520  CG  LEU A 321     6915   6179   6825   -619    532   1013       C  
ATOM   2521  CD1 LEU A 321      17.670   7.262  22.050  1.00 54.36           C  
ANISOU 2521  CD1 LEU A 321     7138   6396   7122   -440    438    836       C  
ATOM   2522  CD2 LEU A 321      17.393   6.856  24.490  1.00 57.78           C  
ANISOU 2522  CD2 LEU A 321     7629   7011   7312   -561    528   1201       C  
ATOM   2523  N   SER A 322      12.731   5.811  23.579  1.00 36.92           N  
ANISOU 2523  N   SER A 322     4658   4538   4833  -1274    857    911       N  
ATOM   2524  CA  SER A 322      11.561   5.851  24.439  1.00 45.68           C  
ANISOU 2524  CA  SER A 322     5644   5910   5804  -1475    983    946       C  
ATOM   2525  C   SER A 322      11.734   6.908  25.535  1.00 38.59           C  
ANISOU 2525  C   SER A 322     4682   5339   4643  -1363    982    979       C  
ATOM   2526  O   SER A 322      12.850   7.173  25.992  1.00 47.12           O  
ANISOU 2526  O   SER A 322     5866   6385   5652  -1195    908   1095       O  
ATOM   2527  CB  SER A 322      11.297   4.476  25.054  1.00 59.24           C  
ANISOU 2527  CB  SER A 322     7466   7451   7592  -1725   1086   1211       C  
ATOM   2528  OG  SER A 322      12.335   4.079  25.932  1.00 70.91           O  
ANISOU 2528  OG  SER A 322     9123   8814   9004  -1646   1055   1506       O  
ATOM   2529  N   PRO A 323      10.642   7.565  25.943  1.00 45.25           N  
ANISOU 2529  N   PRO A 323     5332   6522   5340  -1441   1054    841       N  
ATOM   2530  CA  PRO A 323      10.731   8.500  27.073  1.00 55.14           C  
ANISOU 2530  CA  PRO A 323     6506   8106   6338  -1346   1059    847       C  
ATOM   2531  C   PRO A 323      11.164   7.794  28.350  1.00 66.21           C  
ANISOU 2531  C   PRO A 323     8016   9546   7592  -1438   1127   1172       C  
ATOM   2532  O   PRO A 323      10.336   7.258  29.087  1.00 67.64           O  
ANISOU 2532  O   PRO A 323     8136   9901   7664  -1665   1264   1297       O  
ATOM   2533  CB  PRO A 323       9.306   9.058  27.187  1.00 54.11           C  
ANISOU 2533  CB  PRO A 323     6132   8318   6110  -1448   1140    625       C  
ATOM   2534  CG  PRO A 323       8.433   8.061  26.468  1.00 50.72           C  
ANISOU 2534  CG  PRO A 323     5671   7749   5852  -1683   1222    607       C  
ATOM   2535  CD  PRO A 323       9.286   7.500  25.373  1.00 45.79           C  
ANISOU 2535  CD  PRO A 323     5223   6707   5466  -1603   1125    639       C  
ATOM   2536  N   ALA A 324      12.467   7.769  28.602  1.00 72.01           N  
ANISOU 2536  N   ALA A 324     8909  10134   8316  -1267   1031   1319       N  
ATOM   2537  CA  ALA A 324      13.010   7.114  29.781  1.00 80.45           C  
ANISOU 2537  CA  ALA A 324    10099  11235   9236  -1308   1065   1643       C  
ATOM   2538  C   ALA A 324      14.384   7.699  30.060  1.00 92.75           C  
ANISOU 2538  C   ALA A 324    11734  12781  10724  -1042    928   1659       C  
ATOM   2539  O   ALA A 324      14.886   8.548  29.313  1.00 95.81           O  
ANISOU 2539  O   ALA A 324    12090  13112  11202   -861    824   1434       O  
ATOM   2540  CB  ALA A 324      13.085   5.600  29.598  1.00 79.88           C  
ANISOU 2540  CB  ALA A 324    10206  10805   9340  -1478   1108   1917       C  
ATOM   2541  N   ALA A 325      15.001   7.209  31.136  1.00102.07           N  
ANISOU 2541  N   ALA A 325    13017  14020  11743  -1027    929   1940       N  
ATOM   2542  CA  ALA A 325      16.250   7.782  31.660  1.00103.34           C  
ANISOU 2542  CA  ALA A 325    13216  14265  11783   -785    807   1954       C  
ATOM   2543  C   ALA A 325      16.024   9.288  31.752  1.00103.34           C  
ANISOU 2543  C   ALA A 325    13022  14575  11666   -674    776   1628       C  
ATOM   2544  O   ALA A 325      14.956   9.735  32.194  1.00103.94           O  
ANISOU 2544  O   ALA A 325    12941  14952  11600   -780    869   1516       O  
ATOM   2545  CB  ALA A 325      17.434   7.374  30.798  1.00 93.00           C  
ANISOU 2545  CB  ALA A 325    12057  12575  10702   -628    681   1978       C  
ATOM   2546  N   GLY A 326      16.960  10.090  31.307  1.00 98.77           N  
ANISOU 2546  N   GLY A 326    12443  13925  11159   -469    650   1459       N  
ATOM   2547  CA  GLY A 326      16.625  11.398  30.831  1.00 85.60           C  
ANISOU 2547  CA  GLY A 326    10629  12371   9523   -388    611   1129       C  
ATOM   2548  C   GLY A 326      17.298  11.474  29.491  1.00 67.63           C  
ANISOU 2548  C   GLY A 326     8433   9760   7503   -295    522   1039       C  
ATOM   2549  O   GLY A 326      17.337  12.512  28.820  1.00 45.92           O  
ANISOU 2549  O   GLY A 326     5613   6998   4835   -202    459    804       O  
ATOM   2550  N   GLN A 327      17.820  10.312  29.105  1.00 58.74           N  
ANISOU 2550  N   GLN A 327     7459   8358   6503   -325    517   1241       N  
ATOM   2551  CA  GLN A 327      18.893  10.280  28.131  1.00 42.26           C  
ANISOU 2551  CA  GLN A 327     5453   6005   4597   -194    418   1197       C  
ATOM   2552  C   GLN A 327      18.416  10.643  26.743  1.00 30.77           C  
ANISOU 2552  C   GLN A 327     3957   4409   3326   -213    413    993       C  
ATOM   2553  O   GLN A 327      19.199  11.189  25.965  1.00 31.59           O  
ANISOU 2553  O   GLN A 327     4067   4413   3523    -93    331    878       O  
ATOM   2554  CB  GLN A 327      19.560   8.911  28.122  1.00 52.20           C  
ANISOU 2554  CB  GLN A 327     6875   7012   5946   -196    403   1442       C  
ATOM   2555  CG  GLN A 327      20.860   8.868  28.916  1.00 53.41           C  
ANISOU 2555  CG  GLN A 327     7086   7218   5991    -31    311   1568       C  
ATOM   2556  CD  GLN A 327      21.628  10.197  28.906  1.00 45.24           C  
ANISOU 2556  CD  GLN A 327     5947   6345   4898    121    226   1353       C  
ATOM   2557  OE1 GLN A 327      21.936  10.769  27.837  1.00 35.45           O  
ANISOU 2557  OE1 GLN A 327     4675   4990   3806    171    184   1168       O  
ATOM   2558  NE2 GLN A 327      21.968  10.677  30.108  1.00 30.84           N  
ANISOU 2558  NE2 GLN A 327     4068   4794   2854    187    198   1381       N  
ATOM   2559  N   GLY A 328      17.158  10.348  26.408  1.00 31.81           N  
ANISOU 2559  N   GLY A 328     4036   4552   3499   -365    498    948       N  
ATOM   2560  CA  GLY A 328      16.631  10.795  25.124  1.00 35.58           C  
ANISOU 2560  CA  GLY A 328     4454   4951   4115   -363    481    740       C  
ATOM   2561  C   GLY A 328      16.823  12.283  24.877  1.00 29.27           C  
ANISOU 2561  C   GLY A 328     3569   4271   3280   -224    404    540       C  
ATOM   2562  O   GLY A 328      17.476  12.694  23.904  1.00 30.06           O  
ANISOU 2562  O   GLY A 328     3700   4234   3487   -128    331    461       O  
ATOM   2563  N   ALA A 329      16.249  13.098  25.767  1.00 30.56           N  
ANISOU 2563  N   ALA A 329     3623   4693   3295   -217    421    455       N  
ATOM   2564  CA  ALA A 329      16.432  14.544  25.681  1.00 31.88           C  
ANISOU 2564  CA  ALA A 329     3717   4948   3448    -81    337    261       C  
ATOM   2565  C   ALA A 329      17.893  14.925  25.866  1.00 25.34           C  
ANISOU 2565  C   ALA A 329     2958   4047   2623     39    253    301       C  
ATOM   2566  O   ALA A 329      18.405  15.814  25.168  1.00 23.86           O  
ANISOU 2566  O   ALA A 329     2772   3768   2526    128    175    189       O  
ATOM   2567  CB  ALA A 329      15.574  15.248  26.731  1.00 29.09           C  
ANISOU 2567  CB  ALA A 329     3222   4898   2933    -84    368    141       C  
ATOM   2568  N   SER A 330      18.580  14.258  26.794  1.00 26.56           N  
ANISOU 2568  N   SER A 330     3166   4248   2678     36    267    468       N  
ATOM   2569  CA  SER A 330      19.960  14.635  27.098  1.00 23.90           C  
ANISOU 2569  CA  SER A 330     2861   3895   2324    155    182    481       C  
ATOM   2570  C   SER A 330      20.878  14.412  25.898  1.00 24.13           C  
ANISOU 2570  C   SER A 330     2970   3673   2524    201    132    496       C  
ATOM   2571  O   SER A 330      21.778  15.223  25.636  1.00 23.27           O  
ANISOU 2571  O   SER A 330     2846   3541   2457    283     60    406       O  
ATOM   2572  CB  SER A 330      20.447  13.860  28.320  1.00 25.42           C  
ANISOU 2572  CB  SER A 330     3092   4208   2357    159    198    672       C  
ATOM   2573  OG  SER A 330      19.672  14.168  29.468  1.00 29.12           O  
ANISOU 2573  OG  SER A 330     3467   4969   2629    119    247    646       O  
ATOM   2574  N   GLN A 331      20.670  13.326  25.146  1.00 26.45           N  
ANISOU 2574  N   GLN A 331     3340   3788   2922    139    172    593       N  
ATOM   2575  CA  GLN A 331      21.474  13.134  23.938  1.00 22.87           C  
ANISOU 2575  CA  GLN A 331     2937   3137   2615    188    130    570       C  
ATOM   2576  C   GLN A 331      21.196  14.217  22.911  1.00 22.72           C  
ANISOU 2576  C   GLN A 331     2865   3102   2665    202    102    403       C  
ATOM   2577  O   GLN A 331      22.105  14.620  22.172  1.00 25.05           O  
ANISOU 2577  O   GLN A 331     3170   3324   3025    258     54    362       O  
ATOM   2578  CB  GLN A 331      21.215  11.758  23.315  1.00 23.59           C  
ANISOU 2578  CB  GLN A 331     3107   3042   2816    125    172    665       C  
ATOM   2579  CG  GLN A 331      21.807  10.621  24.122  1.00 22.09           C  
ANISOU 2579  CG  GLN A 331     3006   2785   2602    143    170    861       C  
ATOM   2580  CD  GLN A 331      23.325  10.719  24.207  1.00 26.88           C  
ANISOU 2580  CD  GLN A 331     3631   3375   3207    292     84    876       C  
ATOM   2581  OE1 GLN A 331      24.013  10.818  23.185  1.00 27.99           O  
ANISOU 2581  OE1 GLN A 331     3764   3421   3452    350     47    782       O  
ATOM   2582  NE2 GLN A 331      23.849  10.707  25.420  1.00 27.87           N  
ANISOU 2582  NE2 GLN A 331     3764   3628   3198    352     54    983       N  
ATOM   2583  N   GLY A 332      19.952  14.692  22.844  1.00 22.89           N  
ANISOU 2583  N   GLY A 332     2827   3201   2668    152    131    313       N  
ATOM   2584  CA  GLY A 332      19.643  15.761  21.911  1.00 22.46           C  
ANISOU 2584  CA  GLY A 332     2733   3125   2673    187     87    175       C  
ATOM   2585  C   GLY A 332      20.355  17.045  22.285  1.00 21.45           C  
ANISOU 2585  C   GLY A 332     2580   3039   2529    264     17    101       C  
ATOM   2586  O   GLY A 332      20.805  17.800  21.413  1.00 22.89           O  
ANISOU 2586  O   GLY A 332     2777   3133   2788    297    -33     56       O  
ATOM   2587  N   ILE A 333      20.470  17.308  23.584  1.00 23.88           N  
ANISOU 2587  N   ILE A 333     2846   3491   2736    284     12     88       N  
ATOM   2588  CA  ILE A 333      21.200  18.493  24.004  1.00 25.28           C  
ANISOU 2588  CA  ILE A 333     2988   3702   2914    349    -61    -12       C  
ATOM   2589  C   ILE A 333      22.686  18.347  23.679  1.00 27.58           C  
ANISOU 2589  C   ILE A 333     3323   3903   3253    370    -93     53       C  
ATOM   2590  O   ILE A 333      23.345  19.328  23.307  1.00 25.27           O  
ANISOU 2590  O   ILE A 333     3018   3550   3033    387   -148    -21       O  
ATOM   2591  CB  ILE A 333      20.920  18.772  25.491  1.00 25.75           C  
ANISOU 2591  CB  ILE A 333     2969   3981   2832    372    -60    -75       C  
ATOM   2592  CG1 ILE A 333      19.451  19.216  25.650  1.00 26.07           C  
ANISOU 2592  CG1 ILE A 333     2933   4130   2843    364    -38   -200       C  
ATOM   2593  CG2 ILE A 333      21.889  19.823  26.037  1.00 26.16           C  
ANISOU 2593  CG2 ILE A 333     2979   4070   2889    434   -142   -191       C  
ATOM   2594  CD1 ILE A 333      18.987  19.351  27.068  1.00 35.38           C  
ANISOU 2594  CD1 ILE A 333     4013   5578   3851    375    -15   -272       C  
ATOM   2595  N   GLU A 334      23.238  17.131  23.759  1.00 21.71           N  
ANISOU 2595  N   GLU A 334     2627   3139   2484    366    -63    188       N  
ATOM   2596  CA  GLU A 334      24.613  16.943  23.291  1.00 24.74           C  
ANISOU 2596  CA  GLU A 334     3030   3450   2920    400    -95    222       C  
ATOM   2597  C   GLU A 334      24.735  17.221  21.791  1.00 22.97           C  
ANISOU 2597  C   GLU A 334     2827   3091   2811    373    -93    195       C  
ATOM   2598  O   GLU A 334      25.742  17.784  21.345  1.00 24.04           O  
ANISOU 2598  O   GLU A 334     2941   3205   2990    377   -124    163       O  
ATOM   2599  CB  GLU A 334      25.114  15.534  23.607  1.00 20.20           C  
ANISOU 2599  CB  GLU A 334     2505   2857   2313    430    -78    362       C  
ATOM   2600  CG  GLU A 334      25.359  15.272  25.087  1.00 22.30           C  
ANISOU 2600  CG  GLU A 334     2755   3278   2439    476    -96    427       C  
ATOM   2601  CD  GLU A 334      26.120  13.981  25.326  1.00 29.21           C  
ANISOU 2601  CD  GLU A 334     3693   4104   3302    540   -110    580       C  
ATOM   2602  OE1 GLU A 334      26.974  13.607  24.484  1.00 31.20           O  
ANISOU 2602  OE1 GLU A 334     3959   4242   3653    584   -135    573       O  
ATOM   2603  OE2 GLU A 334      25.869  13.339  26.364  1.00 30.67           O  
ANISOU 2603  OE2 GLU A 334     3911   4371   3373    552   -101    709       O  
ATOM   2604  N   ASP A 335      23.716  16.861  20.998  1.00 21.49           N  
ANISOU 2604  N   ASP A 335     2669   2839   2658    335    -55    203       N  
ATOM   2605  CA  ASP A 335      23.735  17.201  19.572  1.00 21.44           C  
ANISOU 2605  CA  ASP A 335     2675   2748   2723    318    -59    178       C  
ATOM   2606  C   ASP A 335      23.950  18.696  19.379  1.00 21.03           C  
ANISOU 2606  C   ASP A 335     2603   2686   2702    316   -109    115       C  
ATOM   2607  O   ASP A 335      24.825  19.127  18.613  1.00 23.14           O  
ANISOU 2607  O   ASP A 335     2871   2912   3008    297   -121    129       O  
ATOM   2608  CB  ASP A 335      22.425  16.811  18.874  1.00 23.04           C  
ANISOU 2608  CB  ASP A 335     2888   2924   2940    288    -28    161       C  
ATOM   2609  CG  ASP A 335      22.182  15.319  18.789  1.00 23.92           C  
ANISOU 2609  CG  ASP A 335     3028   2995   3067    261     23    212       C  
ATOM   2610  OD1 ASP A 335      23.126  14.500  18.898  1.00 23.95           O  
ANISOU 2610  OD1 ASP A 335     3059   2953   3088    287     26    269       O  
ATOM   2611  OD2 ASP A 335      20.991  14.984  18.588  1.00 24.25           O  
ANISOU 2611  OD2 ASP A 335     3058   3042   3114    216     53    182       O  
ATOM   2612  N   ALA A 336      23.138  19.499  20.064  1.00 22.90           N  
ANISOU 2612  N   ALA A 336     2817   2958   2927    331   -138     43       N  
ATOM   2613  CA  ALA A 336      23.207  20.945  19.909  1.00 23.04           C  
ANISOU 2613  CA  ALA A 336     2829   2917   3008    338   -200    -26       C  
ATOM   2614  C   ALA A 336      24.581  21.467  20.302  1.00 25.83           C  
ANISOU 2614  C   ALA A 336     3160   3266   3390    317   -228    -41       C  
ATOM   2615  O   ALA A 336      25.159  22.302  19.602  1.00 22.55           O  
ANISOU 2615  O   ALA A 336     2760   2757   3050    274   -254    -31       O  
ATOM   2616  CB  ALA A 336      22.132  21.613  20.762  1.00 24.09           C  
ANISOU 2616  CB  ALA A 336     2921   3106   3127    384   -235   -142       C  
ATOM   2617  N   ASN A 337      25.117  20.983  21.428  1.00 22.33           N  
ANISOU 2617  N   ASN A 337     2672   2935   2877    339   -224    -58       N  
ATOM   2618  CA  ASN A 337      26.414  21.451  21.908  1.00 23.23           C  
ANISOU 2618  CA  ASN A 337     2735   3083   3007    326   -258   -104       C  
ATOM   2619  C   ASN A 337      27.536  21.073  20.943  1.00 24.67           C  
ANISOU 2619  C   ASN A 337     2921   3230   3224    283   -232    -30       C  
ATOM   2620  O   ASN A 337      28.376  21.911  20.587  1.00 24.09           O  
ANISOU 2620  O   ASN A 337     2817   3116   3219    219   -251    -61       O  
ATOM   2621  CB  ASN A 337      26.688  20.882  23.301  1.00 23.13           C  
ANISOU 2621  CB  ASN A 337     2671   3238   2879    382   -267   -127       C  
ATOM   2622  CG  ASN A 337      28.074  21.242  23.814  1.00 25.62           C  
ANISOU 2622  CG  ASN A 337     2912   3629   3196    382   -311   -192       C  
ATOM   2623  OD1 ASN A 337      28.939  20.373  23.965  1.00 27.46           O  
ANISOU 2623  OD1 ASN A 337     3124   3936   3374    418   -305   -130       O  
ATOM   2624  ND2 ASN A 337      28.289  22.527  24.094  1.00 26.61           N  
ANISOU 2624  ND2 ASN A 337     2987   3729   3394    346   -365   -333       N  
ATOM   2625  N   VAL A 338      27.577  19.809  20.513  1.00 23.13           N  
ANISOU 2625  N   VAL A 338     2751   3052   2987    312   -186     57       N  
ATOM   2626  CA  VAL A 338      28.644  19.364  19.621  1.00 23.79           C  
ANISOU 2626  CA  VAL A 338     2812   3137   3089    294   -162     94       C  
ATOM   2627  C   VAL A 338      28.562  20.098  18.291  1.00 22.43           C  
ANISOU 2627  C   VAL A 338     2662   2887   2971    214   -143    116       C  
ATOM   2628  O   VAL A 338      29.582  20.509  17.730  1.00 23.97           O  
ANISOU 2628  O   VAL A 338     2812   3107   3190    150   -131    117       O  
ATOM   2629  CB  VAL A 338      28.576  17.840  19.434  1.00 18.76           C  
ANISOU 2629  CB  VAL A 338     2203   2506   2418    359   -130    155       C  
ATOM   2630  CG1 VAL A 338      29.475  17.396  18.271  1.00 23.30           C  
ANISOU 2630  CG1 VAL A 338     2746   3091   3016    353   -103    157       C  
ATOM   2631  CG2 VAL A 338      29.003  17.154  20.711  1.00 20.66           C  
ANISOU 2631  CG2 VAL A 338     2426   2825   2599    439   -159    171       C  
ATOM   2632  N   LEU A 339      27.348  20.276  17.776  1.00 20.87           N  
ANISOU 2632  N   LEU A 339     2529   2618   2783    213   -139    141       N  
ATOM   2633  CA  LEU A 339      27.170  20.977  16.507  1.00 21.66           C  
ANISOU 2633  CA  LEU A 339     2664   2656   2911    156   -133    190       C  
ATOM   2634  C   LEU A 339      27.669  22.412  16.591  1.00 21.89           C  
ANISOU 2634  C   LEU A 339     2691   2613   3014     80   -172    184       C  
ATOM   2635  O   LEU A 339      28.423  22.864  15.720  1.00 21.60           O  
ANISOU 2635  O   LEU A 339     2647   2569   2992     -9   -149    245       O  
ATOM   2636  CB  LEU A 339      25.701  20.929  16.086  1.00 19.56           C  
ANISOU 2636  CB  LEU A 339     2453   2345   2635    196   -144    200       C  
ATOM   2637  CG  LEU A 339      25.374  21.629  14.765  1.00 20.21           C  
ANISOU 2637  CG  LEU A 339     2580   2379   2720    164   -155    269       C  
ATOM   2638  CD1 LEU A 339      26.201  21.104  13.608  1.00 22.18           C  
ANISOU 2638  CD1 LEU A 339     2807   2708   2913    119    -99    327       C  
ATOM   2639  CD2 LEU A 339      23.891  21.471  14.472  1.00 23.78           C  
ANISOU 2639  CD2 LEU A 339     3061   2823   3151    229   -178    248       C  
ATOM   2640  N   ALA A 340      27.272  23.149  17.636  1.00 21.95           N  
ANISOU 2640  N   ALA A 340     2698   2569   3072    104   -229    102       N  
ATOM   2641  CA  ALA A 340      27.721  24.539  17.734  1.00 24.13           C  
ANISOU 2641  CA  ALA A 340     2978   2735   3457     28   -278     73       C  
ATOM   2642  C   ALA A 340      29.228  24.624  17.935  1.00 27.06           C  
ANISOU 2642  C   ALA A 340     3265   3172   3844    -64   -256     49       C  
ATOM   2643  O   ALA A 340      29.887  25.525  17.392  1.00 23.79           O  
ANISOU 2643  O   ALA A 340     2852   2676   3511   -187   -255     87       O  
ATOM   2644  CB  ALA A 340      26.992  25.266  18.868  1.00 22.12           C  
ANISOU 2644  CB  ALA A 340     2720   2428   3257     91   -352    -60       C  
ATOM   2645  N   THR A 341      29.793  23.718  18.741  1.00 21.29           N  
ANISOU 2645  N   THR A 341     2457   2594   3040     -7   -242    -12       N  
ATOM   2646  CA  THR A 341      31.237  23.714  18.935  1.00 20.98           C  
ANISOU 2646  CA  THR A 341     2311   2657   3004    -71   -230    -58       C  
ATOM   2647  C   THR A 341      31.953  23.411  17.629  1.00 21.72           C  
ANISOU 2647  C   THR A 341     2385   2792   3076   -152   -159     37       C  
ATOM   2648  O   THR A 341      32.955  24.063  17.288  1.00 23.16           O  
ANISOU 2648  O   THR A 341     2500   2995   3306   -284   -138     31       O  
ATOM   2649  CB  THR A 341      31.608  22.678  19.996  1.00 21.08           C  
ANISOU 2649  CB  THR A 341     2254   2832   2922     45   -244   -120       C  
ATOM   2650  OG1 THR A 341      30.908  22.997  21.205  1.00 26.23           O  
ANISOU 2650  OG1 THR A 341     2915   3490   3561    110   -300   -205       O  
ATOM   2651  CG2 THR A 341      33.111  22.679  20.253  1.00 25.34           C  
ANISOU 2651  CG2 THR A 341     2661   3509   3460      5   -248   -194       C  
ATOM   2652  N  ASER A 342      31.449  22.422  16.885  0.51 20.04           N  
ANISOU 2652  N  ASER A 342     2216   2609   2788    -83   -118    111       N  
ATOM   2653  N  BSER A 342      31.455  22.415  16.888  0.49 20.01           N  
ANISOU 2653  N  BSER A 342     2212   2607   2785    -83   -118    111       N  
ATOM   2654  CA ASER A 342      32.047  22.073  15.603  0.51 22.30           C  
ANISOU 2654  CA ASER A 342     2469   2975   3028   -142    -50    176       C  
ATOM   2655  CA BSER A 342      32.073  22.039  15.622  0.49 22.44           C  
ANISOU 2655  CA BSER A 342     2485   2998   3045   -139    -49    173       C  
ATOM   2656  C  ASER A 342      32.002  23.244  14.630  0.51 22.67           C  
ANISOU 2656  C  ASER A 342     2564   2936   3115   -288    -29    278       C  
ATOM   2657  C  BSER A 342      32.040  23.189  14.623  0.49 23.09           C  
ANISOU 2657  C  BSER A 342     2611   2997   3163   -286    -27    276       C  
ATOM   2658  O  ASER A 342      32.972  23.495  13.906  0.51 24.90           O  
ANISOU 2658  O  ASER A 342     2775   3308   3377   -410     27    315       O  
ATOM   2659  O  BSER A 342      33.029  23.441  13.925  0.49 23.95           O  
ANISOU 2659  O  BSER A 342     2648   3199   3254   -407     29    310       O  
ATOM   2660  CB ASER A 342      31.336  20.864  15.001  0.51 21.63           C  
ANISOU 2660  CB ASER A 342     2428   2919   2871    -36    -23    205       C  
ATOM   2661  CB BSER A 342      31.375  20.803  15.058  0.49 22.11           C  
ANISOU 2661  CB BSER A 342     2485   2986   2932    -30    -24    200       C  
ATOM   2662  OG ASER A 342      31.954  20.515  13.777  0.51 23.31           O  
ANISOU 2662  OG ASER A 342     2588   3246   3024    -79     40    232       O  
ATOM   2663  OG BSER A 342      31.629  19.677  15.887  0.49 22.06           O  
ANISOU 2663  OG BSER A 342     2441   3040   2902     90    -41    135       O  
ATOM   2664  N  ALEU A 343      30.874  23.959  14.586  0.51 22.68           N  
ANISOU 2664  N  ALEU A 343     2680   2771   3166   -276    -77    331       N  
ATOM   2665  N  BLEU A 343      30.912  23.899  14.546  0.49 21.68           N  
ANISOU 2665  N  BLEU A 343     2550   2654   3034   -276    -72    332       N  
ATOM   2666  CA ALEU A 343      30.756  25.104  13.682  0.51 26.46           C  
ANISOU 2666  CA ALEU A 343     3232   3130   3691   -397    -77    461       C  
ATOM   2667  CA BLEU A 343      30.824  25.060  13.662  0.49 26.39           C  
ANISOU 2667  CA BLEU A 343     3217   3133   3677   -400    -72    460       C  
ATOM   2668  C  ALEU A 343      31.780  26.181  14.020  0.51 27.44           C  
ANISOU 2668  C  ALEU A 343     3311   3188   3927   -561    -81    447       C  
ATOM   2669  C  BLEU A 343      31.873  26.109  14.014  0.49 27.03           C  
ANISOU 2669  C  BLEU A 343     3248   3155   3868   -563    -75    443       C  
ATOM   2670  O  ALEU A 343      32.315  26.845  13.123  0.51 25.06           O  
ANISOU 2670  O  ALEU A 343     3020   2867   3636   -720    -36    575       O  
ATOM   2671  O  BLEU A 343      32.508  26.688  13.124  0.49 27.17           O  
ANISOU 2671  O  BLEU A 343     3260   3176   3887   -725    -23    562       O  
ATOM   2672  CB ALEU A 343      29.338  25.678  13.749  0.51 22.99           C  
ANISOU 2672  CB ALEU A 343     2917   2513   3303   -312   -155    491       C  
ATOM   2673  CB BLEU A 343      29.425  25.670  13.738  0.49 23.24           C  
ANISOU 2673  CB BLEU A 343     2944   2552   3334   -320   -150    491       C  
ATOM   2674  CG ALEU A 343      28.841  26.512  12.563  0.51 30.96           C  
ANISOU 2674  CG ALEU A 343     4036   3412   4317   -364   -171    665       C  
ATOM   2675  CG BLEU A 343      28.253  24.821  13.246  0.49 24.18           C  
ANISOU 2675  CG BLEU A 343     3108   2722   3356   -187   -152    510       C  
ATOM   2676  CD1ALEU A 343      28.403  25.619  11.410  0.51 31.24           C  
ANISOU 2676  CD1ALEU A 343     4077   3600   4191   -308   -122    743       C  
ATOM   2677  CD1BLEU A 343      26.957  25.354  13.842  0.49 26.20           C  
ANISOU 2677  CD1BLEU A 343     3436   2838   3683    -84   -240    460       C  
ATOM   2678  CD2ALEU A 343      27.683  27.362  12.998  0.51 35.04           C  
ANISOU 2678  CD2ALEU A 343     4651   3720   4941   -274   -278    644       C  
ATOM   2679  CD2BLEU A 343      28.178  24.837  11.729  0.49 27.44           C  
ANISOU 2679  CD2BLEU A 343     3559   3191   3675   -232   -113    659       C  
ATOM   2680  N   SER A 344      32.067  26.372  15.309  1.00 24.58           N  
ANISOU 2680  N   SER A 344     2889   2805   3643   -536   -131    293       N  
ATOM   2681  CA  SER A 344      32.987  27.438  15.711  1.00 27.45           C  
ANISOU 2681  CA  SER A 344     3197   3095   4137   -699   -146    239       C  
ATOM   2682  C   SER A 344      34.442  27.056  15.504  1.00 29.15           C  
ANISOU 2682  C   SER A 344     3254   3522   4301   -814    -68    207       C  
ATOM   2683  O   SER A 344      35.282  27.927  15.254  1.00 33.94           O  
ANISOU 2683  O   SER A 344     3811   4091   4994  -1016    -40    228       O  
ATOM   2684  CB  SER A 344      32.759  27.816  17.180  1.00 40.73           C  
ANISOU 2684  CB  SER A 344     4852   4714   5910   -622   -238     48       C  
ATOM   2685  OG  SER A 344      31.441  28.290  17.389  1.00 52.99           O  
ANISOU 2685  OG  SER A 344     6527   6087   7521   -519   -312     48       O  
ATOM   2686  N   LEU A 345      34.764  25.774  15.617  1.00 25.77           N  
ANISOU 2686  N   LEU A 345     2739   3311   3743   -691    -36    148       N  
ATOM   2687  CA  LEU A 345      36.114  25.315  15.348  1.00 26.44           C  
ANISOU 2687  CA  LEU A 345     2655   3625   3766   -763     31     97       C  
ATOM   2688  C   LEU A 345      36.392  25.247  13.852  1.00 29.05           C  
ANISOU 2688  C   LEU A 345     2980   4045   4013   -876    131    242       C  
ATOM   2689  O   LEU A 345      37.532  25.465  13.428  1.00 29.99           O  
ANISOU 2689  O   LEU A 345     2962   4317   4115  -1034    202    230       O  
ATOM   2690  CB  LEU A 345      36.315  23.945  15.992  1.00 28.23           C  
ANISOU 2690  CB  LEU A 345     2803   4027   3896   -558     10    -15       C  
ATOM   2691  CG  LEU A 345      36.317  23.992  17.521  1.00 25.39           C  
ANISOU 2691  CG  LEU A 345     2411   3662   3576   -461    -81   -156       C  
ATOM   2692  CD1 LEU A 345      36.322  22.577  18.114  1.00 26.71           C  
ANISOU 2692  CD1 LEU A 345     2547   3963   3637   -244   -110   -204       C  
ATOM   2693  CD2 LEU A 345      37.505  24.797  18.018  1.00 26.95           C  
ANISOU 2693  CD2 LEU A 345     2455   3938   3846   -604    -93   -283       C  
ATOM   2694  N   ALA A 346      35.365  24.953  13.048  1.00 27.29           N  
ANISOU 2694  N   ALA A 346     2887   3759   3724   -803    140    367       N  
ATOM   2695  CA  ALA A 346      35.553  24.825  11.606  1.00 25.17           C  
ANISOU 2695  CA  ALA A 346     2608   3618   3336   -889    231    499       C  
ATOM   2696  C   ALA A 346      35.586  26.187  10.923  1.00 27.84           C  
ANISOU 2696  C   ALA A 346     3025   3823   3730  -1110    257    684       C  
ATOM   2697  O   ALA A 346      36.321  26.378   9.949  1.00 32.88           O  
ANISOU 2697  O   ALA A 346     3594   4619   4282  -1275    354    784       O  
ATOM   2698  CB  ALA A 346      34.444  23.967  11.003  1.00 25.16           C  
ANISOU 2698  CB  ALA A 346     2702   3624   3235   -721    220    542       C  
ATOM   2699  N   GLY A 347      34.803  27.137  11.418  1.00 32.75           N  
ANISOU 2699  N   GLY A 347     3790   4157   4495  -1115    171    734       N  
ATOM   2700  CA  GLY A 347      34.712  28.442  10.799  1.00 39.23           C  
ANISOU 2700  CA  GLY A 347     4723   4783   5399  -1302    171    931       C  
ATOM   2701  C   GLY A 347      33.635  28.496   9.727  1.00 31.05           C  
ANISOU 2701  C   GLY A 347     3842   3691   4264  -1232    158   1130       C  
ATOM   2702  O   GLY A 347      33.169  27.478   9.219  1.00 32.28           O  
ANISOU 2702  O   GLY A 347     3982   4021   4261  -1086    179   1114       O  
ATOM   2703  N   ARG A 348      33.261  29.733   9.370  1.00 37.84           N  
ANISOU 2703  N   ARG A 348     4851   4295   5231  -1339    112   1319       N  
ATOM   2704  CA  ARG A 348      32.142  29.981   8.461  1.00 40.99           C  
ANISOU 2704  CA  ARG A 348     5415   4604   5556  -1248     64   1516       C  
ATOM   2705  C   ARG A 348      32.393  29.455   7.057  1.00 40.43           C  
ANISOU 2705  C   ARG A 348     5307   4820   5236  -1303    169   1679       C  
ATOM   2706  O   ARG A 348      31.441  29.223   6.304  1.00 43.89           O  
ANISOU 2706  O   ARG A 348     5832   5298   5547  -1170    133   1779       O  
ATOM   2707  CB  ARG A 348      31.857  31.481   8.358  1.00 56.86           C  
ANISOU 2707  CB  ARG A 348     7597   6259   7749  -1359    -16   1704       C  
ATOM   2708  CG  ARG A 348      31.919  32.226   9.655  1.00 73.16           C  
ANISOU 2708  CG  ARG A 348     9674   8045  10080  -1371   -106   1534       C  
ATOM   2709  CD  ARG A 348      31.435  33.662   9.507  1.00 88.57           C  
ANISOU 2709  CD  ARG A 348    11818   9597  12236  -1431   -212   1704       C  
ATOM   2710  NE  ARG A 348      32.240  34.494   8.615  1.00103.36           N  
ANISOU 2710  NE  ARG A 348    13736  11435  14101  -1661   -120   1915       N  
ATOM   2711  CZ  ARG A 348      31.763  35.106   7.532  1.00111.81           C  
ANISOU 2711  CZ  ARG A 348    14958  12435  15088  -1626   -119   2141       C  
ATOM   2712  NH1 ARG A 348      32.562  35.852   6.778  1.00116.03           N  
ANISOU 2712  NH1 ARG A 348    15524  12955  15609  -1832    -18   2312       N  
ATOM   2713  NH2 ARG A 348      30.483  34.975   7.206  1.00107.40           N  
ANISOU 2713  NH2 ARG A 348    14514  11834  14461  -1384   -220   2192       N  
ATOM   2714  N   GLN A 349      33.650  29.324   6.660  1.00 38.30           N  
ANISOU 2714  N   GLN A 349     4896   4773   4883  -1498    295   1699       N  
ATOM   2715  CA  GLN A 349      33.964  28.880   5.311  1.00 40.12           C  
ANISOU 2715  CA  GLN A 349     5067   5321   4856  -1562    405   1838       C  
ATOM   2716  C   GLN A 349      33.907  27.364   5.158  1.00 38.34           C  
ANISOU 2716  C   GLN A 349     4703   5403   4462  -1373    442   1626       C  
ATOM   2717  O   GLN A 349      34.137  26.870   4.047  1.00 40.28           O  
ANISOU 2717  O   GLN A 349     4874   5949   4480  -1395    527   1684       O  
ATOM   2718  CB  GLN A 349      35.350  29.394   4.904  1.00 42.45           C  
ANISOU 2718  CB  GLN A 349     5245   5763   5121  -1867    538   1939       C  
ATOM   2719  CG  GLN A 349      35.464  30.926   4.850  1.00 55.62           C  
ANISOU 2719  CG  GLN A 349     7066   7100   6966  -2026    510   2113       C  
ATOM   2720  CD  GLN A 349      36.885  31.409   4.563  1.00 74.04           C  
ANISOU 2720  CD  GLN A 349     9270   9559   9302  -2276    642   2116       C  
ATOM   2721  OE1 GLN A 349      37.861  30.759   4.940  1.00 80.47           O  
ANISOU 2721  OE1 GLN A 349     9866  10623  10086  -2341    719   1927       O  
ATOM   2722  NE2 GLN A 349      37.003  32.557   3.894  1.00 77.11           N  
ANISOU 2722  NE2 GLN A 349     9788   9778   9731  -2409    669   2328       N  
ATOM   2723  N   ARG A 350      33.617  26.624   6.231  1.00 32.01           N  
ANISOU 2723  N   ARG A 350     3864   4535   3763  -1192    378   1385       N  
ATOM   2724  CA  ARG A 350      33.669  25.161   6.241  1.00 28.47           C  
ANISOU 2724  CA  ARG A 350     3290   4321   3206  -1023    405   1175       C  
ATOM   2725  C   ARG A 350      32.428  24.578   6.901  1.00 26.07           C  
ANISOU 2725  C   ARG A 350     3077   3858   2971   -794    300   1063       C  
ATOM   2726  O   ARG A 350      32.515  23.743   7.806  1.00 26.63           O  
ANISOU 2726  O   ARG A 350     3085   3930   3104   -677    278    873       O  
ATOM   2727  CB  ARG A 350      34.919  24.649   6.966  1.00 31.88           C  
ANISOU 2727  CB  ARG A 350     3539   4889   3685  -1059    455    982       C  
ATOM   2728  CG  ARG A 350      36.241  25.191   6.402  1.00 38.00           C  
ANISOU 2728  CG  ARG A 350     4179   5861   4398  -1306    571   1054       C  
ATOM   2729  CD  ARG A 350      37.468  24.462   6.966  1.00 39.30           C  
ANISOU 2729  CD  ARG A 350     4120   6242   4569  -1295    616    822       C  
ATOM   2730  NE  ARG A 350      37.745  24.786   8.367  1.00 41.77           N  
ANISOU 2730  NE  ARG A 350     4422   6369   5078  -1288    543    704       N  
ATOM   2731  CZ  ARG A 350      38.706  24.216   9.097  1.00 43.85           C  
ANISOU 2731  CZ  ARG A 350     4508   6783   5370  -1242    546    497       C  
ATOM   2732  NH1 ARG A 350      39.481  23.281   8.567  1.00 43.04           N  
ANISOU 2732  NH1 ARG A 350     4225   6996   5133  -1188    614    375       N  
ATOM   2733  NH2 ARG A 350      38.891  24.575  10.363  1.00 43.78           N  
ANISOU 2733  NH2 ARG A 350     4493   6624   5518  -1232    470    395       N  
ATOM   2734  N   VAL A 351      31.246  24.986   6.431  1.00 27.43           N  
ANISOU 2734  N   VAL A 351     2556   4298   3569    217   -388     28       N  
ATOM   2735  CA  VAL A 351      29.997  24.551   7.059  1.00 26.61           C  
ANISOU 2735  CA  VAL A 351     2415   4154   3543    194   -334    105       C  
ATOM   2736  C   VAL A 351      29.806  23.051   6.893  1.00 29.92           C  
ANISOU 2736  C   VAL A 351     2948   4528   3891    105   -302     65       C  
ATOM   2737  O   VAL A 351      29.466  22.344   7.849  1.00 25.18           O  
ANISOU 2737  O   VAL A 351     2398   3862   3306    165   -222     60       O  
ATOM   2738  CB  VAL A 351      28.805  25.322   6.469  1.00 27.17           C  
ANISOU 2738  CB  VAL A 351     2304   4283   3736     91   -393    262       C  
ATOM   2739  CG1 VAL A 351      27.490  24.619   6.799  1.00 28.14           C  
ANISOU 2739  CG1 VAL A 351     2386   4378   3928     20   -358    368       C  
ATOM   2740  CG2 VAL A 351      28.810  26.756   6.980  1.00 37.28           C  
ANISOU 2740  CG2 VAL A 351     3478   5556   5131    213   -351    311       C  
ATOM   2741  N   SER A 352      29.981  22.542   5.666  1.00 25.52           N  
ANISOU 2741  N   SER A 352     2446   3999   3251    -59   -349     33       N  
ATOM   2742  CA  SER A 352      29.749  21.113   5.445  1.00 28.23           C  
ANISOU 2742  CA  SER A 352     2927   4280   3518   -174   -284    -13       C  
ATOM   2743  C   SER A 352      30.693  20.272   6.298  1.00 27.25           C  
ANISOU 2743  C   SER A 352     2930   4048   3376    -12   -157   -107       C  
ATOM   2744  O   SER A 352      30.288  19.247   6.867  1.00 27.55           O  
ANISOU 2744  O   SER A 352     3038   4016   3416     -9    -75   -113       O  
ATOM   2745  CB  SER A 352      29.921  20.760   3.971  1.00 33.11           C  
ANISOU 2745  CB  SER A 352     3629   4927   4024   -410   -320    -53       C  
ATOM   2746  OG  SER A 352      29.741  19.361   3.788  1.00 32.13           O  
ANISOU 2746  OG  SER A 352     3676   4715   3816   -535   -215   -115       O  
ATOM   2747  N   LEU A 353      31.949  20.693   6.400  1.00 23.11           N  
ANISOU 2747  N   LEU A 353     2421   3518   2843    117   -144   -155       N  
ATOM   2748  CA  LEU A 353      32.894  20.023   7.298  1.00 23.69           C  
ANISOU 2748  CA  LEU A 353     2566   3511   2926    274    -40   -179       C  
ATOM   2749  C   LEU A 353      32.376  20.030   8.733  1.00 26.31           C  
ANISOU 2749  C   LEU A 353     2855   3835   3307    375    -23   -126       C  
ATOM   2750  O   LEU A 353      32.417  19.006   9.427  1.00 27.51           O  
ANISOU 2750  O   LEU A 353     3066   3914   3471    419     65   -121       O  
ATOM   2751  CB  LEU A 353      34.269  20.698   7.221  1.00 26.88           C  
ANISOU 2751  CB  LEU A 353     2954   3942   3318    384    -61   -188       C  
ATOM   2752  CG  LEU A 353      35.399  20.086   8.066  1.00 26.17           C  
ANISOU 2752  CG  LEU A 353     2900   3791   3252    529     29   -151       C  
ATOM   2753  CD1 LEU A 353      35.655  18.634   7.672  1.00 27.79           C  
ANISOU 2753  CD1 LEU A 353     3214   3862   3482    503    188   -177       C  
ATOM   2754  CD2 LEU A 353      36.705  20.895   7.994  1.00 27.29           C  
ANISOU 2754  CD2 LEU A 353     3003   3987   3377    620    -21   -120       C  
ATOM   2755  N   ALA A 354      31.880  21.177   9.199  1.00 22.27           N  
ANISOU 2755  N   ALA A 354     2247   3386   2830    405    -86    -83       N  
ATOM   2756  CA  ALA A 354      31.405  21.264  10.579  1.00 24.70           C  
ANISOU 2756  CA  ALA A 354     2540   3671   3173    478    -42    -46       C  
ATOM   2757  C   ALA A 354      30.260  20.289  10.833  1.00 25.48           C  
ANISOU 2757  C   ALA A 354     2656   3720   3306    421      5    -26       C  
ATOM   2758  O   ALA A 354      30.250  19.583  11.849  1.00 25.66           O  
ANISOU 2758  O   ALA A 354     2727   3694   3331    475     69    -23       O  
ATOM   2759  CB  ALA A 354      30.971  22.691  10.904  1.00 26.04           C  
ANISOU 2759  CB  ALA A 354     2625   3881   3389    499    -65    -11       C  
ATOM   2760  N   LEU A 355      29.297  20.220   9.908  1.00 20.34           N  
ANISOU 2760  N   LEU A 355     1961   3091   2674    292    -38      6       N  
ATOM   2761  CA  LEU A 355      28.164  19.312  10.101  1.00 23.20           C  
ANISOU 2761  CA  LEU A 355     2337   3420   3057    216     -8     44       C  
ATOM   2762  C   LEU A 355      28.622  17.855  10.052  1.00 26.75           C  
ANISOU 2762  C   LEU A 355     2927   3795   3441    196     68    -26       C  
ATOM   2763  O   LEU A 355      28.140  17.015  10.826  1.00 21.71           O  
ANISOU 2763  O   LEU A 355     2326   3104   2817    218    127    -17       O  
ATOM   2764  CB  LEU A 355      27.071  19.575   9.051  1.00 23.05           C  
ANISOU 2764  CB  LEU A 355     2230   3467   3060     40    -90    137       C  
ATOM   2765  CG  LEU A 355      26.022  20.600   9.482  1.00 22.74           C  
ANISOU 2765  CG  LEU A 355     2025   3457   3159     70   -106    272       C  
ATOM   2766  CD1 LEU A 355      26.693  21.914   9.858  1.00 23.72           C  
ANISOU 2766  CD1 LEU A 355     2094   3586   3332    203    -90    254       C  
ATOM   2767  CD2 LEU A 355      24.958  20.812   8.394  1.00 24.02           C  
ANISOU 2767  CD2 LEU A 355     2060   3704   3361   -126   -205    429       C  
ATOM   2768  N   HIS A 356      29.544  17.531   9.145  1.00 22.33           N  
ANISOU 2768  N   HIS A 356     2448   3215   2821    153     90    -91       N  
ATOM   2769  CA  HIS A 356      30.003  16.147   9.055  1.00 24.02           C  
ANISOU 2769  CA  HIS A 356     2802   3323   3003    138    217   -149       C  
ATOM   2770  C   HIS A 356      30.859  15.760  10.253  1.00 25.96           C  
ANISOU 2770  C   HIS A 356     3050   3511   3302    325    294   -132       C  
ATOM   2771  O   HIS A 356      30.807  14.607  10.702  1.00 24.87           O  
ANISOU 2771  O   HIS A 356     2980   3287   3184    344    399   -133       O  
ATOM   2772  CB  HIS A 356      30.748  15.913   7.735  1.00 25.47           C  
ANISOU 2772  CB  HIS A 356     3086   3470   3123     31    265   -221       C  
ATOM   2773  CG  HIS A 356      29.824  15.772   6.557  1.00 25.19           C  
ANISOU 2773  CG  HIS A 356     3102   3472   2997   -234    218   -231       C  
ATOM   2774  ND1 HIS A 356      29.600  16.794   5.657  1.00 28.92           N  
ANISOU 2774  ND1 HIS A 356     3496   4058   3435   -357     82   -199       N  
ATOM   2775  CD2 HIS A 356      29.039  14.742   6.156  1.00 27.32           C  
ANISOU 2775  CD2 HIS A 356     3491   3696   3193   -427    278   -248       C  
ATOM   2776  CE1 HIS A 356      28.725  16.397   4.748  1.00 25.99           C  
ANISOU 2776  CE1 HIS A 356     3184   3721   2970   -630     48   -178       C  
ATOM   2777  NE2 HIS A 356      28.366  15.155   5.028  1.00 27.80           N  
ANISOU 2777  NE2 HIS A 356     3545   3855   3162   -686    166   -213       N  
ATOM   2778  N   VAL A 357      31.646  16.695  10.793  1.00 19.96           N  
ANISOU 2778  N   VAL A 357     2217   2807   2561    444    241    -99       N  
ATOM   2779  CA  VAL A 357      32.412  16.408  12.009  1.00 23.56           C  
ANISOU 2779  CA  VAL A 357     2659   3243   3049    574    283    -39       C  
ATOM   2780  C   VAL A 357      31.461  16.157  13.177  1.00 23.53           C  
ANISOU 2780  C   VAL A 357     2639   3239   3062    581    284     -9       C  
ATOM   2781  O   VAL A 357      31.624  15.197  13.942  1.00 24.34           O  
ANISOU 2781  O   VAL A 357     2766   3289   3194    624    353     30       O  
ATOM   2782  CB  VAL A 357      33.383  17.562  12.319  1.00 24.49           C  
ANISOU 2782  CB  VAL A 357     2717   3443   3147    646    208      1       C  
ATOM   2783  CG1 VAL A 357      33.870  17.464  13.778  1.00 24.51           C  
ANISOU 2783  CG1 VAL A 357     2697   3466   3149    714    213     95       C  
ATOM   2784  CG2 VAL A 357      34.560  17.551  11.330  1.00 25.44           C  
ANISOU 2784  CG2 VAL A 357     2852   3545   3267    670    232     -6       C  
ATOM   2785  N   ALA A 358      30.452  17.023  13.333  1.00 21.25           N  
ANISOU 2785  N   ALA A 358     2300   3001   2771    540    221    -14       N  
ATOM   2786  CA  ALA A 358      29.482  16.845  14.412  1.00 23.27           C  
ANISOU 2786  CA  ALA A 358     2546   3243   3053    543    243     13       C  
ATOM   2787  C   ALA A 358      28.831  15.466  14.337  1.00 27.50           C  
ANISOU 2787  C   ALA A 358     3134   3712   3602    500    299      5       C  
ATOM   2788  O   ALA A 358      28.693  14.770  15.350  1.00 23.98           O  
ANISOU 2788  O   ALA A 358     2708   3232   3171    537    344     28       O  
ATOM   2789  CB  ALA A 358      28.434  17.961  14.352  1.00 21.30           C  
ANISOU 2789  CB  ALA A 358     2223   3028   2842    506    208     30       C  
ATOM   2790  N   GLU A 359      28.450  15.054  13.130  1.00 24.36           N  
ANISOU 2790  N   GLU A 359     2771   3299   3184    396    298    -26       N  
ATOM   2791  CA  GLU A 359      27.837  13.745  12.917  1.00 22.41           C  
ANISOU 2791  CA  GLU A 359     2606   2986   2922    317    363    -43       C  
ATOM   2792  C   GLU A 359      28.778  12.611  13.329  1.00 24.38           C  
ANISOU 2792  C   GLU A 359     2930   3140   3192    397    483    -56       C  
ATOM   2793  O   GLU A 359      28.365  11.662  14.015  1.00 26.33           O  
ANISOU 2793  O   GLU A 359     3208   3334   3460    411    542    -42       O  
ATOM   2794  CB  GLU A 359      27.448  13.620  11.438  1.00 28.91           C  
ANISOU 2794  CB  GLU A 359     3483   3821   3682    137    343    -74       C  
ATOM   2795  CG  GLU A 359      26.957  12.258  10.987  1.00 30.48           C  
ANISOU 2795  CG  GLU A 359     3815   3942   3823      0    431   -109       C  
ATOM   2796  CD  GLU A 359      26.679  12.232   9.493  1.00 33.08           C  
ANISOU 2796  CD  GLU A 359     4226   4295   4049   -237    409   -137       C  
ATOM   2797  OE1 GLU A 359      25.538  11.941   9.108  1.00 35.51           O  
ANISOU 2797  OE1 GLU A 359     4551   4647   4297   -425    356    -90       O  
ATOM   2798  OE2 GLU A 359      27.604  12.516   8.703  1.00 37.70           O  
ANISOU 2798  OE2 GLU A 359     4856   4863   4605   -256    439   -193       O  
ATOM   2799  N   ARG A 360      30.053  12.687  12.923  1.00 22.35           N  
ANISOU 2799  N   ARG A 360     2688   2856   2947    455    530    -61       N  
ATOM   2800  CA  ARG A 360      30.992  11.627  13.292  1.00 23.70           C  
ANISOU 2800  CA  ARG A 360     2896   2924   3185    544    669    -23       C  
ATOM   2801  C   ARG A 360      31.172  11.549  14.802  1.00 26.37           C  
ANISOU 2801  C   ARG A 360     3154   3296   3571    648    641     76       C  
ATOM   2802  O   ARG A 360      31.352  10.456  15.359  1.00 27.73           O  
ANISOU 2802  O   ARG A 360     3338   3390   3807    693    741    131       O  
ATOM   2803  CB  ARG A 360      32.350  11.853  12.631  1.00 26.94           C  
ANISOU 2803  CB  ARG A 360     3307   3303   3627    600    727     -7       C  
ATOM   2804  CG  ARG A 360      32.334  11.863  11.133  1.00 41.39           C  
ANISOU 2804  CG  ARG A 360     5239   5086   5400    477    778   -109       C  
ATOM   2805  CD  ARG A 360      32.204  10.478  10.546  1.00 40.35           C  
ANISOU 2805  CD  ARG A 360     5264   4791   5279    392    986   -167       C  
ATOM   2806  NE  ARG A 360      32.777  10.472   9.199  1.00 41.68           N  
ANISOU 2806  NE  ARG A 360     5545   4883   5409    294   1093   -248       N  
ATOM   2807  CZ  ARG A 360      33.873   9.803   8.855  1.00 48.81           C  
ANISOU 2807  CZ  ARG A 360     6514   5626   6406    362   1317   -236       C  
ATOM   2808  NH1 ARG A 360      34.502   9.049   9.752  1.00 41.36           N  
ANISOU 2808  NH1 ARG A 360     5512   4590   5615    531   1447   -119       N  
ATOM   2809  NH2 ARG A 360      34.325   9.874   7.608  1.00 50.97           N  
ANISOU 2809  NH2 ARG A 360     6909   5827   6632    251   1423   -325       N  
ATOM   2810  N   ILE A 361      31.143  12.696  15.486  1.00 21.71           N  
ANISOU 2810  N   ILE A 361     2488   2816   2946    669    518    106       N  
ATOM   2811  CA  ILE A 361      31.362  12.677  16.929  1.00 24.59           C  
ANISOU 2811  CA  ILE A 361     2802   3222   3319    713    491    199       C  
ATOM   2812  C   ILE A 361      30.149  12.093  17.639  1.00 25.95           C  
ANISOU 2812  C   ILE A 361     2996   3371   3492    677    503    177       C  
ATOM   2813  O   ILE A 361      30.283  11.360  18.626  1.00 24.01           O  
ANISOU 2813  O   ILE A 361     2736   3111   3277    702    532    251       O  
ATOM   2814  CB  ILE A 361      31.690  14.093  17.437  1.00 24.99           C  
ANISOU 2814  CB  ILE A 361     2810   3380   3304    704    388    220       C  
ATOM   2815  CG1 ILE A 361      33.097  14.497  16.977  1.00 25.88           C  
ANISOU 2815  CG1 ILE A 361     2889   3526   3418    748    370    284       C  
ATOM   2816  CG2 ILE A 361      31.561  14.165  18.967  1.00 27.59           C  
ANISOU 2816  CG2 ILE A 361     3129   3755   3598    676    363    289       C  
ATOM   2817  CD1 ILE A 361      33.449  15.949  17.329  1.00 29.75           C  
ANISOU 2817  CD1 ILE A 361     3360   4122   3821    718    273    292       C  
ATOM   2818  N   ARG A 362      28.952  12.384  17.128  1.00 22.42           N  
ANISOU 2818  N   ARG A 362     2572   2926   3021    612    477     98       N  
ATOM   2819  CA  ARG A 362      27.711  12.057  17.824  1.00 23.04           C  
ANISOU 2819  CA  ARG A 362     2656   2995   3104    579    476     92       C  
ATOM   2820  C   ARG A 362      27.179  10.670  17.496  1.00 29.53           C  
ANISOU 2820  C   ARG A 362     3540   3739   3942    545    546     72       C  
ATOM   2821  O   ARG A 362      26.485  10.079  18.331  1.00 24.91           O  
ANISOU 2821  O   ARG A 362     2958   3137   3369    544    560     89       O  
ATOM   2822  CB  ARG A 362      26.634  13.089  17.484  1.00 23.32           C  
ANISOU 2822  CB  ARG A 362     2654   3071   3134    525    422     69       C  
ATOM   2823  CG  ARG A 362      26.877  14.475  18.101  1.00 23.69           C  
ANISOU 2823  CG  ARG A 362     2660   3169   3173    551    395     81       C  
ATOM   2824  CD  ARG A 362      26.754  14.427  19.643  1.00 25.91           C  
ANISOU 2824  CD  ARG A 362     2962   3444   3440    558    430    105       C  
ATOM   2825  NE  ARG A 362      25.436  13.932  20.028  1.00 23.92           N  
ANISOU 2825  NE  ARG A 362     2709   3150   3229    536    464    106       N  
ATOM   2826  CZ  ARG A 362      25.208  12.922  20.861  1.00 25.14           C  
ANISOU 2826  CZ  ARG A 362     2893   3277   3381    536    489    120       C  
ATOM   2827  NH1 ARG A 362      26.214  12.300  21.472  1.00 25.05           N  
ANISOU 2827  NH1 ARG A 362     2901   3279   3339    553    487    154       N  
ATOM   2828  NH2 ARG A 362      23.956  12.543  21.089  1.00 26.72           N  
ANISOU 2828  NH2 ARG A 362     3087   3444   3621    516    514    124       N  
ATOM   2829  N   TYR A 363      27.491  10.138  16.311  1.00 27.19           N  
ANISOU 2829  N   TYR A 363     3309   3386   3635    500    606     31       N  
ATOM   2830  CA  TYR A 363      26.671   9.071  15.737  1.00 27.18           C  
ANISOU 2830  CA  TYR A 363     3403   3318   3608    399    670    -12       C  
ATOM   2831  C   TYR A 363      26.722   7.789  16.572  1.00 25.72           C  
ANISOU 2831  C   TYR A 363     3251   3051   3472    453    768     15       C  
ATOM   2832  O   TYR A 363      25.676   7.247  16.953  1.00 24.85           O  
ANISOU 2832  O   TYR A 363     3163   2937   3343    404    758     11       O  
ATOM   2833  CB  TYR A 363      27.103   8.792  14.300  1.00 25.68           C  
ANISOU 2833  CB  TYR A 363     3315   3069   3373    301    745    -75       C  
ATOM   2834  CG  TYR A 363      26.263   7.711  13.659  1.00 28.91           C  
ANISOU 2834  CG  TYR A 363     3861   3410   3715    140    822   -124       C  
ATOM   2835  CD1 TYR A 363      24.991   7.993  13.149  1.00 27.74           C  
ANISOU 2835  CD1 TYR A 363     3715   3343   3482    -31    713   -115       C  
ATOM   2836  CD2 TYR A 363      26.729   6.406  13.583  1.00 30.90           C  
ANISOU 2836  CD2 TYR A 363     4234   3513   3993    144   1014   -156       C  
ATOM   2837  CE1 TYR A 363      24.216   6.997  12.577  1.00 29.96           C  
ANISOU 2837  CE1 TYR A 363     4134   3578   3670   -220    770   -143       C  
ATOM   2838  CE2 TYR A 363      25.961   5.414  13.022  1.00 33.60           C  
ANISOU 2838  CE2 TYR A 363     4732   3785   4251    -30   1102   -212       C  
ATOM   2839  CZ  TYR A 363      24.709   5.708  12.517  1.00 34.47           C  
ANISOU 2839  CZ  TYR A 363     4860   3996   4240   -226    968   -209       C  
ATOM   2840  OH  TYR A 363      23.956   4.710  11.944  1.00 31.55           O  
ANISOU 2840  OH  TYR A 363     4661   3572   3755   -441   1045   -249       O  
ATOM   2841  N   ALA A 364      27.923   7.275  16.847  1.00 29.41           N  
ANISOU 2841  N   ALA A 364     3707   3451   4015    553    869     65       N  
ATOM   2842  CA  ALA A 364      28.033   6.012  17.582  1.00 26.94           C  
ANISOU 2842  CA  ALA A 364     3406   3052   3779    606    978    120       C  
ATOM   2843  C   ALA A 364      27.503   6.139  19.007  1.00 27.32           C  
ANISOU 2843  C   ALA A 364     3369   3181   3829    639    875    180       C  
ATOM   2844  O   ALA A 364      26.768   5.261  19.484  1.00 27.49           O  
ANISOU 2844  O   ALA A 364     3421   3166   3859    621    906    176       O  
ATOM   2845  CB  ALA A 364      29.488   5.541  17.583  1.00 32.28           C  
ANISOU 2845  CB  ALA A 364     4045   3643   4578    713   1113    218       C  
ATOM   2846  N   ARG A 365      27.861   7.225  19.703  1.00 24.64           N  
ANISOU 2846  N   ARG A 365     2941   2948   3472    670    762    230       N  
ATOM   2847  CA  ARG A 365      27.386   7.432  21.069  1.00 24.07           C  
ANISOU 2847  CA  ARG A 365     2820   2944   3380    663    686    274       C  
ATOM   2848  C   ARG A 365      25.859   7.506  21.125  1.00 29.82           C  
ANISOU 2848  C   ARG A 365     3587   3679   4063    601    651    194       C  
ATOM   2849  O   ARG A 365      25.219   6.860  21.968  1.00 24.71           O  
ANISOU 2849  O   ARG A 365     2943   3022   3424    593    656    210       O  
ATOM   2850  CB  ARG A 365      28.034   8.704  21.636  1.00 27.94           C  
ANISOU 2850  CB  ARG A 365     3255   3535   3825    658    597    320       C  
ATOM   2851  CG  ARG A 365      27.540   9.143  23.007  1.00 26.07           C  
ANISOU 2851  CG  ARG A 365     3009   3362   3534    603    541    341       C  
ATOM   2852  CD  ARG A 365      28.361  10.345  23.519  1.00 24.37           C  
ANISOU 2852  CD  ARG A 365     2775   3237   3247    558    480    389       C  
ATOM   2853  NE  ARG A 365      27.740  10.954  24.691  1.00 27.05           N  
ANISOU 2853  NE  ARG A 365     3157   3613   3509    465    465    368       N  
ATOM   2854  CZ  ARG A 365      27.933  10.533  25.938  1.00 27.94           C  
ANISOU 2854  CZ  ARG A 365     3268   3766   3583    387    447    453       C  
ATOM   2855  NH1 ARG A 365      28.737   9.493  26.172  1.00 27.39           N  
ANISOU 2855  NH1 ARG A 365     3126   3713   3570    410    431    595       N  
ATOM   2856  NH2 ARG A 365      27.312  11.139  26.946  1.00 27.91           N  
ANISOU 2856  NH2 ARG A 365     3334   3776   3493    277    462    410       N  
ATOM   2857  N   ALA A 366      25.250   8.288  20.232  1.00 23.80           N  
ANISOU 2857  N   ALA A 366     2839   2939   3263    553    612    133       N  
ATOM   2858  CA  ALA A 366      23.795   8.390  20.230  1.00 27.75           C  
ANISOU 2858  CA  ALA A 366     3343   3451   3749    491    580    111       C  
ATOM   2859  C   ALA A 366      23.150   7.055  19.867  1.00 26.25           C  
ANISOU 2859  C   ALA A 366     3224   3202   3550    438    628     94       C  
ATOM   2860  O   ALA A 366      22.140   6.664  20.469  1.00 28.48           O  
ANISOU 2860  O   ALA A 366     3503   3485   3833    416    614    109       O  
ATOM   2861  CB  ALA A 366      23.339   9.486  19.260  1.00 25.22           C  
ANISOU 2861  CB  ALA A 366     2991   3175   3417    438    527    101       C  
ATOM   2862  N   SER A 367      23.734   6.332  18.902  1.00 25.70           N  
ANISOU 2862  N   SER A 367     3233   3067   3465    407    704     61       N  
ATOM   2863  CA  SER A 367      23.188   5.038  18.500  1.00 28.64           C  
ANISOU 2863  CA  SER A 367     3711   3363   3807    327    783     31       C  
ATOM   2864  C   SER A 367      23.318   4.008  19.617  1.00 32.26           C  
ANISOU 2864  C   SER A 367     4164   3768   4326    408    846     64       C  
ATOM   2865  O   SER A 367      22.442   3.146  19.782  1.00 29.84           O  
ANISOU 2865  O   SER A 367     3912   3432   3994    353    866     53       O  
ATOM   2866  CB  SER A 367      23.894   4.542  17.236  1.00 27.49           C  
ANISOU 2866  CB  SER A 367     3684   3129   3632    259    902    -26       C  
ATOM   2867  OG  SER A 367      23.690   5.445  16.149  1.00 28.46           O  
ANISOU 2867  OG  SER A 367     3815   3315   3683    148    828    -50       O  
ATOM   2868  N   ALA A 368      24.402   4.075  20.391  1.00 27.88           N  
ANISOU 2868  N   ALA A 368     3535   3210   3848    523    868    126       N  
ATOM   2869  CA  ALA A 368      24.560   3.145  21.509  1.00 32.16           C  
ANISOU 2869  CA  ALA A 368     4042   3721   4458    585    910    195       C  
ATOM   2870  C   ALA A 368      23.497   3.380  22.577  1.00 31.07           C  
ANISOU 2870  C   ALA A 368     3865   3658   4284    563    805    199       C  
ATOM   2871  O   ALA A 368      22.891   2.425  23.083  1.00 32.26           O  
ANISOU 2871  O   ALA A 368     4038   3775   4445    554    831    204       O  
ATOM   2872  CB  ALA A 368      25.962   3.273  22.102  1.00 27.03           C  
ANISOU 2872  CB  ALA A 368     3292   3082   3896    677    929    313       C  
ATOM   2873  N   VAL A 369      23.235   4.641  22.927  1.00 28.36           N  
ANISOU 2873  N   VAL A 369     3472   3401   3903    551    709    194       N  
ATOM   2874  CA  VAL A 369      22.162   4.913  23.878  1.00 28.19           C  
ANISOU 2874  CA  VAL A 369     3430   3419   3860    524    655    192       C  
ATOM   2875  C   VAL A 369      20.830   4.398  23.338  1.00 30.07           C  
ANISOU 2875  C   VAL A 369     3715   3634   4078    466    653    159       C  
ATOM   2876  O   VAL A 369      20.016   3.831  24.079  1.00 29.49           O  
ANISOU 2876  O   VAL A 369     3642   3555   4006    456    646    169       O  
ATOM   2877  CB  VAL A 369      22.106   6.419  24.204  1.00 26.68           C  
ANISOU 2877  CB  VAL A 369     3201   3288   3648    513    608    186       C  
ATOM   2878  CG1 VAL A 369      20.942   6.715  25.105  1.00 31.71           C  
ANISOU 2878  CG1 VAL A 369     3833   3930   4285    484    605    182       C  
ATOM   2879  CG2 VAL A 369      23.411   6.870  24.841  1.00 28.82           C  
ANISOU 2879  CG2 VAL A 369     3444   3601   3907    528    596    235       C  
ATOM   2880  N   GLN A 370      20.610   4.556  22.033  1.00 26.08           N  
ANISOU 2880  N   GLN A 370     3247   3123   3540    404    652    133       N  
ATOM   2881  CA  GLN A 370      19.377   4.103  21.405  1.00 28.50           C  
ANISOU 2881  CA  GLN A 370     3596   3431   3802    299    630    137       C  
ATOM   2882  C   GLN A 370      19.248   2.588  21.488  1.00 30.02           C  
ANISOU 2882  C   GLN A 370     3881   3554   3970    271    700    114       C  
ATOM   2883  O   GLN A 370      18.186   2.055  21.834  1.00 30.48           O  
ANISOU 2883  O   GLN A 370     3952   3622   4008    225    673    135       O  
ATOM   2884  CB  GLN A 370      19.370   4.582  19.946  1.00 29.10           C  
ANISOU 2884  CB  GLN A 370     3701   3529   3826    193    609    130       C  
ATOM   2885  CG  GLN A 370      18.049   4.547  19.227  1.00 34.75           C  
ANISOU 2885  CG  GLN A 370     4422   4295   4487     38    542    191       C  
ATOM   2886  CD  GLN A 370      18.146   5.181  17.843  1.00 33.18           C  
ANISOU 2886  CD  GLN A 370     4232   4142   4233    -93    499    209       C  
ATOM   2887  OE1 GLN A 370      19.167   5.063  17.162  1.00 33.66           O  
ANISOU 2887  OE1 GLN A 370     4374   4160   4256   -106    560    132       O  
ATOM   2888  NE2 GLN A 370      17.093   5.858  17.430  1.00 31.94           N  
ANISOU 2888  NE2 GLN A 370     3981   4071   4085   -193    402    330       N  
ATOM   2889  N   LEU A 371      20.327   1.870  21.186  1.00 32.98           N  
ANISOU 2889  N   LEU A 371     4320   3847   4364    303    809     81       N  
ATOM   2890  CA  LEU A 371      20.237   0.414  21.162  1.00 34.66           C  
ANISOU 2890  CA  LEU A 371     4635   3963   4571    274    920     59       C  
ATOM   2891  C   LEU A 371      20.143  -0.161  22.571  1.00 36.56           C  
ANISOU 2891  C   LEU A 371     4807   4204   4880    369    911    106       C  
ATOM   2892  O   LEU A 371      19.439  -1.154  22.784  1.00 35.95           O  
ANISOU 2892  O   LEU A 371     4790   4091   4780    328    941     97       O  
ATOM   2893  CB  LEU A 371      21.421  -0.160  20.385  1.00 37.09           C  
ANISOU 2893  CB  LEU A 371     5028   4149   4913    287   1090     27       C  
ATOM   2894  CG  LEU A 371      21.441   0.248  18.901  1.00 48.36           C  
ANISOU 2894  CG  LEU A 371     6563   5567   6245    147   1115    -36       C  
ATOM   2895  CD1 LEU A 371      22.627  -0.370  18.164  1.00 53.54           C  
ANISOU 2895  CD1 LEU A 371     7325   6069   6949    160   1331    -76       C  
ATOM   2896  CD2 LEU A 371      20.138  -0.100  18.192  1.00 42.74           C  
ANISOU 2896  CD2 LEU A 371     5967   4885   5387    -66   1070    -65       C  
ATOM   2897  N   ILE A 372      20.809   0.455  23.549  1.00 32.04           N  
ANISOU 2897  N   ILE A 372     4119   3682   4374    468    863    161       N  
ATOM   2898  CA  ILE A 372      20.603   0.046  24.937  1.00 33.43           C  
ANISOU 2898  CA  ILE A 372     4231   3884   4588    512    828    213       C  
ATOM   2899  C   ILE A 372      19.142   0.220  25.328  1.00 36.41           C  
ANISOU 2899  C   ILE A 372     4616   4311   4909    456    745    188       C  
ATOM   2900  O   ILE A 372      18.555  -0.634  26.006  1.00 36.11           O  
ANISOU 2900  O   ILE A 372     4585   4259   4874    453    746    199       O  
ATOM   2901  CB  ILE A 372      21.531   0.840  25.869  1.00 37.48           C  
ANISOU 2901  CB  ILE A 372     4638   4464   5138    562    776    285       C  
ATOM   2902  CG1 ILE A 372      22.989   0.469  25.610  1.00 40.63           C  
ANISOU 2902  CG1 ILE A 372     4997   4815   5625    624    860    367       C  
ATOM   2903  CG2 ILE A 372      21.166   0.590  27.316  1.00 41.84           C  
ANISOU 2903  CG2 ILE A 372     5141   5063   5694    551    721    333       C  
ATOM   2904  CD1 ILE A 372      23.943   1.293  26.431  1.00 40.58           C  
ANISOU 2904  CD1 ILE A 372     4888   4898   5630    633    788    468       C  
ATOM   2905  N   SER A 373      18.531   1.326  24.901  1.00 31.41           N  
ANISOU 2905  N   SER A 373     3965   3731   4240    417    683    175       N  
ATOM   2906  CA  SER A 373      17.104   1.532  25.132  1.00 31.74           C  
ANISOU 2906  CA  SER A 373     3991   3806   4261    369    627    192       C  
ATOM   2907  C   SER A 373      16.275   0.386  24.562  1.00 34.74           C  
ANISOU 2907  C   SER A 373     4451   4160   4589    287    635    189       C  
ATOM   2908  O   SER A 373      15.325  -0.083  25.205  1.00 37.74           O  
ANISOU 2908  O   SER A 373     4824   4551   4966    274    606    214       O  
ATOM   2909  CB  SER A 373      16.667   2.867  24.521  1.00 35.74           C  
ANISOU 2909  CB  SER A 373     4447   4358   4776    340    586    218       C  
ATOM   2910  OG  SER A 373      15.254   2.983  24.487  1.00 53.79           O  
ANISOU 2910  OG  SER A 373     6698   6668   7072    287    548    283       O  
ATOM   2911  N   HIS A 374      16.613  -0.076  23.356  1.00 31.46           N  
ANISOU 2911  N   HIS A 374     4130   3706   4118    210    684    157       N  
ATOM   2912  CA  HIS A 374      15.886  -1.194  22.759  1.00 34.35           C  
ANISOU 2912  CA  HIS A 374     4614   4040   4398     84    712    146       C  
ATOM   2913  C   HIS A 374      16.005  -2.435  23.627  1.00 35.73           C  
ANISOU 2913  C   HIS A 374     4824   4148   4603    144    781    125       C  
ATOM   2914  O   HIS A 374      15.016  -3.140  23.865  1.00 36.77           O  
ANISOU 2914  O   HIS A 374     4994   4289   4686     82    753    140       O  
ATOM   2915  CB  HIS A 374      16.416  -1.504  21.358  1.00 34.34           C  
ANISOU 2915  CB  HIS A 374     4749   3983   4316    -38    798     93       C  
ATOM   2916  CG  HIS A 374      16.216  -0.402  20.361  1.00 36.95           C  
ANISOU 2916  CG  HIS A 374     5051   4391   4599   -138    717    125       C  
ATOM   2917  ND1 HIS A 374      16.601  -0.525  19.043  1.00 42.53           N  
ANISOU 2917  ND1 HIS A 374     5885   5063   5210   -290    777     80       N  
ATOM   2918  CD2 HIS A 374      15.669   0.833  20.480  1.00 36.26           C  
ANISOU 2918  CD2 HIS A 374     4822   4402   4553   -119    596    208       C  
ATOM   2919  CE1 HIS A 374      16.313   0.590  18.395  1.00 41.08           C  
ANISOU 2919  CE1 HIS A 374     5625   4977   5007   -362    668    141       C  
ATOM   2920  NE2 HIS A 374      15.745   1.430  19.242  1.00 39.48           N  
ANISOU 2920  NE2 HIS A 374     5251   4850   4899   -251    565    226       N  
ATOM   2921  N   ARG A 375      17.222  -2.715  24.106  1.00 33.16           N  
ANISOU 2921  N   ARG A 375     4472   3760   4368    261    868    116       N  
ATOM   2922  CA  ARG A 375      17.466  -3.912  24.907  1.00 31.85           C  
ANISOU 2922  CA  ARG A 375     4312   3526   4263    323    946    130       C  
ATOM   2923  C   ARG A 375      16.585  -3.933  26.146  1.00 30.19           C  
ANISOU 2923  C   ARG A 375     4023   3389   4058    349    836    164       C  
ATOM   2924  O   ARG A 375      16.108  -4.997  26.560  1.00 29.87           O  
ANISOU 2924  O   ARG A 375     4022   3315   4013    337    862    165       O  
ATOM   2925  CB  ARG A 375      18.943  -3.984  25.305  1.00 31.49           C  
ANISOU 2925  CB  ARG A 375     4190   3429   4345    443   1032    181       C  
ATOM   2926  CG  ARG A 375      19.906  -4.226  24.144  1.00 43.72           C  
ANISOU 2926  CG  ARG A 375     5824   4864   5924    438   1197    154       C  
ATOM   2927  CD  ARG A 375      21.345  -4.288  24.645  1.00 54.15           C  
ANISOU 2927  CD  ARG A 375     7027   6143   7404    569   1276    261       C  
ATOM   2928  NE  ARG A 375      22.230  -4.950  23.688  1.00 74.02           N  
ANISOU 2928  NE  ARG A 375     9630   8495   9999    586   1506    256       N  
ATOM   2929  CZ  ARG A 375      23.546  -5.067  23.842  1.00 85.16           C  
ANISOU 2929  CZ  ARG A 375    10940   9841  11576    699   1619    378       C  
ATOM   2930  NH1 ARG A 375      24.140  -4.554  24.912  1.00 87.58           N  
ANISOU 2930  NH1 ARG A 375    11056  10260  11961    777   1492    521       N  
ATOM   2931  NH2 ARG A 375      24.272  -5.684  22.918  1.00 90.79           N  
ANISOU 2931  NH2 ARG A 375    11747  10373  12376    715   1871    369       N  
ATOM   2932  N   VAL A 376      16.350  -2.768  26.749  1.00 31.32           N  
ANISOU 2932  N   VAL A 376     4069   3619   4211    376    733    188       N  
ATOM   2933  CA  VAL A 376      15.523  -2.720  27.952  1.00 30.21           C  
ANISOU 2933  CA  VAL A 376     3873   3529   4078    388    660    213       C  
ATOM   2934  C   VAL A 376      14.119  -3.224  27.649  1.00 30.58           C  
ANISOU 2934  C   VAL A 376     3971   3585   4062    312    624    215       C  
ATOM   2935  O   VAL A 376      13.602  -4.111  28.339  1.00 30.63           O  
ANISOU 2935  O   VAL A 376     3989   3584   4066    314    616    220       O  
ATOM   2936  CB  VAL A 376      15.506  -1.297  28.542  1.00 32.64           C  
ANISOU 2936  CB  VAL A 376     4103   3895   4403    406    610    226       C  
ATOM   2937  CG1 VAL A 376      14.453  -1.184  29.641  1.00 41.75           C  
ANISOU 2937  CG1 VAL A 376     5228   5074   5560    395    574    239       C  
ATOM   2938  CG2 VAL A 376      16.880  -0.945  29.096  1.00 35.65           C  
ANISOU 2938  CG2 VAL A 376     4437   4288   4820    447    626    246       C  
ATOM   2939  N   ASN A 377      13.476  -2.677  26.609  1.00 29.26           N  
ANISOU 2939  N   ASN A 377     3827   3447   3844    229    590    233       N  
ATOM   2940  CA  ASN A 377      12.085  -3.071  26.410  1.00 30.56           C  
ANISOU 2940  CA  ASN A 377     4013   3647   3950    135    532    286       C  
ATOM   2941  C   ASN A 377      11.961  -4.410  25.698  1.00 32.58           C  
ANISOU 2941  C   ASN A 377     4414   3858   4106     26    578    253       C  
ATOM   2942  O   ASN A 377      10.934  -5.084  25.856  1.00 33.71           O  
ANISOU 2942  O   ASN A 377     4590   4026   4194    -46    534    291       O  
ATOM   2943  CB  ASN A 377      11.284  -1.963  25.704  1.00 33.82           C  
ANISOU 2943  CB  ASN A 377     4359   4127   4365     66    464    380       C  
ATOM   2944  CG  ASN A 377      11.693  -1.727  24.265  1.00 34.86           C  
ANISOU 2944  CG  ASN A 377     4552   4269   4425    -47    468    378       C  
ATOM   2945  OD1 ASN A 377      11.754  -2.655  23.454  1.00 38.03           O  
ANISOU 2945  OD1 ASN A 377     5090   4644   4715   -175    499    343       O  
ATOM   2946  ND2 ASN A 377      11.921  -0.457  23.924  1.00 35.82           N  
ANISOU 2946  ND2 ASN A 377     4585   4422   4603    -21    447    416       N  
ATOM   2947  N   GLU A 378      12.996  -4.833  24.964  1.00 32.16           N  
ANISOU 2947  N   GLU A 378     4460   3728   4032      7    686    184       N  
ATOM   2948  CA  GLU A 378      13.023  -6.199  24.447  1.00 32.38           C  
ANISOU 2948  CA  GLU A 378     4655   3667   3980    -90    797    132       C  
ATOM   2949  C   GLU A 378      13.158  -7.228  25.568  1.00 33.74           C  
ANISOU 2949  C   GLU A 378     4811   3783   4225     16    849    120       C  
ATOM   2950  O   GLU A 378      12.688  -8.361  25.426  1.00 41.47           O  
ANISOU 2950  O   GLU A 378     5912   4711   5135    -67    908     96       O  
ATOM   2951  CB  GLU A 378      14.158  -6.351  23.420  1.00 34.79           C  
ANISOU 2951  CB  GLU A 378     5075   3869   4276   -126    952     63       C  
ATOM   2952  CG  GLU A 378      13.906  -5.551  22.141  1.00 37.35           C  
ANISOU 2952  CG  GLU A 378     5452   4250   4489   -292    900     72       C  
ATOM   2953  CD  GLU A 378      15.129  -5.446  21.224  1.00 47.40           C  
ANISOU 2953  CD  GLU A 378     6815   5426   5771   -304   1049     -1       C  
ATOM   2954  OE1 GLU A 378      16.222  -5.923  21.600  1.00 46.09           O  
ANISOU 2954  OE1 GLU A 378     6646   5142   5724   -161   1200    -37       O  
ATOM   2955  OE2 GLU A 378      14.988  -4.870  20.119  1.00 47.40           O  
ANISOU 2955  OE2 GLU A 378     6875   5469   5667   -465   1015      0       O  
ATOM   2956  N   GLY A 379      13.785  -6.860  26.684  1.00 32.12           N  
ANISOU 2956  N   GLY A 379     4464   3593   4147    176    826    145       N  
ATOM   2957  CA  GLY A 379      13.891  -7.788  27.800  1.00 29.27           C  
ANISOU 2957  CA  GLY A 379     4062   3202   3858    256    851    162       C  
ATOM   2958  C   GLY A 379      12.558  -8.087  28.457  1.00 33.66           C  
ANISOU 2958  C   GLY A 379     4608   3824   4357    216    742    180       C  
ATOM   2959  O   GLY A 379      12.346  -9.191  28.974  1.00 36.30           O  
ANISOU 2959  O   GLY A 379     4973   4120   4701    225    776    178       O  
ATOM   2960  N   TRP A 380      11.639  -7.119  28.438  1.00 30.90           N  
ANISOU 2960  N   TRP A 380     4207   3566   3967    177    624    214       N  
ATOM   2961  CA  TRP A 380      10.382  -7.271  29.163  1.00 30.74           C  
ANISOU 2961  CA  TRP A 380     4151   3605   3925    159    531    257       C  
ATOM   2962  C   TRP A 380       9.579  -8.475  28.684  1.00 32.47           C  
ANISOU 2962  C   TRP A 380     4492   3807   4037     45    536    257       C  
ATOM   2963  O   TRP A 380       8.900  -9.119  29.489  1.00 34.08           O  
ANISOU 2963  O   TRP A 380     4681   4028   4238     59    494    272       O  
ATOM   2964  CB  TRP A 380       9.556  -5.997  29.027  1.00 27.20           C  
ANISOU 2964  CB  TRP A 380     3619   3230   3486    137    449    328       C  
ATOM   2965  CG  TRP A 380      10.199  -4.841  29.698  1.00 30.22           C  
ANISOU 2965  CG  TRP A 380     3903   3618   3961    234    461    317       C  
ATOM   2966  CD1 TRP A 380      11.093  -4.883  30.733  1.00 31.12           C  
ANISOU 2966  CD1 TRP A 380     3981   3713   4128    311    490    276       C  
ATOM   2967  CD2 TRP A 380      10.001  -3.461  29.390  1.00 26.64           C  
ANISOU 2967  CD2 TRP A 380     3381   3191   3550    239    451    362       C  
ATOM   2968  NE1 TRP A 380      11.456  -3.605  31.096  1.00 33.16           N  
ANISOU 2968  NE1 TRP A 380     4179   3988   4432    342    498    278       N  
ATOM   2969  CE2 TRP A 380      10.803  -2.713  30.283  1.00 31.72           C  
ANISOU 2969  CE2 TRP A 380     3976   3821   4254    314    488    321       C  
ATOM   2970  CE3 TRP A 380       9.227  -2.783  28.442  1.00 29.44           C  
ANISOU 2970  CE3 TRP A 380     3702   3584   3900    170    415    455       C  
ATOM   2971  CZ2 TRP A 380      10.861  -1.321  30.249  1.00 29.44           C  
ANISOU 2971  CZ2 TRP A 380     3634   3535   4019    334    515    340       C  
ATOM   2972  CZ3 TRP A 380       9.283  -1.396  28.411  1.00 32.79           C  
ANISOU 2972  CZ3 TRP A 380     4039   4012   4408    211    438    496       C  
ATOM   2973  CH2 TRP A 380      10.096  -0.681  29.310  1.00 31.93           C  
ANISOU 2973  CH2 TRP A 380     3908   3869   4356    298    500    424       C  
ATOM   2974  N   ARG A 381       9.657  -8.811  27.390  1.00 31.42           N  
ANISOU 2974  N   ARG A 381     4498   3641   3800    -91    594    235       N  
ATOM   2975  CA  ARG A 381       8.854  -9.927  26.903  1.00 37.71           C  
ANISOU 2975  CA  ARG A 381     5445   4426   4457   -250    606    235       C  
ATOM   2976  C   ARG A 381       9.262 -11.253  27.538  1.00 38.92           C  
ANISOU 2976  C   ARG A 381     5664   4477   4646   -185    719    169       C  
ATOM   2977  O   ARG A 381       8.439 -12.171  27.592  1.00 42.31           O  
ANISOU 2977  O   ARG A 381     6184   4910   4981   -279    705    175       O  
ATOM   2978  CB  ARG A 381       8.936 -10.017  25.379  1.00 39.76           C  
ANISOU 2978  CB  ARG A 381     5876   4661   4569   -460    668    216       C  
ATOM   2979  CG  ARG A 381      10.240 -10.560  24.862  1.00 52.14           C  
ANISOU 2979  CG  ARG A 381     7573   6075   6164   -440    880    102       C  
ATOM   2980  CD  ARG A 381      10.286 -10.453  23.356  1.00 69.13           C  
ANISOU 2980  CD  ARG A 381     9903   8209   8156   -675    942     75       C  
ATOM   2981  NE  ARG A 381      10.060  -9.077  22.932  1.00 77.56           N  
ANISOU 2981  NE  ARG A 381    10844   9403   9224   -702    791    159       N  
ATOM   2982  CZ  ARG A 381      10.070  -8.672  21.667  1.00 86.73           C  
ANISOU 2982  CZ  ARG A 381    12106  10590  10258   -908    791    169       C  
ATOM   2983  NH1 ARG A 381      10.295  -9.541  20.691  1.00 89.47           N  
ANISOU 2983  NH1 ARG A 381    12711  10838  10445  -1128    949     83       N  
ATOM   2984  NH2 ARG A 381       9.855  -7.396  21.380  1.00 87.55           N  
ANISOU 2984  NH2 ARG A 381    12061  10811  10394   -910    651    267       N  
ATOM   2985  N   ASN A 382      10.494 -11.366  28.039  1.00 34.86           N  
ANISOU 2985  N   ASN A 382     5091   3880   4276    -32    827    133       N  
ATOM   2986  CA  ASN A 382      10.960 -12.586  28.693  1.00 34.22           C  
ANISOU 2986  CA  ASN A 382     5027   3699   4277     45    944    114       C  
ATOM   2987  C   ASN A 382      10.793 -12.556  30.207  1.00 40.54           C  
ANISOU 2987  C   ASN A 382     5654   4571   5177    172    830    166       C  
ATOM   2988  O   ASN A 382      11.204 -13.508  30.880  1.00 45.94           O  
ANISOU 2988  O   ASN A 382     6311   5193   5952    241    904    182       O  
ATOM   2989  CB  ASN A 382      12.434 -12.835  28.368  1.00 43.28           C  
ANISOU 2989  CB  ASN A 382     6184   4708   5552    128   1145     99       C  
ATOM   2990  CG  ASN A 382      12.708 -12.847  26.882  1.00 55.97           C  
ANISOU 2990  CG  ASN A 382     7981   6223   7061     -8   1291     31       C  
ATOM   2991  OD1 ASN A 382      11.973 -13.465  26.110  1.00 56.01           O  
ANISOU 2991  OD1 ASN A 382     8183   6196   6901   -192   1340    -21       O  
ATOM   2992  ND2 ASN A 382      13.765 -12.152  26.468  1.00 60.13           N  
ANISOU 2992  ND2 ASN A 382     8461   6712   7672     57   1360     34       N  
ATOM   2993  N   GLN A 383      10.216 -11.501  30.763  1.00 29.93           N  
ANISOU 2993  N   GLN A 383     4197   3346   3828    192    672    201       N  
ATOM   2994  CA  GLN A 383      10.174 -11.346  32.209  1.00 30.07           C  
ANISOU 2994  CA  GLN A 383     4076   3423   3928    279    587    236       C  
ATOM   2995  C   GLN A 383       8.786 -11.669  32.748  1.00 32.87           C  
ANISOU 2995  C   GLN A 383     4435   3838   4214    236    482    250       C  
ATOM   2996  O   GLN A 383       7.787 -11.627  32.030  1.00 35.02           O  
ANISOU 2996  O   GLN A 383     4780   4141   4384    142    438    265       O  
ATOM   2997  CB  GLN A 383      10.587  -9.927  32.611  1.00 28.47           C  
ANISOU 2997  CB  GLN A 383     3762   3280   3775    323    531    255       C  
ATOM   2998  CG  GLN A 383      12.056  -9.644  32.336  1.00 29.63           C  
ANISOU 2998  CG  GLN A 383     3875   3382   4003    376    615    266       C  
ATOM   2999  CD  GLN A 383      12.390  -8.170  32.317  1.00 30.18           C  
ANISOU 2999  CD  GLN A 383     3883   3504   4079    385    572    269       C  
ATOM   3000  OE1 GLN A 383      11.691  -7.351  32.917  1.00 30.26           O  
ANISOU 3000  OE1 GLN A 383     3854   3575   4070    370    499    270       O  
ATOM   3001  NE2 GLN A 383      13.471  -7.816  31.605  1.00 32.60           N  
ANISOU 3001  NE2 GLN A 383     4192   3774   4422    409    642    272       N  
ATOM   3002  N   ASP A 384       8.740 -12.009  34.036  1.00 29.53           N  
ANISOU 3002  N   ASP A 384     3928   3442   3849    290    436    267       N  
ATOM   3003  CA  ASP A 384       7.482 -12.231  34.748  1.00 26.38           C  
ANISOU 3003  CA  ASP A 384     3516   3101   3406    266    339    282       C  
ATOM   3004  C   ASP A 384       7.559 -11.382  36.010  1.00 28.15           C  
ANISOU 3004  C   ASP A 384     3627   3376   3692    303    286    294       C  
ATOM   3005  O   ASP A 384       8.172 -11.796  36.998  1.00 30.48           O  
ANISOU 3005  O   ASP A 384     3862   3680   4040    324    279    303       O  
ATOM   3006  CB  ASP A 384       7.274 -13.710  35.079  1.00 31.72           C  
ANISOU 3006  CB  ASP A 384     4240   3746   4067    260    355    274       C  
ATOM   3007  CG  ASP A 384       5.928 -13.988  35.755  1.00 35.78           C  
ANISOU 3007  CG  ASP A 384     4745   4324   4526    231    248    294       C  
ATOM   3008  OD1 ASP A 384       5.329 -13.064  36.356  1.00 30.36           O  
ANISOU 3008  OD1 ASP A 384     3986   3694   3857    241    179    318       O  
ATOM   3009  OD2 ASP A 384       5.481 -15.157  35.705  1.00 37.55           O  
ANISOU 3009  OD2 ASP A 384     5042   4529   4698    198    252    286       O  
ATOM   3010  N   TRP A 385       6.958 -10.194  35.971  1.00 28.77           N  
ANISOU 3010  N   TRP A 385     3681   3484   3768    293    263    308       N  
ATOM   3011  CA  TRP A 385       7.054  -9.287  37.102  1.00 31.39           C  
ANISOU 3011  CA  TRP A 385     3949   3835   4144    297    262    299       C  
ATOM   3012  C   TRP A 385       6.200  -9.726  38.285  1.00 35.22           C  
ANISOU 3012  C   TRP A 385     4418   4342   4623    279    219    300       C  
ATOM   3013  O   TRP A 385       6.240  -9.067  39.334  1.00 33.10           O  
ANISOU 3013  O   TRP A 385     4126   4079   4370    247    237    280       O  
ATOM   3014  CB  TRP A 385       6.654  -7.872  36.675  1.00 26.60           C  
ANISOU 3014  CB  TRP A 385     3328   3217   3561    298    301    318       C  
ATOM   3015  CG  TRP A 385       7.535  -7.291  35.623  1.00 26.45           C  
ANISOU 3015  CG  TRP A 385     3318   3185   3547    309    337    313       C  
ATOM   3016  CD1 TRP A 385       8.838  -7.628  35.353  1.00 25.52           C  
ANISOU 3016  CD1 TRP A 385     3207   3056   3432    323    358    288       C  
ATOM   3017  CD2 TRP A 385       7.179  -6.278  34.676  1.00 30.57           C  
ANISOU 3017  CD2 TRP A 385     3829   3701   4086    306    360    353       C  
ATOM   3018  NE1 TRP A 385       9.310  -6.880  34.303  1.00 27.59           N  
ANISOU 3018  NE1 TRP A 385     3482   3304   3698    329    393    288       N  
ATOM   3019  CE2 TRP A 385       8.313  -6.044  33.869  1.00 30.25           C  
ANISOU 3019  CE2 TRP A 385     3808   3651   4037    313    387    325       C  
ATOM   3020  CE3 TRP A 385       6.009  -5.547  34.433  1.00 28.56           C  
ANISOU 3020  CE3 TRP A 385     3533   3448   3872    300    368    437       C  
ATOM   3021  CZ2 TRP A 385       8.311  -5.110  32.838  1.00 28.85           C  
ANISOU 3021  CZ2 TRP A 385     3619   3472   3869    303    404    356       C  
ATOM   3022  CZ3 TRP A 385       6.006  -4.623  33.412  1.00 29.86           C  
ANISOU 3022  CZ3 TRP A 385     3668   3613   4065    292    388    495       C  
ATOM   3023  CH2 TRP A 385       7.152  -4.416  32.623  1.00 24.75           C  
ANISOU 3023  CH2 TRP A 385     3052   2964   3387    288    398    443       C  
ATOM   3024  N   ASP A 386       5.421 -10.801  38.150  1.00 30.16           N  
ANISOU 3024  N   ASP A 386     3805   3710   3945    278    171    316       N  
ATOM   3025  CA  ASP A 386       4.708 -11.284  39.321  1.00 31.14           C  
ANISOU 3025  CA  ASP A 386     3909   3858   4064    263    125    314       C  
ATOM   3026  C   ASP A 386       5.488 -12.384  40.031  1.00 32.83           C  
ANISOU 3026  C   ASP A 386     4101   4088   4285    257     94    300       C  
ATOM   3027  O   ASP A 386       5.656 -12.330  41.254  1.00 32.84           O  
ANISOU 3027  O   ASP A 386     4060   4121   4297    213     67    294       O  
ATOM   3028  CB  ASP A 386       3.323 -11.793  38.943  1.00 32.90           C  
ANISOU 3028  CB  ASP A 386     4159   4095   4247    258     77    362       C  
ATOM   3029  CG  ASP A 386       2.534 -12.235  40.154  1.00 41.48           C  
ANISOU 3029  CG  ASP A 386     5224   5203   5334    250     34    360       C  
ATOM   3030  OD1 ASP A 386       2.273 -11.381  41.052  1.00 36.34           O  
ANISOU 3030  OD1 ASP A 386     4545   4535   4727    239     79    347       O  
ATOM   3031  OD2 ASP A 386       2.205 -13.435  40.224  1.00 39.98           O  
ANISOU 3031  OD2 ASP A 386     5058   5034   5097    243    -27    362       O  
ATOM   3032  N   ALA A 387       5.995 -13.365  39.271  1.00 29.16           N  
ANISOU 3032  N   ALA A 387     3665   3594   3819    283    114    309       N  
ATOM   3033  CA  ALA A 387       6.674 -14.512  39.873  1.00 31.12           C  
ANISOU 3033  CA  ALA A 387     3870   3839   4114    293    111    333       C  
ATOM   3034  C   ALA A 387       8.039 -14.135  40.432  1.00 26.55           C  
ANISOU 3034  C   ALA A 387     3196   3278   3614    283    128    384       C  
ATOM   3035  O   ALA A 387       8.433 -14.618  41.500  1.00 27.87           O  
ANISOU 3035  O   ALA A 387     3277   3490   3822    247     80    441       O  
ATOM   3036  CB  ALA A 387       6.829 -15.623  38.840  1.00 33.51           C  
ANISOU 3036  CB  ALA A 387     4252   4068   4412    320    187    331       C  
ATOM   3037  N   TYR A 388       8.786 -13.307  39.706  1.00 23.20           N  
ANISOU 3037  N   TYR A 388     2777   2830   3209    299    186    384       N  
ATOM   3038  CA  TYR A 388      10.149 -12.962  40.071  1.00 24.38           C  
ANISOU 3038  CA  TYR A 388     2833   3001   3430    282    201    460       C  
ATOM   3039  C   TYR A 388      10.156 -11.764  41.008  1.00 30.03           C  
ANISOU 3039  C   TYR A 388     3529   3789   4093    184    146    449       C  
ATOM   3040  O   TYR A 388       9.376 -10.825  40.833  1.00 28.12           O  
ANISOU 3040  O   TYR A 388     3357   3536   3792    173    160    370       O  
ATOM   3041  CB  TYR A 388      10.959 -12.631  38.823  1.00 27.44           C  
ANISOU 3041  CB  TYR A 388     3247   3323   3856    340    297    463       C  
ATOM   3042  CG  TYR A 388      11.476 -13.834  38.062  1.00 32.46           C  
ANISOU 3042  CG  TYR A 388     3898   3861   4574    410    410    501       C  
ATOM   3043  CD1 TYR A 388      10.697 -14.476  37.102  1.00 32.81           C  
ANISOU 3043  CD1 TYR A 388     4077   3831   4557    422    473    423       C  
ATOM   3044  CD2 TYR A 388      12.757 -14.307  38.286  1.00 40.83           C  
ANISOU 3044  CD2 TYR A 388     4841   4895   5776    445    474    633       C  
ATOM   3045  CE1 TYR A 388      11.200 -15.576  36.390  1.00 31.08           C  
ANISOU 3045  CE1 TYR A 388     3912   3491   4406    461    628    439       C  
ATOM   3046  CE2 TYR A 388      13.261 -15.390  37.588  1.00 46.08           C  
ANISOU 3046  CE2 TYR A 388     5525   5431   6551    518    635    675       C  
ATOM   3047  CZ  TYR A 388      12.483 -16.022  36.648  1.00 34.59           C  
ANISOU 3047  CZ  TYR A 388     4240   3881   5022    523    726    560       C  
ATOM   3048  OH  TYR A 388      13.025 -17.101  35.965  1.00 33.98           O  
ANISOU 3048  OH  TYR A 388     4214   3645   5050    574    936    589       O  
ATOM   3049  N   GLU A 389      11.077 -11.774  41.964  1.00 26.95           N  
ANISOU 3049  N   GLU A 389     3044   3466   3728     95    100    545       N  
ATOM   3050  CA  GLU A 389      11.230 -10.618  42.838  1.00 26.32           C  
ANISOU 3050  CA  GLU A 389     2982   3450   3568    -51     70    531       C  
ATOM   3051  C   GLU A 389      11.575  -9.387  41.999  1.00 28.65           C  
ANISOU 3051  C   GLU A 389     3332   3709   3846    -24    139    482       C  
ATOM   3052  O   GLU A 389      12.260  -9.512  40.977  1.00 28.09           O  
ANISOU 3052  O   GLU A 389     3233   3601   3840     73    181    517       O  
ATOM   3053  CB  GLU A 389      12.331 -10.882  43.869  1.00 31.38           C  
ANISOU 3053  CB  GLU A 389     3506   4192   4224   -194     -7    687       C  
ATOM   3054  CG  GLU A 389      12.251  -9.997  45.096  1.00 42.67           C  
ANISOU 3054  CG  GLU A 389     4990   5699   5522   -422    -49    665       C  
ATOM   3055  CD  GLU A 389      13.317 -10.326  46.126  1.00 49.76           C  
ANISOU 3055  CD  GLU A 389     5765   6729   6414   -617   -155    860       C  
ATOM   3056  OE1 GLU A 389      12.952 -10.564  47.295  1.00 51.58           O  
ANISOU 3056  OE1 GLU A 389     6004   7031   6564   -793   -226    873       O  
ATOM   3057  OE2 GLU A 389      14.514 -10.345  45.763  1.00 49.83           O  
ANISOU 3057  OE2 GLU A 389     5660   6774   6499   -608   -169   1019       O  
ATOM   3058  N   PRO A 390      11.082  -8.200  42.365  1.00 27.63           N  
ANISOU 3058  N   PRO A 390     3287   3574   3639   -105    176    397       N  
ATOM   3059  CA  PRO A 390      11.480  -6.984  41.650  1.00 27.46           C  
ANISOU 3059  CA  PRO A 390     3307   3519   3607    -90    246    362       C  
ATOM   3060  C   PRO A 390      12.990  -6.882  41.507  1.00 30.84           C  
ANISOU 3060  C   PRO A 390     3661   4001   4056   -127    217    468       C  
ATOM   3061  O   PRO A 390      13.743  -7.164  42.445  1.00 33.27           O  
ANISOU 3061  O   PRO A 390     3904   4396   4343   -262    148    577       O  
ATOM   3062  CB  PRO A 390      10.924  -5.866  42.537  1.00 28.78           C  
ANISOU 3062  CB  PRO A 390     3571   3670   3692   -226    311    283       C  
ATOM   3063  CG  PRO A 390       9.715  -6.462  43.130  1.00 31.08           C  
ANISOU 3063  CG  PRO A 390     3887   3939   3981   -221    306    242       C  
ATOM   3064  CD  PRO A 390      10.074  -7.912  43.400  1.00 30.73           C  
ANISOU 3064  CD  PRO A 390     3750   3963   3963   -207    189    326       C  
ATOM   3065  N   ASN A 391      13.420  -6.464  40.314  1.00 29.92           N  
ANISOU 3065  N   ASN A 391     3545   3840   3982    -20    267    458       N  
ATOM   3066  CA  ASN A 391      14.821  -6.436  39.907  1.00 31.48           C  
ANISOU 3066  CA  ASN A 391     3664   4068   4230    -11    259    568       C  
ATOM   3067  C   ASN A 391      15.108  -5.063  39.318  1.00 31.50           C  
ANISOU 3067  C   ASN A 391     3726   4054   4190    -18    309    508       C  
ATOM   3068  O   ASN A 391      14.522  -4.691  38.299  1.00 27.68           O  
ANISOU 3068  O   ASN A 391     3296   3500   3723     87    367    420       O  
ATOM   3069  CB  ASN A 391      15.079  -7.561  38.891  1.00 32.09           C  
ANISOU 3069  CB  ASN A 391     3691   4079   4423    147    298    612       C  
ATOM   3070  CG  ASN A 391      16.491  -7.567  38.317  1.00 34.59           C  
ANISOU 3070  CG  ASN A 391     3923   4392   4828    188    333    734       C  
ATOM   3071  OD1 ASN A 391      17.315  -6.698  38.593  1.00 33.32           O  
ANISOU 3071  OD1 ASN A 391     3730   4296   4636    105    303    798       O  
ATOM   3072  ND2 ASN A 391      16.765  -8.567  37.496  1.00 35.58           N  
ANISOU 3072  ND2 ASN A 391     4023   4430   5066    311    416    772       N  
ATOM   3073  N   GLU A 392      16.008  -4.307  39.951  1.00 32.55           N  
ANISOU 3073  N   GLU A 392     3848   4259   4260   -163    283    572       N  
ATOM   3074  CA  GLU A 392      16.327  -2.974  39.438  1.00 32.16           C  
ANISOU 3074  CA  GLU A 392     3862   4192   4164   -180    337    514       C  
ATOM   3075  C   GLU A 392      16.842  -3.001  37.997  1.00 30.37           C  
ANISOU 3075  C   GLU A 392     3595   3918   4026    -13    368    524       C  
ATOM   3076  O   GLU A 392      16.718  -1.996  37.285  1.00 32.37           O  
ANISOU 3076  O   GLU A 392     3906   4133   4262     23    422    445       O  
ATOM   3077  CB  GLU A 392      17.347  -2.302  40.369  1.00 40.11           C  
ANISOU 3077  CB  GLU A 392     4871   5300   5068   -398    291    606       C  
ATOM   3078  CG  GLU A 392      17.864  -0.964  39.913  1.00 59.91           C  
ANISOU 3078  CG  GLU A 392     7444   7801   7519   -435    343    563       C  
ATOM   3079  CD  GLU A 392      19.113  -1.085  39.055  1.00 73.70           C  
ANISOU 3079  CD  GLU A 392     9080   9582   9341   -347    303    689       C  
ATOM   3080  OE1 GLU A 392      19.880  -2.051  39.264  1.00 83.15           O  
ANISOU 3080  OE1 GLU A 392    10143  10839  10612   -346    232    865       O  
ATOM   3081  OE2 GLU A 392      19.319  -0.225  38.170  1.00 73.13           O  
ANISOU 3081  OE2 GLU A 392     9045   9470   9273   -275    355    626       O  
ATOM   3082  N   GLN A 393      17.386  -4.133  37.537  1.00 30.91           N  
ANISOU 3082  N   GLN A 393     3572   3973   4197     84    358    619       N  
ATOM   3083  CA  GLN A 393      17.850  -4.227  36.155  1.00 35.72           C  
ANISOU 3083  CA  GLN A 393     4173   4515   4884    221    421    614       C  
ATOM   3084  C   GLN A 393      16.719  -4.091  35.140  1.00 35.70           C  
ANISOU 3084  C   GLN A 393     4266   4435   4864    304    472    471       C  
ATOM   3085  O   GLN A 393      16.996  -3.821  33.964  1.00 33.62           O  
ANISOU 3085  O   GLN A 393     4026   4125   4622    370    520    441       O  
ATOM   3086  CB  GLN A 393      18.566  -5.562  35.932  1.00 36.09           C  
ANISOU 3086  CB  GLN A 393     4125   4526   5063    301    456    744       C  
ATOM   3087  CG  GLN A 393      19.772  -5.781  36.820  1.00 45.23           C  
ANISOU 3087  CG  GLN A 393     5138   5769   6278    222    403    959       C  
ATOM   3088  CD  GLN A 393      20.997  -5.107  36.271  1.00 59.31           C  
ANISOU 3088  CD  GLN A 393     6866   7569   8099    235    423   1055       C  
ATOM   3089  OE1 GLN A 393      21.206  -3.913  36.474  1.00 62.21           O  
ANISOU 3089  OE1 GLN A 393     7275   8006   8355    136    370   1023       O  
ATOM   3090  NE2 GLN A 393      21.807  -5.863  35.547  1.00 67.33           N  
ANISOU 3090  NE2 GLN A 393     7800   8506   9278    357    521   1171       N  
ATOM   3091  N   ASN A 394      15.466  -4.290  35.560  1.00 31.91           N  
ANISOU 3091  N   ASN A 394     3833   3946   4347    286    456    403       N  
ATOM   3092  CA  ASN A 394      14.315  -4.280  34.661  1.00 31.89           C  
ANISOU 3092  CA  ASN A 394     3895   3891   4332    338    482    324       C  
ATOM   3093  C   ASN A 394      13.621  -2.927  34.573  1.00 33.97           C  
ANISOU 3093  C   ASN A 394     4192   4151   4566    314    503    272       C  
ATOM   3094  O   ASN A 394      12.606  -2.819  33.870  1.00 33.51           O  
ANISOU 3094  O   ASN A 394     4155   4065   4513    341    513    254       O  
ATOM   3095  CB  ASN A 394      13.259  -5.308  35.096  1.00 29.35           C  
ANISOU 3095  CB  ASN A 394     3590   3559   4003    338    457    313       C  
ATOM   3096  CG  ASN A 394      13.789  -6.726  35.176  1.00 32.38           C  
ANISOU 3096  CG  ASN A 394     3944   3923   4436    369    465    367       C  
ATOM   3097  OD1 ASN A 394      13.295  -7.519  35.980  1.00 38.17           O  
ANISOU 3097  OD1 ASN A 394     4663   4671   5169    351    430    382       O  
ATOM   3098  ND2 ASN A 394      14.777  -7.060  34.349  1.00 31.78           N  
ANISOU 3098  ND2 ASN A 394     3858   3800   4416    419    531    403       N  
ATOM   3099  N   ILE A 395      14.098  -1.898  35.287  1.00 27.14           N  
ANISOU 3099  N   ILE A 395     3329   3310   3672    247    519    266       N  
ATOM   3100  CA  ILE A 395      13.336  -0.655  35.325  1.00 29.28           C  
ANISOU 3100  CA  ILE A 395     3639   3545   3941    228    588    220       C  
ATOM   3101  C   ILE A 395      13.529   0.103  34.023  1.00 31.38           C  
ANISOU 3101  C   ILE A 395     3893   3791   4238    288    612    218       C  
ATOM   3102  O   ILE A 395      14.576   0.025  33.371  1.00 38.73           O  
ANISOU 3102  O   ILE A 395     4807   4744   5164    311    586    233       O  
ATOM   3103  CB  ILE A 395      13.698   0.220  36.542  1.00 34.94           C  
ANISOU 3103  CB  ILE A 395     4406   4272   4596    101    636    195       C  
ATOM   3104  CG1 ILE A 395      15.165   0.647  36.492  1.00 36.12           C  
ANISOU 3104  CG1 ILE A 395     4545   4479   4700     45    605    230       C  
ATOM   3105  CG2 ILE A 395      13.333  -0.498  37.849  1.00 33.35           C  
ANISOU 3105  CG2 ILE A 395     4226   4094   4353      9    612    197       C  
ATOM   3106  CD1 ILE A 395      15.574   1.522  37.663  1.00 44.15           C  
ANISOU 3106  CD1 ILE A 395     5641   5520   5614   -139    648    214       C  
ATOM   3107  N   ALA A 396      12.489   0.849  33.647  1.00 33.11           N  
ANISOU 3107  N   ALA A 396     4110   3966   4505    311    668    220       N  
ATOM   3108  CA  ALA A 396      12.522   1.588  32.392  1.00 37.37           C  
ANISOU 3108  CA  ALA A 396     4621   4498   5082    351    680    243       C  
ATOM   3109  C   ALA A 396      13.489   2.765  32.432  1.00 46.26           C  
ANISOU 3109  C   ALA A 396     5762   5621   6193    331    729    212       C  
ATOM   3110  O   ALA A 396      13.944   3.212  31.373  1.00 52.93           O  
ANISOU 3110  O   ALA A 396     6583   6477   7051    361    714    223       O  
ATOM   3111  CB  ALA A 396      11.120   2.079  32.044  1.00 38.07           C  
ANISOU 3111  CB  ALA A 396     4664   4546   5253    372    727    309       C  
ATOM   3112  N   SER A 397      13.823   3.266  33.624  1.00 44.27           N  
ANISOU 3112  N   SER A 397     5563   5359   5899    254    787    175       N  
ATOM   3113  CA  SER A 397      14.727   4.404  33.759  1.00 49.32           C  
ANISOU 3113  CA  SER A 397     6243   6001   6497    199    839    146       C  
ATOM   3114  C   SER A 397      16.154   4.093  33.324  1.00 57.73           C  
ANISOU 3114  C   SER A 397     7282   7142   7509    198    741    171       C  
ATOM   3115  O   SER A 397      16.960   5.023  33.213  1.00 59.17           O  
ANISOU 3115  O   SER A 397     7487   7340   7655    160    763    162       O  
ATOM   3116  CB  SER A 397      14.737   4.895  35.208  1.00 50.03           C  
ANISOU 3116  CB  SER A 397     6431   6064   6513     57    930    101       C  
ATOM   3117  OG  SER A 397      13.422   5.149  35.670  1.00 55.55           O  
ANISOU 3117  OG  SER A 397     7158   6666   7281     64   1058     83       O  
ATOM   3118  N   LEU A 398      16.493   2.826  33.097  1.00 59.62           N  
ANISOU 3118  N   LEU A 398     7478   7419   7757    239    655    211       N  
ATOM   3119  CA  LEU A 398      17.833   2.488  32.649  1.00 63.34           C  
ANISOU 3119  CA  LEU A 398     7908   7937   8221    258    601    263       C  
ATOM   3120  C   LEU A 398      18.037   2.968  31.211  1.00 66.05           C  
ANISOU 3120  C   LEU A 398     8238   8257   8600    336    613    244       C  
ATOM   3121  O   LEU A 398      17.073   3.093  30.450  1.00 59.19           O  
ANISOU 3121  O   LEU A 398     7373   7351   7765    376    631    216       O  
ATOM   3122  CB  LEU A 398      18.065   0.981  32.743  1.00 62.10           C  
ANISOU 3122  CB  LEU A 398     7708   7788   8100    294    558    321       C  
ATOM   3123  CG  LEU A 398      17.959   0.346  34.132  1.00 62.40           C  
ANISOU 3123  CG  LEU A 398     7736   7864   8110    209    524    365       C  
ATOM   3124  CD1 LEU A 398      18.631  -1.018  34.138  1.00 65.48           C  
ANISOU 3124  CD1 LEU A 398     8050   8264   8567    253    494    467       C  
ATOM   3125  CD2 LEU A 398      18.551   1.248  35.211  1.00 62.60           C  
ANISOU 3125  CD2 LEU A 398     7788   7953   8043     55    512    391       C  
ATOM   3126  N   PRO A 399      19.291   3.236  30.804  1.00 69.94           N  
ANISOU 3126  N   PRO A 399     8708   8782   9086    345    595    279       N  
ATOM   3127  CA  PRO A 399      20.554   3.040  31.530  1.00 70.47           C  
ANISOU 3127  CA  PRO A 399     8737   8911   9129    290    556    372       C  
ATOM   3128  C   PRO A 399      21.010   4.226  32.391  1.00 65.54           C  
ANISOU 3128  C   PRO A 399     8151   8342   8408    160    551    378       C  
ATOM   3129  O   PRO A 399      20.748   5.383  32.051  1.00 67.25           O  
ANISOU 3129  O   PRO A 399     8418   8533   8599    152    599    305       O  
ATOM   3130  CB  PRO A 399      21.551   2.798  30.398  1.00 72.39           C  
ANISOU 3130  CB  PRO A 399     8934   9140   9430    376    563    417       C  
ATOM   3131  CG  PRO A 399      21.040   3.672  29.292  1.00 71.11           C  
ANISOU 3131  CG  PRO A 399     8813   8943   9261    415    589    321       C  
ATOM   3132  CD  PRO A 399      19.528   3.691  29.421  1.00 70.29           C  
ANISOU 3132  CD  PRO A 399     8747   8806   9156    406    607    255       C  
ATOM   3133  N   LEU A 400      21.698   3.917  33.492  1.00 57.52           N  
ANISOU 3133  N   LEU A 400     7114   7402   7337     38    498    481       N  
ATOM   3134  CA  LEU A 400      22.298   4.897  34.399  1.00 53.10           C  
ANISOU 3134  CA  LEU A 400     6614   6916   6647   -152    484    512       C  
ATOM   3135  C   LEU A 400      23.790   4.584  34.473  1.00 56.21           C  
ANISOU 3135  C   LEU A 400     6903   7412   7041   -199    391    704       C  
ATOM   3136  O   LEU A 400      24.272   3.989  35.439  1.00 58.50           O  
ANISOU 3136  O   LEU A 400     7136   7789   7301   -329    318    854       O  
ATOM   3137  CB  LEU A 400      21.638   4.849  35.776  1.00 56.17           C  
ANISOU 3137  CB  LEU A 400     7085   7317   6940   -325    501    485       C  
ATOM   3138  CG  LEU A 400      20.138   5.153  35.802  1.00 60.40           C  
ANISOU 3138  CG  LEU A 400     7710   7738   7503   -275    617    327       C  
ATOM   3139  CD1 LEU A 400      19.555   4.939  37.191  1.00 60.98           C  
ANISOU 3139  CD1 LEU A 400     7865   7815   7491   -447    645    307       C  
ATOM   3140  CD2 LEU A 400      19.886   6.569  35.342  1.00 56.72           C  
ANISOU 3140  CD2 LEU A 400     7327   7201   7021   -270    732    227       C  
ATOM   3141  N   GLU A 401      24.521   4.999  33.440  1.00 43.90           N  
ANISOU 3141  N   GLU A 401     5304   5848   5528   -100    393    723       N  
ATOM   3142  CA  GLU A 401      25.919   4.639  33.248  1.00 48.15           C  
ANISOU 3142  CA  GLU A 401     5716   6458   6121    -91    330    926       C  
ATOM   3143  C   GLU A 401      26.789   5.884  33.271  1.00 42.52           C  
ANISOU 3143  C   GLU A 401     5038   5825   5292   -211    293    964       C  
ATOM   3144  O   GLU A 401      26.458   6.888  32.633  1.00 37.79           O  
ANISOU 3144  O   GLU A 401     4529   5178   4652   -171    346    809       O  
ATOM   3145  CB  GLU A 401      26.115   3.913  31.915  1.00 54.88           C  
ANISOU 3145  CB  GLU A 401     6494   7216   7141    134    390    924       C  
ATOM   3146  CG  GLU A 401      25.352   2.612  31.794  1.00 63.40           C  
ANISOU 3146  CG  GLU A 401     7555   8209   8327    238    442    894       C  
ATOM   3147  CD  GLU A 401      26.005   1.486  32.573  1.00 77.09           C  
ANISOU 3147  CD  GLU A 401     9157   9984  10151    210    413   1115       C  
ATOM   3148  OE1 GLU A 401      27.223   1.572  32.839  1.00 79.49           O  
ANISOU 3148  OE1 GLU A 401     9347  10368  10486    156    366   1330       O  
ATOM   3149  OE2 GLU A 401      25.296   0.517  32.921  1.00 82.64           O  
ANISOU 3149  OE2 GLU A 401     9855  10642  10900    237    435   1096       O  
ATOM   3150  N   THR A 402      27.918   5.799  33.983  1.00 41.01           N  
ANISOU 3150  N   THR A 402     4763   5765   5054   -365    197   1196       N  
ATOM   3151  CA  THR A 402      28.819   6.943  34.095  1.00 36.23           C  
ANISOU 3151  CA  THR A 402     4197   5258   4312   -519    144   1262       C  
ATOM   3152  C   THR A 402      29.350   7.380  32.735  1.00 38.03           C  
ANISOU 3152  C   THR A 402     4386   5436   4629   -329    177   1225       C  
ATOM   3153  O   THR A 402      29.557   8.577  32.498  1.00 34.70           O  
ANISOU 3153  O   THR A 402     4057   5035   4094   -393    181   1143       O  
ATOM   3154  CB  THR A 402      29.990   6.618  35.021  1.00 46.16           C  
ANISOU 3154  CB  THR A 402     5334   6685   5520   -730     12   1582       C  
ATOM   3155  OG1 THR A 402      29.489   6.126  36.272  1.00 55.00           O  
ANISOU 3155  OG1 THR A 402     6484   7858   6554   -925    -27   1625       O  
ATOM   3156  CG2 THR A 402      30.816   7.872  35.276  1.00 43.12           C  
ANISOU 3156  CG2 THR A 402     5026   6418   4938   -952    -51   1644       C  
ATOM   3157  N   TRP A 403      29.600   6.432  31.825  1.00 36.06           N  
ANISOU 3157  N   TRP A 403     4013   5111   4577   -109    217   1283       N  
ATOM   3158  CA  TRP A 403      30.147   6.855  30.539  1.00 37.45           C  
ANISOU 3158  CA  TRP A 403     4167   5238   4824     43    256   1246       C  
ATOM   3159  C   TRP A 403      29.155   7.711  29.768  1.00 31.31           C  
ANISOU 3159  C   TRP A 403     3527   4374   3994    110    319    970       C  
ATOM   3160  O   TRP A 403      29.569   8.446  28.867  1.00 30.38           O  
ANISOU 3160  O   TRP A 403     3421   4248   3876    172    328    921       O  
ATOM   3161  CB  TRP A 403      30.584   5.654  29.693  1.00 32.33           C  
ANISOU 3161  CB  TRP A 403     3394   4495   4397    243    335   1346       C  
ATOM   3162  CG  TRP A 403      29.480   4.789  29.208  1.00 34.19           C  
ANISOU 3162  CG  TRP A 403     3682   4593   4714    369    434   1181       C  
ATOM   3163  CD1 TRP A 403      29.005   3.661  29.808  1.00 37.64           C  
ANISOU 3163  CD1 TRP A 403     4083   4997   5220    376    458   1230       C  
ATOM   3164  CD2 TRP A 403      28.705   4.963  28.013  1.00 33.78           C  
ANISOU 3164  CD2 TRP A 403     3731   4431   4674    480    513    957       C  
ATOM   3165  NE1 TRP A 403      27.988   3.122  29.063  1.00 37.97           N  
ANISOU 3165  NE1 TRP A 403     4209   4913   5306    484    551   1044       N  
ATOM   3166  CE2 TRP A 403      27.785   3.902  27.956  1.00 35.82           C  
ANISOU 3166  CE2 TRP A 403     4018   4598   4994    536    580    885       C  
ATOM   3167  CE3 TRP A 403      28.710   5.908  26.980  1.00 31.26           C  
ANISOU 3167  CE3 TRP A 403     3473   4093   4313    519    524    828       C  
ATOM   3168  CZ2 TRP A 403      26.868   3.761  26.916  1.00 37.42           C  
ANISOU 3168  CZ2 TRP A 403     4316   4703   5201    601    649    703       C  
ATOM   3169  CZ3 TRP A 403      27.801   5.768  25.945  1.00 35.33           C  
ANISOU 3169  CZ3 TRP A 403     4067   4511   4846    589    590    654       C  
ATOM   3170  CH2 TRP A 403      26.888   4.705  25.920  1.00 38.81           C  
ANISOU 3170  CH2 TRP A 403     4542   4873   5331    617    648    599       C  
ATOM   3171  N   ILE A 404      27.869   7.651  30.122  1.00 30.46           N  
ANISOU 3171  N   ILE A 404     3509   4210   3854     94    362    813       N  
ATOM   3172  CA  ILE A 404      26.860   8.521  29.523  1.00 27.72           C  
ANISOU 3172  CA  ILE A 404     3264   3789   3480    139    426    606       C  
ATOM   3173  C   ILE A 404      26.783   9.832  30.293  1.00 29.72           C  
ANISOU 3173  C   ILE A 404     3628   4084   3581    -31    437    551       C  
ATOM   3174  O   ILE A 404      27.140  10.893  29.768  1.00 30.52           O  
ANISOU 3174  O   ILE A 404     3764   4192   3640    -34    449    506       O  
ATOM   3175  CB  ILE A 404      25.479   7.850  29.486  1.00 30.88           C  
ANISOU 3175  CB  ILE A 404     3692   4100   3940    205    482    497       C  
ATOM   3176  CG1 ILE A 404      25.554   6.485  28.808  1.00 30.95           C  
ANISOU 3176  CG1 ILE A 404     3628   4057   4075    334    494    543       C  
ATOM   3177  CG2 ILE A 404      24.508   8.738  28.747  1.00 32.79           C  
ANISOU 3177  CG2 ILE A 404     3992   4275   4192    255    542    349       C  
ATOM   3178  CD1 ILE A 404      24.228   5.766  28.758  1.00 35.36           C  
ANISOU 3178  CD1 ILE A 404     4220   4542   4671    376    535    452       C  
ATOM   3179  N   TYR A 405      26.308   9.779  31.542  1.00 29.93           N  
ANISOU 3179  N   TYR A 405     3728   4127   3518   -189    453    547       N  
ATOM   3180  CA  TYR A 405      25.992  11.035  32.215  1.00 30.55           C  
ANISOU 3180  CA  TYR A 405     3961   4192   3455   -359    532    451       C  
ATOM   3181  C   TYR A 405      27.233  11.785  32.676  1.00 28.73           C  
ANISOU 3181  C   TYR A 405     3774   4078   3062   -556    469    554       C  
ATOM   3182  O   TYR A 405      27.147  12.989  32.933  1.00 34.40           O  
ANISOU 3182  O   TYR A 405     4636   4772   3662   -686    555    461       O  
ATOM   3183  CB  TYR A 405      25.038  10.801  33.391  1.00 30.68           C  
ANISOU 3183  CB  TYR A 405     4075   4167   3415   -489    604    393       C  
ATOM   3184  CG  TYR A 405      25.583   9.989  34.541  1.00 32.12           C  
ANISOU 3184  CG  TYR A 405     4237   4461   3505   -673    504    542       C  
ATOM   3185  CD1 TYR A 405      26.463  10.555  35.466  1.00 31.30           C  
ANISOU 3185  CD1 TYR A 405     4216   4473   3204   -960    455    640       C  
ATOM   3186  CD2 TYR A 405      25.185   8.671  34.728  1.00 38.08           C  
ANISOU 3186  CD2 TYR A 405     4894   5213   4363   -588    457    598       C  
ATOM   3187  CE1 TYR A 405      26.949   9.810  36.543  1.00 41.28           C  
ANISOU 3187  CE1 TYR A 405     5442   5862   4381  -1166    344    817       C  
ATOM   3188  CE2 TYR A 405      25.665   7.920  35.799  1.00 47.01           C  
ANISOU 3188  CE2 TYR A 405     5983   6452   5427   -762    361    760       C  
ATOM   3189  CZ  TYR A 405      26.548   8.495  36.700  1.00 47.28           C  
ANISOU 3189  CZ  TYR A 405     6079   6615   5271  -1056    297    881       C  
ATOM   3190  OH  TYR A 405      27.020   7.749  37.758  1.00 49.53           O  
ANISOU 3190  OH  TYR A 405     6303   7028   5489  -1261    182   1080       O  
ATOM   3191  N   GLY A 406      28.383  11.122  32.775  1.00 30.04           N  
ANISOU 3191  N   GLY A 406     3817   4366   3230   -590    333    763       N  
ATOM   3192  CA  GLY A 406      29.579  11.828  33.179  1.00 30.41           C  
ANISOU 3192  CA  GLY A 406     3888   4546   3118   -796    251    903       C  
ATOM   3193  C   GLY A 406      30.330  12.527  32.067  1.00 31.72           C  
ANISOU 3193  C   GLY A 406     4010   4721   3319   -675    231    906       C  
ATOM   3194  O   GLY A 406      31.336  13.191  32.335  1.00 33.56           O  
ANISOU 3194  O   GLY A 406     4267   5071   3415   -846    158   1025       O  
ATOM   3195  N   HIS A 407      29.859  12.411  30.829  1.00 28.60           N  
ANISOU 3195  N   HIS A 407     3560   4218   3091   -410    287    784       N  
ATOM   3196  CA  HIS A 407      30.617  12.844  29.663  1.00 26.85           C  
ANISOU 3196  CA  HIS A 407     3270   4004   2927   -276    257    801       C  
ATOM   3197  C   HIS A 407      30.476  14.345  29.440  1.00 34.78           C  
ANISOU 3197  C   HIS A 407     4405   4989   3822   -341    316    659       C  
ATOM   3198  O   HIS A 407      29.389  14.909  29.611  1.00 30.72           O  
ANISOU 3198  O   HIS A 407     4003   4376   3294   -355    436    489       O  
ATOM   3199  CB  HIS A 407      30.123  12.095  28.430  1.00 29.76           C  
ANISOU 3199  CB  HIS A 407     3551   4266   3492    -17    301    725       C  
ATOM   3200  CG  HIS A 407      30.899  12.396  27.189  1.00 32.24           C  
ANISOU 3200  CG  HIS A 407     3800   4579   3872    112    281    741       C  
ATOM   3201  ND1 HIS A 407      32.241  12.114  27.065  1.00 31.78           N  
ANISOU 3201  ND1 HIS A 407     3635   4598   3842    117    213    941       N  
ATOM   3202  CD2 HIS A 407      30.520  12.965  26.021  1.00 29.81           C  
ANISOU 3202  CD2 HIS A 407     3510   4204   3612    229    323    598       C  
ATOM   3203  CE1 HIS A 407      32.658  12.499  25.872  1.00 32.26           C  
ANISOU 3203  CE1 HIS A 407     3669   4628   3959    240    225    896       C  
ATOM   3204  NE2 HIS A 407      31.634  13.020  25.219  1.00 27.44           N  
ANISOU 3204  NE2 HIS A 407     3136   3937   3352    299    283    685       N  
ATOM   3205  N   ASP A 408      31.583  14.977  29.042  1.00 29.31           N  
ANISOU 3205  N   ASP A 408     3688   4380   3071   -370    246    744       N  
ATOM   3206  CA  ASP A 408      31.658  16.402  28.685  1.00 28.59           C  
ANISOU 3206  CA  ASP A 408     3703   4274   2884   -416    295    629       C  
ATOM   3207  C   ASP A 408      31.834  16.473  27.169  1.00 29.97           C  
ANISOU 3207  C   ASP A 408     3772   4408   3209   -177    280    583       C  
ATOM   3208  O   ASP A 408      32.958  16.419  26.652  1.00 26.39           O  
ANISOU 3208  O   ASP A 408     3229   4032   2766   -138    189    710       O  
ATOM   3209  CB  ASP A 408      32.815  17.085  29.423  1.00 33.08           C  
ANISOU 3209  CB  ASP A 408     4340   4989   3241   -671    212    769       C  
ATOM   3210  CG  ASP A 408      32.934  18.569  29.118  1.00 40.20           C  
ANISOU 3210  CG  ASP A 408     5373   5871   4029   -738    277    647       C  
ATOM   3211  OD1 ASP A 408      32.291  19.064  28.161  1.00 31.61           O  
ANISOU 3211  OD1 ASP A 408     4277   4671   3062   -551    365    487       O  
ATOM   3212  OD2 ASP A 408      33.691  19.249  29.850  1.00 35.23           O  
ANISOU 3212  OD2 ASP A 408     4855   5348   3182  -1001    237    730       O  
ATOM   3213  N   SER A 409      30.709  16.615  26.459  1.00 28.01           N  
ANISOU 3213  N   SER A 409     3166   3955   3523    370    -75    889       N  
ATOM   3214  CA  SER A 409      30.737  16.553  25.003  1.00 22.65           C  
ANISOU 3214  CA  SER A 409     2477   3202   2928    264    -85    815       C  
ATOM   3215  C   SER A 409      31.516  17.710  24.391  1.00 26.13           C  
ANISOU 3215  C   SER A 409     2976   3676   3275    154   -158    711       C  
ATOM   3216  O   SER A 409      32.160  17.540  23.349  1.00 24.26           O  
ANISOU 3216  O   SER A 409     2699   3440   3078     83   -170    663       O  
ATOM   3217  CB  SER A 409      29.307  16.533  24.459  1.00 27.24           C  
ANISOU 3217  CB  SER A 409     3067   3705   3580    250    -57    841       C  
ATOM   3218  OG  SER A 409      28.594  17.731  24.782  1.00 27.68           O  
ANISOU 3218  OG  SER A 409     3206   3778   3532    289    -63    849       O  
ATOM   3219  N   GLN A 410      31.459  18.890  25.005  1.00 28.03           N  
ANISOU 3219  N   GLN A 410     3334   3932   3384    138   -198    680       N  
ATOM   3220  CA  GLN A 410      32.188  20.030  24.455  1.00 25.03           C  
ANISOU 3220  CA  GLN A 410     3037   3556   2916      1   -265    590       C  
ATOM   3221  C   GLN A 410      33.697  19.811  24.528  1.00 25.52           C  
ANISOU 3221  C   GLN A 410     2999   3760   2937    -89   -327    591       C  
ATOM   3222  O   GLN A 410      34.411  20.023  23.536  1.00 25.92           O  
ANISOU 3222  O   GLN A 410     3002   3841   3006   -192   -355    561       O  
ATOM   3223  CB  GLN A 410      31.787  21.306  25.194  1.00 30.98           C  
ANISOU 3223  CB  GLN A 410     4001   4251   3519      2   -281    553       C  
ATOM   3224  CG  GLN A 410      32.431  22.563  24.639  1.00 29.64           C  
ANISOU 3224  CG  GLN A 410     3969   4035   3259   -165   -340    463       C  
ATOM   3225  CD  GLN A 410      31.879  23.812  25.285  1.00 35.76           C  
ANISOU 3225  CD  GLN A 410     5025   4683   3879   -140   -323    418       C  
ATOM   3226  OE1 GLN A 410      30.694  24.117  25.155  1.00 31.37           O  
ANISOU 3226  OE1 GLN A 410     4560   4032   3329      9   -232    455       O  
ATOM   3227  NE2 GLN A 410      32.729  24.535  26.000  1.00 40.27           N  
ANISOU 3227  NE2 GLN A 410     5746   5262   4293   -283   -406    350       N  
ATOM   3228  N   ALA A 411      34.203  19.401  25.697  1.00 25.56           N  
ANISOU 3228  N   ALA A 411     2952   3887   2873    -41   -345    649       N  
ATOM   3229  CA  ALA A 411      35.638  19.181  25.850  1.00 28.87           C  
ANISOU 3229  CA  ALA A 411     3234   4508   3229   -114   -404    694       C  
ATOM   3230  C   ALA A 411      36.125  18.100  24.896  1.00 27.92           C  
ANISOU 3230  C   ALA A 411     2953   4420   3233    -42   -335    753       C  
ATOM   3231  O   ALA A 411      37.199  18.229  24.288  1.00 27.12           O  
ANISOU 3231  O   ALA A 411     2751   4452   3100   -121   -367    777       O  
ATOM   3232  CB  ALA A 411      35.964  18.804  27.295  1.00 32.02           C  
ANISOU 3232  CB  ALA A 411     3583   5061   3523    -40   -423    771       C  
ATOM   3233  N   TYR A 412      35.349  17.021  24.766  1.00 27.76           N  
ANISOU 3233  N   TYR A 412     2923   4280   3343    106   -232    787       N  
ATOM   3234  CA  TYR A 412      35.682  15.958  23.822  1.00 30.74           C  
ANISOU 3234  CA  TYR A 412     3229   4624   3827    184   -148    818       C  
ATOM   3235  C   TYR A 412      35.801  16.502  22.405  1.00 28.09           C  
ANISOU 3235  C   TYR A 412     2923   4239   3511     79   -171    730       C  
ATOM   3236  O   TYR A 412      36.751  16.183  21.677  1.00 25.64           O  
ANISOU 3236  O   TYR A 412     2531   4017   3193    101   -143    762       O  
ATOM   3237  CB  TYR A 412      34.614  14.861  23.882  1.00 30.19           C  
ANISOU 3237  CB  TYR A 412     3208   4376   3887    294    -51    841       C  
ATOM   3238  CG  TYR A 412      34.907  13.688  22.973  1.00 28.93           C  
ANISOU 3238  CG  TYR A 412     3050   4126   3817    373     49    854       C  
ATOM   3239  CD1 TYR A 412      34.483  13.690  21.647  1.00 28.90           C  
ANISOU 3239  CD1 TYR A 412     3122   3992   3867    297     52    751       C  
ATOM   3240  CD2 TYR A 412      35.617  12.578  23.442  1.00 28.00           C  
ANISOU 3240  CD2 TYR A 412     2880   4051   3709    542    151    973       C  
ATOM   3241  CE1 TYR A 412      34.763  12.627  20.805  1.00 26.89           C  
ANISOU 3241  CE1 TYR A 412     2922   3631   3663    370    148    741       C  
ATOM   3242  CE2 TYR A 412      35.889  11.504  22.613  1.00 28.90           C  
ANISOU 3242  CE2 TYR A 412     3056   4041   3884    642    268    980       C  
ATOM   3243  CZ  TYR A 412      35.450  11.529  21.293  1.00 28.67           C  
ANISOU 3243  CZ  TYR A 412     3136   3859   3898    548    263    851       C  
ATOM   3244  OH  TYR A 412      35.726  10.479  20.450  1.00 30.59           O  
ANISOU 3244  OH  TYR A 412     3494   3957   4173    647    382    835       O  
ATOM   3245  N   THR A 413      34.841  17.328  21.998  1.00 24.95           N  
ANISOU 3245  N   THR A 413     2633   3720   3125     -9   -206    642       N  
ATOM   3246  CA  THR A 413      34.849  17.865  20.643  1.00 27.25           C  
ANISOU 3246  CA  THR A 413     2951   3971   3430    -95   -220    571       C  
ATOM   3247  C   THR A 413      36.074  18.746  20.410  1.00 27.11           C  
ANISOU 3247  C   THR A 413     2882   4102   3318   -209   -286    581       C  
ATOM   3248  O   THR A 413      36.720  18.667  19.359  1.00 27.17           O  
ANISOU 3248  O   THR A 413     2826   4164   3332   -223   -269    587       O  
ATOM   3249  CB  THR A 413      33.563  18.652  20.395  1.00 25.04           C  
ANISOU 3249  CB  THR A 413     2785   3569   3160   -140   -234    513       C  
ATOM   3250  OG1 THR A 413      32.427  17.782  20.539  1.00 26.02           O  
ANISOU 3250  OG1 THR A 413     2916   3600   3371    -65   -183    534       O  
ATOM   3251  CG2 THR A 413      33.558  19.233  18.994  1.00 23.38           C  
ANISOU 3251  CG2 THR A 413     2592   3338   2951   -215   -244    456       C  
ATOM   3252  N   GLU A 414      36.401  19.600  21.379  1.00 24.09           N  
ANISOU 3252  N   GLU A 414     2532   3790   2832   -305   -363    589       N  
ATOM   3253  CA  GLU A 414      37.586  20.439  21.251  1.00 23.22           C  
ANISOU 3253  CA  GLU A 414     2368   3834   2620   -473   -446    614       C  
ATOM   3254  C   GLU A 414      38.844  19.591  21.060  1.00 28.10           C  
ANISOU 3254  C   GLU A 414     2768   4679   3228   -413   -423    735       C  
ATOM   3255  O   GLU A 414      39.684  19.876  20.198  1.00 31.34           O  
ANISOU 3255  O   GLU A 414     3083   5209   3617   -485   -435    780       O  
ATOM   3256  CB  GLU A 414      37.720  21.333  22.490  1.00 28.03           C  
ANISOU 3256  CB  GLU A 414     3079   4476   3095   -605   -542    593       C  
ATOM   3257  CG  GLU A 414      36.566  22.306  22.651  1.00 27.15           C  
ANISOU 3257  CG  GLU A 414     3218   4137   2961   -629   -538    491       C  
ATOM   3258  CD  GLU A 414      36.571  23.028  23.981  1.00 37.26           C  
ANISOU 3258  CD  GLU A 414     4660   5410   4087   -710   -608    454       C  
ATOM   3259  OE1 GLU A 414      37.244  22.555  24.915  1.00 40.06           O  
ANISOU 3259  OE1 GLU A 414     4908   5946   4368   -718   -659    509       O  
ATOM   3260  OE2 GLU A 414      35.885  24.063  24.104  1.00 38.35           O  
ANISOU 3260  OE2 GLU A 414     5046   5364   4160   -747   -602    376       O  
ATOM   3261  N   GLN A 415      38.978  18.527  21.853  1.00 23.61           N  
ANISOU 3261  N   GLN A 415     2116   4185   2669   -254   -372    815       N  
ATOM   3262  CA  GLN A 415      40.179  17.702  21.804  1.00 27.49           C  
ANISOU 3262  CA  GLN A 415     2403   4915   3128   -144   -323    969       C  
ATOM   3263  C   GLN A 415      40.283  16.934  20.501  1.00 27.77           C  
ANISOU 3263  C   GLN A 415     2422   4883   3246      3   -203    978       C  
ATOM   3264  O   GLN A 415      41.390  16.726  19.980  1.00 30.01           O  
ANISOU 3264  O   GLN A 415     2552   5375   3477     57   -167   1099       O  
ATOM   3265  CB  GLN A 415      40.163  16.700  22.954  1.00 29.77           C  
ANISOU 3265  CB  GLN A 415     2637   5265   3411     32   -266   1062       C  
ATOM   3266  CG  GLN A 415      40.508  17.241  24.284  1.00 42.42           C  
ANISOU 3266  CG  GLN A 415     4191   7050   4877    -75   -378   1105       C  
ATOM   3267  CD  GLN A 415      40.432  16.140  25.306  1.00 40.32           C  
ANISOU 3267  CD  GLN A 415     3861   6842   4615    142   -296   1216       C  
ATOM   3268  OE1 GLN A 415      39.345  15.769  25.751  1.00 39.49           O  
ANISOU 3268  OE1 GLN A 415     3888   6527   4590    233   -244   1159       O  
ATOM   3269  NE2 GLN A 415      41.572  15.568  25.636  1.00 41.97           N  
ANISOU 3269  NE2 GLN A 415     3877   7326   4742    238   -253   1387       N  
ATOM   3270  N   GLU A 416      39.153  16.443  20.005  1.00 26.56           N  
ANISOU 3270  N   GLU A 416     2425   4462   3203     78   -135    867       N  
ATOM   3271  CA  GLU A 416      39.136  15.498  18.901  1.00 26.99           C  
ANISOU 3271  CA  GLU A 416     2521   4414   3318    227    -14    853       C  
ATOM   3272  C   GLU A 416      38.899  16.154  17.553  1.00 28.78           C  
ANISOU 3272  C   GLU A 416     2808   4575   3554    130    -38    754       C  
ATOM   3273  O   GLU A 416      38.999  15.468  16.534  1.00 26.26           O  
ANISOU 3273  O   GLU A 416     2533   4194   3249    244     53    733       O  
ATOM   3274  CB  GLU A 416      38.051  14.442  19.143  1.00 28.50           C  
ANISOU 3274  CB  GLU A 416     2855   4360   3613    331     65    797       C  
ATOM   3275  CG  GLU A 416      38.410  13.442  20.237  1.00 25.73           C  
ANISOU 3275  CG  GLU A 416     2454   4059   3264    503    148    927       C  
ATOM   3276  CD  GLU A 416      39.533  12.521  19.804  1.00 37.97           C  
ANISOU 3276  CD  GLU A 416     3944   5710   4772    720    285   1051       C  
ATOM   3277  OE1 GLU A 416      39.293  11.647  18.934  1.00 36.33           O  
ANISOU 3277  OE1 GLU A 416     3888   5305   4612    832    402    997       O  
ATOM   3278  OE2 GLU A 416      40.668  12.698  20.295  1.00 36.96           O  
ANISOU 3278  OE2 GLU A 416     3624   5874   4544    778    278   1209       O  
ATOM   3279  N   PHE A 417      38.591  17.457  17.524  1.00 26.06           N  
ANISOU 3279  N   PHE A 417     2486   4231   3184    -64   -147    696       N  
ATOM   3280  CA  PHE A 417      38.138  18.096  16.292  1.00 26.13           C  
ANISOU 3280  CA  PHE A 417     2565   4156   3206   -141   -160    608       C  
ATOM   3281  C   PHE A 417      39.076  17.825  15.116  1.00 24.36           C  
ANISOU 3281  C   PHE A 417     2260   4052   2944    -63    -97    660       C  
ATOM   3282  O   PHE A 417      38.635  17.372  14.049  1.00 26.10           O  
ANISOU 3282  O   PHE A 417     2563   4167   3185      9    -38    585       O  
ATOM   3283  CB  PHE A 417      37.984  19.598  16.502  1.00 25.13           C  
ANISOU 3283  CB  PHE A 417     2477   4035   3037   -336   -261    582       C  
ATOM   3284  CG  PHE A 417      37.508  20.324  15.265  1.00 25.76           C  
ANISOU 3284  CG  PHE A 417     2623   4042   3124   -395   -260    521       C  
ATOM   3285  CD1 PHE A 417      36.180  20.265  14.890  1.00 25.36           C  
ANISOU 3285  CD1 PHE A 417     2684   3831   3122   -364   -241    434       C  
ATOM   3286  CD2 PHE A 417      38.400  21.031  14.476  1.00 30.62           C  
ANISOU 3286  CD2 PHE A 417     3165   4782   3689   -477   -275    576       C  
ATOM   3287  CE1 PHE A 417      35.733  20.906  13.745  1.00 24.62           C  
ANISOU 3287  CE1 PHE A 417     2630   3707   3017   -399   -236    398       C  
ATOM   3288  CE2 PHE A 417      37.958  21.685  13.328  1.00 29.30           C  
ANISOU 3288  CE2 PHE A 417     3054   4557   3523   -510   -261    536       C  
ATOM   3289  CZ  PHE A 417      36.630  21.613  12.965  1.00 27.26           C  
ANISOU 3289  CZ  PHE A 417     2909   4146   3304   -461   -241    445       C  
ATOM   3290  N   GLU A 418      40.372  18.091  15.289  1.00 26.85           N  
ANISOU 3290  N   GLU A 418     2407   4611   3185    -79   -110    800       N  
ATOM   3291  CA  GLU A 418      41.281  17.989  14.147  1.00 33.00           C  
ANISOU 3291  CA  GLU A 418     3087   5541   3911      5    -44    884       C  
ATOM   3292  C   GLU A 418      41.402  16.555  13.653  1.00 29.57           C  
ANISOU 3292  C   GLU A 418     2705   5051   3479    279    110    893       C  
ATOM   3293  O   GLU A 418      41.562  16.325  12.446  1.00 27.44           O  
ANISOU 3293  O   GLU A 418     2475   4774   3176    382    186    874       O  
ATOM   3294  CB  GLU A 418      42.656  18.552  14.509  1.00 38.61           C  
ANISOU 3294  CB  GLU A 418     3567   6574   4531    -84    -94   1075       C  
ATOM   3295  CG  GLU A 418      42.678  20.062  14.765  1.00 45.11           C  
ANISOU 3295  CG  GLU A 418     4385   7425   5329   -396   -241   1060       C  
ATOM   3296  CD  GLU A 418      42.241  20.893  13.554  1.00 55.82           C  
ANISOU 3296  CD  GLU A 418     5834   8667   6709   -480   -243    984       C  
ATOM   3297  OE1 GLU A 418      42.392  20.424  12.401  1.00 55.55           O  
ANISOU 3297  OE1 GLU A 418     5776   8660   6671   -322   -147   1000       O  
ATOM   3298  OE2 GLU A 418      41.743  22.024  13.758  1.00 55.75           O  
ANISOU 3298  OE2 GLU A 418     5939   8537   6707   -688   -329    913       O  
ATOM   3299  N   MET A 419      41.311  15.586  14.566  1.00 27.90           N  
ANISOU 3299  N   MET A 419     2522   4783   3295    409    166    921       N  
ATOM   3300  CA  MET A 419      41.356  14.181  14.172  1.00 29.88           C  
ANISOU 3300  CA  MET A 419     2892   4914   3547    671    331    922       C  
ATOM   3301  C   MET A 419      40.125  13.803  13.349  1.00 28.61           C  
ANISOU 3301  C   MET A 419     2979   4448   3446    637    345    714       C  
ATOM   3302  O   MET A 419      40.234  13.072  12.354  1.00 29.54           O  
ANISOU 3302  O   MET A 419     3230   4475   3519    786    456    668       O  
ATOM   3303  CB  MET A 419      41.453  13.295  15.415  1.00 31.51           C  
ANISOU 3303  CB  MET A 419     3086   5107   3778    801    392   1012       C  
ATOM   3304  CG  MET A 419      41.953  11.888  15.158  1.00 59.01           C  
ANISOU 3304  CG  MET A 419     6664   8528   7228   1121    598   1093       C  
ATOM   3305  SD  MET A 419      43.719  11.869  14.780  1.00 82.76           S  
ANISOU 3305  SD  MET A 419     9422  11939  10083   1354    709   1365       S  
ATOM   3306  CE  MET A 419      44.396  12.588  16.277  1.00 85.99           C  
ANISOU 3306  CE  MET A 419     9509  12707  10455   1212    571   1558       C  
ATOM   3307  N   VAL A 420      38.941  14.276  13.760  1.00 24.67           N  
ANISOU 3307  N   VAL A 420     2546   3803   3025    444    234    597       N  
ATOM   3308  CA  VAL A 420      37.722  13.980  13.009  1.00 23.48           C  
ANISOU 3308  CA  VAL A 420     2583   3425   2915    373    222    429       C  
ATOM   3309  C   VAL A 420      37.755  14.659  11.645  1.00 24.07           C  
ANISOU 3309  C   VAL A 420     2662   3559   2925    320    196    367       C  
ATOM   3310  O   VAL A 420      37.299  14.093  10.645  1.00 26.35           O  
ANISOU 3310  O   VAL A 420     3105   3726   3182    346    234    255       O  
ATOM   3311  CB  VAL A 420      36.479  14.406  13.807  1.00 24.27           C  
ANISOU 3311  CB  VAL A 420     2702   3422   3096    204    119    373       C  
ATOM   3312  CG1 VAL A 420      35.222  13.988  13.063  1.00 25.31           C  
ANISOU 3312  CG1 VAL A 420     2987   3373   3257    117    102    237       C  
ATOM   3313  CG2 VAL A 420      36.498  13.810  15.220  1.00 25.13           C  
ANISOU 3313  CG2 VAL A 420     2788   3503   3258    268    147    455       C  
ATOM   3314  N   VAL A 421      38.281  15.887  11.583  1.00 23.15           N  
ANISOU 3314  N   VAL A 421     2391   3628   2777    231    128    440       N  
ATOM   3315  CA  VAL A 421      38.446  16.573  10.297  1.00 24.65           C  
ANISOU 3315  CA  VAL A 421     2563   3900   2902    201    119    419       C  
ATOM   3316  C   VAL A 421      39.242  15.702   9.333  1.00 27.43           C  
ANISOU 3316  C   VAL A 421     2958   4296   3166    412    249    441       C  
ATOM   3317  O   VAL A 421      38.840  15.490   8.182  1.00 29.61           O  
ANISOU 3317  O   VAL A 421     3356   4506   3386    441    275    335       O  
ATOM   3318  CB  VAL A 421      39.119  17.943  10.498  1.00 27.25           C  
ANISOU 3318  CB  VAL A 421     2727   4416   3212     72     47    531       C  
ATOM   3319  CG1 VAL A 421      39.618  18.507   9.160  1.00 30.34           C  
ANISOU 3319  CG1 VAL A 421     3066   4932   3529     88     73    566       C  
ATOM   3320  CG2 VAL A 421      38.134  18.915  11.154  1.00 25.68           C  
ANISOU 3320  CG2 VAL A 421     2572   4118   3069   -114    -59    475       C  
ATOM   3321  N   ARG A 422      40.368  15.155   9.805  1.00 27.53           N  
ANISOU 3321  N   ARG A 422     2879   4436   3146    582    340    587       N  
ATOM   3322  CA  ARG A 422      41.185  14.306   8.946  1.00 32.54           C  
ANISOU 3322  CA  ARG A 422     3568   5119   3675    844    499    639       C  
ATOM   3323  C   ARG A 422      40.405  13.081   8.480  1.00 31.11           C  
ANISOU 3323  C   ARG A 422     3694   4642   3483    942    582    462       C  
ATOM   3324  O   ARG A 422      40.477  12.710   7.304  1.00 34.17           O  
ANISOU 3324  O   ARG A 422     4229   4986   3767   1057    660    388       O  
ATOM   3325  CB  ARG A 422      42.475  13.909   9.673  1.00 33.13           C  
ANISOU 3325  CB  ARG A 422     3469   5412   3708   1035    595    868       C  
ATOM   3326  CG  ARG A 422      43.524  15.018   9.631  1.00 47.00           C  
ANISOU 3326  CG  ARG A 422     4925   7519   5414    952    536   1066       C  
ATOM   3327  CD  ARG A 422      44.816  14.659  10.360  1.00 62.24           C  
ANISOU 3327  CD  ARG A 422     6627   9742   7279   1118    614   1330       C  
ATOM   3328  NE  ARG A 422      45.172  13.255  10.200  1.00 79.10           N  
ANISOU 3328  NE  ARG A 422     8895  11810   9350   1484    825   1383       N  
ATOM   3329  CZ  ARG A 422      45.329  12.411  11.215  1.00 95.72           C  
ANISOU 3329  CZ  ARG A 422    11008  13890  11472   1630    900   1465       C  
ATOM   3330  NH1 ARG A 422      45.175  12.838  12.463  1.00 95.95           N  
ANISOU 3330  NH1 ARG A 422    10899  13987  11570   1434    765   1499       N  
ATOM   3331  NH2 ARG A 422      45.653  11.144  10.988  1.00104.80           N  
ANISOU 3331  NH2 ARG A 422    12323  14941  12554   1987   1121   1518       N  
ATOM   3332  N   ALA A 423      39.631  12.456   9.376  1.00 28.11           N  
ANISOU 3332  N   ALA A 423     3429   4055   3199    879    561    391       N  
ATOM   3333  CA  ALA A 423      38.812  11.316   8.967  1.00 31.29           C  
ANISOU 3333  CA  ALA A 423     4140   4153   3596    900    620    221       C  
ATOM   3334  C   ALA A 423      37.789  11.718   7.905  1.00 31.68           C  
ANISOU 3334  C   ALA A 423     4295   4129   3613    704    513     38       C  
ATOM   3335  O   ALA A 423      37.604  11.006   6.909  1.00 33.49           O  
ANISOU 3335  O   ALA A 423     4764   4219   3741    760    574    -92       O  
ATOM   3336  CB  ALA A 423      38.114  10.703  10.183  1.00 29.91           C  
ANISOU 3336  CB  ALA A 423     4027   3793   3543    826    602    210       C  
ATOM   3337  N   VAL A 424      37.117  12.857   8.097  1.00 27.22           N  
ANISOU 3337  N   VAL A 424     3567   3664   3111    484    359     33       N  
ATOM   3338  CA  VAL A 424      36.094  13.282   7.144  1.00 28.11           C  
ANISOU 3338  CA  VAL A 424     3741   3755   3184    312    259   -102       C  
ATOM   3339  C   VAL A 424      36.719  13.571   5.783  1.00 30.25           C  
ANISOU 3339  C   VAL A 424     4024   4156   3312    420    308   -115       C  
ATOM   3340  O   VAL A 424      36.207  13.149   4.738  1.00 32.54           O  
ANISOU 3340  O   VAL A 424     4492   4372   3499    393    303   -259       O  
ATOM   3341  CB  VAL A 424      35.343  14.509   7.689  1.00 27.53           C  
ANISOU 3341  CB  VAL A 424     3489   3778   3194    119    123    -60       C  
ATOM   3342  CG1 VAL A 424      34.471  15.128   6.611  1.00 29.68           C  
ANISOU 3342  CG1 VAL A 424     3769   4110   3400     -8     40   -141       C  
ATOM   3343  CG2 VAL A 424      34.495  14.108   8.878  1.00 35.23           C  
ANISOU 3343  CG2 VAL A 424     4485   4618   4283     19     79    -63       C  
ATOM   3344  N   GLN A 425      37.843  14.290   5.777  1.00 30.56           N  
ANISOU 3344  N   GLN A 425     3871   4410   3332    531    350     43       N  
ATOM   3345  CA  GLN A 425      38.462  14.699   4.517  1.00 30.83           C  
ANISOU 3345  CA  GLN A 425     3874   4607   3236    638    399     71       C  
ATOM   3346  C   GLN A 425      39.139  13.533   3.812  1.00 36.27           C  
ANISOU 3346  C   GLN A 425     4762   5232   3788    901    564     38       C  
ATOM   3347  O   GLN A 425      39.195  13.505   2.580  1.00 36.37           O  
ANISOU 3347  O   GLN A 425     4873   5287   3657    980    602    -28       O  
ATOM   3348  CB  GLN A 425      39.459  15.830   4.775  1.00 32.95           C  
ANISOU 3348  CB  GLN A 425     3863   5130   3526    641    390    278       C  
ATOM   3349  CG  GLN A 425      38.781  17.120   5.227  1.00 34.07           C  
ANISOU 3349  CG  GLN A 425     3879   5303   3764    393    247    292       C  
ATOM   3350  CD  GLN A 425      39.747  18.267   5.452  1.00 38.04           C  
ANISOU 3350  CD  GLN A 425     4157   6018   4280    340    228    480       C  
ATOM   3351  OE1 GLN A 425      40.907  18.063   5.793  1.00 42.91           O  
ANISOU 3351  OE1 GLN A 425     4648   6782   4873    443    290    629       O  
ATOM   3352  NE2 GLN A 425      39.254  19.491   5.276  1.00 48.88           N  
ANISOU 3352  NE2 GLN A 425     5480   7412   5680    170    144    488       N  
ATOM   3353  N   GLU A 426      39.656  12.568   4.564  1.00 30.71           N  
ANISOU 3353  N   GLU A 426     4137   4426   3107   1064    676     91       N  
ATOM   3354  CA  GLU A 426      40.295  11.410   3.960  1.00 35.68           C  
ANISOU 3354  CA  GLU A 426     5006   4956   3593   1361    869     71       C  
ATOM   3355  C   GLU A 426      39.316  10.277   3.694  1.00 36.79           C  
ANISOU 3355  C   GLU A 426     5537   4742   3700   1297    880   -170       C  
ATOM   3356  O   GLU A 426      39.691   9.290   3.048  1.00 41.73           O  
ANISOU 3356  O   GLU A 426     6460   5218   4179   1524   1042   -237       O  
ATOM   3357  CB  GLU A 426      41.441  10.918   4.853  1.00 39.88           C  
ANISOU 3357  CB  GLU A 426     5432   5577   4142   1617   1018    290       C  
ATOM   3358  CG  GLU A 426      42.594  11.909   4.967  1.00 49.76           C  
ANISOU 3358  CG  GLU A 426     6306   7221   5381   1683   1019    553       C  
ATOM   3359  CD  GLU A 426      43.515  11.606   6.138  1.00 63.01           C  
ANISOU 3359  CD  GLU A 426     7798   9044   7098   1833   1098    786       C  
ATOM   3360  OE1 GLU A 426      43.481  10.462   6.641  1.00 61.39           O  
ANISOU 3360  OE1 GLU A 426     7791   8639   6895   2006   1223    769       O  
ATOM   3361  OE2 GLU A 426      44.262  12.516   6.565  1.00 67.46           O  
ANISOU 3361  OE2 GLU A 426     8023   9927   7684   1762   1033    992       O  
ATOM   3362  N   GLY A 427      38.078  10.399   4.169  1.00 41.84           N  
ANISOU 3362  N   GLY A 427     6194   5246   4457    990    718   -291       N  
ATOM   3363  CA  GLY A 427      37.095   9.349   3.989  1.00 40.93           C  
ANISOU 3363  CA  GLY A 427     6421   4812   4317    857    702   -500       C  
ATOM   3364  C   GLY A 427      37.411   8.092   4.762  1.00 44.49           C  
ANISOU 3364  C   GLY A 427     7097   5000   4806   1017    858   -479       C  
ATOM   3365  O   GLY A 427      37.133   6.987   4.280  1.00 50.38           O  
ANISOU 3365  O   GLY A 427     8235   5451   5455   1040    940   -639       O  
ATOM   3366  N   GLU A 428      38.012   8.229   5.939  1.00 38.82           N  
ANISOU 3366  N   GLU A 428     6159   4379   4210   1130    907   -281       N  
ATOM   3367  CA  GLU A 428      38.331   7.099   6.800  1.00 44.40           C  
ANISOU 3367  CA  GLU A 428     7037   4871   4963   1307   1065   -215       C  
ATOM   3368  C   GLU A 428      37.332   7.031   7.950  1.00 40.96           C  
ANISOU 3368  C   GLU A 428     6541   4313   4710   1050    943   -226       C  
ATOM   3369  O   GLU A 428      36.630   7.997   8.252  1.00 36.68           O  
ANISOU 3369  O   GLU A 428     5760   3917   4258    797    756   -230       O  
ATOM   3370  CB  GLU A 428      39.755   7.209   7.358  1.00 45.59           C  
ANISOU 3370  CB  GLU A 428     6962   5265   5096   1644   1217     51       C  
ATOM   3371  CG  GLU A 428      40.852   7.434   6.313  1.00 54.31           C  
ANISOU 3371  CG  GLU A 428     8030   6584   6022   1921   1341    136       C  
ATOM   3372  CD  GLU A 428      41.257   6.168   5.572  1.00 66.69           C  
ANISOU 3372  CD  GLU A 428    10023   7900   7418   2240   1585     71       C  
ATOM   3373  OE1 GLU A 428      40.588   5.126   5.739  1.00 69.32           O  
ANISOU 3373  OE1 GLU A 428    10727   7845   7769   2190   1638    -82       O  
ATOM   3374  OE2 GLU A 428      42.255   6.217   4.819  1.00 69.64           O  
ANISOU 3374  OE2 GLU A 428    10373   8457   7629   2545   1733    183       O  
ATOM   3375  N   GLU A 429      37.276   5.869   8.594  1.00 42.06           N  
ANISOU 3375  N   GLU A 429     6911   4175   4892   1140   1071   -214       N  
ATOM   3376  CA  GLU A 429      36.424   5.727   9.766  1.00 45.52           C  
ANISOU 3376  CA  GLU A 429     7280   4514   5502    938    984   -184       C  
ATOM   3377  C   GLU A 429      37.030   6.471  10.946  1.00 44.57           C  
ANISOU 3377  C   GLU A 429     6779   4681   5473   1035    963     39       C  
ATOM   3378  O   GLU A 429      38.253   6.518  11.114  1.00 42.89           O  
ANISOU 3378  O   GLU A 429     6444   4652   5199   1320   1088    205       O  
ATOM   3379  CB  GLU A 429      36.225   4.251  10.117  1.00 49.12           C  
ANISOU 3379  CB  GLU A 429     8107   4577   5980   1008   1143   -216       C  
ATOM   3380  CG  GLU A 429      35.400   3.502   9.088  1.00 62.19           C  
ANISOU 3380  CG  GLU A 429    10176   5904   7548    802   1121   -466       C  
ATOM   3381  CD  GLU A 429      35.335   2.010   9.348  1.00 76.32           C  
ANISOU 3381  CD  GLU A 429    12406   7254   9339    882   1307   -503       C  
ATOM   3382  OE1 GLU A 429      34.972   1.617  10.478  1.00 83.14           O  
ANISOU 3382  OE1 GLU A 429    13223   8012  10355    827   1323   -393       O  
ATOM   3383  OE2 GLU A 429      35.653   1.233   8.421  1.00 76.47           O  
ANISOU 3383  OE2 GLU A 429    12840   7019   9195   1012   1449   -637       O  
ATOM   3384  N   TYR A 430      36.162   7.080  11.744  1.00 38.65           N  
ANISOU 3384  N   TYR A 430     5842   3994   4849    791    799     51       N  
ATOM   3385  CA  TYR A 430      36.538   7.684  13.012  1.00 33.71           C  
ANISOU 3385  CA  TYR A 430     4919   3588   4301    838    765    231       C  
ATOM   3386  C   TYR A 430      36.025   6.779  14.123  1.00 38.66           C  
ANISOU 3386  C   TYR A 430     5639   4014   5037    838    823    289       C  
ATOM   3387  O   TYR A 430      34.818   6.508  14.201  1.00 38.28           O  
ANISOU 3387  O   TYR A 430     5698   3782   5066    604    742    194       O  
ATOM   3388  CB  TYR A 430      35.963   9.094  13.146  1.00 36.03           C  
ANISOU 3388  CB  TYR A 430     4965   4092   4633    605    563    214       C  
ATOM   3389  CG  TYR A 430      36.192   9.695  14.516  1.00 31.04           C  
ANISOU 3389  CG  TYR A 430     4091   3641   4063    615    514    365       C  
ATOM   3390  CD1 TYR A 430      37.481   9.962  14.961  1.00 31.93           C  
ANISOU 3390  CD1 TYR A 430     4028   3987   4118    797    570    523       C  
ATOM   3391  CD2 TYR A 430      35.125   9.969  15.370  1.00 28.76           C  
ANISOU 3391  CD2 TYR A 430     3750   3311   3868    444    413    361       C  
ATOM   3392  CE1 TYR A 430      37.709  10.494  16.214  1.00 33.60           C  
ANISOU 3392  CE1 TYR A 430     4039   4373   4355    780    510    647       C  
ATOM   3393  CE2 TYR A 430      35.343  10.503  16.630  1.00 29.85           C  
ANISOU 3393  CE2 TYR A 430     3705   3606   4031    467    374    485       C  
ATOM   3394  CZ  TYR A 430      36.640  10.765  17.046  1.00 35.27           C  
ANISOU 3394  CZ  TYR A 430     4241   4510   4650    622    414    614       C  
ATOM   3395  OH  TYR A 430      36.873  11.299  18.292  1.00 34.55           O  
ANISOU 3395  OH  TYR A 430     3984   4589   4555    617    357    723       O  
ATOM   3396  N   HIS A 431      36.938   6.294  14.961  1.00 34.17           N  
ANISOU 3396  N   HIS A 431     5013   3504   4465   1100    965    468       N  
ATOM   3397  CA  HIS A 431      36.595   5.452  16.107  1.00 38.97           C  
ANISOU 3397  CA  HIS A 431     5682   3953   5171   1147   1044    566       C  
ATOM   3398  C   HIS A 431      36.487   6.339  17.344  1.00 38.40           C  
ANISOU 3398  C   HIS A 431     5290   4143   5158   1076    918    687       C  
ATOM   3399  O   HIS A 431      37.491   6.651  17.994  1.00 37.14           O  
ANISOU 3399  O   HIS A 431     4920   4246   4945   1254    953    852       O  
ATOM   3400  CB  HIS A 431      37.625   4.344  16.293  1.00 47.17           C  
ANISOU 3400  CB  HIS A 431     6867   4902   6153   1512   1297    708       C  
ATOM   3401  CG  HIS A 431      37.548   3.282  15.242  1.00 68.67           C  
ANISOU 3401  CG  HIS A 431    10008   7266   8816   1586   1448    574       C  
ATOM   3402  ND1 HIS A 431      38.544   2.350  15.044  1.00 78.20           N  
ANISOU 3402  ND1 HIS A 431    11414   8372   9925   1964   1709    680       N  
ATOM   3403  CD2 HIS A 431      36.588   3.010  14.327  1.00 74.72           C  
ANISOU 3403  CD2 HIS A 431    11051   7754   9584   1331   1377    342       C  
ATOM   3404  CE1 HIS A 431      38.200   1.549  14.051  1.00 81.52           C  
ANISOU 3404  CE1 HIS A 431    12260   8426  10288   1941   1799    497       C  
ATOM   3405  NE2 HIS A 431      37.018   1.929  13.597  1.00 78.07           N  
ANISOU 3405  NE2 HIS A 431    11871   7885   9908   1536   1587    284       N  
ATOM   3406  N   ALA A 432      35.258   6.726  17.671  1.00 32.66           N  
ANISOU 3406  N   ALA A 432     4533   3358   4519    815    775    615       N  
ATOM   3407  CA  ALA A 432      35.019   7.626  18.789  1.00 31.77           C  
ANISOU 3407  CA  ALA A 432     4169   3463   4438    747    659    704       C  
ATOM   3408  C   ALA A 432      35.288   6.924  20.113  1.00 33.09           C  
ANISOU 3408  C   ALA A 432     4293   3633   4645    921    765    882       C  
ATOM   3409  O   ALA A 432      35.051   5.721  20.255  1.00 38.22           O  
ANISOU 3409  O   ALA A 432     5135   4032   5356    998    901    916       O  
ATOM   3410  CB  ALA A 432      33.579   8.142  18.752  1.00 33.62           C  
ANISOU 3410  CB  ALA A 432     4396   3637   4741    474    513    610       C  
ATOM   3411  N   THR A 433      35.795   7.681  21.088  1.00 31.63           N  
ANISOU 3411  N   THR A 433     3872   3731   4414    975    703    997       N  
ATOM   3412  CA  THR A 433      36.007   7.155  22.431  1.00 34.62           C  
ANISOU 3412  CA  THR A 433     4173   4173   4808   1135    782   1175       C  
ATOM   3413  C   THR A 433      35.091   7.823  23.448  1.00 32.45           C  
ANISOU 3413  C   THR A 433     3790   3972   4568    995    658   1188       C  
ATOM   3414  O   THR A 433      35.413   7.860  24.643  1.00 40.20           O  
ANISOU 3414  O   THR A 433     4640   5123   5510   1108    669   1329       O  
ATOM   3415  CB  THR A 433      37.469   7.294  22.864  1.00 38.00           C  
ANISOU 3415  CB  THR A 433     4415   4908   5113   1353    834   1338       C  
ATOM   3416  OG1 THR A 433      37.856   8.672  22.829  1.00 38.12           O  
ANISOU 3416  OG1 THR A 433     4243   5203   5039   1208    662   1296       O  
ATOM   3417  CG2 THR A 433      38.381   6.467  21.956  1.00 39.23           C  
ANISOU 3417  CG2 THR A 433     4685   4998   5222   1573   1009   1379       C  
ATOM   3418  N   ASN A 434      33.955   8.348  22.994  1.00 25.67           N  
ANISOU 3418  N   ASN A 434     2980   3010   3762    772    548   1059       N  
ATOM   3419  CA  ASN A 434      32.924   8.861  23.882  1.00 25.86           C  
ANISOU 3419  CA  ASN A 434     2933   3076   3817    675    465   1090       C  
ATOM   3420  C   ASN A 434      31.856   7.811  24.163  1.00 30.36           C  
ANISOU 3420  C   ASN A 434     3606   3418   4513    634    539   1147       C  
ATOM   3421  O   ASN A 434      30.713   8.155  24.488  1.00 30.12           O  
ANISOU 3421  O   ASN A 434     3534   3387   4522    509    471   1160       O  
ATOM   3422  CB  ASN A 434      32.309  10.146  23.310  1.00 26.31           C  
ANISOU 3422  CB  ASN A 434     2956   3203   3837    490    318    965       C  
ATOM   3423  CG  ASN A 434      31.775   9.979  21.895  1.00 27.54           C  
ANISOU 3423  CG  ASN A 434     3227   3201   4035    341    297    832       C  
ATOM   3424  OD1 ASN A 434      31.714   8.876  21.357  1.00 27.94           O  
ANISOU 3424  OD1 ASN A 434     3417   3055   4145    339    381    809       O  
ATOM   3425  ND2 ASN A 434      31.359  11.093  21.295  1.00 24.46           N  
ANISOU 3425  ND2 ASN A 434     2800   2893   3601    213    188    743       N  
ATOM   3426  N   LEU A 435      32.212   6.542  23.995  1.00 30.09           N  
ANISOU 3426  N   LEU A 435     3714   3187   4533    736    685   1192       N  
ATOM   3427  CA  LEU A 435      31.448   5.388  24.441  1.00 33.56           C  
ANISOU 3427  CA  LEU A 435     4269   3392   5089    717    786   1285       C  
ATOM   3428  C   LEU A 435      32.438   4.259  24.669  1.00 30.98           C  
ANISOU 3428  C   LEU A 435     4060   2948   4763    970    984   1392       C  
ATOM   3429  O   LEU A 435      33.558   4.310  24.149  1.00 33.79           O  
ANISOU 3429  O   LEU A 435     4430   3378   5031   1122   1035   1366       O  
ATOM   3430  CB  LEU A 435      30.384   4.984  23.404  1.00 35.88           C  
ANISOU 3430  CB  LEU A 435     4733   3440   5460    446    741   1158       C  
ATOM   3431  CG  LEU A 435      30.838   4.283  22.117  1.00 35.67           C  
ANISOU 3431  CG  LEU A 435     4962   3176   5415    420    809   1014       C  
ATOM   3432  CD1 LEU A 435      29.637   3.673  21.431  1.00 33.54           C  
ANISOU 3432  CD1 LEU A 435     4871   2656   5218    116    763    925       C  
ATOM   3433  CD2 LEU A 435      31.560   5.223  21.160  1.00 32.69           C  
ANISOU 3433  CD2 LEU A 435     4530   2968   4925    441    730    877       C  
ATOM   3434  N   PRO A 436      32.075   3.244  25.452  1.00 37.64           N  
ANISOU 3434  N   PRO A 436     4980   3627   5695   1042   1112   1541       N  
ATOM   3435  CA  PRO A 436      33.042   2.182  25.758  1.00 35.77           C  
ANISOU 3435  CA  PRO A 436     4833   3350   5408   1285   1300   1615       C  
ATOM   3436  C   PRO A 436      33.528   1.493  24.494  1.00 43.23           C  
ANISOU 3436  C   PRO A 436     6059   4030   6337   1322   1409   1503       C  
ATOM   3437  O   PRO A 436      32.767   1.289  23.546  1.00 37.48           O  
ANISOU 3437  O   PRO A 436     5551   3010   5681   1104   1374   1370       O  
ATOM   3438  CB  PRO A 436      32.249   1.227  26.661  1.00 32.63           C  
ANISOU 3438  CB  PRO A 436     4482   2820   5097   1240   1374   1708       C  
ATOM   3439  CG  PRO A 436      31.183   2.085  27.263  1.00 34.98           C  
ANISOU 3439  CG  PRO A 436     4589   3258   5443   1072   1218   1743       C  
ATOM   3440  CD  PRO A 436      30.805   3.046  26.172  1.00 37.04           C  
ANISOU 3440  CD  PRO A 436     4865   3486   5724    887   1077   1625       C  
ATOM   3441  N   ASP A 437      34.820   1.144  24.500  1.00 42.05           N  
ANISOU 3441  N   ASP A 437     5897   4017   6064   1588   1541   1559       N  
ATOM   3442  CA  ASP A 437      35.490   0.592  23.327  1.00 51.01           C  
ANISOU 3442  CA  ASP A 437     7275   4976   7129   1692   1661   1468       C  
ATOM   3443  C   ASP A 437      34.715  -0.574  22.723  1.00 56.44           C  
ANISOU 3443  C   ASP A 437     8345   5210   7892   1549   1744   1352       C  
ATOM   3444  O   ASP A 437      34.410  -0.584  21.525  1.00 60.61           O  
ANISOU 3444  O   ASP A 437     9103   5509   8417   1404   1708   1174       O  
ATOM   3445  CB  ASP A 437      36.901   0.151  23.720  1.00 51.38           C  
ANISOU 3445  CB  ASP A 437     7234   5267   7023   2005   1829   1617       C  
ATOM   3446  CG  ASP A 437      37.728  -0.299  22.532  1.00 58.84           C  
ANISOU 3446  CG  ASP A 437     8394   6109   7855   2160   1963   1557       C  
ATOM   3447  OD1 ASP A 437      37.494   0.194  21.411  1.00 64.79           O  
ANISOU 3447  OD1 ASP A 437     9255   6743   8618   2050   1878   1396       O  
ATOM   3448  OD2 ASP A 437      38.612  -1.153  22.729  1.00 62.75           O  
ANISOU 3448  OD2 ASP A 437     8953   6652   8236   2400   2165   1684       O  
ATOM   3449  N   LYS A 438      34.385  -1.569  23.536  1.00 59.73           N  
ANISOU 3449  N   LYS A 438     8837   5499   8360   1567   1847   1442       N  
ATOM   3450  CA  LYS A 438      33.743  -2.749  22.981  1.00 68.64           C  
ANISOU 3450  CA  LYS A 438    10341   6201   9537   1417   1920   1336       C  
ATOM   3451  C   LYS A 438      32.279  -2.504  22.635  1.00 63.29           C  
ANISOU 3451  C   LYS A 438     9728   5332   8987   1001   1728   1219       C  
ATOM   3452  O   LYS A 438      31.706  -3.267  21.850  1.00 56.27           O  
ANISOU 3452  O   LYS A 438     9154   4113   8112    785   1723   1077       O  
ATOM   3453  CB  LYS A 438      33.900  -3.921  23.954  1.00 75.48           C  
ANISOU 3453  CB  LYS A 438    11273   6990  10415   1575   2104   1489       C  
ATOM   3454  CG  LYS A 438      35.359  -4.135  24.382  1.00 81.06           C  
ANISOU 3454  CG  LYS A 438    11868   7960  10971   1974   2303   1645       C  
ATOM   3455  CD  LYS A 438      35.698  -5.602  24.641  1.00 88.50           C  
ANISOU 3455  CD  LYS A 438    13073   8681  11874   2156   2561   1730       C  
ATOM   3456  CE  LYS A 438      35.519  -5.996  26.102  1.00 87.87           C  
ANISOU 3456  CE  LYS A 438    12811   8725  11852   2237   2632   1927       C  
ATOM   3457  NZ  LYS A 438      36.654  -5.580  26.988  1.00 82.95           N  
ANISOU 3457  NZ  LYS A 438    11854   8569  11096   2524   2716   2128       N  
ATOM   3458  N   LEU A 439      31.679  -1.429  23.153  1.00 64.06           N  
ANISOU 3458  N   LEU A 439     9529   5659   9153    872   1564   1278       N  
ATOM   3459  CA  LEU A 439      30.246  -1.223  22.966  1.00 60.90           C  
ANISOU 3459  CA  LEU A 439     9132   5147   8859    478   1397   1224       C  
ATOM   3460  C   LEU A 439      29.893  -1.005  21.500  1.00 61.79           C  
ANISOU 3460  C   LEU A 439     9447   5091   8940    220   1299    999       C  
ATOM   3461  O   LEU A 439      28.860  -1.493  21.030  1.00 64.55           O  
ANISOU 3461  O   LEU A 439     9949   5243   9332   -126   1205    910       O  
ATOM   3462  CB  LEU A 439      29.762  -0.044  23.808  1.00 56.60           C  
ANISOU 3462  CB  LEU A 439     8215   4928   8361    445   1268   1350       C  
ATOM   3463  CG  LEU A 439      28.241   0.011  23.946  1.00 57.46           C  
ANISOU 3463  CG  LEU A 439     8259   5001   8571     86   1132   1379       C  
ATOM   3464  CD1 LEU A 439      27.721  -1.324  24.454  1.00 64.52           C  
ANISOU 3464  CD1 LEU A 439     9318   5671   9524      1   1205   1453       C  
ATOM   3465  CD2 LEU A 439      27.827   1.132  24.874  1.00 52.06           C  
ANISOU 3465  CD2 LEU A 439     7212   4668   7901    126   1033   1520       C  
ATOM   3466  N   ARG A 440      30.737  -0.281  20.761  1.00 66.06           N  
ANISOU 3466  N   ARG A 440     9974   5736   9387    370   1307    909       N  
ATOM   3467  CA  ARG A 440      30.439  -0.021  19.356  1.00 78.93           C  
ANISOU 3467  CA  ARG A 440    11769   7272  10947    137   1198    674       C  
ATOM   3468  C   ARG A 440      30.283  -1.316  18.571  1.00 88.24           C  
ANISOU 3468  C   ARG A 440    13360   8087  12080     21   1266    526       C  
ATOM   3469  O   ARG A 440      29.265  -1.527  17.905  1.00 97.05           O  
ANISOU 3469  O   ARG A 440    14595   9078  13202   -355   1123    389       O  
ATOM   3470  CB  ARG A 440      31.522   0.845  18.722  1.00 83.71           C  
ANISOU 3470  CB  ARG A 440    12252   8135  11419    361   1184    601       C  
ATOM   3471  CG  ARG A 440      31.310   1.028  17.224  1.00 90.51           C  
ANISOU 3471  CG  ARG A 440    13294   8919  12179    164   1087    358       C  
ATOM   3472  CD  ARG A 440      32.231   2.085  16.637  1.00 93.54           C  
ANISOU 3472  CD  ARG A 440    13483   9614  12443    341   1042    313       C  
ATOM   3473  NE  ARG A 440      33.640   1.751  16.828  1.00 94.20           N  
ANISOU 3473  NE  ARG A 440    13606   9727  12458    753   1249    425       N  
ATOM   3474  CZ  ARG A 440      34.403   2.260  17.789  1.00 86.61           C  
ANISOU 3474  CZ  ARG A 440    12344   9060  11502    987   1280    616       C  
ATOM   3475  NH1 ARG A 440      33.890   3.131  18.648  1.00 75.67           N  
ANISOU 3475  NH1 ARG A 440    10647   7920  10186    855   1124    689       N  
ATOM   3476  NH2 ARG A 440      35.676   1.896  17.891  1.00 86.33           N  
ANISOU 3476  NH2 ARG A 440    12328   9090  11385   1357   1470    745       N  
ATOM   3477  N   VAL A 441      31.282  -2.199  18.639  1.00 84.15           N  
ANISOU 3477  N   VAL A 441    13026   7457  11488    338   1469    558       N  
ATOM   3478  CA  VAL A 441      31.205  -3.448  17.887  1.00 82.48           C  
ANISOU 3478  CA  VAL A 441    13218   6914  11205    260   1547    416       C  
ATOM   3479  C   VAL A 441      30.159  -4.387  18.487  1.00 90.28           C  
ANISOU 3479  C   VAL A 441    14296   7694  12313     -5   1510    468       C  
ATOM   3480  O   VAL A 441      29.551  -5.188  17.766  1.00 93.41           O  
ANISOU 3480  O   VAL A 441    14981   7827  12683   -270   1465    319       O  
ATOM   3481  CB  VAL A 441      32.601  -4.101  17.816  1.00 79.29           C  
ANISOU 3481  CB  VAL A 441    12976   6479  10670    702   1804    470       C  
ATOM   3482  CG1 VAL A 441      32.540  -5.465  17.129  1.00 76.03           C  
ANISOU 3482  CG1 VAL A 441    13019   5699  10171    651   1921    342       C  
ATOM   3483  CG2 VAL A 441      33.571  -3.185  17.085  1.00 79.70           C  
ANISOU 3483  CG2 VAL A 441    12929   6756  10597    927   1819    427       C  
ATOM   3484  N   GLN A 442      29.897  -4.282  19.794  1.00 93.75           N  
ANISOU 3484  N   GLN A 442    14480   8264  12876     47   1516    685       N  
ATOM   3485  CA  GLN A 442      29.021  -5.249  20.455  1.00102.89           C  
ANISOU 3485  CA  GLN A 442    15717   9230  14146   -154   1510    776       C  
ATOM   3486  C   GLN A 442      27.557  -5.081  20.058  1.00100.48           C  
ANISOU 3486  C   GLN A 442    15364   8894  13922   -659   1267    708       C  
ATOM   3487  O   GLN A 442      26.786  -6.047  20.124  1.00105.79           O  
ANISOU 3487  O   GLN A 442    16192   9341  14663   -908   1239    720       O  
ATOM   3488  CB  GLN A 442      29.162  -5.143  21.977  1.00110.65           C  
ANISOU 3488  CB  GLN A 442    16419  10409  15213     64   1587   1036       C  
ATOM   3489  CG  GLN A 442      30.345  -5.918  22.564  1.00117.85           C  
ANISOU 3489  CG  GLN A 442    17423  11294  16061    493   1851   1147       C  
ATOM   3490  CD  GLN A 442      30.613  -5.580  24.024  1.00116.76           C  
ANISOU 3490  CD  GLN A 442    16942  11456  15967    731   1908   1385       C  
ATOM   3491  OE1 GLN A 442      29.945  -4.724  24.609  1.00115.85           O  
ANISOU 3491  OE1 GLN A 442    16531  11563  15922    601   1757   1463       O  
ATOM   3492  NE2 GLN A 442      31.597  -6.253  24.618  1.00113.65           N  
ANISOU 3492  NE2 GLN A 442    16578  11096  15507   1088   2135   1506       N  
ATOM   3493  N   LEU A 443      27.152  -3.881  19.642  1.00 91.32           N  
ANISOU 3493  N   LEU A 443    13972   7975  12749   -819   1095    654       N  
ATOM   3494  CA  LEU A 443      25.745  -3.564  19.423  1.00 88.67           C  
ANISOU 3494  CA  LEU A 443    13475   7733  12483  -1266    868    652       C  
ATOM   3495  C   LEU A 443      25.331  -3.605  17.952  1.00 88.51           C  
ANISOU 3495  C   LEU A 443    13625   7647  12359  -1559    735    396       C  
ATOM   3496  O   LEU A 443      24.190  -3.250  17.635  1.00 90.49           O  
ANISOU 3496  O   LEU A 443    13691   8056  12634  -1913    546    386       O  
ATOM   3497  CB  LEU A 443      25.421  -2.187  20.011  1.00 82.52           C  
ANISOU 3497  CB  LEU A 443    12292   7321  11740  -1258    772    791       C  
ATOM   3498  CG  LEU A 443      25.005  -2.103  21.484  1.00 77.39           C  
ANISOU 3498  CG  LEU A 443    11388   6822  11194  -1183    801   1068       C  
ATOM   3499  CD1 LEU A 443      25.153  -0.684  22.016  1.00 76.62           C  
ANISOU 3499  CD1 LEU A 443    10942   7083  11089  -1012    782   1165       C  
ATOM   3500  CD2 LEU A 443      23.579  -2.565  21.642  1.00 75.12           C  
ANISOU 3500  CD2 LEU A 443    11013   6527  11002  -1581    656   1177       C  
ATOM   3501  N   GLY A 444      26.211  -4.035  17.050  1.00 82.43           N  
ANISOU 3501  N   GLY A 444    13183   6687  11449  -1401    838    202       N  
ATOM   3502  CA  GLY A 444      25.885  -4.004  15.638  1.00 83.79           C  
ANISOU 3502  CA  GLY A 444    13519   6836  11481  -1648    712    -43       C  
ATOM   3503  C   GLY A 444      26.025  -2.638  15.002  1.00 82.22           C  
ANISOU 3503  C   GLY A 444    13109   6937  11194  -1642    594   -123       C  
ATOM   3504  O   GLY A 444      25.564  -2.449  13.868  1.00 92.18           O  
ANISOU 3504  O   GLY A 444    14425   8266  12334  -1882    449   -301       O  
ATOM   3505  N   ILE A 445      26.655  -1.684  15.694  1.00 68.49           N  
ANISOU 3505  N   ILE A 445    11134   5387   9500  -1375    654      7       N  
ATOM   3506  CA  ILE A 445      26.717  -0.316  15.206  1.00 67.37           C  
ANISOU 3506  CA  ILE A 445    10776   5529   9291  -1393    540    -44       C  
ATOM   3507  C   ILE A 445      27.674  -0.244  14.024  1.00 78.99           C  
ANISOU 3507  C   ILE A 445    12491   6928  10593  -1222    603   -248       C  
ATOM   3508  O   ILE A 445      28.812  -0.729  14.095  1.00 80.79           O  
ANISOU 3508  O   ILE A 445    12914   7000  10782   -867    810   -243       O  
ATOM   3509  CB  ILE A 445      27.140   0.631  16.340  1.00 60.36           C  
ANISOU 3509  CB  ILE A 445     9561   4880   8493  -1137    594    161       C  
ATOM   3510  CG1 ILE A 445      26.166   0.516  17.519  1.00 58.14           C  
ANISOU 3510  CG1 ILE A 445     9065   4665   8362  -1288    553    377       C  
ATOM   3511  CG2 ILE A 445      27.217   2.081  15.844  1.00 57.77           C  
ANISOU 3511  CG2 ILE A 445     8913   4956   8080  -1099    441    112       C  
ATOM   3512  CD1 ILE A 445      26.375   1.542  18.600  1.00 52.21           C  
ANISOU 3512  CD1 ILE A 445     7910   4272   7657  -1036    542    561       C  
ATOM   3513  N   ARG A 446      27.210   0.357  12.929  1.00 83.16           N  
ANISOU 3513  N   ARG A 446    12980   7610  11004  -1451    430   -405       N  
ATOM   3514  CA  ARG A 446      27.994   0.555  11.715  1.00 87.40           C  
ANISOU 3514  CA  ARG A 446    13716   8128  11364  -1314    465   -596       C  
ATOM   3515  C   ARG A 446      28.329   2.038  11.588  1.00 92.56           C  
ANISOU 3515  C   ARG A 446    14011   9167  11990  -1184    381   -556       C  
ATOM   3516  O   ARG A 446      27.421   2.871  11.489  1.00 93.16           O  
ANISOU 3516  O   ARG A 446    13794   9525  12076  -1421    186   -527       O  
ATOM   3517  CB  ARG A 446      27.224   0.069  10.486  1.00 88.12           C  
ANISOU 3517  CB  ARG A 446    13975   8191  11314  -1630    318   -789       C  
ATOM   3518  CG  ARG A 446      28.025   0.075   9.197  1.00 89.83           C  
ANISOU 3518  CG  ARG A 446    14446   8361  11325  -1473    375   -985       C  
ATOM   3519  CD  ARG A 446      27.133   0.350   7.991  1.00 92.30           C  
ANISOU 3519  CD  ARG A 446    14725   8851  11493  -1807    155  -1137       C  
ATOM   3520  NE  ARG A 446      27.866   0.258   6.730  1.00 95.14           N  
ANISOU 3520  NE  ARG A 446    15350   9158  11643  -1655    215  -1321       N  
ATOM   3521  CZ  ARG A 446      27.775  -0.766   5.885  1.00101.71           C  
ANISOU 3521  CZ  ARG A 446    16533   9778  12335  -1740    239  -1471       C  
ATOM   3522  NH1 ARG A 446      26.973  -1.788   6.158  1.00103.78           N  
ANISOU 3522  NH1 ARG A 446    16935   9849  12647  -2002    200  -1470       N  
ATOM   3523  NH2 ARG A 446      28.481  -0.768   4.761  1.00103.66           N  
ANISOU 3523  NH2 ARG A 446    17000  10003  12384  -1564    303  -1617       N  
ATOM   3524  N   ASN A 447      29.625   2.363  11.592  1.00 96.75           N  
ANISOU 3524  N   ASN A 447    14508   9775  12477   -781    526   -522       N  
ATOM   3525  CA  ASN A 447      30.060   3.757  11.549  1.00 97.21           C  
ANISOU 3525  CA  ASN A 447    14186  10235  12515   -631    449   -456       C  
ATOM   3526  C   ASN A 447      29.576   4.444  10.273  1.00 93.21           C  
ANISOU 3526  C   ASN A 447    13642   9899  11876   -834    286   -608       C  
ATOM   3527  O   ASN A 447      29.451   3.823   9.213  1.00 98.92           O  
ANISOU 3527  O   ASN A 447    14680  10440  12466   -955    282   -793       O  
ATOM   3528  CB  ASN A 447      31.588   3.849  11.642  1.00101.60           C  
ANISOU 3528  CB  ASN A 447    14739  10843  13022   -203    632   -387       C  
ATOM   3529  CG  ASN A 447      32.101   3.790  13.077  1.00103.19           C  
ANISOU 3529  CG  ASN A 447    14762  11098  13347     20    737   -170       C  
ATOM   3530  OD1 ASN A 447      31.357   4.036  14.028  1.00101.08           O  
ANISOU 3530  OD1 ASN A 447    14298  10905  13201   -119    651    -66       O  
ATOM   3531  ND2 ASN A 447      33.384   3.477  13.234  1.00104.01           N  
ANISOU 3531  ND2 ASN A 447    14919  11199  13402    383    927    -82       N  
ATOM   3532  N   VAL A 448      29.303   5.744  10.382  1.00 83.83           N  
ANISOU 3532  N   VAL A 448    12085   9059  10708   -861    157   -527       N  
ATOM   3533  CA  VAL A 448      28.807   6.519   9.243  1.00 75.21           C  
ANISOU 3533  CA  VAL A 448    10906   8177   9494  -1025      8   -627       C  
ATOM   3534  C   VAL A 448      29.875   6.657   8.167  1.00 71.25           C  
ANISOU 3534  C   VAL A 448    10540   7690   8840   -809     90   -738       C  
ATOM   3535  O   VAL A 448      29.566   6.917   7.005  1.00 70.78           O  
ANISOU 3535  O   VAL A 448    10533   7720   8639   -934      1   -864       O  
ATOM   3536  CB  VAL A 448      28.298   7.915   9.675  1.00 68.87           C  
ANISOU 3536  CB  VAL A 448     9702   7720   8747  -1054   -112   -486       C  
ATOM   3537  CG1 VAL A 448      26.916   7.809  10.269  1.00 64.66           C  
ANISOU 3537  CG1 VAL A 448     9043   7230   8294  -1329   -227   -397       C  
ATOM   3538  CG2 VAL A 448      29.250   8.566  10.668  1.00 60.67           C  
ANISOU 3538  CG2 VAL A 448     8477   6781   7793   -767    -19   -342       C  
TER    3539      VAL A 448                                                      
HETATM 3540  PA  FAD A 501      10.294  17.293  19.888  1.00 24.12           P  
HETATM 3541  O1A FAD A 501       9.308  16.312  19.383  1.00 23.59           O  
HETATM 3542  O2A FAD A 501      10.338  17.526  21.398  1.00 21.31           O  
HETATM 3543  O5B FAD A 501      10.014  18.655  19.188  1.00 23.50           O  
HETATM 3544  C5B FAD A 501       9.793  18.723  17.763  1.00 26.60           C  
HETATM 3545  C4B FAD A 501       9.140  20.051  17.486  1.00 26.84           C  
HETATM 3546  O4B FAD A 501       9.189  20.335  16.068  1.00 24.09           O  
HETATM 3547  C3B FAD A 501       7.669  20.159  17.907  1.00 24.99           C  
HETATM 3548  O3B FAD A 501       7.485  21.325  18.707  1.00 25.67           O  
HETATM 3549  C2B FAD A 501       6.917  20.219  16.567  1.00 21.70           C  
HETATM 3550  O2B FAD A 501       5.710  20.977  16.653  1.00 22.12           O  
HETATM 3551  C1B FAD A 501       7.957  20.902  15.679  1.00 22.19           C  
HETATM 3552  N9A FAD A 501       7.820  20.653  14.251  1.00 23.62           N  
HETATM 3553  C8A FAD A 501       7.713  19.434  13.633  1.00 24.61           C  
HETATM 3554  N7A FAD A 501       7.670  19.503  12.323  1.00 26.78           N  
HETATM 3555  C5A FAD A 501       7.772  20.862  12.062  1.00 23.06           C  
HETATM 3556  C6A FAD A 501       7.790  21.600  10.863  1.00 25.25           C  
HETATM 3557  N6A FAD A 501       7.709  21.043   9.648  1.00 24.60           N  
HETATM 3558  N1A FAD A 501       7.909  22.947  10.955  1.00 24.39           N  
HETATM 3559  C2A FAD A 501       7.993  23.506  12.168  1.00 23.35           C  
HETATM 3560  N3A FAD A 501       7.997  22.909  13.361  1.00 22.92           N  
HETATM 3561  C4A FAD A 501       7.868  21.582  13.241  1.00 24.81           C  
HETATM 3562  N1  FAD A 501       9.021  13.540  26.320  1.00 26.18           N  
HETATM 3563  C2  FAD A 501       9.008  13.137  27.623  1.00 34.22           C  
HETATM 3564  O2  FAD A 501       9.914  12.434  28.090  1.00 33.03           O  
HETATM 3565  N3  FAD A 501       7.975  13.536  28.449  1.00 31.98           N  
HETATM 3566  C4  FAD A 501       6.892  14.325  28.081  1.00 28.94           C  
HETATM 3567  O4  FAD A 501       6.033  14.628  28.915  1.00 33.74           O  
HETATM 3568  C4X FAD A 501       6.924  14.747  26.691  1.00 26.05           C  
HETATM 3569  N5  FAD A 501       5.938  15.489  26.243  1.00 24.73           N  
HETATM 3570  C5X FAD A 501       5.976  15.887  24.910  1.00 25.86           C  
HETATM 3571  C6  FAD A 501       4.954  16.694  24.419  1.00 26.85           C  
HETATM 3572  C7  FAD A 501       4.949  17.122  23.095  1.00 23.69           C  
HETATM 3573  C7M FAD A 501       3.816  17.985  22.602  1.00 26.19           C  
HETATM 3574  C8  FAD A 501       5.996  16.741  22.239  1.00 28.00           C  
HETATM 3575  C8M FAD A 501       6.020  17.184  20.799  1.00 26.67           C  
HETATM 3576  C9  FAD A 501       7.026  15.941  22.728  1.00 25.33           C  
HETATM 3577  C9A FAD A 501       7.028  15.519  24.053  1.00 24.78           C  
HETATM 3578  N10 FAD A 501       8.053  14.707  24.574  1.00 24.59           N  
HETATM 3579  C10 FAD A 501       8.031  14.299  25.887  1.00 24.90           C  
HETATM 3580  C1' FAD A 501       9.154  14.238  23.708  1.00 26.30           C  
HETATM 3581  C2' FAD A 501      10.490  14.919  23.972  1.00 27.99           C  
HETATM 3582  O2' FAD A 501      10.377  16.317  23.714  1.00 25.73           O  
HETATM 3583  C3' FAD A 501      11.544  14.307  23.042  1.00 26.54           C  
HETATM 3584  O3' FAD A 501      11.478  12.889  23.169  1.00 27.64           O  
HETATM 3585  C4' FAD A 501      12.983  14.766  23.283  1.00 27.29           C  
HETATM 3586  O4' FAD A 501      13.221  14.928  24.682  1.00 31.35           O  
HETATM 3587  C5' FAD A 501      13.323  16.034  22.522  1.00 27.01           C  
HETATM 3588  O5' FAD A 501      13.071  15.807  21.121  1.00 23.98           O  
HETATM 3589  P   FAD A 501      13.149  16.977  20.056  1.00 22.39           P  
HETATM 3590  O1P FAD A 501      14.180  16.501  19.031  1.00 22.89           O  
HETATM 3591  O2P FAD A 501      13.346  18.347  20.646  1.00 20.28           O  
HETATM 3592  O3P FAD A 501      11.735  16.901  19.351  1.00 21.07           O  
HETATM 3593  O   HOH A 601      28.286  -2.849  16.873  1.00 63.17           O  
HETATM 3594  O   HOH A 602       8.937  26.880  -3.533  1.00 44.92           O  
HETATM 3595  O   HOH A 603      -7.204  11.362  29.490  1.00 76.57           O  
HETATM 3596  O   HOH A 604      39.843  22.501   6.519  1.00 54.76           O  
HETATM 3597  O   HOH A 605      34.387  36.984   6.151  1.00 87.20           O  
HETATM 3598  O   HOH A 606      32.743  23.283  -3.963  1.00 47.61           O  
HETATM 3599  O   HOH A 607      29.632  36.022   9.944  1.00110.18           O  
HETATM 3600  O   HOH A 608       2.943 -15.432  39.373  1.00 40.92           O  
HETATM 3601  O   HOH A 609      14.681   9.102  27.092  1.00140.80           O  
HETATM 3602  O   HOH A 610      10.926 -10.794  48.436  1.00 56.56           O  
HETATM 3603  O   HOH A 611       9.624  22.437  -3.436  1.00 42.28           O  
HETATM 3604  O   HOH A 612      15.848  -2.482  32.353  1.00 54.17           O  
HETATM 3605  O   HOH A 613      21.512  -5.769  21.561  1.00 57.33           O  
HETATM 3606  O   HOH A 614      44.527  10.092   9.159  1.00 77.40           O  
HETATM 3607  O   HOH A 615      -2.405   4.856  52.128  1.00 44.80           O  
HETATM 3608  O   HOH A 616       9.370  34.368   7.936  1.00 72.11           O  
HETATM 3609  O   HOH A 617      13.337  10.188  28.403  1.00156.01           O  
HETATM 3610  O   HOH A 618      -4.070  13.617  27.162  1.00 40.29           O  
HETATM 3611  O   HOH A 619      10.261  -5.296  22.572  1.00 49.98           O  
HETATM 3612  O   HOH A 620      10.777  37.186  12.154  1.00 44.30           O  
HETATM 3613  O   HOH A 621      10.115  11.175  30.203  1.00 51.44           O  
HETATM 3614  O   HOH A 622     -13.600  13.556  29.391  1.00 34.37           O  
HETATM 3615  O   HOH A 623      16.053   9.998  48.307  1.00 44.04           O  
HETATM 3616  O   HOH A 624       7.341  10.849  35.788  1.00 47.34           O  
HETATM 3617  O   HOH A 625       3.776   6.115  14.517  1.00 47.47           O  
HETATM 3618  O   HOH A 626     -11.399   6.179  47.986  1.00 48.87           O  
HETATM 3619  O   HOH A 627      30.094  12.634   8.870  1.00 33.11           O  
HETATM 3620  O   HOH A 628      10.670  27.249  37.013  1.00 45.92           O  
HETATM 3621  O   HOH A 629       8.140   6.852  18.835  1.00 36.98           O  
HETATM 3622  O   HOH A 630      24.831  30.662   2.086  1.00 50.50           O  
HETATM 3623  O   HOH A 631       5.431  12.073  19.349  1.00 39.61           O  
HETATM 3624  O   HOH A 632      17.131  -7.204  25.897  1.00 45.75           O  
HETATM 3625  O   HOH A 633       3.358   5.597  53.679  1.00 71.15           O  
HETATM 3626  O   HOH A 634       7.580   9.084  37.272  1.00 42.50           O  
HETATM 3627  O   HOH A 635     -13.378  -3.149  32.397  1.00 35.91           O  
HETATM 3628  O   HOH A 636      -0.279  34.336   6.883  1.00 36.30           O  
HETATM 3629  O   HOH A 637      12.353  29.134  36.866  1.00 54.65           O  
HETATM 3630  O   HOH A 638       9.656  16.751  45.731  1.00 30.02           O  
HETATM 3631  O   HOH A 639      14.462  16.647  16.490  1.00 21.88           O  
HETATM 3632  O   HOH A 640      -0.586  14.387  29.849  1.00 28.39           O  
HETATM 3633  O   HOH A 641      31.073  26.463  10.289  1.00 50.42           O  
HETATM 3634  O   HOH A 642      14.222  20.512  43.612  1.00 44.82           O  
HETATM 3635  O   HOH A 643       1.692  17.767  39.411  1.00 35.14           O  
HETATM 3636  O   HOH A 644      39.501   9.465  21.023  1.00 49.87           O  
HETATM 3637  O   HOH A 645      28.329  20.894  -2.227  1.00 65.29           O  
HETATM 3638  O   HOH A 646       1.424  12.659  29.761  1.00 31.66           O  
HETATM 3639  O   HOH A 647      14.458  10.433  22.339  1.00 30.09           O  
HETATM 3640  O   HOH A 648      20.439  17.890  -1.105  1.00 58.90           O  
HETATM 3641  O   HOH A 649      10.949  11.177  25.027  1.00 67.63           O  
HETATM 3642  O   HOH A 650      10.365   4.909  28.016  1.00 75.52           O  
HETATM 3643  O   HOH A 651      28.372  30.065   1.220  1.00 47.39           O  
HETATM 3644  O   HOH A 652       5.724  -7.889  42.302  1.00 31.02           O  
HETATM 3645  O   HOH A 653      13.484  10.042  47.776  1.00 40.36           O  
HETATM 3646  O   HOH A 654       8.488  -8.370  40.442  1.00 41.44           O  
HETATM 3647  O   HOH A 655      31.898  12.004   7.285  1.00 49.38           O  
HETATM 3648  O   HOH A 656      42.745  18.332  10.889  1.00 35.92           O  
HETATM 3649  O   HOH A 657       5.119  -8.282  29.960  1.00 38.84           O  
HETATM 3650  O   HOH A 658       3.275  20.094  16.973  1.00 55.71           O  
HETATM 3651  O   HOH A 659      28.430  13.765  22.322  1.00 29.39           O  
HETATM 3652  O   HOH A 660      35.440   3.659  22.459  1.00 47.04           O  
HETATM 3653  O   HOH A 661      27.111  11.698   6.272  1.00 46.88           O  
HETATM 3654  O   HOH A 662      22.063   1.363  33.908  1.00 56.70           O  
HETATM 3655  O   HOH A 663       0.440  -5.614  30.614  1.00 31.32           O  
HETATM 3656  O   HOH A 664      -2.912   8.672  24.420  1.00 28.20           O  
HETATM 3657  O   HOH A 665      15.474  -8.738  43.629  1.00 47.31           O  
HETATM 3658  O   HOH A 666       7.350   6.945  14.865  1.00 40.30           O  
HETATM 3659  O   HOH A 667      30.472   8.006  15.714  1.00 32.13           O  
HETATM 3660  O   HOH A 668      -9.653  10.391  29.150  1.00 57.84           O  
HETATM 3661  O   HOH A 669       7.966 -16.670  43.078  1.00 34.88           O  
HETATM 3662  O   HOH A 670      26.235   5.272  38.182  1.00 59.99           O  
HETATM 3663  O   HOH A 671       9.074  16.863  53.290  1.00 59.66           O  
HETATM 3664  O   HOH A 672      -6.729  -2.810  31.603  1.00 42.07           O  
HETATM 3665  O   HOH A 673      11.415   9.741  21.081  1.00 37.06           O  
HETATM 3666  O   HOH A 674      34.559  21.720  29.502  1.00 43.84           O  
HETATM 3667  O   HOH A 675       0.149  30.674  11.328  1.00 35.03           O  
HETATM 3668  O   HOH A 676      12.634  19.005  45.236  1.00 32.41           O  
HETATM 3669  O   HOH A 677       2.770  -7.081  23.905  1.00 48.03           O  
HETATM 3670  O   HOH A 678       7.164 -17.181  35.398  1.00 47.03           O  
HETATM 3671  O   HOH A 679      11.590 -15.629  32.425  1.00 62.53           O  
HETATM 3672  O   HOH A 680      27.353  28.050  22.370  1.00 38.91           O  
HETATM 3673  O   HOH A 681       6.550  35.467  23.043  1.00 27.60           O  
HETATM 3674  O   HOH A 682      13.393   7.362  46.771  1.00 33.82           O  
HETATM 3675  O   HOH A 683      16.257  37.125   9.698  1.00 58.93           O  
HETATM 3676  O   HOH A 684      28.398  10.251   7.546  1.00123.30           O  
HETATM 3677  O   HOH A 685      17.620  23.292  44.100  1.00 46.65           O  
HETATM 3678  O   HOH A 686       8.609  18.022  10.022  1.00 31.67           O  
HETATM 3679  O   HOH A 687      26.739  18.823  42.599  1.00 53.15           O  
HETATM 3680  O   HOH A 688      -5.786  -2.933  45.260  1.00 31.80           O  
HETATM 3681  O   HOH A 689      -4.723  14.013  19.155  1.00 36.73           O  
HETATM 3682  O   HOH A 690      24.083  34.801  26.426  1.00 33.60           O  
HETATM 3683  O   HOH A 691      26.274  13.313  38.169  1.00 32.77           O  
HETATM 3684  O   HOH A 692      14.255 -11.035  40.036  1.00 32.71           O  
HETATM 3685  O   HOH A 693      27.788   3.825  35.792  1.00 50.68           O  
HETATM 3686  O   HOH A 694      -8.697  -2.612  44.267  1.00 45.34           O  
HETATM 3687  O   HOH A 695      39.221  22.025   4.393  1.00 58.25           O  
HETATM 3688  O   HOH A 696       8.640   2.697  50.410  1.00 41.85           O  
HETATM 3689  O   HOH A 697       7.622  19.678   6.249  1.00 46.90           O  
HETATM 3690  O   HOH A 698       4.709  19.280  30.300  1.00 26.53           O  
HETATM 3691  O   HOH A 699      22.786  28.464  32.498  1.00 28.92           O  
HETATM 3692  O   HOH A 700      22.930  12.120  35.642  1.00 28.90           O  
HETATM 3693  O   HOH A 701       0.402  19.100  30.452  1.00 39.84           O  
HETATM 3694  O   HOH A 702       0.537  -8.377  24.682  1.00 53.08           O  
HETATM 3695  O   HOH A 703      13.528  25.431  -0.673  1.00 38.43           O  
HETATM 3696  O   HOH A 704      31.395   0.438  10.923  1.00 52.24           O  
HETATM 3697  O   HOH A 705      22.707   7.240  31.998  1.00 45.48           O  
HETATM 3698  O   HOH A 706      32.005   8.295  27.712  1.00 38.52           O  
HETATM 3699  O   HOH A 707       3.383   3.089  49.205  1.00 45.66           O  
HETATM 3700  O   HOH A 708      23.017  37.661  22.240  1.00 39.27           O  
HETATM 3701  O   HOH A 709      -3.424  16.079  35.611  1.00 39.18           O  
HETATM 3702  O   HOH A 710      12.694  36.625  27.297  1.00 30.13           O  
HETATM 3703  O   HOH A 711      18.452  33.187  36.063  1.00 47.52           O  
HETATM 3704  O   HOH A 712       1.937   1.533  17.692  1.00 40.93           O  
HETATM 3705  O   HOH A 713     -10.528  -1.278  30.932  1.00 46.70           O  
HETATM 3706  O   HOH A 714       5.093  23.208  25.910  1.00 40.01           O  
HETATM 3707  O   HOH A 715      40.978  24.368  12.617  1.00 52.69           O  
HETATM 3708  O   HOH A 716      16.806   6.467  14.539  1.00 30.13           O  
HETATM 3709  O   HOH A 717      20.298   7.634  13.869  1.00 26.33           O  
HETATM 3710  O   HOH A 718      12.888  12.447  30.342  1.00 45.79           O  
HETATM 3711  O   HOH A 719      14.677  37.681  20.159  1.00 27.29           O  
HETATM 3712  O   HOH A 720      10.633   7.460  47.055  1.00 27.46           O  
HETATM 3713  O   HOH A 721       7.127  15.843  17.825  1.00 26.01           O  
HETATM 3714  O   HOH A 722      10.712  12.385   6.230  1.00 49.94           O  
HETATM 3715  O   HOH A 723      -3.906  -0.818  48.003  1.00 32.34           O  
HETATM 3716  O   HOH A 724       8.741   5.290  49.328  1.00 36.94           O  
HETATM 3717  O   HOH A 725      26.225  18.882  35.546  1.00 43.69           O  
HETATM 3718  O   HOH A 726      14.391   3.807  19.376  1.00 29.89           O  
HETATM 3719  O   HOH A 727     -11.252   1.507  26.773  1.00 38.21           O  
HETATM 3720  O   HOH A 728      13.301  18.183  47.629  1.00 33.82           O  
HETATM 3721  O   HOH A 729      13.357  -1.156  14.684  1.00 62.29           O  
HETATM 3722  O   HOH A 730      13.308  20.363  18.800  1.00 21.30           O  
HETATM 3723  O   HOH A 731       0.771  24.931   7.659  1.00 49.96           O  
HETATM 3724  O   HOH A 732      31.528  31.738  16.545  1.00 33.67           O  
HETATM 3725  O   HOH A 733     -13.846  -2.062  35.267  1.00 43.11           O  
HETATM 3726  O   HOH A 734      35.729   6.224  26.818  1.00 51.72           O  
HETATM 3727  O   HOH A 735      32.014  29.952  -4.825  1.00 62.33           O  
HETATM 3728  O   HOH A 736      -1.524  10.261  22.544  1.00 29.88           O  
HETATM 3729  O   HOH A 737       7.372  14.771  55.453  1.00 48.30           O  
HETATM 3730  O   HOH A 738       9.206   8.652  20.622  1.00 49.59           O  
HETATM 3731  O   HOH A 739      15.361  34.758   8.187  1.00 37.85           O  
HETATM 3732  O   HOH A 740      -2.445  -3.372  29.512  1.00 46.47           O  
HETATM 3733  O   HOH A 741      28.268  16.978  28.180  1.00 29.68           O  
HETATM 3734  O   HOH A 742       5.330  19.140   7.352  1.00 54.87           O  
HETATM 3735  O   HOH A 743       7.823   5.315  20.992  1.00 31.67           O  
HETATM 3736  O   HOH A 744       9.772  11.539  49.636  1.00 45.75           O  
HETATM 3737  O   HOH A 745       4.289   0.904  50.160  1.00 52.50           O  
HETATM 3738  O   HOH A 746       7.810  15.232  15.231  1.00 26.79           O  
HETATM 3739  O   HOH A 747      29.450  23.047  32.867  1.00 35.92           O  
HETATM 3740  O   HOH A 748       1.124  26.191  12.149  1.00 50.07           O  
HETATM 3741  O   HOH A 749      31.242  13.789  22.597  1.00 26.42           O  
HETATM 3742  O   HOH A 750      27.190  24.508  26.837  1.00 29.71           O  
HETATM 3743  O   HOH A 751     -14.220   3.828  29.561  1.00 46.54           O  
HETATM 3744  O   HOH A 752      -2.370  15.457  25.889  1.00 34.70           O  
HETATM 3745  O   HOH A 753      19.482  35.943  15.795  1.00 30.91           O  
HETATM 3746  O   HOH A 754       1.337  -8.723  40.467  1.00 31.24           O  
HETATM 3747  O   HOH A 755       5.363  32.368   5.693  1.00 45.81           O  
HETATM 3748  O   HOH A 756       6.699  30.086  -3.251  1.00 56.32           O  
HETATM 3749  O   HOH A 757      20.474  16.214  40.929  1.00 33.77           O  
HETATM 3750  O   HOH A 758      -3.256  14.633  50.186  1.00 42.41           O  
HETATM 3751  O   HOH A 759       7.922  21.949  21.372  1.00 25.81           O  
HETATM 3752  O   HOH A 760      13.126  18.427  42.002  1.00 36.27           O  
HETATM 3753  O   HOH A 761      32.686   6.343  15.966  1.00 37.11           O  
HETATM 3754  O   HOH A 762      30.851  29.593  15.011  1.00 48.96           O  
HETATM 3755  O   HOH A 763      19.983  13.855  44.652  1.00 50.60           O  
HETATM 3756  O   HOH A 764      17.972  34.228  30.689  1.00 33.45           O  
HETATM 3757  O   HOH A 765       1.807  23.185  23.144  1.00 41.75           O  
HETATM 3758  O   HOH A 766      17.112  -7.084  32.828  1.00 46.66           O  
HETATM 3759  O   HOH A 767      12.416  24.039  45.098  1.00 44.40           O  
HETATM 3760  O   HOH A 768      30.246   8.557  19.005  1.00 27.33           O  
HETATM 3761  O   HOH A 769      38.975   3.864   7.650  1.00 56.15           O  
HETATM 3762  O   HOH A 770      -6.830   3.988  26.402  1.00 41.73           O  
HETATM 3763  O   HOH A 771      16.370 -12.431  45.663  1.00 41.49           O  
HETATM 3764  O   HOH A 772       5.661  10.270  33.669  1.00 32.74           O  
HETATM 3765  O   HOH A 773       4.927  -9.438  34.203  1.00 33.23           O  
HETATM 3766  O   HOH A 774       7.328   6.065  30.184  1.00 58.84           O  
HETATM 3767  O   HOH A 775      17.925  11.958  36.568  1.00 49.92           O  
HETATM 3768  O   HOH A 776      21.179   6.708  16.115  1.00 29.45           O  
HETATM 3769  O   HOH A 777       5.506  20.278  26.766  1.00 29.24           O  
HETATM 3770  O   HOH A 778       5.875  26.272  27.435  1.00 37.61           O  
HETATM 3771  O   HOH A 779      15.579  13.239  36.220  1.00 35.48           O  
HETATM 3772  O   HOH A 780       4.102 -10.273  42.868  1.00 55.89           O  
HETATM 3773  O   HOH A 781      17.578  10.524  21.969  1.00 34.55           O  
HETATM 3774  O   HOH A 782      24.293  29.040  37.638  1.00 41.00           O  
HETATM 3775  O   HOH A 783      11.513  17.342   3.558  1.00 41.41           O  
HETATM 3776  O   HOH A 784      22.436  16.769  42.585  1.00 38.68           O  
HETATM 3777  O   HOH A 785      33.892  11.556   4.826  1.00 44.59           O  
HETATM 3778  O   HOH A 786      41.801  10.817  11.745  1.00 35.92           O  
HETATM 3779  O   HOH A 787      -7.815   4.542  45.537  1.00 42.47           O  
HETATM 3780  O   HOH A 788      14.776  31.839  31.038  1.00 29.37           O  
HETATM 3781  O   HOH A 789      18.660  37.628  13.688  1.00 59.41           O  
HETATM 3782  O   HOH A 790       4.897   4.971  51.020  1.00 46.12           O  
HETATM 3783  O   HOH A 791      26.393  13.354   4.132  1.00 34.71           O  
HETATM 3784  O   HOH A 792      40.109  22.508  19.285  1.00 38.31           O  
HETATM 3785  O   HOH A 793     -12.210   0.422  29.944  1.00 49.33           O  
HETATM 3786  O   HOH A 794       5.272  33.680  12.831  1.00 26.81           O  
HETATM 3787  O   HOH A 795      -1.148  26.175  29.097  1.00 44.20           O  
HETATM 3788  O   HOH A 796       3.290 -11.759  34.855  1.00 40.33           O  
HETATM 3789  O   HOH A 797      19.150  33.389  10.010  1.00 48.49           O  
HETATM 3790  O   HOH A 798      42.372  16.202  17.383  1.00 29.84           O  
HETATM 3791  O   HOH A 799      29.762  34.295  15.046  1.00 56.16           O  
HETATM 3792  O   HOH A 800      29.623  19.539  27.341  1.00 29.89           O  
HETATM 3793  O   HOH A 801       2.985 -15.509  36.995  1.00 40.86           O  
HETATM 3794  O   HOH A 802      12.606  -4.214  18.735  1.00 47.70           O  
HETATM 3795  O   HOH A 803      16.678  -8.519  45.664  1.00 72.37           O  
HETATM 3796  O   HOH A 804       7.162  32.894  27.890  1.00 45.71           O  
HETATM 3797  O   HOH A 805      22.341  35.716  31.163  1.00 60.03           O  
HETATM 3798  O   HOH A 806      15.833 -16.711  35.823  1.00 45.46           O  
HETATM 3799  O   HOH A 807       9.823  13.508  19.229  1.00 22.61           O  
HETATM 3800  O   HOH A 808      11.463  36.789  16.754  1.00 36.25           O  
HETATM 3801  O   HOH A 809       7.340  14.545  39.197  1.00 38.67           O  
HETATM 3802  O   HOH A 810      28.746  33.704  24.431  1.00 63.84           O  
HETATM 3803  O   HOH A 811      20.657  14.858   0.930  1.00 40.65           O  
HETATM 3804  O   HOH A 812      12.083  12.667  26.251  1.00 38.01           O  
HETATM 3805  O   HOH A 813      31.918   9.854  31.530  1.00 39.91           O  
HETATM 3806  O   HOH A 814      19.588  40.469  22.828  1.00 54.20           O  
HETATM 3807  O   HOH A 815      -0.868  20.551  39.528  1.00 41.23           O  
HETATM 3808  O   HOH A 816      -0.983  14.650  17.281  1.00 38.91           O  
HETATM 3809  O   HOH A 817       5.454   4.337  48.513  1.00 40.38           O  
HETATM 3810  O   HOH A 818      17.350   3.294   9.486  1.00 46.03           O  
HETATM 3811  O   HOH A 819      14.572  -5.003  30.874  1.00 36.74           O  
HETATM 3812  O   HOH A 820       9.383  34.103  -0.785  1.00 40.13           O  
HETATM 3813  O   HOH A 821       0.645  -0.307  21.455  1.00 44.60           O  
HETATM 3814  O   HOH A 822      12.785  14.340  41.028  1.00 32.22           O  
HETATM 3815  O   HOH A 823      -3.937   8.894  19.006  1.00 43.38           O  
HETATM 3816  O   HOH A 824      41.614  22.263  10.181  1.00 41.90           O  
HETATM 3817  O   HOH A 825       0.092  15.604  32.247  1.00 34.39           O  
HETATM 3818  O   HOH A 826       8.944   8.130  12.926  1.00 43.20           O  
HETATM 3819  O   HOH A 827      20.784  40.228  20.477  1.00 41.35           O  
HETATM 3820  O   HOH A 828      15.180   4.107  11.190  1.00 39.33           O  
HETATM 3821  O   HOH A 829       4.813  -1.164  21.092  1.00 33.06           O  
HETATM 3822  O   HOH A 830       6.480  16.850  53.152  1.00 50.48           O  
HETATM 3823  O   HOH A 831      -2.795   8.833  53.161  1.00 41.80           O  
HETATM 3824  O   HOH A 832      32.932   7.104  11.180  1.00 42.33           O  
HETATM 3825  O   HOH A 833       1.534  22.634  45.844  1.00 49.45           O  
HETATM 3826  O   HOH A 834      10.015  36.894  14.704  1.00 47.49           O  
HETATM 3827  O   HOH A 835       9.969   4.590  30.119  1.00 79.49           O  
HETATM 3828  O   HOH A 836      15.989  34.655   3.590  1.00 38.14           O  
HETATM 3829  O   HOH A 837      21.970   0.580  45.947  1.00 52.79           O  
HETATM 3830  O   HOH A 838       5.583  22.057  23.055  1.00 32.76           O  
HETATM 3831  O   HOH A 839     -11.240   6.027  43.392  1.00 44.52           O  
HETATM 3832  O   HOH A 840      -5.500  -1.340  17.170  1.00 42.99           O  
HETATM 3833  O   HOH A 841       9.852  11.863  33.250  1.00 44.81           O  
HETATM 3834  O   HOH A 842       1.463  26.650   9.461  1.00 36.72           O  
HETATM 3835  O   HOH A 843      13.314   2.205  12.380  1.00 40.95           O  
HETATM 3836  O   HOH A 844      30.072   3.782  32.931  1.00 41.57           O  
HETATM 3837  O   HOH A 845      26.723  28.576  25.162  1.00 46.36           O  
HETATM 3838  O   HOH A 846      -7.222  -6.261  44.809  1.00 34.65           O  
HETATM 3839  O   HOH A 847      -2.027   8.399  20.584  1.00 39.08           O  
HETATM 3840  O   HOH A 848      13.400  11.869  40.962  1.00 40.78           O  
HETATM 3841  O   HOH A 849      28.149  29.124   4.167  1.00 43.21           O  
HETATM 3842  O   HOH A 850      36.261  28.955   7.898  1.00 43.78           O  
HETATM 3843  O   HOH A 851       7.595   8.161  51.933  1.00 48.46           O  
HETATM 3844  O   HOH A 852      -8.216   4.609  48.134  1.00 45.39           O  
HETATM 3845  O   HOH A 853       8.054  -1.940  52.902  1.00 37.94           O  
HETATM 3846  O   HOH A 854      -7.103  21.831  40.949  1.00 67.61           O  
HETATM 3847  O   HOH A 855      -0.723  24.754  18.465  1.00 34.37           O  
HETATM 3848  O   HOH A 856       5.637   1.685  13.582  1.00 55.05           O  
HETATM 3849  O   HOH A 857      24.249   6.348  41.641  1.00 41.92           O  
HETATM 3850  O   HOH A 858      11.513 -12.395  34.900  1.00 44.99           O  
HETATM 3851  O   HOH A 859      20.704  -0.339  49.119  1.00 50.40           O  
HETATM 3852  O   HOH A 860       7.597  12.346  20.732  1.00 32.23           O  
HETATM 3853  O   HOH A 861      30.605  23.923   3.149  1.00 33.22           O  
HETATM 3854  O   HOH A 862      -0.828  -3.780  49.537  1.00 34.64           O  
HETATM 3855  O   HOH A 863      13.003   1.263  26.449  1.00 40.43           O  
HETATM 3856  O   HOH A 864       8.398  -9.682  46.186  1.00 37.23           O  
HETATM 3857  O   HOH A 865      16.670  13.867  21.327  1.00 26.13           O  
HETATM 3858  O   HOH A 866      11.402  -6.789  38.116  1.00 32.42           O  
HETATM 3859  O   HOH A 867      22.011  -4.091  39.303  1.00 78.30           O  
HETATM 3860  O   HOH A 868      39.793   7.016  14.781  1.00 39.00           O  
HETATM 3861  O   HOH A 869      28.021  34.893  12.810  1.00 46.38           O  
HETATM 3862  O   HOH A 870      17.437  -5.647  42.172  1.00 44.85           O  
HETATM 3863  O   HOH A 871       9.466  27.022  41.783  1.00 46.72           O  
HETATM 3864  O   HOH A 872      28.016  -5.865  26.558  1.00 44.84           O  
HETATM 3865  O   HOH A 873      31.079  26.862   4.134  1.00 39.52           O  
HETATM 3866  O   HOH A 874      13.171  10.012  24.697  1.00 43.87           O  
HETATM 3867  O   HOH A 875      18.506   5.039   7.293  1.00 37.10           O  
HETATM 3868  O   HOH A 876      20.422   8.852  21.536  1.00 41.99           O  
HETATM 3869  O   HOH A 877      33.618  10.844  29.388  1.00 49.70           O  
HETATM 3870  O   HOH A 878      12.606  32.168  32.694  1.00 38.86           O  
HETATM 3871  O   HOH A 879      21.621  39.842  30.969  1.00 49.77           O  
HETATM 3872  O   HOH A 880      41.984   9.780   9.134  1.00 47.99           O  
HETATM 3873  O   HOH A 881      -8.039  16.016  39.485  1.00 49.70           O  
HETATM 3874  O   HOH A 882      -1.008  16.385  27.980  1.00 34.13           O  
HETATM 3875  O   HOH A 883     -13.725  -3.127  41.526  1.00 45.33           O  
HETATM 3876  O   HOH A 884      -2.876  23.604  28.321  1.00 53.34           O  
HETATM 3877  O   HOH A 885      20.816  30.205   0.436  1.00 54.99           O  
HETATM 3878  O   HOH A 886      30.591   8.127   4.467  1.00 69.29           O  
HETATM 3879  O   HOH A 887      38.408  28.398   6.697  1.00 49.95           O  
HETATM 3880  O   HOH A 888      28.578  22.957   1.066  1.00 44.61           O  
HETATM 3881  O   HOH A 889      41.437  19.247  17.844  1.00 27.98           O  
HETATM 3882  O   HOH A 890      14.793   6.188   7.367  1.00 63.04           O  
HETATM 3883  O   HOH A 891       7.467 -10.165  43.058  1.00 45.04           O  
HETATM 3884  O   HOH A 892       3.450  21.870  21.390  1.00 32.53           O  
HETATM 3885  O   HOH A 893      18.380  20.453  -2.745  1.00 37.74           O  
HETATM 3886  O   HOH A 894      13.022  35.431   4.188  1.00 62.83           O  
HETATM 3887  O   HOH A 895      17.504  19.969  44.902  1.00 46.20           O  
HETATM 3888  O   HOH A 896      25.129  40.302   8.509  1.00 60.66           O  
HETATM 3889  O   HOH A 897      -9.060  14.159  38.357  1.00 54.29           O  
HETATM 3890  O   HOH A 898      20.598  -6.936  32.959  1.00 66.48           O  
HETATM 3891  O   HOH A 899      35.105  -1.241  26.485  1.00 52.20           O  
HETATM 3892  O   HOH A 900       2.820  14.960  19.854  1.00 28.14           O  
HETATM 3893  O   HOH A 901      33.265  22.523   4.334  1.00 30.93           O  
HETATM 3894  O   HOH A 902       4.698   7.381  52.323  1.00 59.64           O  
HETATM 3895  O   HOH A 903      43.800  18.321  21.002  1.00 55.81           O  
HETATM 3896  O   HOH A 904       8.710  24.604  -4.913  1.00 48.84           O  
HETATM 3897  O   HOH A 905      -4.871   4.072  24.240  1.00 35.28           O  
HETATM 3898  O   HOH A 906      18.829  -4.730  41.236  1.00 68.41           O  
HETATM 3899  O   HOH A 907      13.363   3.119  21.989  1.00 38.90           O  
HETATM 3900  O   HOH A 908       5.275  16.682  14.273  1.00 36.71           O  
HETATM 3901  O   HOH A 909       7.873 -12.552  43.798  1.00 60.48           O  
HETATM 3902  O   HOH A 910      12.452   2.514  28.689  1.00 43.73           O  
HETATM 3903  O   HOH A 911      -4.741  -5.351  19.452  1.00 60.99           O  
HETATM 3904  O   HOH A 912      30.520   6.930  13.049  1.00 45.56           O  
HETATM 3905  O   HOH A 913      38.149  28.586  13.361  1.00 48.70           O  
HETATM 3906  O   HOH A 914      35.613  15.619   2.816  1.00 46.79           O  
HETATM 3907  O   HOH A 915       5.280  18.658  51.957  1.00 51.25           O  
HETATM 3908  O   HOH A 916      10.484  -9.085  38.347  1.00 42.75           O  
HETATM 3909  O   HOH A 917      33.854  -5.106  28.471  1.00 37.48           O  
HETATM 3910  O   HOH A 918      28.137  26.450  25.250  1.00 48.11           O  
HETATM 3911  O   HOH A 919       6.752  -8.099  31.681  1.00 40.11           O  
HETATM 3912  O   HOH A 920      32.680   6.436   9.096  1.00 62.86           O  
HETATM 3913  O   HOH A 921      23.944  23.423  41.511  1.00 55.63           O  
HETATM 3914  O   HOH A 922      14.461 -10.878  37.277  1.00 37.06           O  
HETATM 3915  O   HOH A 923      14.210   9.463  36.619  1.00 49.28           O  
HETATM 3916  O   HOH A 924      40.862  23.244  16.679  1.00 43.25           O  
HETATM 3917  O   HOH A 925      20.285  -2.308  28.247  1.00 45.09           O  
HETATM 3918  O   HOH A 926      -3.117  21.772  31.081  1.00 51.70           O  
HETATM 3919  O   HOH A 927      20.471  -1.367  44.327  1.00 69.67           O  
HETATM 3920  O   HOH A 928      19.279  35.343   5.617  1.00 61.31           O  
HETATM 3921  O   HOH A 929      11.888 -10.506  35.967  1.00 48.97           O  
HETATM 3922  O   HOH A 930      17.284  32.074  32.199  1.00 36.06           O  
HETATM 3923  O   HOH A 931      43.112  18.517   8.284  1.00 42.00           O  
HETATM 3924  O   HOH A 932      22.639  35.936  28.684  1.00 64.45           O  
HETATM 3925  O   HOH A 933      15.266  34.518  30.073  1.00 32.79           O  
HETATM 3926  O   HOH A 934      11.904  31.547  35.300  1.00 47.89           O  
HETATM 3927  O   HOH A 935      44.091  17.867  25.752  1.00 51.56           O  
HETATM 3928  O   HOH A 936       1.770   0.261  51.594  1.00 49.06           O  
HETATM 3929  O   HOH A 937       9.720   7.030  51.172  1.00 54.28           O  
HETATM 3930  O   HOH A 938       9.626   5.735  22.093  1.00 51.74           O  
HETATM 3931  O   HOH A 939      -5.188   7.227  23.365  1.00 49.18           O  
HETATM 3932  O   HOH A 940      22.344  31.647   1.444  1.00 56.18           O  
HETATM 3933  O   HOH A 941      -9.097  -2.779  30.504  1.00 52.12           O  
HETATM 3934  O   HOH A 942      40.909   4.882  14.334  1.00 66.52           O  
HETATM 3935  O   HOH A 943      15.048  11.588  38.567  1.00 39.55           O  
HETATM 3936  O   HOH A 944      33.332   5.901  27.504  1.00 43.10           O  
HETATM 3937  O   HOH A 945      33.170   9.118   4.234  1.00 61.56           O  
HETATM 3938  O   HOH A 946       4.639  -8.808  31.957  1.00 40.08           O  
HETATM 3939  O   HOH A 947      10.349   8.690  49.358  1.00 40.52           O  
HETATM 3940  O   HOH A 948       2.741  20.752  31.612  1.00 30.83           O  
HETATM 3941  O   HOH A 949       5.299   2.953  52.366  1.00 59.38           O  
HETATM 3942  O   HOH A 950      41.301  23.009  21.250  1.00 60.13           O  
HETATM 3943  O   HOH A 951      15.799  27.189  44.042  1.00 63.07           O  
HETATM 3944  O   HOH A 952       1.482  20.028  38.278  1.00 68.99           O  
HETATM 3945  O   HOH A 953       4.953  17.371  17.258  1.00 37.85           O  
HETATM 3946  O   HOH A 954      -2.110  -1.364  50.177  1.00 48.05           O  
HETATM 3947  O   HOH A 955       7.286  32.911   8.183  1.00 48.12           O  
HETATM 3948  O   HOH A 956       2.733  -0.375  19.693  1.00 40.17           O  
HETATM 3949  O   HOH A 957      25.222   4.276  40.033  1.00 50.30           O  
HETATM 3950  O   HOH A 958       7.366  36.644  10.818  1.00 47.45           O  
HETATM 3951  O   HOH A 959      -0.723   0.161  51.900  1.00 54.79           O  
HETATM 3952  O   HOH A 960      37.845  -5.506  30.724  1.00 45.24           O  
HETATM 3953  O   HOH A 961     -14.386  -1.464  30.165  1.00 45.88           O  
HETATM 3954  O   HOH A 962       4.983  14.075  18.439  1.00 37.63           O  
HETATM 3955  O   HOH A 963       3.576  14.757  15.769  1.00 49.16           O  
HETATM 3956  O   HOH A 964     -11.771   9.581  30.119  1.00 40.16           O  
HETATM 3957  O   HOH A 965      23.242  21.627  42.830  1.00 63.15           O  
HETATM 3958  O   HOH A 966      16.264  41.232  21.255  1.00 59.95           O  
HETATM 3959  O   HOH A 967       4.694  32.611  31.409  1.00 62.59           O  
HETATM 3960  O   HOH A 968      -2.641  16.748  16.527  1.00 36.37           O  
HETATM 3961  O   HOH A 969      -3.153   6.558  53.926  1.00 63.15           O  
HETATM 3962  O   HOH A 970       1.925  19.779  19.898  1.00 44.60           O  
HETATM 3963  O   HOH A 971      10.836  27.751  43.885  1.00 52.30           O  
HETATM 3964  O   HOH A 972      13.092  40.354  14.660  1.00 56.41           O  
HETATM 3965  O   HOH A 973      -3.906  18.833  23.185  1.00 53.32           O  
HETATM 3966  O   HOH A 974       4.856  31.654  29.003  1.00 48.22           O  
HETATM 3967  O   HOH A 975      12.667  26.520  45.347  1.00 58.97           O  
HETATM 3968  O   HOH A 976       5.779   5.096  13.338  1.00 58.07           O  
HETATM 3969  O   HOH A 977       2.574  22.054  34.055  1.00 59.24           O  
HETATM 3970  O   HOH A 978       5.329  24.619  40.001  1.00 59.51           O  
HETATM 3971  O   HOH A 979      -0.777  22.286  22.398  1.00 48.85           O  
HETATM 3972  O   HOH A 980      -0.447  22.420  17.964  1.00 55.45           O  
HETATM 3973  O   HOH A 981       1.655  36.224   6.959  1.00 39.74           O  
HETATM 3974  O   HOH A 982       5.690  34.282   9.984  1.00 30.28           O  
HETATM 3975  O   HOH A 983      -4.537  -6.648  50.253  1.00 50.35           O  
HETATM 3976  O   HOH A 984     -11.409   2.979  43.549  1.00 54.60           O  
HETATM 3977  O   HOH A 985      43.807  20.324  18.315  1.00 47.95           O  
HETATM 3978  O   HOH A 986      -9.286   1.014  43.673  1.00 51.93           O  
HETATM 3979  O   HOH A 987       1.195  15.904  17.148  1.00 47.87           O  
HETATM 3980  O   HOH A 988       3.984 -19.004  37.733  1.00 56.40           O  
HETATM 3981  O   HOH A 989      20.593  -1.206  30.802  1.00 59.52           O  
HETATM 3982  O   HOH A 990       3.428  -8.196  21.425  1.00 82.46           O  
HETATM 3983  O   HOH A 991      -7.736  -6.255  32.193  1.00 53.90           O  
HETATM 3984  O   HOH A 992       2.690  32.356  27.811  1.00 59.74           O  
HETATM 3985  O   HOH A 993      32.922  -2.715  27.937  1.00 46.95           O  
HETATM 3986  O   HOH A 994      17.999  36.178   1.886  1.00 73.71           O  
HETATM 3987  O   HOH A 995       6.363   5.612  10.620  1.00 58.23           O  
HETATM 3988  O   HOH A 996      45.153  20.221  20.407  1.00 81.34           O  
HETATM 3989  O   HOH A 997       2.790  21.691  36.868  1.00 63.81           O  
HETATM 3990  O   HOH A 998      -0.319  20.264  20.128  1.00 47.13           O  
HETATM 3991  O   HOH A 999       2.568  17.416  19.063  1.00 61.10           O  
HETATM 3992  O   HOH A1000       4.290  23.597  37.500  1.00 56.02           O  
CONECT 3540 3541 3542 3543 3592                                                 
CONECT 3541 3540                                                                
CONECT 3542 3540                                                                
CONECT 3543 3540 3544                                                           
CONECT 3544 3543 3545                                                           
CONECT 3545 3544 3546 3547                                                      
CONECT 3546 3545 3551                                                           
CONECT 3547 3545 3548 3549                                                      
CONECT 3548 3547                                                                
CONECT 3549 3547 3550 3551                                                      
CONECT 3550 3549                                                                
CONECT 3551 3546 3549 3552                                                      
CONECT 3552 3551 3553 3561                                                      
CONECT 3553 3552 3554                                                           
CONECT 3554 3553 3555                                                           
CONECT 3555 3554 3556 3561                                                      
CONECT 3556 3555 3557 3558                                                      
CONECT 3557 3556                                                                
CONECT 3558 3556 3559                                                           
CONECT 3559 3558 3560                                                           
CONECT 3560 3559 3561                                                           
CONECT 3561 3552 3555 3560                                                      
CONECT 3562 3563 3579                                                           
CONECT 3563 3562 3564 3565                                                      
CONECT 3564 3563                                                                
CONECT 3565 3563 3566                                                           
CONECT 3566 3565 3567 3568                                                      
CONECT 3567 3566                                                                
CONECT 3568 3566 3569 3579                                                      
CONECT 3569 3568 3570                                                           
CONECT 3570 3569 3571 3577                                                      
CONECT 3571 3570 3572                                                           
CONECT 3572 3571 3573 3574                                                      
CONECT 3573 3572                                                                
CONECT 3574 3572 3575 3576                                                      
CONECT 3575 3574                                                                
CONECT 3576 3574 3577                                                           
CONECT 3577 3570 3576 3578                                                      
CONECT 3578 3577 3579 3580                                                      
CONECT 3579 3562 3568 3578                                                      
CONECT 3580 3578 3581                                                           
CONECT 3581 3580 3582 3583                                                      
CONECT 3582 3581                                                                
CONECT 3583 3581 3584 3585                                                      
CONECT 3584 3583                                                                
CONECT 3585 3583 3586 3587                                                      
CONECT 3586 3585                                                                
CONECT 3587 3585 3588                                                           
CONECT 3588 3587 3589                                                           
CONECT 3589 3588 3590 3591 3592                                                 
CONECT 3590 3589                                                                
CONECT 3591 3589                                                                
CONECT 3592 3540 3589                                                           
MASTER      388    0    1   18   17    0    9    6 3961    1   53   36          
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: October 18th, 2018.