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HEADER    HYDROLASE                               24-JAN-16   5HRT              
TITLE     CRYSTAL STRUCTURE OF MOUSE AUTOTAXIN IN COMPLEX WITH A DNA APTAMER    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ECTONUCLEOTIDE PYROPHOSPHATASE/PHOSPHODIESTERASE FAMILY    
COMPND   3 MEMBER 2;                                                            
COMPND   4 CHAIN: A;                                                            
COMPND   5 FRAGMENT: UNP RESIDUES 36-862;                                       
COMPND   6 SYNONYM: E-NPP 2,AUTOTAXIN,EXTRACELLULAR LYSOPHOSPHOLIPASE D,LYSOPLD;
COMPND   7 EC: 3.1.4.39;                                                        
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: MODIFIED DNA (34-MER);                                     
COMPND  11 CHAIN: B;                                                            
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: MOUSE;                                              
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 GENE: ENPP2, NPPS2, PDNP2;                                           
SOURCE   6 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 SYNTHETIC: YES;                                                      
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_TAXID: 9606                                                 
KEYWDS    PHOSPHOLIPASE D, DNA APTAMER, HYDROLASE                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.KATO,H.NISHIMASU,J.MORITA,R.ISHITANI,O.NUREKI                       
REVDAT   4   29-JUL-20 5HRT    1       COMPND REMARK HETNAM LINK                
REVDAT   4 2                   1       SITE   ATOM                              
REVDAT   3   19-FEB-20 5HRT    1       REMARK                                   
REVDAT   2   25-MAY-16 5HRT    1       JRNL                                     
REVDAT   1   06-APR-16 5HRT    0                                                
JRNL        AUTH   K.KATO,H.IKEDA,S.MIYAKAWA,S.FUTAKAWA,Y.NONAKA,M.FUJIWARA,    
JRNL        AUTH 2 S.OKUDAIRA,K.KANO,J.AOKI,J.MORITA,R.ISHITANI,H.NISHIMASU,    
JRNL        AUTH 3 Y.NAKAMURA,O.NUREKI                                          
JRNL        TITL   STRUCTURAL BASIS FOR SPECIFIC INHIBITION OF AUTOTAXIN BY A   
JRNL        TITL 2 DNA APTAMER                                                  
JRNL        REF    NAT.STRUCT.MOL.BIOL.          V.  23   395 2016              
JRNL        REFN                   ESSN 1545-9985                               
JRNL        PMID   27043297                                                     
JRNL        DOI    10.1038/NSMB.3200                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.10_2155: ???)                              
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 : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 45.15                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 75910                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.165                           
REMARK   3   R VALUE            (WORKING SET) : 0.164                           
REMARK   3   FREE R VALUE                     : 0.202                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.610                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1979                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 45.1637 -  4.8113    1.00     5574   149  0.1721 0.2049        
REMARK   3     2  4.8113 -  3.8195    1.00     5462   145  0.1312 0.1426        
REMARK   3     3  3.8195 -  3.3369    1.00     5326   147  0.1466 0.1804        
REMARK   3     4  3.3369 -  3.0319    1.00     5401   146  0.1561 0.2124        
REMARK   3     5  3.0319 -  2.8146    1.00     5328   138  0.1637 0.2178        
REMARK   3     6  2.8146 -  2.6487    1.00     5320   138  0.1673 0.2054        
REMARK   3     7  2.6487 -  2.5160    1.00     5313   144  0.1682 0.2138        
REMARK   3     8  2.5160 -  2.4065    1.00     5306   143  0.1695 0.2138        
REMARK   3     9  2.4065 -  2.3139    1.00     5268   140  0.1630 0.2055        
REMARK   3    10  2.3139 -  2.2340    1.00     5299   146  0.1824 0.2271        
REMARK   3    11  2.2340 -  2.1642    0.99     5283   142  0.1891 0.2619        
REMARK   3    12  2.1642 -  2.1023    1.00     5249   140  0.1982 0.2622        
REMARK   3    13  2.1023 -  2.0470    0.99     5288   138  0.2224 0.2754        
REMARK   3    14  2.0470 -  1.9970    0.86     4514   123  0.2760 0.3288        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.230            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.100           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.018           7497                                  
REMARK   3   ANGLE     :  1.491          10353                                  
REMARK   3   CHIRALITY :  0.094           1127                                  
REMARK   3   PLANARITY :  0.010           1193                                  
REMARK   3   DIHEDRAL  : 15.201           4325                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 8                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 52 THROUGH 103 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): -27.2612 -10.4012  17.8816              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6889 T22:   0.4641                                     
REMARK   3      T33:   0.7675 T12:   0.1496                                     
REMARK   3      T13:   0.1740 T23:   0.0735                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3785 L22:   2.2478                                     
REMARK   3      L33:   2.7450 L12:  -0.3066                                     
REMARK   3      L13:  -0.7445 L23:  -1.0173                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1830 S12:  -0.3811 S13:   0.9001                       
REMARK   3      S21:   0.4884 S22:   0.4052 S23:   0.8691                       
REMARK   3      S31:  -0.7174 S32:  -0.5303 S33:  -0.6087                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 104 THROUGH 280 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -22.7390 -28.0068  10.0883              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3010 T22:   0.2312                                     
REMARK   3      T33:   0.2493 T12:   0.0138                                     
REMARK   3      T13:  -0.0105 T23:  -0.0044                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5068 L22:   1.0559                                     
REMARK   3      L33:   0.6030 L12:   0.7062                                     
REMARK   3      L13:  -0.1461 L23:   0.0844                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0756 S12:  -0.0882 S13:   0.2413                       
REMARK   3      S21:   0.0680 S22:  -0.0769 S23:   0.0443                       
REMARK   3      S31:  -0.1644 S32:   0.0209 S33:   0.0018                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 281 THROUGH 454 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -36.5349 -33.7802   1.5251              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2316 T22:   0.2223                                     
REMARK   3      T33:   0.2487 T12:   0.0529                                     
REMARK   3      T13:   0.0190 T23:   0.0014                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7364 L22:   0.8470                                     
REMARK   3      L33:   0.5663 L12:   0.8104                                     
REMARK   3      L13:   0.4775 L23:   0.1220                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0438 S12:   0.0488 S13:   0.2086                       
REMARK   3      S21:  -0.0485 S22:   0.0084 S23:   0.1607                       
REMARK   3      S31:  -0.0968 S32:  -0.0825 S33:   0.0527                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 455 THROUGH 591 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -30.6825 -51.7357   7.8935              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1891 T22:   0.2308                                     
REMARK   3      T33:   0.1700 T12:   0.0141                                     
REMARK   3      T13:  -0.0014 T23:  -0.0076                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6861 L22:   1.2466                                     
REMARK   3      L33:   0.5306 L12:   0.5528                                     
REMARK   3      L13:  -0.0507 L23:  -0.1150                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0466 S12:  -0.0665 S13:  -0.0783                       
REMARK   3      S21:   0.0292 S22:  -0.0621 S23:  -0.0016                       
REMARK   3      S31:   0.0317 S32:  -0.0330 S33:   0.0106                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 592 THROUGH 770 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -41.6962 -73.1521   6.4807              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2054 T22:   0.1910                                     
REMARK   3      T33:   0.1654 T12:  -0.0147                                     
REMARK   3      T13:   0.0017 T23:   0.0023                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3259 L22:   0.7692                                     
REMARK   3      L33:   0.8426 L12:   0.2323                                     
REMARK   3      L13:   0.0458 L23:  -0.0805                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0145 S12:   0.0025 S13:  -0.1088                       
REMARK   3      S21:   0.0487 S22:  -0.0017 S23:   0.0212                       
REMARK   3      S31:   0.1566 S32:  -0.0462 S33:  -0.0116                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 771 THROUGH 858 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -32.7055 -60.3890   1.2640              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2242 T22:   0.2208                                     
REMARK   3      T33:   0.1783 T12:  -0.0020                                     
REMARK   3      T13:   0.0154 T23:   0.0082                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5221 L22:   1.1913                                     
REMARK   3      L33:   1.1337 L12:   0.1925                                     
REMARK   3      L13:   0.8431 L23:   0.2817                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0384 S12:   0.2070 S13:   0.0180                       
REMARK   3      S21:  -0.1034 S22:  -0.0001 S23:  -0.0724                       
REMARK   3      S31:  -0.0080 S32:   0.1044 S33:   0.0413                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 2001 THROUGH 2012 )               
REMARK   3    ORIGIN FOR THE GROUP (A): -47.1546 -15.1968 -13.8603              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7013 T22:   0.5305                                     
REMARK   3      T33:   0.8569 T12:   0.0303                                     
REMARK   3      T13:  -0.1619 T23:   0.2408                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3047 L22:   5.3727                                     
REMARK   3      L33:   3.1247 L12:   0.6270                                     
REMARK   3      L13:  -0.8114 L23:  -3.5990                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3271 S12:   0.4782 S13:   1.1696                       
REMARK   3      S21:   0.0364 S22:   0.5223 S23:   1.2134                       
REMARK   3      S31:  -0.9463 S32:  -0.4244 S33:  -0.3183                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 2013 THROUGH 2031 )               
REMARK   3    ORIGIN FOR THE GROUP (A): -48.4331 -16.3210  -3.1037              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6373 T22:   0.4364                                     
REMARK   3      T33:   0.6285 T12:   0.2213                                     
REMARK   3      T13:  -0.0267 T23:   0.0182                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.5111 L22:   6.9174                                     
REMARK   3      L33:   5.6949 L12:   0.8096                                     
REMARK   3      L13:  -0.4197 L23:  -1.4623                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0203 S12:  -0.5805 S13:   0.8481                       
REMARK   3      S21:   0.9904 S22:   0.3878 S23:   0.5785                       
REMARK   3      S31:  -0.9479 S32:  -0.9853 S33:  -0.4953                       
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 5HRT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 28-JAN-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000217595.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-NOV-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL32XU                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX225HE                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 75910                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.997                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 45.200                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.8                               
REMARK 200  DATA REDUNDANCY                : 14.80                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.56                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.65                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG3350, CALCIUM CHLORIDE, TRIS, PH      
REMARK 280  7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       45.01800            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       45.01800            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       60.03100            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000      104.37850            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       60.03100            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000      104.37850            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       45.01800            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       60.03100            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000      104.37850            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       45.01800            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       60.03100            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000      104.37850            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 13110 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 36200 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -39.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
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     ALA A    36                                                      
REMARK 465     GLU A    37                                                      
REMARK 465     TRP A    38                                                      
REMARK 465     ASP A    39                                                      
REMARK 465     GLU A    40                                                      
REMARK 465     GLY A    41                                                      
REMARK 465     PRO A    42                                                      
REMARK 465     PRO A    43                                                      
REMARK 465     THR A    44                                                      
REMARK 465     VAL A    45                                                      
REMARK 465     LEU A    46                                                      
REMARK 465     SER A    47                                                      
REMARK 465     ASP A    48                                                      
REMARK 465     SER A    49                                                      
REMARK 465     PRO A    50                                                      
REMARK 465     TRP A    51                                                      
REMARK 465     GLU A    67                                                      
REMARK 465     VAL A    68                                                      
REMARK 465     GLY A    69                                                      
REMARK 465     PRO A    70                                                      
REMARK 465     PRO A    71                                                      
REMARK 465     ASP A   570                                                      
REMARK 465     LYS A   571                                                      
REMARK 465     ASN A   572                                                      
REMARK 465     LYS A   573                                                      
REMARK 465     LEU A   574                                                      
REMARK 465     GLU A   575                                                      
REMARK 465     GLU A   576                                                      
REMARK 465     LEU A   577                                                      
REMARK 465     ASN A   578                                                      
REMARK 465     LYS A   579                                                      
REMARK 465     ARG A   580                                                      
REMARK 465     LEU A   581                                                      
REMARK 465     HIS A   582                                                      
REMARK 465     THR A   583                                                      
REMARK 465     LYS A   584                                                      
REMARK 465     GLY A   585                                                      
REMARK 465     SER A   859                                                      
REMARK 465     ARG A   860                                                      
REMARK 465     GLU A   861                                                      
REMARK 465     ASN A   862                                                      
REMARK 465     LEU A   863                                                      
REMARK 465     TYR A   864                                                      
REMARK 465     PHE A   865                                                      
REMARK 465     GLN A   866                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A  59    CG   CD   CE   NZ                                   
REMARK 470     ASP A  72    CG   OD1  OD2                                       
REMARK 470     GLU A  91    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 104    CG   CD   CE   NZ                                   
REMARK 470     GLU A 113    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 114    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 183    CG   CD   CE   NZ                                   
REMARK 470     ARG A 246    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     PHE A 274    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ILE A 396    CG1  CG2  CD1                                       
REMARK 470     ASN A 398    CG   OD1  ND2                                       
REMARK 470     LEU A 400    CG   CD1  CD2                                       
REMARK 470     LYS A 401    CG   CD   CE   NZ                                   
REMARK 470     LYS A 405    CD   CE   NZ                                        
REMARK 470     ASP A 417    CG   OD1  OD2                                       
REMARK 470     LYS A 462    CG   CD   CE   NZ                                   
REMARK 470     LYS A 463    CG   CD   CE   NZ                                   
REMARK 470     ARG A 540    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 589    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 636    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 642    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 686    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 745    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 746    CG   OD1  OD2                                       
REMARK 470     GLN A 750    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 857    CG   CD   OE1  OE2                                  
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  1008     O    HOH A  1406              2.02            
REMARK 500   OE2  GLU A   546     NH1  ARG A   596              2.05            
REMARK 500   OE2  GLU A   855     O    HOH A  1001              2.13            
REMARK 500   O    HOH A  1374     O    HOH A  1387              2.14            
REMARK 500   NH2  ARG A   794     O    HOH A  1002              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    VAL A 480   CB    VAL A 480   CG2     0.146                       
REMARK 500     DC B2012   O3'    DC B2012   C3'    -0.063                       
REMARK 500     DC B2013   O3'    DC B2013   C3'    -0.046                       
REMARK 500     DT B2027   O3'    DT B2027   C3'    -0.038                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    CYS A 148   CA  -  CB  -  SG  ANGL. DEV. = -13.4 DEGREES          
REMARK 500    CYS A 194   CA  -  CB  -  SG  ANGL. DEV. = -16.0 DEGREES          
REMARK 500    ARG A 549   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500    ARG A 596   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.7 DEGREES          
REMARK 500    ASP A 743   C   -  N   -  CA  ANGL. DEV. = -16.5 DEGREES          
REMARK 500    ASP A 743   CB  -  CG  -  OD2 ANGL. DEV. =  -9.7 DEGREES          
REMARK 500     DT B2003   O4' -  C1' -  N1  ANGL. DEV. =   1.9 DEGREES          
REMARK 500     DT B2027   O4' -  C1' -  N1  ANGL. DEV. =   1.9 DEGREES          
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  94       54.85   -118.56                                   
REMARK 500    PRO A 157      153.82    -47.65                                   
REMARK 500    PRO A 386     -168.26   -102.96                                   
REMARK 500    ALA A 435      -33.44   -154.94                                   
REMARK 500    ARG A 450        0.47     84.82                                   
REMARK 500    ASP A 477      129.92    -34.18                                   
REMARK 500    SER A 672     -157.73   -111.56                                   
REMARK 500    ASN A 724       62.88     62.51                                   
REMARK 500    ARG A 742      129.95    -39.76                                   
REMARK 500    TRP A 810      -26.65   -155.42                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K A 917   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 147   OD2                                                    
REMARK 620 2 TYR A 665   O    66.6                                              
REMARK 620 3 ASP A 668   O    68.1   2.4                                        
REMARK 620 4 MET A 671   O    67.6   1.1   1.6                                  
REMARK 620 5 HOH A1136   O    68.9   2.3   2.1   1.4                            
REMARK 620 6 HOH A1368   O    67.8   2.2   3.6   2.1   2.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 912  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 171   OD1                                                    
REMARK 620 2 THR A 209   OG1 120.8                                              
REMARK 620 3 ASP A 358   OD2 105.9 110.6                                        
REMARK 620 4 HIS A 359   NE2 104.9 111.9 100.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 913  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 311   OD1                                                    
REMARK 620 2 ASP A 311   OD2  54.7                                              
REMARK 620 3 HIS A 315   NE2 100.5 102.6                                        
REMARK 620 4 HIS A 474   NE2  87.2 135.4 106.9                                  
REMARK 620 5 HOH B2206   O   139.8  95.2 112.9 103.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 914  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 735   OD1                                                    
REMARK 620 2 ASN A 737   OD1  83.5                                              
REMARK 620 3 ASN A 739   OD1  83.1  85.0                                        
REMARK 620 4 LEU A 741   O    93.3 168.8  83.9                                  
REMARK 620 5 HOH A1155   O   169.7  89.9  88.5  91.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 915  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN A 797   O                                                      
REMARK 620 2 SER A 800   O    84.3                                              
REMARK 620 3 SER A 803   OG   90.3  82.7                                        
REMARK 620 4 HOH A1193   O    84.2 166.3  89.9                                  
REMARK 620 5 HOH A1298   O   104.3  91.6 163.7  98.5                            
REMARK 620 6 HOH A1392   O   164.6 110.4  87.2  80.6  80.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B2101  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 OMG B2009   O6                                                     
REMARK 620 2  DG B2025   OP2 105.9                                              
REMARK 620 3 HOH B2207   O    81.1  81.7                                        
REMARK 620 4 HOH B2213   O    87.4 166.7 100.5                                  
REMARK 620 5 HOH B2214   O   144.3  80.7 134.5  88.6                            
REMARK 620 6 HOH B2215   O    83.8  82.7 154.3  99.4  62.0                      
REMARK 620 7 HOH B2218   O   138.0  92.5  64.3  76.9  74.9 136.8                
REMARK 620 N                    1     2     3     4     5     6                 
DBREF  5HRT A   36   858  UNP    Q9R1E6   ENPP2_MOUSE     36    862             
DBREF  5HRT B 2001  2034  PDB    5HRT     5HRT          2001   2034             
SEQADV 5HRT     A       UNP  Q9R1E6    LYS   571 DELETION                       
SEQADV 5HRT     A       UNP  Q9R1E6    VAL   572 DELETION                       
SEQADV 5HRT     A       UNP  Q9R1E6    GLU   573 DELETION                       
SEQADV 5HRT     A       UNP  Q9R1E6    PRO   574 DELETION                       
SEQADV 5HRT SER A  859  UNP  Q9R1E6              EXPRESSION TAG                 
SEQADV 5HRT ARG A  860  UNP  Q9R1E6              EXPRESSION TAG                 
SEQADV 5HRT GLU A  861  UNP  Q9R1E6              EXPRESSION TAG                 
SEQADV 5HRT ASN A  862  UNP  Q9R1E6              EXPRESSION TAG                 
SEQADV 5HRT LEU A  863  UNP  Q9R1E6              EXPRESSION TAG                 
SEQADV 5HRT TYR A  864  UNP  Q9R1E6              EXPRESSION TAG                 
SEQADV 5HRT PHE A  865  UNP  Q9R1E6              EXPRESSION TAG                 
SEQADV 5HRT GLN A  866  UNP  Q9R1E6              EXPRESSION TAG                 
SEQRES   1 A  831  ALA GLU TRP ASP GLU GLY PRO PRO THR VAL LEU SER ASP          
SEQRES   2 A  831  SER PRO TRP THR ASN THR SER GLY SER CYS LYS GLY ARG          
SEQRES   3 A  831  CYS PHE GLU LEU GLN GLU VAL GLY PRO PRO ASP CYS ARG          
SEQRES   4 A  831  CYS ASP ASN LEU CYS LYS SER TYR SER SER CYS CYS HIS          
SEQRES   5 A  831  ASP PHE ASP GLU LEU CYS LEU LYS THR ALA ARG GLY TRP          
SEQRES   6 A  831  GLU CYS THR LYS ASP ARG CYS GLY GLU VAL ARG ASN GLU          
SEQRES   7 A  831  GLU ASN ALA CYS HIS CYS SER GLU ASP CYS LEU SER ARG          
SEQRES   8 A  831  GLY ASP CYS CYS THR ASN TYR GLN VAL VAL CYS LYS GLY          
SEQRES   9 A  831  GLU SER HIS TRP VAL ASP ASP ASP CYS GLU GLU ILE ARG          
SEQRES  10 A  831  VAL PRO GLU CYS PRO ALA GLY PHE VAL ARG PRO PRO LEU          
SEQRES  11 A  831  ILE ILE PHE SER VAL ASP GLY PHE ARG ALA SER TYR MET          
SEQRES  12 A  831  LYS LYS GLY SER LYS VAL MET PRO ASN ILE GLU LYS LEU          
SEQRES  13 A  831  ARG SER CYS GLY THR HIS ALA PRO TYR MET ARG PRO VAL          
SEQRES  14 A  831  TYR PRO THR LYS THR PHE PRO ASN LEU TYR THR LEU ALA          
SEQRES  15 A  831  THR GLY LEU TYR PRO GLU SER HIS GLY ILE VAL GLY ASN          
SEQRES  16 A  831  SER MET TYR ASP PRO VAL PHE ASP ALA THR PHE HIS LEU          
SEQRES  17 A  831  ARG GLY ARG GLU LYS PHE ASN HIS ARG TRP TRP GLY GLY          
SEQRES  18 A  831  GLN PRO LEU TRP ILE THR ALA THR LYS GLN GLY VAL ARG          
SEQRES  19 A  831  ALA GLY THR PHE PHE TRP SER VAL SER ILE PRO HIS GLU          
SEQRES  20 A  831  ARG ARG ILE LEU THR ILE LEU GLN TRP LEU SER LEU PRO          
SEQRES  21 A  831  ASP ASN GLU ARG PRO SER VAL TYR ALA PHE TYR SER GLU          
SEQRES  22 A  831  GLN PRO ASP PHE SER GLY HIS LYS TYR GLY PRO PHE GLY          
SEQRES  23 A  831  PRO GLU MET THR ASN PRO LEU ARG GLU ILE ASP LYS THR          
SEQRES  24 A  831  VAL GLY GLN LEU MET ASP GLY LEU LYS GLN LEU LYS LEU          
SEQRES  25 A  831  HIS ARG CYS VAL ASN VAL ILE PHE VAL GLY ASP HIS GLY          
SEQRES  26 A  831  MET GLU ASP VAL THR CYS ASP ARG THR GLU PHE LEU SER          
SEQRES  27 A  831  ASN TYR LEU THR ASN VAL ASP ASP ILE THR LEU VAL PRO          
SEQRES  28 A  831  GLY THR LEU GLY ARG ILE ARG PRO LYS ILE PRO ASN ASN          
SEQRES  29 A  831  LEU LYS TYR ASP PRO LYS ALA ILE ILE ALA ASN LEU THR          
SEQRES  30 A  831  CYS LYS LYS PRO ASP GLN HIS PHE LYS PRO TYR MET LYS          
SEQRES  31 A  831  GLN HIS LEU PRO LYS ARG LEU HIS TYR ALA ASN ASN ARG          
SEQRES  32 A  831  ARG ILE GLU ASP LEU HIS LEU LEU VAL GLU ARG ARG TRP          
SEQRES  33 A  831  HIS VAL ALA ARG LYS PRO LEU ASP VAL TYR LYS LYS PRO          
SEQRES  34 A  831  SER GLY LYS CYS PHE PHE GLN GLY ASP HIS GLY PHE ASP          
SEQRES  35 A  831  ASN LYS VAL ASN SER MET GLN THR VAL PHE VAL GLY TYR          
SEQRES  36 A  831  GLY PRO THR PHE LYS TYR ARG THR LYS VAL PRO PRO PHE          
SEQRES  37 A  831  GLU ASN ILE GLU LEU TYR ASN VAL MET CYS ASP LEU LEU          
SEQRES  38 A  831  GLY LEU LYS PRO ALA PRO ASN ASN GLY THR HIS GLY SER          
SEQRES  39 A  831  LEU ASN HIS LEU LEU ARG THR ASN THR PHE ARG PRO THR          
SEQRES  40 A  831  LEU PRO GLU GLU VAL SER ARG PRO ASN TYR PRO GLY ILE          
SEQRES  41 A  831  MET TYR LEU GLN SER ASP PHE ASP LEU GLY CYS THR CYS          
SEQRES  42 A  831  ASP ASP LYS ASN LYS LEU GLU GLU LEU ASN LYS ARG LEU          
SEQRES  43 A  831  HIS THR LYS GLY SER THR GLU GLU ARG HIS LEU LEU TYR          
SEQRES  44 A  831  GLY ARG PRO ALA VAL LEU TYR ARG THR SER TYR ASP ILE          
SEQRES  45 A  831  LEU TYR HIS THR ASP PHE GLU SER GLY TYR SER GLU ILE          
SEQRES  46 A  831  PHE LEU MET PRO LEU TRP THR SER TYR THR ILE SER LYS          
SEQRES  47 A  831  GLN ALA GLU VAL SER SER ILE PRO GLU HIS LEU THR ASN          
SEQRES  48 A  831  CYS VAL ARG PRO ASP VAL ARG VAL SER PRO GLY PHE SER          
SEQRES  49 A  831  GLN ASN CYS LEU ALA TYR LYS ASN ASP LYS GLN MET SER          
SEQRES  50 A  831  TYR GLY PHE LEU PHE PRO PRO TYR LEU SER SER SER PRO          
SEQRES  51 A  831  GLU ALA LYS TYR ASP ALA PHE LEU VAL THR ASN MET VAL          
SEQRES  52 A  831  PRO MET TYR PRO ALA PHE LYS ARG VAL TRP THR TYR PHE          
SEQRES  53 A  831  GLN ARG VAL LEU VAL LYS LYS TYR ALA SER GLU ARG ASN          
SEQRES  54 A  831  GLY VAL ASN VAL ILE SER GLY PRO ILE PHE ASP TYR ASN          
SEQRES  55 A  831  TYR ASN GLY LEU ARG ASP ILE GLU ASP GLU ILE LYS GLN          
SEQRES  56 A  831  TYR VAL GLU GLY SER SER ILE PRO VAL PRO THR HIS TYR          
SEQRES  57 A  831  TYR SER ILE ILE THR SER CYS LEU ASP PHE THR GLN PRO          
SEQRES  58 A  831  ALA ASP LYS CYS ASP GLY PRO LEU SER VAL SER SER PHE          
SEQRES  59 A  831  ILE LEU PRO HIS ARG PRO ASP ASN ASP GLU SER CYS ASN          
SEQRES  60 A  831  SER SER GLU ASP GLU SER LYS TRP VAL GLU GLU LEU MET          
SEQRES  61 A  831  LYS MET HIS THR ALA ARG VAL ARG ASP ILE GLU HIS LEU          
SEQRES  62 A  831  THR GLY LEU ASP PHE TYR ARG LYS THR SER ARG SER TYR          
SEQRES  63 A  831  SER GLU ILE LEU THR LEU LYS THR TYR LEU HIS THR TYR          
SEQRES  64 A  831  GLU SER GLU ILE SER ARG GLU ASN LEU TYR PHE GLN              
SEQRES   1 B   34   DC  DC  DT  DG  DG  DA OMC  DG OMG  DA  DA  DC  DC          
SEQRES   2 B   34  A2M OMG  DA  DA  DT A2M OMC  DT  DT  DT  DT  DG  DG          
SEQRES   3 B   34   DT  DC  DT  DC  DC A2M OMG OMG                              
HET    OMC  B2007      21                                                       
HET    OMG  B2009      24                                                       
HET    A2M  B2014      23                                                       
HET    OMG  B2015      24                                                       
HET    A2M  B2019      23                                                       
HET    OMC  B2020      21                                                       
HET    A2M  B2032      23                                                       
HET    OMG  B2033      24                                                       
HET    OMG  B2034      24                                                       
HET    NAG  C   1      14                                                       
HET    NAG  C   2      14                                                       
HET    BMA  C   3      11                                                       
HET    MAN  C   4      11                                                       
HET    MAN  C   5      11                                                       
HET    MAN  C   6      11                                                       
HET    MAN  C   7      11                                                       
HET    NAG  D   1      14                                                       
HET    NAG  D   2      14                                                       
HET    BMA  D   3      11                                                       
HET    MAN  D   4      11                                                       
HET     ZN  A 912       1                                                       
HET     ZN  A 913       1                                                       
HET     CA  A 914       1                                                       
HET     NA  A 915       1                                                       
HET     CL  A 916       1                                                       
HET      K  A 917       1                                                       
HET    GOL  A 918       6                                                       
HET    GOL  A 919       6                                                       
HET    GOL  A 920       6                                                       
HET    GOL  A 921       6                                                       
HET    GOL  A 922       6                                                       
HET    GOL  A 923       6                                                       
HET    GOL  A 924       6                                                       
HET    GOL  A 925       6                                                       
HET    GOL  A 926       6                                                       
HET    GOL  A 927       6                                                       
HET     CA  B2101       1                                                       
HETNAM     OMC O2'-METHYLYCYTIDINE-5'-MONOPHOSPHATE                             
HETNAM     OMG O2'-METHYLGUANOSINE-5'-MONOPHOSPHATE                             
HETNAM     A2M 2'-O-METHYLADENOSINE 5'-(DIHYDROGEN PHOSPHATE)                   
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     BMA BETA-D-MANNOPYRANOSE                                             
HETNAM     MAN ALPHA-D-MANNOPYRANOSE                                            
HETNAM      ZN ZINC ION                                                         
HETNAM      CA CALCIUM ION                                                      
HETNAM      NA SODIUM ION                                                       
HETNAM      CL CHLORIDE ION                                                     
HETNAM       K POTASSIUM ION                                                    
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   2  OMC    2(C10 H16 N3 O8 P)                                           
FORMUL   2  OMG    4(C11 H16 N5 O8 P)                                           
FORMUL   2  A2M    3(C11 H16 N5 O7 P)                                           
FORMUL   3  NAG    4(C8 H15 N O6)                                               
FORMUL   3  BMA    2(C6 H12 O6)                                                 
FORMUL   3  MAN    5(C6 H12 O6)                                                 
FORMUL   5   ZN    2(ZN 2+)                                                     
FORMUL   7   CA    2(CA 2+)                                                     
FORMUL   8   NA    NA 1+                                                        
FORMUL   9   CL    CL 1-                                                        
FORMUL  10    K    K 1+                                                         
FORMUL  11  GOL    10(C3 H8 O3)                                                 
FORMUL  22  HOH   *459(H2 O)                                                    
HELIX    1 AA1 LEU A   78  SER A   83  1                                   6    
HELIX    2 AA2 ASP A   88  LEU A   94  1                                   7    
HELIX    3 AA3 THR A  103  CYS A  107  5                                   5    
HELIX    4 AA4 ASP A  122  GLY A  127  1                                   6    
HELIX    5 AA5 ASN A  132  GLY A  139  1                                   8    
HELIX    6 AA6 HIS A  142  ASP A  146  5                                   5    
HELIX    7 AA7 ARG A  174  LYS A  179  5                                   6    
HELIX    8 AA8 LYS A  180  MET A  185  1                                   6    
HELIX    9 AA9 MET A  185  GLY A  195  1                                  11    
HELIX   10 AB1 LYS A  208  GLY A  219  1                                  12    
HELIX   11 AB2 TYR A  221  GLY A  226  1                                   6    
HELIX   12 AB3 ARG A  246  TRP A  254  5                                   9    
HELIX   13 AB4 PRO A  258  GLN A  266  1                                   9    
HELIX   14 AB5 PRO A  280  SER A  293  1                                  14    
HELIX   15 AB6 ASP A  311  GLY A  318  1                                   8    
HELIX   16 AB7 GLY A  321  GLU A  323  5                                   3    
HELIX   17 AB8 MET A  324  LEU A  345  1                                  22    
HELIX   18 AB9 SER A  373  TYR A  375  5                                   3    
HELIX   19 AC1 ASN A  378  ASP A  380  5                                   3    
HELIX   20 AC2 ASP A  403  LEU A  411  1                                   9    
HELIX   21 AC3 GLN A  426  LEU A  428  5                                   3    
HELIX   22 AC4 PRO A  429  HIS A  433  5                                   5    
HELIX   23 AC5 VAL A  480  GLN A  484  5                                   5    
HELIX   24 AC6 GLU A  507  LEU A  516  1                                  10    
HELIX   25 AC7 LEU A  530  LEU A  534  5                                   5    
HELIX   26 AC8 LEU A  558  PHE A  562  5                                   5    
HELIX   27 AC9 THR A  587  LEU A  592  1                                   6    
HELIX   28 AD1 PRO A  641  THR A  645  5                                   5    
HELIX   29 AD2 SER A  655  SER A  659  5                                   5    
HELIX   30 AD3 ASN A  661  ASP A  668  1                                   8    
HELIX   31 AD4 PRO A  678  SER A  682  5                                   5    
HELIX   32 AD5 SER A  684  PHE A  692  1                                   9    
HELIX   33 AD6 LEU A  693  THR A  695  5                                   3    
HELIX   34 AD7 TYR A  701  VAL A  714  1                                  14    
HELIX   35 AD8 VAL A  714  ASN A  724  1                                  11    
HELIX   36 AD9 PRO A  776  CYS A  780  5                                   5    
HELIX   37 AE1 ASP A  806  LYS A  809  5                                   4    
HELIX   38 AE2 TRP A  810  HIS A  818  1                                   9    
HELIX   39 AE3 ARG A  821  GLY A  830  1                                  10    
HELIX   40 AE4 SER A  840  TYR A  850  1                                  11    
SHEET    1 AA1 6 VAL A 302  PRO A 310  0                                        
SHEET    2 AA1 6 LEU A 165  ASP A 171  1  N  ILE A 167   O  PHE A 305           
SHEET    3 AA1 6 ASN A 352  GLY A 357  1  O  ILE A 354   N  PHE A 168           
SHEET    4 AA1 6 THR A 485  TYR A 490 -1  O  TYR A 490   N  VAL A 353           
SHEET    5 AA1 6 THR A 196  ARG A 202 -1  N  THR A 196   O  GLY A 489           
SHEET    6 AA1 6 THR A 498  LYS A 499  1  O  THR A 498   N  HIS A 197           
SHEET    1 AA2 6 VAL A 302  PRO A 310  0                                        
SHEET    2 AA2 6 LEU A 165  ASP A 171  1  N  ILE A 167   O  PHE A 305           
SHEET    3 AA2 6 ASN A 352  GLY A 357  1  O  ILE A 354   N  PHE A 168           
SHEET    4 AA2 6 THR A 485  TYR A 490 -1  O  TYR A 490   N  VAL A 353           
SHEET    5 AA2 6 THR A 196  ARG A 202 -1  N  THR A 196   O  GLY A 489           
SHEET    6 AA2 6 PHE A 503  GLU A 504  1  O  PHE A 503   N  ARG A 202           
SHEET    1 AA3 2 MET A 232  ASP A 234  0                                        
SHEET    2 AA3 2 ALA A 239  PHE A 241 -1  O  ALA A 239   N  ASP A 234           
SHEET    1 AA4 2 GLU A 362  ASP A 363  0                                        
SHEET    2 AA4 2 GLY A 472  ASP A 473 -1  O  ASP A 473   N  GLU A 362           
SHEET    1 AA5 2 THR A 369  PHE A 371  0                                        
SHEET    2 AA5 2 HIS A 452  ALA A 454  1  O  ALA A 454   N  GLU A 370           
SHEET    1 AA6 4 ILE A 382  VAL A 385  0                                        
SHEET    2 AA6 4 LEU A 389  PRO A 394 -1  O  ARG A 393   N  THR A 383           
SHEET    3 AA6 4 LEU A 443  VAL A 447 -1  O  LEU A 445   N  GLY A 390           
SHEET    4 AA6 4 PHE A 420  MET A 424 -1  N  TYR A 423   O  HIS A 444           
SHEET    1 AA7 2 ALA A 598  VAL A 599  0                                        
SHEET    2 AA7 2 LEU A 831  ASP A 832 -1  O  ASP A 832   N  ALA A 598           
SHEET    1 AA8 7 TYR A 605  TYR A 609  0                                        
SHEET    2 AA8 7 GLU A 614  SER A 618 -1  O  TYR A 617   N  ASP A 606           
SHEET    3 AA8 7 PRO A 624  ILE A 631 -1  O  SER A 628   N  GLU A 614           
SHEET    4 AA8 7 VAL A 726  ILE A 733 -1  O  VAL A 728   N  TYR A 629           
SHEET    5 AA8 7 HIS A 762  CYS A 770 -1  O  THR A 768   N  ASN A 727           
SHEET    6 AA8 7 LEU A 784  PRO A 792 -1  O  SER A 787   N  ILE A 767           
SHEET    7 AA8 7 THR A 819  ALA A 820 -1  O  ALA A 820   N  SER A 788           
SHEET    1 AA9 2 SER A 672  PHE A 675  0                                        
SHEET    2 AA9 2 MET A 697  MET A 700 -1  O  VAL A 698   N  GLY A 674           
SSBOND   1 CYS A   58    CYS A   75                          1555   1555  2.05  
SSBOND   2 CYS A   62    CYS A   93                          1555   1555  2.04  
SSBOND   3 CYS A   73    CYS A   86                          1555   1555  2.09  
SSBOND   4 CYS A   79    CYS A   85                          1555   1555  2.07  
SSBOND   5 CYS A  102    CYS A  119                          1555   1555  2.07  
SSBOND   6 CYS A  107    CYS A  137                          1555   1555  2.07  
SSBOND   7 CYS A  117    CYS A  130                          1555   1555  2.11  
SSBOND   8 CYS A  123    CYS A  129                          1555   1555  2.09  
SSBOND   9 CYS A  148    CYS A  194                          1555   1555  2.00  
SSBOND  10 CYS A  156    CYS A  350                          1555   1555  2.07  
SSBOND  11 CYS A  366    CYS A  468                          1555   1555  2.08  
SSBOND  12 CYS A  413    CYS A  801                          1555   1555  2.09  
SSBOND  13 CYS A  566    CYS A  662                          1555   1555  2.12  
SSBOND  14 CYS A  568    CYS A  647                          1555   1555  2.06  
SSBOND  15 CYS A  770    CYS A  780                          1555   1555  2.14  
LINK         ND2 ASN A 410                 C1  NAG D   1     1555   1555  1.46  
LINK         ND2 ASN A 524                 C1  NAG C   1     1555   1555  1.45  
LINK         O3'  DA B2006                 P   OMC B2007     1555   1555  1.61  
LINK         O3' OMC B2007                 P    DG B2008     1555   1555  1.63  
LINK         O3'  DG B2008                 P   OMG B2009     1555   1555  1.60  
LINK         O3' OMG B2009                 P    DA B2010     1555   1555  1.61  
LINK         O3'  DC B2013                 P   A2M B2014     1555   1555  1.59  
LINK         O3' A2M B2014                 P   OMG B2015     1555   1555  1.62  
LINK         O3' OMG B2015                 P    DA B2016     1555   1555  1.59  
LINK         O3'  DT B2018                 P   A2M B2019     1555   1555  1.61  
LINK         O3' A2M B2019                 P   OMC B2020     1555   1555  1.61  
LINK         O3' OMC B2020                 P    DT B2021     1555   1555  1.61  
LINK         O3'  DC B2031                 P   A2M B2032     1555   1555  1.62  
LINK         O3' A2M B2032                 P   OMG B2033     1555   1555  1.61  
LINK         O3' OMG B2033                 P   OMG B2034     1555   1555  1.61  
LINK         O4  NAG C   1                 C1  NAG C   2     1555   1555  1.40  
LINK         O4  NAG C   2                 C1  BMA C   3     1555   1555  1.44  
LINK         O6  BMA C   3                 C1  MAN C   4     1555   1555  1.45  
LINK         O3  BMA C   3                 C1  MAN C   7     1555   1555  1.43  
LINK         O3  MAN C   4                 C1  MAN C   5     1555   1555  1.46  
LINK         O2  MAN C   5                 C1  MAN C   6     1555   1555  1.43  
LINK         O4  NAG D   1                 C1  NAG D   2     1555   1555  1.44  
LINK         O4  NAG D   2                 C1  BMA D   3     1555   1555  1.45  
LINK         O3  BMA D   3                 C1  MAN D   4     1555   1555  1.47  
LINK         OD2 ASP A 147                 K     K A 917     1555   8545  2.34  
LINK         OD1 ASP A 171                ZN    ZN A 912     1555   1555  1.87  
LINK         OG1 THR A 209                ZN    ZN A 912     1555   1555  1.97  
LINK         OD1 ASP A 311                ZN    ZN A 913     1555   1555  2.61  
LINK         OD2 ASP A 311                ZN    ZN A 913     1555   1555  2.03  
LINK         NE2 HIS A 315                ZN    ZN A 913     1555   1555  1.99  
LINK         OD2 ASP A 358                ZN    ZN A 912     1555   1555  2.08  
LINK         NE2 HIS A 359                ZN    ZN A 912     1555   1555  2.08  
LINK         NE2 HIS A 474                ZN    ZN A 913     1555   1555  2.11  
LINK         O   TYR A 665                 K     K A 917     1555   1555  2.34  
LINK         O   ASP A 668                 K     K A 917     1555   1555  2.36  
LINK         O   MET A 671                 K     K A 917     1555   1555  2.42  
LINK         OD1 ASP A 735                CA    CA A 914     1555   1555  2.29  
LINK         OD1 ASN A 737                CA    CA A 914     1555   1555  2.35  
LINK         OD1 ASN A 739                CA    CA A 914     1555   1555  2.42  
LINK         O   LEU A 741                CA    CA A 914     1555   1555  2.29  
LINK         O   ASN A 797                NA    NA A 915     1555   1555  2.37  
LINK         O   SER A 800                NA    NA A 915     1555   1555  2.35  
LINK         OG  SER A 803                NA    NA A 915     1555   1555  2.45  
LINK        ZN    ZN A 913                 O   HOH B2206     1555   1555  1.98  
LINK        CA    CA A 914                 O   HOH A1155     1555   1555  2.43  
LINK        NA    NA A 915                 O   HOH A1193     1555   1555  2.73  
LINK        NA    NA A 915                 O   HOH A1298     1555   1555  2.27  
LINK        NA    NA A 915                 O   HOH A1392     1555   1555  2.61  
LINK         K     K A 917                 O   HOH A1136     1555   8445  2.42  
LINK         K     K A 917                 O   HOH A1368     1555   1555  2.40  
LINK         O6  OMG B2009                CA    CA B2101     1555   1555  2.48  
LINK         OP2  DG B2025                CA    CA B2101     1555   1555  2.28  
LINK        CA    CA B2101                 O   HOH B2207     1555   1555  2.45  
LINK        CA    CA B2101                 O   HOH B2213     1555   1555  2.27  
LINK        CA    CA B2101                 O   HOH B2214     1555   1555  2.55  
LINK        CA    CA B2101                 O   HOH B2215     1555   1555  2.50  
LINK        CA    CA B2101                 O   HOH B2218     1555   1555  2.66  
CISPEP   1 TYR A  205    PRO A  206          0        -4.45                     
CISPEP   2 GLN A  309    PRO A  310          0        14.55                     
CISPEP   3 GLN A  309    PRO A  310          0        -0.39                     
CRYST1  120.062  208.757   90.036  90.00  90.00  90.00 C 2 2 21      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.008329  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.004790  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011107        0.00000                         
ATOM      1  N   THR A  52     -41.275 -10.268  26.662  1.00 85.65           N  
ANISOU    1  N   THR A  52     9002  10278  13265   3993   5045   2472       N  
ATOM      2  CA  THR A  52     -39.847 -10.058  26.477  1.00 84.08           C  
ANISOU    2  CA  THR A  52     9163   9907  12876   3871   4914   2116       C  
ATOM      3  C   THR A  52     -39.458  -8.556  26.442  1.00 85.63           C  
ANISOU    3  C   THR A  52     9652   9759  13126   4016   5044   1820       C  
ATOM      4  O   THR A  52     -40.013  -7.754  25.683  1.00 86.89           O  
ANISOU    4  O   THR A  52     9691   9746  13577   4119   5024   1983       O  
ATOM      5  CB  THR A  52     -39.375 -10.789  25.185  1.00 81.16           C  
ANISOU    5  CB  THR A  52     8712   9556  12569   3551   4422   2270       C  
ATOM      6  OG1 THR A  52     -37.982 -10.538  24.936  1.00 76.97           O  
ANISOU    6  OG1 THR A  52     8553   8856  11835   3370   4219   1928       O  
ATOM      7  CG2 THR A  52     -40.221 -10.359  23.981  1.00 84.66           C  
ANISOU    7  CG2 THR A  52     8836   9921  13409   3643   4318   2614       C  
ATOM      8  N   ASN A  53     -38.492  -8.182  27.282  1.00 86.28           N  
ANISOU    8  N   ASN A  53    10126   9751  12905   3986   5148   1383       N  
ATOM      9  CA  ASN A  53     -38.009  -6.804  27.365  1.00 88.84           C  
ANISOU    9  CA  ASN A  53    10763   9746  13245   4054   5240   1052       C  
ATOM     10  C   ASN A  53     -36.881  -6.631  26.351  1.00 86.43           C  
ANISOU   10  C   ASN A  53    10616   9227  12996   3892   4984    937       C  
ATOM     11  O   ASN A  53     -35.714  -6.935  26.622  1.00 84.50           O  
ANISOU   11  O   ASN A  53    10639   8998  12468   3691   4848    642       O  
ATOM     12  CB  ASN A  53     -37.548  -6.485  28.782  1.00 91.60           C  
ANISOU   12  CB  ASN A  53    11441  10127  13236   4070   5441    632       C  
ATOM     13  CG  ASN A  53     -37.133  -5.039  28.945  1.00 95.66           C  
ANISOU   13  CG  ASN A  53    12257  10303  13784   4126   5540    283       C  
ATOM     14  OD1 ASN A  53     -37.451  -4.205  28.101  1.00 97.15           O  
ANISOU   14  OD1 ASN A  53    12380  10240  14294   4207   5526    411       O  
ATOM     15  ND2 ASN A  53     -36.424  -4.730  30.035  1.00 97.42           N  
ANISOU   15  ND2 ASN A  53    12806  10533  13677   4072   5629   -149       N  
ATOM     16  N   THR A  54     -37.219  -6.149  25.157  1.00 85.61           N  
ANISOU   16  N   THR A  54    10347   8952  13228   3929   4855   1185       N  
ATOM     17  CA  THR A  54     -36.176  -5.993  24.154  1.00 82.93           C  
ANISOU   17  CA  THR A  54    10154   8431  12925   3739   4567   1105       C  
ATOM     18  C   THR A  54     -35.402  -4.707  24.335  1.00 84.58           C  
ANISOU   18  C   THR A  54    10719   8291  13127   3757   4678    735       C  
ATOM     19  O   THR A  54     -34.610  -4.346  23.455  1.00 84.15           O  
ANISOU   19  O   THR A  54    10781   8031  13163   3636   4488    690       O  
ATOM     20  CB  THR A  54     -36.754  -6.054  22.735  1.00 82.30           C  
ANISOU   20  CB  THR A  54     9764   8341  13164   3737   4337   1528       C  
ATOM     21  OG1 THR A  54     -37.618  -4.938  22.532  1.00 86.42           O  
ANISOU   21  OG1 THR A  54    10192   8686  13958   3960   4522   1665       O  
ATOM     22  CG2 THR A  54     -37.538  -7.352  22.505  1.00 80.15           C  
ANISOU   22  CG2 THR A  54     9134   8428  12893   3642   4158   1886       C  
ATOM     23  N   SER A  55     -35.608  -4.019  25.455  1.00 86.81           N  
ANISOU   23  N   SER A  55    11176   8521  13285   3861   4940    473       N  
ATOM     24  CA  SER A  55     -34.897  -2.782  25.727  1.00 89.57           C  
ANISOU   24  CA  SER A  55    11863   8559  13611   3826   5011     97       C  
ATOM     25  C   SER A  55     -33.467  -3.013  26.180  1.00 89.08           C  
ANISOU   25  C   SER A  55    12125   8493  13227   3588   4888   -314       C  
ATOM     26  O   SER A  55     -32.683  -2.059  26.207  1.00 91.05           O  
ANISOU   26  O   SER A  55    12639   8481  13474   3491   4869   -615       O  
ATOM     27  CB  SER A  55     -35.639  -1.977  26.787  1.00 92.99           C  
ANISOU   27  CB  SER A  55    12364   8948  14021   4023   5320    -50       C  
ATOM     28  OG  SER A  55     -37.029  -2.154  26.627  1.00 95.06           O  
ANISOU   28  OG  SER A  55    12286   9341  14490   4235   5444    348       O  
ATOM     29  N   GLY A  56     -33.117  -4.240  26.549  1.00 87.27           N  
ANISOU   29  N   GLY A  56    11872   8557  12728   3483   4803   -323       N  
ATOM     30  CA  GLY A  56     -31.749  -4.566  26.879  1.00 86.85           C  
ANISOU   30  CA  GLY A  56    12098   8542  12359   3244   4653   -668       C  
ATOM     31  C   GLY A  56     -30.841  -4.465  25.661  1.00 84.99           C  
ANISOU   31  C   GLY A  56    11902   8148  12242   3011   4317   -622       C  
ATOM     32  O   GLY A  56     -31.237  -4.051  24.570  1.00 86.01           O  
ANISOU   32  O   GLY A  56    11880   8093  12706   3080   4260   -355       O  
ATOM     33  N   SER A  57     -29.586  -4.852  25.867  1.00 81.73           N  
ANISOU   33  N   SER A  57    11688   7831  11533   2735   4092   -878       N  
ATOM     34  CA  SER A  57     -28.585  -4.707  24.822  1.00 79.64           C  
ANISOU   34  CA  SER A  57    11490   7425  11344   2505   3795   -880       C  
ATOM     35  C   SER A  57     -27.759  -5.971  24.706  1.00 76.79           C  
ANISOU   35  C   SER A  57    11105   7381  10691   2237   3460   -848       C  
ATOM     36  O   SER A  57     -27.485  -6.642  25.708  1.00 76.53           O  
ANISOU   36  O   SER A  57    11144   7607  10328   2178   3471  -1005       O  
ATOM     37  CB  SER A  57     -27.648  -3.533  25.089  1.00 80.52           C  
ANISOU   37  CB  SER A  57    11919   7220  11457   2427   3879  -1287       C  
ATOM     38  OG  SER A  57     -26.666  -3.444  24.078  1.00 77.31           O  
ANISOU   38  OG  SER A  57    11554   6702  11120   2198   3597  -1260       O  
ATOM     39  N   CYS A  58     -27.343  -6.268  23.470  1.00 74.69           N  
ANISOU   39  N   CYS A  58    10746   7089  10543   2086   3172   -640       N  
ATOM     40  CA  CYS A  58     -26.467  -7.389  23.167  1.00 74.80           C  
ANISOU   40  CA  CYS A  58    10749   7349  10322   1837   2849   -605       C  
ATOM     41  C   CYS A  58     -24.993  -7.055  23.317  1.00 75.98           C  
ANISOU   41  C   CYS A  58    11148   7433  10289   1617   2722   -935       C  
ATOM     42  O   CYS A  58     -24.158  -7.729  22.697  1.00 74.08           O  
ANISOU   42  O   CYS A  58    10893   7310   9944   1418   2442   -873       O  
ATOM     43  CB  CYS A  58     -26.719  -7.896  21.748  1.00 74.68           C  
ANISOU   43  CB  CYS A  58    10522   7354  10499   1784   2604   -237       C  
ATOM     44  SG  CYS A  58     -28.234  -8.823  21.626  1.00 76.31           S  
ANISOU   44  SG  CYS A  58    10399   7778  10818   1933   2633    160       S  
ATOM     45  N   LYS A  59     -24.655  -6.030  24.106  1.00 78.81           N  
ANISOU   45  N   LYS A  59    11728   7606  10612   1645   2922  -1285       N  
ATOM     46  CA  LYS A  59     -23.264  -5.615  24.253  1.00 77.77           C  
ANISOU   46  CA  LYS A  59    11817   7401  10332   1415   2800  -1609       C  
ATOM     47  C   LYS A  59     -22.495  -6.683  25.020  1.00 76.30           C  
ANISOU   47  C   LYS A  59    11672   7584   9735   1254   2636  -1735       C  
ATOM     48  O   LYS A  59     -22.894  -7.066  26.124  1.00 77.99           O  
ANISOU   48  O   LYS A  59    11909   8003   9722   1345   2775  -1829       O  
ATOM     49  CB  LYS A  59     -23.181  -4.264  24.963  1.00 79.84           C  
ANISOU   49  CB  LYS A  59    12309   7363  10663   1477   3062  -1973       C  
ATOM     50  N   GLY A  60     -21.415  -7.183  24.432  1.00 73.60           N  
ANISOU   50  N   GLY A  60    11329   7339   9296   1032   2351  -1711       N  
ATOM     51  CA  GLY A  60     -20.669  -8.246  25.071  1.00 72.29           C  
ANISOU   51  CA  GLY A  60    11180   7525   8762    896   2186  -1782       C  
ATOM     52  C   GLY A  60     -21.370  -9.583  25.166  1.00 71.39           C  
ANISOU   52  C   GLY A  60    10886   7696   8544    979   2140  -1490       C  
ATOM     53  O   GLY A  60     -20.859 -10.479  25.844  1.00 72.39           O  
ANISOU   53  O   GLY A  60    11029   8114   8361    903   2044  -1534       O  
ATOM     54  N   ARG A  61     -22.510  -9.767  24.492  1.00 69.05           N  
ANISOU   54  N   ARG A  61    10407   7326   8501   1125   2196  -1179       N  
ATOM     55  CA  ARG A  61     -23.273 -11.008  24.594  1.00 64.47           C  
ANISOU   55  CA  ARG A  61     9644   6991   7859   1189   2165   -899       C  
ATOM     56  C   ARG A  61     -23.550 -11.692  23.268  1.00 57.61           C  
ANISOU   56  C   ARG A  61     8591   6113   7184   1142   1955   -562       C  
ATOM     57  O   ARG A  61     -24.326 -12.653  23.254  1.00 57.54           O  
ANISOU   57  O   ARG A  61     8414   6262   7185   1189   1937   -317       O  
ATOM     58  CB  ARG A  61     -24.634 -10.761  25.262  1.00 65.45           C  
ANISOU   58  CB  ARG A  61     9681   7110   8078   1425   2460   -823       C  
ATOM     59  CG  ARG A  61     -24.580 -10.205  26.638  1.00 68.50           C  
ANISOU   59  CG  ARG A  61    10241   7540   8248   1509   2702  -1137       C  
ATOM     60  CD  ARG A  61     -25.957  -9.691  27.026  1.00 72.22           C  
ANISOU   60  CD  ARG A  61    10619   7922   8898   1772   3022  -1050       C  
ATOM     61  NE  ARG A  61     -26.952 -10.756  26.950  1.00 71.80           N  
ANISOU   61  NE  ARG A  61    10312   8073   8894   1852   3025   -688       N  
ATOM     62  CZ  ARG A  61     -28.258 -10.580  26.749  1.00 73.14           C  
ANISOU   62  CZ  ARG A  61    10283   8181   9327   2051   3207   -446       C  
ATOM     63  NH1 ARG A  61     -28.776  -9.364  26.585  1.00 75.26           N  
ANISOU   63  NH1 ARG A  61    10575   8178   9843   2223   3418   -508       N  
ATOM     64  NH2 ARG A  61     -29.051 -11.638  26.699  1.00 71.88           N  
ANISOU   64  NH2 ARG A  61     9886   8228   9198   2075   3178   -125       N  
ATOM     65  N   CYS A  62     -23.014 -11.197  22.157  1.00 53.31           N  
ANISOU   65  N   CYS A  62     8068   5386   6800   1053   1810   -538       N  
ATOM     66  CA  CYS A  62     -23.447 -11.701  20.864  1.00 52.14           C  
ANISOU   66  CA  CYS A  62     7747   5222   6842   1037   1637   -223       C  
ATOM     67  C   CYS A  62     -23.189 -13.205  20.777  1.00 49.10           C  
ANISOU   67  C   CYS A  62     7293   5091   6272    924   1434    -90       C  
ATOM     68  O   CYS A  62     -22.148 -13.694  21.217  1.00 49.60           O  
ANISOU   68  O   CYS A  62     7471   5288   6088    804   1337   -240       O  
ATOM     69  CB  CYS A  62     -22.744 -10.950  19.737  1.00 53.30           C  
ANISOU   69  CB  CYS A  62     7953   5162   7136    952   1514   -231       C  
ATOM     70  SG  CYS A  62     -23.425  -9.255  19.441  1.00 59.46           S  
ANISOU   70  SG  CYS A  62     8748   5582   8261   1125   1750   -240       S  
ATOM     71  N   PHE A  63     -24.188 -13.943  20.304  1.00 46.55           N  
ANISOU   71  N   PHE A  63     6776   4837   6073    970   1388    193       N  
ATOM     72  CA  PHE A  63     -24.103 -15.402  20.174  1.00 45.29           C  
ANISOU   72  CA  PHE A  63     6546   4877   5787    867   1212    338       C  
ATOM     73  C   PHE A  63     -23.646 -16.084  21.466  1.00 47.21           C  
ANISOU   73  C   PHE A  63     6876   5317   5744    846   1278    208       C  
ATOM     74  O   PHE A  63     -22.898 -17.070  21.437  1.00 45.37           O  
ANISOU   74  O   PHE A  63     6685   5215   5339    731   1116    218       O  
ATOM     75  CB  PHE A  63     -23.198 -15.774  18.999  1.00 41.15           C  
ANISOU   75  CB  PHE A  63     6065   4328   5243    717    947    371       C  
ATOM     76  CG  PHE A  63     -23.694 -15.241  17.704  1.00 42.53           C  
ANISOU   76  CG  PHE A  63     6141   4355   5662    739    867    537       C  
ATOM     77  CD1 PHE A  63     -24.780 -15.832  17.071  1.00 44.70           C  
ANISOU   77  CD1 PHE A  63     6221   4676   6089    761    792    800       C  
ATOM     78  CD2 PHE A  63     -23.142 -14.095  17.152  1.00 42.35           C  
ANISOU   78  CD2 PHE A  63     6210   4152   5729    741    877    443       C  
ATOM     79  CE1 PHE A  63     -25.295 -15.286  15.864  1.00 45.24           C  
ANISOU   79  CE1 PHE A  63     6183   4638   6370    793    710    972       C  
ATOM     80  CE2 PHE A  63     -23.650 -13.551  15.962  1.00 43.64           C  
ANISOU   80  CE2 PHE A  63     6275   4190   6117    784    816    631       C  
ATOM     81  CZ  PHE A  63     -24.721 -14.142  15.322  1.00 44.89           C  
ANISOU   81  CZ  PHE A  63     6236   4422   6399    816    728    895       C  
ATOM     82  N   GLU A  64     -24.099 -15.564  22.615  1.00 49.16           N  
ANISOU   82  N   GLU A  64     7154   5594   5932    972   1525     92       N  
ATOM     83  CA  GLU A  64     -23.792 -16.194  23.889  1.00 48.76           C  
ANISOU   83  CA  GLU A  64     7173   5764   5592    974   1604     -3       C  
ATOM     84  C   GLU A  64     -24.493 -17.543  23.959  1.00 46.89           C  
ANISOU   84  C   GLU A  64     6773   5684   5358    970   1567    275       C  
ATOM     85  O   GLU A  64     -25.533 -17.753  23.346  1.00 46.85           O  
ANISOU   85  O   GLU A  64     6585   5622   5592   1007   1567    509       O  
ATOM     86  CB  GLU A  64     -24.236 -15.295  25.065  1.00 55.54           C  
ANISOU   86  CB  GLU A  64     8102   6622   6380   1127   1897   -189       C  
ATOM     87  CG  GLU A  64     -25.744 -15.157  25.157  1.00 60.78           C  
ANISOU   87  CG  GLU A  64     8582   7250   7263   1302   2104     15       C  
ATOM     88  CD  GLU A  64     -26.220 -14.037  26.104  1.00 67.03           C  
ANISOU   88  CD  GLU A  64     9455   7973   8040   1484   2420   -184       C  
ATOM     89  OE1 GLU A  64     -25.426 -13.572  26.970  1.00 67.66           O  
ANISOU   89  OE1 GLU A  64     9745   8095   7868   1465   2489   -495       O  
ATOM     90  OE2 GLU A  64     -27.407 -13.643  25.965  1.00 68.64           O  
ANISOU   90  OE2 GLU A  64     9504   8088   8486   1648   2597    -24       O  
ATOM     91  N   LEU A  65     -23.902 -18.474  24.696  1.00 49.37           N  
ANISOU   91  N   LEU A  65     7147   6198   5413    916   1527    260       N  
ATOM     92  CA  LEU A  65     -24.374 -19.851  24.738  1.00 49.62           C  
ANISOU   92  CA  LEU A  65     7051   6355   5448    883   1474    522       C  
ATOM     93  C   LEU A  65     -25.286 -20.146  25.926  1.00 57.06           C  
ANISOU   93  C   LEU A  65     7908   7454   6319   1009   1719    625       C  
ATOM     94  O   LEU A  65     -25.893 -21.221  25.968  1.00 58.67           O  
ANISOU   94  O   LEU A  65     7974   7735   6583    986   1710    877       O  
ATOM     95  CB  LEU A  65     -23.180 -20.798  24.768  1.00 44.95           C  
ANISOU   95  CB  LEU A  65     6564   5877   4637    764   1288    496       C  
ATOM     96  CG  LEU A  65     -22.218 -20.704  23.577  1.00 43.87           C  
ANISOU   96  CG  LEU A  65     6500   5617   4552    641   1047    425       C  
ATOM     97  CD1 LEU A  65     -20.869 -21.280  23.933  1.00 43.19           C  
ANISOU   97  CD1 LEU A  65     6542   5671   4199    569    929    325       C  
ATOM     98  CD2 LEU A  65     -22.791 -21.461  22.376  1.00 41.18           C  
ANISOU   98  CD2 LEU A  65     6033   5172   4442    570    891    656       C  
ATOM     99  N   GLN A  66     -25.408 -19.242  26.888  1.00 62.75           N  
ANISOU   99  N   GLN A  66     8708   8219   6915   1137   1946    439       N  
ATOM    100  CA  GLN A  66     -26.259 -19.535  28.038  1.00 68.55           C  
ANISOU  100  CA  GLN A  66     9366   9127   7553   1271   2200    543       C  
ATOM    101  C   GLN A  66     -27.737 -19.339  27.737  1.00 67.69           C  
ANISOU  101  C   GLN A  66     9030   8933   7755   1380   2355    766       C  
ATOM    102  O   GLN A  66     -28.121 -18.333  27.158  1.00 66.59           O  
ANISOU  102  O   GLN A  66     8863   8610   7829   1444   2397    706       O  
ATOM    103  CB  GLN A  66     -25.855 -18.676  29.224  1.00 76.79           C  
ANISOU  103  CB  GLN A  66    10591  10272   8314   1375   2396    243       C  
ATOM    104  CG  GLN A  66     -25.678 -17.206  28.911  1.00 82.28           C  
ANISOU  104  CG  GLN A  66    11402  10750   9112   1415   2451    -31       C  
ATOM    105  CD  GLN A  66     -24.906 -16.504  30.010  1.00 89.14           C  
ANISOU  105  CD  GLN A  66    12500  11721   9650   1444   2560   -388       C  
ATOM    106  OE1 GLN A  66     -23.871 -17.006  30.465  1.00 90.92           O  
ANISOU  106  OE1 GLN A  66    12836  12129   9579   1340   2424   -488       O  
ATOM    107  NE2 GLN A  66     -25.409 -15.354  30.464  1.00 92.87           N  
ANISOU  107  NE2 GLN A  66    13042  12082  10161   1587   2806   -582       N  
ATOM    108  N   ASP A  72     -36.025 -11.104  30.109  1.00 87.27           N  
ANISOU  108  N   ASP A  72    10820  10634  11704   3442   4971    793       N  
ATOM    109  CA  ASP A  72     -34.792 -10.613  29.485  1.00 82.69           C  
ANISOU  109  CA  ASP A  72    10510   9832  11074   3258   4709    511       C  
ATOM    110  C   ASP A  72     -34.710 -10.984  27.991  1.00 77.31           C  
ANISOU  110  C   ASP A  72     9652   9059  10663   3073   4338    770       C  
ATOM    111  O   ASP A  72     -35.140 -12.071  27.591  1.00 74.90           O  
ANISOU  111  O   ASP A  72     9098   8938  10423   2956   4164   1088       O  
ATOM    112  CB  ASP A  72     -33.577 -11.150  30.241  1.00 80.95           C  
ANISOU  112  CB  ASP A  72    10569   9774  10412   3063   4582    220       C  
ATOM    113  N   CYS A  73     -34.186 -10.069  27.169  1.00 75.51           N  
ANISOU  113  N   CYS A  73     9553   8543  10593   3046   4228    637       N  
ATOM    114  CA  CYS A  73     -34.088 -10.294  25.731  1.00 73.73           C  
ANISOU  114  CA  CYS A  73     9183   8232  10600   2893   3895    866       C  
ATOM    115  C   CYS A  73     -32.823 -11.089  25.405  1.00 71.05           C  
ANISOU  115  C   CYS A  73     9006   7971  10018   2583   3543    743       C  
ATOM    116  O   CYS A  73     -31.856 -11.090  26.171  1.00 69.83           O  
ANISOU  116  O   CYS A  73     9118   7855   9557   2498   3553    428       O  
ATOM    117  CB  CYS A  73     -34.088  -8.968  24.959  1.00 73.47           C  
ANISOU  117  CB  CYS A  73     9206   7861  10847   3013   3944    819       C  
ATOM    118  SG  CYS A  73     -32.725  -7.809  25.388  1.00 75.54           S  
ANISOU  118  SG  CYS A  73     9925   7839  10939   2965   4015    293       S  
ATOM    119  N   ARG A  74     -32.826 -11.737  24.234  1.00 70.68           N  
ANISOU  119  N   ARG A  74     8795   7950  10108   2420   3229    991       N  
ATOM    120  CA  ARG A  74     -31.838 -12.757  23.885  1.00 68.71           C  
ANISOU  120  CA  ARG A  74     8636   7818   9653   2145   2904    954       C  
ATOM    121  C   ARG A  74     -30.904 -12.310  22.754  1.00 68.41           C  
ANISOU  121  C   ARG A  74     8728   7590   9674   2005   2649    866       C  
ATOM    122  O   ARG A  74     -31.236 -11.431  21.946  1.00 67.69           O  
ANISOU  122  O   ARG A  74     8575   7303   9840   2097   2661    952       O  
ATOM    123  CB  ARG A  74     -32.545 -14.057  23.492  1.00 69.00           C  
ANISOU  123  CB  ARG A  74     8398   8057   9762   2043   2742   1295       C  
ATOM    124  CG  ARG A  74     -33.606 -14.512  24.500  1.00 73.70           C  
ANISOU  124  CG  ARG A  74     8807   8840  10354   2181   3002   1454       C  
ATOM    125  CD  ARG A  74     -33.987 -15.960  24.296  1.00 74.74           C  
ANISOU  125  CD  ARG A  74     8734   9171  10492   2013   2821   1726       C  
ATOM    126  NE  ARG A  74     -33.791 -16.377  22.910  1.00 74.70           N  
ANISOU  126  NE  ARG A  74     8651   9103  10627   1823   2468   1859       N  
ATOM    127  CZ  ARG A  74     -34.096 -17.585  22.453  1.00 75.43           C  
ANISOU  127  CZ  ARG A  74     8576   9315  10770   1644   2258   2081       C  
ATOM    128  NH1 ARG A  74     -34.614 -18.486  23.278  1.00 76.79           N  
ANISOU  128  NH1 ARG A  74     8628   9661  10888   1630   2373   2219       N  
ATOM    129  NH2 ARG A  74     -33.894 -17.892  21.176  1.00 74.57           N  
ANISOU  129  NH2 ARG A  74     8424   9147  10764   1479   1943   2164       N  
ATOM    130  N   CYS A  75     -29.712 -12.928  22.711  1.00 66.76           N  
ANISOU  130  N   CYS A  75     8693   7451   9220   1791   2429    711       N  
ATOM    131  CA  CYS A  75     -28.673 -12.585  21.746  1.00 65.91           C  
ANISOU  131  CA  CYS A  75     8725   7197   9120   1645   2199    609       C  
ATOM    132  C   CYS A  75     -28.072 -13.830  21.106  1.00 62.78           C  
ANISOU  132  C   CYS A  75     8306   6947   8600   1425   1883    709       C  
ATOM    133  O   CYS A  75     -27.005 -13.746  20.495  1.00 58.75           O  
ANISOU  133  O   CYS A  75     7937   6369   8014   1287   1696    594       O  
ATOM    134  CB  CYS A  75     -27.563 -11.746  22.399  1.00 68.79           C  
ANISOU  134  CB  CYS A  75     9383   7446   9307   1618   2288    230       C  
ATOM    135  SG  CYS A  75     -28.164 -10.181  23.153  1.00 76.49           S  
ANISOU  135  SG  CYS A  75    10447   8188  10430   1874   2678     44       S  
ATOM    136  N   ASP A  76     -28.714 -14.980  21.271  1.00 63.80           N  
ANISOU  136  N   ASP A  76     8268   7265   8710   1391   1836    915       N  
ATOM    137  CA  ASP A  76     -28.328 -16.201  20.601  1.00 61.77           C  
ANISOU  137  CA  ASP A  76     7975   7114   8383   1198   1554   1033       C  
ATOM    138  C   ASP A  76     -28.854 -16.175  19.178  1.00 62.50           C  
ANISOU  138  C   ASP A  76     7901   7132   8715   1159   1363   1258       C  
ATOM    139  O   ASP A  76     -29.646 -15.318  18.785  1.00 62.90           O  
ANISOU  139  O   ASP A  76     7824   7081   8995   1294   1456   1373       O  
ATOM    140  CB  ASP A  76     -28.871 -17.422  21.337  1.00 61.26           C  
ANISOU  140  CB  ASP A  76     7794   7249   8235   1171   1594   1176       C  
ATOM    141  CG  ASP A  76     -30.392 -17.453  21.351  1.00 62.84           C  
ANISOU  141  CG  ASP A  76     7710   7488   8678   1286   1725   1444       C  
ATOM    142  OD1 ASP A  76     -30.987 -16.603  22.053  1.00 64.50           O  
ANISOU  142  OD1 ASP A  76     7886   7670   8950   1480   2001   1410       O  
ATOM    143  OD2 ASP A  76     -30.983 -18.295  20.642  1.00 61.96           O  
ANISOU  143  OD2 ASP A  76     7408   7433   8702   1181   1554   1682       O  
ATOM    144  N   ASN A  77     -28.421 -17.149  18.416  1.00 62.40           N  
ANISOU  144  N   ASN A  77     7890   7179   8640    982   1098   1325       N  
ATOM    145  CA  ASN A  77     -28.645 -17.170  16.989  1.00 66.45           C  
ANISOU  145  CA  ASN A  77     8301   7642   9304    913    872   1487       C  
ATOM    146  C   ASN A  77     -29.981 -17.780  16.610  1.00 70.15           C  
ANISOU  146  C   ASN A  77     8484   8205   9965    906    814   1775       C  
ATOM    147  O   ASN A  77     -30.160 -18.180  15.455  1.00 71.55           O  
ANISOU  147  O   ASN A  77     8572   8400  10215    797    573   1910       O  
ATOM    148  CB  ASN A  77     -27.491 -17.936  16.329  1.00 66.04           C  
ANISOU  148  CB  ASN A  77     8408   7611   9072    727    620   1396       C  
ATOM    149  CG  ASN A  77     -27.213 -19.264  17.027  1.00 65.60           C  
ANISOU  149  CG  ASN A  77     8393   7687   8844    624    586   1374       C  
ATOM    150  OD1 ASN A  77     -26.613 -19.324  18.123  1.00 61.94           O  
ANISOU  150  OD1 ASN A  77     8061   7272   8200    651    720   1215       O  
ATOM    151  ND2 ASN A  77     -27.700 -20.339  16.409  1.00 67.69           N  
ANISOU  151  ND2 ASN A  77     8539   8012   9170    504    408   1543       N  
ATOM    152  N   LEU A  78     -30.904 -17.909  17.556  1.00 73.45           N  
ANISOU  152  N   LEU A  78     8752   8702  10455   1007   1023   1870       N  
ATOM    153  CA  LEU A  78     -32.287 -18.236  17.248  1.00 75.12           C  
ANISOU  153  CA  LEU A  78     8646   8998  10897   1026   1008   2162       C  
ATOM    154  C   LEU A  78     -33.252 -17.178  17.743  1.00 75.82           C  
ANISOU  154  C   LEU A  78     8577   9056  11177   1269   1289   2255       C  
ATOM    155  O   LEU A  78     -34.467 -17.346  17.586  1.00 77.82           O  
ANISOU  155  O   LEU A  78     8532   9397  11640   1314   1312   2517       O  
ATOM    156  CB  LEU A  78     -32.684 -19.591  17.845  1.00 78.32           C  
ANISOU  156  CB  LEU A  78     8952   9549  11259    905    995   2267       C  
ATOM    157  CG  LEU A  78     -32.735 -20.763  16.854  1.00 79.57           C  
ANISOU  157  CG  LEU A  78     9037   9752  11443    667    675   2384       C  
ATOM    158  CD1 LEU A  78     -32.975 -20.305  15.399  1.00 79.82           C  
ANISOU  158  CD1 LEU A  78     8975   9744  11610    631    444   2481       C  
ATOM    159  CD2 LEU A  78     -31.483 -21.622  16.958  1.00 77.85           C  
ANISOU  159  CD2 LEU A  78     9085   9517  10978    519    552   2196       C  
ATOM    160  N   CYS A  79     -32.755 -16.101  18.346  1.00 73.68           N  
ANISOU  160  N   CYS A  79     8492   8658  10845   1426   1508   2046       N  
ATOM    161  CA  CYS A  79     -33.663 -15.089  18.857  1.00 74.16           C  
ANISOU  161  CA  CYS A  79     8425   8663  11089   1681   1806   2116       C  
ATOM    162  C   CYS A  79     -34.534 -14.531  17.749  1.00 75.62           C  
ANISOU  162  C   CYS A  79     8364   8803  11564   1764   1722   2381       C  
ATOM    163  O   CYS A  79     -35.692 -14.166  17.990  1.00 77.86           O  
ANISOU  163  O   CYS A  79     8398   9125  12059   1946   1908   2584       O  
ATOM    164  CB  CYS A  79     -32.870 -13.970  19.527  1.00 71.12           C  
ANISOU  164  CB  CYS A  79     8321   8105  10596   1809   2023   1808       C  
ATOM    165  SG  CYS A  79     -31.892 -12.964  18.394  1.00 67.41           S  
ANISOU  165  SG  CYS A  79     8043   7399  10172   1770   1863   1683       S  
ATOM    166  N   LYS A  80     -33.994 -14.457  16.531  1.00 75.25           N  
ANISOU  166  N   LYS A  80     8374   8695  11521   1644   1448   2398       N  
ATOM    167  CA  LYS A  80     -34.732 -13.833  15.443  1.00 79.60           C  
ANISOU  167  CA  LYS A  80     8710   9216  12320   1735   1359   2654       C  
ATOM    168  C   LYS A  80     -35.935 -14.673  15.060  1.00 82.12           C  
ANISOU  168  C   LYS A  80     8670   9744  12787   1672   1224   2969       C  
ATOM    169  O   LYS A  80     -37.009 -14.141  14.778  1.00 84.71           O  
ANISOU  169  O   LYS A  80     8719  10106  13362   1834   1297   3226       O  
ATOM    170  CB  LYS A  80     -33.802 -13.614  14.249  1.00 78.04           C  
ANISOU  170  CB  LYS A  80     8673   8930  12048   1613   1099   2596       C  
ATOM    171  CG  LYS A  80     -33.490 -12.141  14.006  1.00 79.79           C  
ANISOU  171  CG  LYS A  80     9013   8918  12386   1798   1250   2544       C  
ATOM    172  CD  LYS A  80     -32.464 -11.942  12.901  1.00 78.32           C  
ANISOU  172  CD  LYS A  80     9001   8652  12105   1670   1016   2485       C  
ATOM    173  CE  LYS A  80     -32.637 -10.597  12.200  1.00 80.28           C  
ANISOU  173  CE  LYS A  80     9221   8715  12567   1855   1096   2620       C  
ATOM    174  NZ  LYS A  80     -32.672  -9.499  13.185  1.00 81.71           N  
ANISOU  174  NZ  LYS A  80     9510   8670  12864   2067   1457   2473       N  
ATOM    175  N   SER A  81     -35.773 -15.994  15.076  1.00 81.68           N  
ANISOU  175  N   SER A  81     8611   9828  12596   1435   1032   2957       N  
ATOM    176  CA  SER A  81     -36.873 -16.884  14.742  1.00 83.00           C  
ANISOU  176  CA  SER A  81     8446  10185  12906   1326    887   3234       C  
ATOM    177  C   SER A  81     -37.958 -16.887  15.803  1.00 84.68           C  
ANISOU  177  C   SER A  81     8416  10488  13269   1479   1179   3385       C  
ATOM    178  O   SER A  81     -39.100 -17.235  15.501  1.00 88.56           O  
ANISOU  178  O   SER A  81     8556  11129  13965   1458   1115   3674       O  
ATOM    179  CB  SER A  81     -36.331 -18.290  14.521  1.00 82.26           C  
ANISOU  179  CB  SER A  81     8453  10166  12636   1029    627   3152       C  
ATOM    180  OG  SER A  81     -35.286 -18.246  13.577  1.00 79.91           O  
ANISOU  180  OG  SER A  81     8389   9788  12185    915    391   3002       O  
ATOM    181  N   TYR A  82     -37.636 -16.510  17.033  1.00 82.75           N  
ANISOU  181  N   TYR A  82     8343  10176  12922   1628   1496   3202       N  
ATOM    182  CA  TYR A  82     -38.630 -16.362  18.085  1.00 83.16           C  
ANISOU  182  CA  TYR A  82     8188  10311  13096   1819   1825   3332       C  
ATOM    183  C   TYR A  82     -39.022 -14.909  18.307  1.00 83.79           C  
ANISOU  183  C   TYR A  82     8242  10261  13332   2145   2118   3340       C  
ATOM    184  O   TYR A  82     -39.876 -14.634  19.155  1.00 84.10           O  
ANISOU  184  O   TYR A  82     8111  10358  13484   2350   2429   3446       O  
ATOM    185  CB  TYR A  82     -38.103 -16.956  19.394  1.00 80.76           C  
ANISOU  185  CB  TYR A  82     8086  10049  12552   1787   2010   3134       C  
ATOM    186  CG  TYR A  82     -37.915 -18.463  19.399  1.00 78.59           C  
ANISOU  186  CG  TYR A  82     7796   9899  12164   1504   1796   3178       C  
ATOM    187  CD1 TYR A  82     -38.930 -19.313  19.855  1.00 79.16           C  
ANISOU  187  CD1 TYR A  82     7577  10140  12361   1454   1866   3430       C  
ATOM    188  CD2 TYR A  82     -36.707 -19.038  18.985  1.00 75.73           C  
ANISOU  188  CD2 TYR A  82     7714   9475  11585   1295   1546   2974       C  
ATOM    189  CE1 TYR A  82     -38.762 -20.688  19.880  1.00 77.83           C  
ANISOU  189  CE1 TYR A  82     7407  10048  12117   1194   1689   3474       C  
ATOM    190  CE2 TYR A  82     -36.522 -20.426  19.005  1.00 74.81           C  
ANISOU  190  CE2 TYR A  82     7601   9441  11382   1054   1372   3012       C  
ATOM    191  CZ  TYR A  82     -37.563 -21.241  19.457  1.00 76.63           C  
ANISOU  191  CZ  TYR A  82     7551   9812  11754   1001   1445   3262       C  
ATOM    192  OH  TYR A  82     -37.394 -22.607  19.487  1.00 77.24           O  
ANISOU  192  OH  TYR A  82     7640   9934  11773    760   1288   3306       O  
ATOM    193  N   SER A  83     -38.401 -13.978  17.575  1.00 83.34           N  
ANISOU  193  N   SER A  83     8357  10019  13289   2202   2043   3233       N  
ATOM    194  CA  SER A  83     -38.640 -12.544  17.743  1.00 86.65           C  
ANISOU  194  CA  SER A  83     8803  10254  13868   2508   2324   3214       C  
ATOM    195  C   SER A  83     -38.361 -12.095  19.178  1.00 87.26           C  
ANISOU  195  C   SER A  83     9100  10244  13811   2673   2703   2944       C  
ATOM    196  O   SER A  83     -39.167 -11.410  19.805  1.00 89.78           O  
ANISOU  196  O   SER A  83     9296  10531  14284   2946   3034   3018       O  
ATOM    197  CB  SER A  83     -40.063 -12.172  17.319  1.00 90.93           C  
ANISOU  197  CB  SER A  83     8925  10884  14740   2699   2394   3601       C  
ATOM    198  OG  SER A  83     -40.268 -12.485  15.957  1.00 90.59           O  
ANISOU  198  OG  SER A  83     8697  10931  14792   2547   2027   3830       O  
ATOM    199  N   SER A  84     -37.185 -12.467  19.688  1.00 84.73           N  
ANISOU  199  N   SER A  84     9111   9892  13190   2513   2654   2623       N  
ATOM    200  CA  SER A  84     -36.803 -12.153  21.060  1.00 83.77           C  
ANISOU  200  CA  SER A  84     9223   9730  12877   2628   2967   2337       C  
ATOM    201  C   SER A  84     -35.498 -11.375  21.172  1.00 79.50           C  
ANISOU  201  C   SER A  84     9075   8967  12164   2599   2976   1962       C  
ATOM    202  O   SER A  84     -34.959 -11.241  22.279  1.00 79.72           O  
ANISOU  202  O   SER A  84     9338   8987  11966   2630   3167   1674       O  
ATOM    203  CB  SER A  84     -36.702 -13.437  21.874  1.00 83.49           C  
ANISOU  203  CB  SER A  84     9186   9925  12610   2471   2943   2318       C  
ATOM    204  OG  SER A  84     -37.963 -13.721  22.417  1.00 86.56           O  
ANISOU  204  OG  SER A  84     9270  10475  13143   2611   3154   2574       O  
ATOM    205  N   CYS A  85     -34.980 -10.847  20.075  1.00 76.43           N  
ANISOU  205  N   CYS A  85     8757   8411  11871   2537   2777   1961       N  
ATOM    206  CA  CYS A  85     -33.672 -10.216  20.138  1.00 74.18           C  
ANISOU  206  CA  CYS A  85     8828   7929  11428   2462   2756   1619       C  
ATOM    207  C   CYS A  85     -33.738  -8.879  20.866  1.00 73.57           C  
ANISOU  207  C   CYS A  85     8908   7613  11432   2704   3113   1412       C  
ATOM    208  O   CYS A  85     -34.759  -8.193  20.870  1.00 76.47           O  
ANISOU  208  O   CYS A  85     9103   7896  12057   2956   3339   1584       O  
ATOM    209  CB  CYS A  85     -33.104 -10.022  18.737  1.00 74.16           C  
ANISOU  209  CB  CYS A  85     8849   7819  11509   2330   2460   1701       C  
ATOM    210  SG  CYS A  85     -33.166 -11.500  17.665  1.00 72.65           S  
ANISOU  210  SG  CYS A  85     8464   7879  11260   2066   2036   1956       S  
ATOM    211  N   CYS A  86     -32.643  -8.533  21.526  1.00 71.45           N  
ANISOU  211  N   CYS A  86     8968   7240  10938   2626   3170   1032       N  
ATOM    212  CA  CYS A  86     -32.476  -7.166  21.979  1.00 74.67           C  
ANISOU  212  CA  CYS A  86     9582   7355  11436   2800   3451    786       C  
ATOM    213  C   CYS A  86     -32.460  -6.242  20.770  1.00 74.41           C  
ANISOU  213  C   CYS A  86     9519   7051  11701   2852   3379    929       C  
ATOM    214  O   CYS A  86     -32.121  -6.654  19.654  1.00 72.41           O  
ANISOU  214  O   CYS A  86     9188   6846  11478   2687   3068   1104       O  
ATOM    215  CB  CYS A  86     -31.192  -7.031  22.790  1.00 76.22           C  
ANISOU  215  CB  CYS A  86    10129   7509  11322   2646   3456    347       C  
ATOM    216  SG  CYS A  86     -31.101  -8.240  24.149  1.00 79.01           S  
ANISOU  216  SG  CYS A  86    10515   8229  11277   2570   3497    220       S  
ATOM    217  N   HIS A  87     -32.847  -4.981  20.992  1.00 74.68           N  
ANISOU  217  N   HIS A  87     9619   6797  11958   3095   3681    863       N  
ATOM    218  CA  HIS A  87     -33.102  -4.086  19.867  1.00 74.45           C  
ANISOU  218  CA  HIS A  87     9505   6518  12264   3208   3661   1087       C  
ATOM    219  C   HIS A  87     -31.871  -3.881  19.000  1.00 71.15           C  
ANISOU  219  C   HIS A  87     9273   5962  11800   2972   3398    989       C  
ATOM    220  O   HIS A  87     -32.000  -3.584  17.808  1.00 70.23           O  
ANISOU  220  O   HIS A  87     9032   5762  11890   2988   3254   1263       O  
ATOM    221  CB  HIS A  87     -33.596  -2.733  20.368  1.00 77.67           C  
ANISOU  221  CB  HIS A  87    10004   6637  12871   3458   4015    980       C  
ATOM    222  CG  HIS A  87     -32.566  -1.976  21.137  1.00 79.84           C  
ANISOU  222  CG  HIS A  87    10663   6687  12986   3354   4127    505       C  
ATOM    223  ND1 HIS A  87     -32.230  -2.292  22.435  1.00 81.09           N  
ANISOU  223  ND1 HIS A  87    11009   6948  12856   3321   4269    156       N  
ATOM    224  CD2 HIS A  87     -31.795  -0.917  20.794  1.00 82.47           C  
ANISOU  224  CD2 HIS A  87    11216   6724  13397   3254   4098    326       C  
ATOM    225  CE1 HIS A  87     -31.294  -1.460  22.858  1.00 83.44           C  
ANISOU  225  CE1 HIS A  87    11622   7027  13055   3195   4301   -230       C  
ATOM    226  NE2 HIS A  87     -31.017  -0.612  21.884  1.00 84.22           N  
ANISOU  226  NE2 HIS A  87    11741   6868  13389   3151   4207   -134       N  
ATOM    227  N   ASP A  88     -30.677  -4.012  19.574  1.00 69.64           N  
ANISOU  227  N   ASP A  88     9365   5759  11338   2759   3337    616       N  
ATOM    228  CA  ASP A  88     -29.442  -3.751  18.851  1.00 69.58           C  
ANISOU  228  CA  ASP A  88     9536   5615  11287   2536   3122    502       C  
ATOM    229  C   ASP A  88     -28.773  -5.026  18.370  1.00 67.47           C  
ANISOU  229  C   ASP A  88     9222   5649  10765   2266   2760    562       C  
ATOM    230  O   ASP A  88     -27.572  -5.016  18.060  1.00 65.99           O  
ANISOU  230  O   ASP A  88     9208   5416  10450   2052   2589    397       O  
ATOM    231  CB  ASP A  88     -28.479  -2.943  19.724  1.00 71.66           C  
ANISOU  231  CB  ASP A  88    10138   5643  11447   2465   3284     47       C  
ATOM    232  CG  ASP A  88     -28.200  -3.601  21.077  1.00 72.34           C  
ANISOU  232  CG  ASP A  88    10345   5956  11184   2390   3345   -260       C  
ATOM    233  OD1 ASP A  88     -28.417  -4.820  21.237  1.00 70.96           O  
ANISOU  233  OD1 ASP A  88    10026   6125  10811   2321   3198   -133       O  
ATOM    234  OD2 ASP A  88     -27.730  -2.888  21.986  1.00 73.71           O  
ANISOU  234  OD2 ASP A  88    10769   5962  11275   2390   3537   -635       O  
ATOM    235  N   PHE A  89     -29.516  -6.132  18.330  1.00 66.64           N  
ANISOU  235  N   PHE A  89     8885   5844  10590   2270   2651    790       N  
ATOM    236  CA  PHE A  89     -28.906  -7.379  17.893  1.00 63.02           C  
ANISOU  236  CA  PHE A  89     8399   5645   9902   2024   2325    837       C  
ATOM    237  C   PHE A  89     -28.349  -7.227  16.485  1.00 62.15           C  
ANISOU  237  C   PHE A  89     8281   5460   9874   1908   2075    988       C  
ATOM    238  O   PHE A  89     -27.181  -7.549  16.231  1.00 60.82           O  
ANISOU  238  O   PHE A  89     8268   5323   9520   1698   1890    839       O  
ATOM    239  CB  PHE A  89     -29.914  -8.531  17.970  1.00 62.46           C  
ANISOU  239  CB  PHE A  89     8064   5864   9804   2046   2256   1088       C  
ATOM    240  CG  PHE A  89     -29.372  -9.841  17.463  1.00 60.09           C  
ANISOU  240  CG  PHE A  89     7737   5796   9300   1804   1930   1148       C  
ATOM    241  CD1 PHE A  89     -28.523 -10.603  18.235  1.00 58.73           C  
ANISOU  241  CD1 PHE A  89     7724   5759   8831   1649   1876    917       C  
ATOM    242  CD2 PHE A  89     -29.704 -10.295  16.205  1.00 60.31           C  
ANISOU  242  CD2 PHE A  89     7584   5904   9426   1739   1681   1432       C  
ATOM    243  CE1 PHE A  89     -28.011 -11.823  17.754  1.00 57.58           C  
ANISOU  243  CE1 PHE A  89     7561   5801   8515   1444   1593    977       C  
ATOM    244  CE2 PHE A  89     -29.211 -11.481  15.718  1.00 58.20           C  
ANISOU  244  CE2 PHE A  89     7314   5822   8978   1525   1398   1464       C  
ATOM    245  CZ  PHE A  89     -28.359 -12.265  16.499  1.00 56.91           C  
ANISOU  245  CZ  PHE A  89     7314   5768   8541   1381   1361   1238       C  
ATOM    246  N   ASP A  90     -29.159  -6.688  15.572  1.00 63.78           N  
ANISOU  246  N   ASP A  90     8306   5573  10353   2057   2082   1291       N  
ATOM    247  CA  ASP A  90     -28.720  -6.500  14.196  1.00 65.28           C  
ANISOU  247  CA  ASP A  90     8478   5713  10614   1973   1859   1470       C  
ATOM    248  C   ASP A  90     -27.469  -5.640  14.129  1.00 65.89           C  
ANISOU  248  C   ASP A  90     8825   5538  10674   1877   1895   1229       C  
ATOM    249  O   ASP A  90     -26.486  -6.015  13.479  1.00 62.54           O  
ANISOU  249  O   ASP A  90     8485   5175  10101   1678   1671   1197       O  
ATOM    250  CB  ASP A  90     -29.845  -5.882  13.369  1.00 68.66           C  
ANISOU  250  CB  ASP A  90     8669   6072  11347   2189   1905   1838       C  
ATOM    251  CG  ASP A  90     -30.787  -6.932  12.811  1.00 70.31           C  
ANISOU  251  CG  ASP A  90     8582   6590  11542   2173   1697   2143       C  
ATOM    252  OD1 ASP A  90     -30.728  -8.080  13.288  1.00 69.74           O  
ANISOU  252  OD1 ASP A  90     8492   6744  11261   2028   1589   2054       O  
ATOM    253  OD2 ASP A  90     -31.585  -6.622  11.901  1.00 73.10           O  
ANISOU  253  OD2 ASP A  90     8715   6963  12094   2296   1637   2477       O  
ATOM    254  N   GLU A  91     -27.470  -4.516  14.850  1.00 68.79           N  
ANISOU  254  N   GLU A  91     9332   5619  11187   2007   2185   1042       N  
ATOM    255  CA  GLU A  91     -26.386  -3.541  14.771  1.00 68.21           C  
ANISOU  255  CA  GLU A  91     9500   5255  11162   1916   2244    826       C  
ATOM    256  C   GLU A  91     -25.077  -4.068  15.366  1.00 65.17           C  
ANISOU  256  C   GLU A  91     9319   4975  10466   1654   2125    483       C  
ATOM    257  O   GLU A  91     -23.995  -3.739  14.865  1.00 64.96           O  
ANISOU  257  O   GLU A  91     9421   4843  10418   1489   2020    399       O  
ATOM    258  CB  GLU A  91     -26.819  -2.252  15.476  1.00 72.24           C  
ANISOU  258  CB  GLU A  91    10115   5418  11915   2124   2599    690       C  
ATOM    259  N   LEU A  92     -25.145  -4.866  16.441  1.00 62.09           N  
ANISOU  259  N   LEU A  92     8950   4803   9840   1619   2147    299       N  
ATOM    260  CA  LEU A  92     -23.956  -5.317  17.165  1.00 59.86           C  
ANISOU  260  CA  LEU A  92     8852   4636   9257   1400   2060    -28       C  
ATOM    261  C   LEU A  92     -23.481  -6.720  16.772  1.00 58.62           C  
ANISOU  261  C   LEU A  92     8618   4807   8849   1227   1765     68       C  
ATOM    262  O   LEU A  92     -22.271  -6.962  16.745  1.00 57.41           O  
ANISOU  262  O   LEU A  92     8588   4710   8514   1030   1621    -97       O  
ATOM    263  CB  LEU A  92     -24.211  -5.304  18.676  1.00 60.07           C  
ANISOU  263  CB  LEU A  92     8976   4706   9140   1471   2277   -308       C  
ATOM    264  CG  LEU A  92     -24.404  -3.953  19.367  1.00 64.01           C  
ANISOU  264  CG  LEU A  92     9636   4877   9810   1606   2589   -542       C  
ATOM    265  CD1 LEU A  92     -24.750  -4.124  20.863  1.00 65.52           C  
ANISOU  265  CD1 LEU A  92     9910   5186   9798   1689   2795   -802       C  
ATOM    266  CD2 LEU A  92     -23.155  -3.116  19.170  1.00 63.25           C  
ANISOU  266  CD2 LEU A  92     9751   4540   9741   1420   2549   -781       C  
ATOM    267  N   CYS A  93     -24.403  -7.640  16.461  1.00 58.34           N  
ANISOU  267  N   CYS A  93     8377   4980   8811   1296   1677    331       N  
ATOM    268  CA  CYS A  93     -24.089  -9.041  16.210  1.00 55.88           C  
ANISOU  268  CA  CYS A  93     8002   4958   8273   1148   1428    407       C  
ATOM    269  C   CYS A  93     -24.074  -9.420  14.733  1.00 53.88           C  
ANISOU  269  C   CYS A  93     7635   4754   8082   1087   1187    678       C  
ATOM    270  O   CYS A  93     -23.483 -10.447  14.377  1.00 52.83           O  
ANISOU  270  O   CYS A  93     7510   4807   7757    936    971    689       O  
ATOM    271  CB  CYS A  93     -25.091  -9.937  16.943  1.00 58.09           C  
ANISOU  271  CB  CYS A  93     8140   5444   8489   1230   1487    494       C  
ATOM    272  SG  CYS A  93     -25.312  -9.517  18.701  1.00 63.31           S  
ANISOU  272  SG  CYS A  93     8917   6087   9051   1345   1802    209       S  
ATOM    273  N   LEU A  94     -24.687  -8.632  13.863  1.00 54.33           N  
ANISOU  273  N   LEU A  94     7594   4660   8391   1207   1219    895       N  
ATOM    274  CA  LEU A  94     -24.680  -8.972  12.450  1.00 52.92           C  
ANISOU  274  CA  LEU A  94     7314   4559   8237   1152    985   1151       C  
ATOM    275  C   LEU A  94     -23.983  -7.877  11.647  1.00 53.47           C  
ANISOU  275  C   LEU A  94     7482   4405   8430   1143    998   1174       C  
ATOM    276  O   LEU A  94     -24.554  -7.335  10.698  1.00 55.86           O  
ANISOU  276  O   LEU A  94     7671   4632   8923   1251    981   1439       O  
ATOM    277  CB  LEU A  94     -26.099  -9.203  11.949  1.00 52.41           C  
ANISOU  277  CB  LEU A  94     6994   4587   8334   1290    955   1467       C  
ATOM    278  CG  LEU A  94     -26.917 -10.222  12.730  1.00 52.80           C  
ANISOU  278  CG  LEU A  94     6913   4840   8310   1301    966   1484       C  
ATOM    279  CD1 LEU A  94     -28.280 -10.365  12.106  1.00 53.62           C  
ANISOU  279  CD1 LEU A  94     6737   5037   8600   1417    915   1817       C  
ATOM    280  CD2 LEU A  94     -26.217 -11.586  12.798  1.00 50.24           C  
ANISOU  280  CD2 LEU A  94     6654   4725   7708   1096    758   1381       C  
ATOM    281  N   LYS A  95     -22.747  -7.553  12.023  1.00 52.47           N  
ANISOU  281  N   LYS A  95     7555   4182   8200   1011   1025    914       N  
ATOM    282  CA  LYS A  95     -21.941  -6.609  11.251  1.00 53.04           C  
ANISOU  282  CA  LYS A  95     7721   4051   8380    962   1026    936       C  
ATOM    283  C   LYS A  95     -21.630  -7.164   9.868  1.00 49.38           C  
ANISOU  283  C   LYS A  95     7188   3743   7831    886    781   1168       C  
ATOM    284  O   LYS A  95     -21.529  -8.376   9.663  1.00 46.00           O  
ANISOU  284  O   LYS A  95     6716   3571   7189    797    589   1188       O  
ATOM    285  CB  LYS A  95     -20.655  -6.278  11.996  1.00 54.25           C  
ANISOU  285  CB  LYS A  95     8078   4112   8422    802   1082    600       C  
ATOM    286  CG  LYS A  95     -20.908  -5.297  13.146  1.00 59.23           C  
ANISOU  286  CG  LYS A  95     8814   4500   9190    887   1354    366       C  
ATOM    287  CD  LYS A  95     -19.724  -5.181  14.069  1.00 60.45           C  
ANISOU  287  CD  LYS A  95     9154   4638   9176    706   1377     -2       C  
ATOM    288  CE  LYS A  95     -20.121  -4.522  15.361  1.00 64.08           C  
ANISOU  288  CE  LYS A  95     9719   4941   9686    793   1626   -266       C  
ATOM    289  NZ  LYS A  95     -20.955  -3.343  15.075  1.00 66.78           N  
ANISOU  289  NZ  LYS A  95    10047   4956  10369    986   1841   -144       N  
ATOM    290  N   THR A  96     -21.533  -6.260   8.897  1.00 49.51           N  
ANISOU  290  N   THR A  96     7197   3594   8021    934    799   1357       N  
ATOM    291  CA  THR A  96     -21.264  -6.670   7.529  1.00 48.44           C  
ANISOU  291  CA  THR A  96     7002   3610   7793    882    584   1590       C  
ATOM    292  C   THR A  96     -20.256  -5.780   6.822  1.00 49.93           C  
ANISOU  292  C   THR A  96     7294   3625   8053    817    614   1628       C  
ATOM    293  O   THR A  96     -19.886  -6.091   5.684  1.00 49.50           O  
ANISOU  293  O   THR A  96     7212   3707   7890    769    450   1808       O  
ATOM    294  CB  THR A  96     -22.548  -6.686   6.689  1.00 49.62           C  
ANISOU  294  CB  THR A  96     6950   3840   8063   1044    517   1935       C  
ATOM    295  OG1 THR A  96     -23.122  -5.379   6.692  1.00 55.42           O  
ANISOU  295  OG1 THR A  96     7651   4300   9105   1223    728   2069       O  
ATOM    296  CG2 THR A  96     -23.566  -7.707   7.221  1.00 49.66           C  
ANISOU  296  CG2 THR A  96     6817   4055   7998   1079    453   1942       C  
ATOM    297  N   ALA A  97     -19.799  -4.699   7.450  1.00 50.72           N  
ANISOU  297  N   ALA A  97     7513   3431   8325    807    819   1462       N  
ATOM    298  CA  ALA A  97     -19.013  -3.701   6.737  1.00 53.63           C  
ANISOU  298  CA  ALA A  97     7955   3588   8834    759    878   1550       C  
ATOM    299  C   ALA A  97     -17.703  -4.312   6.231  1.00 49.58           C  
ANISOU  299  C   ALA A  97     7503   3254   8081    557    710   1488       C  
ATOM    300  O   ALA A  97     -17.049  -5.080   6.939  1.00 46.98           O  
ANISOU  300  O   ALA A  97     7235   3077   7540    421    641   1233       O  
ATOM    301  CB  ALA A  97     -18.759  -2.486   7.649  1.00 51.87           C  
ANISOU  301  CB  ALA A  97     7865   2994   8848    755   1133   1328       C  
ATOM    302  N   ARG A  98     -17.337  -3.980   4.985  1.00 48.29           N  
ANISOU  302  N   ARG A  98     7314   3089   7945    554    652   1746       N  
ATOM    303  CA  ARG A  98     -16.131  -4.431   4.291  1.00 46.80           C  
ANISOU  303  CA  ARG A  98     7167   3064   7553    397    520   1753       C  
ATOM    304  C   ARG A  98     -16.124  -5.921   3.962  1.00 44.54           C  
ANISOU  304  C   ARG A  98     6835   3145   6943    362    293   1751       C  
ATOM    305  O   ARG A  98     -15.079  -6.451   3.567  1.00 44.53           O  
ANISOU  305  O   ARG A  98     6878   3298   6745    239    195   1704       O  
ATOM    306  CB  ARG A  98     -14.863  -4.108   5.081  1.00 50.22           C  
ANISOU  306  CB  ARG A  98     7720   3379   7981    205    598   1454       C  
ATOM    307  CG  ARG A  98     -14.748  -2.630   5.469  1.00 57.90           C  
ANISOU  307  CG  ARG A  98     8767   3951   9283    198    826   1401       C  
ATOM    308  CD  ARG A  98     -13.695  -1.980   4.635  1.00 64.52           C  
ANISOU  308  CD  ARG A  98     9631   4686  10197     81    849   1531       C  
ATOM    309  NE  ARG A  98     -12.623  -1.389   5.427  1.00 71.93           N  
ANISOU  309  NE  ARG A  98    10672   5440  11219   -125    945   1244       N  
ATOM    310  CZ  ARG A  98     -11.443  -1.030   4.915  1.00 77.70           C  
ANISOU  310  CZ  ARG A  98    11414   6137  11971   -292    944   1287       C  
ATOM    311  NH1 ARG A  98     -10.500  -0.490   5.685  1.00 80.39           N  
ANISOU  311  NH1 ARG A  98    11830   6317  12397   -501   1016   1015       N  
ATOM    312  NH2 ARG A  98     -11.195  -1.224   3.620  1.00 78.51           N  
ANISOU  312  NH2 ARG A  98    11445   6386  11998   -256    868   1606       N  
ATOM    313  N   GLY A  99     -17.238  -6.615   4.107  1.00 43.25           N  
ANISOU  313  N   GLY A  99     6584   3120   6730    463    215   1800       N  
ATOM    314  CA  GLY A  99     -17.254  -7.988   3.629  1.00 41.19           C  
ANISOU  314  CA  GLY A  99     6290   3174   6188    421     -3   1821       C  
ATOM    315  C   GLY A  99     -16.456  -8.946   4.507  1.00 42.76           C  
ANISOU  315  C   GLY A  99     6570   3498   6180    286    -50   1527       C  
ATOM    316  O   GLY A  99     -16.115  -8.645   5.648  1.00 43.16           O  
ANISOU  316  O   GLY A  99     6681   3432   6286    236     70   1296       O  
ATOM    317  N   TRP A 100     -16.143 -10.119   3.938  1.00 37.35           N  
ANISOU  317  N   TRP A 100     5890   3060   5244    234   -229   1540       N  
ATOM    318  CA  TRP A 100     -15.665 -11.242   4.710  1.00 37.66           C  
ANISOU  318  CA  TRP A 100     5979   3243   5086    147   -292   1317       C  
ATOM    319  C   TRP A 100     -14.217 -11.628   4.437  1.00 36.37           C  
ANISOU  319  C   TRP A 100     5898   3182   4739     36   -338   1225       C  
ATOM    320  O   TRP A 100     -13.772 -12.661   4.961  1.00 34.25           O  
ANISOU  320  O   TRP A 100     5667   3054   4294    -19   -402   1072       O  
ATOM    321  CB  TRP A 100     -16.568 -12.459   4.445  1.00 39.37           C  
ANISOU  321  CB  TRP A 100     6135   3646   5179    181   -451   1383       C  
ATOM    322  CG  TRP A 100     -18.041 -12.099   4.505  1.00 40.47           C  
ANISOU  322  CG  TRP A 100     6149   3724   5503    294   -425   1531       C  
ATOM    323  CD1 TRP A 100     -18.879 -11.836   3.460  1.00 43.29           C  
ANISOU  323  CD1 TRP A 100     6406   4116   5926    377   -505   1788       C  
ATOM    324  CD2 TRP A 100     -18.805 -11.917   5.692  1.00 40.86           C  
ANISOU  324  CD2 TRP A 100     6150   3682   5691    347   -301   1441       C  
ATOM    325  NE1 TRP A 100     -20.142 -11.531   3.931  1.00 44.98           N  
ANISOU  325  NE1 TRP A 100     6493   4268   6330    480   -442   1873       N  
ATOM    326  CE2 TRP A 100     -20.117 -11.577   5.301  1.00 44.16           C  
ANISOU  326  CE2 TRP A 100     6424   4081   6274    468   -305   1660       C  
ATOM    327  CE3 TRP A 100     -18.515 -12.050   7.053  1.00 39.97           C  
ANISOU  327  CE3 TRP A 100     6098   3530   5560    311   -188   1204       C  
ATOM    328  CZ2 TRP A 100     -21.142 -11.354   6.231  1.00 45.56           C  
ANISOU  328  CZ2 TRP A 100     6511   4186   6615    561   -179   1649       C  
ATOM    329  CZ3 TRP A 100     -19.532 -11.820   7.978  1.00 42.27           C  
ANISOU  329  CZ3 TRP A 100     6318   3752   5991    401    -63   1182       C  
ATOM    330  CH2 TRP A 100     -20.826 -11.477   7.565  1.00 43.36           C  
ANISOU  330  CH2 TRP A 100     6309   3859   6308    528    -50   1403       C  
ATOM    331  N   GLU A 101     -13.475 -10.844   3.650  1.00 37.03           N  
ANISOU  331  N   GLU A 101     6001   3202   4868     11   -297   1331       N  
ATOM    332  CA  GLU A 101     -12.122 -11.192   3.219  1.00 37.53           C  
ANISOU  332  CA  GLU A 101     6114   3384   4761    -79   -334   1292       C  
ATOM    333  C   GLU A 101     -11.129 -10.106   3.577  1.00 37.80           C  
ANISOU  333  C   GLU A 101     6169   3257   4935   -176   -196   1220       C  
ATOM    334  O   GLU A 101     -11.370  -8.936   3.262  1.00 37.46           O  
ANISOU  334  O   GLU A 101     6112   3012   5109   -152    -92   1346       O  
ATOM    335  CB  GLU A 101     -12.098 -11.416   1.706  1.00 38.35           C  
ANISOU  335  CB  GLU A 101     6211   3618   4744    -28   -429   1522       C  
ATOM    336  CG  GLU A 101     -12.694 -12.806   1.407  1.00 41.68           C  
ANISOU  336  CG  GLU A 101     6640   4242   4957     11   -597   1511       C  
ATOM    337  CD  GLU A 101     -12.825 -13.113  -0.070  1.00 48.56           C  
ANISOU  337  CD  GLU A 101     7518   5263   5672     62   -712   1708       C  
ATOM    338  OE1 GLU A 101     -12.337 -12.338  -0.911  1.00 50.26           O  
ANISOU  338  OE1 GLU A 101     7731   5459   5905     77   -659   1872       O  
ATOM    339  OE2 GLU A 101     -13.428 -14.154  -0.403  1.00 52.82           O  
ANISOU  339  OE2 GLU A 101     8065   5943   6059     82   -857   1699       O  
ATOM    340  N   CYS A 102     -10.003 -10.477   4.201  1.00 36.98           N  
ANISOU  340  N   CYS A 102     6092   3240   4720   -288   -197   1033       N  
ATOM    341  CA  CYS A 102      -8.916  -9.504   4.280  1.00 41.63           C  
ANISOU  341  CA  CYS A 102     6681   3711   5424   -410    -96    995       C  
ATOM    342  C   CYS A 102      -8.356  -9.254   2.884  1.00 36.92           C  
ANISOU  342  C   CYS A 102     6064   3164   4802   -400    -99   1237       C  
ATOM    343  O   CYS A 102      -8.444 -10.106   2.000  1.00 36.04           O  
ANISOU  343  O   CYS A 102     5954   3246   4495   -323   -200   1360       O  
ATOM    344  CB  CYS A 102      -7.794  -9.974   5.213  1.00 44.31           C  
ANISOU  344  CB  CYS A 102     7024   4176   5637   -536   -115    763       C  
ATOM    345  SG  CYS A 102      -8.269  -9.874   6.981  1.00 51.32           S  
ANISOU  345  SG  CYS A 102     7946   4979   6574   -574    -69    467       S  
ATOM    346  N   THR A 103      -7.763  -8.090   2.697  1.00 39.12           N  
ANISOU  346  N   THR A 103     6328   3264   5272   -485     18   1300       N  
ATOM    347  CA  THR A 103      -7.086  -7.705   1.457  1.00 41.96           C  
ANISOU  347  CA  THR A 103     6658   3660   5626   -493     50   1541       C  
ATOM    348  C   THR A 103      -5.716  -7.158   1.842  1.00 44.45           C  
ANISOU  348  C   THR A 103     6939   3927   6021   -679    129   1441       C  
ATOM    349  O   THR A 103      -5.495  -6.766   2.997  1.00 41.32           O  
ANISOU  349  O   THR A 103     6554   3404   5742   -798    170   1206       O  
ATOM    350  CB  THR A 103      -7.834  -6.603   0.664  1.00 43.04           C  
ANISOU  350  CB  THR A 103     6787   3582   5983   -408    139   1806       C  
ATOM    351  OG1 THR A 103      -7.916  -5.449   1.497  1.00 43.60           O  
ANISOU  351  OG1 THR A 103     6876   3335   6356   -488    277   1699       O  
ATOM    352  CG2 THR A 103      -9.241  -7.024   0.249  1.00 41.80           C  
ANISOU  352  CG2 THR A 103     6631   3481   5771   -231     52   1934       C  
ATOM    353  N   LYS A 104      -4.804  -7.079   0.862  1.00 39.18           N  
ANISOU  353  N   LYS A 104     5608   3431   5847  -1037    291    548       N  
ATOM    354  CA  LYS A 104      -3.456  -6.593   1.178  1.00 40.64           C  
ANISOU  354  CA  LYS A 104     5763   3613   6064  -1145    328    492       C  
ATOM    355  C   LYS A 104      -3.493  -5.215   1.824  1.00 43.85           C  
ANISOU  355  C   LYS A 104     6197   3855   6609  -1187    349    448       C  
ATOM    356  O   LYS A 104      -2.698  -4.933   2.731  1.00 46.34           O  
ANISOU  356  O   LYS A 104     6481   4170   6956  -1254    365    337       O  
ATOM    357  CB  LYS A 104      -2.579  -6.550  -0.077  1.00 40.57           C  
ANISOU  357  CB  LYS A 104     5754   3648   6012  -1221    362    592       C  
ATOM    358  N   ASP A 105      -4.405  -4.337   1.374  1.00 44.97           N  
ANISOU  358  N   ASP A 105     6393   3853   6841  -1152    348    533       N  
ATOM    359  CA  ASP A 105      -4.457  -2.979   1.935  1.00 46.90           C  
ANISOU  359  CA  ASP A 105     6660   3919   7239  -1192    377    490       C  
ATOM    360  C   ASP A 105      -5.052  -2.936   3.347  1.00 44.03           C  
ANISOU  360  C   ASP A 105     6286   3520   6925  -1149    372    337       C  
ATOM    361  O   ASP A 105      -4.821  -1.970   4.068  1.00 43.24           O  
ANISOU  361  O   ASP A 105     6191   3305   6934  -1204    405    251       O  
ATOM    362  CB  ASP A 105      -5.262  -2.042   1.033  1.00 50.41           C  
ANISOU  362  CB  ASP A 105     7159   4209   7786  -1163    374    635       C  
ATOM    363  CG  ASP A 105      -4.548  -1.713  -0.305  1.00 56.52           C  
ANISOU  363  CG  ASP A 105     7956   4987   8533  -1241    391    787       C  
ATOM    364  OD1 ASP A 105      -3.350  -1.317  -0.318  1.00 59.19           O  
ANISOU  364  OD1 ASP A 105     8281   5328   8881  -1351    432    762       O  
ATOM    365  OD2 ASP A 105      -5.216  -1.832  -1.358  1.00 57.85           O  
ANISOU  365  OD2 ASP A 105     8156   5157   8668  -1198    362    935       O  
ATOM    366  N   ARG A 106      -5.793  -3.958   3.775  1.00 42.32           N  
ANISOU  366  N   ARG A 106     6053   3401   6627  -1062    337    295       N  
ATOM    367  CA  ARG A 106      -6.274  -3.972   5.159  1.00 44.34           C  
ANISOU  367  CA  ARG A 106     6297   3642   6909  -1038    338    142       C  
ATOM    368  C   ARG A 106      -5.262  -4.523   6.160  1.00 45.51           C  
ANISOU  368  C   ARG A 106     6401   3916   6976  -1108    335     13       C  
ATOM    369  O   ARG A 106      -5.457  -4.338   7.367  1.00 46.08           O  
ANISOU  369  O   ARG A 106     6467   3973   7070  -1123    343   -122       O  
ATOM    370  CB  ARG A 106      -7.576  -4.771   5.273  1.00 44.13           C  
ANISOU  370  CB  ARG A 106     6272   3657   6837   -920    304    149       C  
ATOM    371  CG  ARG A 106      -8.740  -4.112   4.529  1.00 44.36           C  
ANISOU  371  CG  ARG A 106     6336   3546   6972   -845    301    257       C  
ATOM    372  CD  ARG A 106     -10.052  -4.782   4.878  1.00 42.31           C  
ANISOU  372  CD  ARG A 106     6069   3316   6689   -735    274    232       C  
ATOM    373  NE  ARG A 106     -10.330  -4.773   6.312  1.00 42.18           N  
ANISOU  373  NE  ARG A 106     6038   3295   6693   -736    296     61       N  
ATOM    374  CZ  ARG A 106     -11.268  -5.527   6.882  1.00 41.56           C  
ANISOU  374  CZ  ARG A 106     5947   3278   6567   -661    280      5       C  
ATOM    375  NH1 ARG A 106     -11.994  -6.342   6.135  1.00 39.64           N  
ANISOU  375  NH1 ARG A 106     5701   3100   6261   -578    239    105       N  
ATOM    376  NH2 ARG A 106     -11.473  -5.468   8.187  1.00 42.19           N  
ANISOU  376  NH2 ARG A 106     6016   3357   6656   -678    307   -152       N  
ATOM    377  N   CYS A 107      -4.201  -5.201   5.702  1.00 46.85           N  
ANISOU  377  N   CYS A 107     6535   4211   7053  -1155    324     51       N  
ATOM    378  CA  CYS A 107      -3.275  -5.854   6.623  1.00 47.00           C  
ANISOU  378  CA  CYS A 107     6500   4360   6996  -1210    306    -55       C  
ATOM    379  C   CYS A 107      -2.712  -4.842   7.595  1.00 46.15           C  
ANISOU  379  C   CYS A 107     6391   4178   6968  -1307    333   -174       C  
ATOM    380  O   CYS A 107      -2.160  -3.832   7.181  1.00 45.37           O  
ANISOU  380  O   CYS A 107     6306   3977   6956  -1379    371   -149       O  
ATOM    381  CB  CYS A 107      -2.123  -6.515   5.880  1.00 48.01           C  
ANISOU  381  CB  CYS A 107     6583   4605   7054  -1254    301      6       C  
ATOM    382  SG  CYS A 107      -2.667  -7.913   4.906  1.00 49.94           S  
ANISOU  382  SG  CYS A 107     6820   4968   7188  -1152    271    110       S  
ATOM    383  N   GLY A 108      -2.850  -5.132   8.885  1.00 46.23           N  
ANISOU  383  N   GLY A 108     6384   4242   6940  -1317    314   -303       N  
ATOM    384  CA  GLY A 108      -2.339  -4.260   9.912  1.00 48.12           C  
ANISOU  384  CA  GLY A 108     6620   4430   7234  -1418    338   -434       C  
ATOM    385  C   GLY A 108      -3.150  -3.012  10.150  1.00 49.95           C  
ANISOU  385  C   GLY A 108     6903   4474   7602  -1417    391   -485       C  
ATOM    386  O   GLY A 108      -2.663  -2.114  10.834  1.00 52.49           O  
ANISOU  386  O   GLY A 108     7227   4727   7991  -1513    424   -591       O  
ATOM    387  N   GLU A 109      -4.365  -2.935   9.605  1.00 49.23           N  
ANISOU  387  N   GLU A 109     6849   4295   7561  -1311    399   -414       N  
ATOM    388  CA  GLU A 109      -5.255  -1.796   9.809  1.00 48.21           C  
ANISOU  388  CA  GLU A 109     6759   3975   7582  -1292    449   -456       C  
ATOM    389  C   GLU A 109      -5.436  -1.521  11.296  1.00 49.07           C  
ANISOU  389  C   GLU A 109     6865   4081   7698  -1341    474   -649       C  
ATOM    390  O   GLU A 109      -5.352  -2.421  12.131  1.00 47.94           O  
ANISOU  390  O   GLU A 109     6699   4091   7426  -1349    440   -725       O  
ATOM    391  CB  GLU A 109      -6.621  -2.088   9.181  1.00 44.07           C  
ANISOU  391  CB  GLU A 109     6259   3404   7083  -1157    436   -361       C  
ATOM    392  CG  GLU A 109      -7.348  -3.186   9.917  1.00 42.93           C  
ANISOU  392  CG  GLU A 109     6098   3386   6826  -1090    405   -425       C  
ATOM    393  CD  GLU A 109      -8.609  -3.663   9.248  1.00 45.46           C  
ANISOU  393  CD  GLU A 109     6431   3692   7151   -961    383   -326       C  
ATOM    394  OE1 GLU A 109      -8.875  -3.220   8.103  1.00 45.84           O  
ANISOU  394  OE1 GLU A 109     6498   3645   7273   -922    381   -188       O  
ATOM    395  OE2 GLU A 109      -9.334  -4.507   9.864  1.00 44.23           O  
ANISOU  395  OE2 GLU A 109     6264   3624   6917   -904    364   -382       O  
ATOM    396  N   VAL A 110      -5.697  -0.263  11.637  1.00 51.60           N  
ANISOU  396  N   VAL A 110     7210   4224   8172  -1379    536   -729       N  
ATOM    397  CA  VAL A 110      -6.171   0.022  12.984  1.00 53.73           C  
ANISOU  397  CA  VAL A 110     7484   4476   8457  -1412    574   -917       C  
ATOM    398  C   VAL A 110      -7.566  -0.562  13.138  1.00 52.86           C  
ANISOU  398  C   VAL A 110     7380   4376   8329  -1289    568   -916       C  
ATOM    399  O   VAL A 110      -8.441  -0.319  12.298  1.00 53.46           O  
ANISOU  399  O   VAL A 110     7471   4338   8505  -1189    575   -809       O  
ATOM    400  CB  VAL A 110      -6.164   1.532  13.255  1.00 57.95           C  
ANISOU  400  CB  VAL A 110     8039   4800   9180  -1479    653  -1010       C  
ATOM    401  CG1 VAL A 110      -6.911   1.837  14.562  1.00 58.45           C  
ANISOU  401  CG1 VAL A 110     8109   4829   9272  -1496    706  -1210       C  
ATOM    402  CG2 VAL A 110      -4.715   2.074  13.256  1.00 58.48           C  
ANISOU  402  CG2 VAL A 110     8094   4872   9252  -1618    659  -1033       C  
ATOM    403  N   ARG A 111      -7.780  -1.338  14.205  1.00 52.59           N  
ANISOU  403  N   ARG A 111     7333   4482   8167  -1300    553  -1030       N  
ATOM    404  CA  ARG A 111      -9.054  -2.041  14.394  1.00 51.54           C  
ANISOU  404  CA  ARG A 111     7202   4385   7996  -1191    545  -1030       C  
ATOM    405  C   ARG A 111     -10.248  -1.085  14.327  1.00 53.84           C  
ANISOU  405  C   ARG A 111     7510   4474   8474  -1125    613  -1066       C  
ATOM    406  O   ARG A 111     -10.194   0.051  14.820  1.00 55.57           O  
ANISOU  406  O   ARG A 111     7738   4550   8824  -1189    682  -1182       O  
ATOM    407  CB  ARG A 111      -9.051  -2.791  15.737  1.00 51.54           C  
ANISOU  407  CB  ARG A 111     7191   4548   7844  -1243    533  -1172       C  
ATOM    408  CG  ARG A 111     -10.424  -3.307  16.172  1.00 53.43           C  
ANISOU  408  CG  ARG A 111     7434   4804   8063  -1153    548  -1215       C  
ATOM    409  CD  ARG A 111     -10.410  -4.158  17.448  1.00 54.27           C  
ANISOU  409  CD  ARG A 111     7533   5088   7997  -1210    530  -1333       C  
ATOM    410  NE  ARG A 111      -9.779  -5.458  17.262  1.00 53.34           N  
ANISOU  410  NE  ARG A 111     7394   5158   7713  -1203    440  -1232       N  
ATOM    411  CZ  ARG A 111     -10.428  -6.588  16.993  1.00 55.23           C  
ANISOU  411  CZ  ARG A 111     7626   5490   7869  -1108    397  -1148       C  
ATOM    412  NH1 ARG A 111      -9.747  -7.725  16.848  1.00 54.43           N  
ANISOU  412  NH1 ARG A 111     7501   5547   7632  -1109    320  -1064       N  
ATOM    413  NH2 ARG A 111     -11.756  -6.602  16.878  1.00 56.50           N  
ANISOU  413  NH2 ARG A 111     7797   5583   8088  -1012    432  -1151       N  
ATOM    414  N   ASN A 112     -11.340  -1.552  13.728  1.00 53.44           N  
ANISOU  414  N   ASN A 112     7456   4406   8441   -997    594   -969       N  
ATOM    415  CA  ASN A 112     -12.548  -0.749  13.567  1.00 56.58           C  
ANISOU  415  CA  ASN A 112     7856   4616   9025   -916    647   -980       C  
ATOM    416  C   ASN A 112     -13.751  -1.623  13.892  1.00 55.58           C  
ANISOU  416  C   ASN A 112     7715   4567   8838   -820    637  -1001       C  
ATOM    417  O   ASN A 112     -14.093  -2.532  13.122  1.00 54.96           O  
ANISOU  417  O   ASN A 112     7628   4574   8680   -736    574   -861       O  
ATOM    418  CB  ASN A 112     -12.644  -0.184  12.150  1.00 57.95           C  
ANISOU  418  CB  ASN A 112     8038   4651   9330   -853    625   -791       C  
ATOM    419  CG  ASN A 112     -13.860   0.695  11.945  1.00 59.12           C  
ANISOU  419  CG  ASN A 112     8179   4591   9693   -766    670   -785       C  
ATOM    420  OD1 ASN A 112     -14.883   0.546  12.618  1.00 59.02           O  
ANISOU  420  OD1 ASN A 112     8147   4566   9710   -712    704   -887       O  
ATOM    421  ND2 ASN A 112     -13.764   1.603  10.983  1.00 60.26           N  
ANISOU  421  ND2 ASN A 112     8334   4568   9993   -751    669   -658       N  
ATOM    422  N   GLU A 113     -14.415  -1.314  15.010  1.00 54.81           N  
ANISOU  422  N   GLU A 113     7610   4432   8783   -837    706  -1180       N  
ATOM    423  CA  GLU A 113     -15.517  -2.124  15.528  1.00 53.27           C  
ANISOU  423  CA  GLU A 113     7399   4320   8521   -768    710  -1231       C  
ATOM    424  C   GLU A 113     -16.661  -2.317  14.527  1.00 52.35           C  
ANISOU  424  C   GLU A 113     7263   4132   8496   -621    683  -1087       C  
ATOM    425  O   GLU A 113     -17.461  -3.242  14.702  1.00 53.54           O  
ANISOU  425  O   GLU A 113     7398   4384   8561   -557    663  -1084       O  
ATOM    426  CB  GLU A 113     -16.028  -1.485  16.829  1.00 54.18           C  
ANISOU  426  CB  GLU A 113     7510   4372   8703   -823    810  -1458       C  
ATOM    427  N   GLU A 114     -16.735  -1.510  13.466  1.00 51.48           N  
ANISOU  427  N   GLU A 114     7153   3859   8549   -572    674   -959       N  
ATOM    428  CA  GLU A 114     -17.787  -1.633  12.453  1.00 50.56           C  
ANISOU  428  CA  GLU A 114     7015   3674   8520   -440    636   -807       C  
ATOM    429  C   GLU A 114     -17.598  -2.806  11.493  1.00 49.94           C  
ANISOU  429  C   GLU A 114     6943   3756   8278   -395    541   -632       C  
ATOM    430  O   GLU A 114     -18.563  -3.204  10.832  1.00 50.45           O  
ANISOU  430  O   GLU A 114     6987   3816   8365   -291    503   -528       O  
ATOM    431  CB  GLU A 114     -17.852  -0.340  11.629  1.00 50.57           C  
ANISOU  431  CB  GLU A 114     7018   3448   8748   -415    651   -713       C  
ATOM    432  N   ASN A 115     -16.390  -3.356  11.377  1.00 48.81           N  
ANISOU  432  N   ASN A 115     6820   3747   7977   -472    502   -599       N  
ATOM    433  CA  ASN A 115     -16.097  -4.326  10.328  1.00 46.75           C  
ANISOU  433  CA  ASN A 115     6564   3612   7586   -437    423   -431       C  
ATOM    434  C   ASN A 115     -16.677  -5.690  10.652  1.00 46.17           C  
ANISOU  434  C   ASN A 115     6474   3706   7362   -386    390   -448       C  
ATOM    435  O   ASN A 115     -16.760  -6.099  11.811  1.00 47.01           O  
ANISOU  435  O   ASN A 115     6575   3892   7396   -421    417   -590       O  
ATOM    436  CB  ASN A 115     -14.587  -4.445  10.106  1.00 46.18           C  
ANISOU  436  CB  ASN A 115     6509   3622   7415   -535    401   -400       C  
ATOM    437  CG  ASN A 115     -13.984  -3.175   9.510  1.00 47.99           C  
ANISOU  437  CG  ASN A 115     6757   3691   7786   -583    425   -343       C  
ATOM    438  OD1 ASN A 115     -12.839  -2.799   9.812  1.00 49.69           O  
ANISOU  438  OD1 ASN A 115     6982   3914   7982   -687    443   -395       O  
ATOM    439  ND2 ASN A 115     -14.766  -2.495   8.678  1.00 45.99           N  
ANISOU  439  ND2 ASN A 115     6506   3288   7681   -511    421   -234       N  
ATOM    440  N   ALA A 116     -17.081  -6.404   9.607  1.00 43.58           N  
ANISOU  440  N   ALA A 116     6140   3435   6983   -312    330   -299       N  
ATOM    441  CA  ALA A 116     -17.599  -7.744   9.815  1.00 41.31           C  
ANISOU  441  CA  ALA A 116     5838   3303   6557   -266    297   -305       C  
ATOM    442  C   ALA A 116     -16.547  -8.675  10.418  1.00 40.41           C  
ANISOU  442  C   ALA A 116     5728   3358   6268   -342    279   -358       C  
ATOM    443  O   ALA A 116     -16.885  -9.557  11.212  1.00 41.97           O  
ANISOU  443  O   ALA A 116     5915   3665   6366   -336    276   -433       O  
ATOM    444  CB  ALA A 116     -18.123  -8.307   8.501  1.00 41.37           C  
ANISOU  444  CB  ALA A 116     5839   3341   6540   -185    236   -135       C  
ATOM    445  N   CYS A 117     -15.277  -8.517  10.037  1.00 38.81           N  
ANISOU  445  N   CYS A 117     5538   3180   6030   -413    265   -315       N  
ATOM    446  CA  CYS A 117     -14.183  -9.290  10.626  1.00 38.56           C  
ANISOU  446  CA  CYS A 117     5500   3295   5856   -488    245   -364       C  
ATOM    447  C   CYS A 117     -12.924  -8.443  10.495  1.00 39.59           C  
ANISOU  447  C   CYS A 117     5639   3375   6027   -582    260   -366       C  
ATOM    448  O   CYS A 117     -12.941  -7.369   9.876  1.00 40.07           O  
ANISOU  448  O   CYS A 117     5715   3293   6215   -583    284   -318       O  
ATOM    449  CB  CYS A 117     -14.044 -10.679   9.982  1.00 38.38           C  
ANISOU  449  CB  CYS A 117     5463   3419   5700   -448    187   -267       C  
ATOM    450  SG  CYS A 117     -13.915 -10.726   8.164  1.00 40.87           S  
ANISOU  450  SG  CYS A 117     5785   3714   6029   -405    155    -80       S  
ATOM    451  N   HIS A 118     -11.839  -8.858  11.139  1.00 38.03           N  
ANISOU  451  N   HIS A 118     5429   3286   5734   -664    246   -425       N  
ATOM    452  CA  HIS A 118     -10.749  -7.902  11.304  1.00 39.82           C  
ANISOU  452  CA  HIS A 118     5661   3454   6016   -765    271   -466       C  
ATOM    453  C   HIS A 118      -9.454  -8.385  10.688  1.00 37.81           C  
ANISOU  453  C   HIS A 118     5386   3293   5687   -814    235   -388       C  
ATOM    454  O   HIS A 118      -9.239  -9.589  10.535  1.00 36.48           O  
ANISOU  454  O   HIS A 118     5194   3262   5407   -788    191   -344       O  
ATOM    455  CB  HIS A 118     -10.551  -7.583  12.781  1.00 43.00           C  
ANISOU  455  CB  HIS A 118     6062   3875   6402   -847    299   -636       C  
ATOM    456  CG  HIS A 118     -11.775  -6.999  13.404  1.00 42.26           C  
ANISOU  456  CG  HIS A 118     5984   3678   6395   -810    352   -732       C  
ATOM    457  ND1 HIS A 118     -12.818  -7.779  13.861  1.00 41.82           N  
ANISOU  457  ND1 HIS A 118     5924   3686   6281   -745    346   -763       N  
ATOM    458  CD2 HIS A 118     -12.164  -5.718  13.562  1.00 42.15           C  
ANISOU  458  CD2 HIS A 118     5986   3493   6536   -823    416   -799       C  
ATOM    459  CE1 HIS A 118     -13.775  -6.994  14.331  1.00 42.02           C  
ANISOU  459  CE1 HIS A 118     5958   3590   6417   -723    409   -855       C  
ATOM    460  NE2 HIS A 118     -13.404  -5.738  14.158  1.00 43.33           N  
ANISOU  460  NE2 HIS A 118     6135   3609   6720   -768    452   -879       N  
ATOM    461  N   CYS A 119      -8.612  -7.419  10.284  1.00 37.95           N  
ANISOU  461  N   CYS A 119     5410   3227   5782   -883    259   -369       N  
ATOM    462  CA  CYS A 119      -7.270  -7.711   9.788  1.00 40.23           C  
ANISOU  462  CA  CYS A 119     5672   3595   6018   -947    238   -316       C  
ATOM    463  C   CYS A 119      -6.221  -6.910  10.547  1.00 40.76           C  
ANISOU  463  C   CYS A 119     5728   3638   6119  -1068    260   -416       C  
ATOM    464  O   CYS A 119      -5.124  -6.727  10.046  1.00 41.50           O  
ANISOU  464  O   CYS A 119     5802   3748   6217  -1132    260   -373       O  
ATOM    465  CB  CYS A 119      -7.120  -7.415   8.289  1.00 44.05           C  
ANISOU  465  CB  CYS A 119     6170   4021   6546   -926    245   -168       C  
ATOM    466  SG  CYS A 119      -8.527  -7.844   7.316  1.00 46.65           S  
ANISOU  466  SG  CYS A 119     6523   4324   6877   -798    228    -51       S  
ATOM    467  N   SER A 120      -6.541  -6.430  11.737  1.00 42.51           N  
ANISOU  467  N   SER A 120     5960   3826   6365  -1106    283   -553       N  
ATOM    468  CA  SER A 120      -5.549  -5.758  12.560  1.00 46.18           C  
ANISOU  468  CA  SER A 120     6413   4289   6846  -1231    299   -663       C  
ATOM    469  C   SER A 120      -4.596  -6.771  13.207  1.00 46.77           C  
ANISOU  469  C   SER A 120     6438   4550   6783  -1287    240   -693       C  
ATOM    470  O   SER A 120      -4.869  -7.975  13.303  1.00 45.00           O  
ANISOU  470  O   SER A 120     6194   4448   6455  -1227    192   -657       O  
ATOM    471  CB  SER A 120      -6.265  -4.945  13.632  1.00 46.31           C  
ANISOU  471  CB  SER A 120     6457   4213   6925  -1259    349   -811       C  
ATOM    472  OG  SER A 120      -7.357  -5.732  14.103  1.00 46.18           O  
ANISOU  472  OG  SER A 120     6447   4257   6842  -1179    335   -837       O  
ATOM    473  N   GLU A 121      -3.489  -6.251  13.728  1.00 50.19           N  
ANISOU  473  N   GLU A 121     6848   5000   7223  -1406    240   -763       N  
ATOM    474  CA  GLU A 121      -2.482  -7.099  14.355  1.00 54.35           C  
ANISOU  474  CA  GLU A 121     7317   5696   7636  -1468    176   -786       C  
ATOM    475  C   GLU A 121      -3.027  -7.853  15.571  1.00 55.34           C  
ANISOU  475  C   GLU A 121     7443   5932   7651  -1463    138   -867       C  
ATOM    476  O   GLU A 121      -2.559  -8.954  15.883  1.00 56.79           O  
ANISOU  476  O   GLU A 121     7581   6266   7730  -1462     69   -837       O  
ATOM    477  CB  GLU A 121      -1.268  -6.240  14.719  1.00 60.45           C  
ANISOU  477  CB  GLU A 121     8064   6453   8450  -1605    186   -856       C  
ATOM    478  CG  GLU A 121      -0.042  -7.004  15.219  1.00 65.93           C  
ANISOU  478  CG  GLU A 121     8684   7314   9050  -1677    114   -862       C  
ATOM    479  CD  GLU A 121       0.637  -7.885  14.161  1.00 69.90           C  
ANISOU  479  CD  GLU A 121     9133   7889   9536  -1626     81   -727       C  
ATOM    480  OE1 GLU A 121       0.159  -7.969  12.998  1.00 71.09           O  
ANISOU  480  OE1 GLU A 121     9309   7975   9728  -1539    114   -625       O  
ATOM    481  OE2 GLU A 121       1.664  -8.506  14.514  1.00 71.15           O  
ANISOU  481  OE2 GLU A 121     9219   8174   9641  -1678     23   -726       O  
ATOM    482  N   ASP A 122      -4.038  -7.330  16.243  1.00 54.80           N  
ANISOU  482  N   ASP A 122     7422   5794   7607  -1457    182   -964       N  
ATOM    483  CA  ASP A 122      -4.524  -8.011  17.442  1.00 55.98           C  
ANISOU  483  CA  ASP A 122     7574   6057   7641  -1470    152  -1047       C  
ATOM    484  C   ASP A 122      -5.599  -9.052  17.171  1.00 53.24           C  
ANISOU  484  C   ASP A 122     7236   5751   7240  -1345    134   -975       C  
ATOM    485  O   ASP A 122      -6.084  -9.674  18.122  1.00 54.07           O  
ANISOU  485  O   ASP A 122     7347   5951   7246  -1351    112  -1032       O  
ATOM    486  CB  ASP A 122      -5.071  -6.988  18.440  1.00 60.07           C  
ANISOU  486  CB  ASP A 122     8132   6495   8197  -1540    218  -1212       C  
ATOM    487  CG  ASP A 122      -6.254  -6.207  17.890  1.00 62.48           C  
ANISOU  487  CG  ASP A 122     8482   6620   8638  -1456    299  -1216       C  
ATOM    488  OD1 ASP A 122      -6.786  -6.592  16.834  1.00 62.82           O  
ANISOU  488  OD1 ASP A 122     8528   6623   8719  -1339    292  -1089       O  
ATOM    489  OD2 ASP A 122      -6.668  -5.216  18.518  1.00 64.90           O  
ANISOU  489  OD2 ASP A 122     8817   6825   9019  -1507    368  -1350       O  
ATOM    490  N   CYS A 123      -6.026  -9.227  15.918  1.00 48.99           N  
ANISOU  490  N   CYS A 123     6705   5147   6762  -1239    145   -854       N  
ATOM    491  CA  CYS A 123      -7.220 -10.031  15.696  1.00 45.66           C  
ANISOU  491  CA  CYS A 123     6299   4743   6306  -1125    140   -806       C  
ATOM    492  C   CYS A 123      -6.943 -11.469  16.041  1.00 43.63           C  
ANISOU  492  C   CYS A 123     6006   4655   5916  -1110     66   -763       C  
ATOM    493  O   CYS A 123      -7.863 -12.210  16.386  1.00 41.93           O  
ANISOU  493  O   CYS A 123     5802   4487   5641  -1051     56   -765       O  
ATOM    494  CB  CYS A 123      -7.715  -9.925  14.239  1.00 44.58           C  
ANISOU  494  CB  CYS A 123     6174   4509   6253  -1023    160   -681       C  
ATOM    495  SG  CYS A 123      -6.655 -10.757  12.990  1.00 41.92           S  
ANISOU  495  SG  CYS A 123     5796   4253   5881  -1002    112   -531       S  
ATOM    496  N   LEU A 124      -5.681 -11.883  15.935  1.00 44.96           N  
ANISOU  496  N   LEU A 124     6126   4909   6047  -1161     15   -721       N  
ATOM    497  CA  LEU A 124      -5.345 -13.253  16.285  1.00 48.28           C  
ANISOU  497  CA  LEU A 124     6503   5481   6359  -1147    -59   -674       C  
ATOM    498  C   LEU A 124      -5.639 -13.498  17.764  1.00 49.50           C  
ANISOU  498  C   LEU A 124     6669   5722   6416  -1208    -85   -771       C  
ATOM    499  O   LEU A 124      -6.416 -14.393  18.107  1.00 48.63           O  
ANISOU  499  O   LEU A 124     6568   5674   6234  -1155   -107   -755       O  
ATOM    500  CB  LEU A 124      -3.874 -13.524  15.943  1.00 50.09           C  
ANISOU  500  CB  LEU A 124     6668   5775   6589  -1197   -105   -620       C  
ATOM    501  CG  LEU A 124      -3.455 -14.561  14.886  1.00 49.81           C  
ANISOU  501  CG  LEU A 124     6584   5787   6554  -1123   -134   -498       C  
ATOM    502  CD1 LEU A 124      -4.549 -14.856  13.889  1.00 49.73           C  
ANISOU  502  CD1 LEU A 124     6612   5716   6567  -1008    -97   -430       C  
ATOM    503  CD2 LEU A 124      -2.208 -14.123  14.148  1.00 48.40           C  
ANISOU  503  CD2 LEU A 124     6360   5589   6439  -1173   -125   -463       C  
ATOM    504  N   SER A 125      -5.087 -12.665  18.656  1.00 52.86           N  
ANISOU  504  N   SER A 125     7099   6152   6834  -1328    -78   -878       N  
ATOM    505  CA  SER A 125      -5.371 -12.901  20.070  1.00 56.55           C  
ANISOU  505  CA  SER A 125     7580   6716   7191  -1400   -102   -973       C  
ATOM    506  C   SER A 125      -6.853 -12.726  20.397  1.00 58.46           C  
ANISOU  506  C   SER A 125     7879   6900   7432  -1351    -37  -1040       C  
ATOM    507  O   SER A 125      -7.388 -13.472  21.220  1.00 60.52           O  
ANISOU  507  O   SER A 125     8150   7258   7586  -1356    -63  -1062       O  
ATOM    508  CB  SER A 125      -4.500 -12.026  20.964  1.00 59.11           C  
ANISOU  508  CB  SER A 125     7898   7063   7499  -1549   -106  -1085       C  
ATOM    509  OG  SER A 125      -4.504 -10.692  20.544  1.00 61.46           O  
ANISOU  509  OG  SER A 125     8223   7211   7919  -1573    -25  -1148       O  
ATOM    510  N   ARG A 126      -7.561 -11.818  19.731  1.00 58.72           N  
ANISOU  510  N   ARG A 126     7947   6778   7588  -1297     44  -1062       N  
ATOM    511  CA  ARG A 126      -8.986 -11.674  20.038  1.00 58.75           C  
ANISOU  511  CA  ARG A 126     7991   6725   7606  -1244    107  -1126       C  
ATOM    512  C   ARG A 126      -9.858 -12.658  19.273  1.00 56.88           C  
ANISOU  512  C   ARG A 126     7751   6497   7362  -1109     91  -1014       C  
ATOM    513  O   ARG A 126     -11.082 -12.659  19.454  1.00 56.82           O  
ANISOU  513  O   ARG A 126     7769   6450   7370  -1055    137  -1055       O  
ATOM    514  CB  ARG A 126      -9.436 -10.236  19.770  1.00 62.06           C  
ANISOU  514  CB  ARG A 126     8441   6965   8174  -1246    200  -1207       C  
ATOM    515  CG  ARG A 126      -8.529  -9.190  20.479  1.00 64.61           C  
ANISOU  515  CG  ARG A 126     8767   7266   8516  -1387    223  -1328       C  
ATOM    516  CD  ARG A 126      -9.156  -7.805  20.494  1.00 67.97           C  
ANISOU  516  CD  ARG A 126     9224   7511   9089  -1397    326  -1438       C  
ATOM    517  NE  ARG A 126     -10.616  -7.898  20.466  1.00 70.02           N  
ANISOU  517  NE  ARG A 126     9504   7708   9391  -1299    379  -1458       N  
ATOM    518  CZ  ARG A 126     -11.441  -6.854  20.525  1.00 72.26           C  
ANISOU  518  CZ  ARG A 126     9808   7832   9814  -1282    472  -1553       C  
ATOM    519  NH1 ARG A 126     -10.955  -5.618  20.642  1.00 72.43           N  
ANISOU  519  NH1 ARG A 126     9838   7735   9945  -1360    526  -1642       N  
ATOM    520  NH2 ARG A 126     -12.760  -7.060  20.475  1.00 73.02           N  
ANISOU  520  NH2 ARG A 126     9910   7885   9949  -1187    512  -1561       N  
ATOM    521  N   GLY A 127      -9.255 -13.489  18.424  1.00 55.05           N  
ANISOU  521  N   GLY A 127     7486   6317   7115  -1058     31   -882       N  
ATOM    522  CA  GLY A 127      -9.974 -14.520  17.696  1.00 51.53           C  
ANISOU  522  CA  GLY A 127     7035   5893   6653   -941     11   -778       C  
ATOM    523  C   GLY A 127     -11.054 -14.053  16.745  1.00 49.98           C  
ANISOU  523  C   GLY A 127     6862   5567   6561   -842     67   -746       C  
ATOM    524  O   GLY A 127     -11.993 -14.811  16.489  1.00 48.43           O  
ANISOU  524  O   GLY A 127     6670   5391   6342   -757     63   -702       O  
ATOM    525  N   ASP A 128     -10.957 -12.832  16.191  1.00 48.48           N  
ANISOU  525  N   ASP A 128     6688   5243   6491   -849    116   -759       N  
ATOM    526  CA  ASP A 128     -12.008 -12.418  15.252  1.00 46.42           C  
ANISOU  526  CA  ASP A 128     6445   4859   6334   -751    156   -709       C  
ATOM    527  C   ASP A 128     -11.435 -11.975  13.894  1.00 44.63           C  
ANISOU  527  C   ASP A 128     6214   4558   6187   -726    152   -597       C  
ATOM    528  O   ASP A 128     -12.039 -11.154  13.191  1.00 43.53           O  
ANISOU  528  O   ASP A 128     6093   4286   6160   -680    189   -566       O  
ATOM    529  CB  ASP A 128     -12.893 -11.333  15.867  1.00 44.71           C  
ANISOU  529  CB  ASP A 128     6255   4526   6209   -761    230   -827       C  
ATOM    530  CG  ASP A 128     -12.103 -10.119  16.280  1.00 46.47           C  
ANISOU  530  CG  ASP A 128     6486   4671   6498   -862    267   -915       C  
ATOM    531  OD1 ASP A 128     -10.852 -10.149  16.116  1.00 44.45           O  
ANISOU  531  OD1 ASP A 128     6215   4465   6209   -926    230   -881       O  
ATOM    532  OD2 ASP A 128     -12.719  -9.129  16.794  1.00 49.28           O  
ANISOU  532  OD2 ASP A 128     6860   4916   6947   -880    336  -1026       O  
ATOM    533  N   CYS A 129     -10.282 -12.522  13.502  1.00 42.19           N  
ANISOU  533  N   CYS A 129     5877   4331   5822   -759    108   -533       N  
ATOM    534  CA  CYS A 129      -9.781 -12.334  12.143  1.00 39.18           C  
ANISOU  534  CA  CYS A 129     5491   3906   5492   -735    106   -419       C  
ATOM    535  C   CYS A 129     -10.773 -12.830  11.094  1.00 37.02           C  
ANISOU  535  C   CYS A 129     5227   3612   5227   -627    101   -318       C  
ATOM    536  O   CYS A 129     -11.515 -13.805  11.306  1.00 31.70           O  
ANISOU  536  O   CYS A 129     4547   3009   4488   -569     80   -314       O  
ATOM    537  CB  CYS A 129      -8.487 -13.099  11.953  1.00 40.43           C  
ANISOU  537  CB  CYS A 129     5606   4177   5579   -778     62   -374       C  
ATOM    538  SG  CYS A 129      -7.232 -12.756  13.178  1.00 44.56           S  
ANISOU  538  SG  CYS A 129     6102   4758   6071   -909     44   -477       S  
ATOM    539  N   CYS A 130     -10.750 -12.171   9.918  1.00 35.63           N  
ANISOU  539  N   CYS A 130     5065   3345   5127   -607    118   -230       N  
ATOM    540  CA  CYS A 130     -11.273 -12.811   8.707  1.00 33.92           C  
ANISOU  540  CA  CYS A 130     4850   3149   4889   -529     99   -112       C  
ATOM    541  C   CYS A 130     -10.607 -14.188   8.516  1.00 28.55           C  
ANISOU  541  C   CYS A 130     4135   2616   4098   -527     61    -78       C  
ATOM    542  O   CYS A 130      -9.460 -14.391   8.890  1.00 30.24           O  
ANISOU  542  O   CYS A 130     4319   2891   4278   -593     50   -107       O  
ATOM    543  CB  CYS A 130     -11.017 -11.907   7.495  1.00 34.53           C  
ANISOU  543  CB  CYS A 130     4947   3130   5044   -539    117    -15       C  
ATOM    544  SG  CYS A 130     -11.928 -10.226   7.656  1.00 37.85           S  
ANISOU  544  SG  CYS A 130     5404   3344   5633   -526    160    -41       S  
ATOM    545  N   THR A 131     -11.325 -15.140   7.947  1.00 28.35           N  
ANISOU  545  N   THR A 131     4106   2643   4023   -453     41    -21       N  
ATOM    546  CA  THR A 131     -10.743 -16.482   7.863  1.00 28.54           C  
ANISOU  546  CA  THR A 131     4092   2795   3957   -449     10     -2       C  
ATOM    547  C   THR A 131      -9.519 -16.539   6.956  1.00 28.62           C  
ANISOU  547  C   THR A 131     4079   2835   3962   -494     16     56       C  
ATOM    548  O   THR A 131      -8.769 -17.507   7.048  1.00 28.17           O  
ANISOU  548  O   THR A 131     3978   2872   3853   -506     -3     53       O  
ATOM    549  CB  THR A 131     -11.733 -17.513   7.337  1.00 29.37           C  
ANISOU  549  CB  THR A 131     4198   2947   4015   -366     -7     46       C  
ATOM    550  OG1 THR A 131     -12.053 -17.149   5.983  1.00 28.56           O  
ANISOU  550  OG1 THR A 131     4116   2798   3939   -340      5    137       O  
ATOM    551  CG2 THR A 131     -12.997 -17.579   8.208  1.00 29.93           C  
ANISOU  551  CG2 THR A 131     4285   2999   4088   -320     -8    -11       C  
ATOM    552  N   ASN A 132      -9.290 -15.544   6.078  1.00 29.63           N  
ANISOU  552  N   ASN A 132     4230   2883   4147   -521     44    109       N  
ATOM    553  CA  ASN A 132      -8.131 -15.581   5.194  1.00 27.98           C  
ANISOU  553  CA  ASN A 132     3998   2706   3928   -573     60    160       C  
ATOM    554  C   ASN A 132      -7.003 -14.680   5.696  1.00 29.34           C  
ANISOU  554  C   ASN A 132     4157   2841   4150   -664     77    114       C  
ATOM    555  O   ASN A 132      -6.033 -14.435   4.954  1.00 30.49           O  
ANISOU  555  O   ASN A 132     4286   2993   4306   -719    100    154       O  
ATOM    556  CB  ASN A 132      -8.509 -15.205   3.734  1.00 30.50           C  
ANISOU  556  CB  ASN A 132     4351   2982   4257   -557     79    267       C  
ATOM    557  CG  ASN A 132      -8.867 -13.732   3.587  1.00 34.04           C  
ANISOU  557  CG  ASN A 132     4845   3292   4796   -576     98    294       C  
ATOM    558  OD1 ASN A 132      -9.291 -13.124   4.571  1.00 34.87           O  
ANISOU  558  OD1 ASN A 132     4963   3329   4959   -571     98    225       O  
ATOM    559  ND2 ASN A 132      -8.703 -13.133   2.358  1.00 35.41           N  
ANISOU  559  ND2 ASN A 132     5045   3423   4987   -602    116    395       N  
ATOM    560  N   TYR A 133      -7.081 -14.216   6.946  1.00 29.10           N  
ANISOU  560  N   TYR A 133     4130   2781   4145   -689     69     24       N  
ATOM    561  CA  TYR A 133      -6.128 -13.204   7.420  1.00 32.36           C  
ANISOU  561  CA  TYR A 133     4536   3146   4613   -783     88    -27       C  
ATOM    562  C   TYR A 133      -4.673 -13.685   7.302  1.00 34.41           C  
ANISOU  562  C   TYR A 133     4734   3495   4845   -846     79    -24       C  
ATOM    563  O   TYR A 133      -3.809 -12.977   6.772  1.00 34.53           O  
ANISOU  563  O   TYR A 133     4743   3474   4905   -912    108     -2       O  
ATOM    564  CB  TYR A 133      -6.458 -12.825   8.862  1.00 31.38           C  
ANISOU  564  CB  TYR A 133     4422   3001   4500   -806     80   -139       C  
ATOM    565  CG  TYR A 133      -5.350 -12.035   9.536  1.00 33.76           C  
ANISOU  565  CG  TYR A 133     4704   3287   4835   -914     89   -210       C  
ATOM    566  CD1 TYR A 133      -5.110 -10.700   9.201  1.00 32.26           C  
ANISOU  566  CD1 TYR A 133     4542   2973   4740   -967    133   -211       C  
ATOM    567  CD2 TYR A 133      -4.520 -12.629  10.505  1.00 33.48           C  
ANISOU  567  CD2 TYR A 133     4620   3361   4740   -968     48   -272       C  
ATOM    568  CE1 TYR A 133      -4.087  -9.978   9.810  1.00 37.12           C  
ANISOU  568  CE1 TYR A 133     5139   3575   5389  -1073    143   -282       C  
ATOM    569  CE2 TYR A 133      -3.474 -11.884  11.130  1.00 32.17           C  
ANISOU  569  CE2 TYR A 133     4432   3189   4604  -1077     51   -340       C  
ATOM    570  CZ  TYR A 133      -3.273 -10.583  10.755  1.00 37.15           C  
ANISOU  570  CZ  TYR A 133     5091   3697   5326  -1128    101   -348       C  
ATOM    571  OH  TYR A 133      -2.268  -9.861  11.364  1.00 40.88           O  
ANISOU  571  OH  TYR A 133     5542   4163   5829  -1239    105   -420       O  
ATOM    572  N   GLN A 134      -4.381 -14.889   7.807  1.00 32.89           N  
ANISOU  572  N   GLN A 134     4492   3416   4588   -827     39    -46       N  
ATOM    573  CA  GLN A 134      -3.018 -15.415   7.782  1.00 34.41           C  
ANISOU  573  CA  GLN A 134     4611   3693   4769   -879     25    -46       C  
ATOM    574  C   GLN A 134      -2.519 -15.597   6.358  1.00 32.83           C  
ANISOU  574  C   GLN A 134     4394   3502   4578   -878     63     32       C  
ATOM    575  O   GLN A 134      -1.314 -15.521   6.098  1.00 34.50           O  
ANISOU  575  O   GLN A 134     4553   3744   4813   -942     78     32       O  
ATOM    576  CB  GLN A 134      -2.988 -16.783   8.461  1.00 41.17           C  
ANISOU  576  CB  GLN A 134     5418   4660   5566   -840    -29    -63       C  
ATOM    577  CG  GLN A 134      -2.407 -16.859   9.821  1.00 46.28           C  
ANISOU  577  CG  GLN A 134     6027   5361   6197   -896    -79   -132       C  
ATOM    578  CD  GLN A 134      -2.422 -18.325  10.334  1.00 46.45           C  
ANISOU  578  CD  GLN A 134     5999   5487   6163   -848   -137   -120       C  
ATOM    579  OE1 GLN A 134      -2.552 -19.322   9.572  1.00 44.60           O  
ANISOU  579  OE1 GLN A 134     5740   5286   5918   -783   -133    -65       O  
ATOM    580  NE2 GLN A 134      -2.304 -18.447  11.627  1.00 51.17           N  
ANISOU  580  NE2 GLN A 134     6583   6134   6725   -887   -190   -171       N  
ATOM    581  N   VAL A 135      -3.411 -15.972   5.446  1.00 31.01           N  
ANISOU  581  N   VAL A 135     4200   3261   4320   -809     79     94       N  
ATOM    582  CA  VAL A 135      -2.988 -16.183   4.055  1.00 31.22           C  
ANISOU  582  CA  VAL A 135     4216   3308   4336   -818    120    165       C  
ATOM    583  C   VAL A 135      -2.615 -14.856   3.407  1.00 35.19           C  
ANISOU  583  C   VAL A 135     4755   3724   4890   -887    164    202       C  
ATOM    584  O   VAL A 135      -1.546 -14.717   2.805  1.00 38.28           O  
ANISOU  584  O   VAL A 135     5110   4139   5295   -953    199    219       O  
ATOM    585  CB  VAL A 135      -4.083 -16.906   3.256  1.00 29.55           C  
ANISOU  585  CB  VAL A 135     4039   3116   4073   -736    120    220       C  
ATOM    586  CG1 VAL A 135      -3.742 -16.914   1.749  1.00 30.15           C  
ANISOU  586  CG1 VAL A 135     4119   3208   4127   -762    169    293       C  
ATOM    587  CG2 VAL A 135      -4.249 -18.356   3.783  1.00 27.59           C  
ANISOU  587  CG2 VAL A 135     3744   2959   3780   -676     84    187       C  
ATOM    588  N   VAL A 136      -3.468 -13.844   3.552  1.00 34.46           N  
ANISOU  588  N   VAL A 136     4729   3526   4838   -877    165    214       N  
ATOM    589  CA  VAL A 136      -3.198 -12.557   2.888  1.00 34.41           C  
ANISOU  589  CA  VAL A 136     4762   3421   4891   -940    205    264       C  
ATOM    590  C   VAL A 136      -2.081 -11.779   3.583  1.00 36.89           C  
ANISOU  590  C   VAL A 136     5046   3706   5265  -1035    219    199       C  
ATOM    591  O   VAL A 136      -1.312 -11.038   2.951  1.00 37.15           O  
ANISOU  591  O   VAL A 136     5079   3700   5336  -1112    259    235       O  
ATOM    592  CB  VAL A 136      -4.498 -11.746   2.868  1.00 34.34           C  
ANISOU  592  CB  VAL A 136     4824   3295   4928   -891    199    297       C  
ATOM    593  CG1 VAL A 136      -4.241 -10.293   2.343  1.00 39.16           C  
ANISOU  593  CG1 VAL A 136     5476   3779   5625   -958    235    350       C  
ATOM    594  CG2 VAL A 136      -5.523 -12.507   2.099  1.00 36.04           C  
ANISOU  594  CG2 VAL A 136     5062   3548   5083   -808    182    367       C  
ATOM    595  N   CYS A 137      -2.025 -11.843   4.906  1.00 38.83           N  
ANISOU  595  N   CYS A 137     5270   3965   5519  -1041    186    103       N  
ATOM    596  CA  CYS A 137      -1.181 -10.926   5.652  1.00 40.15           C  
ANISOU  596  CA  CYS A 137     5421   4089   5746  -1134    196     33       C  
ATOM    597  C   CYS A 137       0.061 -11.562   6.248  1.00 39.30           C  
ANISOU  597  C   CYS A 137     5227   4092   5614  -1189    171    -23       C  
ATOM    598  O   CYS A 137       1.010 -10.837   6.576  1.00 39.14           O  
ANISOU  598  O   CYS A 137     5180   4051   5642  -1283    183    -65       O  
ATOM    599  CB  CYS A 137      -1.982 -10.277   6.790  1.00 42.15           C  
ANISOU  599  CB  CYS A 137     5715   4266   6035  -1126    182    -48       C  
ATOM    600  SG  CYS A 137      -3.411  -9.278   6.265  1.00 47.42           S  
ANISOU  600  SG  CYS A 137     6470   4771   6775  -1067    212      5       S  
ATOM    601  N   LYS A 138       0.087 -12.872   6.448  1.00 35.94           N  
ANISOU  601  N   LYS A 138     4752   3779   5125  -1135    132    -25       N  
ATOM    602  CA  LYS A 138       1.264 -13.464   7.069  1.00 36.88           C  
ANISOU  602  CA  LYS A 138     4781   3997   5237  -1183     98    -71       C  
ATOM    603  C   LYS A 138       1.929 -14.529   6.211  1.00 39.18           C  
ANISOU  603  C   LYS A 138     5001   4375   5509  -1160    109    -22       C  
ATOM    604  O   LYS A 138       2.736 -15.302   6.734  1.00 41.25           O  
ANISOU  604  O   LYS A 138     5178   4726   5770  -1172     70    -49       O  
ATOM    605  CB  LYS A 138       0.901 -14.066   8.434  1.00 36.35           C  
ANISOU  605  CB  LYS A 138     4698   3988   5124  -1158     30   -135       C  
ATOM    606  CG  LYS A 138       0.225 -13.083   9.373  1.00 39.02           C  
ANISOU  606  CG  LYS A 138     5102   4250   5476  -1187     28   -204       C  
ATOM    607  CD  LYS A 138       1.213 -12.013   9.844  1.00 43.80           C  
ANISOU  607  CD  LYS A 138     5687   4821   6135  -1305     39   -265       C  
ATOM    608  CE  LYS A 138       0.556 -11.010  10.825  1.00 46.80           C  
ANISOU  608  CE  LYS A 138     6130   5120   6534  -1342     47   -355       C  
ATOM    609  NZ  LYS A 138       1.491  -9.878  11.228  1.00 47.95           N  
ANISOU  609  NZ  LYS A 138     6260   5218   6739  -1465     66   -422       N  
ATOM    610  N   GLY A 139       1.618 -14.611   4.925  1.00 36.87           N  
ANISOU  610  N   GLY A 139     4739   4063   5205  -1131    159     49       N  
ATOM    611  CA  GLY A 139       2.391 -15.508   4.106  1.00 35.82           C  
ANISOU  611  CA  GLY A 139     4535   4011   5064  -1129    186     76       C  
ATOM    612  C   GLY A 139       2.004 -16.972   4.183  1.00 35.29           C  
ANISOU  612  C   GLY A 139     4431   4024   4953  -1040    153     79       C  
ATOM    613  O   GLY A 139       2.757 -17.797   3.674  1.00 36.32           O  
ANISOU  613  O   GLY A 139     4486   4222   5093  -1040    174     83       O  
ATOM    614  N   GLU A 140       0.876 -17.329   4.790  1.00 34.42           N  
ANISOU  614  N   GLU A 140     4368   3905   4803   -968    109     72       N  
ATOM    615  CA  GLU A 140       0.508 -18.740   4.946  1.00 34.61           C  
ANISOU  615  CA  GLU A 140     4358   4002   4791   -888     75     74       C  
ATOM    616  C   GLU A 140      -0.251 -19.215   3.711  1.00 34.25           C  
ANISOU  616  C   GLU A 140     4353   3956   4706   -832    119    127       C  
ATOM    617  O   GLU A 140      -0.670 -18.417   2.873  1.00 34.34           O  
ANISOU  617  O   GLU A 140     4429   3911   4707   -849    161    169       O  
ATOM    618  CB  GLU A 140      -0.334 -18.948   6.188  1.00 39.12           C  
ANISOU  618  CB  GLU A 140     4959   4574   5333   -847     10     42       C  
ATOM    619  CG  GLU A 140       0.352 -18.572   7.459  1.00 47.37           C  
ANISOU  619  CG  GLU A 140     5967   5636   6397   -909    -39    -14       C  
ATOM    620  CD  GLU A 140       1.294 -19.664   7.954  1.00 54.56           C  
ANISOU  620  CD  GLU A 140     6772   6639   7321   -909    -89    -21       C  
ATOM    621  OE1 GLU A 140       1.026 -20.864   7.688  1.00 54.69           O  
ANISOU  621  OE1 GLU A 140     6758   6698   7322   -837   -100      7       O  
ATOM    622  OE2 GLU A 140       2.303 -19.307   8.608  1.00 58.52           O  
ANISOU  622  OE2 GLU A 140     7215   7166   7855   -982   -119    -52       O  
ATOM    623  N   SER A 141      -0.448 -20.530   3.598  1.00 29.76           N  
ANISOU  623  N   SER A 141     3746   3450   4114   -769    106    128       N  
ATOM    624  CA  SER A 141      -1.163 -21.058   2.454  1.00 29.34           C  
ANISOU  624  CA  SER A 141     3726   3406   4015   -723    146    168       C  
ATOM    625  C   SER A 141      -2.604 -21.369   2.849  1.00 29.20           C  
ANISOU  625  C   SER A 141     3772   3371   3952   -646    106    177       C  
ATOM    626  O   SER A 141      -2.883 -21.665   4.016  1.00 28.09           O  
ANISOU  626  O   SER A 141     3623   3237   3813   -618     50    145       O  
ATOM    627  CB  SER A 141      -0.459 -22.338   1.944  1.00 32.67           C  
ANISOU  627  CB  SER A 141     4061   3901   4450   -706    172    154       C  
ATOM    628  OG  SER A 141      -0.374 -23.270   3.015  1.00 32.27           O  
ANISOU  628  OG  SER A 141     3953   3884   4422   -661    111    124       O  
ATOM    629  N   HIS A 142      -3.503 -21.352   1.862  1.00 26.77           N  
ANISOU  629  N   HIS A 142     3523   3048   3599   -617    134    222       N  
ATOM    630  CA  HIS A 142      -4.838 -21.891   2.050  1.00 26.02           C  
ANISOU  630  CA  HIS A 142     3471   2952   3463   -540    102    230       C  
ATOM    631  C   HIS A 142      -4.751 -23.370   2.432  1.00 29.50           C  
ANISOU  631  C   HIS A 142     3851   3459   3897   -490     80    199       C  
ATOM    632  O   HIS A 142      -3.935 -24.110   1.884  1.00 25.63           O  
ANISOU  632  O   HIS A 142     3299   3017   3423   -503    112    190       O  
ATOM    633  CB  HIS A 142      -5.673 -21.751   0.767  1.00 28.88           C  
ANISOU  633  CB  HIS A 142     3891   3304   3776   -525    133    288       C  
ATOM    634  CG  HIS A 142      -6.113 -20.342   0.468  1.00 30.96           C  
ANISOU  634  CG  HIS A 142     4224   3487   4052   -553    138    337       C  
ATOM    635  ND1 HIS A 142      -7.019 -19.655   1.261  1.00 29.92           N  
ANISOU  635  ND1 HIS A 142     4138   3284   3946   -521    101    332       N  
ATOM    636  CD2 HIS A 142      -5.746 -19.485  -0.524  1.00 31.73           C  
ANISOU  636  CD2 HIS A 142     4351   3557   4149   -613    177    392       C  
ATOM    637  CE1 HIS A 142      -7.196 -18.435   0.765  1.00 31.18           C  
ANISOU  637  CE1 HIS A 142     4347   3367   4132   -553    116    383       C  
ATOM    638  NE2 HIS A 142      -6.439 -18.306  -0.316  1.00 31.84           N  
ANISOU  638  NE2 HIS A 142     4424   3476   4196   -610    158    427       N  
ATOM    639  N   TRP A 143      -5.650 -23.818   3.308  1.00 24.87           N  
ANISOU  639  N   TRP A 143     3284   2872   3294   -435     32    185       N  
ATOM    640  CA  TRP A 143      -5.681 -25.243   3.651  1.00 24.39           C  
ANISOU  640  CA  TRP A 143     3172   2865   3231   -387      9    167       C  
ATOM    641  C   TRP A 143      -5.766 -26.120   2.407  1.00 29.09           C  
ANISOU  641  C   TRP A 143     3752   3495   3807   -365     57    180       C  
ATOM    642  O   TRP A 143      -5.092 -27.157   2.329  1.00 25.91           O  
ANISOU  642  O   TRP A 143     3276   3132   3436   -355     67    160       O  
ATOM    643  CB  TRP A 143      -6.846 -25.529   4.599  1.00 23.81           C  
ANISOU  643  CB  TRP A 143     3137   2783   3128   -335    -39    158       C  
ATOM    644  CG  TRP A 143      -7.003 -26.980   4.900  1.00 23.36           C  
ANISOU  644  CG  TRP A 143     3037   2772   3068   -286    -62    152       C  
ATOM    645  CD1 TRP A 143      -6.355 -27.705   5.869  1.00 23.44           C  
ANISOU  645  CD1 TRP A 143     2985   2814   3108   -286   -107    139       C  
ATOM    646  CD2 TRP A 143      -7.916 -27.899   4.248  1.00 23.95           C  
ANISOU  646  CD2 TRP A 143     3126   2862   3112   -231    -47    162       C  
ATOM    647  NE1 TRP A 143      -6.782 -29.045   5.815  1.00 25.55           N  
ANISOU  647  NE1 TRP A 143     3227   3108   3375   -231   -116    145       N  
ATOM    648  CE2 TRP A 143      -7.721 -29.174   4.828  1.00 24.59           C  
ANISOU  648  CE2 TRP A 143     3152   2976   3216   -199    -75    152       C  
ATOM    649  CE3 TRP A 143      -8.815 -27.770   3.175  1.00 24.34           C  
ANISOU  649  CE3 TRP A 143     3226   2902   3120   -212    -13    183       C  
ATOM    650  CZ2 TRP A 143      -8.429 -30.305   4.412  1.00 25.48           C  
ANISOU  650  CZ2 TRP A 143     3262   3105   3315   -149    -65    153       C  
ATOM    651  CZ3 TRP A 143      -9.553 -28.908   2.778  1.00 25.12           C  
ANISOU  651  CZ3 TRP A 143     3321   3028   3194   -164     -8    181       C  
ATOM    652  CH2 TRP A 143      -9.329 -30.158   3.410  1.00 24.81           C  
ANISOU  652  CH2 TRP A 143     3228   3015   3184   -134    -30    162       C  
ATOM    653  N   VAL A 144      -6.524 -25.691   1.384  1.00 24.25           N  
ANISOU  653  N   VAL A 144     3200   2867   3146   -364     88    213       N  
ATOM    654  CA  VAL A 144      -6.692 -26.556   0.195  1.00 26.93           C  
ANISOU  654  CA  VAL A 144     3531   3252   3452   -353    134    217       C  
ATOM    655  C   VAL A 144      -5.397 -26.732  -0.635  1.00 27.38           C  
ANISOU  655  C   VAL A 144     3529   3343   3533   -409    198    200       C  
ATOM    656  O   VAL A 144      -5.264 -27.701  -1.408  1.00 25.85           O  
ANISOU  656  O   VAL A 144     3301   3194   3328   -403    243    177       O  
ATOM    657  CB  VAL A 144      -7.842 -26.029  -0.695  1.00 26.78           C  
ANISOU  657  CB  VAL A 144     3591   3218   3366   -346    141    265       C  
ATOM    658  CG1 VAL A 144      -7.442 -24.762  -1.446  1.00 24.89           C  
ANISOU  658  CG1 VAL A 144     3388   2952   3117   -412    171    311       C  
ATOM    659  CG2 VAL A 144      -8.270 -27.114  -1.684  1.00 27.40           C  
ANISOU  659  CG2 VAL A 144     3663   3353   3395   -328    173    258       C  
ATOM    660  N   ASP A 145      -4.429 -25.821  -0.504  1.00 26.38           N  
ANISOU  660  N   ASP A 145     3384   3197   3442   -468    211    204       N  
ATOM    661  CA  ASP A 145      -3.163 -25.902  -1.218  1.00 27.47           C  
ANISOU  661  CA  ASP A 145     3460   3367   3611   -528    276    183       C  
ATOM    662  C   ASP A 145      -2.104 -26.737  -0.489  1.00 32.70           C  
ANISOU  662  C   ASP A 145     4014   4051   4359   -516    266    135       C  
ATOM    663  O   ASP A 145      -0.995 -26.915  -1.012  1.00 26.94           O  
ANISOU  663  O   ASP A 145     3213   3348   3673   -560    322    108       O  
ATOM    664  CB  ASP A 145      -2.640 -24.497  -1.433  1.00 26.81           C  
ANISOU  664  CB  ASP A 145     3408   3249   3531   -602    295    214       C  
ATOM    665  CG  ASP A 145      -3.512 -23.696  -2.410  1.00 36.25           C  
ANISOU  665  CG  ASP A 145     4699   4424   4651   -623    313    277       C  
ATOM    666  OD1 ASP A 145      -4.122 -24.327  -3.295  1.00 35.48           O  
ANISOU  666  OD1 ASP A 145     4623   4366   4491   -607    338    288       O  
ATOM    667  OD2 ASP A 145      -3.528 -22.452  -2.332  1.00 37.98           O  
ANISOU  667  OD2 ASP A 145     4965   4586   4877   -662    304    317       O  
ATOM    668  N   ASP A 146      -2.398 -27.230   0.703  1.00 25.78           N  
ANISOU  668  N   ASP A 146     3120   3165   3510   -463    194    126       N  
ATOM    669  CA  ASP A 146      -1.410 -28.009   1.447  1.00 26.02           C  
ANISOU  669  CA  ASP A 146     3044   3215   3627   -452    168     98       C  
ATOM    670  C   ASP A 146      -1.539 -29.491   1.080  1.00 25.84           C  
ANISOU  670  C   ASP A 146     2969   3217   3632   -397    191     74       C  
ATOM    671  O   ASP A 146      -2.604 -29.955   0.734  1.00 25.30           O  
ANISOU  671  O   ASP A 146     2955   3149   3508   -357    195     79       O  
ATOM    672  CB  ASP A 146      -1.633 -27.887   2.966  1.00 27.32           C  
ANISOU  672  CB  ASP A 146     3214   3366   3802   -431     74    107       C  
ATOM    673  CG  ASP A 146      -1.398 -26.470   3.501  1.00 33.15           C  
ANISOU  673  CG  ASP A 146     3991   4075   4528   -490     51    114       C  
ATOM    674  OD1 ASP A 146      -0.601 -25.745   2.881  1.00 35.58           O  
ANISOU  674  OD1 ASP A 146     4284   4378   4857   -551     99    110       O  
ATOM    675  OD2 ASP A 146      -2.002 -26.104   4.559  1.00 36.55           O  
ANISOU  675  OD2 ASP A 146     4467   4489   4932   -480    -11    116       O  
ATOM    676  N   ASP A 147      -0.481 -30.237   1.286  1.00 26.34           N  
ANISOU  676  N   ASP A 147     2921   3294   3791   -393    196     48       N  
ATOM    677  CA  ASP A 147      -0.495 -31.672   1.033  1.00 26.32           C  
ANISOU  677  CA  ASP A 147     2856   3301   3845   -339    218     21       C  
ATOM    678  C   ASP A 147      -1.433 -32.372   2.011  1.00 31.03           C  
ANISOU  678  C   ASP A 147     3478   3883   4428   -272    137     47       C  
ATOM    679  O   ASP A 147      -1.602 -31.925   3.147  1.00 31.29           O  
ANISOU  679  O   ASP A 147     3535   3909   4446   -271     56     79       O  
ATOM    680  CB  ASP A 147       0.941 -32.191   1.199  1.00 27.18           C  
ANISOU  680  CB  ASP A 147     2826   3416   4085   -349    231     -6       C  
ATOM    681  CG  ASP A 147       1.897 -31.582   0.158  1.00 35.52           C  
ANISOU  681  CG  ASP A 147     3847   4491   5157   -421    326    -40       C  
ATOM    682  OD1 ASP A 147       2.970 -31.086   0.524  1.00 33.95           O  
ANISOU  682  OD1 ASP A 147     3580   4297   5024   -462    314    -42       O  
ATOM    683  OD2 ASP A 147       1.565 -31.641  -1.028  1.00 36.13           O  
ANISOU  683  OD2 ASP A 147     3964   4584   5178   -442    413    -67       O  
ATOM    684  N   CYS A 148      -2.036 -33.489   1.574  1.00 33.47           N  
ANISOU  684  N   CYS A 148     3784   4190   4743   -223    164     29       N  
ATOM    685  CA  CYS A 148      -2.650 -34.432   2.509  1.00 34.56           C  
ANISOU  685  CA  CYS A 148     3915   4312   4903   -161     95     51       C  
ATOM    686  C   CYS A 148      -1.601 -35.044   3.397  1.00 35.11           C  
ANISOU  686  C   CYS A 148     3873   4375   5094   -146     41     66       C  
ATOM    687  O   CYS A 148      -0.646 -35.631   2.910  1.00 39.34           O  
ANISOU  687  O   CYS A 148     4309   4906   5734   -144     89     34       O  
ATOM    688  CB  CYS A 148      -3.400 -35.555   1.790  1.00 43.09           C  
ANISOU  688  CB  CYS A 148     5004   5388   5981   -118    142     22       C  
ATOM    689  SG  CYS A 148      -4.733 -34.668   1.112  1.00 54.45           S  
ANISOU  689  SG  CYS A 148     6577   6841   7269   -137    163     30       S  
ATOM    690  N   GLU A 149      -1.800 -34.977   4.706  1.00 34.06           N  
ANISOU  690  N   GLU A 149     3750   4241   4949   -134    -58    113       N  
ATOM    691  CA  GLU A 149      -0.878 -35.629   5.629  1.00 34.74           C  
ANISOU  691  CA  GLU A 149     3729   4325   5144   -120   -128    145       C  
ATOM    692  C   GLU A 149      -1.706 -36.412   6.636  1.00 31.18           C  
ANISOU  692  C   GLU A 149     3304   3867   4674    -76   -208    194       C  
ATOM    693  O   GLU A 149      -2.569 -35.834   7.293  1.00 28.11           O  
ANISOU  693  O   GLU A 149     3008   3493   4179    -89   -252    214       O  
ATOM    694  CB  GLU A 149       0.036 -34.603   6.328  1.00 37.37           C  
ANISOU  694  CB  GLU A 149     4034   4683   5480   -179   -180    162       C  
ATOM    695  CG  GLU A 149       0.911 -35.188   7.475  1.00 47.72           C  
ANISOU  695  CG  GLU A 149     5240   6005   6887   -172   -280    212       C  
ATOM    696  CD  GLU A 149       1.534 -34.105   8.426  1.00 56.63           C  
ANISOU  696  CD  GLU A 149     6366   7170   7981   -241   -355    232       C  
ATOM    697  OE1 GLU A 149       2.428 -34.449   9.243  1.00 58.94           O  
ANISOU  697  OE1 GLU A 149     6560   7482   8352   -250   -437    273       O  
ATOM    698  OE2 GLU A 149       1.123 -32.911   8.357  1.00 60.86           O  
ANISOU  698  OE2 GLU A 149     6995   7713   8415   -289   -333    208       O  
ATOM    699  N   GLU A 150      -1.455 -37.719   6.751  1.00 28.93           N  
ANISOU  699  N   GLU A 150     2938   3556   4498    -26   -222    211       N  
ATOM    700  CA  GLU A 150      -2.186 -38.537   7.721  1.00 28.07           C  
ANISOU  700  CA  GLU A 150     2849   3438   4379     11   -300    267       C  
ATOM    701  C   GLU A 150      -2.151 -37.907   9.105  1.00 29.21           C  
ANISOU  701  C   GLU A 150     3021   3621   4456    -28   -408    324       C  
ATOM    702  O   GLU A 150      -1.124 -37.366   9.526  1.00 30.44           O  
ANISOU  702  O   GLU A 150     3119   3801   4647    -68   -450    339       O  
ATOM    703  CB  GLU A 150      -1.568 -39.937   7.793  1.00 30.68           C  
ANISOU  703  CB  GLU A 150     3061   3725   4869     63   -315    292       C  
ATOM    704  CG  GLU A 150      -2.398 -40.890   8.623  1.00 33.53           C  
ANISOU  704  CG  GLU A 150     3448   4068   5224    101   -382    353       C  
ATOM    705  CD  GLU A 150      -1.954 -42.355   8.450  1.00 38.21           C  
ANISOU  705  CD  GLU A 150     3931   4597   5990    160   -375    370       C  
ATOM    706  OE1 GLU A 150      -0.837 -42.592   7.962  1.00 40.36           O  
ANISOU  706  OE1 GLU A 150     4090   4845   6399    170   -341    345       O  
ATOM    707  OE2 GLU A 150      -2.736 -43.267   8.785  1.00 38.09           O  
ANISOU  707  OE2 GLU A 150     3940   4551   5982    195   -398    405       O  
ATOM    708  N   ILE A 151      -3.282 -37.968   9.815  1.00 29.42           N  
ANISOU  708  N   ILE A 151     3136   3659   4384    -24   -450    352       N  
ATOM    709  CA  ILE A 151      -3.411 -37.471  11.181  1.00 31.56           C  
ANISOU  709  CA  ILE A 151     3443   3973   4574    -68   -546    398       C  
ATOM    710  C   ILE A 151      -3.514 -38.703  12.088  1.00 35.10           C  
ANISOU  710  C   ILE A 151     3851   4418   5068    -40   -628    476       C  
ATOM    711  O   ILE A 151      -4.609 -39.236  12.270  1.00 33.62           O  
ANISOU  711  O   ILE A 151     3726   4221   4828    -15   -625    488       O  
ATOM    712  CB  ILE A 151      -4.646 -36.568  11.346  1.00 31.49           C  
ANISOU  712  CB  ILE A 151     3564   3981   4419    -92   -524    365       C  
ATOM    713  CG1 ILE A 151      -4.719 -35.469  10.262  1.00 32.32           C  
ANISOU  713  CG1 ILE A 151     3716   4075   4492   -108   -437    299       C  
ATOM    714  CG2 ILE A 151      -4.739 -35.994  12.783  1.00 30.34           C  
ANISOU  714  CG2 ILE A 151     3456   3886   4185   -151   -612    395       C  
ATOM    715  CD1 ILE A 151      -6.131 -34.815  10.208  1.00 30.60           C  
ANISOU  715  CD1 ILE A 151     3615   3853   4157   -109   -406    270       C  
ATOM    716  N   ARG A 152      -2.385 -39.172  12.675  1.00 37.00           N  
ANISOU  716  N   ARG A 152     3983   4666   5409    -45   -706    537       N  
ATOM    717  CA  ARG A 152      -2.405 -40.420  13.457  1.00 42.10           C  
ANISOU  717  CA  ARG A 152     4580   5298   6118    -15   -788    628       C  
ATOM    718  C   ARG A 152      -2.932 -40.253  14.899  1.00 43.21           C  
ANISOU  718  C   ARG A 152     4785   5500   6134    -68   -890    695       C  
ATOM    719  O   ARG A 152      -3.424 -41.228  15.485  1.00 43.73           O  
ANISOU  719  O   ARG A 152     4855   5554   6206    -47   -940    766       O  
ATOM    720  CB  ARG A 152      -1.005 -41.057  13.538  1.00 46.20           C  
ANISOU  720  CB  ARG A 152     4947   5795   6810      4   -840    681       C  
ATOM    721  CG  ARG A 152      -0.332 -41.305  12.205  1.00 51.61           C  
ANISOU  721  CG  ARG A 152     5550   6424   7635     49   -738    612       C  
ATOM    722  CD  ARG A 152       0.563 -42.572  12.168  1.00 60.31           C  
ANISOU  722  CD  ARG A 152     6502   7465   8947    107   -768    666       C  
ATOM    723  NE  ARG A 152       0.015 -43.540  11.209  1.00 67.85           N  
ANISOU  723  NE  ARG A 152     7455   8345   9981    172   -671    618       N  
ATOM    724  CZ  ARG A 152      -0.503 -44.737  11.512  1.00 73.43           C  
ANISOU  724  CZ  ARG A 152     8152   8998  10752    220   -699    673       C  
ATOM    725  NH1 ARG A 152      -1.034 -45.499  10.544  1.00 75.48           N  
ANISOU  725  NH1 ARG A 152     8416   9191  11071    270   -596    608       N  
ATOM    726  NH2 ARG A 152      -0.479 -45.186  12.765  1.00 75.28           N  
ANISOU  726  NH2 ARG A 152     8369   9245  10988    213   -829    794       N  
ATOM    727  N   VAL A 153      -2.737 -39.091  15.516  1.00 40.54           N  
ANISOU  727  N   VAL A 153     4488   5225   5689   -142   -925    677       N  
ATOM    728  CA  VAL A 153      -3.350 -38.724  16.794  1.00 39.12           C  
ANISOU  728  CA  VAL A 153     4388   5114   5363   -208   -997    709       C  
ATOM    729  C   VAL A 153      -3.807 -37.274  16.687  1.00 38.58           C  
ANISOU  729  C   VAL A 153     4414   5072   5172   -259   -939    615       C  
ATOM    730  O   VAL A 153      -3.311 -36.527  15.832  1.00 39.66           O  
ANISOU  730  O   VAL A 153     4535   5187   5348   -258   -876    552       O  
ATOM    731  CB  VAL A 153      -2.376 -38.906  17.990  1.00 41.02           C  
ANISOU  731  CB  VAL A 153     4556   5416   5616   -264  -1134    803       C  
ATOM    732  CG1 VAL A 153      -1.784 -40.324  18.026  1.00 42.23           C  
ANISOU  732  CG1 VAL A 153     4596   5525   5924   -205  -1196    906       C  
ATOM    733  CG2 VAL A 153      -1.261 -37.957  17.919  1.00 41.67           C  
ANISOU  733  CG2 VAL A 153     4583   5527   5721   -312  -1148    769       C  
ATOM    734  N   PRO A 154      -4.803 -36.868  17.489  1.00 33.14           N  
ANISOU  734  N   PRO A 154     3824   4424   4342   -304   -949    600       N  
ATOM    735  CA  PRO A 154      -5.231 -35.458  17.485  1.00 32.93           C  
ANISOU  735  CA  PRO A 154     3883   4415   4216   -355   -896    509       C  
ATOM    736  C   PRO A 154      -4.083 -34.524  17.873  1.00 35.85           C  
ANISOU  736  C   PRO A 154     4211   4825   4585   -428   -939    493       C  
ATOM    737  O   PRO A 154      -3.359 -34.782  18.830  1.00 36.95           O  
ANISOU  737  O   PRO A 154     4299   5023   4717   -480  -1041    555       O  
ATOM    738  CB  PRO A 154      -6.352 -35.421  18.546  1.00 33.91           C  
ANISOU  738  CB  PRO A 154     4097   4585   4203   -398   -918    509       C  
ATOM    739  CG  PRO A 154      -6.746 -36.825  18.769  1.00 34.11           C  
ANISOU  739  CG  PRO A 154     4101   4602   4257   -353   -955    592       C  
ATOM    740  CD  PRO A 154      -5.549 -37.673  18.474  1.00 33.37           C  
ANISOU  740  CD  PRO A 154     3890   4485   4304   -316  -1009    667       C  
ATOM    741  N   GLU A 155      -3.896 -33.444  17.128  1.00 33.93           N  
ANISOU  741  N   GLU A 155     3988   4553   4352   -438   -867    416       N  
ATOM    742  CA  GLU A 155      -2.855 -32.459  17.501  1.00 36.05           C  
ANISOU  742  CA  GLU A 155     4224   4858   4618   -517   -900    390       C  
ATOM    743  C   GLU A 155      -3.629 -31.219  17.953  1.00 37.34           C  
ANISOU  743  C   GLU A 155     4493   5031   4663   -579   -861    308       C  
ATOM    744  O   GLU A 155      -4.038 -30.404  17.129  1.00 39.00           O  
ANISOU  744  O   GLU A 155     4752   5186   4880   -560   -772    243       O  
ATOM    745  CB  GLU A 155      -1.907 -32.160  16.326  1.00 38.07           C  
ANISOU  745  CB  GLU A 155     4410   5067   4989   -491   -846    367       C  
ATOM    746  CG  GLU A 155      -1.189 -33.405  15.756  1.00 41.24           C  
ANISOU  746  CG  GLU A 155     4699   5444   5526   -422   -862    430       C  
ATOM    747  CD  GLU A 155      -0.444 -33.152  14.418  1.00 42.84           C  
ANISOU  747  CD  GLU A 155     4844   5599   5835   -393   -779    391       C  
ATOM    748  OE1 GLU A 155      -0.370 -32.012  13.915  1.00 42.07           O  
ANISOU  748  OE1 GLU A 155     4788   5487   5711   -429   -717    328       O  
ATOM    749  OE2 GLU A 155       0.069 -34.132  13.864  1.00 44.69           O  
ANISOU  749  OE2 GLU A 155     4989   5806   6186   -336   -772    423       O  
ATOM    750  N   CYS A 156      -3.916 -31.136  19.251  1.00 36.14           N  
ANISOU  750  N   CYS A 156     4379   4949   4405   -650   -925    313       N  
ATOM    751  CA  CYS A 156      -4.803 -30.138  19.840  1.00 38.40           C  
ANISOU  751  CA  CYS A 156     4765   5247   4578   -709   -885    229       C  
ATOM    752  C   CYS A 156      -4.028 -29.274  20.830  1.00 40.27           C  
ANISOU  752  C   CYS A 156     4994   5551   4754   -827   -941    194       C  
ATOM    753  O   CYS A 156      -3.234 -29.800  21.615  1.00 39.98           O  
ANISOU  753  O   CYS A 156     4897   5590   4702   -877  -1046    261       O  
ATOM    754  CB  CYS A 156      -5.995 -30.790  20.577  1.00 41.83           C  
ANISOU  754  CB  CYS A 156     5263   5713   4918   -705   -895    246       C  
ATOM    755  SG  CYS A 156      -7.174 -31.806  19.518  1.00 45.03           S  
ANISOU  755  SG  CYS A 156     5690   6043   5377   -575   -824    274       S  
ATOM    756  N   PRO A 157      -4.258 -27.954  20.824  1.00 41.50           N  
ANISOU  756  N   PRO A 157     5209   5681   4877   -877   -877     92       N  
ATOM    757  CA  PRO A 157      -3.709 -27.073  21.878  1.00 40.92           C  
ANISOU  757  CA  PRO A 157     5144   5674   4728  -1004   -920     36       C  
ATOM    758  C   PRO A 157      -3.935 -27.604  23.290  1.00 39.97           C  
ANISOU  758  C   PRO A 157     5043   5664   4480  -1082  -1006     66       C  
ATOM    759  O   PRO A 157      -4.891 -28.355  23.539  1.00 38.12           O  
ANISOU  759  O   PRO A 157     4848   5440   4195  -1045  -1001     98       O  
ATOM    760  CB  PRO A 157      -4.458 -25.744  21.673  1.00 41.68           C  
ANISOU  760  CB  PRO A 157     5326   5704   4806  -1025   -815    -86       C  
ATOM    761  CG  PRO A 157      -5.106 -25.830  20.258  1.00 41.10           C  
ANISOU  761  CG  PRO A 157     5270   5522   4824   -903   -724    -78       C  
ATOM    762  CD  PRO A 157      -5.250 -27.291  19.933  1.00 40.00           C  
ANISOU  762  CD  PRO A 157     5089   5397   4711   -819   -762     23       C  
ATOM    763  N   ALA A 158      -3.067 -27.219  24.233  1.00 42.68           N  
ANISOU  763  N   ALA A 158     5358   6095   4765  -1198  -1085     58       N  
ATOM    764  CA  ALA A 158      -3.283 -27.597  25.630  1.00 46.88           C  
ANISOU  764  CA  ALA A 158     5916   6745   5151  -1295  -1167     81       C  
ATOM    765  C   ALA A 158      -4.618 -27.033  26.099  1.00 48.22           C  
ANISOU  765  C   ALA A 158     6198   6908   5214  -1328  -1078    -25       C  
ATOM    766  O   ALA A 158      -5.044 -25.956  25.660  1.00 48.70           O  
ANISOU  766  O   ALA A 158     6308   6893   5302  -1323   -974   -140       O  
ATOM    767  CB  ALA A 158      -2.138 -27.093  26.533  1.00 49.30           C  
ANISOU  767  CB  ALA A 158     6178   7152   5401  -1430  -1263     73       C  
ATOM    768  N   GLY A 159      -5.310 -27.793  26.950  1.00 47.22           N  
ANISOU  768  N   GLY A 159     6108   6855   4976  -1356  -1115     17       N  
ATOM    769  CA  GLY A 159      -6.640 -27.431  27.396  1.00 46.07           C  
ANISOU  769  CA  GLY A 159     6060   6708   4736  -1381  -1027    -79       C  
ATOM    770  C   GLY A 159      -7.802 -28.031  26.604  1.00 45.08           C  
ANISOU  770  C   GLY A 159     5965   6497   4666  -1253   -949    -60       C  
ATOM    771  O   GLY A 159      -8.902 -28.123  27.148  1.00 46.75           O  
ANISOU  771  O   GLY A 159     6242   6732   4789  -1274   -903   -103       O  
ATOM    772  N   PHE A 160      -7.613 -28.415  25.331  1.00 41.61           N  
ANISOU  772  N   PHE A 160     5479   5963   4368  -1127   -928     -4       N  
ATOM    773  CA  PHE A 160      -8.638 -29.219  24.655  1.00 37.55           C  
ANISOU  773  CA  PHE A 160     4983   5388   3896  -1014   -878     33       C  
ATOM    774  C   PHE A 160      -8.691 -30.624  25.282  1.00 41.27           C  
ANISOU  774  C   PHE A 160     5432   5930   4317  -1017   -966    156       C  
ATOM    775  O   PHE A 160      -7.674 -31.321  25.330  1.00 44.39           O  
ANISOU  775  O   PHE A 160     5754   6357   4755  -1015  -1064    261       O  
ATOM    776  CB  PHE A 160      -8.360 -29.273  23.144  1.00 33.66           C  
ANISOU  776  CB  PHE A 160     4447   4788   3556   -895   -834     57       C  
ATOM    777  CG  PHE A 160      -8.812 -28.030  22.400  1.00 31.31           C  
ANISOU  777  CG  PHE A 160     4192   4400   3305   -871   -727    -51       C  
ATOM    778  CD1 PHE A 160      -8.158 -26.822  22.580  1.00 31.36           C  
ANISOU  778  CD1 PHE A 160     4201   4401   3313   -945   -715   -127       C  
ATOM    779  CD2 PHE A 160      -9.916 -28.057  21.539  1.00 27.36           C  
ANISOU  779  CD2 PHE A 160     3727   3818   2849   -778   -643    -74       C  
ATOM    780  CE1 PHE A 160      -8.592 -25.659  21.909  1.00 30.54           C  
ANISOU  780  CE1 PHE A 160     4136   4202   3264   -922   -618   -218       C  
ATOM    781  CE2 PHE A 160     -10.344 -26.917  20.902  1.00 26.87           C  
ANISOU  781  CE2 PHE A 160     3701   3673   2835   -757   -556   -158       C  
ATOM    782  CZ  PHE A 160      -9.685 -25.712  21.086  1.00 28.65           C  
ANISOU  782  CZ  PHE A 160     3931   3884   3071   -827   -542   -228       C  
ATOM    783  N   VAL A 161      -9.850 -31.035  25.832  1.00 39.27           N  
ANISOU  783  N   VAL A 161     5240   5706   3976  -1028   -937    146       N  
ATOM    784  CA  VAL A 161      -9.914 -32.355  26.473  1.00 38.86           C  
ANISOU  784  CA  VAL A 161     5172   5719   3872  -1040  -1022    270       C  
ATOM    785  C   VAL A 161     -10.287 -33.442  25.493  1.00 39.01           C  
ANISOU  785  C   VAL A 161     5160   5657   4004   -909  -1005    348       C  
ATOM    786  O   VAL A 161     -10.172 -34.638  25.821  1.00 41.55           O  
ANISOU  786  O   VAL A 161     5452   6008   4327   -900  -1081    468       O  
ATOM    787  CB  VAL A 161     -10.903 -32.412  27.664  1.00 41.99           C  
ANISOU  787  CB  VAL A 161     5646   6201   4106  -1134  -1007    236       C  
ATOM    788  CG1 VAL A 161     -10.540 -31.336  28.676  1.00 44.55           C  
ANISOU  788  CG1 VAL A 161     6003   6614   4308  -1278  -1017    143       C  
ATOM    789  CG2 VAL A 161     -12.331 -32.249  27.195  1.00 40.97           C  
ANISOU  789  CG2 VAL A 161     5575   6006   3987  -1071   -883    151       C  
ATOM    790  N   ARG A 162     -10.728 -33.079  24.299  1.00 35.66           N  
ANISOU  790  N   ARG A 162     4741   5131   3676   -813   -912    288       N  
ATOM    791  CA  ARG A 162     -11.137 -34.083  23.334  1.00 31.94           C  
ANISOU  791  CA  ARG A 162     4245   4589   3304   -698   -888    347       C  
ATOM    792  C   ARG A 162     -11.177 -33.385  21.979  1.00 30.92           C  
ANISOU  792  C   ARG A 162     4109   4364   3277   -617   -803    279       C  
ATOM    793  O   ARG A 162     -11.388 -32.171  21.921  1.00 31.87           O  
ANISOU  793  O   ARG A 162     4269   4467   3374   -646   -744    180       O  
ATOM    794  CB  ARG A 162     -12.502 -34.682  23.702  1.00 28.21           C  
ANISOU  794  CB  ARG A 162     3829   4127   2763   -691   -849    346       C  
ATOM    795  CG  ARG A 162     -13.704 -33.737  23.559  1.00 29.14           C  
ANISOU  795  CG  ARG A 162     4017   4216   2839   -689   -738    219       C  
ATOM    796  CD  ARG A 162     -15.047 -34.401  23.949  1.00 31.33           C  
ANISOU  796  CD  ARG A 162     4340   4510   3055   -685   -700    219       C  
ATOM    797  NE  ARG A 162     -15.134 -34.565  25.409  1.00 35.06           N  
ANISOU  797  NE  ARG A 162     4846   5089   3384   -803   -746    235       N  
ATOM    798  CZ  ARG A 162     -15.413 -33.569  26.253  1.00 39.35           C  
ANISOU  798  CZ  ARG A 162     5440   5688   3823   -899   -710    133       C  
ATOM    799  NH1 ARG A 162     -15.636 -32.333  25.795  1.00 38.70           N  
ANISOU  799  NH1 ARG A 162     5376   5550   3779   -884   -628     11       N  
ATOM    800  NH2 ARG A 162     -15.484 -33.789  27.563  1.00 42.45           N  
ANISOU  800  NH2 ARG A 162     5865   6190   4074  -1017   -752    150       N  
ATOM    801  N   PRO A 163     -11.017 -34.097  20.884  1.00 31.33           N  
ANISOU  801  N   PRO A 163     4115   4351   3440   -522   -790    326       N  
ATOM    802  CA  PRO A 163     -11.205 -33.468  19.556  1.00 28.33           C  
ANISOU  802  CA  PRO A 163     3738   3887   3138   -451   -705    265       C  
ATOM    803  C   PRO A 163     -12.631 -32.968  19.359  1.00 26.11           C  
ANISOU  803  C   PRO A 163     3529   3575   2815   -429   -620    189       C  
ATOM    804  O   PRO A 163     -13.615 -33.720  19.496  1.00 26.00           O  
ANISOU  804  O   PRO A 163     3540   3565   2775   -402   -605    206       O  
ATOM    805  CB  PRO A 163     -10.849 -34.590  18.568  1.00 28.90           C  
ANISOU  805  CB  PRO A 163     3748   3914   3320   -365   -711    334       C  
ATOM    806  CG  PRO A 163     -10.551 -35.822  19.397  1.00 30.85           C  
ANISOU  806  CG  PRO A 163     3956   4204   3560   -381   -798    433       C  
ATOM    807  CD  PRO A 163     -10.310 -35.407  20.824  1.00 30.95           C  
ANISOU  807  CD  PRO A 163     3993   4305   3462   -487   -865    441       C  
ATOM    808  N   PRO A 164     -12.801 -31.684  19.014  1.00 25.05           N  
ANISOU  808  N   PRO A 164     3428   3404   2686   -438   -561    105       N  
ATOM    809  CA  PRO A 164     -14.146 -31.186  18.688  1.00 27.16           C  
ANISOU  809  CA  PRO A 164     3750   3628   2942   -404   -480     38       C  
ATOM    810  C   PRO A 164     -14.687 -31.872  17.436  1.00 25.76           C  
ANISOU  810  C   PRO A 164     3558   3396   2834   -306   -446     71       C  
ATOM    811  O   PRO A 164     -13.940 -32.394  16.615  1.00 25.69           O  
ANISOU  811  O   PRO A 164     3502   3367   2893   -266   -463    121       O  
ATOM    812  CB  PRO A 164     -13.934 -29.689  18.423  1.00 29.21           C  
ANISOU  812  CB  PRO A 164     4030   3843   3225   -428   -435    -40       C  
ATOM    813  CG  PRO A 164     -12.657 -29.323  19.138  1.00 29.12           C  
ANISOU  813  CG  PRO A 164     3994   3879   3190   -511   -493    -36       C  
ATOM    814  CD  PRO A 164     -11.783 -30.621  18.959  1.00 27.06           C  
ANISOU  814  CD  PRO A 164     3667   3652   2964   -485   -567     70       C  
ATOM    815  N   LEU A 165     -16.004 -31.873  17.314  1.00 22.39           N  
ANISOU  815  N   LEU A 165     3169   2949   2390   -273   -396     36       N  
ATOM    816  CA  LEU A 165     -16.711 -32.369  16.139  1.00 21.66           C  
ANISOU  816  CA  LEU A 165     3069   2809   2350   -190   -358     53       C  
ATOM    817  C   LEU A 165     -17.471 -31.221  15.517  1.00 25.44           C  
ANISOU  817  C   LEU A 165     3580   3232   2854   -163   -296     -9       C  
ATOM    818  O   LEU A 165     -18.248 -30.539  16.213  1.00 24.35           O  
ANISOU  818  O   LEU A 165     3478   3094   2681   -191   -265    -71       O  
ATOM    819  CB  LEU A 165     -17.746 -33.457  16.506  1.00 21.46           C  
ANISOU  819  CB  LEU A 165     3054   2809   2291   -171   -357     73       C  
ATOM    820  CG  LEU A 165     -18.639 -33.970  15.355  1.00 26.59           C  
ANISOU  820  CG  LEU A 165     3699   3417   2986    -94   -317     79       C  
ATOM    821  CD1 LEU A 165     -17.817 -34.697  14.228  1.00 20.45           C  
ANISOU  821  CD1 LEU A 165     2876   2616   2279    -48   -332    132       C  
ATOM    822  CD2 LEU A 165     -19.584 -34.931  16.031  1.00 26.22           C  
ANISOU  822  CD2 LEU A 165     3664   3403   2895    -98   -319     92       C  
ATOM    823  N   ILE A 166     -17.308 -31.045  14.207  1.00 22.00           N  
ANISOU  823  N   ILE A 166     3130   2749   2480   -112   -276      9       N  
ATOM    824  CA  ILE A 166     -18.115 -30.089  13.482  1.00 21.54           C  
ANISOU  824  CA  ILE A 166     3096   2633   2453    -78   -227    -26       C  
ATOM    825  C   ILE A 166     -18.889 -30.844  12.411  1.00 23.70           C  
ANISOU  825  C   ILE A 166     3360   2894   2749    -11   -211      5       C  
ATOM    826  O   ILE A 166     -18.289 -31.532  11.568  1.00 24.31           O  
ANISOU  826  O   ILE A 166     3410   2977   2851     12   -223     49       O  
ATOM    827  CB  ILE A 166     -17.267 -28.977  12.858  1.00 24.21           C  
ANISOU  827  CB  ILE A 166     3434   2927   2837    -91   -216    -31       C  
ATOM    828  CG1 ILE A 166     -16.430 -28.286  13.919  1.00 28.59           C  
ANISOU  828  CG1 ILE A 166     3994   3499   3369   -166   -234    -67       C  
ATOM    829  CG2 ILE A 166     -18.208 -28.011  12.044  1.00 22.72           C  
ANISOU  829  CG2 ILE A 166     3271   2671   2691    -50   -172    -50       C  
ATOM    830  CD1 ILE A 166     -15.471 -27.251  13.344  1.00 27.67           C  
ANISOU  830  CD1 ILE A 166     3872   3340   3301   -188   -225    -70       C  
ATOM    831  N   ILE A 167     -20.212 -30.740  12.454  1.00 21.99           N  
ANISOU  831  N   ILE A 167     3163   2665   2527     17   -183    -23       N  
ATOM    832  CA  ILE A 167     -21.059 -31.386  11.452  1.00 23.67           C  
ANISOU  832  CA  ILE A 167     3366   2870   2757     75   -172      2       C  
ATOM    833  C   ILE A 167     -21.411 -30.339  10.396  1.00 24.61           C  
ANISOU  833  C   ILE A 167     3494   2935   2920    106   -150      3       C  
ATOM    834  O   ILE A 167     -22.052 -29.344  10.728  1.00 24.29           O  
ANISOU  834  O   ILE A 167     3471   2857   2901    107   -128    -35       O  
ATOM    835  CB  ILE A 167     -22.337 -31.940  12.085  1.00 25.38           C  
ANISOU  835  CB  ILE A 167     3590   3108   2947     85   -158    -23       C  
ATOM    836  CG1 ILE A 167     -21.967 -32.996  13.125  1.00 30.22           C  
ANISOU  836  CG1 ILE A 167     4196   3774   3511     47   -185     -8       C  
ATOM    837  CG2 ILE A 167     -23.234 -32.549  10.938  1.00 25.33           C  
ANISOU  837  CG2 ILE A 167     3568   3095   2961    142   -148      0       C  
ATOM    838  CD1 ILE A 167     -22.959 -33.094  14.272  1.00 32.85           C  
ANISOU  838  CD1 ILE A 167     4548   4135   3799     21   -167    -49       C  
ATOM    839  N   PHE A 168     -21.082 -30.592   9.105  1.00 22.12           N  
ANISOU  839  N   PHE A 168     3166   2616   2622    130   -153     46       N  
ATOM    840  CA  PHE A 168     -21.326 -29.617   8.047  1.00 21.62           C  
ANISOU  840  CA  PHE A 168     3115   2509   2593    150   -141     66       C  
ATOM    841  C   PHE A 168     -22.402 -30.247   7.170  1.00 21.61           C  
ANISOU  841  C   PHE A 168     3104   2522   2585    194   -141     87       C  
ATOM    842  O   PHE A 168     -22.122 -31.179   6.410  1.00 21.54           O  
ANISOU  842  O   PHE A 168     3080   2548   2556    198   -145    111       O  
ATOM    843  CB  PHE A 168     -20.018 -29.340   7.276  1.00 24.11           C  
ANISOU  843  CB  PHE A 168     3425   2820   2918    125   -143     99       C  
ATOM    844  CG  PHE A 168     -20.084 -28.169   6.339  1.00 25.71           C  
ANISOU  844  CG  PHE A 168     3645   2973   3152    130   -134    127       C  
ATOM    845  CD1 PHE A 168     -20.848 -28.222   5.168  1.00 25.93           C  
ANISOU  845  CD1 PHE A 168     3676   3001   3177    161   -136    167       C  
ATOM    846  CD2 PHE A 168     -19.356 -27.008   6.621  1.00 26.54           C  
ANISOU  846  CD2 PHE A 168     3763   3032   3288     96   -127    119       C  
ATOM    847  CE1 PHE A 168     -20.908 -27.142   4.305  1.00 26.11           C  
ANISOU  847  CE1 PHE A 168     3715   2979   3227    160   -136    210       C  
ATOM    848  CE2 PHE A 168     -19.416 -25.912   5.751  1.00 26.17           C  
ANISOU  848  CE2 PHE A 168     3735   2931   3279     97   -120    157       C  
ATOM    849  CZ  PHE A 168     -20.162 -25.988   4.585  1.00 26.07           C  
ANISOU  849  CZ  PHE A 168     3725   2919   3260    129   -127    209       C  
ATOM    850  N   SER A 169     -23.660 -29.824   7.321  1.00 22.29           N  
ANISOU  850  N   SER A 169     3194   2585   2691    223   -134     70       N  
ATOM    851  CA  SER A 169     -24.702 -30.519   6.583  1.00 26.00           C  
ANISOU  851  CA  SER A 169     3649   3079   3152    259   -140     87       C  
ATOM    852  C   SER A 169     -25.183 -29.683   5.407  1.00 25.70           C  
ANISOU  852  C   SER A 169     3612   3010   3142    283   -151    131       C  
ATOM    853  O   SER A 169     -25.308 -28.457   5.518  1.00 29.92           O  
ANISOU  853  O   SER A 169     4156   3485   3727    290   -148    134       O  
ATOM    854  CB  SER A 169     -25.856 -30.903   7.531  1.00 30.44           C  
ANISOU  854  CB  SER A 169     4201   3651   3714    274   -129     43       C  
ATOM    855  OG  SER A 169     -26.604 -29.803   7.875  1.00 32.10           O  
ANISOU  855  OG  SER A 169     4412   3812   3973    291   -115     18       O  
ATOM    856  N   VAL A 170     -25.401 -30.313   4.253  1.00 24.52           N  
ANISOU  856  N   VAL A 170     3455   2899   2964    291   -165    168       N  
ATOM    857  CA  VAL A 170     -25.845 -29.581   3.055  1.00 24.84           C  
ANISOU  857  CA  VAL A 170     3497   2923   3016    305   -187    226       C  
ATOM    858  C   VAL A 170     -27.179 -30.184   2.643  1.00 28.29           C  
ANISOU  858  C   VAL A 170     3910   3394   3445    335   -205    230       C  
ATOM    859  O   VAL A 170     -27.395 -31.385   2.811  1.00 31.88           O  
ANISOU  859  O   VAL A 170     4352   3897   3865    332   -196    199       O  
ATOM    860  CB  VAL A 170     -24.827 -29.693   1.879  1.00 27.49           C  
ANISOU  860  CB  VAL A 170     3846   3290   3308    269   -188    270       C  
ATOM    861  CG1 VAL A 170     -23.635 -28.742   2.100  1.00 27.87           C  
ANISOU  861  CG1 VAL A 170     3915   3294   3381    239   -175    280       C  
ATOM    862  CG2 VAL A 170     -24.294 -31.171   1.801  1.00 25.68           C  
ANISOU  862  CG2 VAL A 170     3604   3124   3030    249   -171    237       C  
ATOM    863  N   ASP A 171     -28.045 -29.395   2.042  1.00 25.52           N  
ANISOU  863  N   ASP A 171     3550   3017   3131    362   -232    274       N  
ATOM    864  CA  ASP A 171     -29.403 -29.839   1.743  1.00 26.10           C  
ANISOU  864  CA  ASP A 171     3589   3118   3208    393   -255    278       C  
ATOM    865  C   ASP A 171     -29.495 -30.237   0.271  1.00 26.97           C  
ANISOU  865  C   ASP A 171     3700   3289   3258    373   -289    336       C  
ATOM    866  O   ASP A 171     -29.132 -29.446  -0.586  1.00 28.29           O  
ANISOU  866  O   ASP A 171     3884   3443   3420    359   -313    403       O  
ATOM    867  CB  ASP A 171     -30.368 -28.674   2.047  1.00 27.80           C  
ANISOU  867  CB  ASP A 171     3783   3263   3518    438   -269    291       C  
ATOM    868  CG  ASP A 171     -31.792 -29.145   2.250  1.00 30.32           C  
ANISOU  868  CG  ASP A 171     4054   3601   3863    473   -278    267       C  
ATOM    869  OD1 ASP A 171     -32.280 -29.999   1.480  1.00 32.64           O  
ANISOU  869  OD1 ASP A 171     4333   3963   4107    467   -304    286       O  
ATOM    870  OD2 ASP A 171     -32.408 -28.690   3.223  1.00 34.47           O  
ANISOU  870  OD2 ASP A 171     4558   4078   4460    502   -253    218       O  
ATOM    871  N   GLY A 172     -29.981 -31.447  -0.047  1.00 23.64           N  
ANISOU  871  N   GLY A 172     3261   2936   2787    364   -291    311       N  
ATOM    872  CA  GLY A 172     -30.183 -31.703  -1.469  1.00 25.40           C  
ANISOU  872  CA  GLY A 172     3483   3220   2946    337   -325    361       C  
ATOM    873  C   GLY A 172     -28.904 -32.011  -2.266  1.00 25.51           C  
ANISOU  873  C   GLY A 172     3530   3274   2890    282   -304    370       C  
ATOM    874  O   GLY A 172     -28.902 -31.915  -3.511  1.00 24.42           O  
ANISOU  874  O   GLY A 172     3402   3185   2692    246   -329    421       O  
ATOM    875  N   PHE A 173     -27.865 -32.489  -1.584  1.00 25.83           N  
ANISOU  875  N   PHE A 173     3582   3300   2931    268   -257    319       N  
ATOM    876  CA  PHE A 173     -26.571 -32.810  -2.202  1.00 24.08           C  
ANISOU  876  CA  PHE A 173     3380   3108   2661    219   -226    314       C  
ATOM    877  C   PHE A 173     -26.591 -34.267  -2.666  1.00 22.47           C  
ANISOU  877  C   PHE A 173     3161   2968   2408    193   -201    262       C  
ATOM    878  O   PHE A 173     -26.296 -35.191  -1.896  1.00 21.66           O  
ANISOU  878  O   PHE A 173     3044   2856   2330    201   -171    205       O  
ATOM    879  CB  PHE A 173     -25.450 -32.552  -1.201  1.00 25.49           C  
ANISOU  879  CB  PHE A 173     3567   3235   2883    221   -194    288       C  
ATOM    880  CG  PHE A 173     -24.081 -32.334  -1.819  1.00 26.56           C  
ANISOU  880  CG  PHE A 173     3719   3381   2993    174   -168    301       C  
ATOM    881  CD1 PHE A 173     -23.412 -33.392  -2.415  1.00 27.42           C  
ANISOU  881  CD1 PHE A 173     3817   3540   3061    138   -131    264       C  
ATOM    882  CD2 PHE A 173     -23.458 -31.054  -1.783  1.00 25.11           C  
ANISOU  882  CD2 PHE A 173     3557   3149   2835    164   -172    345       C  
ATOM    883  CE1 PHE A 173     -22.096 -33.224  -2.970  1.00 25.20           C  
ANISOU  883  CE1 PHE A 173     3542   3269   2763     92    -96    266       C  
ATOM    884  CE2 PHE A 173     -22.194 -30.860  -2.357  1.00 26.47           C  
ANISOU  884  CE2 PHE A 173     3740   3333   2984    116   -143    355       C  
ATOM    885  CZ  PHE A 173     -21.508 -31.943  -2.966  1.00 25.13           C  
ANISOU  885  CZ  PHE A 173     3555   3221   2771     79   -103    315       C  
ATOM    886  N   ARG A 174     -26.892 -34.466  -3.938  1.00 22.73           N  
ANISOU  886  N   ARG A 174     3198   3065   2374    156   -214    283       N  
ATOM    887  CA  ARG A 174     -26.987 -35.804  -4.491  1.00 22.70           C  
ANISOU  887  CA  ARG A 174     3179   3122   2323    123   -187    224       C  
ATOM    888  C   ARG A 174     -25.602 -36.439  -4.506  1.00 25.61           C  
ANISOU  888  C   ARG A 174     3548   3488   2693     92   -125    174       C  
ATOM    889  O   ARG A 174     -24.593 -35.756  -4.700  1.00 26.30           O  
ANISOU  889  O   ARG A 174     3652   3561   2778     72   -109    199       O  
ATOM    890  CB  ARG A 174     -27.586 -35.705  -5.912  1.00 22.09           C  
ANISOU  890  CB  ARG A 174     3110   3125   2160     76   -219    261       C  
ATOM    891  CG  ARG A 174     -27.737 -36.991  -6.615  1.00 25.25           C  
ANISOU  891  CG  ARG A 174     3498   3594   2503     30   -189    194       C  
ATOM    892  CD  ARG A 174     -28.442 -36.744  -8.004  1.00 26.56           C  
ANISOU  892  CD  ARG A 174     3673   3850   2569    -25   -235    241       C  
ATOM    893  NE  ARG A 174     -28.368 -37.930  -8.865  1.00 25.25           N  
ANISOU  893  NE  ARG A 174     3502   3762   2330    -92   -193    164       N  
ATOM    894  CZ  ARG A 174     -29.168 -38.202  -9.900  1.00 28.33           C  
ANISOU  894  CZ  ARG A 174     3890   4243   2631   -147   -227    169       C  
ATOM    895  NH1 ARG A 174     -30.225 -37.440 -10.191  1.00 25.65           N  
ANISOU  895  NH1 ARG A 174     3546   3930   2270   -134   -314    256       N  
ATOM    896  NH2 ARG A 174     -28.912 -39.293 -10.655  1.00 31.03           N  
ANISOU  896  NH2 ARG A 174     4230   4651   2909   -217   -172     79       N  
ATOM    897  N   ALA A 175     -25.551 -37.755  -4.285  1.00 24.43           N  
ANISOU  897  N   ALA A 175     3375   3347   2558     89    -88    103       N  
ATOM    898  CA  ALA A 175     -24.260 -38.437  -4.195  1.00 22.98           C  
ANISOU  898  CA  ALA A 175     3179   3149   2405     71    -29     53       C  
ATOM    899  C   ALA A 175     -23.439 -38.246  -5.476  1.00 26.29           C  
ANISOU  899  C   ALA A 175     3610   3618   2762      7      7     48       C  
ATOM    900  O   ALA A 175     -22.227 -38.020  -5.434  1.00 25.31           O  
ANISOU  900  O   ALA A 175     3482   3473   2661     -8     43     43       O  
ATOM    901  CB  ALA A 175     -24.506 -39.930  -3.903  1.00 20.22           C  
ANISOU  901  CB  ALA A 175     2798   2795   2088     76      2    -18       C  
ATOM    902  N   SER A 176     -24.100 -38.300  -6.630  1.00 24.55           N  
ANISOU  902  N   SER A 176     3402   3469   2455    -39     -3     53       N  
ATOM    903  CA  SER A 176     -23.366 -38.212  -7.872  1.00 26.08           C  
ANISOU  903  CA  SER A 176     3611   3724   2574   -114     38     41       C  
ATOM    904  C   SER A 176     -22.805 -36.816  -8.159  1.00 26.36           C  
ANISOU  904  C   SER A 176     3677   3755   2582   -132     18    124       C  
ATOM    905  O   SER A 176     -22.010 -36.671  -9.098  1.00 26.55           O  
ANISOU  905  O   SER A 176     3714   3826   2547   -199     60    117       O  
ATOM    906  CB  SER A 176     -24.320 -38.671  -8.975  1.00 29.29           C  
ANISOU  906  CB  SER A 176     4025   4219   2883   -166     24     25       C  
ATOM    907  OG  SER A 176     -25.434 -37.798  -9.035  1.00 29.10           O  
ANISOU  907  OG  SER A 176     4018   4210   2829   -146    -61    113       O  
ATOM    908  N   TYR A 177     -23.185 -35.776  -7.393  1.00 22.27           N  
ANISOU  908  N   TYR A 177     3173   3180   2109    -78    -40    198       N  
ATOM    909  CA  TYR A 177     -22.505 -34.485  -7.555  1.00 25.74           C  
ANISOU  909  CA  TYR A 177     3639   3597   2544    -95    -50    269       C  
ATOM    910  C   TYR A 177     -20.997 -34.577  -7.248  1.00 25.59           C  
ANISOU  910  C   TYR A 177     3607   3548   2568   -111     14    228       C  
ATOM    911  O   TYR A 177     -20.207 -33.753  -7.751  1.00 24.96           O  
ANISOU  911  O   TYR A 177     3548   3473   2465   -155     30    268       O  
ATOM    912  CB  TYR A 177     -23.108 -33.431  -6.613  1.00 22.26           C  
ANISOU  912  CB  TYR A 177     3206   3081   2169    -30   -111    335       C  
ATOM    913  CG  TYR A 177     -24.523 -32.981  -6.864  1.00 25.77           C  
ANISOU  913  CG  TYR A 177     3658   3538   2597     -6   -182    396       C  
ATOM    914  CD1 TYR A 177     -25.146 -33.198  -8.080  1.00 26.05           C  
ANISOU  914  CD1 TYR A 177     3700   3657   2539    -55   -206    423       C  
ATOM    915  CD2 TYR A 177     -25.235 -32.258  -5.867  1.00 23.65           C  
ANISOU  915  CD2 TYR A 177     3381   3195   2408     62   -225    428       C  
ATOM    916  CE1 TYR A 177     -26.454 -32.726  -8.321  1.00 26.73           C  
ANISOU  916  CE1 TYR A 177     3783   3755   2619    -31   -283    491       C  
ATOM    917  CE2 TYR A 177     -26.544 -31.801  -6.099  1.00 24.67           C  
ANISOU  917  CE2 TYR A 177     3503   3328   2541     90   -290    485       C  
ATOM    918  CZ  TYR A 177     -27.141 -32.017  -7.321  1.00 26.42           C  
ANISOU  918  CZ  TYR A 177     3728   3632   2677     46   -323    523       C  
ATOM    919  OH  TYR A 177     -28.458 -31.568  -7.568  1.00 26.10           O  
ANISOU  919  OH  TYR A 177     3670   3598   2648     74   -398    588       O  
ATOM    920  N   MET A 178     -20.575 -35.532  -6.387  1.00 24.99           N  
ANISOU  920  N   MET A 178     3493   3436   2564    -77     47    156       N  
ATOM    921  CA  MET A 178     -19.149 -35.669  -6.089  1.00 26.34           C  
ANISOU  921  CA  MET A 178     3639   3581   2789    -90    101    120       C  
ATOM    922  C   MET A 178     -18.336 -35.972  -7.346  1.00 27.55           C  
ANISOU  922  C   MET A 178     3787   3796   2885   -167    170     81       C  
ATOM    923  O   MET A 178     -17.127 -35.703  -7.376  1.00 28.18           O  
ANISOU  923  O   MET A 178     3851   3863   2994   -193    214     70       O  
ATOM    924  CB  MET A 178     -18.895 -36.773  -5.050  1.00 28.57           C  
ANISOU  924  CB  MET A 178     3877   3820   3160    -43    117     58       C  
ATOM    925  CG  MET A 178     -19.320 -36.424  -3.609  1.00 31.47           C  
ANISOU  925  CG  MET A 178     4245   4125   3587     20     63     89       C  
ATOM    926  SD  MET A 178     -18.591 -34.831  -3.084  1.00 33.37           S  
ANISOU  926  SD  MET A 178     4508   4321   3851     19     38    151       S  
ATOM    927  CE  MET A 178     -18.501 -35.107  -1.353  1.00 35.51           C  
ANISOU  927  CE  MET A 178     4756   4535   4202     71     10    137       C  
ATOM    928  N   LYS A 179     -18.971 -36.466  -8.406  1.00 27.97           N  
ANISOU  928  N   LYS A 179     3854   3922   2852   -212    182     59       N  
ATOM    929  CA  LYS A 179     -18.226 -36.726  -9.647  1.00 30.50           C  
ANISOU  929  CA  LYS A 179     4174   4313   3103   -300    257     14       C  
ATOM    930  C   LYS A 179     -17.696 -35.464 -10.302  1.00 29.14           C  
ANISOU  930  C   LYS A 179     4039   4165   2867   -357    254     90       C  
ATOM    931  O   LYS A 179     -16.854 -35.568 -11.192  1.00 28.08           O  
ANISOU  931  O   LYS A 179     3903   4084   2684   -434    326     52       O  
ATOM    932  CB  LYS A 179     -19.064 -37.441 -10.682  1.00 34.68           C  
ANISOU  932  CB  LYS A 179     4717   4927   3534   -352    267    -25       C  
ATOM    933  CG  LYS A 179     -19.571 -38.792 -10.198  1.00 37.60           C  
ANISOU  933  CG  LYS A 179     5048   5275   3963   -311    282   -110       C  
ATOM    934  CD  LYS A 179     -20.378 -39.541 -11.305  1.00 39.92           C  
ANISOU  934  CD  LYS A 179     5353   5660   4154   -376    298   -164       C  
ATOM    935  CE  LYS A 179     -20.837 -40.921 -10.727  1.00 43.18           C  
ANISOU  935  CE  LYS A 179     5724   6033   4647   -333    318   -251       C  
ATOM    936  NZ  LYS A 179     -20.913 -41.966 -11.749  1.00 49.65           N  
ANISOU  936  NZ  LYS A 179     6533   6920   5412   -408    388   -359       N  
ATOM    937  N   LYS A 180     -18.173 -34.289  -9.907  1.00 27.66           N  
ANISOU  937  N   LYS A 180     3886   3939   2683   -325    179    192       N  
ATOM    938  CA  LYS A 180     -17.602 -33.071 -10.483  1.00 32.34           C  
ANISOU  938  CA  LYS A 180     4514   4542   3231   -380    179    270       C  
ATOM    939  C   LYS A 180     -16.176 -32.788  -9.981  1.00 33.58           C  
ANISOU  939  C   LYS A 180     4644   4650   3465   -385    233    244       C  
ATOM    940  O   LYS A 180     -15.414 -32.100 -10.666  1.00 31.68           O  
ANISOU  940  O   LYS A 180     4422   4434   3181   -454    266    276       O  
ATOM    941  CB  LYS A 180     -18.542 -31.915 -10.188  1.00 31.17           C  
ANISOU  941  CB  LYS A 180     4404   4353   3087   -341     85    384       C  
ATOM    942  CG  LYS A 180     -19.917 -32.121 -10.935  1.00 32.09           C  
ANISOU  942  CG  LYS A 180     4542   4535   3116   -352     28    422       C  
ATOM    943  CD  LYS A 180     -20.930 -31.116 -10.410  1.00 33.12           C  
ANISOU  943  CD  LYS A 180     4689   4604   3291   -289    -66    521       C  
ATOM    944  CE  LYS A 180     -22.390 -31.403 -10.840  1.00 32.28           C  
ANISOU  944  CE  LYS A 180     4584   4548   3133   -277   -133    553       C  
ATOM    945  NZ  LYS A 180     -22.578 -31.350 -12.273  1.00 34.75           N  
ANISOU  945  NZ  LYS A 180     4926   4966   3312   -369   -145    601       N  
ATOM    946  N   GLY A 181     -15.805 -33.295  -8.803  1.00 33.77           N  
ANISOU  946  N   GLY A 181     4624   4609   3599   -318    238    191       N  
ATOM    947  CA  GLY A 181     -14.379 -33.375  -8.492  1.00 32.39           C  
ANISOU  947  CA  GLY A 181     4405   4408   3495   -333    298    145       C  
ATOM    948  C   GLY A 181     -13.804 -32.003  -8.147  1.00 32.56           C  
ANISOU  948  C   GLY A 181     4447   4382   3541   -343    275    218       C  
ATOM    949  O   GLY A 181     -14.541 -31.030  -7.877  1.00 30.26           O  
ANISOU  949  O   GLY A 181     4200   4056   3240   -319    208    299       O  
ATOM    950  N   SER A 182     -12.455 -31.934  -8.151  1.00 29.44           N  
ANISOU  950  N   SER A 182     4014   3981   3190   -379    335    184       N  
ATOM    951  CA  SER A 182     -11.760 -30.752  -7.631  1.00 27.56           C  
ANISOU  951  CA  SER A 182     3784   3690   2998   -388    318    235       C  
ATOM    952  C   SER A 182     -11.851 -29.567  -8.569  1.00 29.09           C  
ANISOU  952  C   SER A 182     4038   3903   3111   -455    314    321       C  
ATOM    953  O   SER A 182     -11.565 -28.438  -8.144  1.00 31.73           O  
ANISOU  953  O   SER A 182     4392   4180   3482   -458    287    379       O  
ATOM    954  CB  SER A 182     -10.277 -31.054  -7.384  1.00 28.39           C  
ANISOU  954  CB  SER A 182     3821   3787   3179   -411    382    173       C  
ATOM    955  OG  SER A 182      -9.831 -31.473  -8.660  1.00 32.89           O  
ANISOU  955  OG  SER A 182     4383   4431   3684   -486    464    133       O  
ATOM    956  N   LYS A 183     -12.185 -29.770  -9.845  1.00 29.46           N  
ANISOU  956  N   LYS A 183     4115   4031   3049   -519    342    333       N  
ATOM    957  CA  LYS A 183     -12.321 -28.603 -10.717  1.00 32.35           C  
ANISOU  957  CA  LYS A 183     4542   4415   3333   -587    326    435       C  
ATOM    958  C   LYS A 183     -13.459 -27.699 -10.247  1.00 32.30           C  
ANISOU  958  C   LYS A 183     4582   4346   3345   -529    226    534       C  
ATOM    959  O   LYS A 183     -13.411 -26.485 -10.450  1.00 33.58           O  
ANISOU  959  O   LYS A 183     4784   4470   3504   -558    199    628       O  
ATOM    960  CB  LYS A 183     -12.559 -29.026 -12.178  1.00 35.05           C  
ANISOU  960  CB  LYS A 183     4911   4869   3537   -674    365    435       C  
ATOM    961  N   VAL A 184     -14.491 -28.273  -9.635  1.00 33.06           N  
ANISOU  961  N   VAL A 184     4669   4425   3467   -450    176    513       N  
ATOM    962  CA  VAL A 184     -15.630 -27.515  -9.154  1.00 25.77           C  
ANISOU  962  CA  VAL A 184     3777   3442   2573   -390     89    591       C  
ATOM    963  C   VAL A 184     -15.564 -27.331  -7.637  1.00 30.11           C  
ANISOU  963  C   VAL A 184     4301   3898   3242   -311     67    556       C  
ATOM    964  O   VAL A 184     -15.974 -26.293  -7.115  1.00 27.85           O  
ANISOU  964  O   VAL A 184     4037   3535   3009   -280     20    615       O  
ATOM    965  CB  VAL A 184     -16.957 -28.209  -9.571  1.00 25.67           C  
ANISOU  965  CB  VAL A 184     3772   3483   2500   -365     46    595       C  
ATOM    966  CG1 VAL A 184     -18.166 -27.454  -8.981  1.00 25.47           C  
ANISOU  966  CG1 VAL A 184     3764   3388   2527   -293    -41    668       C  
ATOM    967  CG2 VAL A 184     -17.129 -28.292 -11.139  1.00 26.70           C  
ANISOU  967  CG2 VAL A 184     3936   3719   2491   -457     57    640       C  
ATOM    968  N   MET A 185     -15.111 -28.338  -6.885  1.00 24.26           N  
ANISOU  968  N   MET A 185     3512   3159   2546   -279     97    462       N  
ATOM    969  CA  MET A 185     -15.207 -28.303  -5.409  1.00 23.51           C  
ANISOU  969  CA  MET A 185     3395   2992   2544   -210     67    431       C  
ATOM    970  C   MET A 185     -13.890 -28.765  -4.819  1.00 27.58           C  
ANISOU  970  C   MET A 185     3861   3502   3114   -222    112    364       C  
ATOM    971  O   MET A 185     -13.769 -29.888  -4.294  1.00 26.32           O  
ANISOU  971  O   MET A 185     3658   3357   2984   -189    124    298       O  
ATOM    972  CB  MET A 185     -16.372 -29.174  -4.916  1.00 22.87           C  
ANISOU  972  CB  MET A 185     3304   2919   2465   -145     32    400       C  
ATOM    973  CG  MET A 185     -17.800 -28.728  -5.384  1.00 29.85           C  
ANISOU  973  CG  MET A 185     4225   3807   3312   -123    -23    466       C  
ATOM    974  SD  MET A 185     -19.011 -30.017  -4.799  1.00 34.43           S  
ANISOU  974  SD  MET A 185     4779   4407   3895    -57    -47    408       S  
ATOM    975  CE  MET A 185     -18.717 -31.305  -6.015  1.00 34.00           C  
ANISOU  975  CE  MET A 185     4709   4452   3757   -111      4    359       C  
ATOM    976  N   PRO A 186     -12.857 -27.923  -4.893  1.00 25.36           N  
ANISOU  976  N   PRO A 186     3580   3199   2857   -269    137    383       N  
ATOM    977  CA  PRO A 186     -11.541 -28.412  -4.500  1.00 24.89           C  
ANISOU  977  CA  PRO A 186     3462   3146   2850   -288    182    321       C  
ATOM    978  C   PRO A 186     -11.432 -28.658  -3.006  1.00 27.90           C  
ANISOU  978  C   PRO A 186     3810   3482   3310   -233    144    285       C  
ATOM    979  O   PRO A 186     -10.751 -29.628  -2.615  1.00 24.54           O  
ANISOU  979  O   PRO A 186     3325   3074   2926   -222    164    229       O  
ATOM    980  CB  PRO A 186     -10.573 -27.306  -4.985  1.00 24.54           C  
ANISOU  980  CB  PRO A 186     3429   3088   2806   -360    213    358       C  
ATOM    981  CG  PRO A 186     -11.396 -26.115  -5.164  1.00 25.53           C  
ANISOU  981  CG  PRO A 186     3621   3170   2910   -360    169    442       C  
ATOM    982  CD  PRO A 186     -12.781 -26.634  -5.594  1.00 25.87           C  
ANISOU  982  CD  PRO A 186     3692   3244   2894   -321    134    463       C  
ATOM    983  N   ASN A 187     -12.087 -27.853  -2.145  1.00 22.90           N  
ANISOU  983  N   ASN A 187     3210   2792   2700   -201     92    313       N  
ATOM    984  CA  ASN A 187     -11.940 -28.145  -0.709  1.00 24.81           C  
ANISOU  984  CA  ASN A 187     3422   3006   2999   -163     60    273       C  
ATOM    985  C   ASN A 187     -12.668 -29.425  -0.341  1.00 21.84           C  
ANISOU  985  C   ASN A 187     3027   2656   2615   -110     44    241       C  
ATOM    986  O   ASN A 187     -12.158 -30.248   0.398  1.00 23.41           O  
ANISOU  986  O   ASN A 187     3178   2863   2853    -94     38    205       O  
ATOM    987  CB  ASN A 187     -12.490 -27.020   0.150  1.00 22.39           C  
ANISOU  987  CB  ASN A 187     3155   2636   2717   -148     19    294       C  
ATOM    988  CG  ASN A 187     -11.598 -25.803   0.149  1.00 27.24           C  
ANISOU  988  CG  ASN A 187     3778   3209   3362   -202     32    312       C  
ATOM    989  OD1 ASN A 187     -10.674 -25.688   0.962  1.00 26.03           O  
ANISOU  989  OD1 ASN A 187     3591   3047   3251   -224     30    280       O  
ATOM    990  ND2 ASN A 187     -11.892 -24.895  -0.720  1.00 26.49           N  
ANISOU  990  ND2 ASN A 187     3726   3089   3249   -226     41    368       N  
ATOM    991  N   ILE A 188     -13.891 -29.595  -0.831  1.00 21.66           N  
ANISOU  991  N   ILE A 188     3038   2645   2547    -83     31    260       N  
ATOM    992  CA  ILE A 188     -14.652 -30.816  -0.522  1.00 21.16           C  
ANISOU  992  CA  ILE A 188     2958   2605   2476    -38     19    229       C  
ATOM    993  C   ILE A 188     -13.967 -32.042  -1.106  1.00 22.00           C  
ANISOU  993  C   ILE A 188     3017   2755   2587    -51     64    187       C  
ATOM    994  O   ILE A 188     -13.947 -33.116  -0.500  1.00 24.17           O  
ANISOU  994  O   ILE A 188     3255   3033   2898    -21     59    152       O  
ATOM    995  CB  ILE A 188     -16.086 -30.657  -1.066  1.00 24.88           C  
ANISOU  995  CB  ILE A 188     3471   3083   2898    -14     -3    259       C  
ATOM    996  CG1 ILE A 188     -16.823 -29.563  -0.271  1.00 25.05           C  
ANISOU  996  CG1 ILE A 188     3526   3049   2944     12    -45    287       C  
ATOM    997  CG2 ILE A 188     -16.843 -31.998  -1.133  1.00 23.64           C  
ANISOU  997  CG2 ILE A 188     3296   2963   2723     17     -3    224       C  
ATOM    998  CD1 ILE A 188     -18.156 -29.080  -1.002  1.00 21.53           C  
ANISOU  998  CD1 ILE A 188     3115   2601   2465     31    -70    335       C  
ATOM    999  N   GLU A 189     -13.451 -31.929  -2.329  1.00 21.78           N  
ANISOU  999  N   GLU A 189     2989   2761   2524   -100    111    189       N  
ATOM   1000  CA  GLU A 189     -12.803 -33.094  -2.928  1.00 22.80           C  
ANISOU 1000  CA  GLU A 189     3068   2928   2666   -117    168    133       C  
ATOM   1001  C   GLU A 189     -11.526 -33.493  -2.174  1.00 26.62           C  
ANISOU 1001  C   GLU A 189     3483   3390   3240   -114    181    101       C  
ATOM   1002  O   GLU A 189     -11.213 -34.681  -2.104  1.00 28.01           O  
ANISOU 1002  O   GLU A 189     3605   3572   3466    -95    205     54       O  
ATOM   1003  CB  GLU A 189     -12.492 -32.817  -4.393  1.00 25.12           C  
ANISOU 1003  CB  GLU A 189     3378   3271   2893   -183    224    136       C  
ATOM   1004  CG  GLU A 189     -11.491 -33.842  -4.962  1.00 29.38           C  
ANISOU 1004  CG  GLU A 189     3855   3843   3465   -213    302     63       C  
ATOM   1005  CD  GLU A 189     -12.109 -35.240  -4.993  1.00 36.65           C  
ANISOU 1005  CD  GLU A 189     4751   4777   4397   -178    313      7       C  
ATOM   1006  OE1 GLU A 189     -13.329 -35.368  -4.839  1.00 39.26           O  
ANISOU 1006  OE1 GLU A 189     5121   5110   4688   -145    267     28       O  
ATOM   1007  OE2 GLU A 189     -11.389 -36.220  -5.180  1.00 41.03           O  
ANISOU 1007  OE2 GLU A 189     5244   5335   5010   -182    369    -60       O  
ATOM   1008  N   LYS A 190     -10.797 -32.537  -1.553  1.00 24.48           N  
ANISOU 1008  N   LYS A 190     3209   3090   3002   -130    161    125       N  
ATOM   1009  CA  LYS A 190      -9.663 -32.932  -0.723  1.00 24.44           C  
ANISOU 1009  CA  LYS A 190     3133   3069   3084   -125    156    102       C  
ATOM   1010  C   LYS A 190     -10.113 -33.597   0.593  1.00 22.94           C  
ANISOU 1010  C   LYS A 190     2928   2856   2932    -70     95    103       C  
ATOM   1011  O   LYS A 190      -9.520 -34.600   1.019  1.00 22.31           O  
ANISOU 1011  O   LYS A 190     2782   2773   2922    -51     94     82       O  
ATOM   1012  CB  LYS A 190      -8.788 -31.718  -0.420  1.00 26.64           C  
ANISOU 1012  CB  LYS A 190     3413   3329   3382   -167    149    125       C  
ATOM   1013  CG  LYS A 190      -7.629 -32.058   0.529  1.00 27.26           C  
ANISOU 1013  CG  LYS A 190     3412   3395   3549   -165    129    107       C  
ATOM   1014  CD  LYS A 190      -6.811 -30.807   0.927  1.00 28.85           C  
ANISOU 1014  CD  LYS A 190     3615   3580   3768   -213    116    125       C  
ATOM   1015  CE  LYS A 190      -5.738 -31.158   1.961  1.00 31.71           C  
ANISOU 1015  CE  LYS A 190     3896   3939   4213   -213     80    114       C  
ATOM   1016  NZ  LYS A 190      -5.044 -29.901   2.401  1.00 30.55           N  
ANISOU 1016  NZ  LYS A 190     3755   3777   4076   -266     63    126       N  
ATOM   1017  N   LEU A 191     -11.123 -33.042   1.269  1.00 22.26           N  
ANISOU 1017  N   LEU A 191     2899   2752   2805    -49     45    131       N  
ATOM   1018  CA  LEU A 191     -11.725 -33.742   2.426  1.00 22.99           C  
ANISOU 1018  CA  LEU A 191     2986   2834   2914     -5     -5    131       C  
ATOM   1019  C   LEU A 191     -12.107 -35.181   2.054  1.00 21.76           C  
ANISOU 1019  C   LEU A 191     2802   2692   2775     26     16    107       C  
ATOM   1020  O   LEU A 191     -11.784 -36.142   2.772  1.00 22.81           O  
ANISOU 1020  O   LEU A 191     2886   2815   2966     49     -4    102       O  
ATOM   1021  CB  LEU A 191     -12.992 -33.006   2.908  1.00 23.98           C  
ANISOU 1021  CB  LEU A 191     3180   2945   2986     12    -40    151       C  
ATOM   1022  CG  LEU A 191     -12.951 -31.630   3.578  1.00 26.00           C  
ANISOU 1022  CG  LEU A 191     3472   3173   3234    -10    -66    166       C  
ATOM   1023  CD1 LEU A 191     -14.377 -31.242   3.932  1.00 26.65           C  
ANISOU 1023  CD1 LEU A 191     3607   3238   3280     19    -87    171       C  
ATOM   1024  CD2 LEU A 191     -12.063 -31.778   4.875  1.00 24.63           C  
ANISOU 1024  CD2 LEU A 191     3258   2999   3101    -24   -103    158       C  
ATOM   1025  N   ARG A 192     -12.743 -35.343   0.904  1.00 23.20           N  
ANISOU 1025  N   ARG A 192     3010   2895   2909     22     56     93       N  
ATOM   1026  CA  ARG A 192     -13.245 -36.672   0.511  1.00 25.87           C  
ANISOU 1026  CA  ARG A 192     3328   3244   3258     45     80     59       C  
ATOM   1027  C   ARG A 192     -12.100 -37.638   0.211  1.00 27.29           C  
ANISOU 1027  C   ARG A 192     3429   3419   3520     39    125     19       C  
ATOM   1028  O   ARG A 192     -12.147 -38.822   0.586  1.00 27.35           O  
ANISOU 1028  O   ARG A 192     3396   3407   3589     71    123      1       O  
ATOM   1029  CB  ARG A 192     -14.155 -36.541  -0.733  1.00 25.06           C  
ANISOU 1029  CB  ARG A 192     3272   3177   3074     28    110     50       C  
ATOM   1030  CG  ARG A 192     -14.807 -37.880  -1.195  1.00 26.31           C  
ANISOU 1030  CG  ARG A 192     3413   3349   3232     44    137      6       C  
ATOM   1031  CD  ARG A 192     -15.276 -37.774  -2.685  1.00 33.76           C  
ANISOU 1031  CD  ARG A 192     4389   4347   4093      2    180    -13       C  
ATOM   1032  NE  ARG A 192     -14.083 -37.795  -3.571  1.00 39.51           N  
ANISOU 1032  NE  ARG A 192     5084   5096   4833    -47    249    -49       N  
ATOM   1033  CZ  ARG A 192     -13.411 -38.889  -3.940  1.00 42.38           C  
ANISOU 1033  CZ  ARG A 192     5388   5458   5257    -56    311   -118       C  
ATOM   1034  NH1 ARG A 192     -13.814 -40.103  -3.557  1.00 46.15           N  
ANISOU 1034  NH1 ARG A 192     5835   5910   5789    -18    311   -153       N  
ATOM   1035  NH2 ARG A 192     -12.329 -38.792  -4.689  1.00 41.02           N  
ANISOU 1035  NH2 ARG A 192     5182   5305   5098   -103    378   -154       N  
ATOM   1036  N   SER A 193     -11.071 -37.169  -0.483  1.00 24.11           N  
ANISOU 1036  N   SER A 193     3002   3030   3130     -1    171      4       N  
ATOM   1037  CA  SER A 193     -10.049 -38.122  -0.856  1.00 26.41           C  
ANISOU 1037  CA  SER A 193     3211   3314   3510     -5    226    -45       C  
ATOM   1038  C   SER A 193      -9.012 -38.342   0.252  1.00 27.13           C  
ANISOU 1038  C   SER A 193     3229   3370   3708     16    186    -26       C  
ATOM   1039  O   SER A 193      -8.434 -39.436   0.320  1.00 27.47           O  
ANISOU 1039  O   SER A 193     3195   3388   3854     38    208    -54       O  
ATOM   1040  CB  SER A 193      -9.386 -37.669  -2.153  1.00 28.82           C  
ANISOU 1040  CB  SER A 193     3510   3655   3783    -65    306    -80       C  
ATOM   1041  OG  SER A 193      -8.830 -36.388  -1.983  1.00 29.09           O  
ANISOU 1041  OG  SER A 193     3565   3693   3796    -97    287    -40       O  
ATOM   1042  N   CYS A 194      -8.786 -37.360   1.146  1.00 23.73           N  
ANISOU 1042  N   CYS A 194     2818   2934   3262      8    126     23       N  
ATOM   1043  CA  CYS A 194      -7.839 -37.547   2.259  1.00 27.87           C  
ANISOU 1043  CA  CYS A 194     3275   3437   3876     19     74     49       C  
ATOM   1044  C   CYS A 194      -8.456 -38.217   3.487  1.00 25.24           C  
ANISOU 1044  C   CYS A 194     2947   3086   3557     61     -1     87       C  
ATOM   1045  O   CYS A 194      -7.723 -38.863   4.261  1.00 22.61           O  
ANISOU 1045  O   CYS A 194     2542   2734   3315     77    -41    110       O  
ATOM   1046  CB  CYS A 194      -7.181 -36.195   2.644  1.00 39.61           C  
ANISOU 1046  CB  CYS A 194     4775   4934   5340    -23     48     74       C  
ATOM   1047  SG  CYS A 194      -6.336 -35.869   1.073  1.00 54.81           S  
ANISOU 1047  SG  CYS A 194     6674   6880   7272    -72    151     26       S  
ATOM   1048  N   GLY A 195      -9.750 -38.077   3.676  1.00 22.84           N  
ANISOU 1048  N   GLY A 195     2720   2789   3170     74    -21     98       N  
ATOM   1049  CA  GLY A 195     -10.458 -38.607   4.821  1.00 21.32           C  
ANISOU 1049  CA  GLY A 195     2543   2586   2972    102    -84    133       C  
ATOM   1050  C   GLY A 195     -11.050 -39.963   4.492  1.00 25.86           C  
ANISOU 1050  C   GLY A 195     3101   3142   3584    137    -60    115       C  
ATOM   1051  O   GLY A 195     -10.496 -40.743   3.683  1.00 24.05           O  
ANISOU 1051  O   GLY A 195     2814   2897   3428    145     -5     77       O  
ATOM   1052  N   THR A 196     -12.197 -40.234   5.120  1.00 22.11           N  
ANISOU 1052  N   THR A 196     2673   2667   3059    155    -94    135       N  
ATOM   1053  CA  THR A 196     -12.955 -41.467   4.945  1.00 22.31           C  
ANISOU 1053  CA  THR A 196     2693   2673   3110    184    -78    122       C  
ATOM   1054  C   THR A 196     -14.251 -41.081   4.235  1.00 26.07           C  
ANISOU 1054  C   THR A 196     3241   3175   3491    181    -48     93       C  
ATOM   1055  O   THR A 196     -14.908 -40.108   4.649  1.00 24.76           O  
ANISOU 1055  O   THR A 196     3132   3028   3246    172    -77    111       O  
ATOM   1056  CB  THR A 196     -13.288 -42.091   6.318  1.00 25.68           C  
ANISOU 1056  CB  THR A 196     3118   3085   3554    199   -146    177       C  
ATOM   1057  OG1 THR A 196     -12.103 -42.525   6.976  1.00 25.59           O  
ANISOU 1057  OG1 THR A 196     3033   3052   3637    202   -185    217       O  
ATOM   1058  CG2 THR A 196     -14.236 -43.298   6.179  1.00 26.77           C  
ANISOU 1058  CG2 THR A 196     3260   3199   3712    224   -128    166       C  
ATOM   1059  N   HIS A 197     -14.630 -41.820   3.173  1.00 23.14           N  
ANISOU 1059  N   HIS A 197     2862   2802   3128    185      8     45       N  
ATOM   1060  CA  HIS A 197     -15.843 -41.464   2.454  1.00 21.74           C  
ANISOU 1060  CA  HIS A 197     2745   2657   2859    178     27     23       C  
ATOM   1061  C   HIS A 197     -16.543 -42.741   2.006  1.00 21.95           C  
ANISOU 1061  C   HIS A 197     2758   2672   2908    190     59    -16       C  
ATOM   1062  O   HIS A 197     -15.904 -43.796   1.872  1.00 23.30           O  
ANISOU 1062  O   HIS A 197     2872   2809   3171    198     89    -42       O  
ATOM   1063  CB  HIS A 197     -15.566 -40.592   1.233  1.00 20.15           C  
ANISOU 1063  CB  HIS A 197     2563   2489   2603    144     70      0       C  
ATOM   1064  CG  HIS A 197     -15.138 -41.373   0.025  1.00 26.17           C  
ANISOU 1064  CG  HIS A 197     3290   3261   3394    125    143    -62       C  
ATOM   1065  ND1 HIS A 197     -13.850 -41.866  -0.133  1.00 27.37           N  
ANISOU 1065  ND1 HIS A 197     3372   3390   3638    120    182    -90       N  
ATOM   1066  CD2 HIS A 197     -15.820 -41.726  -1.096  1.00 27.45           C  
ANISOU 1066  CD2 HIS A 197     3471   3456   3502    104    187   -108       C  
ATOM   1067  CE1 HIS A 197     -13.774 -42.529  -1.283  1.00 28.39           C  
ANISOU 1067  CE1 HIS A 197     3480   3532   3773     97    256   -159       C  
ATOM   1068  NE2 HIS A 197     -14.949 -42.444  -1.885  1.00 28.32           N  
ANISOU 1068  NE2 HIS A 197     3528   3563   3669     83    259   -171       N  
ATOM   1069  N   ALA A 198     -17.915 -42.658   1.906  1.00 20.68           N  
ANISOU 1069  N   ALA A 198     2648   2536   2674    193     47    -17       N  
ATOM   1070  CA  ALA A 198     -18.767 -43.681   1.261  1.00 23.48           C  
ANISOU 1070  CA  ALA A 198     3001   2894   3028    192     81    -63       C  
ATOM   1071  C   ALA A 198     -19.122 -43.245  -0.158  1.00 25.02           C  
ANISOU 1071  C   ALA A 198     3221   3141   3145    158    120   -104       C  
ATOM   1072  O   ALA A 198     -19.286 -42.043  -0.406  1.00 24.24           O  
ANISOU 1072  O   ALA A 198     3161   3075   2975    146    100    -74       O  
ATOM   1073  CB  ALA A 198     -20.070 -43.865   2.044  1.00 22.73           C  
ANISOU 1073  CB  ALA A 198     2937   2799   2900    209     40    -39       C  
ATOM   1074  N   PRO A 199     -19.237 -44.146  -1.122  1.00 25.74           N  
ANISOU 1074  N   PRO A 199     3292   3242   3243    137    175   -168       N  
ATOM   1075  CA  PRO A 199     -19.746 -43.712  -2.440  1.00 26.03           C  
ANISOU 1075  CA  PRO A 199     3363   3346   3182     94    201   -199       C  
ATOM   1076  C   PRO A 199     -21.125 -43.074  -2.347  1.00 23.85           C  
ANISOU 1076  C   PRO A 199     3136   3105   2822    100    147   -159       C  
ATOM   1077  O   PRO A 199     -21.399 -42.152  -3.115  1.00 24.39           O  
ANISOU 1077  O   PRO A 199     3237   3223   2807     74    137   -139       O  
ATOM   1078  CB  PRO A 199     -19.781 -44.998  -3.289  1.00 28.98           C  
ANISOU 1078  CB  PRO A 199     3704   3722   3584     67    268   -287       C  
ATOM   1079  CG  PRO A 199     -19.368 -46.113  -2.368  1.00 31.13           C  
ANISOU 1079  CG  PRO A 199     3926   3915   3986    105    275   -296       C  
ATOM   1080  CD  PRO A 199     -18.811 -45.552  -1.092  1.00 28.53           C  
ANISOU 1080  CD  PRO A 199     3592   3547   3701    145    217   -217       C  
ATOM   1081  N   TYR A 200     -21.943 -43.437  -1.349  1.00 20.29           N  
ANISOU 1081  N   TYR A 200     2687   2626   2396    136    109   -138       N  
ATOM   1082  CA  TYR A 200     -23.179 -42.706  -1.100  1.00 22.36           C  
ANISOU 1082  CA  TYR A 200     2986   2914   2597    148     59    -99       C  
ATOM   1083  C   TYR A 200     -23.647 -43.114   0.291  1.00 23.49           C  
ANISOU 1083  C   TYR A 200     3123   3015   2787    184     29    -77       C  
ATOM   1084  O   TYR A 200     -23.209 -44.135   0.840  1.00 22.69           O  
ANISOU 1084  O   TYR A 200     2993   2873   2756    193     45    -91       O  
ATOM   1085  CB  TYR A 200     -24.282 -42.973  -2.162  1.00 24.09           C  
ANISOU 1085  CB  TYR A 200     3216   3190   2749    120     64   -130       C  
ATOM   1086  CG  TYR A 200     -24.830 -44.383  -2.159  1.00 24.74           C  
ANISOU 1086  CG  TYR A 200     3273   3261   2866    115     90   -186       C  
ATOM   1087  CD1 TYR A 200     -25.796 -44.725  -1.273  1.00 26.94           C  
ANISOU 1087  CD1 TYR A 200     3551   3520   3165    141     62   -172       C  
ATOM   1088  CD2 TYR A 200     -24.411 -45.333  -3.090  1.00 30.39           C  
ANISOU 1088  CD2 TYR A 200     3967   3987   3593     77    150   -259       C  
ATOM   1089  CE1 TYR A 200     -26.333 -46.004  -1.236  1.00 31.90           C  
ANISOU 1089  CE1 TYR A 200     4158   4133   3830    133     85   -219       C  
ATOM   1090  CE2 TYR A 200     -24.973 -46.639  -3.086  1.00 31.67           C  
ANISOU 1090  CE2 TYR A 200     4105   4130   3797     69    177   -316       C  
ATOM   1091  CZ  TYR A 200     -25.923 -46.935  -2.151  1.00 34.46           C  
ANISOU 1091  CZ  TYR A 200     4461   4460   4173     97    141   -289       C  
ATOM   1092  OH  TYR A 200     -26.536 -48.177  -2.038  1.00 41.53           O  
ANISOU 1092  OH  TYR A 200     5336   5330   5114     89    164   -336       O  
ATOM   1093  N   MET A 201     -24.572 -42.338   0.818  1.00 18.78           N  
ANISOU 1093  N   MET A 201     2553   2429   2155    201    -11    -43       N  
ATOM   1094  CA  MET A 201     -25.237 -42.630   2.086  1.00 19.81           C  
ANISOU 1094  CA  MET A 201     2683   2534   2308    224    -34    -28       C  
ATOM   1095  C   MET A 201     -26.749 -42.650   1.849  1.00 21.70           C  
ANISOU 1095  C   MET A 201     2929   2805   2510    226    -47    -39       C  
ATOM   1096  O   MET A 201     -27.290 -41.785   1.146  1.00 21.72           O  
ANISOU 1096  O   MET A 201     2945   2840   2467    225    -64    -28       O  
ATOM   1097  CB  MET A 201     -24.857 -41.599   3.162  1.00 19.44           C  
ANISOU 1097  CB  MET A 201     2654   2468   2263    238    -64     14       C  
ATOM   1098  CG  MET A 201     -25.539 -41.847   4.514  1.00 20.68           C  
ANISOU 1098  CG  MET A 201     2816   2611   2429    248    -83     26       C  
ATOM   1099  SD  MET A 201     -25.089 -40.645   5.802  1.00 25.64           S  
ANISOU 1099  SD  MET A 201     3467   3226   3048    250   -111     58       S  
ATOM   1100  CE  MET A 201     -26.013 -39.210   5.125  1.00 23.84           C  
ANISOU 1100  CE  MET A 201     3261   3014   2784    263   -117     54       C  
ATOM   1101  N   ARG A 202     -27.408 -43.642   2.392  1.00 20.64           N  
ANISOU 1101  N   ARG A 202     2782   2660   2401    227    -41    -56       N  
ATOM   1102  CA  ARG A 202     -28.839 -43.803   2.119  1.00 22.35           C  
ANISOU 1102  CA  ARG A 202     2995   2908   2590    225    -48    -74       C  
ATOM   1103  C   ARG A 202     -29.661 -42.969   3.108  1.00 20.96           C  
ANISOU 1103  C   ARG A 202     2829   2731   2405    247    -75    -48       C  
ATOM   1104  O   ARG A 202     -29.487 -43.125   4.328  1.00 19.81           O  
ANISOU 1104  O   ARG A 202     2688   2557   2282    252    -75    -34       O  
ATOM   1105  CB  ARG A 202     -29.262 -45.282   2.202  1.00 21.36           C  
ANISOU 1105  CB  ARG A 202     2848   2770   2499    209    -23   -110       C  
ATOM   1106  CG  ARG A 202     -30.862 -45.531   2.043  1.00 21.45           C  
ANISOU 1106  CG  ARG A 202     2847   2816   2487    202    -31   -133       C  
ATOM   1107  CD  ARG A 202     -31.181 -47.134   2.115  1.00 23.47           C  
ANISOU 1107  CD  ARG A 202     3082   3048   2787    178      2   -174       C  
ATOM   1108  NE  ARG A 202     -30.275 -47.799   1.187  1.00 24.18           N  
ANISOU 1108  NE  ARG A 202     3163   3127   2898    157     35   -212       N  
ATOM   1109  CZ  ARG A 202     -29.438 -48.755   1.562  1.00 25.06           C  
ANISOU 1109  CZ  ARG A 202     3261   3179   3082    156     64   -219       C  
ATOM   1110  NH1 ARG A 202     -29.469 -49.219   2.822  1.00 24.53           N  
ANISOU 1110  NH1 ARG A 202     3192   3064   3063    169     55   -180       N  
ATOM   1111  NH2 ARG A 202     -28.593 -49.244   0.677  1.00 22.79           N  
ANISOU 1111  NH2 ARG A 202     2959   2879   2821    140    102   -263       N  
ATOM   1112  N   PRO A 203     -30.555 -42.078   2.648  1.00 18.47           N  
ANISOU 1112  N   PRO A 203     2513   2444   2061    258    -97    -40       N  
ATOM   1113  CA  PRO A 203     -31.424 -41.317   3.577  1.00 19.23           C  
ANISOU 1113  CA  PRO A 203     2609   2532   2165    281   -111    -30       C  
ATOM   1114  C   PRO A 203     -32.568 -42.194   4.103  1.00 20.41           C  
ANISOU 1114  C   PRO A 203     2737   2692   2327    275    -99    -57       C  
ATOM   1115  O   PRO A 203     -32.707 -43.340   3.721  1.00 21.07           O  
ANISOU 1115  O   PRO A 203     2807   2784   2413    254    -85    -81       O  
ATOM   1116  CB  PRO A 203     -31.989 -40.180   2.733  1.00 18.69           C  
ANISOU 1116  CB  PRO A 203     2537   2484   2082    297   -141     -9       C  
ATOM   1117  CG  PRO A 203     -31.979 -40.757   1.221  1.00 18.95           C  
ANISOU 1117  CG  PRO A 203     2561   2562   2076    270   -146    -17       C  
ATOM   1118  CD  PRO A 203     -30.706 -41.674   1.229  1.00 18.94           C  
ANISOU 1118  CD  PRO A 203     2571   2544   2081    247   -111    -38       C  
ATOM   1119  N   VAL A 204     -33.389 -41.644   5.014  1.00 19.52           N  
ANISOU 1119  N   VAL A 204     2618   2575   2225    289    -99    -60       N  
ATOM   1120  CA  VAL A 204     -34.621 -42.340   5.387  1.00 21.26           C  
ANISOU 1120  CA  VAL A 204     2810   2812   2455    280    -85    -88       C  
ATOM   1121  C   VAL A 204     -35.779 -41.842   4.520  1.00 21.97           C  
ANISOU 1121  C   VAL A 204     2865   2934   2548    297   -109    -95       C  
ATOM   1122  O   VAL A 204     -35.802 -40.717   3.982  1.00 22.33           O  
ANISOU 1122  O   VAL A 204     2908   2980   2596    322   -137    -71       O  
ATOM   1123  CB  VAL A 204     -35.031 -42.189   6.887  1.00 21.40           C  
ANISOU 1123  CB  VAL A 204     2832   2817   2481    275    -62    -98       C  
ATOM   1124  CG1 VAL A 204     -34.132 -42.943   7.827  1.00 19.27           C  
ANISOU 1124  CG1 VAL A 204     2590   2527   2203    247    -48    -83       C  
ATOM   1125  CG2 VAL A 204     -35.155 -40.656   7.294  1.00 18.89           C  
ANISOU 1125  CG2 VAL A 204     2518   2485   2174    302    -67    -98       C  
ATOM   1126  N   TYR A 205     -36.827 -42.641   4.496  1.00 20.72           N  
ANISOU 1126  N   TYR A 205     2674   2800   2397    282    -99   -124       N  
ATOM   1127  CA  TYR A 205     -38.046 -42.254   3.768  1.00 22.06           C  
ANISOU 1127  CA  TYR A 205     2797   3006   2577    295   -128   -129       C  
ATOM   1128  C   TYR A 205     -38.984 -41.492   4.740  1.00 23.98           C  
ANISOU 1128  C   TYR A 205     3012   3236   2863    321   -115   -142       C  
ATOM   1129  O   TYR A 205     -39.089 -41.848   5.908  1.00 23.84           O  
ANISOU 1129  O   TYR A 205     3002   3204   2853    307    -74   -166       O  
ATOM   1130  CB  TYR A 205     -38.759 -43.516   3.232  1.00 20.91           C  
ANISOU 1130  CB  TYR A 205     2624   2898   2424    260   -122   -163       C  
ATOM   1131  CG  TYR A 205     -40.042 -43.193   2.417  1.00 22.25           C  
ANISOU 1131  CG  TYR A 205     2738   3117   2601    266   -162   -166       C  
ATOM   1132  CD1 TYR A 205     -39.934 -42.784   1.121  1.00 22.34           C  
ANISOU 1132  CD1 TYR A 205     2744   3164   2578    264   -210   -139       C  
ATOM   1133  CD2 TYR A 205     -41.330 -43.270   2.992  1.00 22.15           C  
ANISOU 1133  CD2 TYR A 205     2672   3114   2628    272   -151   -192       C  
ATOM   1134  CE1 TYR A 205     -41.064 -42.437   0.347  1.00 24.57           C  
ANISOU 1134  CE1 TYR A 205     2972   3496   2865    269   -261   -126       C  
ATOM   1135  CE2 TYR A 205     -42.483 -42.961   2.230  1.00 22.48           C  
ANISOU 1135  CE2 TYR A 205     2652   3202   2687    280   -196   -189       C  
ATOM   1136  CZ  TYR A 205     -42.339 -42.570   0.904  1.00 23.67           C  
ANISOU 1136  CZ  TYR A 205     2799   3391   2802    278   -255   -153       C  
ATOM   1137  OH  TYR A 205     -43.434 -42.238   0.136  1.00 22.39           O  
ANISOU 1137  OH  TYR A 205     2574   3279   2654    284   -312   -136       O  
ATOM   1138  N   PRO A 206     -39.680 -40.447   4.260  1.00 26.00           N  
ANISOU 1138  N   PRO A 206     3231   3497   3151    357   -148   -126       N  
ATOM   1139  CA  PRO A 206     -39.646 -39.818   2.936  1.00 24.69           C  
ANISOU 1139  CA  PRO A 206     3054   3351   2975    373   -206    -81       C  
ATOM   1140  C   PRO A 206     -38.371 -39.018   2.769  1.00 21.29           C  
ANISOU 1140  C   PRO A 206     2675   2887   2527    383   -215    -42       C  
ATOM   1141  O   PRO A 206     -37.832 -38.489   3.764  1.00 20.37           O  
ANISOU 1141  O   PRO A 206     2584   2724   2430    395   -185    -50       O  
ATOM   1142  CB  PRO A 206     -40.896 -38.894   2.938  1.00 27.80           C  
ANISOU 1142  CB  PRO A 206     3384   3742   3437    414   -232    -73       C  
ATOM   1143  CG  PRO A 206     -41.201 -38.636   4.294  1.00 27.45           C  
ANISOU 1143  CG  PRO A 206     3331   3660   3439    428   -179   -115       C  
ATOM   1144  CD  PRO A 206     -40.626 -39.773   5.172  1.00 26.75           C  
ANISOU 1144  CD  PRO A 206     3286   3573   3304    383   -126   -152       C  
ATOM   1145  N   THR A 207     -37.866 -38.931   1.536  1.00 22.22           N  
ANISOU 1145  N   THR A 207     2808   3032   2602    370   -252     -5       N  
ATOM   1146  CA  THR A 207     -36.551 -38.320   1.337  1.00 21.05           C  
ANISOU 1146  CA  THR A 207     2711   2857   2432    369   -253     29       C  
ATOM   1147  C   THR A 207     -36.687 -36.796   1.264  1.00 20.96           C  
ANISOU 1147  C   THR A 207     2692   2807   2465    409   -284     77       C  
ATOM   1148  O   THR A 207     -36.416 -36.160   0.249  1.00 22.04           O  
ANISOU 1148  O   THR A 207     2838   2955   2582    407   -326    133       O  
ATOM   1149  CB  THR A 207     -35.860 -38.940   0.129  1.00 22.01           C  
ANISOU 1149  CB  THR A 207     2854   3023   2486    327   -264     38       C  
ATOM   1150  OG1 THR A 207     -36.732 -38.989  -1.020  1.00 21.75           O  
ANISOU 1150  OG1 THR A 207     2789   3050   2424    313   -311     58       O  
ATOM   1151  CG2 THR A 207     -35.385 -40.408   0.507  1.00 23.91           C  
ANISOU 1151  CG2 THR A 207     3108   3268   2710    293   -215    -17       C  
ATOM   1152  N   LYS A 208     -37.220 -36.244   2.355  1.00 20.69           N  
ANISOU 1152  N   LYS A 208     2638   2728   2496    442   -262     53       N  
ATOM   1153  CA  LYS A 208     -37.461 -34.813   2.574  1.00 21.15           C  
ANISOU 1153  CA  LYS A 208     2681   2729   2626    485   -276     80       C  
ATOM   1154  C   LYS A 208     -36.535 -34.328   3.695  1.00 24.77           C  
ANISOU 1154  C   LYS A 208     3182   3133   3097    483   -229     51       C  
ATOM   1155  O   LYS A 208     -35.931 -35.113   4.417  1.00 22.05           O  
ANISOU 1155  O   LYS A 208     2867   2799   2711    453   -191     14       O  
ATOM   1156  CB  LYS A 208     -38.933 -34.575   2.957  1.00 21.71           C  
ANISOU 1156  CB  LYS A 208     2682   2792   2774    520   -277     56       C  
ATOM   1157  CG  LYS A 208     -39.911 -35.034   1.912  1.00 27.98           C  
ANISOU 1157  CG  LYS A 208     3426   3646   3560    518   -330     83       C  
ATOM   1158  CD  LYS A 208     -40.244 -33.838   1.026  1.00 29.27           C  
ANISOU 1158  CD  LYS A 208     3559   3787   3775    555   -398    164       C  
ATOM   1159  CE  LYS A 208     -41.289 -34.199  -0.077  1.00 30.34           C  
ANISOU 1159  CE  LYS A 208     3636   3991   3900    550   -468    204       C  
ATOM   1160  NZ  LYS A 208     -41.585 -32.932  -0.875  1.00 32.12           N  
ANISOU 1160  NZ  LYS A 208     3831   4187   4185    588   -543    301       N  
ATOM   1161  N   THR A 209     -36.490 -33.011   3.882  1.00 23.91           N  
ANISOU 1161  N   THR A 209     3070   2961   3052    514   -233     69       N  
ATOM   1162  CA  THR A 209     -35.438 -32.393   4.683  1.00 23.77           C  
ANISOU 1162  CA  THR A 209     3097   2895   3038    504   -199     51       C  
ATOM   1163  C   THR A 209     -35.616 -32.632   6.187  1.00 25.28           C  
ANISOU 1163  C   THR A 209     3290   3077   3237    490   -140    -28       C  
ATOM   1164  O   THR A 209     -34.714 -33.138   6.848  1.00 25.02           O  
ANISOU 1164  O   THR A 209     3298   3057   3150    453   -116    -49       O  
ATOM   1165  CB  THR A 209     -35.446 -30.873   4.407  1.00 28.68           C  
ANISOU 1165  CB  THR A 209     3712   3445   3740    539   -219     89       C  
ATOM   1166  OG1 THR A 209     -35.163 -30.616   3.036  1.00 31.87           O  
ANISOU 1166  OG1 THR A 209     4124   3863   4122    539   -276    174       O  
ATOM   1167  CG2 THR A 209     -34.413 -30.222   5.289  1.00 29.82           C  
ANISOU 1167  CG2 THR A 209     3900   3539   3891    521   -180     59       C  
ATOM   1168  N   PHE A 210     -36.752 -32.211   6.771  1.00 24.41           N  
ANISOU 1168  N   PHE A 210     3134   2944   3198    517   -115    -71       N  
ATOM   1169  CA  PHE A 210     -36.880 -32.329   8.230  1.00 25.71           C  
ANISOU 1169  CA  PHE A 210     3305   3104   3360    492    -50   -151       C  
ATOM   1170  C   PHE A 210     -36.831 -33.765   8.732  1.00 22.87           C  
ANISOU 1170  C   PHE A 210     2962   2810   2919    447    -32   -172       C  
ATOM   1171  O   PHE A 210     -36.223 -33.998   9.796  1.00 20.82           O  
ANISOU 1171  O   PHE A 210     2740   2558   2614    406      3   -205       O  
ATOM   1172  CB  PHE A 210     -38.168 -31.666   8.725  1.00 32.43           C  
ANISOU 1172  CB  PHE A 210     4095   3922   4307    525    -16   -204       C  
ATOM   1173  CG  PHE A 210     -38.033 -30.180   8.946  1.00 43.43           C  
ANISOU 1173  CG  PHE A 210     5482   5229   5790    554      0   -219       C  
ATOM   1174  CD1 PHE A 210     -37.191 -29.417   8.150  1.00 45.86           C  
ANISOU 1174  CD1 PHE A 210     5819   5494   6112    569    -44   -152       C  
ATOM   1175  CD2 PHE A 210     -38.746 -29.548   9.969  1.00 50.41           C  
ANISOU 1175  CD2 PHE A 210     6332   6073   6749    561     66   -307       C  
ATOM   1176  CE1 PHE A 210     -37.057 -28.046   8.330  1.00 51.57           C  
ANISOU 1176  CE1 PHE A 210     6538   6129   6930    594    -29   -163       C  
ATOM   1177  CE2 PHE A 210     -38.628 -28.164  10.169  1.00 55.12           C  
ANISOU 1177  CE2 PHE A 210     6920   6579   7444    587     87   -330       C  
ATOM   1178  CZ  PHE A 210     -37.769 -27.411   9.339  1.00 55.06           C  
ANISOU 1178  CZ  PHE A 210     6943   6521   7457    605     36   -254       C  
ATOM   1179  N   PRO A 211     -37.469 -34.747   8.094  1.00 22.07           N  
ANISOU 1179  N   PRO A 211     2832   2753   2799    448    -52   -155       N  
ATOM   1180  CA  PRO A 211     -37.300 -36.118   8.620  1.00 22.67           C  
ANISOU 1180  CA  PRO A 211     2928   2876   2808    403    -32   -171       C  
ATOM   1181  C   PRO A 211     -35.839 -36.541   8.604  1.00 23.27           C  
ANISOU 1181  C   PRO A 211     3061   2956   2824    373    -45   -139       C  
ATOM   1182  O   PRO A 211     -35.419 -37.250   9.517  1.00 25.67           O  
ANISOU 1182  O   PRO A 211     3392   3276   3087    334    -22   -152       O  
ATOM   1183  CB  PRO A 211     -38.184 -36.972   7.676  1.00 20.35           C  
ANISOU 1183  CB  PRO A 211     2593   2623   2517    411    -58   -157       C  
ATOM   1184  CG  PRO A 211     -39.287 -35.960   7.224  1.00 21.02           C  
ANISOU 1184  CG  PRO A 211     2616   2686   2684    460    -75   -158       C  
ATOM   1185  CD  PRO A 211     -38.545 -34.653   7.069  1.00 22.16           C  
ANISOU 1185  CD  PRO A 211     2784   2775   2860    486    -90   -130       C  
ATOM   1186  N   ASN A 212     -35.057 -36.179   7.561  1.00 19.61           N  
ANISOU 1186  N   ASN A 212     2613   2480   2357    388    -84    -91       N  
ATOM   1187  CA  ASN A 212     -33.695 -36.672   7.500  1.00 21.18           C  
ANISOU 1187  CA  ASN A 212     2854   2684   2510    361    -92    -66       C  
ATOM   1188  C   ASN A 212     -32.771 -35.931   8.455  1.00 20.90           C  
ANISOU 1188  C   ASN A 212     2853   2620   2470    344    -77    -75       C  
ATOM   1189  O   ASN A 212     -31.896 -36.534   9.059  1.00 22.45           O  
ANISOU 1189  O   ASN A 212     3074   2826   2630    312    -73    -70       O  
ATOM   1190  CB  ASN A 212     -33.168 -36.605   6.069  1.00 19.08           C  
ANISOU 1190  CB  ASN A 212     2591   2423   2233    371   -128    -21       C  
ATOM   1191  CG  ASN A 212     -33.552 -37.857   5.289  1.00 20.85           C  
ANISOU 1191  CG  ASN A 212     2797   2691   2433    359   -136    -20       C  
ATOM   1192  OD1 ASN A 212     -32.908 -38.897   5.403  1.00 19.27           O  
ANISOU 1192  OD1 ASN A 212     2612   2503   2209    333   -124    -25       O  
ATOM   1193  ND2 ASN A 212     -34.660 -37.761   4.555  1.00 21.08           N  
ANISOU 1193  ND2 ASN A 212     2791   2742   2476    376   -156    -17       N  
ATOM   1194  N   LEU A 213     -32.910 -34.617   8.568  1.00 22.79           N  
ANISOU 1194  N   LEU A 213     3089   2818   2750    365    -73    -86       N  
ATOM   1195  CA  LEU A 213     -32.041 -33.899   9.491  1.00 22.33           C  
ANISOU 1195  CA  LEU A 213     3064   2735   2686    340    -56   -105       C  
ATOM   1196  C   LEU A 213     -32.275 -34.383  10.916  1.00 22.53           C  
ANISOU 1196  C   LEU A 213     3099   2787   2677    300    -20   -154       C  
ATOM   1197  O   LEU A 213     -31.321 -34.639  11.664  1.00 24.77           O  
ANISOU 1197  O   LEU A 213     3413   3085   2913    257    -21   -150       O  
ATOM   1198  CB  LEU A 213     -32.330 -32.378   9.397  1.00 22.80           C  
ANISOU 1198  CB  LEU A 213     3115   2735   2814    369    -48   -120       C  
ATOM   1199  CG  LEU A 213     -31.906 -31.603   8.147  1.00 24.46           C  
ANISOU 1199  CG  LEU A 213     3327   2911   3058    398    -85    -62       C  
ATOM   1200  CD1 LEU A 213     -32.300 -30.042   8.285  1.00 27.09           C  
ANISOU 1200  CD1 LEU A 213     3647   3166   3480    427    -72    -79       C  
ATOM   1201  CD2 LEU A 213     -30.422 -31.758   7.989  1.00 26.35           C  
ANISOU 1201  CD2 LEU A 213     3604   3158   3250    366   -100    -32       C  
ATOM   1202  N   TYR A 214     -33.549 -34.597  11.287  1.00 20.01           N  
ANISOU 1202  N   TYR A 214     2748   2480   2374    306     10   -193       N  
ATOM   1203  CA  TYR A 214     -33.788 -35.056  12.648  1.00 21.27           C  
ANISOU 1203  CA  TYR A 214     2921   2673   2489    256     49   -238       C  
ATOM   1204  C   TYR A 214     -33.400 -36.533  12.805  1.00 23.20           C  
ANISOU 1204  C   TYR A 214     3180   2960   2674    222     31   -198       C  
ATOM   1205  O   TYR A 214     -32.913 -36.922  13.867  1.00 22.94           O  
ANISOU 1205  O   TYR A 214     3176   2954   2585    169     40   -199       O  
ATOM   1206  CB  TYR A 214     -35.236 -34.778  13.062  1.00 22.74           C  
ANISOU 1206  CB  TYR A 214     3066   2858   2716    267     97   -300       C  
ATOM   1207  CG  TYR A 214     -35.391 -34.693  14.591  1.00 22.79           C  
ANISOU 1207  CG  TYR A 214     3091   2890   2677    205    154   -366       C  
ATOM   1208  CD1 TYR A 214     -36.283 -35.501  15.250  1.00 22.59           C  
ANISOU 1208  CD1 TYR A 214     3052   2910   2623    172    192   -396       C  
ATOM   1209  CD2 TYR A 214     -34.602 -33.811  15.351  1.00 23.63           C  
ANISOU 1209  CD2 TYR A 214     3233   2982   2763    171    169   -399       C  
ATOM   1210  CE1 TYR A 214     -36.412 -35.455  16.691  1.00 24.39           C  
ANISOU 1210  CE1 TYR A 214     3302   3174   2790     99    248   -455       C  
ATOM   1211  CE2 TYR A 214     -34.705 -33.754  16.765  1.00 23.21           C  
ANISOU 1211  CE2 TYR A 214     3202   2966   2650     98    221   -463       C  
ATOM   1212  CZ  TYR A 214     -35.608 -34.576  17.432  1.00 25.51           C  
ANISOU 1212  CZ  TYR A 214     3482   3309   2903     61    261   -489       C  
ATOM   1213  OH  TYR A 214     -35.728 -34.550  18.829  1.00 23.36           O  
ANISOU 1213  OH  TYR A 214     3235   3085   2556    -23    315   -551       O  
ATOM   1214  N   THR A 215     -33.483 -37.343  11.744  1.00 20.34           N  
ANISOU 1214  N   THR A 215     2801   2604   2324    248      3   -158       N  
ATOM   1215  CA  THR A 215     -32.858 -38.681  11.861  1.00 20.06           C  
ANISOU 1215  CA  THR A 215     2781   2592   2251    218    -14   -118       C  
ATOM   1216  C   THR A 215     -31.346 -38.582  12.092  1.00 22.39           C  
ANISOU 1216  C   THR A 215     3107   2877   2523    199    -41    -82       C  
ATOM   1217  O   THR A 215     -30.779 -39.295  12.946  1.00 26.44           O  
ANISOU 1217  O   THR A 215     3638   3408   3000    158    -49    -58       O  
ATOM   1218  CB  THR A 215     -33.190 -39.523  10.604  1.00 19.73           C  
ANISOU 1218  CB  THR A 215     2713   2553   2231    245    -31    -97       C  
ATOM   1219  OG1 THR A 215     -34.568 -39.946  10.691  1.00 20.33           O  
ANISOU 1219  OG1 THR A 215     2757   2648   2319    246     -7   -128       O  
ATOM   1220  CG2 THR A 215     -32.214 -40.772  10.504  1.00 19.52           C  
ANISOU 1220  CG2 THR A 215     2699   2527   2190    224    -50    -55       C  
ATOM   1221  N   LEU A 216     -30.665 -37.659  11.386  1.00 23.00           N  
ANISOU 1221  N   LEU A 216     3189   2927   2623    224    -58    -73       N  
ATOM   1222  CA  LEU A 216     -29.228 -37.514  11.608  1.00 21.53           C  
ANISOU 1222  CA  LEU A 216     3025   2734   2421    204    -82    -43       C  
ATOM   1223  C   LEU A 216     -28.937 -37.230  13.068  1.00 23.21           C  
ANISOU 1223  C   LEU A 216     3262   2965   2592    153    -75    -61       C  
ATOM   1224  O   LEU A 216     -27.960 -37.754  13.627  1.00 25.14           O  
ANISOU 1224  O   LEU A 216     3518   3225   2809    119   -101    -25       O  
ATOM   1225  CB  LEU A 216     -28.646 -36.380  10.738  1.00 26.42           C  
ANISOU 1225  CB  LEU A 216     3647   3321   3070    230    -94    -37       C  
ATOM   1226  CG  LEU A 216     -28.671 -36.703   9.215  1.00 28.59           C  
ANISOU 1226  CG  LEU A 216     3905   3592   3368    264   -107    -10       C  
ATOM   1227  CD1 LEU A 216     -28.323 -35.567   8.237  1.00 27.33           C  
ANISOU 1227  CD1 LEU A 216     3749   3404   3232    286   -118      6       C  
ATOM   1228  CD2 LEU A 216     -27.711 -37.808   8.993  1.00 28.47           C  
ANISOU 1228  CD2 LEU A 216     3885   3587   3344    250   -120     20       C  
ATOM   1229  N   ALA A 217     -29.778 -36.404  13.710  1.00 21.98           N  
ANISOU 1229  N   ALA A 217     3110   2810   2433    144    -39   -117       N  
ATOM   1230  CA  ALA A 217     -29.511 -35.951  15.078  1.00 23.52           C  
ANISOU 1230  CA  ALA A 217     3331   3027   2577     85    -23   -150       C  
ATOM   1231  C   ALA A 217     -29.843 -36.980  16.156  1.00 23.84           C  
ANISOU 1231  C   ALA A 217     3383   3120   2555     30    -16   -142       C  
ATOM   1232  O   ALA A 217     -29.411 -36.805  17.305  1.00 24.34           O  
ANISOU 1232  O   ALA A 217     3473   3218   2556    -35    -16   -153       O  
ATOM   1233  CB  ALA A 217     -30.328 -34.688  15.371  1.00 22.99           C  
ANISOU 1233  CB  ALA A 217     3260   2936   2538     91     26   -228       C  
ATOM   1234  N   THR A 218     -30.636 -38.021  15.830  1.00 23.05           N  
ANISOU 1234  N   THR A 218     3264   3029   2465     46     -9   -124       N  
ATOM   1235  CA  THR A 218     -31.237 -38.916  16.841  1.00 22.28           C  
ANISOU 1235  CA  THR A 218     3175   2977   2314     -9     10   -121       C  
ATOM   1236  C   THR A 218     -30.931 -40.394  16.609  1.00 22.36           C  
ANISOU 1236  C   THR A 218     3180   2989   2326    -11    -25    -46       C  
ATOM   1237  O   THR A 218     -31.057 -41.204  17.552  1.00 21.92           O  
ANISOU 1237  O   THR A 218     3140   2969   2221    -68    -26    -16       O  
ATOM   1238  CB  THR A 218     -32.786 -38.781  16.878  1.00 22.30           C  
ANISOU 1238  CB  THR A 218     3153   2985   2334      1     69   -186       C  
ATOM   1239  OG1 THR A 218     -33.350 -39.080  15.576  1.00 20.26           O  
ANISOU 1239  OG1 THR A 218     2858   2697   2144     68     61   -177       O  
ATOM   1240  CG2 THR A 218     -33.312 -37.396  17.338  1.00 21.65           C  
ANISOU 1240  CG2 THR A 218     3069   2896   2262     -3    120   -274       C  
ATOM   1241  N   GLY A 219     -30.515 -40.770  15.402  1.00 19.75           N  
ANISOU 1241  N   GLY A 219     2828   2623   2054     42    -52    -14       N  
ATOM   1242  CA  GLY A 219     -30.384 -42.188  15.061  1.00 22.08           C  
ANISOU 1242  CA  GLY A 219     3110   2907   2372     46    -71     40       C  
ATOM   1243  C   GLY A 219     -31.706 -42.942  14.929  1.00 19.69           C  
ANISOU 1243  C   GLY A 219     2790   2612   2080     45    -37     18       C  
ATOM   1244  O   GLY A 219     -31.700 -44.177  14.868  1.00 20.02           O  
ANISOU 1244  O   GLY A 219     2824   2643   2140     34    -46     59       O  
ATOM   1245  N   LEU A 220     -32.847 -42.253  14.916  1.00 21.14           N  
ANISOU 1245  N   LEU A 220     2962   2810   2262     54      4    -45       N  
ATOM   1246  CA  LEU A 220     -34.137 -42.941  14.843  1.00 22.23           C  
ANISOU 1246  CA  LEU A 220     3076   2960   2412     49     38    -69       C  
ATOM   1247  C   LEU A 220     -34.790 -42.834  13.457  1.00 25.94           C  
ANISOU 1247  C   LEU A 220     3505   3411   2938    107     39    -97       C  
ATOM   1248  O   LEU A 220     -34.658 -41.813  12.753  1.00 19.43           O  
ANISOU 1248  O   LEU A 220     2673   2572   2138    150     29   -115       O  
ATOM   1249  CB  LEU A 220     -35.101 -42.340  15.857  1.00 20.45           C  
ANISOU 1249  CB  LEU A 220     2851   2769   2149     12     89   -127       C  
ATOM   1250  CG  LEU A 220     -34.688 -42.411  17.329  1.00 24.41           C  
ANISOU 1250  CG  LEU A 220     3394   3309   2571    -65     97   -111       C  
ATOM   1251  CD1 LEU A 220     -35.586 -41.513  18.185  1.00 21.54           C  
ANISOU 1251  CD1 LEU A 220     3029   2979   2176    -98    160   -193       C  
ATOM   1252  CD2 LEU A 220     -34.809 -43.882  17.784  1.00 23.71           C  
ANISOU 1252  CD2 LEU A 220     3314   3234   2460   -112     90    -50       C  
ATOM   1253  N   TYR A 221     -35.588 -43.864  13.120  1.00 23.66           N  
ANISOU 1253  N   TYR A 221     3193   3127   2670    101     52    -99       N  
ATOM   1254  CA  TYR A 221     -36.546 -43.759  12.018  1.00 23.28           C  
ANISOU 1254  CA  TYR A 221     3102   3081   2663    139     57   -134       C  
ATOM   1255  C   TYR A 221     -37.551 -42.647  12.310  1.00 23.35           C  
ANISOU 1255  C   TYR A 221     3085   3105   2682    154     86   -188       C  
ATOM   1256  O   TYR A 221     -37.930 -42.443  13.480  1.00 22.55           O  
ANISOU 1256  O   TYR A 221     2993   3022   2553    117    124   -214       O  
ATOM   1257  CB  TYR A 221     -37.335 -45.045  11.851  1.00 22.04           C  
ANISOU 1257  CB  TYR A 221     2921   2931   2520    115     73   -138       C  
ATOM   1258  CG  TYR A 221     -36.475 -46.254  11.535  1.00 21.17           C  
ANISOU 1258  CG  TYR A 221     2828   2794   2424    101     53    -93       C  
ATOM   1259  CD1 TYR A 221     -35.706 -46.290  10.375  1.00 19.28           C  
ANISOU 1259  CD1 TYR A 221     2584   2532   2209    134     25    -84       C  
ATOM   1260  CD2 TYR A 221     -36.469 -47.344  12.371  1.00 24.24           C  
ANISOU 1260  CD2 TYR A 221     3230   3174   2806     54     66    -61       C  
ATOM   1261  CE1 TYR A 221     -34.893 -47.406  10.084  1.00 19.26           C  
ANISOU 1261  CE1 TYR A 221     2588   2495   2235    124     16    -54       C  
ATOM   1262  CE2 TYR A 221     -35.672 -48.507  12.059  1.00 19.89           C  
ANISOU 1262  CE2 TYR A 221     2685   2581   2293     47     49    -18       C  
ATOM   1263  CZ  TYR A 221     -34.919 -48.510  10.899  1.00 19.57           C  
ANISOU 1263  CZ  TYR A 221     2635   2515   2287     85     28    -23       C  
ATOM   1264  OH  TYR A 221     -34.131 -49.600  10.599  1.00 23.78           O  
ANISOU 1264  OH  TYR A 221     3167   3000   2871     80     20      7       O  
ATOM   1265  N   PRO A 222     -38.028 -41.963  11.271  1.00 19.86           N  
ANISOU 1265  N   PRO A 222     2608   2657   2282    203     69   -205       N  
ATOM   1266  CA  PRO A 222     -39.084 -40.943  11.471  1.00 20.66           C  
ANISOU 1266  CA  PRO A 222     2670   2761   2420    226     95   -255       C  
ATOM   1267  C   PRO A 222     -40.304 -41.448  12.228  1.00 20.77           C  
ANISOU 1267  C   PRO A 222     2651   2804   2438    193    146   -300       C  
ATOM   1268  O   PRO A 222     -40.866 -40.658  13.005  1.00 21.48           O  
ANISOU 1268  O   PRO A 222     2723   2895   2542    189    190   -350       O  
ATOM   1269  CB  PRO A 222     -39.473 -40.526  10.034  1.00 20.26           C  
ANISOU 1269  CB  PRO A 222     2578   2704   2416    280     53   -243       C  
ATOM   1270  CG  PRO A 222     -38.158 -40.668   9.292  1.00 19.76           C  
ANISOU 1270  CG  PRO A 222     2556   2626   2326    286     12   -193       C  
ATOM   1271  CD  PRO A 222     -37.487 -41.942   9.890  1.00 19.52           C  
ANISOU 1271  CD  PRO A 222     2561   2601   2254    239     24   -176       C  
ATOM   1272  N   GLU A 223     -40.742 -42.712  12.047  1.00 20.76           N  
ANISOU 1272  N   GLU A 223     2637   2823   2429    165    149   -290       N  
ATOM   1273  CA  GLU A 223     -41.932 -43.145  12.791  1.00 24.10           C  
ANISOU 1273  CA  GLU A 223     3026   3275   2857    127    203   -334       C  
ATOM   1274  C   GLU A 223     -41.667 -43.137  14.301  1.00 25.79           C  
ANISOU 1274  C   GLU A 223     3283   3503   3013     67    251   -345       C  
ATOM   1275  O   GLU A 223     -42.616 -42.997  15.100  1.00 25.65           O  
ANISOU 1275  O   GLU A 223     3239   3512   2996     36    311   -399       O  
ATOM   1276  CB  GLU A 223     -42.410 -44.554  12.320  1.00 21.29           C  
ANISOU 1276  CB  GLU A 223     2651   2932   2504     99    199   -320       C  
ATOM   1277  CG  GLU A 223     -41.402 -45.622  12.688  1.00 21.03           C  
ANISOU 1277  CG  GLU A 223     2677   2885   2430     58    189   -267       C  
ATOM   1278  CD  GLU A 223     -41.832 -47.090  12.261  1.00 28.10           C  
ANISOU 1278  CD  GLU A 223     3556   3779   3342     25    191   -257       C  
ATOM   1279  OE1 GLU A 223     -42.928 -47.274  11.593  1.00 27.53           O  
ANISOU 1279  OE1 GLU A 223     3427   3726   3307     33    197   -296       O  
ATOM   1280  OE2 GLU A 223     -41.030 -48.036  12.611  1.00 28.07           O  
ANISOU 1280  OE2 GLU A 223     3595   3750   3321     -8    185   -207       O  
ATOM   1281  N   SER A 224     -40.393 -43.268  14.706  1.00 23.39           N  
ANISOU 1281  N   SER A 224     3041   3188   2658     46    226   -296       N  
ATOM   1282  CA  SER A 224     -40.030 -43.178  16.134  1.00 23.89           C  
ANISOU 1282  CA  SER A 224     3150   3276   2652    -18    259   -298       C  
ATOM   1283  C   SER A 224     -39.725 -41.763  16.615  1.00 24.93           C  
ANISOU 1283  C   SER A 224     3293   3403   2776     -8    277   -343       C  
ATOM   1284  O   SER A 224     -40.119 -41.421  17.737  1.00 28.07           O  
ANISOU 1284  O   SER A 224     3700   3833   3134    -61    334   -393       O  
ATOM   1285  CB  SER A 224     -38.789 -44.043  16.440  1.00 23.51           C  
ANISOU 1285  CB  SER A 224     3157   3220   2554    -53    216   -216       C  
ATOM   1286  OG  SER A 224     -39.180 -45.396  16.388  1.00 26.22           O  
ANISOU 1286  OG  SER A 224     3494   3566   2903    -83    219   -182       O  
ATOM   1287  N   HIS A 225     -38.983 -40.934  15.850  1.00 22.19           N  
ANISOU 1287  N   HIS A 225     2951   3019   2462     49    234   -330       N  
ATOM   1288  CA  HIS A 225     -38.688 -39.583  16.375  1.00 21.93           C  
ANISOU 1288  CA  HIS A 225     2930   2974   2429     53    256   -377       C  
ATOM   1289  C   HIS A 225     -39.853 -38.614  16.174  1.00 26.73           C  
ANISOU 1289  C   HIS A 225     3478   3563   3115     94    301   -454       C  
ATOM   1290  O   HIS A 225     -39.922 -37.561  16.848  1.00 29.69           O  
ANISOU 1290  O   HIS A 225     3853   3927   3500     85    345   -518       O  
ATOM   1291  CB  HIS A 225     -37.339 -39.038  15.815  1.00 21.49           C  
ANISOU 1291  CB  HIS A 225     2908   2883   2375     84    198   -330       C  
ATOM   1292  CG  HIS A 225     -37.269 -38.778  14.317  1.00 20.76           C  
ANISOU 1292  CG  HIS A 225     2786   2751   2349    160    152   -301       C  
ATOM   1293  ND1 HIS A 225     -38.211 -38.027  13.633  1.00 21.03           N  
ANISOU 1293  ND1 HIS A 225     2769   2763   2459    214    161   -335       N  
ATOM   1294  CD2 HIS A 225     -36.277 -39.043  13.417  1.00 20.30           C  
ANISOU 1294  CD2 HIS A 225     2746   2675   2291    184     97   -240       C  
ATOM   1295  CE1 HIS A 225     -37.827 -37.882  12.370  1.00 20.77           C  
ANISOU 1295  CE1 HIS A 225     2728   2707   2457    262    108   -289       C  
ATOM   1296  NE2 HIS A 225     -36.650 -38.485  12.207  1.00 21.97           N  
ANISOU 1296  NE2 HIS A 225     2923   2863   2562    243     74   -237       N  
ATOM   1297  N   GLY A 226     -40.779 -38.941  15.280  1.00 24.93           N  
ANISOU 1297  N   GLY A 226     3193   3331   2950    138    291   -452       N  
ATOM   1298  CA  GLY A 226     -42.054 -38.258  15.176  1.00 26.19           C  
ANISOU 1298  CA  GLY A 226     3279   3478   3192    172    333   -520       C  
ATOM   1299  C   GLY A 226     -42.124 -37.186  14.108  1.00 26.56           C  
ANISOU 1299  C   GLY A 226     3287   3473   3332    255    292   -510       C  
ATOM   1300  O   GLY A 226     -43.214 -36.623  13.886  1.00 24.21           O  
ANISOU 1300  O   GLY A 226     2915   3157   3124    295    314   -554       O  
ATOM   1301  N   ILE A 227     -41.005 -36.871  13.456  1.00 27.28           N  
ANISOU 1301  N   ILE A 227     3420   3536   3409    280    234   -451       N  
ATOM   1302  CA  ILE A 227     -41.006 -35.855  12.380  1.00 25.44           C  
ANISOU 1302  CA  ILE A 227     3157   3253   3257    352    188   -426       C  
ATOM   1303  C   ILE A 227     -41.128 -36.653  11.092  1.00 24.29           C  
ANISOU 1303  C   ILE A 227     2993   3129   3107    375    124   -361       C  
ATOM   1304  O   ILE A 227     -40.142 -36.982  10.410  1.00 23.28           O  
ANISOU 1304  O   ILE A 227     2909   3003   2935    374     76   -303       O  
ATOM   1305  CB  ILE A 227     -39.763 -34.949  12.437  1.00 27.85           C  
ANISOU 1305  CB  ILE A 227     3516   3516   3550    357    171   -406       C  
ATOM   1306  CG1 ILE A 227     -39.606 -34.349  13.859  1.00 25.18           C  
ANISOU 1306  CG1 ILE A 227     3202   3171   3194    312    241   -483       C  
ATOM   1307  CG2 ILE A 227     -39.841 -33.862  11.345  1.00 29.40           C  
ANISOU 1307  CG2 ILE A 227     3680   3656   3836    427    126   -372       C  
ATOM   1308  CD1 ILE A 227     -40.812 -33.412  14.324  1.00 23.50           C  
ANISOU 1308  CD1 ILE A 227     2923   2925   3082    336    308   -572       C  
ATOM   1309  N   VAL A 228     -42.370 -37.056  10.792  1.00 25.95           N  
ANISOU 1309  N   VAL A 228     3137   3363   3360    387    129   -380       N  
ATOM   1310  CA  VAL A 228     -42.636 -37.968   9.684  1.00 25.28           C  
ANISOU 1310  CA  VAL A 228     3032   3312   3260    391     77   -336       C  
ATOM   1311  C   VAL A 228     -42.861 -37.230   8.366  1.00 28.46           C  
ANISOU 1311  C   VAL A 228     3396   3699   3720    449     10   -289       C  
ATOM   1312  O   VAL A 228     -42.988 -37.878   7.304  1.00 27.24           O  
ANISOU 1312  O   VAL A 228     3229   3580   3543    447    -41   -250       O  
ATOM   1313  CB  VAL A 228     -43.835 -38.878  10.025  1.00 25.09           C  
ANISOU 1313  CB  VAL A 228     2956   3330   3246    363    113   -378       C  
ATOM   1314  CG1 VAL A 228     -43.599 -39.494  11.397  1.00 26.00           C  
ANISOU 1314  CG1 VAL A 228     3116   3462   3301    299    180   -415       C  
ATOM   1315  CG2 VAL A 228     -45.214 -38.089  10.009  1.00 24.88           C  
ANISOU 1315  CG2 VAL A 228     2834   3294   3326    405    130   -422       C  
ATOM   1316  N   GLY A 229     -42.887 -35.892   8.385  1.00 26.19           N  
ANISOU 1316  N   GLY A 229     3089   3358   3503    494      6   -288       N  
ATOM   1317  CA  GLY A 229     -42.899 -35.186   7.107  1.00 27.91           C  
ANISOU 1317  CA  GLY A 229     3283   3558   3765    542    -69   -220       C  
ATOM   1318  C   GLY A 229     -42.520 -33.730   7.352  1.00 31.13           C  
ANISOU 1318  C   GLY A 229     3696   3889   4242    582    -62   -217       C  
ATOM   1319  O   GLY A 229     -42.371 -33.304   8.497  1.00 31.03           O  
ANISOU 1319  O   GLY A 229     3699   3843   4247    570      4   -280       O  
ATOM   1320  N   ASN A 230     -42.368 -32.951   6.267  1.00 31.48           N  
ANISOU 1320  N   ASN A 230     3730   3906   4327    622   -130   -142       N  
ATOM   1321  CA  ASN A 230     -42.199 -31.513   6.488  1.00 34.83           C  
ANISOU 1321  CA  ASN A 230     4146   4242   4844    664   -122   -138       C  
ATOM   1322  C   ASN A 230     -43.507 -30.886   6.974  1.00 36.14           C  
ANISOU 1322  C   ASN A 230     4219   4366   5146    709    -89   -191       C  
ATOM   1323  O   ASN A 230     -43.489 -29.835   7.612  1.00 38.23           O  
ANISOU 1323  O   ASN A 230     4473   4553   5500    734    -45   -232       O  
ATOM   1324  CB  ASN A 230     -41.726 -30.774   5.216  1.00 35.48           C  
ANISOU 1324  CB  ASN A 230     4240   4298   4943    692   -204    -34       C  
ATOM   1325  CG  ASN A 230     -40.267 -31.074   4.837  1.00 35.53           C  
ANISOU 1325  CG  ASN A 230     4337   4326   4836    650   -220      7       C  
ATOM   1326  OD1 ASN A 230     -39.460 -31.500   5.638  1.00 33.03           O  
ANISOU 1326  OD1 ASN A 230     4076   4018   4456    611   -171    -40       O  
ATOM   1327  ND2 ASN A 230     -39.939 -30.810   3.600  1.00 38.45           N  
ANISOU 1327  ND2 ASN A 230     4718   4706   5186    655   -291     97       N  
ATOM   1328  N   SER A 231     -44.653 -31.476   6.667  1.00 35.29           N  
ANISOU 1328  N   SER A 231     4037   4304   5067    719   -107   -196       N  
ATOM   1329  CA  SER A 231     -45.873 -31.033   7.330  1.00 36.11           C  
ANISOU 1329  CA  SER A 231     4048   4374   5299    753    -56   -266       C  
ATOM   1330  C   SER A 231     -46.629 -32.267   7.806  1.00 35.52           C  
ANISOU 1330  C   SER A 231     3945   4378   5174    711    -14   -327       C  
ATOM   1331  O   SER A 231     -46.437 -33.359   7.261  1.00 35.75           O  
ANISOU 1331  O   SER A 231     4005   4479   5099    673    -52   -291       O  
ATOM   1332  CB  SER A 231     -46.719 -30.171   6.424  1.00 39.47           C  
ANISOU 1332  CB  SER A 231     4380   4754   5863    826   -126   -201       C  
ATOM   1333  OG  SER A 231     -47.232 -30.967   5.408  1.00 43.43           O  
ANISOU 1333  OG  SER A 231     4848   5334   6320    819   -205   -138       O  
ATOM   1334  N   MET A 232     -47.411 -32.113   8.883  1.00 32.78           N  
ANISOU 1334  N   MET A 232     3547   4014   4896    709     74   -426       N  
ATOM   1335  CA  MET A 232     -48.031 -33.241   9.564  1.00 31.44           C  
ANISOU 1335  CA  MET A 232     3361   3914   4671    655    133   -493       C  
ATOM   1336  C   MET A 232     -49.280 -32.782  10.273  1.00 33.89           C  
ANISOU 1336  C   MET A 232     3568   4199   5111    678    207   -584       C  
ATOM   1337  O   MET A 232     -49.336 -31.654  10.769  1.00 36.79           O  
ANISOU 1337  O   MET A 232     3908   4489   5580    713    253   -631       O  
ATOM   1338  CB  MET A 232     -47.144 -33.826  10.650  1.00 32.53           C  
ANISOU 1338  CB  MET A 232     3598   4079   4684    580    203   -541       C  
ATOM   1339  CG  MET A 232     -45.783 -34.224  10.209  1.00 32.19           C  
ANISOU 1339  CG  MET A 232     3656   4050   4524    555    151   -470       C  
ATOM   1340  SD  MET A 232     -44.888 -34.793  11.656  1.00 34.61           S  
ANISOU 1340  SD  MET A 232     4058   4383   4709    470    230   -526       S  
ATOM   1341  CE  MET A 232     -44.167 -33.250  12.301  1.00 33.13           C  
ANISOU 1341  CE  MET A 232     3902   4116   4571    489    268   -565       C  
ATOM   1342  N   TYR A 233     -50.254 -33.672  10.374  1.00 31.16           N  
ANISOU 1342  N   TYR A 233     3162   3915   4764    652    227   -617       N  
ATOM   1343  CA  TYR A 233     -51.410 -33.432  11.222  1.00 33.60           C  
ANISOU 1343  CA  TYR A 233     3376   4214   5178    656    319   -721       C  
ATOM   1344  C   TYR A 233     -51.379 -34.462  12.343  1.00 34.76           C  
ANISOU 1344  C   TYR A 233     3575   4427   5207    562    412   -795       C  
ATOM   1345  O   TYR A 233     -51.233 -35.660  12.087  1.00 36.28           O  
ANISOU 1345  O   TYR A 233     3808   4686   5292    513    382   -757       O  
ATOM   1346  CB  TYR A 233     -52.717 -33.516  10.417  1.00 33.86           C  
ANISOU 1346  CB  TYR A 233     3275   4263   5328    704    266   -699       C  
ATOM   1347  CG  TYR A 233     -53.929 -33.438  11.290  1.00 36.71           C  
ANISOU 1347  CG  TYR A 233     3530   4624   5795    699    368   -812       C  
ATOM   1348  CD1 TYR A 233     -54.685 -34.570  11.583  1.00 35.77           C  
ANISOU 1348  CD1 TYR A 233     3378   4585   5630    640    407   -855       C  
ATOM   1349  CD2 TYR A 233     -54.304 -32.226  11.855  1.00 36.87           C  
ANISOU 1349  CD2 TYR A 233     3484   4559   5966    749    435   -885       C  
ATOM   1350  CE1 TYR A 233     -55.813 -34.477  12.396  1.00 39.35           C  
ANISOU 1350  CE1 TYR A 233     3728   5040   6182    631    509   -964       C  
ATOM   1351  CE2 TYR A 233     -55.396 -32.127  12.672  1.00 38.57           C  
ANISOU 1351  CE2 TYR A 233     3598   4773   6285    742    540  -1001       C  
ATOM   1352  CZ  TYR A 233     -56.149 -33.241  12.945  1.00 41.24           C  
ANISOU 1352  CZ  TYR A 233     3900   5198   6571    683    578  -1040       C  
ATOM   1353  OH  TYR A 233     -57.241 -33.109  13.762  1.00 45.27           O  
ANISOU 1353  OH  TYR A 233     4304   5709   7187    672    691  -1161       O  
ATOM   1354  N   ASP A 234     -51.445 -34.007  13.578  1.00 34.24           N  
ANISOU 1354  N   ASP A 234     3514   4341   5156    531    523   -898       N  
ATOM   1355  CA  ASP A 234     -51.483 -34.951  14.680  1.00 35.23           C  
ANISOU 1355  CA  ASP A 234     3687   4534   5166    434    611   -961       C  
ATOM   1356  C   ASP A 234     -52.913 -34.967  15.196  1.00 36.77           C  
ANISOU 1356  C   ASP A 234     3763   4745   5461    427    698  -1059       C  
ATOM   1357  O   ASP A 234     -53.380 -33.925  15.696  1.00 38.15           O  
ANISOU 1357  O   ASP A 234     3874   4865   5756    459    769  -1146       O  
ATOM   1358  CB  ASP A 234     -50.485 -34.565  15.792  1.00 34.53           C  
ANISOU 1358  CB  ASP A 234     3699   4435   4987    377    678  -1009       C  
ATOM   1359  CG  ASP A 234     -50.440 -35.601  16.949  1.00 36.29           C  
ANISOU 1359  CG  ASP A 234     3981   4737   5069    264    758  -1054       C  
ATOM   1360  OD1 ASP A 234     -51.483 -35.802  17.603  1.00 38.85           O  
ANISOU 1360  OD1 ASP A 234     4239   5093   5428    228    847  -1140       O  
ATOM   1361  OD2 ASP A 234     -49.373 -36.203  17.222  1.00 35.22           O  
ANISOU 1361  OD2 ASP A 234     3954   4633   4794    208    732  -1001       O  
ATOM   1362  N   PRO A 235     -53.649 -36.098  15.084  1.00 36.12           N  
ANISOU 1362  N   PRO A 235     3645   4732   5347    386    699  -1055       N  
ATOM   1363  CA  PRO A 235     -55.072 -36.106  15.509  1.00 38.20           C  
ANISOU 1363  CA  PRO A 235     3782   5013   5718    381    782  -1149       C  
ATOM   1364  C   PRO A 235     -55.265 -36.035  17.007  1.00 42.22           C  
ANISOU 1364  C   PRO A 235     4309   5545   6189    300    931  -1272       C  
ATOM   1365  O   PRO A 235     -56.345 -35.618  17.436  1.00 45.47           O  
ANISOU 1365  O   PRO A 235     4608   5947   6721    309   1018  -1373       O  
ATOM   1366  CB  PRO A 235     -55.617 -37.435  14.962  1.00 36.46           C  
ANISOU 1366  CB  PRO A 235     3539   4866   5450    344    737  -1102       C  
ATOM   1367  CG  PRO A 235     -54.394 -38.339  14.949  1.00 34.98           C  
ANISOU 1367  CG  PRO A 235     3497   4710   5084    285    693  -1025       C  
ATOM   1368  CD  PRO A 235     -53.181 -37.433  14.693  1.00 33.73           C  
ANISOU 1368  CD  PRO A 235     3416   4491   4908    333    641   -976       C  
ATOM   1369  N   VAL A 236     -54.271 -36.409  17.817  1.00 41.02           N  
ANISOU 1369  N   VAL A 236     4287   5424   5875    218    964  -1270       N  
ATOM   1370  CA  VAL A 236     -54.398 -36.252  19.268  1.00 41.47           C  
ANISOU 1370  CA  VAL A 236     4368   5512   5879    130   1105  -1387       C  
ATOM   1371  C   VAL A 236     -54.190 -34.797  19.700  1.00 43.53           C  
ANISOU 1371  C   VAL A 236     4611   5698   6229    169   1162  -1473       C  
ATOM   1372  O   VAL A 236     -54.954 -34.264  20.510  1.00 45.38           O  
ANISOU 1372  O   VAL A 236     4777   5928   6538    146   1286  -1605       O  
ATOM   1373  CB  VAL A 236     -53.424 -37.191  19.994  1.00 39.97           C  
ANISOU 1373  CB  VAL A 236     4319   5386   5480     21   1109  -1342       C  
ATOM   1374  CG1 VAL A 236     -53.290 -36.784  21.461  1.00 41.39           C  
ANISOU 1374  CG1 VAL A 236     4544   5597   5587    -72   1238  -1453       C  
ATOM   1375  CG2 VAL A 236     -53.879 -38.629  19.814  1.00 40.10           C  
ANISOU 1375  CG2 VAL A 236     4335   5469   5432    -32   1090  -1288       C  
ATOM   1376  N   PHE A 237     -53.137 -34.128  19.217  1.00 41.34           N  
ANISOU 1376  N   PHE A 237     4398   5362   5948    222   1084  -1409       N  
ATOM   1377  CA  PHE A 237     -53.023 -32.692  19.490  1.00 41.31           C  
ANISOU 1377  CA  PHE A 237     4365   5271   6060    269   1134  -1490       C  
ATOM   1378  C   PHE A 237     -54.160 -31.914  18.841  1.00 44.89           C  
ANISOU 1378  C   PHE A 237     4662   5650   6744    375   1135  -1524       C  
ATOM   1379  O   PHE A 237     -54.492 -30.797  19.282  1.00 46.20           O  
ANISOU 1379  O   PHE A 237     4766   5743   7045    406   1217  -1630       O  
ATOM   1380  CB  PHE A 237     -51.716 -32.110  18.967  1.00 40.32           C  
ANISOU 1380  CB  PHE A 237     4328   5089   5902    310   1042  -1405       C  
ATOM   1381  CG  PHE A 237     -50.474 -32.763  19.500  1.00 37.95           C  
ANISOU 1381  CG  PHE A 237     4173   4850   5395    220   1023  -1358       C  
ATOM   1382  CD1 PHE A 237     -50.479 -33.405  20.740  1.00 39.21           C  
ANISOU 1382  CD1 PHE A 237     4386   5094   5417    100   1115  -1424       C  
ATOM   1383  CD2 PHE A 237     -49.286 -32.701  18.771  1.00 33.98           C  
ANISOU 1383  CD2 PHE A 237     3750   4321   4839    253    912  -1244       C  
ATOM   1384  CE1 PHE A 237     -49.298 -34.014  21.224  1.00 38.82           C  
ANISOU 1384  CE1 PHE A 237     4467   5100   5183     19   1083  -1364       C  
ATOM   1385  CE2 PHE A 237     -48.104 -33.303  19.257  1.00 33.28           C  
ANISOU 1385  CE2 PHE A 237     3786   4285   4575    175    889  -1197       C  
ATOM   1386  CZ  PHE A 237     -48.126 -33.965  20.477  1.00 36.20           C  
ANISOU 1386  CZ  PHE A 237     4204   4736   4814     61    970  -1252       C  
ATOM   1387  N   ASP A 238     -54.750 -32.484  17.793  1.00 44.64           N  
ANISOU 1387  N   ASP A 238     4563   5633   6764    428   1042  -1435       N  
ATOM   1388  CA  ASP A 238     -55.555 -31.749  16.824  1.00 47.63           C  
ANISOU 1388  CA  ASP A 238     4807   5937   7352    545    983  -1409       C  
ATOM   1389  C   ASP A 238     -54.827 -30.472  16.367  1.00 48.07           C  
ANISOU 1389  C   ASP A 238     4882   5883   7500    625    931  -1370       C  
ATOM   1390  O   ASP A 238     -55.350 -29.365  16.454  1.00 50.95           O  
ANISOU 1390  O   ASP A 238     5152   6156   8052    691    975  -1436       O  
ATOM   1391  CB  ASP A 238     -56.947 -31.452  17.407  1.00 50.65           C  
ANISOU 1391  CB  ASP A 238     5042   6310   7892    552   1100  -1541       C  
ATOM   1392  CG  ASP A 238     -57.902 -30.875  16.392  1.00 54.45           C  
ANISOU 1392  CG  ASP A 238     5367   6726   8596    669   1028  -1501       C  
ATOM   1393  OD1 ASP A 238     -58.820 -30.149  16.827  1.00 58.92           O  
ANISOU 1393  OD1 ASP A 238     5806   7238   9344    705   1121  -1612       O  
ATOM   1394  OD2 ASP A 238     -57.748 -31.117  15.169  1.00 52.93           O  
ANISOU 1394  OD2 ASP A 238     5172   6536   8402    724    880  -1361       O  
ATOM   1395  N   ALA A 239     -53.607 -30.633  15.857  1.00 44.86           N  
ANISOU 1395  N   ALA A 239     4596   5481   6969    620    836  -1262       N  
ATOM   1396  CA  ALA A 239     -52.818 -29.486  15.390  1.00 42.97           C  
ANISOU 1396  CA  ALA A 239     4386   5142   6799    685    783  -1214       C  
ATOM   1397  C   ALA A 239     -51.986 -29.875  14.179  1.00 40.65           C  
ANISOU 1397  C   ALA A 239     4162   4865   6418    711    634  -1052       C  
ATOM   1398  O   ALA A 239     -51.757 -31.061  13.897  1.00 38.07           O  
ANISOU 1398  O   ALA A 239     3889   4627   5948    663    587   -993       O  
ATOM   1399  CB  ALA A 239     -51.896 -28.920  16.470  1.00 40.05           C  
ANISOU 1399  CB  ALA A 239     4113   4747   6359    626    872  -1300       C  
ATOM   1400  N   THR A 240     -51.523 -28.860  13.459  1.00 40.00           N  
ANISOU 1400  N   THR A 240     4079   4692   6427    784    565   -984       N  
ATOM   1401  CA  THR A 240     -50.788 -29.080  12.227  1.00 41.38           C  
ANISOU 1401  CA  THR A 240     4309   4878   6534    810    427   -834       C  
ATOM   1402  C   THR A 240     -49.423 -28.444  12.327  1.00 40.71           C  
ANISOU 1402  C   THR A 240     4335   4745   6390    798    417   -807       C  
ATOM   1403  O   THR A 240     -49.305 -27.262  12.666  1.00 40.17           O  
ANISOU 1403  O   THR A 240     4249   4577   6438    832    460   -855       O  
ATOM   1404  CB  THR A 240     -51.548 -28.531  11.009  1.00 44.58           C  
ANISOU 1404  CB  THR A 240     4604   5234   7099    905    326   -742       C  
ATOM   1405  OG1 THR A 240     -52.667 -29.383  10.772  1.00 46.43           O  
ANISOU 1405  OG1 THR A 240     4749   5541   7349    902    313   -748       O  
ATOM   1406  CG2 THR A 240     -50.683 -28.589   9.777  1.00 43.10           C  
ANISOU 1406  CG2 THR A 240     4486   5057   6835    922    194   -593       C  
ATOM   1407  N   PHE A 241     -48.408 -29.247  12.047  1.00 36.90           N  
ANISOU 1407  N   PHE A 241     3960   4327   5733    748    365   -738       N  
ATOM   1408  CA  PHE A 241     -47.016 -28.843  11.981  1.00 36.58           C  
ANISOU 1408  CA  PHE A 241     4026   4257   5615    731    337   -694       C  
ATOM   1409  C   PHE A 241     -46.714 -28.435  10.543  1.00 40.44           C  
ANISOU 1409  C   PHE A 241     4509   4711   6145    793    215   -558       C  
ATOM   1410  O   PHE A 241     -47.025 -29.180   9.595  1.00 36.81           O  
ANISOU 1410  O   PHE A 241     4029   4310   5646    802    135   -477       O  
ATOM   1411  CB  PHE A 241     -46.175 -30.042  12.427  1.00 31.51           C  
ANISOU 1411  CB  PHE A 241     3488   3710   4776    644    345   -689       C  
ATOM   1412  CG  PHE A 241     -44.688 -29.892  12.307  1.00 32.24           C  
ANISOU 1412  CG  PHE A 241     3687   3793   4770    618    309   -635       C  
ATOM   1413  CD1 PHE A 241     -44.048 -29.997  11.081  1.00 30.68           C  
ANISOU 1413  CD1 PHE A 241     3520   3596   4540    645    207   -517       C  
ATOM   1414  CD2 PHE A 241     -43.906 -29.792  13.462  1.00 31.20           C  
ANISOU 1414  CD2 PHE A 241     3628   3669   4558    552    377   -705       C  
ATOM   1415  CE1 PHE A 241     -42.662 -29.956  11.002  1.00 32.62           C  
ANISOU 1415  CE1 PHE A 241     3860   3842   4694    615    180   -474       C  
ATOM   1416  CE2 PHE A 241     -42.487 -29.721  13.375  1.00 29.35           C  
ANISOU 1416  CE2 PHE A 241     3488   3433   4232    523    340   -654       C  
ATOM   1417  CZ  PHE A 241     -41.872 -29.803  12.147  1.00 29.76           C  
ANISOU 1417  CZ  PHE A 241     3562   3478   4267    558    244   -541       C  
ATOM   1418  N   HIS A 242     -46.083 -27.273  10.386  1.00 43.84           N  
ANISOU 1418  N   HIS A 242     4962   5048   6646    826    203   -534       N  
ATOM   1419  CA  HIS A 242     -45.811 -26.704   9.076  1.00 47.89           C  
ANISOU 1419  CA  HIS A 242     5469   5518   7210    881     93   -403       C  
ATOM   1420  C   HIS A 242     -44.508 -25.933   9.156  1.00 46.31           C  
ANISOU 1420  C   HIS A 242     5357   5256   6981    867     94   -382       C  
ATOM   1421  O   HIS A 242     -44.240 -25.305  10.181  1.00 46.72           O  
ANISOU 1421  O   HIS A 242     5427   5252   7070    848    182   -481       O  
ATOM   1422  CB  HIS A 242     -46.964 -25.769   8.659  1.00 55.26           C  
ANISOU 1422  CB  HIS A 242     6277   6365   8355    968     71   -386       C  
ATOM   1423  CG  HIS A 242     -47.152 -25.674   7.183  1.00 62.13           C  
ANISOU 1423  CG  HIS A 242     7114   7240   9253   1015    -62   -234       C  
ATOM   1424  ND1 HIS A 242     -46.358 -24.879   6.380  1.00 65.28           N  
ANISOU 1424  ND1 HIS A 242     7557   7579   9666   1036   -134   -127       N  
ATOM   1425  CD2 HIS A 242     -48.033 -26.285   6.355  1.00 64.72           C  
ANISOU 1425  CD2 HIS A 242     7371   7634   9586   1033   -138   -170       C  
ATOM   1426  CE1 HIS A 242     -46.750 -24.994   5.123  1.00 66.53           C  
ANISOU 1426  CE1 HIS A 242     7675   7769   9832   1065   -249      1       C  
ATOM   1427  NE2 HIS A 242     -47.766 -25.840   5.080  1.00 66.46           N  
ANISOU 1427  NE2 HIS A 242     7596   7838   9817   1064   -256    -25       N  
ATOM   1428  N   LEU A 243     -43.721 -25.949   8.076  1.00 46.77           N  
ANISOU 1428  N   LEU A 243     5468   5327   6976    869      2   -261       N  
ATOM   1429  CA  LEU A 243     -42.507 -25.120   8.051  1.00 50.19           C  
ANISOU 1429  CA  LEU A 243     5975   5695   7399    857     -1   -233       C  
ATOM   1430  C   LEU A 243     -42.806 -23.636   8.241  1.00 53.09           C  
ANISOU 1430  C   LEU A 243     6292   5922   7957    913     25   -254       C  
ATOM   1431  O   LEU A 243     -41.973 -22.909   8.798  1.00 52.60           O  
ANISOU 1431  O   LEU A 243     6283   5796   7906    891     72   -298       O  
ATOM   1432  CB  LEU A 243     -41.748 -25.304   6.752  1.00 50.81           C  
ANISOU 1432  CB  LEU A 243     6104   5806   7395    853   -103    -96       C  
ATOM   1433  CG  LEU A 243     -41.271 -26.735   6.541  1.00 51.45           C  
ANISOU 1433  CG  LEU A 243     6241   6012   7297    794   -122    -82       C  
ATOM   1434  CD1 LEU A 243     -40.228 -26.801   5.403  1.00 49.85           C  
ANISOU 1434  CD1 LEU A 243     6102   5834   7004    775   -198     30       C  
ATOM   1435  CD2 LEU A 243     -40.771 -27.392   7.845  1.00 51.47           C  
ANISOU 1435  CD2 LEU A 243     6296   6055   7206    733    -36   -190       C  
ATOM   1436  N   ARG A 244     -43.962 -23.163   7.760  1.00 53.16           N  
ANISOU 1436  N   ARG A 244     6195   5878   8124    986     -7   -222       N  
ATOM   1437  CA  ARG A 244     -44.444 -21.823   8.053  1.00 54.33           C  
ANISOU 1437  CA  ARG A 244     6274   5883   8486   1047     31   -258       C  
ATOM   1438  C   ARG A 244     -45.358 -21.889   9.265  1.00 57.97           C  
ANISOU 1438  C   ARG A 244     6668   6335   9024   1046    147   -418       C  
ATOM   1439  O   ARG A 244     -46.399 -22.570   9.236  1.00 61.38           O  
ANISOU 1439  O   ARG A 244     7024   6826   9470   1061    145   -436       O  
ATOM   1440  CB  ARG A 244     -45.230 -21.226   6.892  1.00 54.80           C  
ANISOU 1440  CB  ARG A 244     6243   5881   8698   1130    -71   -128       C  
ATOM   1441  CG  ARG A 244     -44.485 -20.881   5.652  1.00 52.44           C  
ANISOU 1441  CG  ARG A 244     5995   5571   8359   1135   -184     37       C  
ATOM   1442  CD  ARG A 244     -45.467 -20.139   4.743  1.00 51.86           C  
ANISOU 1442  CD  ARG A 244     5812   5421   8472   1220   -274    152       C  
ATOM   1443  NE  ARG A 244     -45.241 -18.703   4.688  1.00 51.20           N  
ANISOU 1443  NE  ARG A 244     5713   5173   8570   1268   -273    189       N  
ATOM   1444  CZ  ARG A 244     -45.925 -17.896   3.883  1.00 52.21           C  
ANISOU 1444  CZ  ARG A 244     5751   5209   8875   1344   -359    310       C  
ATOM   1445  NH1 ARG A 244     -45.688 -16.592   3.845  1.00 51.60           N  
ANISOU 1445  NH1 ARG A 244     5662   4971   8972   1386   -356    347       N  
ATOM   1446  NH2 ARG A 244     -46.862 -18.421   3.113  1.00 53.73           N  
ANISOU 1446  NH2 ARG A 244     5865   5475   9073   1374   -451    396       N  
ATOM   1447  N   GLY A 245     -45.007 -21.158  10.312  1.00 55.88           N  
ANISOU 1447  N   GLY A 245     6424   5994   8811   1024    251   -539       N  
ATOM   1448  CA  GLY A 245     -45.822 -21.138  11.506  1.00 56.20           C  
ANISOU 1448  CA  GLY A 245     6406   6027   8921   1011    376   -705       C  
ATOM   1449  C   GLY A 245     -45.005 -21.414  12.751  1.00 54.80           C  
ANISOU 1449  C   GLY A 245     6324   5901   8597    913    476   -831       C  
ATOM   1450  O   GLY A 245     -43.856 -21.851  12.705  1.00 53.46           O  
ANISOU 1450  O   GLY A 245     6262   5793   8259    854    442   -786       O  
ATOM   1451  N   ARG A 246     -45.639 -21.127  13.888  1.00 54.60           N  
ANISOU 1451  N   ARG A 246     6251   5850   8644    893    602   -994       N  
ATOM   1452  CA  ARG A 246     -44.996 -21.290  15.182  1.00 52.89           C  
ANISOU 1452  CA  ARG A 246     6114   5684   8296    791    706  -1127       C  
ATOM   1453  C   ARG A 246     -45.234 -22.660  15.824  1.00 50.15           C  
ANISOU 1453  C   ARG A 246     5795   5490   7767    714    739  -1169       C  
ATOM   1454  O   ARG A 246     -44.636 -22.945  16.862  1.00 48.33           O  
ANISOU 1454  O   ARG A 246     5641   5323   7398    619    807  -1256       O  
ATOM   1455  CB  ARG A 246     -45.470 -20.193  16.140  1.00 51.27           C  
ANISOU 1455  CB  ARG A 246     5853   5373   8254    791    839  -1295       C  
ATOM   1456  N   GLU A 247     -46.110 -23.502  15.269  1.00 48.65           N  
ANISOU 1456  N   GLU A 247     5544   5361   7578    748    693  -1111       N  
ATOM   1457  CA  GLU A 247     -46.447 -24.726  15.990  1.00 47.79           C  
ANISOU 1457  CA  GLU A 247     5454   5382   7321    672    741  -1166       C  
ATOM   1458  C   GLU A 247     -45.245 -25.674  16.018  1.00 43.50           C  
ANISOU 1458  C   GLU A 247     5036   4940   6553    597    687  -1094       C  
ATOM   1459  O   GLU A 247     -45.061 -26.427  16.990  1.00 41.11           O  
ANISOU 1459  O   GLU A 247     4785   4727   6106    506    745  -1157       O  
ATOM   1460  CB  GLU A 247     -47.692 -25.361  15.366  1.00 48.62           C  
ANISOU 1460  CB  GLU A 247     5456   5521   7495    725    706  -1125       C  
ATOM   1461  CG  GLU A 247     -48.024 -26.763  15.786  1.00 50.26           C  
ANISOU 1461  CG  GLU A 247     5684   5862   7552    655    727  -1140       C  
ATOM   1462  CD  GLU A 247     -48.551 -26.846  17.186  1.00 52.77           C  
ANISOU 1462  CD  GLU A 247     5986   6215   7849    581    872  -1302       C  
ATOM   1463  OE1 GLU A 247     -47.965 -27.601  18.004  1.00 52.26           O  
ANISOU 1463  OE1 GLU A 247     6013   6242   7600    481    908  -1331       O  
ATOM   1464  OE2 GLU A 247     -49.555 -26.163  17.473  1.00 54.07           O  
ANISOU 1464  OE2 GLU A 247     6045   6318   8183    620    950  -1400       O  
ATOM   1465  N   LYS A 248     -44.368 -25.562  15.017  1.00 39.82           N  
ANISOU 1465  N   LYS A 248     4619   4451   6062    630    580   -965       N  
ATOM   1466  CA  LYS A 248     -43.217 -26.430  14.899  1.00 41.72           C  
ANISOU 1466  CA  LYS A 248     4963   4773   6115    572    522   -890       C  
ATOM   1467  C   LYS A 248     -42.191 -26.166  15.992  1.00 41.44           C  
ANISOU 1467  C   LYS A 248     5014   4751   5981    488    581   -964       C  
ATOM   1468  O   LYS A 248     -41.296 -26.997  16.201  1.00 37.56           O  
ANISOU 1468  O   LYS A 248     4603   4340   5330    426    550   -922       O  
ATOM   1469  CB  LYS A 248     -42.568 -26.257  13.518  1.00 42.76           C  
ANISOU 1469  CB  LYS A 248     5116   4873   6259    627    404   -745       C  
ATOM   1470  CG  LYS A 248     -41.938 -24.889  13.230  1.00 43.93           C  
ANISOU 1470  CG  LYS A 248     5277   4907   6509    662    392   -729       C  
ATOM   1471  CD  LYS A 248     -40.979 -24.998  12.038  1.00 44.20           C  
ANISOU 1471  CD  LYS A 248     5363   4945   6485    679    283   -585       C  
ATOM   1472  CE  LYS A 248     -40.176 -23.694  11.736  1.00 45.75           C  
ANISOU 1472  CE  LYS A 248     5587   5032   6764    700    268   -556       C  
ATOM   1473  NZ  LYS A 248     -41.066 -22.518  11.366  1.00 48.63           N  
ANISOU 1473  NZ  LYS A 248     5863   5272   7341    782    272   -556       N  
ATOM   1474  N   PHE A 249     -42.298 -25.028  16.676  1.00 42.40           N  
ANISOU 1474  N   PHE A 249     5116   4793   6202    484    663  -1073       N  
ATOM   1475  CA  PHE A 249     -41.400 -24.681  17.767  1.00 43.46           C  
ANISOU 1475  CA  PHE A 249     5326   4941   6246    396    724  -1160       C  
ATOM   1476  C   PHE A 249     -41.795 -25.342  19.070  1.00 44.42           C  
ANISOU 1476  C   PHE A 249     5461   5160   6256    301    818  -1272       C  
ATOM   1477  O   PHE A 249     -41.020 -25.299  20.040  1.00 45.40           O  
ANISOU 1477  O   PHE A 249     5658   5330   6264    207    858  -1333       O  
ATOM   1478  CB  PHE A 249     -41.376 -23.149  17.965  1.00 48.37           C  
ANISOU 1478  CB  PHE A 249     5920   5432   7027    423    782  -1245       C  
ATOM   1479  CG  PHE A 249     -40.713 -22.405  16.830  1.00 49.48           C  
ANISOU 1479  CG  PHE A 249     6070   5477   7253    493    693  -1131       C  
ATOM   1480  CD1 PHE A 249     -39.342 -22.522  16.601  1.00 48.35           C  
ANISOU 1480  CD1 PHE A 249     6017   5361   6993    453    629  -1056       C  
ATOM   1481  CD2 PHE A 249     -41.457 -21.594  15.990  1.00 51.94           C  
ANISOU 1481  CD2 PHE A 249     6297   5673   7766    595    671  -1094       C  
ATOM   1482  CE1 PHE A 249     -38.738 -21.850  15.556  1.00 49.46           C  
ANISOU 1482  CE1 PHE A 249     6168   5420   7206    508    553   -951       C  
ATOM   1483  CE2 PHE A 249     -40.850 -20.925  14.936  1.00 50.96           C  
ANISOU 1483  CE2 PHE A 249     6186   5466   7711    650    585   -977       C  
ATOM   1484  CZ  PHE A 249     -39.503 -21.051  14.720  1.00 49.99           C  
ANISOU 1484  CZ  PHE A 249     6157   5375   7463    604    531   -910       C  
ATOM   1485  N   ASN A 250     -42.979 -25.934  19.114  1.00 44.07           N  
ANISOU 1485  N   ASN A 250     5349   5151   6244    317    851  -1297       N  
ATOM   1486  CA  ASN A 250     -43.462 -26.625  20.299  1.00 44.06           C  
ANISOU 1486  CA  ASN A 250     5357   5248   6137    223    943  -1395       C  
ATOM   1487  C   ASN A 250     -42.742 -27.958  20.460  1.00 42.76           C  
ANISOU 1487  C   ASN A 250     5277   5202   5770    152    882  -1305       C  
ATOM   1488  O   ASN A 250     -42.769 -28.800  19.552  1.00 39.14           O  
ANISOU 1488  O   ASN A 250     4812   4767   5291    196    794  -1187       O  
ATOM   1489  CB  ASN A 250     -44.950 -26.867  20.153  1.00 47.54           C  
ANISOU 1489  CB  ASN A 250     5690   5686   6687    269    989  -1437       C  
ATOM   1490  CG  ASN A 250     -45.641 -27.128  21.451  1.00 54.57           C  
ANISOU 1490  CG  ASN A 250     6566   6644   7523    177   1120  -1579       C  
ATOM   1491  OD1 ASN A 250     -45.157 -27.859  22.351  1.00 54.07           O  
ANISOU 1491  OD1 ASN A 250     6583   6686   7274     65   1145  -1595       O  
ATOM   1492  ND2 ASN A 250     -46.824 -26.540  21.562  1.00 59.72           N  
ANISOU 1492  ND2 ASN A 250     7110   7239   8342    221   1206  -1683       N  
ATOM   1493  N   HIS A 251     -42.167 -28.179  21.643  1.00 42.55           N  
ANISOU 1493  N   HIS A 251     5322   5250   5596     38    932  -1365       N  
ATOM   1494  CA  HIS A 251     -41.356 -29.367  21.909  1.00 42.61           C  
ANISOU 1494  CA  HIS A 251     5411   5360   5418    -34    871  -1274       C  
ATOM   1495  C   HIS A 251     -42.118 -30.676  21.786  1.00 37.53           C  
ANISOU 1495  C   HIS A 251     4745   4788   4727    -42    860  -1223       C  
ATOM   1496  O   HIS A 251     -41.480 -31.700  21.577  1.00 35.24           O  
ANISOU 1496  O   HIS A 251     4506   4552   4330    -65    784  -1116       O  
ATOM   1497  CB  HIS A 251     -40.746 -29.290  23.317  1.00 52.49           C  
ANISOU 1497  CB  HIS A 251     6735   6685   6525   -166    931  -1355       C  
ATOM   1498  CG  HIS A 251     -39.607 -28.321  23.430  1.00 61.69           C  
ANISOU 1498  CG  HIS A 251     7949   7805   7686   -181    911  -1371       C  
ATOM   1499  ND1 HIS A 251     -38.823 -28.222  24.563  1.00 66.40           N  
ANISOU 1499  ND1 HIS A 251     8617   8470   8141   -301    938  -1424       N  
ATOM   1500  CD2 HIS A 251     -39.115 -27.408  22.552  1.00 64.34           C  
ANISOU 1500  CD2 HIS A 251     8272   8036   8138    -98    864  -1339       C  
ATOM   1501  CE1 HIS A 251     -37.894 -27.297  24.374  1.00 67.08           C  
ANISOU 1501  CE1 HIS A 251     8729   8495   8262   -290    910  -1429       C  
ATOM   1502  NE2 HIS A 251     -38.049 -26.786  23.165  1.00 66.11           N  
ANISOU 1502  NE2 HIS A 251     8559   8264   8298   -168    868  -1378       N  
ATOM   1503  N   ARG A 252     -43.453 -30.678  21.933  1.00 34.80           N  
ANISOU 1503  N   ARG A 252     4319   4440   4464    -26    937  -1301       N  
ATOM   1504  CA  ARG A 252     -44.221 -31.917  21.797  1.00 35.28           C  
ANISOU 1504  CA  ARG A 252     4353   4566   4486    -37    929  -1256       C  
ATOM   1505  C   ARG A 252     -44.059 -32.616  20.444  1.00 34.12           C  
ANISOU 1505  C   ARG A 252     4195   4401   4366     44    811  -1116       C  
ATOM   1506  O   ARG A 252     -44.381 -33.810  20.311  1.00 36.27           O  
ANISOU 1506  O   ARG A 252     4469   4733   4580     22    787  -1060       O  
ATOM   1507  CB  ARG A 252     -45.685 -31.604  22.007  1.00 37.81           C  
ANISOU 1507  CB  ARG A 252     4572   4870   4925    -17   1028  -1367       C  
ATOM   1508  CG  ARG A 252     -46.279 -30.709  20.944  1.00 39.38           C  
ANISOU 1508  CG  ARG A 252     4675   4961   5327    111   1002  -1366       C  
ATOM   1509  CD  ARG A 252     -47.775 -30.513  21.261  1.00 42.78           C  
ANISOU 1509  CD  ARG A 252     4993   5384   5879    125   1105  -1479       C  
ATOM   1510  NE  ARG A 252     -48.421 -29.510  20.412  1.00 43.27           N  
ANISOU 1510  NE  ARG A 252     4951   5334   6156    244   1091  -1491       N  
ATOM   1511  CZ  ARG A 252     -49.709 -29.200  20.494  1.00 44.53           C  
ANISOU 1511  CZ  ARG A 252     4992   5465   6463    280   1165  -1579       C  
ATOM   1512  NH1 ARG A 252     -50.489 -29.815  21.386  1.00 43.93           N  
ANISOU 1512  NH1 ARG A 252     4890   5468   6334    202   1267  -1671       N  
ATOM   1513  NH2 ARG A 252     -50.214 -28.269  19.688  1.00 45.06           N  
ANISOU 1513  NH2 ARG A 252     4962   5424   6735    393   1137  -1572       N  
ATOM   1514  N   TRP A 253     -43.609 -31.926  19.406  1.00 31.90           N  
ANISOU 1514  N   TRP A 253     3902   4042   4175    132    739  -1059       N  
ATOM   1515  CA  TRP A 253     -43.482 -32.664  18.142  1.00 31.73           C  
ANISOU 1515  CA  TRP A 253     3874   4020   4162    192    635   -935       C  
ATOM   1516  C   TRP A 253     -42.241 -33.551  18.107  1.00 29.30           C  
ANISOU 1516  C   TRP A 253     3657   3760   3715    147    566   -840       C  
ATOM   1517  O   TRP A 253     -42.196 -34.529  17.334  1.00 29.09           O  
ANISOU 1517  O   TRP A 253     3632   3757   3665    166    501   -754       O  
ATOM   1518  CB  TRP A 253     -43.475 -31.680  16.963  1.00 31.75           C  
ANISOU 1518  CB  TRP A 253     3831   3931   4300    296    577   -895       C  
ATOM   1519  CG  TRP A 253     -44.823 -30.944  16.831  1.00 32.50           C  
ANISOU 1519  CG  TRP A 253     3816   3973   4559    356    628   -967       C  
ATOM   1520  CD1 TRP A 253     -45.183 -29.738  17.397  1.00 33.22           C  
ANISOU 1520  CD1 TRP A 253     3866   3996   4759    371    708  -1072       C  
ATOM   1521  CD2 TRP A 253     -45.975 -31.414  16.126  1.00 32.27           C  
ANISOU 1521  CD2 TRP A 253     3699   3955   4606    405    606   -944       C  
ATOM   1522  NE1 TRP A 253     -46.492 -29.434  17.067  1.00 34.58           N  
ANISOU 1522  NE1 TRP A 253     3924   4131   5083    433    734  -1110       N  
ATOM   1523  CE2 TRP A 253     -46.994 -30.449  16.286  1.00 34.18           C  
ANISOU 1523  CE2 TRP A 253     3843   4133   5011    454    668  -1029       C  
ATOM   1524  CE3 TRP A 253     -46.241 -32.567  15.356  1.00 33.33           C  
ANISOU 1524  CE3 TRP A 253     3823   4145   4694    411    539   -861       C  
ATOM   1525  CZ2 TRP A 253     -48.260 -30.596  15.706  1.00 34.64           C  
ANISOU 1525  CZ2 TRP A 253     3791   4187   5185    510    658  -1027       C  
ATOM   1526  CZ3 TRP A 253     -47.521 -32.697  14.746  1.00 31.95           C  
ANISOU 1526  CZ3 TRP A 253     3542   3969   4627    462    529   -863       C  
ATOM   1527  CH2 TRP A 253     -48.496 -31.723  14.954  1.00 33.38           C  
ANISOU 1527  CH2 TRP A 253     3625   4092   4966    510    585   -942       C  
ATOM   1528  N   TRP A 254     -41.203 -33.199  18.873  1.00 30.73           N  
ANISOU 1528  N   TRP A 254     3909   3951   3816     89    575   -855       N  
ATOM   1529  CA  TRP A 254     -39.821 -33.646  18.616  1.00 28.58           C  
ANISOU 1529  CA  TRP A 254     3709   3694   3456     72    495   -759       C  
ATOM   1530  C   TRP A 254     -39.481 -34.756  19.599  1.00 27.70           C  
ANISOU 1530  C   TRP A 254     3653   3668   3205    -25    503   -739       C  
ATOM   1531  O   TRP A 254     -39.242 -34.469  20.769  1.00 31.27           O  
ANISOU 1531  O   TRP A 254     4142   4158   3583   -105    554   -799       O  
ATOM   1532  CB  TRP A 254     -38.839 -32.479  18.785  1.00 28.71           C  
ANISOU 1532  CB  TRP A 254     3761   3663   3483     71    490   -782       C  
ATOM   1533  CG  TRP A 254     -39.182 -31.354  17.880  1.00 27.65           C  
ANISOU 1533  CG  TRP A 254     3576   3437   3493    161    482   -794       C  
ATOM   1534  CD1 TRP A 254     -40.106 -30.346  18.112  1.00 29.22           C  
ANISOU 1534  CD1 TRP A 254     3715   3580   3807    190    554   -892       C  
ATOM   1535  CD2 TRP A 254     -38.664 -31.136  16.568  1.00 28.05           C  
ANISOU 1535  CD2 TRP A 254     3623   3437   3597    234    399   -702       C  
ATOM   1536  NE1 TRP A 254     -40.200 -29.522  17.013  1.00 28.60           N  
ANISOU 1536  NE1 TRP A 254     3595   3414   3856    282    511   -852       N  
ATOM   1537  CE2 TRP A 254     -39.313 -29.978  16.049  1.00 28.78           C  
ANISOU 1537  CE2 TRP A 254     3655   3444   3834    305    415   -734       C  
ATOM   1538  CE3 TRP A 254     -37.697 -31.787  15.783  1.00 28.93           C  
ANISOU 1538  CE3 TRP A 254     3774   3567   3652    243    316   -596       C  
ATOM   1539  CZ2 TRP A 254     -39.007 -29.453  14.797  1.00 26.27           C  
ANISOU 1539  CZ2 TRP A 254     3325   3066   3590    377    345   -653       C  
ATOM   1540  CZ3 TRP A 254     -37.403 -31.265  14.495  1.00 28.92           C  
ANISOU 1540  CZ3 TRP A 254     3758   3509   3722    313    255   -529       C  
ATOM   1541  CH2 TRP A 254     -38.082 -30.121  14.011  1.00 26.45           C  
ANISOU 1541  CH2 TRP A 254     3392   3119   3539    377    266   -552       C  
ATOM   1542  N   GLY A 255     -39.448 -36.018  19.159  1.00 26.96           N  
ANISOU 1542  N   GLY A 255     3565   3605   3073    -25    454   -654       N  
ATOM   1543  CA  GLY A 255     -39.177 -37.127  20.061  1.00 28.73           C  
ANISOU 1543  CA  GLY A 255     3837   3901   3180   -114    456   -619       C  
ATOM   1544  C   GLY A 255     -37.715 -37.571  20.079  1.00 30.08           C  
ANISOU 1544  C   GLY A 255     4070   4081   3277   -137    380   -526       C  
ATOM   1545  O   GLY A 255     -36.821 -36.938  19.507  1.00 29.69           O  
ANISOU 1545  O   GLY A 255     4033   3989   3258    -95    333   -501       O  
ATOM   1546  N   GLY A 256     -37.480 -38.726  20.712  1.00 23.56           N  
ANISOU 1546  N   GLY A 256     3280   3309   2365   -206    364   -467       N  
ATOM   1547  CA  GLY A 256     -36.112 -39.239  20.744  1.00 26.76           C  
ANISOU 1547  CA  GLY A 256     3732   3720   2717   -225    286   -372       C  
ATOM   1548  C   GLY A 256     -35.235 -38.363  21.639  1.00 30.59           C  
ANISOU 1548  C   GLY A 256     4260   4230   3134   -282    287   -400       C  
ATOM   1549  O   GLY A 256     -35.730 -37.555  22.434  1.00 28.76           O  
ANISOU 1549  O   GLY A 256     4031   4022   2875   -328    356   -496       O  
ATOM   1550  N   GLN A 257     -33.913 -38.514  21.519  1.00 28.44           N  
ANISOU 1550  N   GLN A 257     4017   3952   2838   -284    212   -323       N  
ATOM   1551  CA  GLN A 257     -32.974 -37.685  22.284  1.00 26.88           C  
ANISOU 1551  CA  GLN A 257     3857   3778   2578   -340    200   -346       C  
ATOM   1552  C   GLN A 257     -31.877 -37.252  21.319  1.00 27.66           C  
ANISOU 1552  C   GLN A 257     3950   3820   2741   -272    137   -302       C  
ATOM   1553  O   GLN A 257     -31.021 -38.069  20.937  1.00 26.76           O  
ANISOU 1553  O   GLN A 257     3839   3700   2629   -258     68   -206       O  
ATOM   1554  CB  GLN A 257     -32.368 -38.423  23.480  1.00 29.13           C  
ANISOU 1554  CB  GLN A 257     4187   4142   2739   -446    167   -284       C  
ATOM   1555  CG  GLN A 257     -31.302 -37.616  24.261  1.00 31.78           C  
ANISOU 1555  CG  GLN A 257     4560   4514   3001   -513    141   -301       C  
ATOM   1556  CD  GLN A 257     -30.740 -38.415  25.409  1.00 33.42           C  
ANISOU 1556  CD  GLN A 257     4809   4807   3081   -621     95   -223       C  
ATOM   1557  OE1 GLN A 257     -31.450 -38.703  26.395  1.00 36.11           O  
ANISOU 1557  OE1 GLN A 257     5172   5218   3329   -709    143   -250       O  
ATOM   1558  NE2 GLN A 257     -29.504 -38.844  25.273  1.00 30.83           N  
ANISOU 1558  NE2 GLN A 257     4487   4477   2752   -617      0   -119       N  
ATOM   1559  N   PRO A 258     -31.918 -36.018  20.826  1.00 28.79           N  
ANISOU 1559  N   PRO A 258     4078   3912   2950   -226    163   -369       N  
ATOM   1560  CA  PRO A 258     -30.937 -35.618  19.809  1.00 26.86           C  
ANISOU 1560  CA  PRO A 258     3826   3612   2767   -164    108   -325       C  
ATOM   1561  C   PRO A 258     -29.558 -35.400  20.423  1.00 25.88           C  
ANISOU 1561  C   PRO A 258     3736   3515   2581   -221     60   -293       C  
ATOM   1562  O   PRO A 258     -29.388 -35.272  21.649  1.00 24.61           O  
ANISOU 1562  O   PRO A 258     3607   3415   2330   -311     72   -322       O  
ATOM   1563  CB  PRO A 258     -31.521 -34.318  19.230  1.00 28.72           C  
ANISOU 1563  CB  PRO A 258     4038   3784   3091   -107    154   -404       C  
ATOM   1564  CG  PRO A 258     -32.382 -33.765  20.380  1.00 28.63           C  
ANISOU 1564  CG  PRO A 258     4031   3802   3045   -168    235   -510       C  
ATOM   1565  CD  PRO A 258     -32.982 -35.012  21.020  1.00 27.01           C  
ANISOU 1565  CD  PRO A 258     3831   3666   2766   -217    246   -484       C  
ATOM   1566  N   LEU A 259     -28.554 -35.380  19.534  1.00 21.98           N  
ANISOU 1566  N   LEU A 259     3233   2983   2136   -174      4   -233       N  
ATOM   1567  CA  LEU A 259     -27.150 -35.377  19.947  1.00 23.90           C  
ANISOU 1567  CA  LEU A 259     3494   3250   2336   -219    -56   -185       C  
ATOM   1568  C   LEU A 259     -26.819 -34.245  20.923  1.00 26.99           C  
ANISOU 1568  C   LEU A 259     3914   3667   2675   -291    -33   -260       C  
ATOM   1569  O   LEU A 259     -26.023 -34.443  21.855  1.00 24.64           O  
ANISOU 1569  O   LEU A 259     3639   3430   2295   -371    -73   -233       O  
ATOM   1570  CB  LEU A 259     -26.249 -35.268  18.710  1.00 25.17           C  
ANISOU 1570  CB  LEU A 259     3633   3356   2575   -151    -98   -135       C  
ATOM   1571  CG  LEU A 259     -24.727 -35.390  18.921  1.00 26.37           C  
ANISOU 1571  CG  LEU A 259     3787   3526   2709   -184   -164    -75       C  
ATOM   1572  CD1 LEU A 259     -24.338 -36.786  19.488  1.00 26.20           C  
ANISOU 1572  CD1 LEU A 259     3761   3550   2644   -218   -218     13       C  
ATOM   1573  CD2 LEU A 259     -24.038 -35.108  17.588  1.00 24.29           C  
ANISOU 1573  CD2 LEU A 259     3498   3202   2529   -116   -182    -49       C  
ATOM   1574  N   TRP A 260     -27.382 -33.035  20.732  1.00 26.65           N  
ANISOU 1574  N   TRP A 260     3868   3577   2682   -270     29   -354       N  
ATOM   1575  CA  TRP A 260     -26.992 -31.980  21.676  1.00 28.87           C  
ANISOU 1575  CA  TRP A 260     4176   3877   2916   -346     55   -435       C  
ATOM   1576  C   TRP A 260     -27.442 -32.297  23.101  1.00 29.05           C  
ANISOU 1576  C   TRP A 260     4227   3989   2821   -450     86   -480       C  
ATOM   1577  O   TRP A 260     -26.770 -31.915  24.064  1.00 30.87           O  
ANISOU 1577  O   TRP A 260     4487   4274   2966   -544     75   -509       O  
ATOM   1578  CB  TRP A 260     -27.527 -30.603  21.231  1.00 30.17           C  
ANISOU 1578  CB  TRP A 260     4328   3961   3176   -303    120   -532       C  
ATOM   1579  CG  TRP A 260     -28.979 -30.513  20.899  1.00 29.00           C  
ANISOU 1579  CG  TRP A 260     4152   3775   3093   -247    186   -583       C  
ATOM   1580  CD1 TRP A 260     -29.998 -30.066  21.740  1.00 31.30           C  
ANISOU 1580  CD1 TRP A 260     4442   4079   3373   -287    271   -694       C  
ATOM   1581  CD2 TRP A 260     -29.606 -30.800  19.621  1.00 30.68           C  
ANISOU 1581  CD2 TRP A 260     4327   3931   3400   -145    176   -535       C  
ATOM   1582  NE1 TRP A 260     -31.205 -30.070  21.045  1.00 31.05           N  
ANISOU 1582  NE1 TRP A 260     4366   3997   3434   -208    310   -711       N  
ATOM   1583  CE2 TRP A 260     -30.992 -30.533  19.760  1.00 31.73           C  
ANISOU 1583  CE2 TRP A 260     4432   4046   3579   -123    248   -611       C  
ATOM   1584  CE3 TRP A 260     -29.130 -31.277  18.369  1.00 29.59           C  
ANISOU 1584  CE3 TRP A 260     4173   3763   3307    -75    115   -438       C  
ATOM   1585  CZ2 TRP A 260     -31.901 -30.710  18.697  1.00 30.60           C  
ANISOU 1585  CZ2 TRP A 260     4244   3856   3525    -34    249   -585       C  
ATOM   1586  CZ3 TRP A 260     -30.046 -31.447  17.328  1.00 31.18           C  
ANISOU 1586  CZ3 TRP A 260     4338   3924   3585      6    122   -420       C  
ATOM   1587  CH2 TRP A 260     -31.413 -31.159  17.508  1.00 32.13           C  
ANISOU 1587  CH2 TRP A 260     4431   4029   3750     26    183   -488       C  
ATOM   1588  N   ILE A 261     -28.533 -33.043  23.261  1.00 27.56           N  
ANISOU 1588  N   ILE A 261     4031   3824   2617   -445    122   -481       N  
ATOM   1589  CA  ILE A 261     -29.007 -33.421  24.590  1.00 28.49           C  
ANISOU 1589  CA  ILE A 261     4178   4033   2613   -552    157   -517       C  
ATOM   1590  C   ILE A 261     -28.169 -34.551  25.149  1.00 27.68           C  
ANISOU 1590  C   ILE A 261     4098   4006   2412   -614     70   -398       C  
ATOM   1591  O   ILE A 261     -27.775 -34.512  26.313  1.00 28.99           O  
ANISOU 1591  O   ILE A 261     4301   4257   2458   -726     59   -408       O  
ATOM   1592  CB  ILE A 261     -30.509 -33.811  24.559  1.00 28.65           C  
ANISOU 1592  CB  ILE A 261     4177   4051   2657   -528    232   -562       C  
ATOM   1593  CG1 ILE A 261     -31.382 -32.603  24.203  1.00 30.88           C  
ANISOU 1593  CG1 ILE A 261     4429   4261   3041   -477    320   -687       C  
ATOM   1594  CG2 ILE A 261     -31.000 -34.310  25.929  1.00 28.87           C  
ANISOU 1594  CG2 ILE A 261     4237   4182   2549   -649    271   -590       C  
ATOM   1595  CD1 ILE A 261     -31.128 -31.482  25.149  1.00 31.54           C  
ANISOU 1595  CD1 ILE A 261     4539   4365   3079   -560    373   -801       C  
ATOM   1596  N   THR A 262     -27.905 -35.585  24.331  1.00 27.60           N  
ANISOU 1596  N   THR A 262     4066   3967   2455   -545      8   -284       N  
ATOM   1597  CA  THR A 262     -26.996 -36.653  24.754  1.00 27.99           C  
ANISOU 1597  CA  THR A 262     4126   4067   2443   -589    -82   -159       C  
ATOM   1598  C   THR A 262     -25.661 -36.077  25.241  1.00 25.52           C  
ANISOU 1598  C   THR A 262     3827   3787   2084   -647   -143   -144       C  
ATOM   1599  O   THR A 262     -25.126 -36.485  26.283  1.00 28.20           O  
ANISOU 1599  O   THR A 262     4191   4209   2314   -744   -195    -91       O  
ATOM   1600  CB  THR A 262     -26.775 -37.628  23.582  1.00 29.30           C  
ANISOU 1600  CB  THR A 262     4254   4169   2709   -490   -130    -61       C  
ATOM   1601  OG1 THR A 262     -28.059 -38.060  23.077  1.00 28.35           O  
ANISOU 1601  OG1 THR A 262     4119   4020   2635   -440    -71    -89       O  
ATOM   1602  CG2 THR A 262     -25.983 -38.826  24.050  1.00 27.17           C  
ANISOU 1602  CG2 THR A 262     3986   3938   2399   -530   -217     68       C  
ATOM   1603  N   ALA A 263     -25.117 -35.111  24.492  1.00 25.10           N  
ANISOU 1603  N   ALA A 263     3757   3670   2109   -592   -140   -186       N  
ATOM   1604  CA  ALA A 263     -23.871 -34.452  24.870  1.00 28.30           C  
ANISOU 1604  CA  ALA A 263     4170   4100   2482   -645   -191   -185       C  
ATOM   1605  C   ALA A 263     -23.984 -33.760  26.243  1.00 31.35           C  
ANISOU 1605  C   ALA A 263     4598   4570   2741   -774   -158   -273       C  
ATOM   1606  O   ALA A 263     -23.188 -34.023  27.159  1.00 27.48           O  
ANISOU 1606  O   ALA A 263     4126   4165   2149   -870   -225   -222       O  
ATOM   1607  CB  ALA A 263     -23.514 -33.454  23.750  1.00 27.50           C  
ANISOU 1607  CB  ALA A 263     4045   3906   2497   -563   -172   -229       C  
ATOM   1608  N   THR A 264     -24.960 -32.856  26.398  1.00 31.01           N  
ANISOU 1608  N   THR A 264     4569   4506   2707   -781    -56   -407       N  
ATOM   1609  CA  THR A 264     -25.128 -32.138  27.671  1.00 33.27           C  
ANISOU 1609  CA  THR A 264     4894   4869   2878   -908     -5   -516       C  
ATOM   1610  C   THR A 264     -25.322 -33.078  28.840  1.00 33.91           C  
ANISOU 1610  C   THR A 264     5009   5071   2807  -1019    -29   -466       C  
ATOM   1611  O   THR A 264     -24.820 -32.820  29.942  1.00 35.89           O  
ANISOU 1611  O   THR A 264     5294   5417   2926  -1148    -49   -490       O  
ATOM   1612  CB  THR A 264     -26.322 -31.179  27.590  1.00 37.28           C  
ANISOU 1612  CB  THR A 264     5399   5322   3444   -885    122   -669       C  
ATOM   1613  OG1 THR A 264     -26.153 -30.361  26.436  1.00 40.12           O  
ANISOU 1613  OG1 THR A 264     5728   5564   3952   -778    133   -692       O  
ATOM   1614  CG2 THR A 264     -26.356 -30.263  28.792  1.00 38.20           C  
ANISOU 1614  CG2 THR A 264     5552   5502   3460  -1014    185   -805       C  
ATOM   1615  N   LYS A 265     -26.046 -34.171  28.645  1.00 32.72           N  
ANISOU 1615  N   LYS A 265     4848   4920   2662   -982    -29   -394       N  
ATOM   1616  CA  LYS A 265     -26.266 -35.056  29.772  1.00 33.23           C  
ANISOU 1616  CA  LYS A 265     4948   5098   2581  -1095    -49   -339       C  
ATOM   1617  C   LYS A 265     -24.983 -35.709  30.250  1.00 33.66           C  
ANISOU 1617  C   LYS A 265     5010   5218   2561  -1155   -180   -198       C  
ATOM   1618  O   LYS A 265     -24.901 -36.160  31.400  1.00 35.38           O  
ANISOU 1618  O   LYS A 265     5265   5549   2629  -1282   -212   -156       O  
ATOM   1619  CB  LYS A 265     -27.278 -36.150  29.378  1.00 35.86           C  
ANISOU 1619  CB  LYS A 265     5265   5405   2954  -1037    -25   -282       C  
ATOM   1620  CG  LYS A 265     -28.744 -35.764  29.594  1.00 38.74           C  
ANISOU 1620  CG  LYS A 265     5632   5769   3317  -1048    107   -415       C  
ATOM   1621  CD  LYS A 265     -29.657 -36.767  28.884  1.00 39.96           C  
ANISOU 1621  CD  LYS A 265     5757   5876   3550   -964    123   -358       C  
ATOM   1622  CE  LYS A 265     -30.954 -37.106  29.587  1.00 42.36           C  
ANISOU 1622  CE  LYS A 265     6074   6236   3787  -1030    215   -418       C  
ATOM   1623  NZ  LYS A 265     -31.425 -36.044  30.478  1.00 45.29           N  
ANISOU 1623  NZ  LYS A 265     6466   6659   4083  -1122    316   -576       N  
ATOM   1624  N   GLN A 266     -23.980 -35.774  29.404  1.00 33.77           N  
ANISOU 1624  N   GLN A 266     4988   5169   2676  -1072   -258   -122       N  
ATOM   1625  CA  GLN A 266     -22.746 -36.472  29.718  1.00 33.80           C  
ANISOU 1625  CA  GLN A 266     4981   5219   2643  -1109   -388     22       C  
ATOM   1626  C   GLN A 266     -21.558 -35.523  29.821  1.00 34.48           C  
ANISOU 1626  C   GLN A 266     5059   5318   2723  -1143   -435     -8       C  
ATOM   1627  O   GLN A 266     -20.415 -35.964  29.843  1.00 36.06           O  
ANISOU 1627  O   GLN A 266     5233   5537   2933  -1150   -545    106       O  
ATOM   1628  CB  GLN A 266     -22.531 -37.574  28.677  1.00 33.04           C  
ANISOU 1628  CB  GLN A 266     4837   5039   2677   -988   -442    149       C  
ATOM   1629  CG  GLN A 266     -23.633 -38.681  28.816  1.00 31.89           C  
ANISOU 1629  CG  GLN A 266     4704   4900   2514   -983   -411    197       C  
ATOM   1630  CD  GLN A 266     -23.569 -39.725  27.686  1.00 34.10           C  
ANISOU 1630  CD  GLN A 266     4936   5084   2936   -860   -444    295       C  
ATOM   1631  OE1 GLN A 266     -22.590 -40.477  27.571  1.00 32.87           O  
ANISOU 1631  OE1 GLN A 266     4750   4916   2823   -843   -542    421       O  
ATOM   1632  NE2 GLN A 266     -24.636 -39.807  26.888  1.00 35.68           N  
ANISOU 1632  NE2 GLN A 266     5127   5218   3213   -780   -362    235       N  
ATOM   1633  N   GLY A 267     -21.795 -34.232  29.955  1.00 33.64           N  
ANISOU 1633  N   GLY A 267     4972   5204   2604  -1174   -354   -161       N  
ATOM   1634  CA  GLY A 267     -20.695 -33.353  30.273  1.00 33.54           C  
ANISOU 1634  CA  GLY A 267     4960   5222   2563  -1236   -397   -196       C  
ATOM   1635  C   GLY A 267     -19.990 -32.756  29.070  1.00 35.43           C  
ANISOU 1635  C   GLY A 267     5156   5351   2956  -1127   -407   -202       C  
ATOM   1636  O   GLY A 267     -18.965 -32.075  29.251  1.00 37.23           O  
ANISOU 1636  O   GLY A 267     5375   5598   3173  -1174   -451   -220       O  
ATOM   1637  N   VAL A 268     -20.512 -32.972  27.863  1.00 31.67           N  
ANISOU 1637  N   VAL A 268     4651   4767   2614   -991   -367   -191       N  
ATOM   1638  CA  VAL A 268     -19.943 -32.446  26.620  1.00 31.33           C  
ANISOU 1638  CA  VAL A 268     4569   4620   2714   -887   -369   -193       C  
ATOM   1639  C   VAL A 268     -20.786 -31.263  26.157  1.00 29.64           C  
ANISOU 1639  C   VAL A 268     4369   4328   2565   -846   -256   -334       C  
ATOM   1640  O   VAL A 268     -21.981 -31.417  25.907  1.00 32.47           O  
ANISOU 1640  O   VAL A 268     4734   4654   2951   -799   -186   -372       O  
ATOM   1641  CB  VAL A 268     -19.908 -33.546  25.547  1.00 31.42           C  
ANISOU 1641  CB  VAL A 268     4539   4570   2828   -771   -406    -79       C  
ATOM   1642  CG1 VAL A 268     -19.438 -32.988  24.207  1.00 31.69           C  
ANISOU 1642  CG1 VAL A 268     4538   4503   2999   -670   -394    -89       C  
ATOM   1643  CG2 VAL A 268     -19.023 -34.754  26.030  1.00 31.15           C  
ANISOU 1643  CG2 VAL A 268     4483   4600   2754   -806   -521     68       C  
ATOM   1644  N   ARG A 269     -20.190 -30.075  26.055  1.00 29.83           N  
ANISOU 1644  N   ARG A 269     4394   4319   2622   -866   -240   -410       N  
ATOM   1645  CA  ARG A 269     -20.928 -28.862  25.738  1.00 29.28           C  
ANISOU 1645  CA  ARG A 269     4335   4169   2621   -838   -136   -542       C  
ATOM   1646  C   ARG A 269     -21.198 -28.732  24.245  1.00 29.21           C  
ANISOU 1646  C   ARG A 269     4295   4042   2763   -700   -115   -514       C  
ATOM   1647  O   ARG A 269     -20.317 -29.024  23.421  1.00 28.61           O  
ANISOU 1647  O   ARG A 269     4189   3936   2745   -646   -177   -425       O  
ATOM   1648  CB  ARG A 269     -20.110 -27.667  26.235  1.00 34.11           C  
ANISOU 1648  CB  ARG A 269     4961   4787   3212   -923   -131   -629       C  
ATOM   1649  CG  ARG A 269     -20.780 -26.349  26.237  1.00 39.18           C  
ANISOU 1649  CG  ARG A 269     5618   5355   3913   -925    -24   -780       C  
ATOM   1650  CD  ARG A 269     -19.833 -25.314  26.947  1.00 43.61           C  
ANISOU 1650  CD  ARG A 269     6196   5943   4430  -1037    -29   -864       C  
ATOM   1651  NE  ARG A 269     -19.444 -25.787  28.291  1.00 47.88           N  
ANISOU 1651  NE  ARG A 269     6764   6631   4796  -1178    -76   -862       N  
ATOM   1652  CZ  ARG A 269     -18.209 -26.115  28.706  1.00 48.70           C  
ANISOU 1652  CZ  ARG A 269     6860   6818   4824  -1250   -182   -784       C  
ATOM   1653  NH1 ARG A 269     -17.148 -26.009  27.908  1.00 48.31           N  
ANISOU 1653  NH1 ARG A 269     6774   6720   4862  -1198   -247   -711       N  
ATOM   1654  NH2 ARG A 269     -18.029 -26.543  29.953  1.00 48.89           N  
ANISOU 1654  NH2 ARG A 269     6912   6981   4684  -1382   -224   -779       N  
ATOM   1655  N   ALA A 270     -22.413 -28.277  23.876  1.00 29.39           N  
ANISOU 1655  N   ALA A 270     4319   3999   2850   -644    -28   -589       N  
ATOM   1656  CA  ALA A 270     -22.805 -28.155  22.466  1.00 34.27           C  
ANISOU 1656  CA  ALA A 270     4907   4513   3600   -518    -12   -557       C  
ATOM   1657  C   ALA A 270     -22.987 -26.697  22.044  1.00 38.76           C  
ANISOU 1657  C   ALA A 270     5475   4983   4268   -493     52   -649       C  
ATOM   1658  O   ALA A 270     -23.496 -25.879  22.826  1.00 38.77           O  
ANISOU 1658  O   ALA A 270     5494   4979   4257   -548    121   -768       O  
ATOM   1659  CB  ALA A 270     -24.101 -28.910  22.200  1.00 36.69           C  
ANISOU 1659  CB  ALA A 270     5203   4815   3921   -460     24   -545       C  
ATOM   1660  N   GLY A 271     -22.536 -26.365  20.815  1.00 37.47           N  
ANISOU 1660  N   GLY A 271     5290   4739   4205   -415     29   -594       N  
ATOM   1661  CA  GLY A 271     -22.959 -25.144  20.153  1.00 40.01           C  
ANISOU 1661  CA  GLY A 271     5606   4950   4645   -364     85   -651       C  
ATOM   1662  C   GLY A 271     -24.359 -25.306  19.552  1.00 43.88           C  
ANISOU 1662  C   GLY A 271     6076   5392   5205   -277    129   -655       C  
ATOM   1663  O   GLY A 271     -24.983 -26.363  19.628  1.00 44.44           O  
ANISOU 1663  O   GLY A 271     6139   5516   5230   -259    120   -619       O  
ATOM   1664  N   THR A 272     -24.845 -24.253  18.898  1.00 47.30           N  
ANISOU 1664  N   THR A 272     6496   5719   5758   -222    172   -690       N  
ATOM   1665  CA  THR A 272     -26.157 -24.334  18.259  1.00 48.89           C  
ANISOU 1665  CA  THR A 272     6668   5871   6038   -136    204   -686       C  
ATOM   1666  C   THR A 272     -26.181 -25.385  17.161  1.00 50.15           C  
ANISOU 1666  C   THR A 272     6810   6052   6194    -67    144   -565       C  
ATOM   1667  O   THR A 272     -25.185 -25.641  16.480  1.00 53.94           O  
ANISOU 1667  O   THR A 272     7294   6539   6663    -59     88   -484       O  
ATOM   1668  CB  THR A 272     -26.564 -22.996  17.642  1.00 53.15           C  
ANISOU 1668  CB  THR A 272     7190   6283   6723    -84    245   -722       C  
ATOM   1669  OG1 THR A 272     -27.991 -22.969  17.425  1.00 55.25           O  
ANISOU 1669  OG1 THR A 272     7420   6509   7064    -19    288   -750       O  
ATOM   1670  CG2 THR A 272     -25.856 -22.784  16.304  1.00 50.92           C  
ANISOU 1670  CG2 THR A 272     6904   5948   6497    -30    188   -614       C  
ATOM   1671  N   PHE A 273     -27.335 -26.003  16.987  1.00 47.31           N  
ANISOU 1671  N   PHE A 273     6427   5705   5844    -21    160   -561       N  
ATOM   1672  CA  PHE A 273     -27.567 -26.844  15.836  1.00 47.37           C  
ANISOU 1672  CA  PHE A 273     6414   5719   5867     48    115   -463       C  
ATOM   1673  C   PHE A 273     -28.585 -26.264  14.863  1.00 51.25           C  
ANISOU 1673  C   PHE A 273     6870   6132   6471    131    131   -454       C  
ATOM   1674  O   PHE A 273     -28.797 -26.858  13.806  1.00 54.70           O  
ANISOU 1674  O   PHE A 273     7290   6575   6919    184     91   -375       O  
ATOM   1675  CB  PHE A 273     -28.037 -28.242  16.262  1.00 44.23           C  
ANISOU 1675  CB  PHE A 273     6013   5407   5387     34    105   -444       C  
ATOM   1676  CG  PHE A 273     -26.919 -29.181  16.640  1.00 39.72           C  
ANISOU 1676  CG  PHE A 273     5463   4908   4721    -17     54   -389       C  
ATOM   1677  CD1 PHE A 273     -26.042 -28.857  17.654  1.00 41.23           C  
ANISOU 1677  CD1 PHE A 273     5681   5133   4851    -98     50   -422       C  
ATOM   1678  CD2 PHE A 273     -26.781 -30.386  15.995  1.00 35.82           C  
ANISOU 1678  CD2 PHE A 273     4958   4447   4207     13     10   -306       C  
ATOM   1679  CE1 PHE A 273     -25.027 -29.749  18.023  1.00 40.76           C  
ANISOU 1679  CE1 PHE A 273     5632   5140   4714   -143     -8   -361       C  
ATOM   1680  CE2 PHE A 273     -25.804 -31.282  16.347  1.00 36.40           C  
ANISOU 1680  CE2 PHE A 273     5040   4575   4214    -28    -37   -253       C  
ATOM   1681  CZ  PHE A 273     -24.923 -30.965  17.389  1.00 38.04           C  
ANISOU 1681  CZ  PHE A 273     5271   4819   4365   -104    -50   -275       C  
ATOM   1682  N   PHE A 274     -29.232 -25.151  15.195  1.00 50.70           N  
ANISOU 1682  N   PHE A 274     6787   5990   6487    141    186   -532       N  
ATOM   1683  CA  PHE A 274     -30.149 -24.464  14.299  1.00 49.10           C  
ANISOU 1683  CA  PHE A 274     6544   5700   6411    221    193   -514       C  
ATOM   1684  C   PHE A 274     -29.607 -23.081  13.982  1.00 46.55           C  
ANISOU 1684  C   PHE A 274     6229   5275   6183    227    200   -520       C  
ATOM   1685  O   PHE A 274     -29.089 -22.372  14.864  1.00 45.30           O  
ANISOU 1685  O   PHE A 274     6094   5094   6025    169    241   -601       O  
ATOM   1686  CB  PHE A 274     -31.550 -24.338  14.912  1.00 50.03           C  
ANISOU 1686  CB  PHE A 274     6621   5804   6585    239    257   -602       C  
ATOM   1687  N   TRP A 275     -29.769 -22.664  12.734  1.00 44.81           N  
ANISOU 1687  N   TRP A 275     5989   4990   6045    292    162   -434       N  
ATOM   1688  CA  TRP A 275     -29.356 -21.320  12.354  1.00 43.11           C  
ANISOU 1688  CA  TRP A 275     5780   4666   5936    302    167   -425       C  
ATOM   1689  C   TRP A 275     -30.534 -20.533  11.792  1.00 44.38           C  
ANISOU 1689  C   TRP A 275     5888   4724   6249    380    178   -413       C  
ATOM   1690  O   TRP A 275     -31.256 -21.016  10.914  1.00 43.76           O  
ANISOU 1690  O   TRP A 275     5778   4664   6186    438    135   -336       O  
ATOM   1691  CB  TRP A 275     -28.219 -21.387  11.336  1.00 41.75           C  
ANISOU 1691  CB  TRP A 275     5636   4502   5725    295    106   -317       C  
ATOM   1692  CG  TRP A 275     -26.926 -21.911  11.928  1.00 39.22           C  
ANISOU 1692  CG  TRP A 275     5356   4259   5288    219     97   -333       C  
ATOM   1693  CD1 TRP A 275     -26.431 -23.205  11.852  1.00 36.63           C  
ANISOU 1693  CD1 TRP A 275     5038   4036   4844    200     60   -291       C  
ATOM   1694  CD2 TRP A 275     -25.986 -21.163  12.686  1.00 34.96           C  
ANISOU 1694  CD2 TRP A 275     4845   3693   4747    153    123   -395       C  
ATOM   1695  NE1 TRP A 275     -25.230 -23.286  12.509  1.00 35.80           N  
ANISOU 1695  NE1 TRP A 275     4961   3970   4671    130     56   -314       N  
ATOM   1696  CE2 TRP A 275     -24.923 -22.048  13.027  1.00 35.06           C  
ANISOU 1696  CE2 TRP A 275     4880   3804   4638     96     92   -378       C  
ATOM   1697  CE3 TRP A 275     -25.931 -19.836  13.116  1.00 33.01           C  
ANISOU 1697  CE3 TRP A 275     4602   3346   4594    134    170   -466       C  
ATOM   1698  CZ2 TRP A 275     -23.831 -21.644  13.779  1.00 31.77           C  
ANISOU 1698  CZ2 TRP A 275     4488   3398   4185     20     99   -425       C  
ATOM   1699  CZ3 TRP A 275     -24.827 -19.424  13.847  1.00 32.72           C  
ANISOU 1699  CZ3 TRP A 275     4596   3319   4518     52    183   -521       C  
ATOM   1700  CH2 TRP A 275     -23.783 -20.332  14.170  1.00 32.03           C  
ANISOU 1700  CH2 TRP A 275     4529   3341   4300     -5    144   -497       C  
ATOM   1701  N   SER A 276     -30.715 -19.326  12.291  1.00 46.19           N  
ANISOU 1701  N   SER A 276     6105   4846   6597    380    233   -490       N  
ATOM   1702  CA  SER A 276     -31.701 -18.435  11.706  1.00 52.00           C  
ANISOU 1702  CA  SER A 276     6788   5465   7507    458    237   -466       C  
ATOM   1703  C   SER A 276     -31.387 -18.145  10.236  1.00 53.21           C  
ANISOU 1703  C   SER A 276     6943   5576   7698    502    156   -310       C  
ATOM   1704  O   SER A 276     -30.272 -17.736   9.888  1.00 50.97           O  
ANISOU 1704  O   SER A 276     6705   5272   7390    465    134   -263       O  
ATOM   1705  CB  SER A 276     -31.743 -17.147  12.500  1.00 54.99           C  
ANISOU 1705  CB  SER A 276     7157   5722   8015    442    315   -579       C  
ATOM   1706  OG  SER A 276     -32.989 -16.544  12.316  1.00 60.24           O  
ANISOU 1706  OG  SER A 276     7751   6288   8850    519    340   -595       O  
ATOM   1707  N   VAL A 277     -32.395 -18.342   9.381  1.00 54.99           N  
ANISOU 1707  N   VAL A 277     7118   5793   7981    573    111   -231       N  
ATOM   1708  CA  VAL A 277     -32.292 -18.120   7.937  1.00 57.07           C  
ANISOU 1708  CA  VAL A 277     7381   6033   8271    611     28    -75       C  
ATOM   1709  C   VAL A 277     -31.643 -16.779   7.583  1.00 56.52           C  
ANISOU 1709  C   VAL A 277     7331   5835   8311    607     25    -31       C  
ATOM   1710  O   VAL A 277     -30.901 -16.686   6.599  1.00 57.05           O  
ANISOU 1710  O   VAL A 277     7432   5909   8334    592    -31     84       O  
ATOM   1711  CB  VAL A 277     -33.701 -18.264   7.309  1.00 60.19           C  
ANISOU 1711  CB  VAL A 277     7702   6416   8751    690    -11    -20       C  
ATOM   1712  CG1 VAL A 277     -33.849 -17.441   6.039  1.00 60.24           C  
ANISOU 1712  CG1 VAL A 277     7690   6339   8860    737    -84    127       C  
ATOM   1713  CG2 VAL A 277     -33.960 -19.726   7.026  1.00 60.58           C  
ANISOU 1713  CG2 VAL A 277     7751   6611   8654    682    -46      4       C  
ATOM   1714  N   SER A 278     -31.852 -15.745   8.389  1.00 53.98           N  
ANISOU 1714  N   SER A 278     6990   5394   8126    612     93   -128       N  
ATOM   1715  CA  SER A 278     -31.293 -14.465   7.998  1.00 55.16           C  
ANISOU 1715  CA  SER A 278     7156   5409   8395    610     90    -80       C  
ATOM   1716  C   SER A 278     -29.817 -14.297   8.362  1.00 54.38           C  
ANISOU 1716  C   SER A 278     7128   5330   8205    522    112   -113       C  
ATOM   1717  O   SER A 278     -29.231 -13.257   8.038  1.00 53.85           O  
ANISOU 1717  O   SER A 278     7080   5154   8226    508    112    -74       O  
ATOM   1718  CB  SER A 278     -32.097 -13.324   8.613  1.00 57.20           C  
ANISOU 1718  CB  SER A 278     7359   5509   8864    653    155   -167       C  
ATOM   1719  OG  SER A 278     -31.927 -13.301  10.007  1.00 60.23           O  
ANISOU 1719  OG  SER A 278     7755   5904   9225    599    251   -346       O  
ATOM   1720  N   ILE A 279     -29.176 -15.246   9.029  1.00 49.35           N  
ANISOU 1720  N   ILE A 279     6527   4820   7402    460    129   -181       N  
ATOM   1721  CA  ILE A 279     -27.770 -15.103   9.390  1.00 46.60           C  
ANISOU 1721  CA  ILE A 279     6236   4496   6973    377    144   -210       C  
ATOM   1722  C   ILE A 279     -26.943 -15.636   8.228  1.00 40.43           C  
ANISOU 1722  C   ILE A 279     5486   3786   6089    363     71    -72       C  
ATOM   1723  O   ILE A 279     -27.110 -16.813   7.860  1.00 40.58           O  
ANISOU 1723  O   ILE A 279     5502   3922   5995    374     33    -29       O  
ATOM   1724  CB  ILE A 279     -27.433 -15.817  10.701  1.00 47.82           C  
ANISOU 1724  CB  ILE A 279     6410   4752   7007    312    191   -342       C  
ATOM   1725  CG1 ILE A 279     -28.187 -15.102  11.842  1.00 50.54           C  
ANISOU 1725  CG1 ILE A 279     6727   5018   7458    310    276   -491       C  
ATOM   1726  CG2 ILE A 279     -25.909 -15.786  10.918  1.00 45.52           C  
ANISOU 1726  CG2 ILE A 279     6170   4502   6624    227    185   -347       C  
ATOM   1727  CD1 ILE A 279     -28.163 -15.837  13.151  1.00 51.77           C  
ANISOU 1727  CD1 ILE A 279     6897   5282   7493    248    324   -619       C  
ATOM   1728  N   PRO A 280     -26.108 -14.811   7.590  1.00 38.92           N  
ANISOU 1728  N   PRO A 280     5322   3525   5941    338     55     -1       N  
ATOM   1729  CA  PRO A 280     -25.386 -15.285   6.393  1.00 38.79           C  
ANISOU 1729  CA  PRO A 280     5331   3577   5829    322     -6    130       C  
ATOM   1730  C   PRO A 280     -24.385 -16.382   6.742  1.00 38.02           C  
ANISOU 1730  C   PRO A 280     5261   3617   5568    261     -6     94       C  
ATOM   1731  O   PRO A 280     -23.870 -16.445   7.859  1.00 40.10           O  
ANISOU 1731  O   PRO A 280     5535   3902   5798    213     34    -14       O  
ATOM   1732  CB  PRO A 280     -24.666 -14.033   5.857  1.00 41.33           C  
ANISOU 1732  CB  PRO A 280     5677   3784   6244    294     -7    193       C  
ATOM   1733  CG  PRO A 280     -24.721 -12.989   6.968  1.00 41.68           C  
ANISOU 1733  CG  PRO A 280     5716   3708   6414    279     62     70       C  
ATOM   1734  CD  PRO A 280     -25.878 -13.375   7.884  1.00 39.71           C  
ANISOU 1734  CD  PRO A 280     5426   3471   6189    323     97    -38       C  
ATOM   1735  N   HIS A 281     -24.088 -17.221   5.739  1.00 33.50           N  
ANISOU 1735  N   HIS A 281     4481   3211   5037    317   -101     63       N  
ATOM   1736  CA  HIS A 281     -23.173 -18.337   5.920  1.00 34.63           C  
ANISOU 1736  CA  HIS A 281     4647   3475   5038    283    -41     69       C  
ATOM   1737  C   HIS A 281     -21.833 -17.895   6.496  1.00 33.97           C  
ANISOU 1737  C   HIS A 281     4587   3384   4937    233    -40     60       C  
ATOM   1738  O   HIS A 281     -21.318 -18.538   7.421  1.00 32.05           O  
ANISOU 1738  O   HIS A 281     4352   3204   4622    223     12     -1       O  
ATOM   1739  CB  HIS A 281     -22.978 -19.072   4.605  1.00 35.50           C  
ANISOU 1739  CB  HIS A 281     4761   3661   5067    254    -49    177       C  
ATOM   1740  CG  HIS A 281     -24.173 -19.870   4.216  1.00 38.59           C  
ANISOU 1740  CG  HIS A 281     5130   4091   5440    297    -33    171       C  
ATOM   1741  ND1 HIS A 281     -24.176 -20.743   3.145  1.00 38.62           N  
ANISOU 1741  ND1 HIS A 281     5133   4179   5361    277    -27    240       N  
ATOM   1742  CD2 HIS A 281     -25.412 -19.930   4.768  1.00 38.06           C  
ANISOU 1742  CD2 HIS A 281     5037   3995   5428    357    -20     96       C  
ATOM   1743  CE1 HIS A 281     -25.381 -21.281   3.037  1.00 39.24           C  
ANISOU 1743  CE1 HIS A 281     5191   4271   5448    322    -18    217       C  
ATOM   1744  NE2 HIS A 281     -26.146 -20.805   4.011  1.00 38.89           N  
ANISOU 1744  NE2 HIS A 281     5130   4160   5487    372    -14    132       N  
ATOM   1745  N   GLU A 282     -21.250 -16.804   5.980  1.00 33.18           N  
ANISOU 1745  N   GLU A 282     4496   3207   4902    195   -102    128       N  
ATOM   1746  CA  GLU A 282     -19.928 -16.403   6.460  1.00 32.76           C  
ANISOU 1746  CA  GLU A 282     4465   3152   4830    141   -103    127       C  
ATOM   1747  C   GLU A 282     -19.959 -16.103   7.950  1.00 33.69           C  
ANISOU 1747  C   GLU A 282     4584   3237   4978    160    -74     -4       C  
ATOM   1748  O   GLU A 282     -18.965 -16.325   8.672  1.00 30.57           O  
ANISOU 1748  O   GLU A 282     4206   2889   4522    122    -47    -33       O  
ATOM   1749  CB  GLU A 282     -19.449 -15.167   5.694  1.00 34.91           C  
ANISOU 1749  CB  GLU A 282     4745   3334   5185     94   -184    221       C  
ATOM   1750  CG  GLU A 282     -19.276 -15.417   4.200  1.00 38.32           C  
ANISOU 1750  CG  GLU A 282     5176   3818   5564     51   -213    359       C  
ATOM   1751  CD  GLU A 282     -20.571 -15.326   3.411  1.00 42.80           C  
ANISOU 1751  CD  GLU A 282     5726   4349   6187     87   -255    402       C  
ATOM   1752  OE1 GLU A 282     -21.687 -15.473   3.990  1.00 43.69           O  
ANISOU 1752  OE1 GLU A 282     5820   4426   6354    160   -238    316       O  
ATOM   1753  OE2 GLU A 282     -20.471 -15.108   2.194  1.00 45.39           O  
ANISOU 1753  OE2 GLU A 282     6055   4691   6501     36   -306    526       O  
ATOM   1754  N   ARG A 283     -21.078 -15.527   8.405  1.00 33.45           N  
ANISOU 1754  N   ARG A 283     4534   3128   5049    212    -83    -88       N  
ATOM   1755  CA  ARG A 283     -21.248 -15.183   9.818  1.00 36.04           C  
ANISOU 1755  CA  ARG A 283     4856   3432   5405    226    -49   -233       C  
ATOM   1756  C   ARG A 283     -21.428 -16.454  10.671  1.00 33.80           C  
ANISOU 1756  C   ARG A 283     4572   3276   4995    231     30   -301       C  
ATOM   1757  O   ARG A 283     -20.909 -16.531  11.788  1.00 34.72           O  
ANISOU 1757  O   ARG A 283     4700   3431   5061    199     62   -378       O  
ATOM   1758  CB  ARG A 283     -22.445 -14.221   9.965  1.00 37.54           C  
ANISOU 1758  CB  ARG A 283     5010   3502   5751    283    -78   -312       C  
ATOM   1759  CG  ARG A 283     -22.845 -13.857  11.379  1.00 39.61           C  
ANISOU 1759  CG  ARG A 283     5254   3747   6049    300    -33   -488       C  
ATOM   1760  CD  ARG A 283     -21.693 -13.282  12.182  1.00 39.63           C  
ANISOU 1760  CD  ARG A 283     5286   3736   6038    242    -36   -533       C  
ATOM   1761  NE  ARG A 283     -21.243 -11.980  11.684  1.00 38.62           N  
ANISOU 1761  NE  ARG A 283     5161   3466   6047    227   -119   -488       N  
ATOM   1762  CZ  ARG A 283     -20.047 -11.462  11.965  1.00 38.07           C  
ANISOU 1762  CZ  ARG A 283     5122   3376   5968    166   -143   -471       C  
ATOM   1763  NH1 ARG A 283     -19.176 -12.174  12.710  1.00 37.27           N  
ANISOU 1763  NH1 ARG A 283     5047   3391   5723    117    -92   -492       N  
ATOM   1764  NH2 ARG A 283     -19.692 -10.274  11.471  1.00 37.44           N  
ANISOU 1764  NH2 ARG A 283     5044   3161   6022    149   -225   -421       N  
ATOM   1765  N   ARG A 284     -22.124 -17.463  10.151  1.00 31.16           N  
ANISOU 1765  N   ARG A 284     4225   3008   4607    261     55   -265       N  
ATOM   1766  CA  ARG A 284     -22.213 -18.741  10.866  1.00 30.77           C  
ANISOU 1766  CA  ARG A 284     4175   3076   4439    256    118   -306       C  
ATOM   1767  C   ARG A 284     -20.828 -19.339  11.096  1.00 31.12           C  
ANISOU 1767  C   ARG A 284     4245   3190   4387    198    126   -259       C  
ATOM   1768  O   ARG A 284     -20.492 -19.759  12.215  1.00 34.16           O  
ANISOU 1768  O   ARG A 284     4638   3635   4708    169    157   -318       O  
ATOM   1769  CB  ARG A 284     -23.089 -19.726  10.094  1.00 33.15           C  
ANISOU 1769  CB  ARG A 284     4459   3427   4707    293    133   -259       C  
ATOM   1770  CG  ARG A 284     -24.528 -19.248   9.834  1.00 35.51           C  
ANISOU 1770  CG  ARG A 284     4724   3664   5104    353    122   -300       C  
ATOM   1771  CD  ARG A 284     -25.295 -20.216   8.918  1.00 37.86           C  
ANISOU 1771  CD  ARG A 284     5007   4012   5364    381    127   -237       C  
ATOM   1772  NE  ARG A 284     -26.560 -19.572   8.516  1.00 39.16           N  
ANISOU 1772  NE  ARG A 284     5135   4100   5644    434     98   -256       N  
ATOM   1773  CZ  ARG A 284     -27.603 -20.152   7.917  1.00 40.16           C  
ANISOU 1773  CZ  ARG A 284     5235   4250   5772    470     99   -233       C  
ATOM   1774  NH1 ARG A 284     -27.617 -21.447   7.588  1.00 38.87           N  
ANISOU 1774  NH1 ARG A 284     5082   4187   5502    460    130   -191       N  
ATOM   1775  NH2 ARG A 284     -28.663 -19.396   7.643  1.00 41.53           N  
ANISOU 1775  NH2 ARG A 284     5370   4340   6071    517     63   -254       N  
ATOM   1776  N   ILE A 285     -20.012 -19.393  10.040  1.00 28.86           N  
ANISOU 1776  N   ILE A 285     3969   2905   4091    176     96   -152       N  
ATOM   1777  CA  ILE A 285     -18.649 -19.907  10.151  1.00 28.62           C  
ANISOU 1777  CA  ILE A 285     3951   2935   3990    125    101   -107       C  
ATOM   1778  C   ILE A 285     -17.838 -19.089  11.149  1.00 28.08           C  
ANISOU 1778  C   ILE A 285     3898   2832   3938     83     88   -157       C  
ATOM   1779  O   ILE A 285     -17.103 -19.640  11.973  1.00 27.71           O  
ANISOU 1779  O   ILE A 285     3857   2846   3825     47    104   -175       O  
ATOM   1780  CB  ILE A 285     -17.968 -19.910   8.765  1.00 29.57           C  
ANISOU 1780  CB  ILE A 285     4069   3060   4105    104     75      4       C  
ATOM   1781  CG1 ILE A 285     -18.670 -20.872   7.820  1.00 29.29           C  
ANISOU 1781  CG1 ILE A 285     4018   3078   4035    135     93     44       C  
ATOM   1782  CG2 ILE A 285     -16.433 -20.278   8.880  1.00 28.17           C  
ANISOU 1782  CG2 ILE A 285     3893   2936   3874     49     79     41       C  
ATOM   1783  CD1 ILE A 285     -18.610 -22.349   8.319  1.00 29.54           C  
ANISOU 1783  CD1 ILE A 285     4039   3200   3987    144    138     17       C  
ATOM   1784  N   LEU A 286     -17.941 -17.766  11.088  1.00 28.16           N  
ANISOU 1784  N   LEU A 286     3915   2742   4044     82     51   -176       N  
ATOM   1785  CA  LEU A 286     -17.136 -16.959  11.985  1.00 29.81           C  
ANISOU 1785  CA  LEU A 286     4139   2915   4272     37     35   -227       C  
ATOM   1786  C   LEU A 286     -17.596 -17.110  13.422  1.00 31.60           C  
ANISOU 1786  C   LEU A 286     4365   3177   4465     36     75   -354       C  
ATOM   1787  O   LEU A 286     -16.790 -16.985  14.338  1.00 32.10           O  
ANISOU 1787  O   LEU A 286     4443   3267   4489    -16     76   -392       O  
ATOM   1788  CB  LEU A 286     -17.163 -15.479  11.601  1.00 31.14           C  
ANISOU 1788  CB  LEU A 286     4311   2955   4567     36    -20   -222       C  
ATOM   1789  CG  LEU A 286     -16.415 -14.985  10.343  1.00 30.27           C  
ANISOU 1789  CG  LEU A 286     4206   2804   4491      3    -74    -91       C  
ATOM   1790  CD1 LEU A 286     -16.691 -13.520  10.031  1.00 31.99           C  
ANISOU 1790  CD1 LEU A 286     4425   2879   4853      4   -141    -85       C  
ATOM   1791  CD2 LEU A 286     -14.970 -15.127  10.531  1.00 29.70           C  
ANISOU 1791  CD2 LEU A 286     4146   2782   4357    -62    -76    -50       C  
ATOM   1792  N   THR A 287     -18.883 -17.358  13.632  1.00 33.01           N  
ANISOU 1792  N   THR A 287     4525   3362   4655     84    107   -421       N  
ATOM   1793  CA  THR A 287     -19.373 -17.610  14.977  1.00 33.15           C  
ANISOU 1793  CA  THR A 287     4536   3438   4620     71    153   -543       C  
ATOM   1794  C   THR A 287     -18.780 -18.911  15.538  1.00 28.74           C  
ANISOU 1794  C   THR A 287     3988   3005   3927     26    177   -506       C  
ATOM   1795  O   THR A 287     -18.304 -18.963  16.678  1.00 30.22           O  
ANISOU 1795  O   THR A 287     4186   3245   4050    -31    187   -561       O  
ATOM   1796  CB  THR A 287     -20.903 -17.661  14.918  1.00 35.67           C  
ANISOU 1796  CB  THR A 287     4824   3745   4985    134    183   -612       C  
ATOM   1797  OG1 THR A 287     -21.380 -16.359  14.492  1.00 37.12           O  
ANISOU 1797  OG1 THR A 287     4991   3796   5316    173    148   -649       O  
ATOM   1798  CG2 THR A 287     -21.485 -17.979  16.322  1.00 36.18           C  
ANISOU 1798  CG2 THR A 287     4876   3893   4979    109    242   -744       C  
ATOM   1799  N   ILE A 288     -18.823 -19.984  14.755  1.00 26.36           N  
ANISOU 1799  N   ILE A 288     3680   2750   3586     48    180   -414       N  
ATOM   1800  CA  ILE A 288     -18.249 -21.247  15.231  1.00 24.22           C  
ANISOU 1800  CA  ILE A 288     3412   2580   3212      9    190   -372       C  
ATOM   1801  C   ILE A 288     -16.771 -21.063  15.594  1.00 26.79           C  
ANISOU 1801  C   ILE A 288     3752   2914   3515    -52    158   -336       C  
ATOM   1802  O   ILE A 288     -16.295 -21.489  16.670  1.00 28.65           O  
ANISOU 1802  O   ILE A 288     3993   3214   3679   -109    157   -355       O  
ATOM   1803  CB  ILE A 288     -18.448 -22.316  14.162  1.00 24.35           C  
ANISOU 1803  CB  ILE A 288     3414   2624   3216     48    193   -285       C  
ATOM   1804  CG1 ILE A 288     -19.928 -22.619  14.072  1.00 25.12           C  
ANISOU 1804  CG1 ILE A 288     3494   2729   3320     96    224   -328       C  
ATOM   1805  CG2 ILE A 288     -17.550 -23.606  14.472  1.00 24.93           C  
ANISOU 1805  CG2 ILE A 288     3482   2777   3215      9    185   -224       C  
ATOM   1806  CD1 ILE A 288     -20.298 -23.411  12.751  1.00 25.19           C  
ANISOU 1806  CD1 ILE A 288     3489   2744   3338    142    222   -248       C  
ATOM   1807  N   LEU A 289     -16.033 -20.373  14.728  1.00 26.95           N  
ANISOU 1807  N   LEU A 289     3777   2870   3595    -50    128   -280       N  
ATOM   1808  CA  LEU A 289     -14.617 -20.149  14.992  1.00 30.48           C  
ANISOU 1808  CA  LEU A 289     4231   3322   4028   -109     97   -243       C  
ATOM   1809  C   LEU A 289     -14.421 -19.304  16.240  1.00 33.24           C  
ANISOU 1809  C   LEU A 289     4600   3659   4372   -158     90   -333       C  
ATOM   1810  O   LEU A 289     -13.462 -19.512  17.001  1.00 32.76           O  
ANISOU 1810  O   LEU A 289     4544   3644   4259   -219     72   -324       O  
ATOM   1811  CB  LEU A 289     -13.941 -19.479  13.776  1.00 29.96           C  
ANISOU 1811  CB  LEU A 289     4164   3194   4026   -105     68   -166       C  
ATOM   1812  CG  LEU A 289     -13.919 -20.390  12.505  1.00 27.53           C  
ANISOU 1812  CG  LEU A 289     3833   2921   3705    -74     78    -79       C  
ATOM   1813  CD1 LEU A 289     -13.509 -19.529  11.344  1.00 28.57           C  
ANISOU 1813  CD1 LEU A 289     3965   2997   3893    -82     52    -15       C  
ATOM   1814  CD2 LEU A 289     -12.924 -21.564  12.671  1.00 26.44           C  
ANISOU 1814  CD2 LEU A 289     3673   2862   3511   -101     81    -34       C  
ATOM   1815  N   GLN A 290     -15.292 -18.326  16.458  1.00 35.19           N  
ANISOU 1815  N   GLN A 290     4851   3841   4677   -134    101   -425       N  
ATOM   1816  CA  GLN A 290     -15.183 -17.541  17.690  1.00 38.87           C  
ANISOU 1816  CA  GLN A 290     5331   4303   5137   -184    102   -537       C  
ATOM   1817  C   GLN A 290     -15.515 -18.381  18.935  1.00 34.49           C  
ANISOU 1817  C   GLN A 290     4775   3863   4467   -226    136   -597       C  
ATOM   1818  O   GLN A 290     -14.827 -18.276  19.954  1.00 31.74           O  
ANISOU 1818  O   GLN A 290     4440   3563   4058   -301    125   -631       O  
ATOM   1819  CB  GLN A 290     -16.096 -16.324  17.608  1.00 47.56           C  
ANISOU 1819  CB  GLN A 290     6424   5299   6346   -142    107   -636       C  
ATOM   1820  CG  GLN A 290     -16.026 -15.466  18.840  1.00 57.00           C  
ANISOU 1820  CG  GLN A 290     7628   6485   7545   -191    114   -774       C  
ATOM   1821  CD  GLN A 290     -15.473 -14.120  18.502  1.00 64.62           C  
ANISOU 1821  CD  GLN A 290     8602   7323   8629   -196     66   -782       C  
ATOM   1822  OE1 GLN A 290     -15.893 -13.507  17.499  1.00 67.43           O  
ANISOU 1822  OE1 GLN A 290     8947   7571   9102   -140     39   -746       O  
ATOM   1823  NE2 GLN A 290     -14.504 -13.647  19.301  1.00 65.26           N  
ANISOU 1823  NE2 GLN A 290     8702   7412   8681   -270     45   -819       N  
ATOM   1824  N   TRP A 291     -16.543 -19.236  18.865  1.00 31.66           N  
ANISOU 1824  N   TRP A 291     4400   3556   4072   -189    173   -602       N  
ATOM   1825  CA  TRP A 291     -16.806 -20.139  19.991  1.00 29.47           C  
ANISOU 1825  CA  TRP A 291     4122   3399   3678   -244    197   -635       C  
ATOM   1826  C   TRP A 291     -15.591 -21.017  20.306  1.00 29.36           C  
ANISOU 1826  C   TRP A 291     4115   3451   3588   -307    157   -533       C  
ATOM   1827  O   TRP A 291     -15.257 -21.216  21.474  1.00 28.63           O  
ANISOU 1827  O   TRP A 291     4033   3438   3409   -389    149   -562       O  
ATOM   1828  CB  TRP A 291     -18.003 -21.022  19.680  1.00 26.43           C  
ANISOU 1828  CB  TRP A 291     3716   3054   3273   -194    234   -629       C  
ATOM   1829  CG  TRP A 291     -19.312 -20.281  19.795  1.00 28.29           C  
ANISOU 1829  CG  TRP A 291     3932   3254   3563   -150    280   -754       C  
ATOM   1830  CD1 TRP A 291     -19.590 -19.169  20.555  1.00 27.90           C  
ANISOU 1830  CD1 TRP A 291     3879   3179   3544   -170    301   -895       C  
ATOM   1831  CD2 TRP A 291     -20.516 -20.620  19.097  1.00 28.55           C  
ANISOU 1831  CD2 TRP A 291     3939   3272   3637    -77    307   -755       C  
ATOM   1832  NE1 TRP A 291     -20.932 -18.827  20.388  1.00 31.16           N  
ANISOU 1832  NE1 TRP A 291     4257   3559   4021   -108    343   -988       N  
ATOM   1833  CE2 TRP A 291     -21.512 -19.712  19.504  1.00 29.81           C  
ANISOU 1833  CE2 TRP A 291     4074   3397   3854    -53    345   -897       C  
ATOM   1834  CE3 TRP A 291     -20.858 -21.665  18.205  1.00 27.64           C  
ANISOU 1834  CE3 TRP A 291     3815   3173   3514    -33    304   -654       C  
ATOM   1835  CZ2 TRP A 291     -22.825 -19.778  19.016  1.00 29.79           C  
ANISOU 1835  CZ2 TRP A 291     4036   3372   3909     17    375   -933       C  
ATOM   1836  CZ3 TRP A 291     -22.138 -21.738  17.722  1.00 29.06           C  
ANISOU 1836  CZ3 TRP A 291     3967   3335   3739     31    333   -686       C  
ATOM   1837  CH2 TRP A 291     -23.127 -20.769  18.132  1.00 29.80           C  
ANISOU 1837  CH2 TRP A 291     4035   3392   3897     57    367   -823       C  
ATOM   1838  N   LEU A 292     -14.898 -21.508  19.269  1.00 28.05           N  
ANISOU 1838  N   LEU A 292     3942   3254   3462   -274    128   -417       N  
ATOM   1839  CA  LEU A 292     -13.713 -22.353  19.453  1.00 29.68           C  
ANISOU 1839  CA  LEU A 292     4142   3509   3627   -322     85   -321       C  
ATOM   1840  C   LEU A 292     -12.536 -21.629  20.108  1.00 32.09           C  
ANISOU 1840  C   LEU A 292     4461   3809   3924   -393     47   -329       C  
ATOM   1841  O   LEU A 292     -11.623 -22.320  20.567  1.00 31.39           O  
ANISOU 1841  O   LEU A 292     4363   3771   3793   -447      6   -262       O  
ATOM   1842  CB  LEU A 292     -13.244 -22.939  18.119  1.00 26.60           C  
ANISOU 1842  CB  LEU A 292     3729   3085   3293   -267     72   -219       C  
ATOM   1843  CG  LEU A 292     -13.977 -24.197  17.647  1.00 27.09           C  
ANISOU 1843  CG  LEU A 292     3771   3183   3341   -222     90   -179       C  
ATOM   1844  CD1 LEU A 292     -13.783 -24.359  16.059  1.00 27.42           C  
ANISOU 1844  CD1 LEU A 292     3792   3175   3451   -156     95   -116       C  
ATOM   1845  CD2 LEU A 292     -13.519 -25.475  18.433  1.00 23.93           C  
ANISOU 1845  CD2 LEU A 292     3355   2858   2881   -273     57   -123       C  
ATOM   1846  N   SER A 293     -12.551 -20.289  20.178  1.00 31.53           N  
ANISOU 1846  N   SER A 293     4408   3672   3900   -397     52   -406       N  
ATOM   1847  CA  SER A 293     -11.582 -19.466  20.909  1.00 35.28           C  
ANISOU 1847  CA  SER A 293     4899   4139   4368   -470     19   -437       C  
ATOM   1848  C   SER A 293     -11.948 -19.192  22.369  1.00 35.63           C  
ANISOU 1848  C   SER A 293     4960   4251   4327   -545     33   -550       C  
ATOM   1849  O   SER A 293     -11.159 -18.576  23.071  1.00 36.72           O  
ANISOU 1849  O   SER A 293     5113   4395   4445   -616      4   -582       O  
ATOM   1850  CB  SER A 293     -11.398 -18.113  20.211  1.00 38.04           C  
ANISOU 1850  CB  SER A 293     5258   4372   4824   -441     10   -465       C  
ATOM   1851  OG  SER A 293     -10.970 -18.343  18.876  1.00 41.64           O  
ANISOU 1851  OG  SER A 293     5698   4785   5340   -392     -4   -356       O  
ATOM   1852  N   LEU A 294     -13.103 -19.622  22.843  1.00 34.60           N  
ANISOU 1852  N   LEU A 294     4826   4181   4141   -538     78   -615       N  
ATOM   1853  CA  LEU A 294     -13.507 -19.381  24.209  1.00 34.58           C  
ANISOU 1853  CA  LEU A 294     4834   4262   4044   -619    102   -733       C  
ATOM   1854  C   LEU A 294     -12.606 -20.127  25.195  1.00 35.78           C  
ANISOU 1854  C   LEU A 294     4993   4523   4079   -729     54   -667       C  
ATOM   1855  O   LEU A 294     -11.926 -21.085  24.830  1.00 35.16           O  
ANISOU 1855  O   LEU A 294     4903   4459   3996   -728      9   -530       O  
ATOM   1856  CB  LEU A 294     -14.952 -19.848  24.388  1.00 34.73           C  
ANISOU 1856  CB  LEU A 294     4837   4335   4025   -589    164   -800       C  
ATOM   1857  CG  LEU A 294     -16.058 -19.009  23.770  1.00 36.06           C  
ANISOU 1857  CG  LEU A 294     4990   4411   4299   -498    214   -902       C  
ATOM   1858  CD1 LEU A 294     -17.404 -19.709  23.893  1.00 35.04           C  
ANISOU 1858  CD1 LEU A 294     4837   4349   4127   -470    270   -943       C  
ATOM   1859  CD2 LEU A 294     -16.058 -17.628  24.468  1.00 37.16           C  
ANISOU 1859  CD2 LEU A 294     5135   4512   4472   -532    230  -1062       C  
ATOM   1860  N   PRO A 295     -12.662 -19.761  26.476  1.00 37.58           N  
ANISOU 1860  N   PRO A 295     5234   4835   4208   -829     63   -767       N  
ATOM   1861  CA  PRO A 295     -11.862 -20.475  27.486  1.00 35.69           C  
ANISOU 1861  CA  PRO A 295     5003   4711   3848   -949      8   -696       C  
ATOM   1862  C   PRO A 295     -12.299 -21.931  27.648  1.00 32.92           C  
ANISOU 1862  C   PRO A 295     4637   4450   3420   -966     -3   -596       C  
ATOM   1863  O   PRO A 295     -13.428 -22.304  27.341  1.00 32.28           O  
ANISOU 1863  O   PRO A 295     4544   4379   3343   -911     50   -626       O  
ATOM   1864  CB  PRO A 295     -12.126 -19.686  28.772  1.00 37.05           C  
ANISOU 1864  CB  PRO A 295     5192   4964   3922  -1052     37   -853       C  
ATOM   1865  CG  PRO A 295     -12.679 -18.363  28.329  1.00 40.46           C  
ANISOU 1865  CG  PRO A 295     5624   5285   4466   -977     92  -1001       C  
ATOM   1866  CD  PRO A 295     -13.396 -18.616  27.050  1.00 39.09           C  
ANISOU 1866  CD  PRO A 295     5431   5018   4404   -842    120   -954       C  
ATOM   1867  N   ASP A 296     -11.387 -22.750  28.186  1.00 33.24           N  
ANISOU 1867  N   ASP A 296     4675   4556   3397  -1050    -80   -476       N  
ATOM   1868  CA  ASP A 296     -11.627 -24.194  28.235  1.00 37.73           C  
ANISOU 1868  CA  ASP A 296     5224   5186   3924  -1064   -112   -354       C  
ATOM   1869  C   ASP A 296     -12.924 -24.501  28.947  1.00 37.61           C  
ANISOU 1869  C   ASP A 296     5212   5278   3798  -1110    -56   -430       C  
ATOM   1870  O   ASP A 296     -13.609 -25.466  28.603  1.00 40.06           O  
ANISOU 1870  O   ASP A 296     5506   5603   4110  -1072    -47   -369       O  
ATOM   1871  CB  ASP A 296     -10.478 -24.941  28.937  1.00 43.78           C  
ANISOU 1871  CB  ASP A 296     5984   6012   4636  -1168   -216   -221       C  
ATOM   1872  CG  ASP A 296      -9.117 -24.650  28.333  1.00 47.99           C  
ANISOU 1872  CG  ASP A 296     6504   6453   5276  -1135   -273   -150       C  
ATOM   1873  OD1 ASP A 296      -9.047 -24.376  27.125  1.00 51.12           O  
ANISOU 1873  OD1 ASP A 296     6888   6740   5794  -1019   -243   -149       O  
ATOM   1874  OD2 ASP A 296      -8.108 -24.691  29.064  1.00 49.43           O  
ANISOU 1874  OD2 ASP A 296     6686   6679   5417  -1232   -349    -93       O  
ATOM   1875  N   ASN A 297     -13.282 -23.711  29.949  1.00 37.53           N  
ANISOU 1875  N   ASN A 297     5220   5350   3690  -1196    -14   -568       N  
ATOM   1876  CA  ASN A 297     -14.472 -24.079  30.701  1.00 42.19           C  
ANISOU 1876  CA  ASN A 297     5804   6066   4159  -1258     41   -639       C  
ATOM   1877  C   ASN A 297     -15.765 -23.474  30.124  1.00 43.71           C  
ANISOU 1877  C   ASN A 297     5983   6208   4419  -1152    145   -783       C  
ATOM   1878  O   ASN A 297     -16.820 -23.577  30.758  1.00 44.94           O  
ANISOU 1878  O   ASN A 297     6126   6468   4482  -1199    208   -877       O  
ATOM   1879  CB  ASN A 297     -14.294 -23.734  32.188  1.00 42.02           C  
ANISOU 1879  CB  ASN A 297     5800   6195   3971  -1427     36   -716       C  
ATOM   1880  CG  ASN A 297     -14.238 -22.252  32.437  1.00 44.17           C  
ANISOU 1880  CG  ASN A 297     6085   6433   4265  -1428     90   -902       C  
ATOM   1881  OD1 ASN A 297     -14.168 -21.461  31.501  1.00 44.60           O  
ANISOU 1881  OD1 ASN A 297     6138   6340   4470  -1305    113   -950       O  
ATOM   1882  ND2 ASN A 297     -14.242 -21.861  33.720  1.00 45.96           N  
ANISOU 1882  ND2 ASN A 297     6323   6799   4341  -1575    104  -1007       N  
ATOM   1883  N   GLU A 298     -15.715 -22.887  28.924  1.00 42.25           N  
ANISOU 1883  N   GLU A 298     5794   5869   4392  -1014    161   -794       N  
ATOM   1884  CA  GLU A 298     -16.910 -22.430  28.217  1.00 42.05           C  
ANISOU 1884  CA  GLU A 298     5748   5777   4453   -903    240   -897       C  
ATOM   1885  C   GLU A 298     -16.981 -22.912  26.764  1.00 39.29           C  
ANISOU 1885  C   GLU A 298     5387   5311   4232   -772    224   -785       C  
ATOM   1886  O   GLU A 298     -18.032 -22.778  26.123  1.00 41.46           O  
ANISOU 1886  O   GLU A 298     5643   5540   4571   -683    278   -839       O  
ATOM   1887  CB  GLU A 298     -16.971 -20.902  28.225  1.00 46.53           C  
ANISOU 1887  CB  GLU A 298     6318   6265   5098   -873    280  -1061       C  
ATOM   1888  CG  GLU A 298     -16.941 -20.283  29.620  1.00 55.55           C  
ANISOU 1888  CG  GLU A 298     7468   7518   6122  -1000    306  -1206       C  
ATOM   1889  CD  GLU A 298     -16.569 -18.794  29.592  1.00 63.25           C  
ANISOU 1889  CD  GLU A 298     8450   8389   7193   -977    316  -1340       C  
ATOM   1890  OE1 GLU A 298     -16.885 -18.125  28.574  1.00 65.58           O  
ANISOU 1890  OE1 GLU A 298     8733   8535   7649   -854    330  -1368       O  
ATOM   1891  OE2 GLU A 298     -15.946 -18.295  30.572  1.00 66.90           O  
ANISOU 1891  OE2 GLU A 298     8930   8915   7574  -1087    302  -1411       O  
ATOM   1892  N   ARG A 299     -15.908 -23.403  26.222  1.00 33.20           N  
ANISOU 1892  N   ARG A 299     4622   4490   3501   -758    155   -644       N  
ATOM   1893  CA  ARG A 299     -15.868 -23.743  24.818  1.00 30.16           C  
ANISOU 1893  CA  ARG A 299     4224   4000   3233   -642    145   -556       C  
ATOM   1894  C   ARG A 299     -16.677 -25.013  24.557  1.00 28.77           C  
ANISOU 1894  C   ARG A 299     4030   3870   3032   -616    154   -488       C  
ATOM   1895  O   ARG A 299     -16.491 -26.004  25.256  1.00 28.23           O  
ANISOU 1895  O   ARG A 299     3958   3890   2877   -695    116   -413       O  
ATOM   1896  CB  ARG A 299     -14.401 -23.946  24.436  1.00 28.20           C  
ANISOU 1896  CB  ARG A 299     3980   3707   3028   -650     72   -437       C  
ATOM   1897  CG  ARG A 299     -14.149 -24.268  22.966  1.00 27.89           C  
ANISOU 1897  CG  ARG A 299     3924   3571   3103   -544     62   -350       C  
ATOM   1898  CD  ARG A 299     -12.600 -24.453  22.742  1.00 30.94           C  
ANISOU 1898  CD  ARG A 299     4302   3929   3525   -567     -7   -247       C  
ATOM   1899  NE  ARG A 299     -12.090 -25.524  23.606  1.00 35.96           N  
ANISOU 1899  NE  ARG A 299     4927   4648   4089   -650    -65   -164       N  
ATOM   1900  CZ  ARG A 299     -11.194 -25.357  24.576  1.00 38.04           C  
ANISOU 1900  CZ  ARG A 299     5199   4958   4297   -748   -117   -147       C  
ATOM   1901  NH1 ARG A 299     -10.670 -24.165  24.791  1.00 39.39           N  
ANISOU 1901  NH1 ARG A 299     5390   5101   4477   -774   -114   -213       N  
ATOM   1902  NH2 ARG A 299     -10.827 -26.379  25.327  1.00 39.29           N  
ANISOU 1902  NH2 ARG A 299     5344   5189   4396   -825   -180    -58       N  
ATOM   1903  N   PRO A 300     -17.599 -25.015  23.605  1.00 28.54           N  
ANISOU 1903  N   PRO A 300     3986   3783   3076   -516    197   -509       N  
ATOM   1904  CA  PRO A 300     -18.263 -26.278  23.213  1.00 27.81           C  
ANISOU 1904  CA  PRO A 300     3874   3720   2972   -488    197   -432       C  
ATOM   1905  C   PRO A 300     -17.311 -27.256  22.528  1.00 29.44           C  
ANISOU 1905  C   PRO A 300     4073   3889   3225   -466    133   -287       C  
ATOM   1906  O   PRO A 300     -16.280 -26.870  21.945  1.00 28.97           O  
ANISOU 1906  O   PRO A 300     4016   3760   3232   -439    102   -249       O  
ATOM   1907  CB  PRO A 300     -19.337 -25.826  22.214  1.00 27.61           C  
ANISOU 1907  CB  PRO A 300     3835   3623   3033   -379    253   -493       C  
ATOM   1908  CG  PRO A 300     -19.445 -24.278  22.417  1.00 28.13           C  
ANISOU 1908  CG  PRO A 300     3908   3639   3140   -369    287   -626       C  
ATOM   1909  CD  PRO A 300     -18.123 -23.833  22.893  1.00 26.25           C  
ANISOU 1909  CD  PRO A 300     3694   3396   2885   -432    241   -605       C  
ATOM   1910  N   SER A 301     -17.701 -28.555  22.559  1.00 27.02           N  
ANISOU 1910  N   SER A 301     3749   3627   2890   -477    113   -210       N  
ATOM   1911  CA  SER A 301     -16.974 -29.566  21.791  1.00 24.84           C  
ANISOU 1911  CA  SER A 301     3453   3304   2681   -441     59    -91       C  
ATOM   1912  C   SER A 301     -17.686 -30.036  20.546  1.00 26.72           C  
ANISOU 1912  C   SER A 301     3673   3487   2992   -340     88    -78       C  
ATOM   1913  O   SER A 301     -17.053 -30.733  19.758  1.00 28.88           O  
ANISOU 1913  O   SER A 301     3925   3713   3334   -300     53     -3       O  
ATOM   1914  CB  SER A 301     -16.679 -30.856  22.590  1.00 25.52           C  
ANISOU 1914  CB  SER A 301     3526   3456   2715   -523    -10     11       C  
ATOM   1915  OG  SER A 301     -15.853 -30.661  23.710  1.00 30.12           O  
ANISOU 1915  OG  SER A 301     4120   4094   3229   -628    -59     32       O  
ATOM   1916  N   VAL A 302     -18.981 -29.770  20.366  1.00 25.22           N  
ANISOU 1916  N   VAL A 302     3484   3307   2791   -303    148   -150       N  
ATOM   1917  CA  VAL A 302     -19.683 -30.210  19.157  1.00 23.28           C  
ANISOU 1917  CA  VAL A 302     3221   3013   2611   -213    170   -135       C  
ATOM   1918  C   VAL A 302     -20.447 -29.040  18.564  1.00 25.10           C  
ANISOU 1918  C   VAL A 302     3458   3196   2882   -148    226   -226       C  
ATOM   1919  O   VAL A 302     -21.057 -28.246  19.296  1.00 24.66           O  
ANISOU 1919  O   VAL A 302     3409   3170   2791   -173    263   -318       O  
ATOM   1920  CB  VAL A 302     -20.642 -31.401  19.414  1.00 24.03           C  
ANISOU 1920  CB  VAL A 302     3300   3164   2667   -230    171   -104       C  
ATOM   1921  CG1 VAL A 302     -21.693 -31.050  20.426  1.00 24.01           C  
ANISOU 1921  CG1 VAL A 302     3302   3244   2578   -283    216   -184       C  
ATOM   1922  CG2 VAL A 302     -21.312 -31.918  18.082  1.00 24.72           C  
ANISOU 1922  CG2 VAL A 302     3368   3198   2824   -138    189    -87       C  
ATOM   1923  N   TYR A 303     -20.369 -28.913  17.234  1.00 24.69           N  
ANISOU 1923  N   TYR A 303     3399   3071   2910    -70    228   -200       N  
ATOM   1924  CA  TYR A 303     -20.916 -27.782  16.504  1.00 26.30           C  
ANISOU 1924  CA  TYR A 303     3608   3213   3173    -10    260   -258       C  
ATOM   1925  C   TYR A 303     -21.656 -28.318  15.289  1.00 27.70           C  
ANISOU 1925  C   TYR A 303     3767   3363   3393     59    270   -226       C  
ATOM   1926  O   TYR A 303     -21.339 -29.402  14.790  1.00 24.24           O  
ANISOU 1926  O   TYR A 303     3318   2937   2957     66    250   -158       O  
ATOM   1927  CB  TYR A 303     -19.794 -26.851  16.011  1.00 24.84           C  
ANISOU 1927  CB  TYR A 303     3436   2963   3038     -4    237   -243       C  
ATOM   1928  CG  TYR A 303     -18.904 -26.296  17.116  1.00 26.26           C  
ANISOU 1928  CG  TYR A 303     3633   3163   3181    -75    219   -269       C  
ATOM   1929  CD1 TYR A 303     -17.849 -27.035  17.644  1.00 27.18           C  
ANISOU 1929  CD1 TYR A 303     3748   3320   3259   -131    179   -205       C  
ATOM   1930  CD2 TYR A 303     -19.170 -25.070  17.677  1.00 27.03           C  
ANISOU 1930  CD2 TYR A 303     3744   3239   3288    -88    239   -361       C  
ATOM   1931  CE1 TYR A 303     -17.043 -26.504  18.686  1.00 26.60           C  
ANISOU 1931  CE1 TYR A 303     3692   3271   3146   -205    157   -226       C  
ATOM   1932  CE2 TYR A 303     -18.374 -24.543  18.738  1.00 26.23           C  
ANISOU 1932  CE2 TYR A 303     3659   3162   3144   -161    223   -396       C  
ATOM   1933  CZ  TYR A 303     -17.322 -25.256  19.199  1.00 26.25           C  
ANISOU 1933  CZ  TYR A 303     3665   3211   3099   -220    181   -323       C  
ATOM   1934  OH  TYR A 303     -16.555 -24.766  20.232  1.00 27.72           O  
ANISOU 1934  OH  TYR A 303     3867   3426   3239   -299    160   -351       O  
ATOM   1935  N   ALA A 304     -22.610 -27.528  14.777  1.00 27.74           N  
ANISOU 1935  N   ALA A 304     3768   3329   3445    110    297   -277       N  
ATOM   1936  CA  ALA A 304     -23.267 -27.859  13.521  1.00 28.86           C  
ANISOU 1936  CA  ALA A 304     3896   3442   3630    171    300   -243       C  
ATOM   1937  C   ALA A 304     -23.340 -26.621  12.633  1.00 30.48           C  
ANISOU 1937  C   ALA A 304     4105   3568   3910    213    293   -253       C  
ATOM   1938  O   ALA A 304     -23.644 -25.531  13.115  1.00 29.56           O  
ANISOU 1938  O   ALA A 304     3989   3415   3826    215    301   -321       O  
ATOM   1939  CB  ALA A 304     -24.671 -28.408  13.766  1.00 28.45           C  
ANISOU 1939  CB  ALA A 304     3822   3430   3558    187    329   -279       C  
ATOM   1940  N   PHE A 305     -23.055 -26.803  11.343  1.00 29.88           N  
ANISOU 1940  N   PHE A 305     4027   3465   3861    240    275   -186       N  
ATOM   1941  CA  PHE A 305     -23.302 -25.801  10.303  1.00 28.81           C  
ANISOU 1941  CA  PHE A 305     3892   3262   3791    273    258   -170       C  
ATOM   1942  C   PHE A 305     -24.328 -26.394   9.339  1.00 24.81           C  
ANISOU 1942  C   PHE A 305     3367   2765   3293    314    261   -144       C  
ATOM   1943  O   PHE A 305     -24.278 -27.589   9.039  1.00 24.60           O  
ANISOU 1943  O   PHE A 305     3334   2790   3225    311    269   -113       O  
ATOM   1944  CB  PHE A 305     -22.005 -25.404   9.537  1.00 26.27           C  
ANISOU 1944  CB  PHE A 305     3584   2916   3480    250    230   -107       C  
ATOM   1945  CG  PHE A 305     -22.257 -24.527   8.283  1.00 27.92           C  
ANISOU 1945  CG  PHE A 305     3793   3069   3746    269    202    -62       C  
ATOM   1946  CD1 PHE A 305     -22.455 -25.097   7.043  1.00 29.82           C  
ANISOU 1946  CD1 PHE A 305     4024   3335   3971    279    197     -4       C  
ATOM   1947  CD2 PHE A 305     -22.283 -23.141   8.370  1.00 27.56           C  
ANISOU 1947  CD2 PHE A 305     3757   2945   3771    269    175    -76       C  
ATOM   1948  CE1 PHE A 305     -22.715 -24.266   5.879  1.00 28.15           C  
ANISOU 1948  CE1 PHE A 305     3813   3080   3802    281    162     52       C  
ATOM   1949  CE2 PHE A 305     -22.519 -22.361   7.261  1.00 28.45           C  
ANISOU 1949  CE2 PHE A 305     3868   3003   3941    277    136    -19       C  
ATOM   1950  CZ  PHE A 305     -22.724 -22.929   6.017  1.00 28.57           C  
ANISOU 1950  CZ  PHE A 305     3875   3053   3927    279    127     51       C  
ATOM   1951  N   TYR A 306     -25.260 -25.579   8.866  1.00 22.78           N  
ANISOU 1951  N   TYR A 306     3100   2457   3100    349    249   -157       N  
ATOM   1952  CA  TYR A 306     -26.251 -26.052   7.887  1.00 25.71           C  
ANISOU 1952  CA  TYR A 306     3452   2836   3481    383    244   -125       C  
ATOM   1953  C   TYR A 306     -26.258 -25.122   6.679  1.00 27.35           C  
ANISOU 1953  C   TYR A 306     3662   2984   3747    393    199    -66       C  
ATOM   1954  O   TYR A 306     -26.290 -23.902   6.855  1.00 25.75           O  
ANISOU 1954  O   TYR A 306     3459   2707   3616    399    174    -83       O  
ATOM   1955  CB  TYR A 306     -27.666 -26.109   8.519  1.00 28.63           C  
ANISOU 1955  CB  TYR A 306     3793   3210   3875    416    267   -194       C  
ATOM   1956  CG  TYR A 306     -28.795 -26.252   7.517  1.00 31.36           C  
ANISOU 1956  CG  TYR A 306     4114   3545   4256    455    250   -165       C  
ATOM   1957  CD1 TYR A 306     -29.059 -27.490   6.915  1.00 33.09           C  
ANISOU 1957  CD1 TYR A 306     4329   3823   4421    454    257   -125       C  
ATOM   1958  CD2 TYR A 306     -29.592 -25.154   7.166  1.00 33.68           C  
ANISOU 1958  CD2 TYR A 306     4385   3763   4647    491    221   -176       C  
ATOM   1959  CE1 TYR A 306     -30.100 -27.643   5.965  1.00 33.85           C  
ANISOU 1959  CE1 TYR A 306     4404   3915   4544    483    238    -96       C  
ATOM   1960  CE2 TYR A 306     -30.641 -25.285   6.234  1.00 36.03           C  
ANISOU 1960  CE2 TYR A 306     4657   4051   4981    522    195   -140       C  
ATOM   1961  CZ  TYR A 306     -30.874 -26.523   5.623  1.00 34.10           C  
ANISOU 1961  CZ  TYR A 306     4413   3876   4666    515    205    -99       C  
ATOM   1962  OH  TYR A 306     -31.894 -26.667   4.694  1.00 33.53           O  
ANISOU 1962  OH  TYR A 306     4317   3801   4623    539    176    -62       O  
ATOM   1963  N   SER A 307     -26.270 -25.686   5.456  1.00 24.64           N  
ANISOU 1963  N   SER A 307     3317   2671   3374    388    185      2       N  
ATOM   1964  CA  SER A 307     -26.505 -24.902   4.244  1.00 24.95           C  
ANISOU 1964  CA  SER A 307     3356   2670   3456    386    136     70       C  
ATOM   1965  C   SER A 307     -27.771 -25.383   3.548  1.00 25.39           C  
ANISOU 1965  C   SER A 307     3388   2741   3517    415    126     86       C  
ATOM   1966  O   SER A 307     -27.919 -26.592   3.273  1.00 24.97           O  
ANISOU 1966  O   SER A 307     3330   2759   3399    413    153     86       O  
ATOM   1967  CB  SER A 307     -25.348 -25.018   3.245  1.00 27.51           C  
ANISOU 1967  CB  SER A 307     3696   3031   3726    335    124    143       C  
ATOM   1968  OG  SER A 307     -25.717 -24.333   2.049  1.00 32.66           O  
ANISOU 1968  OG  SER A 307     4346   3658   4406    320     71    220       O  
ATOM   1969  N   GLU A 308     -28.648 -24.448   3.194  1.00 22.13           N  
ANISOU 1969  N   GLU A 308     2958   2260   3191    439     80    104       N  
ATOM   1970  CA  GLU A 308     -29.785 -24.839   2.348  1.00 26.21           C  
ANISOU 1970  CA  GLU A 308     3451   2793   3715    458     56    138       C  
ATOM   1971  C   GLU A 308     -29.381 -25.163   0.910  1.00 27.63           C  
ANISOU 1971  C   GLU A 308     3645   3025   3828    410     27    232       C  
ATOM   1972  O   GLU A 308     -30.172 -25.785   0.181  1.00 27.35           O  
ANISOU 1972  O   GLU A 308     3595   3029   3766    414     17    256       O  
ATOM   1973  CB  GLU A 308     -30.844 -23.731   2.353  1.00 31.93           C  
ANISOU 1973  CB  GLU A 308     4142   3422   4566    499      5    135       C  
ATOM   1974  CG  GLU A 308     -30.352 -22.484   1.720  1.00 40.81           C  
ANISOU 1974  CG  GLU A 308     5279   4470   5758    472    -66    211       C  
ATOM   1975  CD  GLU A 308     -29.375 -21.592   2.565  1.00 47.95           C  
ANISOU 1975  CD  GLU A 308     6202   5314   6702    461    -60    173       C  
ATOM   1976  OE1 GLU A 308     -29.040 -21.845   3.777  1.00 43.05           O  
ANISOU 1976  OE1 GLU A 308     5587   4710   6059    473      0     78       O  
ATOM   1977  OE2 GLU A 308     -28.964 -20.576   1.940  1.00 53.71           O  
ANISOU 1977  OE2 GLU A 308     6941   5977   7489    431   -128    250       O  
ATOM   1978  N  AGLN A 309     -28.183 -24.785   0.467  0.59 26.60           N  
ANISOU 1978  N  AGLN A 309     3539   2904   3663    358     16    281       N  
ATOM   1979  N  BGLN A 309     -28.162 -24.793   0.504  0.41 26.62           N  
ANISOU 1979  N  BGLN A 309     3543   2907   3665    359     18    278       N  
ATOM   1980  CA AGLN A 309     -27.807 -25.126  -0.923  0.59 25.94           C  
ANISOU 1980  CA AGLN A 309     3463   2891   3500    300     -3    359       C  
ATOM   1981  CA BGLN A 309     -27.642 -25.143  -0.827  0.41 26.12           C  
ANISOU 1981  CA BGLN A 309     3489   2916   3519    298      4    354       C  
ATOM   1982  C  AGLN A 309     -27.122 -26.482  -0.868  0.59 25.81           C  
ANISOU 1982  C  AGLN A 309     3450   2968   3389    287     65    312       C  
ATOM   1983  C  BGLN A 309     -27.177 -26.586  -0.792  0.41 25.94           C  
ANISOU 1983  C  BGLN A 309     3465   2987   3405    292     69    304       C  
ATOM   1984  O  AGLN A 309     -26.509 -26.816   0.137  0.59 25.86           O  
ANISOU 1984  O  AGLN A 309     3461   2972   3393    303    107    252       O  
ATOM   1985  O  BGLN A 309     -26.775 -27.076   0.268  0.41 25.86           O  
ANISOU 1985  O  BGLN A 309     3456   2976   3393    316    114    237       O  
ATOM   1986  CB AGLN A 309     -26.920 -24.029  -1.547  0.59 25.74           C  
ANISOU 1986  CB AGLN A 309     3455   2841   3484    240    -51    442       C  
ATOM   1987  CB BGLN A 309     -26.474 -24.228  -1.233  0.41 25.10           C  
ANISOU 1987  CB BGLN A 309     3379   2772   3384    238    -25    417       C  
ATOM   1988  CG AGLN A 309     -27.736 -22.831  -2.075  0.59 27.83           C  
ANISOU 1988  CG AGLN A 309     3711   3020   3843    238   -142    522       C  
ATOM   1989  CG BGLN A 309     -26.762 -22.738  -1.341  0.41 25.56           C  
ANISOU 1989  CG BGLN A 309     3439   2726   3548    234   -103    478       C  
ATOM   1990  CD AGLN A 309     -28.170 -22.890  -3.600  0.59 32.49           C  
ANISOU 1990  CD AGLN A 309     4297   3666   4381    179   -199    629       C  
ATOM   1991  CD BGLN A 309     -25.530 -21.990  -1.846  0.41 27.56           C  
ANISOU 1991  CD BGLN A 309     3712   2982   3777    159   -131    552       C  
ATOM   1992  OE1AGLN A 309     -28.916 -23.716  -4.047  0.59 22.72           O  
ANISOU 1992  OE1AGLN A 309     3047   2486   3099    188   -189    620       O  
ATOM   1993  OE1BGLN A 309     -24.570 -21.746  -1.096  0.41 27.67           O  
ANISOU 1993  OE1BGLN A 309     3738   2978   3797    154   -103    514       O  
ATOM   1994  NE2AGLN A 309     -27.678 -21.925  -4.350  0.59 38.21           N  
ANISOU 1994  NE2AGLN A 309     5033   4371   5115    110   -267    734       N  
ATOM   1995  NE2BGLN A 309     -25.518 -21.701  -3.136  0.41 29.92           N  
ANISOU 1995  NE2BGLN A 309     4012   3318   4036     90   -184    658       N  
ATOM   1996  N   PRO A 310     -27.221 -27.280  -1.939  1.00 25.44           N  
ANISOU 1996  N   PRO A 310     3396   3002   3267    255     70    335       N  
ATOM   1997  CA  PRO A 310     -27.672 -26.845  -3.265  1.00 24.76           C  
ANISOU 1997  CA  PRO A 310     3309   2940   3159    209     15    421       C  
ATOM   1998  C   PRO A 310     -29.119 -27.255  -3.618  1.00 27.48           C  
ANISOU 1998  C   PRO A 310     3635   3287   3519    239    -10    425       C  
ATOM   1999  O   PRO A 310     -29.450 -27.421  -4.797  1.00 26.99           O  
ANISOU 1999  O   PRO A 310     3570   3284   3403    192    -41    481       O  
ATOM   2000  CB  PRO A 310     -26.649 -27.549  -4.182  1.00 24.91           C  
ANISOU 2000  CB  PRO A 310     3329   3069   3068    141     52    424       C  
ATOM   2001  CG  PRO A 310     -26.484 -28.816  -3.544  1.00 24.35           C  
ANISOU 2001  CG  PRO A 310     3246   3027   2978    180    116    331       C  
ATOM   2002  CD  PRO A 310     -26.512 -28.569  -2.027  1.00 22.74           C  
ANISOU 2002  CD  PRO A 310     3047   2740   2851    241    129    284       C  
ATOM   2003  N   ASP A 311     -29.971 -27.403  -2.594  1.00 26.34           N  
ANISOU 2003  N   ASP A 311     3476   3088   3444    310      3    367       N  
ATOM   2004  CA  ASP A 311     -31.335 -27.878  -2.805  1.00 25.41           C  
ANISOU 2004  CA  ASP A 311     3334   2976   3345    342    -13    361       C  
ATOM   2005  C   ASP A 311     -32.123 -26.905  -3.669  1.00 24.98           C  
ANISOU 2005  C   ASP A 311     3267   2880   3344    327   -100    452       C  
ATOM   2006  O   ASP A 311     -32.875 -27.321  -4.579  1.00 24.98           O  
ANISOU 2006  O   ASP A 311     3255   2926   3310    306   -131    492       O  
ATOM   2007  CB  ASP A 311     -32.034 -28.058  -1.444  1.00 25.50           C  
ANISOU 2007  CB  ASP A 311     3326   2938   3424    413     20    279       C  
ATOM   2008  CG  ASP A 311     -33.353 -28.791  -1.559  1.00 26.48           C  
ANISOU 2008  CG  ASP A 311     3420   3085   3556    442     18    260       C  
ATOM   2009  OD1 ASP A 311     -33.316 -29.979  -1.958  1.00 25.12           O  
ANISOU 2009  OD1 ASP A 311     3250   2985   3307    423     47    245       O  
ATOM   2010  OD2 ASP A 311     -34.398 -28.216  -1.220  1.00 26.37           O  
ANISOU 2010  OD2 ASP A 311     3375   3013   3630    485     -9    253       O  
ATOM   2011  N   PHE A 312     -32.006 -25.603  -3.393  1.00 25.23           N  
ANISOU 2011  N   PHE A 312     3299   2820   3468    335   -148    488       N  
ATOM   2012  CA  PHE A 312     -32.877 -24.695  -4.157  1.00 26.01           C  
ANISOU 2012  CA  PHE A 312     3377   2862   3644    327   -246    581       C  
ATOM   2013  C   PHE A 312     -32.511 -24.711  -5.634  1.00 25.99           C  
ANISOU 2013  C   PHE A 312     3392   2938   3544    232   -294    690       C  
ATOM   2014  O   PHE A 312     -33.394 -24.791  -6.505  1.00 28.43           O  
ANISOU 2014  O   PHE A 312     3684   3270   3848    210   -353    755       O  
ATOM   2015  CB  PHE A 312     -32.859 -23.253  -3.652  1.00 34.43           C  
ANISOU 2015  CB  PHE A 312     4433   3798   4850    352   -302    602       C  
ATOM   2016  CG  PHE A 312     -33.693 -22.326  -4.555  1.00 41.40           C  
ANISOU 2016  CG  PHE A 312     5289   4614   5826    336   -421    717       C  
ATOM   2017  CD1 PHE A 312     -35.095 -22.327  -4.478  1.00 43.40           C  
ANISOU 2017  CD1 PHE A 312     5493   4821   6176    395   -457    703       C  
ATOM   2018  CD2 PHE A 312     -33.085 -21.557  -5.566  1.00 43.33           C  
ANISOU 2018  CD2 PHE A 312     5556   4857   6051    250   -501    848       C  
ATOM   2019  CE1 PHE A 312     -35.877 -21.514  -5.345  1.00 46.27           C  
ANISOU 2019  CE1 PHE A 312     5826   5120   6636    377   -579    818       C  
ATOM   2020  CE2 PHE A 312     -33.865 -20.729  -6.436  1.00 45.06           C  
ANISOU 2020  CE2 PHE A 312     5750   5014   6358    224   -628    973       C  
ATOM   2021  CZ  PHE A 312     -35.255 -20.723  -6.321  1.00 46.48           C  
ANISOU 2021  CZ  PHE A 312     5878   5136   6648    291   -669    958       C  
ATOM   2022  N   SER A 313     -31.223 -24.591  -5.963  1.00 24.58           N  
ANISOU 2022  N   SER A 313     3245   2809   3287    166   -274    716       N  
ATOM   2023  CA  SER A 313     -30.855 -24.633  -7.389  1.00 25.14           C  
ANISOU 2023  CA  SER A 313     3329   2977   3246     61   -312    813       C  
ATOM   2024  C   SER A 313     -31.211 -25.987  -8.036  1.00 23.68           C  
ANISOU 2024  C   SER A 313     3137   2913   2945     40   -266    772       C  
ATOM   2025  O   SER A 313     -31.569 -26.043  -9.220  1.00 26.12           O  
ANISOU 2025  O   SER A 313     3445   3294   3185    -33   -317    849       O  
ATOM   2026  CB  SER A 313     -29.357 -24.356  -7.545  1.00 28.76           C  
ANISOU 2026  CB  SER A 313     3812   3479   3635     -7   -281    829       C  
ATOM   2027  OG  SER A 313     -29.021 -23.145  -6.922  1.00 33.60           O  
ANISOU 2027  OG  SER A 313     4433   3978   4358     10   -323    862       O  
ATOM   2028  N   GLY A 314     -31.121 -27.078  -7.285  1.00 22.73           N  
ANISOU 2028  N   GLY A 314     3013   2817   2805     96   -179    654       N  
ATOM   2029  CA  GLY A 314     -31.561 -28.370  -7.821  1.00 22.47           C  
ANISOU 2029  CA  GLY A 314     2971   2879   2688     85   -142    607       C  
ATOM   2030  C   GLY A 314     -33.041 -28.364  -8.213  1.00 25.16           C  
ANISOU 2030  C   GLY A 314     3289   3200   3069    103   -207    649       C  
ATOM   2031  O   GLY A 314     -33.424 -28.856  -9.293  1.00 23.96           O  
ANISOU 2031  O   GLY A 314     3134   3136   2834     44   -229    682       O  
ATOM   2032  N   HIS A 315     -33.891 -27.765  -7.364  1.00 22.85           N  
ANISOU 2032  N   HIS A 315     2976   2797   2908    181   -238    647       N  
ATOM   2033  CA  HIS A 315     -35.305 -27.611  -7.699  1.00 24.89           C  
ANISOU 2033  CA  HIS A 315     3203   3025   3229    203   -307    692       C  
ATOM   2034  C   HIS A 315     -35.495 -26.801  -8.985  1.00 27.41           C  
ANISOU 2034  C   HIS A 315     3524   3360   3532    120   -414    832       C  
ATOM   2035  O   HIS A 315     -36.314 -27.160  -9.841  1.00 27.15           O  
ANISOU 2035  O   HIS A 315     3476   3380   3460     85   -461    879       O  
ATOM   2036  CB  HIS A 315     -36.053 -26.948  -6.513  1.00 27.45           C  
ANISOU 2036  CB  HIS A 315     3495   3223   3713    300   -318    653       C  
ATOM   2037  CG  HIS A 315     -36.320 -27.902  -5.378  1.00 26.54           C  
ANISOU 2037  CG  HIS A 315     3367   3114   3603    368   -229    529       C  
ATOM   2038  ND1 HIS A 315     -37.143 -29.010  -5.522  1.00 24.22           N  
ANISOU 2038  ND1 HIS A 315     3055   2878   3271    379   -207    492       N  
ATOM   2039  CD2 HIS A 315     -35.870 -27.915  -4.088  1.00 21.83           C  
ANISOU 2039  CD2 HIS A 315     2774   2478   3041    418   -163    442       C  
ATOM   2040  CE1 HIS A 315     -37.171 -29.678  -4.384  1.00 27.46           C  
ANISOU 2040  CE1 HIS A 315     3458   3283   3691    430   -133    395       C  
ATOM   2041  NE2 HIS A 315     -36.385 -29.050  -3.505  1.00 33.06           N  
ANISOU 2041  NE2 HIS A 315     4182   3940   4438    450   -104    363       N  
ATOM   2042  N   LYS A 316     -34.743 -25.707  -9.137  1.00 26.31           N  
ANISOU 2042  N   LYS A 316     3401   3178   3418     80   -458    908       N  
ATOM   2043  CA  LYS A 316     -34.986 -24.801 -10.252  1.00 30.01           C  
ANISOU 2043  CA  LYS A 316     3868   3643   3891     -2   -578   1060       C  
ATOM   2044  C   LYS A 316     -34.418 -25.361 -11.556  1.00 30.98           C  
ANISOU 2044  C   LYS A 316     4015   3926   3828   -128   -572   1110       C  
ATOM   2045  O   LYS A 316     -35.082 -25.332 -12.595  1.00 31.93           O  
ANISOU 2045  O   LYS A 316     4127   4100   3904   -197   -651   1204       O  
ATOM   2046  CB  LYS A 316     -34.347 -23.434  -9.943  1.00 33.00           C  
ANISOU 2046  CB  LYS A 316     4255   3915   4368     -9   -632   1127       C  
ATOM   2047  CG  LYS A 316     -34.639 -22.408 -11.032  1.00 40.53           C  
ANISOU 2047  CG  LYS A 316     5203   4846   5350    -96   -775   1304       C  
ATOM   2048  CD  LYS A 316     -34.188 -20.976 -10.631  1.00 45.20           C  
ANISOU 2048  CD  LYS A 316     5795   5297   6081    -90   -846   1371       C  
ATOM   2049  CE  LYS A 316     -34.626 -19.971 -11.694  1.00 50.57           C  
ANISOU 2049  CE  LYS A 316     6462   5937   6813   -176  -1009   1562       C  
ATOM   2050  NZ  LYS A 316     -34.316 -18.569 -11.288  1.00 53.15           N  
ANISOU 2050  NZ  LYS A 316     6782   6105   7308   -163  -1093   1629       N  
ATOM   2051  N   TYR A 317     -33.189 -25.875 -11.530  1.00 26.13           N  
ANISOU 2051  N   TYR A 317     3429   3397   3104   -165   -480   1045       N  
ATOM   2052  CA  TYR A 317     -32.497 -26.254 -12.771  1.00 31.21           C  
ANISOU 2052  CA  TYR A 317     4089   4199   3572   -296   -469   1082       C  
ATOM   2053  C   TYR A 317     -32.434 -27.773 -12.980  1.00 30.80           C  
ANISOU 2053  C   TYR A 317     4033   4265   3405   -296   -370    956       C  
ATOM   2054  O   TYR A 317     -32.138 -28.225 -14.093  1.00 33.88           O  
ANISOU 2054  O   TYR A 317     4427   4797   3649   -403   -361    969       O  
ATOM   2055  CB  TYR A 317     -31.075 -25.669 -12.755  1.00 30.73           C  
ANISOU 2055  CB  TYR A 317     4049   4157   3469   -354   -441   1102       C  
ATOM   2056  CG  TYR A 317     -31.078 -24.163 -12.542  1.00 37.77           C  
ANISOU 2056  CG  TYR A 317     4945   4922   4483   -357   -542   1225       C  
ATOM   2057  CD1 TYR A 317     -30.491 -23.564 -11.408  1.00 40.95           C  
ANISOU 2057  CD1 TYR A 317     5354   5208   4997   -284   -516   1183       C  
ATOM   2058  CD2 TYR A 317     -31.685 -23.366 -13.457  1.00 41.30           C  
ANISOU 2058  CD2 TYR A 317     5388   5362   4942   -434   -670   1382       C  
ATOM   2059  CE1 TYR A 317     -30.528 -22.158 -11.258  1.00 43.87           C  
ANISOU 2059  CE1 TYR A 317     5724   5451   5493   -290   -618   1291       C  
ATOM   2060  CE2 TYR A 317     -31.729 -21.982 -13.317  1.00 45.97           C  
ANISOU 2060  CE2 TYR A 317     5978   5823   5665   -440   -778   1502       C  
ATOM   2061  CZ  TYR A 317     -31.158 -21.401 -12.236  1.00 46.26           C  
ANISOU 2061  CZ  TYR A 317     6019   5742   5816   -366   -750   1451       C  
ATOM   2062  OH  TYR A 317     -31.270 -20.045 -12.212  1.00 51.78           O  
ANISOU 2062  OH  TYR A 317     6713   6310   6652   -379   -867   1570       O  
ATOM   2063  N   GLY A 318     -32.732 -28.553 -11.964  1.00 25.02           N  
ANISOU 2063  N   GLY A 318     3290   3480   2738   -188   -303    838       N  
ATOM   2064  CA  GLY A 318     -32.585 -29.995 -12.013  1.00 24.43           C  
ANISOU 2064  CA  GLY A 318     3209   3492   2583   -179   -212    713       C  
ATOM   2065  C   GLY A 318     -31.165 -30.437 -11.709  1.00 27.07           C  
ANISOU 2065  C   GLY A 318     3550   3870   2867   -188   -117    624       C  
ATOM   2066  O   GLY A 318     -30.181 -29.677 -11.840  1.00 27.74           O  
ANISOU 2066  O   GLY A 318     3646   3964   2929   -238   -119    669       O  
ATOM   2067  N   PRO A 319     -31.014 -31.713 -11.374  1.00 25.75           N  
ANISOU 2067  N   PRO A 319     3370   3733   2682   -147    -38    498       N  
ATOM   2068  CA  PRO A 319     -29.683 -32.203 -10.922  1.00 25.09           C  
ANISOU 2068  CA  PRO A 319     3282   3670   2582   -139     49    405       C  
ATOM   2069  C   PRO A 319     -28.619 -32.205 -12.005  1.00 28.77           C  
ANISOU 2069  C   PRO A 319     3743   4266   2923   -249     80    401       C  
ATOM   2070  O   PRO A 319     -27.441 -32.084 -11.662  1.00 29.22           O  
ANISOU 2070  O   PRO A 319     3795   4325   2981   -253    129    366       O  
ATOM   2071  CB  PRO A 319     -29.964 -33.630 -10.418  1.00 27.40           C  
ANISOU 2071  CB  PRO A 319     3556   3957   2899    -74    107    282       C  
ATOM   2072  CG  PRO A 319     -31.273 -34.090 -11.137  1.00 22.52           C  
ANISOU 2072  CG  PRO A 319     2931   3377   2249    -92     64    299       C  
ATOM   2073  CD  PRO A 319     -32.053 -32.764 -11.481  1.00 24.26           C  
ANISOU 2073  CD  PRO A 319     3166   3562   2492   -117    -33    443       C  
ATOM   2074  N   PHE A 320     -28.977 -32.265 -13.301  1.00 28.57           N  
ANISOU 2074  N   PHE A 320     3715   4354   2786   -348     52    440       N  
ATOM   2075  CA  PHE A 320     -27.995 -32.290 -14.381  1.00 31.31           C  
ANISOU 2075  CA  PHE A 320     4052   4850   2996   -470     89    428       C  
ATOM   2076  C   PHE A 320     -27.844 -30.937 -15.098  1.00 32.20           C  
ANISOU 2076  C   PHE A 320     4185   4998   3052   -575     12    586       C  
ATOM   2077  O   PHE A 320     -27.175 -30.859 -16.134  1.00 32.37           O  
ANISOU 2077  O   PHE A 320     4198   5163   2938   -701     30    598       O  
ATOM   2078  CB  PHE A 320     -28.376 -33.365 -15.415  1.00 37.38           C  
ANISOU 2078  CB  PHE A 320     4800   5749   3653   -533    118    349       C  
ATOM   2079  CG  PHE A 320     -28.554 -34.731 -14.826  1.00 41.63           C  
ANISOU 2079  CG  PHE A 320     5315   6250   4251   -441    183    200       C  
ATOM   2080  CD1 PHE A 320     -27.482 -35.406 -14.330  1.00 44.41           C  
ANISOU 2080  CD1 PHE A 320     5640   6598   4635   -403    269     78       C  
ATOM   2081  CD2 PHE A 320     -29.775 -35.343 -14.830  1.00 45.29           C  
ANISOU 2081  CD2 PHE A 320     5780   6687   4742   -402    151    188       C  
ATOM   2082  CE1 PHE A 320     -27.625 -36.679 -13.795  1.00 45.99           C  
ANISOU 2082  CE1 PHE A 320     5815   6754   4904   -324    316    -50       C  
ATOM   2083  CE2 PHE A 320     -29.925 -36.654 -14.282  1.00 47.83           C  
ANISOU 2083  CE2 PHE A 320     6079   6970   5124   -325    205     54       C  
ATOM   2084  CZ  PHE A 320     -28.836 -37.294 -13.771  1.00 45.82           C  
ANISOU 2084  CZ  PHE A 320     5798   6701   4908   -287    283    -59       C  
ATOM   2085  N   GLY A 321     -28.480 -29.886 -14.613  1.00 31.75           N  
ANISOU 2085  N   GLY A 321     4149   4817   3095   -534    -79    706       N  
ATOM   2086  CA  GLY A 321     -28.357 -28.608 -15.298  1.00 32.29           C  
ANISOU 2086  CA  GLY A 321     4236   4906   3129   -637   -167    867       C  
ATOM   2087  C   GLY A 321     -26.944 -28.044 -15.140  1.00 32.78           C  
ANISOU 2087  C   GLY A 321     4299   4986   3169   -681   -127    872       C  
ATOM   2088  O   GLY A 321     -26.332 -28.166 -14.074  1.00 34.32           O  
ANISOU 2088  O   GLY A 321     4492   5099   3451   -590    -69    793       O  
ATOM   2089  N   PRO A 322     -26.391 -27.438 -16.186  1.00 34.00           N  
ANISOU 2089  N   PRO A 322     4457   5257   3205   -828   -157    967       N  
ATOM   2090  CA  PRO A 322     -25.081 -26.803 -16.028  1.00 36.21           C  
ANISOU 2090  CA  PRO A 322     4737   5551   3472   -875   -127    986       C  
ATOM   2091  C   PRO A 322     -25.097 -25.689 -14.979  1.00 34.79           C  
ANISOU 2091  C   PRO A 322     4578   5185   3456   -794   -191   1064       C  
ATOM   2092  O   PRO A 322     -24.030 -25.361 -14.440  1.00 33.50           O  
ANISOU 2092  O   PRO A 322     4413   4995   3319   -787   -149   1039       O  
ATOM   2093  CB  PRO A 322     -24.768 -26.273 -17.436  1.00 35.52           C  
ANISOU 2093  CB  PRO A 322     4650   5625   3222  -1064   -171   1103       C  
ATOM   2094  CG  PRO A 322     -26.053 -26.108 -18.067  1.00 35.04           C  
ANISOU 2094  CG  PRO A 322     4602   5563   3147  -1097   -274   1207       C  
ATOM   2095  CD  PRO A 322     -26.925 -27.246 -17.546  1.00 31.69           C  
ANISOU 2095  CD  PRO A 322     4169   5092   2782   -968   -227   1073       C  
ATOM   2096  N   GLU A 323     -26.282 -25.159 -14.636  1.00 31.79           N  
ANISOU 2096  N   GLU A 323     4213   4674   3194   -728   -287   1142       N  
ATOM   2097  CA  GLU A 323     -26.411 -24.158 -13.583  1.00 32.94           C  
ANISOU 2097  CA  GLU A 323     4371   4635   3510   -641   -344   1189       C  
ATOM   2098  C   GLU A 323     -26.067 -24.710 -12.195  1.00 33.58           C  
ANISOU 2098  C   GLU A 323     4447   4630   3681   -505   -253   1041       C  
ATOM   2099  O   GLU A 323     -25.900 -23.911 -11.267  1.00 31.74           O  
ANISOU 2099  O   GLU A 323     4224   4264   3571   -444   -279   1057       O  
ATOM   2100  CB  GLU A 323     -27.827 -23.565 -13.577  1.00 32.16           C  
ANISOU 2100  CB  GLU A 323     4273   4422   3524   -598   -461   1285       C  
ATOM   2101  CG  GLU A 323     -28.272 -22.903 -14.920  1.00 35.65           C  
ANISOU 2101  CG  GLU A 323     4719   4931   3896   -737   -581   1461       C  
ATOM   2102  CD  GLU A 323     -28.994 -23.865 -15.897  1.00 38.39           C  
ANISOU 2102  CD  GLU A 323     5056   5418   4113   -792   -575   1446       C  
ATOM   2103  OE1 GLU A 323     -28.997 -25.120 -15.685  1.00 34.56           O  
ANISOU 2103  OE1 GLU A 323     4560   4997   3572   -739   -467   1292       O  
ATOM   2104  OE2 GLU A 323     -29.553 -23.345 -16.888  1.00 42.34           O  
ANISOU 2104  OE2 GLU A 323     5558   5960   4570   -896   -686   1593       O  
ATOM   2105  N   MET A 324     -25.959 -26.047 -12.013  1.00 29.56           N  
ANISOU 2105  N   MET A 324     3921   4189   3119   -460   -153    901       N  
ATOM   2106  CA  MET A 324     -25.612 -26.564 -10.694  1.00 27.45           C  
ANISOU 2106  CA  MET A 324     3650   3843   2936   -345    -80    779       C  
ATOM   2107  C   MET A 324     -24.175 -26.233 -10.269  1.00 28.56           C  
ANISOU 2107  C   MET A 324     3791   3988   3075   -366    -32    756       C  
ATOM   2108  O   MET A 324     -23.876 -26.297  -9.072  1.00 30.07           O  
ANISOU 2108  O   MET A 324     3984   4089   3354   -279      0    690       O  
ATOM   2109  CB  MET A 324     -25.798 -28.089 -10.636  1.00 26.85           C  
ANISOU 2109  CB  MET A 324     3554   3832   2817   -301      3    646       C  
ATOM   2110  CG  MET A 324     -27.297 -28.497 -10.666  1.00 29.29           C  
ANISOU 2110  CG  MET A 324     3862   4107   3162   -248    -38    649       C  
ATOM   2111  SD  MET A 324     -28.335 -27.584  -9.450  1.00 31.34           S  
ANISOU 2111  SD  MET A 324     4131   4181   3596   -137   -107    692       S  
ATOM   2112  CE  MET A 324     -27.637 -28.185  -7.885  1.00 26.93           C  
ANISOU 2112  CE  MET A 324     3570   3560   3104    -38    -17    561       C  
ATOM   2113  N   THR A 325     -23.282 -25.928 -11.219  1.00 28.08           N  
ANISOU 2113  N   THR A 325     3724   4039   2908   -486    -26    806       N  
ATOM   2114  CA  THR A 325     -21.849 -25.764 -10.919  1.00 30.52           C  
ANISOU 2114  CA  THR A 325     4022   4374   3202   -515     30    772       C  
ATOM   2115  C   THR A 325     -21.614 -24.606  -9.949  1.00 32.27           C  
ANISOU 2115  C   THR A 325     4266   4450   3545   -473    -22    831       C  
ATOM   2116  O   THR A 325     -20.816 -24.723  -9.012  1.00 30.15           O  
ANISOU 2116  O   THR A 325     3992   4138   3326   -422     28    760       O  
ATOM   2117  CB  THR A 325     -21.086 -25.522 -12.232  1.00 35.30           C  
ANISOU 2117  CB  THR A 325     4612   5137   3662   -670     37    832       C  
ATOM   2118  OG1 THR A 325     -21.114 -26.711 -13.041  1.00 37.90           O  
ANISOU 2118  OG1 THR A 325     4912   5613   3876   -707    107    738       O  
ATOM   2119  CG2 THR A 325     -19.676 -25.114 -12.000  1.00 35.79           C  
ANISOU 2119  CG2 THR A 325     4660   5223   3715   -713     77    824       C  
ATOM   2120  N   ASN A 326     -22.312 -23.484 -10.163  1.00 33.83           N  
ANISOU 2120  N   ASN A 326     4487   4568   3799   -496   -128    959       N  
ATOM   2121  CA  ASN A 326     -22.135 -22.289  -9.337  1.00 35.38           C  
ANISOU 2121  CA  ASN A 326     4702   4619   4121   -464   -187   1013       C  
ATOM   2122  C   ASN A 326     -22.563 -22.469  -7.882  1.00 30.05           C  
ANISOU 2122  C   ASN A 326     4032   3814   3573   -324   -163    915       C  
ATOM   2123  O   ASN A 326     -21.766 -22.128  -7.001  1.00 28.80           O  
ANISOU 2123  O   ASN A 326     3878   3599   3467   -298   -139    877       O  
ATOM   2124  CB  ASN A 326     -22.874 -21.104  -9.967  1.00 44.91           C  
ANISOU 2124  CB  ASN A 326     5924   5762   5379   -519   -316   1171       C  
ATOM   2125  CG  ASN A 326     -22.149 -20.542 -11.151  1.00 55.68           C  
ANISOU 2125  CG  ASN A 326     7289   7232   6634   -676   -355   1294       C  
ATOM   2126  OD1 ASN A 326     -20.919 -20.699 -11.275  1.00 61.14           O  
ANISOU 2126  OD1 ASN A 326     7972   8015   7244   -737   -288   1264       O  
ATOM   2127  ND2 ASN A 326     -22.883 -19.850 -12.034  1.00 59.67           N  
ANISOU 2127  ND2 ASN A 326     7803   7730   7141   -750   -468   1440       N  
ATOM   2128  N   PRO A 327     -23.749 -22.984  -7.539  1.00 29.27           N  
ANISOU 2128  N   PRO A 327     3929   3671   3521   -240   -166    868       N  
ATOM   2129  CA  PRO A 327     -23.998 -23.232  -6.105  1.00 26.79           C  
ANISOU 2129  CA  PRO A 327     3615   3260   3304   -125   -128    765       C  
ATOM   2130  C   PRO A 327     -23.041 -24.228  -5.501  1.00 27.00           C  
ANISOU 2130  C   PRO A 327     3633   3345   3282   -102    -31    656       C  
ATOM   2131  O   PRO A 327     -22.763 -24.145  -4.292  1.00 27.72           O  
ANISOU 2131  O   PRO A 327     3728   3363   3440    -41     -7    594       O  
ATOM   2132  CB  PRO A 327     -25.440 -23.779  -6.066  1.00 26.37           C  
ANISOU 2132  CB  PRO A 327     3551   3185   3282    -59   -142    737       C  
ATOM   2133  CG  PRO A 327     -25.637 -24.338  -7.471  1.00 29.19           C  
ANISOU 2133  CG  PRO A 327     3901   3668   3521   -138   -149    786       C  
ATOM   2134  CD  PRO A 327     -24.977 -23.271  -8.317  1.00 32.71           C  
ANISOU 2134  CD  PRO A 327     4358   4134   3936   -246   -211    910       C  
ATOM   2135  N   LEU A 328     -22.539 -25.197  -6.284  1.00 23.87           N  
ANISOU 2135  N   LEU A 328     3218   3077   2774   -151     25    624       N  
ATOM   2136  CA  LEU A 328     -21.554 -26.128  -5.708  1.00 23.38           C  
ANISOU 2136  CA  LEU A 328     3137   3057   2690   -127    108    522       C  
ATOM   2137  C   LEU A 328     -20.232 -25.409  -5.434  1.00 26.60           C  
ANISOU 2137  C   LEU A 328     3545   3456   3104   -171    115    544       C  
ATOM   2138  O   LEU A 328     -19.618 -25.618  -4.384  1.00 27.85           O  
ANISOU 2138  O   LEU A 328     3701   3573   3309   -125    148    482       O  
ATOM   2139  CB  LEU A 328     -21.335 -27.310  -6.654  1.00 24.01           C  
ANISOU 2139  CB  LEU A 328     3187   3269   2667   -167    166    469       C  
ATOM   2140  CG  LEU A 328     -22.596 -28.225  -6.763  1.00 26.51           C  
ANISOU 2140  CG  LEU A 328     3500   3588   2983   -115    167    428       C  
ATOM   2141  CD1 LEU A 328     -22.409 -29.338  -7.802  1.00 24.91           C  
ANISOU 2141  CD1 LEU A 328     3267   3517   2682   -163    219    369       C  
ATOM   2142  CD2 LEU A 328     -22.920 -28.853  -5.381  1.00 24.24           C  
ANISOU 2142  CD2 LEU A 328     3212   3217   2780    -11    192    348       C  
ATOM   2143  N   ARG A 329     -19.792 -24.534  -6.347  1.00 25.72           N  
ANISOU 2143  N   ARG A 329     3439   3385   2948   -267     77    639       N  
ATOM   2144  CA  ARG A 329     -18.605 -23.709  -6.068  1.00 26.62           C  
ANISOU 2144  CA  ARG A 329     3555   3481   3079   -314     72    673       C  
ATOM   2145  C   ARG A 329     -18.778 -22.870  -4.794  1.00 27.00           C  
ANISOU 2145  C   ARG A 329     3630   3379   3251   -246     30    673       C  
ATOM   2146  O   ARG A 329     -17.819 -22.694  -4.020  1.00 27.68           O  
ANISOU 2146  O   ARG A 329     3713   3439   3365   -240     54    640       O  
ATOM   2147  CB  ARG A 329     -18.306 -22.770  -7.238  1.00 25.57           C  
ANISOU 2147  CB  ARG A 329     3427   3403   2885   -436     18    798       C  
ATOM   2148  CG  ARG A 329     -17.946 -23.446  -8.535  1.00 30.21           C  
ANISOU 2148  CG  ARG A 329     3985   4161   3332   -530     64    796       C  
ATOM   2149  CD  ARG A 329     -17.293 -22.437  -9.514  1.00 35.02           C  
ANISOU 2149  CD  ARG A 329     4596   4838   3872   -671     19    921       C  
ATOM   2150  NE  ARG A 329     -17.034 -23.099 -10.798  1.00 41.49           N  
ANISOU 2150  NE  ARG A 329     5384   5841   4539   -774     68    911       N  
ATOM   2151  CZ  ARG A 329     -15.919 -23.772 -11.059  1.00 42.28           C  
ANISOU 2151  CZ  ARG A 329     5438   6065   4563   -816    163    823       C  
ATOM   2152  NH1 ARG A 329     -15.754 -24.381 -12.224  1.00 43.79           N  
ANISOU 2152  NH1 ARG A 329     5596   6428   4616   -909    212    795       N  
ATOM   2153  NH2 ARG A 329     -14.982 -23.824 -10.143  1.00 41.64           N  
ANISOU 2153  NH2 ARG A 329     5340   5935   4547   -766    205    759       N  
ATOM   2154  N   GLU A 330     -19.987 -22.306  -4.586  1.00 26.11           N  
ANISOU 2154  N   GLU A 330     3538   3170   3215   -200    -33    708       N  
ATOM   2155  CA  GLU A 330     -20.249 -21.482  -3.407  1.00 25.53           C  
ANISOU 2155  CA  GLU A 330     3482   2956   3263   -137    -69    691       C  
ATOM   2156  C   GLU A 330     -20.150 -22.288  -2.122  1.00 26.42           C  
ANISOU 2156  C   GLU A 330     3590   3051   3397    -56     -4    571       C  
ATOM   2157  O   GLU A 330     -19.579 -21.823  -1.133  1.00 25.78           O  
ANISOU 2157  O   GLU A 330     3518   2908   3368    -39     -1    538       O  
ATOM   2158  CB  GLU A 330     -21.634 -20.832  -3.521  1.00 28.34           C  
ANISOU 2158  CB  GLU A 330     3845   3219   3704   -101   -144    737       C  
ATOM   2159  CG  GLU A 330     -21.654 -19.709  -4.579  1.00 37.12           C  
ANISOU 2159  CG  GLU A 330     4964   4310   4830   -187   -238    879       C  
ATOM   2160  CD  GLU A 330     -23.080 -19.096  -4.862  1.00 49.04           C  
ANISOU 2160  CD  GLU A 330     6470   5725   6436   -155   -328    939       C  
ATOM   2161  OE1 GLU A 330     -24.116 -19.507  -4.233  1.00 48.92           O  
ANISOU 2161  OE1 GLU A 330     6444   5663   6480    -61   -313    863       O  
ATOM   2162  OE2 GLU A 330     -23.149 -18.202  -5.761  1.00 55.98           O  
ANISOU 2162  OE2 GLU A 330     7353   6583   7334   -231   -421   1072       O  
ATOM   2163  N   ILE A 331     -20.734 -23.486  -2.090  1.00 23.41           N  
ANISOU 2163  N   ILE A 331     3196   2722   2979    -11     42    508       N  
ATOM   2164  CA  ILE A 331     -20.609 -24.317  -0.896  1.00 23.12           C  
ANISOU 2164  CA  ILE A 331     3153   2676   2957     52     95    409       C  
ATOM   2165  C   ILE A 331     -19.130 -24.606  -0.651  1.00 22.88           C  
ANISOU 2165  C   ILE A 331     3110   2691   2892     17    135    386       C  
ATOM   2166  O   ILE A 331     -18.646 -24.571   0.482  1.00 25.24           O  
ANISOU 2166  O   ILE A 331     3413   2949   3227     42    147    341       O  
ATOM   2167  CB  ILE A 331     -21.395 -25.639  -1.082  1.00 25.22           C  
ANISOU 2167  CB  ILE A 331     3403   2997   3184     92    131    359       C  
ATOM   2168  CG1 ILE A 331     -22.887 -25.358  -1.233  1.00 26.69           C  
ANISOU 2168  CG1 ILE A 331     3594   3135   3411    130     91    379       C  
ATOM   2169  CG2 ILE A 331     -21.138 -26.626   0.089  1.00 25.29           C  
ANISOU 2169  CG2 ILE A 331     3401   3006   3201    141    179    272       C  
ATOM   2170  CD1 ILE A 331     -23.655 -26.589  -1.566  1.00 28.64           C  
ANISOU 2170  CD1 ILE A 331     3825   3440   3616    156    120    341       C  
ATOM   2171  N   ASP A 332     -18.399 -24.934  -1.715  1.00 22.50           N  
ANISOU 2171  N   ASP A 332     3040   2736   2771    -46    157    411       N  
ATOM   2172  CA  ASP A 332     -16.983 -25.271  -1.547  1.00 22.69           C  
ANISOU 2172  CA  ASP A 332     3039   2811   2772    -77    199    381       C  
ATOM   2173  C   ASP A 332     -16.207 -24.097  -0.956  1.00 24.86           C  
ANISOU 2173  C   ASP A 332     3331   3022   3092   -106    166    418       C  
ATOM   2174  O   ASP A 332     -15.327 -24.286  -0.121  1.00 26.03           O  
ANISOU 2174  O   ASP A 332     3468   3161   3261    -97    187    377       O  
ATOM   2175  CB  ASP A 332     -16.351 -25.646  -2.858  1.00 25.50           C  
ANISOU 2175  CB  ASP A 332     3361   3284   3043   -150    230    396       C  
ATOM   2176  CG  ASP A 332     -14.994 -26.362  -2.633  1.00 30.53           C  
ANISOU 2176  CG  ASP A 332     3952   3978   3671   -162    287    333       C  
ATOM   2177  OD1 ASP A 332     -15.065 -27.575  -2.304  1.00 31.53           O  
ANISOU 2177  OD1 ASP A 332     4051   4120   3808   -110    325    253       O  
ATOM   2178  OD2 ASP A 332     -13.916 -25.714  -2.750  1.00 29.70           O  
ANISOU 2178  OD2 ASP A 332     3835   3893   3558   -222    287    364       O  
ATOM   2179  N   LYS A 333     -16.521 -22.877  -1.385  1.00 24.87           N  
ANISOU 2179  N   LYS A 333     3358   2975   3117   -144    107    500       N  
ATOM   2180  CA  LYS A 333     -15.898 -21.690  -0.774  1.00 26.73           C  
ANISOU 2180  CA  LYS A 333     3613   3132   3413   -168     67    533       C  
ATOM   2181  C   LYS A 333     -16.171 -21.593   0.737  1.00 26.30           C  
ANISOU 2181  C   LYS A 333     3576   2985   3432    -96     66    461       C  
ATOM   2182  O   LYS A 333     -15.284 -21.214   1.512  1.00 27.29           O  
ANISOU 2182  O   LYS A 333     3704   3082   3583   -110     66    443       O  
ATOM   2183  CB  LYS A 333     -16.415 -20.449  -1.494  1.00 32.28           C  
ANISOU 2183  CB  LYS A 333     4337   3777   4149   -213    -10    635       C  
ATOM   2184  CG  LYS A 333     -15.812 -19.121  -1.043  1.00 38.78           C  
ANISOU 2184  CG  LYS A 333     5179   4509   5045   -248    -65    681       C  
ATOM   2185  CD  LYS A 333     -16.516 -17.932  -1.770  1.00 44.07           C  
ANISOU 2185  CD  LYS A 333     5867   5103   5774   -285   -158    790       C  
ATOM   2186  CE  LYS A 333     -15.836 -16.570  -1.541  1.00 49.93           C  
ANISOU 2186  CE  LYS A 333     6624   5753   6593   -339   -224    852       C  
ATOM   2187  NZ  LYS A 333     -16.558 -15.504  -2.360  1.00 53.05           N  
ANISOU 2187  NZ  LYS A 333     7031   6071   7054   -380   -328    972       N  
ATOM   2188  N   THR A 334     -17.386 -21.933   1.182  1.00 24.42           N  
ANISOU 2188  N   THR A 334     3347   2709   3224    -27     66    417       N  
ATOM   2189  CA  THR A 334     -17.684 -21.923   2.626  1.00 25.51           C  
ANISOU 2189  CA  THR A 334     3497   2783   3413     30     74    339       C  
ATOM   2190  C   THR A 334     -16.896 -23.007   3.373  1.00 25.51           C  
ANISOU 2190  C   THR A 334     3480   2841   3371     38    124    280       C  
ATOM   2191  O   THR A 334     -16.369 -22.770   4.466  1.00 23.52           O  
ANISOU 2191  O   THR A 334     3236   2557   3142     39    124    243       O  
ATOM   2192  CB  THR A 334     -19.183 -22.094   2.828  1.00 25.08           C  
ANISOU 2192  CB  THR A 334     3446   2692   3391     93     68    307       C  
ATOM   2193  OG1 THR A 334     -19.822 -21.048   2.085  1.00 26.83           O  
ANISOU 2193  OG1 THR A 334     3676   2852   3668     81      8    372       O  
ATOM   2194  CG2 THR A 334     -19.594 -21.999   4.298  1.00 25.77           C  
ANISOU 2194  CG2 THR A 334     3541   2726   3523    140     80    220       C  
ATOM   2195  N   VAL A 335     -16.814 -24.204   2.803  1.00 23.17           N  
ANISOU 2195  N   VAL A 335     3157   2625   3020     43    162    270       N  
ATOM   2196  CA  VAL A 335     -15.926 -25.222   3.361  1.00 21.51           C  
ANISOU 2196  CA  VAL A 335     2921   2462   2790     45    198    227       C  
ATOM   2197  C   VAL A 335     -14.466 -24.727   3.449  1.00 23.46           C  
ANISOU 2197  C   VAL A 335     3155   2718   3040     -8    194    248       C  
ATOM   2198  O   VAL A 335     -13.794 -24.973   4.443  1.00 24.57           O  
ANISOU 2198  O   VAL A 335     3289   2851   3197     -6    196    217       O  
ATOM   2199  CB  VAL A 335     -16.015 -26.512   2.546  1.00 22.10           C  
ANISOU 2199  CB  VAL A 335     2960   2613   2822     55    235    209       C  
ATOM   2200  CG1 VAL A 335     -15.064 -27.559   3.187  1.00 21.20           C  
ANISOU 2200  CG1 VAL A 335     2811   2528   2716     62    259    164       C  
ATOM   2201  CG2 VAL A 335     -17.484 -27.001   2.583  1.00 20.19           C  
ANISOU 2201  CG2 VAL A 335     2733   2358   2582    107    234    188       C  
ATOM   2202  N   GLY A 336     -13.965 -24.031   2.420  1.00 24.03           N  
ANISOU 2202  N   GLY A 336     3222   2814   3094    -65    184    306       N  
ATOM   2203  CA  GLY A 336     -12.622 -23.481   2.476  1.00 25.54           C  
ANISOU 2203  CA  GLY A 336     3399   3016   3289   -122    179    330       C  
ATOM   2204  C   GLY A 336     -12.459 -22.415   3.544  1.00 26.87           C  
ANISOU 2204  C   GLY A 336     3602   3095   3512   -126    138    332       C  
ATOM   2205  O   GLY A 336     -11.403 -22.324   4.175  1.00 23.10           O  
ANISOU 2205  O   GLY A 336     3113   2619   3046   -151    138    322       O  
ATOM   2206  N   GLN A 337     -13.504 -21.598   3.775  1.00 26.17           N  
ANISOU 2206  N   GLN A 337     3552   2926   3464   -101    102    339       N  
ATOM   2207  CA  GLN A 337     -13.408 -20.623   4.856  1.00 24.31           C  
ANISOU 2207  CA  GLN A 337     3346   2604   3288   -102     68    316       C  
ATOM   2208  C   GLN A 337     -13.335 -21.310   6.210  1.00 24.73           C  
ANISOU 2208  C   GLN A 337     3399   2663   3336    -68     90    240       C  
ATOM   2209  O   GLN A 337     -12.542 -20.909   7.066  1.00 25.99           O  
ANISOU 2209  O   GLN A 337     3564   2801   3510    -96     77    222       O  
ATOM   2210  CB  GLN A 337     -14.580 -19.648   4.820  1.00 23.26           C  
ANISOU 2210  CB  GLN A 337     3242   2379   3219    -76     26    323       C  
ATOM   2211  CG  GLN A 337     -14.533 -18.657   3.656  1.00 29.17           C  
ANISOU 2211  CG  GLN A 337     3995   3097   3992   -126    -24    419       C  
ATOM   2212  CD  GLN A 337     -15.878 -17.889   3.543  1.00 36.61           C  
ANISOU 2212  CD  GLN A 337     4954   3942   5014    -87    -72    426       C  
ATOM   2213  OE1 GLN A 337     -16.821 -18.109   4.350  1.00 40.60           O  
ANISOU 2213  OE1 GLN A 337     5462   4411   5552    -20    -57    346       O  
ATOM   2214  NE2 GLN A 337     -15.966 -16.994   2.560  1.00 36.65           N  
ANISOU 2214  NE2 GLN A 337     4964   3908   5055   -132   -133    522       N  
ATOM   2215  N   LEU A 338     -14.112 -22.366   6.413  1.00 25.58           N  
ANISOU 2215  N   LEU A 338     3498   2803   3418    -19    120    200       N  
ATOM   2216  CA  LEU A 338     -13.998 -23.122   7.657  1.00 23.55           C  
ANISOU 2216  CA  LEU A 338     3239   2564   3146     -3    134    144       C  
ATOM   2217  C   LEU A 338     -12.602 -23.705   7.822  1.00 23.99           C  
ANISOU 2217  C   LEU A 338     3262   2668   3185    -38    140    158       C  
ATOM   2218  O   LEU A 338     -11.995 -23.565   8.892  1.00 23.73           O  
ANISOU 2218  O   LEU A 338     3234   2624   3156    -61    124    138       O  
ATOM   2219  CB  LEU A 338     -15.050 -24.252   7.717  1.00 23.16           C  
ANISOU 2219  CB  LEU A 338     3181   2547   3073     47    160    114       C  
ATOM   2220  CG  LEU A 338     -14.994 -25.174   8.950  1.00 24.95           C  
ANISOU 2220  CG  LEU A 338     3402   2801   3278     53    168     73       C  
ATOM   2221  CD1 LEU A 338     -15.373 -24.355  10.197  1.00 23.27           C  
ANISOU 2221  CD1 LEU A 338     3220   2547   3072     44    155     23       C  
ATOM   2222  CD2 LEU A 338     -16.019 -26.367   8.847  1.00 26.97           C  
ANISOU 2222  CD2 LEU A 338     3646   3090   3512     96    189     56       C  
ATOM   2223  N   MET A 339     -12.119 -24.467   6.815  1.00 24.88           N  
ANISOU 2223  N   MET A 339     3335   2839   3279    -43    163    184       N  
ATOM   2224  CA  MET A 339     -10.804 -25.099   6.961  1.00 23.78           C  
ANISOU 2224  CA  MET A 339     3151   2743   3142    -69    169    186       C  
ATOM   2225  C   MET A 339      -9.706 -24.045   7.138  1.00 23.37           C  
ANISOU 2225  C   MET A 339     3101   2672   3107   -126    145    215       C  
ATOM   2226  O   MET A 339      -8.756 -24.258   7.905  1.00 21.88           O  
ANISOU 2226  O   MET A 339     2892   2491   2933   -147    131    208       O  
ATOM   2227  CB  MET A 339     -10.462 -26.021   5.779  1.00 23.83           C  
ANISOU 2227  CB  MET A 339     3103   2816   3134    -65    206    189       C  
ATOM   2228  CG  MET A 339     -11.478 -27.184   5.599  1.00 25.95           C  
ANISOU 2228  CG  MET A 339     3365   3102   3392    -11    226    157       C  
ATOM   2229  SD  MET A 339     -11.893 -28.012   7.192  1.00 26.88           S  
ANISOU 2229  SD  MET A 339     3494   3191   3529     22    203    126       S  
ATOM   2230  CE  MET A 339     -10.404 -28.867   7.665  1.00 27.07           C  
ANISOU 2230  CE  MET A 339     3455   3237   3595      3    189    125       C  
ATOM   2231  N   ASP A 340      -9.765 -22.942   6.399  1.00 25.40           N  
ANISOU 2231  N   ASP A 340     3379   2906   3367   -156    134    254       N  
ATOM   2232  CA  ASP A 340      -8.722 -21.933   6.599  1.00 24.92           C  
ANISOU 2232  CA  ASP A 340     3320   2821   3327   -216    106    284       C  
ATOM   2233  C   ASP A 340      -8.816 -21.383   8.023  1.00 26.86           C  
ANISOU 2233  C   ASP A 340     3603   3003   3598   -214     74    247       C  
ATOM   2234  O   ASP A 340      -7.789 -21.100   8.679  1.00 27.51           O  
ANISOU 2234  O   ASP A 340     3677   3082   3692   -255     54    249       O  
ATOM   2235  CB  ASP A 340      -8.864 -20.768   5.605  1.00 27.82           C  
ANISOU 2235  CB  ASP A 340     3708   3162   3701   -257     86    344       C  
ATOM   2236  CG  ASP A 340      -8.447 -21.117   4.144  1.00 32.34           C  
ANISOU 2236  CG  ASP A 340     4237   3820   4229   -294    117    390       C  
ATOM   2237  OD1 ASP A 340      -7.896 -22.206   3.856  1.00 32.43           O  
ANISOU 2237  OD1 ASP A 340     4196   3911   4215   -288    160    363       O  
ATOM   2238  OD2 ASP A 340      -8.691 -20.250   3.255  1.00 34.74           O  
ANISOU 2238  OD2 ASP A 340     4558   4113   4527   -336     94    453       O  
ATOM   2239  N   GLY A 341     -10.048 -21.175   8.502  1.00 24.75           N  
ANISOU 2239  N   GLY A 341     3376   2689   3339   -173     69    209       N  
ATOM   2240  CA  GLY A 341     -10.220 -20.612   9.833  1.00 26.50           C  
ANISOU 2240  CA  GLY A 341     3630   2861   3577   -178     46    156       C  
ATOM   2241  C   GLY A 341      -9.715 -21.553  10.913  1.00 26.30           C  
ANISOU 2241  C   GLY A 341     3590   2884   3520   -185     49    127       C  
ATOM   2242  O   GLY A 341      -9.108 -21.122  11.885  1.00 26.45           O  
ANISOU 2242  O   GLY A 341     3620   2891   3540   -225     24    108       O  
ATOM   2243  N   LEU A 342      -9.953 -22.852  10.747  1.00 24.17           N  
ANISOU 2243  N   LEU A 342     3292   2668   3225   -152     73    129       N  
ATOM   2244  CA  LEU A 342      -9.417 -23.857  11.678  1.00 23.85           C  
ANISOU 2244  CA  LEU A 342     3227   2668   3165   -163     62    122       C  
ATOM   2245  C   LEU A 342      -7.895 -23.886  11.621  1.00 26.10           C  
ANISOU 2245  C   LEU A 342     3472   2973   3471   -208     42    159       C  
ATOM   2246  O   LEU A 342      -7.219 -24.021  12.653  1.00 26.48           O  
ANISOU 2246  O   LEU A 342     3515   3031   3516   -244      9    158       O  
ATOM   2247  CB  LEU A 342      -9.957 -25.255  11.308  1.00 20.30           C  
ANISOU 2247  CB  LEU A 342     2749   2259   2705   -117     85    124       C  
ATOM   2248  CG  LEU A 342     -11.440 -25.438  11.581  1.00 23.43           C  
ANISOU 2248  CG  LEU A 342     3178   2647   3078    -78    102     87       C  
ATOM   2249  CD1 LEU A 342     -11.932 -26.886  11.146  1.00 21.56           C  
ANISOU 2249  CD1 LEU A 342     2909   2446   2836    -36    120     94       C  
ATOM   2250  CD2 LEU A 342     -11.781 -25.222  13.093  1.00 24.38           C  
ANISOU 2250  CD2 LEU A 342     3330   2767   3167   -106     83     47       C  
ATOM   2251  N   LYS A 343      -7.332 -23.786  10.406  1.00 21.16           N  
ANISOU 2251  N   LYS A 343     2813   2364   2864   -212     61    192       N  
ATOM   2252  CA  LYS A 343      -5.885 -23.784  10.304  1.00 22.47           C  
ANISOU 2252  CA  LYS A 343     2930   2555   3054   -256     48    221       C  
ATOM   2253  C   LYS A 343      -5.310 -22.556  11.022  1.00 25.62           C  
ANISOU 2253  C   LYS A 343     3361   2914   3460   -312     10    227       C  
ATOM   2254  O   LYS A 343      -4.294 -22.642  11.711  1.00 24.56           O  
ANISOU 2254  O   LYS A 343     3201   2791   3339   -351    -20    237       O  
ATOM   2255  CB  LYS A 343      -5.462 -23.877   8.820  1.00 24.85           C  
ANISOU 2255  CB  LYS A 343     3185   2896   3361   -260     86    246       C  
ATOM   2256  CG  LYS A 343      -3.945 -23.791   8.635  1.00 29.77           C  
ANISOU 2256  CG  LYS A 343     3748   3553   4012   -310     80    270       C  
ATOM   2257  CD  LYS A 343      -3.521 -23.975   7.140  1.00 28.64           C  
ANISOU 2257  CD  LYS A 343     3548   3473   3861   -323    129    281       C  
ATOM   2258  CE  LYS A 343      -2.003 -23.667   7.029  1.00 29.45           C  
ANISOU 2258  CE  LYS A 343     3589   3610   3991   -384    125    303       C  
ATOM   2259  NZ  LYS A 343      -1.546 -23.700   5.631  1.00 31.08           N  
ANISOU 2259  NZ  LYS A 343     3739   3892   4177   -416    177    310       N  
ATOM   2260  N   GLN A 344      -6.003 -21.425  10.937  1.00 23.61           N  
ANISOU 2260  N   GLN A 344     3161   2605   3206   -316      5    218       N  
ATOM   2261  CA  GLN A 344      -5.566 -20.210  11.618  1.00 25.79           C  
ANISOU 2261  CA  GLN A 344     3470   2830   3499   -368    -32    211       C  
ATOM   2262  C   GLN A 344      -5.570 -20.371  13.148  1.00 27.96           C  
ANISOU 2262  C   GLN A 344     3767   3106   3753   -384    -58    163       C  
ATOM   2263  O   GLN A 344      -4.700 -19.829  13.838  1.00 31.55           O  
ANISOU 2263  O   GLN A 344     4223   3551   4214   -440    -93    164       O  
ATOM   2264  CB  GLN A 344      -6.513 -19.073  11.174  1.00 27.73           C  
ANISOU 2264  CB  GLN A 344     3764   3004   3770   -356    -36    202       C  
ATOM   2265  CG  GLN A 344      -6.100 -17.698  11.540  1.00 33.52           C  
ANISOU 2265  CG  GLN A 344     4525   3667   4542   -407    -77    199       C  
ATOM   2266  CD  GLN A 344      -6.702 -16.664  10.531  1.00 35.70           C  
ANISOU 2266  CD  GLN A 344     4823   3874   4866   -403    -91    233       C  
ATOM   2267  OE1 GLN A 344      -5.981 -16.081   9.707  1.00 37.83           O  
ANISOU 2267  OE1 GLN A 344     5080   4139   5156   -452   -109    302       O  
ATOM   2268  NE2 GLN A 344      -8.017 -16.466  10.610  1.00 32.70           N  
ANISOU 2268  NE2 GLN A 344     4473   3445   4507   -351    -86    189       N  
ATOM   2269  N   LEU A 345      -6.536 -21.105  13.698  1.00 29.53           N  
ANISOU 2269  N   LEU A 345     3979   3321   3918   -346    -44    125       N  
ATOM   2270  CA  LEU A 345      -6.605 -21.476  15.113  1.00 30.40           C  
ANISOU 2270  CA  LEU A 345     4105   3457   3987   -372    -66     88       C  
ATOM   2271  C   LEU A 345      -5.695 -22.666  15.497  1.00 28.61           C  
ANISOU 2271  C   LEU A 345     3828   3288   3753   -392    -91    133       C  
ATOM   2272  O   LEU A 345      -5.752 -23.114  16.648  1.00 25.65           O  
ANISOU 2272  O   LEU A 345     3462   2944   3338   -423   -119    121       O  
ATOM   2273  CB  LEU A 345      -8.081 -21.828  15.502  1.00 29.38           C  
ANISOU 2273  CB  LEU A 345     4006   3335   3824   -330    -38     34       C  
ATOM   2274  CG  LEU A 345      -9.116 -20.682  15.370  1.00 31.73           C  
ANISOU 2274  CG  LEU A 345     4345   3568   4142   -307    -19    -28       C  
ATOM   2275  CD1 LEU A 345     -10.525 -21.131  15.831  1.00 31.67           C  
ANISOU 2275  CD1 LEU A 345     4353   3579   4099   -269     13    -87       C  
ATOM   2276  CD2 LEU A 345      -8.632 -19.454  16.168  1.00 33.66           C  
ANISOU 2276  CD2 LEU A 345     4618   3772   4400   -364    -48    -74       C  
ATOM   2277  N   LYS A 346      -4.931 -23.233  14.567  1.00 27.13           N  
ANISOU 2277  N   LYS A 346     3584   3117   3606   -376    -84    182       N  
ATOM   2278  CA  LYS A 346      -4.109 -24.404  14.849  1.00 27.62           C  
ANISOU 2278  CA  LYS A 346     3586   3219   3689   -383   -113    219       C  
ATOM   2279  C   LYS A 346      -4.964 -25.599  15.261  1.00 26.77           C  
ANISOU 2279  C   LYS A 346     3478   3134   3561   -348   -113    214       C  
ATOM   2280  O   LYS A 346      -4.501 -26.464  16.006  1.00 26.86           O  
ANISOU 2280  O   LYS A 346     3457   3167   3580   -370   -160    245       O  
ATOM   2281  CB  LYS A 346      -3.028 -24.078  15.906  1.00 30.69           C  
ANISOU 2281  CB  LYS A 346     3967   3616   4078   -455   -172    239       C  
ATOM   2282  CG  LYS A 346      -1.959 -23.065  15.325  1.00 34.33           C  
ANISOU 2282  CG  LYS A 346     4409   4058   4575   -492   -174    257       C  
ATOM   2283  CD  LYS A 346      -1.097 -22.427  16.403  1.00 42.61           C  
ANISOU 2283  CD  LYS A 346     5469   5105   5615   -569   -231    263       C  
ATOM   2284  CE  LYS A 346      -0.152 -21.327  15.813  1.00 47.28           C  
ANISOU 2284  CE  LYS A 346     6048   5674   6243   -610   -233    281       C  
ATOM   2285  NZ  LYS A 346      -0.447 -21.037  14.333  1.00 48.40           N  
ANISOU 2285  NZ  LYS A 346     6180   5803   6408   -569   -176    290       N  
ATOM   2286  N   LEU A 347      -6.184 -25.703  14.709  1.00 24.61           N  
ANISOU 2286  N   LEU A 347     3231   2852   3268   -296    -68    185       N  
ATOM   2287  CA  LEU A 347      -7.105 -26.821  14.968  1.00 23.37           C  
ANISOU 2287  CA  LEU A 347     3073   2714   3092   -262    -64    181       C  
ATOM   2288  C   LEU A 347      -7.368 -27.731  13.755  1.00 26.84           C  
ANISOU 2288  C   LEU A 347     3470   3158   3571   -199    -29    188       C  
ATOM   2289  O   LEU A 347      -8.226 -28.616  13.841  1.00 26.56           O  
ANISOU 2289  O   LEU A 347     3435   3131   3525   -167    -23    183       O  
ATOM   2290  CB  LEU A 347      -8.435 -26.281  15.483  1.00 22.50           C  
ANISOU 2290  CB  LEU A 347     3027   2599   2923   -257    -41    130       C  
ATOM   2291  CG  LEU A 347      -8.343 -25.516  16.824  1.00 26.18           C  
ANISOU 2291  CG  LEU A 347     3535   3075   3339   -324    -70    100       C  
ATOM   2292  CD1 LEU A 347      -9.646 -24.903  17.290  1.00 25.66           C  
ANISOU 2292  CD1 LEU A 347     3519   3005   3225   -318    -37     28       C  
ATOM   2293  CD2 LEU A 347      -7.916 -26.546  17.862  1.00 28.01           C  
ANISOU 2293  CD2 LEU A 347     3743   3353   3545   -372   -123    142       C  
ATOM   2294  N   HIS A 348      -6.635 -27.581  12.651  1.00 25.38           N  
ANISOU 2294  N   HIS A 348     3243   2972   3427   -187     -6    197       N  
ATOM   2295  CA  HIS A 348      -7.011 -28.325  11.441  1.00 26.34           C  
ANISOU 2295  CA  HIS A 348     3330   3108   3572   -134     37    186       C  
ATOM   2296  C   HIS A 348      -6.588 -29.784  11.512  1.00 26.10           C  
ANISOU 2296  C   HIS A 348     3230   3087   3598   -112     16    194       C  
ATOM   2297  O   HIS A 348      -6.959 -30.561  10.635  1.00 27.10           O  
ANISOU 2297  O   HIS A 348     3325   3224   3748    -68     49    173       O  
ATOM   2298  CB  HIS A 348      -6.387 -27.664  10.178  1.00 20.74           C  
ANISOU 2298  CB  HIS A 348     2595   2412   2874   -142     75    188       C  
ATOM   2299  CG  HIS A 348      -4.884 -27.504  10.255  1.00 22.86           C  
ANISOU 2299  CG  HIS A 348     2808   2693   3184   -184     55    208       C  
ATOM   2300  ND1 HIS A 348      -4.253 -26.805  11.267  1.00 26.29           N  
ANISOU 2300  ND1 HIS A 348     3263   3110   3617   -234      9    229       N  
ATOM   2301  CD2 HIS A 348      -3.895 -27.897   9.411  1.00 25.86           C  
ANISOU 2301  CD2 HIS A 348     3108   3107   3609   -187     78    205       C  
ATOM   2302  CE1 HIS A 348      -2.941 -26.830  11.086  1.00 27.17           C  
ANISOU 2302  CE1 HIS A 348     3310   3239   3774   -264     -2    246       C  
ATOM   2303  NE2 HIS A 348      -2.699 -27.476   9.960  1.00 28.61           N  
ANISOU 2303  NE2 HIS A 348     3428   3454   3988   -235     42    229       N  
ATOM   2304  N   ARG A 349      -5.782 -30.144  12.503  1.00 23.80           N  
ANISOU 2304  N   ARG A 349     2912   2791   3339   -145    -42    224       N  
ATOM   2305  CA  ARG A 349      -5.360 -31.519  12.734  1.00 23.82           C  
ANISOU 2305  CA  ARG A 349     2846   2787   3419   -128    -83    243       C  
ATOM   2306  C   ARG A 349      -5.837 -31.989  14.118  1.00 28.06           C  
ANISOU 2306  C   ARG A 349     3416   3319   3927   -159   -148    281       C  
ATOM   2307  O   ARG A 349      -5.287 -32.946  14.719  1.00 27.69           O  
ANISOU 2307  O   ARG A 349     3318   3259   3944   -172   -215    323       O  
ATOM   2308  CB  ARG A 349      -3.841 -31.611  12.544  1.00 24.67           C  
ANISOU 2308  CB  ARG A 349     2871   2896   3608   -145   -105    255       C  
ATOM   2309  CG  ARG A 349      -3.407 -31.436  11.038  1.00 26.24           C  
ANISOU 2309  CG  ARG A 349     3017   3118   3833   -118    -32    209       C  
ATOM   2310  CD  ARG A 349      -1.838 -31.386  10.834  1.00 27.61           C  
ANISOU 2310  CD  ARG A 349     3101   3305   4086   -143    -44    212       C  
ATOM   2311  NE  ARG A 349      -1.181 -32.596  11.330  1.00 32.26           N  
ANISOU 2311  NE  ARG A 349     3604   3865   4787   -126   -104    225       N  
ATOM   2312  CZ  ARG A 349      -1.173 -33.762  10.666  1.00 35.64           C  
ANISOU 2312  CZ  ARG A 349     3954   4284   5304    -72    -88    182       C  
ATOM   2313  NH1 ARG A 349      -1.746 -33.856   9.470  1.00 32.26           N  
ANISOU 2313  NH1 ARG A 349     3524   3885   4848    -37     -7    120       N  
ATOM   2314  NH2 ARG A 349      -0.577 -34.830  11.189  1.00 38.18           N  
ANISOU 2314  NH2 ARG A 349     4195   4563   5749    -57   -157    199       N  
ATOM   2315  N   CYS A 350      -6.892 -31.343  14.622  1.00 29.02           N  
ANISOU 2315  N   CYS A 350     3618   3452   3956   -175   -130    266       N  
ATOM   2316  CA  CYS A 350      -7.476 -31.606  15.940  1.00 30.35           C  
ANISOU 2316  CA  CYS A 350     3827   3637   4067   -220   -177    292       C  
ATOM   2317  C   CYS A 350      -8.998 -31.883  15.843  1.00 32.31           C  
ANISOU 2317  C   CYS A 350     4117   3896   4263   -189   -138    263       C  
ATOM   2318  O   CYS A 350      -9.543 -32.693  16.604  1.00 36.14           O  
ANISOU 2318  O   CYS A 350     4608   4397   4727   -211   -174    292       O  
ATOM   2319  CB  CYS A 350      -7.185 -30.380  16.841  1.00 34.21           C  
ANISOU 2319  CB  CYS A 350     4367   4144   4488   -287   -190    283       C  
ATOM   2320  SG  CYS A 350      -8.143 -30.375  18.372  1.00 42.39           S  
ANISOU 2320  SG  CYS A 350     5465   5227   5415   -354   -218    282       S  
ATOM   2321  N   VAL A 351      -9.697 -31.278  14.871  1.00 29.14           N  
ANISOU 2321  N   VAL A 351     3741   3485   3844   -141    -69    214       N  
ATOM   2322  CA  VAL A 351     -11.165 -31.340  14.782  1.00 26.63           C  
ANISOU 2322  CA  VAL A 351     3464   3177   3478   -112    -31    182       C  
ATOM   2323  C   VAL A 351     -11.592 -32.438  13.813  1.00 26.38           C  
ANISOU 2323  C   VAL A 351     3393   3135   3495    -54    -13    183       C  
ATOM   2324  O   VAL A 351     -11.020 -32.579  12.730  1.00 27.87           O  
ANISOU 2324  O   VAL A 351     3541   3310   3737    -20      8    174       O  
ATOM   2325  CB  VAL A 351     -11.714 -29.966  14.330  1.00 27.56           C  
ANISOU 2325  CB  VAL A 351     3628   3283   3560    -98     21    133       C  
ATOM   2326  CG1 VAL A 351     -13.177 -30.004  14.054  1.00 27.46           C  
ANISOU 2326  CG1 VAL A 351     3643   3274   3517    -59     61     98       C  
ATOM   2327  CG2 VAL A 351     -11.379 -28.883  15.361  1.00 26.64           C  
ANISOU 2327  CG2 VAL A 351     3550   3172   3402   -156      3    116       C  
ATOM   2328  N   ASN A 352     -12.593 -33.246  14.201  1.00 24.60           N  
ANISOU 2328  N   ASN A 352     3177   2921   3248    -48    -21    189       N  
ATOM   2329  CA  ASN A 352     -13.245 -34.144  13.258  1.00 23.53           C  
ANISOU 2329  CA  ASN A 352     3017   2774   3149      7      2    177       C  
ATOM   2330  C   ASN A 352     -14.342 -33.391  12.500  1.00 23.38           C  
ANISOU 2330  C   ASN A 352     3038   2761   3086     44     65    131       C  
ATOM   2331  O   ASN A 352     -15.146 -32.683  13.107  1.00 22.50           O  
ANISOU 2331  O   ASN A 352     2972   2664   2915     28     80    111       O  
ATOM   2332  CB  ASN A 352     -13.828 -35.365  13.985  1.00 22.28           C  
ANISOU 2332  CB  ASN A 352     2848   2620   2996     -9    -42    213       C  
ATOM   2333  CG  ASN A 352     -12.730 -36.261  14.567  1.00 25.56           C  
ANISOU 2333  CG  ASN A 352     3211   3015   3484    -40   -120    272       C  
ATOM   2334  OD1 ASN A 352     -11.870 -36.722  13.837  1.00 23.37           O  
ANISOU 2334  OD1 ASN A 352     2876   2705   3298     -7   -128    267       O  
ATOM   2335  ND2 ASN A 352     -12.756 -36.496  15.897  1.00 25.15           N  
ANISOU 2335  ND2 ASN A 352     3176   2987   3392   -109   -181    326       N  
ATOM   2336  N   VAL A 353     -14.308 -33.453  11.171  1.00 23.18           N  
ANISOU 2336  N   VAL A 353     2989   2727   3091     88    101    110       N  
ATOM   2337  CA  VAL A 353     -15.297 -32.751  10.356  1.00 24.11           C  
ANISOU 2337  CA  VAL A 353     3139   2847   3174    118    148     81       C  
ATOM   2338  C   VAL A 353     -16.137 -33.806   9.649  1.00 24.06           C  
ANISOU 2338  C   VAL A 353     3113   2846   3182    157    163     69       C  
ATOM   2339  O   VAL A 353     -15.572 -34.757   9.079  1.00 23.40           O  
ANISOU 2339  O   VAL A 353     2980   2760   3150    172    157     67       O  
ATOM   2340  CB  VAL A 353     -14.661 -31.796   9.339  1.00 26.23           C  
ANISOU 2340  CB  VAL A 353     3405   3112   3447    120    175     75       C  
ATOM   2341  CG1 VAL A 353     -15.777 -31.076   8.583  1.00 25.20           C  
ANISOU 2341  CG1 VAL A 353     3309   2980   3287    144    206     61       C  
ATOM   2342  CG2 VAL A 353     -13.775 -30.721  10.015  1.00 27.24           C  
ANISOU 2342  CG2 VAL A 353     3552   3229   3569     78    156     87       C  
ATOM   2343  N   ILE A 354     -17.464 -33.677   9.726  1.00 21.70           N  
ANISOU 2343  N   ILE A 354     2846   2554   2846    173    179     56       N  
ATOM   2344  CA  ILE A 354     -18.364 -34.561   8.963  1.00 22.42           C  
ANISOU 2344  CA  ILE A 354     2921   2651   2945    208    194     44       C  
ATOM   2345  C   ILE A 354     -19.112 -33.703   7.929  1.00 25.57           C  
ANISOU 2345  C   ILE A 354     3342   3054   3318    233    230     26       C  
ATOM   2346  O   ILE A 354     -19.707 -32.669   8.279  1.00 27.53           O  
ANISOU 2346  O   ILE A 354     3626   3294   3541    231    237     20       O  
ATOM   2347  CB  ILE A 354     -19.370 -35.278   9.874  1.00 23.35           C  
ANISOU 2347  CB  ILE A 354     3049   2778   3046    201    177     52       C  
ATOM   2348  CG1 ILE A 354     -18.688 -36.360  10.694  1.00 21.01           C  
ANISOU 2348  CG1 ILE A 354     2723   2474   2786    172    126     86       C  
ATOM   2349  CG2 ILE A 354     -20.606 -35.833   9.013  1.00 21.71           C  
ANISOU 2349  CG2 ILE A 354     2836   2577   2835    239    199     33       C  
ATOM   2350  CD1 ILE A 354     -19.669 -37.039  11.727  1.00 22.99           C  
ANISOU 2350  CD1 ILE A 354     2986   2745   3006    144    102    110       C  
ATOM   2351  N   PHE A 355     -19.007 -34.084   6.639  1.00 21.88           N  
ANISOU 2351  N   PHE A 355     2850   2601   2864    251    249     16       N  
ATOM   2352  CA  PHE A 355     -19.692 -33.403   5.542  1.00 20.59           C  
ANISOU 2352  CA  PHE A 355     2703   2448   2672    263    271     14       C  
ATOM   2353  C   PHE A 355     -20.785 -34.373   5.087  1.00 23.08           C  
ANISOU 2353  C   PHE A 355     3008   2778   2986    289    277     -2       C  
ATOM   2354  O   PHE A 355     -20.481 -35.453   4.557  1.00 21.60           O  
ANISOU 2354  O   PHE A 355     2783   2603   2820    296    282    -23       O  
ATOM   2355  CB  PHE A 355     -18.710 -33.111   4.383  1.00 22.30           C  
ANISOU 2355  CB  PHE A 355     2897   2690   2885    245    289     15       C  
ATOM   2356  CG  PHE A 355     -19.336 -32.359   3.211  1.00 22.60           C  
ANISOU 2356  CG  PHE A 355     2953   2748   2887    239    300     31       C  
ATOM   2357  CD1 PHE A 355     -19.475 -30.985   3.265  1.00 22.68           C  
ANISOU 2357  CD1 PHE A 355     2996   2731   2888    225    286     64       C  
ATOM   2358  CD2 PHE A 355     -19.726 -33.012   2.056  1.00 22.85           C  
ANISOU 2358  CD2 PHE A 355     2964   2822   2898    242    318     14       C  
ATOM   2359  CE1 PHE A 355     -20.039 -30.241   2.140  1.00 22.44           C  
ANISOU 2359  CE1 PHE A 355     2980   2713   2834    212    281     97       C  
ATOM   2360  CE2 PHE A 355     -20.339 -32.295   0.987  1.00 22.12           C  
ANISOU 2360  CE2 PHE A 355     2888   2752   2764    225    318     43       C  
ATOM   2361  CZ  PHE A 355     -20.470 -30.930   1.039  1.00 23.40           C  
ANISOU 2361  CZ  PHE A 355     3083   2884   2923    210    295     91       C  
ATOM   2362  N   VAL A 356     -22.044 -34.001   5.285  1.00 21.94           N  
ANISOU 2362  N   VAL A 356     2888   2626   2822    305    277      0       N  
ATOM   2363  CA  VAL A 356     -23.141 -34.947   5.134  1.00 22.16           C  
ANISOU 2363  CA  VAL A 356     2905   2664   2849    326    278    -12       C  
ATOM   2364  C   VAL A 356     -24.350 -34.244   4.518  1.00 24.06           C  
ANISOU 2364  C   VAL A 356     3164   2908   3071    343    284     -7       C  
ATOM   2365  O   VAL A 356     -24.640 -33.086   4.848  1.00 27.30           O  
ANISOU 2365  O   VAL A 356     3595   3296   3482    345    280      0       O  
ATOM   2366  CB  VAL A 356     -23.500 -35.564   6.517  1.00 24.50           C  
ANISOU 2366  CB  VAL A 356     3203   2953   3152    318    262    -10       C  
ATOM   2367  CG1 VAL A 356     -24.008 -34.508   7.500  1.00 22.41           C  
ANISOU 2367  CG1 VAL A 356     2968   2683   2865    310    266    -14       C  
ATOM   2368  CG2 VAL A 356     -24.504 -36.623   6.378  1.00 25.79           C  
ANISOU 2368  CG2 VAL A 356     3352   3127   3319    332    258    -16       C  
ATOM   2369  N   GLY A 357     -25.086 -34.958   3.628  1.00 21.77           N  
ANISOU 2369  N   GLY A 357     2859   2639   2774    356    287    -14       N  
ATOM   2370  CA  GLY A 357     -26.314 -34.428   3.073  1.00 20.09           C  
ANISOU 2370  CA  GLY A 357     2654   2428   2550    371    282     -4       C  
ATOM   2371  C   GLY A 357     -27.569 -35.071   3.648  1.00 24.15           C  
ANISOU 2371  C   GLY A 357     3160   2943   3071    390    281    -17       C  
ATOM   2372  O   GLY A 357     -27.530 -36.135   4.272  1.00 26.17           O  
ANISOU 2372  O   GLY A 357     3405   3205   3334    386    280    -29       O  
ATOM   2373  N   ASP A 358     -28.708 -34.421   3.447  1.00 23.25           N  
ANISOU 2373  N   ASP A 358     3049   2822   2962    408    275    -11       N  
ATOM   2374  CA  ASP A 358     -29.940 -35.011   3.949  1.00 23.22           C  
ANISOU 2374  CA  ASP A 358     3030   2828   2964    423    277    -26       C  
ATOM   2375  C   ASP A 358     -30.676 -35.888   2.921  1.00 23.64           C  
ANISOU 2375  C   ASP A 358     3067   2907   3009    428    268    -22       C  
ATOM   2376  O   ASP A 358     -31.275 -36.898   3.321  1.00 22.84           O  
ANISOU 2376  O   ASP A 358     2950   2818   2909    427    270    -34       O  
ATOM   2377  CB  ASP A 358     -30.869 -33.919   4.495  1.00 20.31           C  
ANISOU 2377  CB  ASP A 358     2659   2437   2621    444    278    -38       C  
ATOM   2378  CG  ASP A 358     -31.318 -32.911   3.441  1.00 22.82           C  
ANISOU 2378  CG  ASP A 358     2976   2731   2963    460    255    -11       C  
ATOM   2379  OD1 ASP A 358     -30.705 -32.814   2.349  1.00 21.70           O  
ANISOU 2379  OD1 ASP A 358     2845   2597   2803    444    239     23       O  
ATOM   2380  OD2 ASP A 358     -32.323 -32.192   3.739  1.00 24.34           O  
ANISOU 2380  OD2 ASP A 358     3152   2899   3198    486    249    -25       O  
ATOM   2381  N   HIS A 359     -30.579 -35.592   1.620  1.00 21.77           N  
ANISOU 2381  N   HIS A 359     2833   2683   2757    422    257     -3       N  
ATOM   2382  CA  HIS A 359     -31.185 -36.417   0.557  1.00 19.97           C  
ANISOU 2382  CA  HIS A 359     2590   2489   2509    416    249     -5       C  
ATOM   2383  C   HIS A 359     -30.633 -35.905  -0.777  1.00 21.25           C  
ANISOU 2383  C   HIS A 359     2760   2679   2636    388    241     17       C  
ATOM   2384  O   HIS A 359     -30.033 -34.829  -0.835  1.00 23.08           O  
ANISOU 2384  O   HIS A 359     3007   2895   2867    379    235     45       O  
ATOM   2385  CB  HIS A 359     -32.743 -36.275   0.544  1.00 19.13           C  
ANISOU 2385  CB  HIS A 359     2469   2380   2419    436    232      5       C  
ATOM   2386  CG  HIS A 359     -33.169 -34.834   0.499  1.00 20.53           C  
ANISOU 2386  CG  HIS A 359     2651   2528   2623    452    213     35       C  
ATOM   2387  ND1 HIS A 359     -32.983 -34.059  -0.632  1.00 23.10           N  
ANISOU 2387  ND1 HIS A 359     2985   2857   2936    434    184     79       N  
ATOM   2388  CD2 HIS A 359     -33.554 -33.977   1.483  1.00 17.88           C  
ANISOU 2388  CD2 HIS A 359     2310   2154   2332    477    217     24       C  
ATOM   2389  CE1 HIS A 359     -33.282 -32.797  -0.357  1.00 18.43           C  
ANISOU 2389  CE1 HIS A 359     2393   2216   2393    452    162    102       C  
ATOM   2390  NE2 HIS A 359     -33.684 -32.734   0.897  1.00 22.39           N  
ANISOU 2390  NE2 HIS A 359     2883   2691   2933    483    185     60       N  
ATOM   2391  N   GLY A 360     -30.908 -36.637  -1.857  1.00 20.73           N  
ANISOU 2391  N   GLY A 360     2682   2658   2536    369    237      6       N  
ATOM   2392  CA  GLY A 360     -30.509 -36.251  -3.212  1.00 20.24           C  
ANISOU 2392  CA  GLY A 360     2624   2646   2420    325    230     26       C  
ATOM   2393  C   GLY A 360     -31.562 -35.397  -3.911  1.00 21.81           C  
ANISOU 2393  C   GLY A 360     2828   2850   2608    316    187     88       C  
ATOM   2394  O   GLY A 360     -32.324 -34.677  -3.259  1.00 23.92           O  
ANISOU 2394  O   GLY A 360     3096   3066   2927    350    164    116       O  
ATOM   2395  N   MET A 361     -31.636 -35.541  -5.259  1.00 20.86           N  
ANISOU 2395  N   MET A 361     2705   2797   2423    266    173    103       N  
ATOM   2396  CA  MET A 361     -32.434 -34.691  -6.135  1.00 23.21           C  
ANISOU 2396  CA  MET A 361     3007   3110   2701    237    118    178       C  
ATOM   2397  C   MET A 361     -32.640 -35.419  -7.471  1.00 22.87           C  
ANISOU 2397  C   MET A 361     2955   3160   2574    177    114    167       C  
ATOM   2398  O   MET A 361     -31.662 -35.914  -8.076  1.00 22.66           O  
ANISOU 2398  O   MET A 361     2926   3200   2485    131    152    121       O  
ATOM   2399  CB  MET A 361     -31.753 -33.336  -6.411  1.00 21.39           C  
ANISOU 2399  CB  MET A 361     2794   2867   2464    204     91    249       C  
ATOM   2400  CG  MET A 361     -32.615 -32.352  -7.258  1.00 22.54           C  
ANISOU 2400  CG  MET A 361     2942   3011   2611    172     14    348       C  
ATOM   2401  SD  MET A 361     -34.090 -31.679  -6.323  1.00 23.82           S  
ANISOU 2401  SD  MET A 361     3085   3064   2903    255    -34    374       S  
ATOM   2402  CE  MET A 361     -33.222 -30.780  -5.002  1.00 25.19           C  
ANISOU 2402  CE  MET A 361     3272   3150   3150    298     -9    354       C  
ATOM   2403  N   GLU A 362     -33.877 -35.411  -7.958  1.00 21.25           N  
ANISOU 2403  N   GLU A 362     2742   2964   2368    173     67    205       N  
ATOM   2404  CA  GLU A 362     -34.276 -36.160  -9.156  1.00 23.16           C  
ANISOU 2404  CA  GLU A 362     2975   3296   2530    115     57    190       C  
ATOM   2405  C   GLU A 362     -34.846 -35.190 -10.179  1.00 25.59           C  
ANISOU 2405  C   GLU A 362     3289   3638   2797     56    -17    296       C  
ATOM   2406  O   GLU A 362     -35.319 -34.118  -9.809  1.00 25.12           O  
ANISOU 2406  O   GLU A 362     3230   3508   2805     85    -68    374       O  
ATOM   2407  CB  GLU A 362     -35.356 -37.214  -8.783  1.00 23.11           C  
ANISOU 2407  CB  GLU A 362     2948   3270   2562    158     58    142       C  
ATOM   2408  CG  GLU A 362     -35.927 -38.078  -9.937  1.00 24.58           C  
ANISOU 2408  CG  GLU A 362     3124   3541   2676    102     45    116       C  
ATOM   2409  CD  GLU A 362     -34.818 -38.823 -10.714  1.00 30.72           C  
ANISOU 2409  CD  GLU A 362     3899   4403   3370     43     97     33       C  
ATOM   2410  OE1 GLU A 362     -34.142 -38.221 -11.603  1.00 32.01           O  
ANISOU 2410  OE1 GLU A 362     4072   4639   3450    -29     96     62       O  
ATOM   2411  OE2 GLU A 362     -34.588 -40.017 -10.419  1.00 34.56           O  
ANISOU 2411  OE2 GLU A 362     4369   4881   3881     66    140    -66       O  
ATOM   2412  N   ASP A 363     -34.809 -35.576 -11.459  1.00 24.41           N  
ANISOU 2412  N   ASP A 363     3138   3596   2539    -29    -25    295       N  
ATOM   2413  CA  ASP A 363     -35.484 -34.828 -12.528  1.00 27.77           C  
ANISOU 2413  CA  ASP A 363     3567   4070   2914   -101   -108    405       C  
ATOM   2414  C   ASP A 363     -36.992 -35.003 -12.439  1.00 26.24           C  
ANISOU 2414  C   ASP A 363     3354   3837   2779    -63   -165    436       C  
ATOM   2415  O   ASP A 363     -37.506 -36.113 -12.631  1.00 25.92           O  
ANISOU 2415  O   ASP A 363     3300   3835   2713    -62   -144    367       O  
ATOM   2416  CB  ASP A 363     -35.021 -35.328 -13.898  1.00 33.60           C  
ANISOU 2416  CB  ASP A 363     4309   4956   3503   -216    -94    381       C  
ATOM   2417  CG  ASP A 363     -33.704 -34.792 -14.265  1.00 46.23           C  
ANISOU 2417  CG  ASP A 363     5921   6612   5033   -281    -63    392       C  
ATOM   2418  OD1 ASP A 363     -33.636 -33.618 -14.754  1.00 50.90           O  
ANISOU 2418  OD1 ASP A 363     6526   7214   5599   -342   -129    517       O  
ATOM   2419  OD2 ASP A 363     -32.724 -35.549 -14.052  1.00 52.76           O  
ANISOU 2419  OD2 ASP A 363     6739   7467   5839   -272     24    277       O  
ATOM   2420  N   VAL A 364     -37.715 -33.906 -12.210  1.00 24.56           N  
ANISOU 2420  N   VAL A 364     3134   3548   2651    -35   -241    538       N  
ATOM   2421  CA  VAL A 364     -39.166 -33.931 -12.087  1.00 27.44           C  
ANISOU 2421  CA  VAL A 364     3468   3869   3090      6   -299    571       C  
ATOM   2422  C   VAL A 364     -39.650 -32.648 -12.725  1.00 32.16           C  
ANISOU 2422  C   VAL A 364     4059   4443   3719    -34   -409    714       C  
ATOM   2423  O   VAL A 364     -39.207 -31.589 -12.290  1.00 35.62           O  
ANISOU 2423  O   VAL A 364     4503   4806   4225    -11   -430    763       O  
ATOM   2424  CB  VAL A 364     -39.625 -33.969 -10.599  1.00 28.46           C  
ANISOU 2424  CB  VAL A 364     3575   3886   3351    122   -264    517       C  
ATOM   2425  CG1 VAL A 364     -41.136 -34.099 -10.510  1.00 28.50           C  
ANISOU 2425  CG1 VAL A 364     3539   3861   3428    159   -315    538       C  
ATOM   2426  CG2 VAL A 364     -38.896 -35.080  -9.764  1.00 27.54           C  
ANISOU 2426  CG2 VAL A 364     3470   3775   3219    159   -163    393       C  
ATOM   2427  N   THR A 365     -40.571 -32.726 -13.717  1.00 32.37           N  
ANISOU 2427  N   THR A 365     4069   4523   3706    -93   -488    783       N  
ATOM   2428  CA  THR A 365     -41.145 -31.556 -14.399  1.00 35.23           C  
ANISOU 2428  CA  THR A 365     4419   4860   4108   -138   -614    937       C  
ATOM   2429  C   THR A 365     -42.667 -31.616 -14.429  1.00 35.76           C  
ANISOU 2429  C   THR A 365     4438   4886   4264   -101   -689    975       C  
ATOM   2430  O   THR A 365     -43.292 -32.656 -14.175  1.00 33.31           O  
ANISOU 2430  O   THR A 365     4110   4598   3949    -65   -645    891       O  
ATOM   2431  CB  THR A 365     -40.689 -31.400 -15.885  1.00 35.55           C  
ANISOU 2431  CB  THR A 365     4485   5033   3988   -289   -667   1025       C  
ATOM   2432  OG1 THR A 365     -41.227 -32.503 -16.567  1.00 37.34           O  
ANISOU 2432  OG1 THR A 365     4706   5365   4115   -338   -656    976       O  
ATOM   2433  CG2 THR A 365     -39.161 -31.503 -16.051  1.00 38.05           C  
ANISOU 2433  CG2 THR A 365     4842   5425   4190   -347   -584    975       C  
ATOM   2434  N   CYS A 366     -43.265 -30.484 -14.857  1.00 36.15           N  
ANISOU 2434  N   CYS A 366     4462   4879   4394   -121   -814   1115       N  
ATOM   2435  CA  CYS A 366     -44.718 -30.369 -14.968  1.00 41.45           C  
ANISOU 2435  CA  CYS A 366     5077   5504   5169    -89   -903   1170       C  
ATOM   2436  C   CYS A 366     -45.324 -31.386 -15.940  1.00 44.34           C  
ANISOU 2436  C   CYS A 366     5442   5996   5410   -167   -923   1169       C  
ATOM   2437  O   CYS A 366     -46.483 -31.795 -15.764  1.00 45.73           O  
ANISOU 2437  O   CYS A 366     5571   6147   5655   -121   -948   1154       O  
ATOM   2438  CB  CYS A 366     -45.092 -28.945 -15.424  1.00 48.88           C  
ANISOU 2438  CB  CYS A 366     5990   6364   6217   -114  -1051   1336       C  
ATOM   2439  SG  CYS A 366     -44.471 -27.632 -14.314  1.00 55.34           S  
ANISOU 2439  SG  CYS A 366     6802   7017   7209    -22  -1044   1337       S  
ATOM   2440  N   ASP A 367     -44.571 -31.815 -16.962  1.00 41.81           N  
ANISOU 2440  N   ASP A 367     5168   5813   4903   -289   -908   1178       N  
ATOM   2441  CA  ASP A 367     -45.101 -32.822 -17.887  1.00 43.18           C  
ANISOU 2441  CA  ASP A 367     5342   6114   4950   -370   -920   1158       C  
ATOM   2442  C   ASP A 367     -45.334 -34.190 -17.251  1.00 39.28           C  
ANISOU 2442  C   ASP A 367     4842   5632   4452   -303   -812    996       C  
ATOM   2443  O   ASP A 367     -45.891 -35.063 -17.923  1.00 40.61           O  
ANISOU 2443  O   ASP A 367     5004   5888   4536   -359   -823    969       O  
ATOM   2444  CB  ASP A 367     -44.151 -32.995 -19.057  1.00 50.28           C  
ANISOU 2444  CB  ASP A 367     6289   7170   5646   -519   -910   1176       C  
ATOM   2445  CG  ASP A 367     -44.011 -31.730 -19.832  1.00 59.02           C  
ANISOU 2445  CG  ASP A 367     7402   8286   6737   -613  -1033   1356       C  
ATOM   2446  OD1 ASP A 367     -44.916 -31.458 -20.659  1.00 63.31           O  
ANISOU 2446  OD1 ASP A 367     7924   8862   7269   -685  -1157   1479       O  
ATOM   2447  OD2 ASP A 367     -43.046 -30.985 -19.555  1.00 62.04           O  
ANISOU 2447  OD2 ASP A 367     7808   8631   7133   -613  -1013   1383       O  
ATOM   2448  N   ARG A 368     -44.919 -34.409 -16.003  1.00 31.82           N  
ANISOU 2448  N   ARG A 368     3898   4603   3590   -195   -715    893       N  
ATOM   2449  CA  ARG A 368     -45.064 -35.700 -15.352  1.00 31.15           C  
ANISOU 2449  CA  ARG A 368     3808   4523   3506   -139   -620    753       C  
ATOM   2450  C   ARG A 368     -45.813 -35.535 -14.031  1.00 30.97           C  
ANISOU 2450  C   ARG A 368     3741   4376   3650    -13   -604    725       C  
ATOM   2451  O   ARG A 368     -45.215 -35.782 -12.977  1.00 29.42           O  
ANISOU 2451  O   ARG A 368     3556   4131   3492     55   -515    638       O  
ATOM   2452  CB  ARG A 368     -43.603 -36.363 -15.123  1.00 29.32           C  
ANISOU 2452  CB  ARG A 368     3620   4335   3185   -150   -501    636       C  
ATOM   2453  CG  ARG A 368     -42.907 -36.622 -16.486  1.00 28.51           C  
ANISOU 2453  CG  ARG A 368     3549   4377   2907   -283   -505    639       C  
ATOM   2454  CD  ARG A 368     -41.631 -37.502 -16.344  1.00 30.16           C  
ANISOU 2454  CD  ARG A 368     3784   4636   3041   -291   -387    500       C  
ATOM   2455  NE  ARG A 368     -40.593 -36.841 -15.536  1.00 29.49           N  
ANISOU 2455  NE  ARG A 368     3715   4483   3008   -240   -339    497       N  
ATOM   2456  CZ  ARG A 368     -39.630 -36.109 -16.076  1.00 31.60           C  
ANISOU 2456  CZ  ARG A 368     4005   4800   3200   -310   -342    545       C  
ATOM   2457  NH1 ARG A 368     -39.609 -35.941 -17.411  1.00 27.27           N  
ANISOU 2457  NH1 ARG A 368     3466   4378   2519   -438   -391    604       N  
ATOM   2458  NH2 ARG A 368     -38.727 -35.532 -15.291  1.00 29.40           N  
ANISOU 2458  NH2 ARG A 368     3739   4454   2977   -260   -301    540       N  
ATOM   2459  N   THR A 369     -47.124 -35.259 -14.104  1.00 29.08           N  
ANISOU 2459  N   THR A 369     3450   4101   3499     10   -685    788       N  
ATOM   2460  CA  THR A 369     -48.022 -35.167 -12.965  1.00 30.11           C  
ANISOU 2460  CA  THR A 369     3524   4134   3782    117   -671    754       C  
ATOM   2461  C   THR A 369     -49.180 -36.116 -13.166  1.00 30.13           C  
ANISOU 2461  C   THR A 369     3488   4176   3783    111   -688    730       C  
ATOM   2462  O   THR A 369     -49.812 -36.076 -14.221  1.00 32.24           O  
ANISOU 2462  O   THR A 369     3742   4496   4012     43   -779    809       O  
ATOM   2463  CB  THR A 369     -48.614 -33.755 -12.817  1.00 33.79           C  
ANISOU 2463  CB  THR A 369     3941   4501   4395    160   -763    854       C  
ATOM   2464  OG1 THR A 369     -47.579 -32.792 -12.915  1.00 37.90           O  
ANISOU 2464  OG1 THR A 369     4500   4992   4908    141   -774    904       O  
ATOM   2465  CG2 THR A 369     -49.381 -33.619 -11.467  1.00 30.10           C  
ANISOU 2465  CG2 THR A 369     3411   3939   4088    276   -722    786       C  
ATOM   2466  N   GLU A 370     -49.491 -36.923 -12.154  1.00 28.48           N  
ANISOU 2466  N   GLU A 370     3259   3943   3619    174   -610    631       N  
ATOM   2467  CA  GLU A 370     -50.779 -37.599 -12.079  1.00 32.23           C  
ANISOU 2467  CA  GLU A 370     3680   4429   4138    188   -632    617       C  
ATOM   2468  C   GLU A 370     -51.738 -36.766 -11.239  1.00 30.94           C  
ANISOU 2468  C   GLU A 370     3439   4175   4142    274   -658    639       C  
ATOM   2469  O   GLU A 370     -51.337 -36.185 -10.220  1.00 32.04           O  
ANISOU 2469  O   GLU A 370     3572   4245   4356    341   -605    601       O  
ATOM   2470  CB  GLU A 370     -50.636 -38.977 -11.430  1.00 34.40           C  
ANISOU 2470  CB  GLU A 370     3969   4729   4373    200   -538    502       C  
ATOM   2471  CG  GLU A 370     -49.838 -39.930 -12.233  1.00 34.97           C  
ANISOU 2471  CG  GLU A 370     4099   4882   4305    123   -511    457       C  
ATOM   2472  CD  GLU A 370     -50.715 -40.887 -12.998  1.00 35.98           C  
ANISOU 2472  CD  GLU A 370     4209   5075   4387     66   -552    449       C  
ATOM   2473  OE1 GLU A 370     -51.972 -40.670 -13.054  1.00 33.81           O  
ANISOU 2473  OE1 GLU A 370     3876   4787   4183     80   -617    504       O  
ATOM   2474  OE2 GLU A 370     -50.125 -41.874 -13.502  1.00 36.44           O  
ANISOU 2474  OE2 GLU A 370     4306   5193   4344     11   -516    380       O  
ATOM   2475  N   PHE A 371     -53.008 -36.732 -11.632  1.00 29.61           N  
ANISOU 2475  N   PHE A 371     3206   4009   4037    271   -736    690       N  
ATOM   2476  CA  PHE A 371     -54.040 -36.036 -10.877  1.00 27.40           C  
ANISOU 2476  CA  PHE A 371     2835   3649   3927    353   -759    695       C  
ATOM   2477  C   PHE A 371     -55.001 -37.051 -10.284  1.00 31.67           C  
ANISOU 2477  C   PHE A 371     3325   4217   4493    375   -713    624       C  
ATOM   2478  O   PHE A 371     -55.584 -37.849 -11.034  1.00 32.51           O  
ANISOU 2478  O   PHE A 371     3427   4388   4539    318   -754    645       O  
ATOM   2479  CB  PHE A 371     -54.821 -35.073 -11.772  1.00 28.68           C  
ANISOU 2479  CB  PHE A 371     2944   3781   4174    337   -899    820       C  
ATOM   2480  CG  PHE A 371     -54.025 -33.899 -12.205  1.00 36.28           C  
ANISOU 2480  CG  PHE A 371     3940   4697   5149    321   -956    904       C  
ATOM   2481  CD1 PHE A 371     -53.929 -32.770 -11.376  1.00 34.15           C  
ANISOU 2481  CD1 PHE A 371     3630   4314   5030    404   -952    895       C  
ATOM   2482  CD2 PHE A 371     -53.352 -33.904 -13.427  1.00 35.03           C  
ANISOU 2482  CD2 PHE A 371     3850   4610   4850    216  -1013    987       C  
ATOM   2483  CE1 PHE A 371     -53.175 -31.659 -11.766  1.00 33.15           C  
ANISOU 2483  CE1 PHE A 371     3536   4136   4926    386  -1013    978       C  
ATOM   2484  CE2 PHE A 371     -52.566 -32.787 -13.812  1.00 36.06           C  
ANISOU 2484  CE2 PHE A 371     4012   4701   4988    191  -1069   1074       C  
ATOM   2485  CZ  PHE A 371     -52.489 -31.669 -12.979  1.00 34.07           C  
ANISOU 2485  CZ  PHE A 371     3722   4324   4898    277  -1073   1074       C  
ATOM   2486  N   LEU A 372     -55.238 -36.972  -8.973  1.00 31.23           N  
ANISOU 2486  N   LEU A 372     3224   4117   4526    450   -635    545       N  
ATOM   2487  CA  LEU A 372     -56.200 -37.896  -8.340  1.00 32.41           C  
ANISOU 2487  CA  LEU A 372     3316   4297   4700    464   -591    483       C  
ATOM   2488  C   LEU A 372     -57.641 -37.723  -8.841  1.00 34.62           C  
ANISOU 2488  C   LEU A 372     3501   4577   5074    467   -680    537       C  
ATOM   2489  O   LEU A 372     -58.425 -38.690  -8.791  1.00 33.47           O  
ANISOU 2489  O   LEU A 372     3324   4482   4911    444   -669    512       O  
ATOM   2490  CB  LEU A 372     -56.179 -37.742  -6.824  1.00 32.89           C  
ANISOU 2490  CB  LEU A 372     3342   4325   4831    531   -491    391       C  
ATOM   2491  CG  LEU A 372     -54.873 -38.072  -6.120  1.00 36.36           C  
ANISOU 2491  CG  LEU A 372     3863   4767   5184    527   -399    331       C  
ATOM   2492  CD1 LEU A 372     -55.088 -38.116  -4.612  1.00 37.03           C  
ANISOU 2492  CD1 LEU A 372     3903   4843   5322    574   -305    242       C  
ATOM   2493  CD2 LEU A 372     -54.226 -39.388  -6.616  1.00 36.00           C  
ANISOU 2493  CD2 LEU A 372     3898   4785   4997    458   -378    321       C  
ATOM   2494  N   SER A 373     -58.001 -36.528  -9.342  1.00 28.69           N  
ANISOU 2494  N   SER A 373     2703   3768   4429    490   -776    617       N  
ATOM   2495  CA  SER A 373     -59.298 -36.313  -9.939  1.00 33.33           C  
ANISOU 2495  CA  SER A 373     3200   4351   5113    488   -879    684       C  
ATOM   2496  C   SER A 373     -59.529 -37.183 -11.161  1.00 34.79           C  
ANISOU 2496  C   SER A 373     3424   4622   5174    392   -947    747       C  
ATOM   2497  O   SER A 373     -60.667 -37.270 -11.617  1.00 32.47           O  
ANISOU 2497  O   SER A 373     3056   4341   4941    380  -1026    795       O  
ATOM   2498  CB  SER A 373     -59.481 -34.828 -10.363  1.00 34.80           C  
ANISOU 2498  CB  SER A 373     3335   4445   5440    523   -989    776       C  
ATOM   2499  OG  SER A 373     -58.292 -34.364 -11.032  1.00 34.42           O  
ANISOU 2499  OG  SER A 373     3385   4394   5299    475  -1021    842       O  
ATOM   2500  N   ASN A 374     -58.483 -37.766 -11.748  1.00 33.34           N  
ANISOU 2500  N   ASN A 374     3348   4496   4823    321   -925    747       N  
ATOM   2501  CA  ASN A 374     -58.702 -38.676 -12.879  1.00 34.93           C  
ANISOU 2501  CA  ASN A 374     3585   4789   4899    224   -978    782       C  
ATOM   2502  C   ASN A 374     -59.085 -40.062 -12.407  1.00 32.28           C  
ANISOU 2502  C   ASN A 374     3245   4502   4518    213   -904    691       C  
ATOM   2503  O   ASN A 374     -59.408 -40.916 -13.229  1.00 33.00           O  
ANISOU 2503  O   ASN A 374     3353   4663   4521    138   -943    701       O  
ATOM   2504  CB  ASN A 374     -57.443 -38.789 -13.766  1.00 35.06           C  
ANISOU 2504  CB  ASN A 374     3708   4860   4752    143   -980    803       C  
ATOM   2505  CG  ASN A 374     -57.169 -37.520 -14.520  1.00 38.11           C  
ANISOU 2505  CG  ASN A 374     4100   5219   5159    120  -1081    923       C  
ATOM   2506  OD1 ASN A 374     -58.082 -36.772 -14.790  1.00 41.47           O  
ANISOU 2506  OD1 ASN A 374     4453   5604   5701    135  -1184   1011       O  
ATOM   2507  ND2 ASN A 374     -55.910 -37.250 -14.823  1.00 38.01           N  
ANISOU 2507  ND2 ASN A 374     4170   5226   5048     82  -1054    928       N  
ATOM   2508  N   TYR A 375     -59.044 -40.285 -11.118  1.00 29.21           N  
ANISOU 2508  N   TYR A 375     2834   4078   4184    279   -804    605       N  
ATOM   2509  CA  TYR A 375     -59.304 -41.556 -10.468  1.00 31.17           C  
ANISOU 2509  CA  TYR A 375     3081   4363   4400    269   -728    522       C  
ATOM   2510  C   TYR A 375     -60.478 -41.505  -9.506  1.00 33.51           C  
ANISOU 2510  C   TYR A 375     3269   4639   4823    325   -704    494       C  
ATOM   2511  O   TYR A 375     -61.197 -42.497  -9.363  1.00 31.63           O  
ANISOU 2511  O   TYR A 375     3000   4442   4574    295   -693    467       O  
ATOM   2512  CB  TYR A 375     -58.075 -41.980  -9.681  1.00 29.66           C  
ANISOU 2512  CB  TYR A 375     2965   4161   4143    282   -621    445       C  
ATOM   2513  CG  TYR A 375     -56.853 -42.232 -10.539  1.00 29.88           C  
ANISOU 2513  CG  TYR A 375     3093   4218   4042    225   -624    447       C  
ATOM   2514  CD1 TYR A 375     -56.035 -41.183 -10.933  1.00 28.96           C  
ANISOU 2514  CD1 TYR A 375     3015   4079   3912    231   -647    493       C  
ATOM   2515  CD2 TYR A 375     -56.499 -43.524 -10.924  1.00 31.34           C  
ANISOU 2515  CD2 TYR A 375     3329   4453   4126    163   -601    397       C  
ATOM   2516  CE1 TYR A 375     -54.942 -41.389 -11.686  1.00 30.28           C  
ANISOU 2516  CE1 TYR A 375     3262   4283   3959    174   -643    490       C  
ATOM   2517  CE2 TYR A 375     -55.363 -43.758 -11.660  1.00 31.55           C  
ANISOU 2517  CE2 TYR A 375     3436   4510   4042    114   -592    378       C  
ATOM   2518  CZ  TYR A 375     -54.590 -42.673 -12.058  1.00 33.61           C  
ANISOU 2518  CZ  TYR A 375     3729   4760   4280    117   -611    426       C  
ATOM   2519  OH  TYR A 375     -53.460 -42.835 -12.834  1.00 34.30           O  
ANISOU 2519  OH  TYR A 375     3888   4892   4252     60   -599    408       O  
ATOM   2520  N   LEU A 376     -60.648 -40.384  -8.802  1.00 33.69           N  
ANISOU 2520  N   LEU A 376     3231   4600   4968    401   -691    489       N  
ATOM   2521  CA  LEU A 376     -61.571 -40.248  -7.681  1.00 34.65           C  
ANISOU 2521  CA  LEU A 376     3249   4709   5209    459   -639    432       C  
ATOM   2522  C   LEU A 376     -62.619 -39.226  -8.062  1.00 36.29           C  
ANISOU 2522  C   LEU A 376     3347   4873   5568    501   -731    488       C  
ATOM   2523  O   LEU A 376     -62.270 -38.165  -8.579  1.00 35.71           O  
ANISOU 2523  O   LEU A 376     3282   4742   5545    523   -798    548       O  
ATOM   2524  CB  LEU A 376     -60.843 -39.756  -6.410  1.00 32.69           C  
ANISOU 2524  CB  LEU A 376     3011   4423   4986    516   -534    354       C  
ATOM   2525  CG  LEU A 376     -59.808 -40.704  -5.819  1.00 32.78           C  
ANISOU 2525  CG  LEU A 376     3117   4467   4870    482   -443    298       C  
ATOM   2526  CD1 LEU A 376     -59.177 -40.083  -4.543  1.00 31.20           C  
ANISOU 2526  CD1 LEU A 376     2917   4234   4703    535   -350    228       C  
ATOM   2527  CD2 LEU A 376     -60.511 -42.045  -5.551  1.00 34.09           C  
ANISOU 2527  CD2 LEU A 376     3260   4697   4997    433   -416    272       C  
ATOM   2528  N   THR A 377     -63.885 -39.517  -7.796  1.00 36.15           N  
ANISOU 2528  N   THR A 377     3222   4879   5634    511   -739    472       N  
ATOM   2529  CA  THR A 377     -64.868 -38.504  -8.156  1.00 42.22           C  
ANISOU 2529  CA  THR A 377     3876   5596   6570    558   -834    524       C  
ATOM   2530  C   THR A 377     -65.022 -37.380  -7.122  1.00 45.57           C  
ANISOU 2530  C   THR A 377     4210   5947   7156    655   -783    454       C  
ATOM   2531  O   THR A 377     -65.543 -36.336  -7.489  1.00 49.78           O  
ANISOU 2531  O   THR A 377     4662   6409   7844    703   -873    502       O  
ATOM   2532  CB  THR A 377     -66.234 -39.144  -8.462  1.00 43.99           C  
ANISOU 2532  CB  THR A 377     4005   5869   6838    530   -883    544       C  
ATOM   2533  OG1 THR A 377     -66.498 -40.151  -7.498  1.00 47.40           O  
ANISOU 2533  OG1 THR A 377     4421   6363   7223    515   -772    454       O  
ATOM   2534  CG2 THR A 377     -66.232 -39.820  -9.867  1.00 41.44           C  
ANISOU 2534  CG2 THR A 377     3752   5597   6397    436   -987    641       C  
ATOM   2535  N   ASN A 378     -64.539 -37.493  -5.872  1.00 48.43           N  
ANISOU 2535  N   ASN A 378     4585   6320   7496    684   -651    345       N  
ATOM   2536  CA  ASN A 378     -64.721 -36.387  -4.912  1.00 53.57           C  
ANISOU 2536  CA  ASN A 378     5144   6907   8302    772   -602    264       C  
ATOM   2537  C   ASN A 378     -63.412 -36.013  -4.225  1.00 48.10           C  
ANISOU 2537  C   ASN A 378     4542   6186   7546    790   -520    210       C  
ATOM   2538  O   ASN A 378     -63.254 -36.238  -3.035  1.00 49.78           O  
ANISOU 2538  O   ASN A 378     4744   6435   7735    801   -401    104       O  
ATOM   2539  CB  ASN A 378     -65.784 -36.711  -3.862  1.00 62.94           C  
ANISOU 2539  CB  ASN A 378     6205   8147   9563    794   -516    159       C  
ATOM   2540  CG  ASN A 378     -67.185 -36.664  -4.417  1.00 70.35           C  
ANISOU 2540  CG  ASN A 378     7014   9087  10630    804   -603    199       C  
ATOM   2541  OD1 ASN A 378     -67.663 -37.667  -4.957  1.00 73.59           O  
ANISOU 2541  OD1 ASN A 378     7437   9564  10960    739   -637    250       O  
ATOM   2542  ND2 ASN A 378     -67.868 -35.510  -4.283  1.00 72.34           N  
ANISOU 2542  ND2 ASN A 378     7134   9260  11093    886   -643    173       N  
ATOM   2543  N   VAL A 379     -62.505 -35.354  -4.942  1.00 44.27           N  
ANISOU 2543  N   VAL A 379     4139   5639   7043    790   -586    283       N  
ATOM   2544  CA  VAL A 379     -61.240 -35.001  -4.320  1.00 43.17           C  
ANISOU 2544  CA  VAL A 379     4085   5473   6843    803   -512    235       C  
ATOM   2545  C   VAL A 379     -61.384 -33.834  -3.363  1.00 43.66           C  
ANISOU 2545  C   VAL A 379     4060   5462   7065    888   -469    145       C  
ATOM   2546  O   VAL A 379     -60.439 -33.542  -2.607  1.00 42.26           O  
ANISOU 2546  O   VAL A 379     3938   5270   6848    902   -391     82       O  
ATOM   2547  CB  VAL A 379     -60.113 -34.676  -5.340  1.00 42.92           C  
ANISOU 2547  CB  VAL A 379     4171   5407   6730    768   -586    336       C  
ATOM   2548  CG1 VAL A 379     -59.662 -35.925  -5.986  1.00 39.85           C  
ANISOU 2548  CG1 VAL A 379     3882   5103   6158    684   -583    377       C  
ATOM   2549  CG2 VAL A 379     -60.565 -33.668  -6.414  1.00 42.77           C  
ANISOU 2549  CG2 VAL A 379     4104   5312   6833    783   -733    448       C  
ATOM   2550  N   ASP A 380     -62.533 -33.165  -3.367  1.00 44.09           N  
ANISOU 2550  N   ASP A 380     3976   5469   7306    944   -518    130       N  
ATOM   2551  CA  ASP A 380     -62.758 -32.102  -2.400  1.00 48.24           C  
ANISOU 2551  CA  ASP A 380     4402   5927   8000   1027   -468     17       C  
ATOM   2552  C   ASP A 380     -62.991 -32.615  -0.984  1.00 49.66           C  
ANISOU 2552  C   ASP A 380     4537   6194   8139   1028   -312   -135       C  
ATOM   2553  O   ASP A 380     -62.792 -31.868  -0.020  1.00 51.98           O  
ANISOU 2553  O   ASP A 380     4786   6454   8509   1078   -238   -251       O  
ATOM   2554  CB  ASP A 380     -63.944 -31.258  -2.843  1.00 52.05           C  
ANISOU 2554  CB  ASP A 380     4735   6327   8713   1089   -570     39       C  
ATOM   2555  CG  ASP A 380     -63.578 -30.318  -3.970  1.00 58.22           C  
ANISOU 2555  CG  ASP A 380     5548   6994   9578   1100   -724    175       C  
ATOM   2556  OD1 ASP A 380     -62.356 -30.162  -4.269  1.00 57.88           O  
ANISOU 2556  OD1 ASP A 380     5635   6932   9424   1068   -733    230       O  
ATOM   2557  OD2 ASP A 380     -64.522 -29.708  -4.540  1.00 63.34           O  
ANISOU 2557  OD2 ASP A 380     6085   7571  10412   1138   -839    230       O  
ATOM   2558  N   ASP A 381     -63.422 -33.852  -0.832  1.00 48.86           N  
ANISOU 2558  N   ASP A 381     4442   6204   7920    968   -265   -138       N  
ATOM   2559  CA  ASP A 381     -63.650 -34.442   0.478  1.00 48.18           C  
ANISOU 2559  CA  ASP A 381     4317   6216   7773    946   -125   -262       C  
ATOM   2560  C   ASP A 381     -62.391 -35.043   1.094  1.00 44.02           C  
ANISOU 2560  C   ASP A 381     3925   5739   7060    892    -41   -280       C  
ATOM   2561  O   ASP A 381     -62.477 -35.645   2.165  1.00 44.42           O  
ANISOU 2561  O   ASP A 381     3961   5882   7034    854     67   -362       O  
ATOM   2562  CB  ASP A 381     -64.729 -35.522   0.387  1.00 51.57           C  
ANISOU 2562  CB  ASP A 381     4686   6741   8169    897   -121   -248       C  
ATOM   2563  CG  ASP A 381     -66.103 -34.967  -0.076  1.00 56.68           C  
ANISOU 2563  CG  ASP A 381     5173   7349   9012    950   -195   -245       C  
ATOM   2564  OD1 ASP A 381     -66.417 -33.761   0.160  1.00 58.77           O  
ANISOU 2564  OD1 ASP A 381     5337   7531   9464   1033   -207   -309       O  
ATOM   2565  OD2 ASP A 381     -66.866 -35.765  -0.686  1.00 56.94           O  
ANISOU 2565  OD2 ASP A 381     5182   7432   9021    908   -247   -178       O  
ATOM   2566  N   ILE A 382     -61.223 -34.905   0.462  1.00 41.40           N  
ANISOU 2566  N   ILE A 382     3721   5354   6653    881    -90   -201       N  
ATOM   2567  CA  ILE A 382     -60.006 -35.421   1.071  1.00 41.41           C  
ANISOU 2567  CA  ILE A 382     3841   5395   6498    836    -14   -221       C  
ATOM   2568  C   ILE A 382     -58.957 -34.315   1.100  1.00 40.91           C  
ANISOU 2568  C   ILE A 382     3831   5241   6470    879    -24   -228       C  
ATOM   2569  O   ILE A 382     -58.988 -33.375   0.308  1.00 40.29           O  
ANISOU 2569  O   ILE A 382     3736   5070   6504    925   -115   -175       O  
ATOM   2570  CB  ILE A 382     -59.451 -36.663   0.339  1.00 41.18           C  
ANISOU 2570  CB  ILE A 382     3927   5410   6308    762    -47   -126       C  
ATOM   2571  CG1 ILE A 382     -59.012 -36.306  -1.082  1.00 43.62           C  
ANISOU 2571  CG1 ILE A 382     4300   5653   6622    765   -162    -14       C  
ATOM   2572  CG2 ILE A 382     -60.437 -37.816   0.323  1.00 39.58           C  
ANISOU 2572  CG2 ILE A 382     3679   5292   6069    712    -40   -116       C  
ATOM   2573  CD1 ILE A 382     -58.170 -37.387  -1.718  1.00 45.00           C  
ANISOU 2573  CD1 ILE A 382     4596   5866   6635    696   -176     50       C  
ATOM   2574  N   THR A 383     -58.022 -34.456   2.030  1.00 40.34           N  
ANISOU 2574  N   THR A 383     3824   5200   6302    857     63   -287       N  
ATOM   2575  CA  THR A 383     -56.786 -33.678   2.091  1.00 39.55           C  
ANISOU 2575  CA  THR A 383     3803   5032   6192    876     62   -285       C  
ATOM   2576  C   THR A 383     -55.650 -34.560   1.583  1.00 36.98           C  
ANISOU 2576  C   THR A 383     3617   4733   5702    815     48   -202       C  
ATOM   2577  O   THR A 383     -55.538 -35.712   1.999  1.00 36.25           O  
ANISOU 2577  O   THR A 383     3560   4722   5492    758     98   -208       O  
ATOM   2578  CB  THR A 383     -56.505 -33.246   3.538  1.00 42.39           C  
ANISOU 2578  CB  THR A 383     4136   5416   6555    888    172   -418       C  
ATOM   2579  OG1 THR A 383     -57.586 -32.440   4.011  1.00 46.30           O  
ANISOU 2579  OG1 THR A 383     4490   5891   7212    945    193   -517       O  
ATOM   2580  CG2 THR A 383     -55.222 -32.455   3.630  1.00 43.88           C  
ANISOU 2580  CG2 THR A 383     4406   5534   6733    904    169   -417       C  
ATOM   2581  N   LEU A 384     -54.811 -34.017   0.704  1.00 35.70           N  
ANISOU 2581  N   LEU A 384     3526   4502   5538    824    -21   -126       N  
ATOM   2582  CA  LEU A 384     -53.680 -34.733   0.131  1.00 34.79           C  
ANISOU 2582  CA  LEU A 384     3531   4406   5280    770    -35    -58       C  
ATOM   2583  C   LEU A 384     -52.404 -33.951   0.422  1.00 35.04           C  
ANISOU 2583  C   LEU A 384     3629   4385   5298    784    -17    -70       C  
ATOM   2584  O   LEU A 384     -52.329 -32.765   0.095  1.00 37.20           O  
ANISOU 2584  O   LEU A 384     3882   4578   5675    826    -67    -52       O  
ATOM   2585  CB  LEU A 384     -53.860 -34.901  -1.404  1.00 32.11           C  
ANISOU 2585  CB  LEU A 384     3216   4054   4929    748   -141     54       C  
ATOM   2586  CG  LEU A 384     -52.632 -35.397  -2.176  1.00 29.66           C  
ANISOU 2586  CG  LEU A 384     3022   3758   4489    696   -161    116       C  
ATOM   2587  CD1 LEU A 384     -52.438 -36.904  -1.904  1.00 27.19           C  
ANISOU 2587  CD1 LEU A 384     2752   3524   4055    643   -108     93       C  
ATOM   2588  CD2 LEU A 384     -52.669 -35.133  -3.731  1.00 31.00           C  
ANISOU 2588  CD2 LEU A 384     3215   3912   4653    670   -271    224       C  
ATOM   2589  N   VAL A 385     -51.408 -34.600   1.019  1.00 31.54           N  
ANISOU 2589  N   VAL A 385     3262   3984   4739    746     46    -93       N  
ATOM   2590  CA  VAL A 385     -50.047 -34.071   0.939  1.00 32.12           C  
ANISOU 2590  CA  VAL A 385     3416   4015   4775    743     44    -74       C  
ATOM   2591  C   VAL A 385     -49.532 -34.584  -0.401  1.00 31.74           C  
ANISOU 2591  C   VAL A 385     3436   3974   4651    704    -21     22       C  
ATOM   2592  O   VAL A 385     -49.436 -35.822  -0.591  1.00 30.46           O  
ANISOU 2592  O   VAL A 385     3308   3872   4393    658     -6     34       O  
ATOM   2593  CB  VAL A 385     -49.141 -34.519   2.107  1.00 30.38           C  
ANISOU 2593  CB  VAL A 385     3243   3833   4467    716    130   -134       C  
ATOM   2594  CG1 VAL A 385     -47.706 -34.039   1.890  1.00 33.37           C  
ANISOU 2594  CG1 VAL A 385     3704   4169   4805    710    121   -106       C  
ATOM   2595  CG2 VAL A 385     -49.686 -34.056   3.467  1.00 29.91           C  
ANISOU 2595  CG2 VAL A 385     3113   3790   4462    739    203   -240       C  
ATOM   2596  N   PRO A 386     -49.168 -33.680  -1.339  1.00 31.39           N  
ANISOU 2596  N   PRO A 386     3412   3872   4644    713    -93     89       N  
ATOM   2597  CA  PRO A 386     -48.899 -34.098  -2.726  1.00 29.85           C  
ANISOU 2597  CA  PRO A 386     3265   3700   4375    665   -161    179       C  
ATOM   2598  C   PRO A 386     -47.427 -34.186  -3.098  1.00 31.30           C  
ANISOU 2598  C   PRO A 386     3540   3892   4459    626   -150    204       C  
ATOM   2599  O   PRO A 386     -46.539 -34.137  -2.232  1.00 31.64           O  
ANISOU 2599  O   PRO A 386     3617   3927   4477    634    -88    154       O  
ATOM   2600  CB  PRO A 386     -49.591 -32.984  -3.526  1.00 31.65           C  
ANISOU 2600  CB  PRO A 386     3442   3866   4716    689   -258    249       C  
ATOM   2601  CG  PRO A 386     -49.329 -31.720  -2.691  1.00 32.21           C  
ANISOU 2601  CG  PRO A 386     3487   3853   4900    746   -242    205       C  
ATOM   2602  CD  PRO A 386     -49.296 -32.202  -1.224  1.00 32.52           C  
ANISOU 2602  CD  PRO A 386     3512   3925   4920    765   -129     87       C  
ATOM   2603  N   GLY A 387     -47.144 -34.323  -4.399  1.00 30.30           N  
ANISOU 2603  N   GLY A 387     3452   3792   4271    578   -211    280       N  
ATOM   2604  CA  GLY A 387     -45.786 -34.228  -4.892  1.00 27.39           C  
ANISOU 2604  CA  GLY A 387     3157   3434   3818    538   -207    306       C  
ATOM   2605  C   GLY A 387     -45.140 -35.575  -5.119  1.00 28.38           C  
ANISOU 2605  C   GLY A 387     3330   3631   3823    491   -161    273       C  
ATOM   2606  O   GLY A 387     -45.687 -36.407  -5.842  1.00 28.28           O  
ANISOU 2606  O   GLY A 387     3311   3669   3765    457   -185    285       O  
ATOM   2607  N   THR A 388     -43.988 -35.817  -4.481  1.00 24.13           N  
ANISOU 2607  N   THR A 388     2834   3091   3241    490    -99    227       N  
ATOM   2608  CA  THR A 388     -43.216 -37.033  -4.661  1.00 23.36           C  
ANISOU 2608  CA  THR A 388     2777   3044   3053    452    -59    191       C  
ATOM   2609  C   THR A 388     -43.641 -38.150  -3.717  1.00 25.26           C  
ANISOU 2609  C   THR A 388     2999   3296   3301    464    -13    131       C  
ATOM   2610  O   THR A 388     -43.012 -39.213  -3.727  1.00 24.74           O  
ANISOU 2610  O   THR A 388     2960   3256   3184    438     16     97       O  
ATOM   2611  CB  THR A 388     -41.725 -36.747  -4.424  1.00 25.76           C  
ANISOU 2611  CB  THR A 388     3129   3336   3321    443    -23    176       C  
ATOM   2612  OG1 THR A 388     -41.613 -36.127  -3.141  1.00 23.63           O  
ANISOU 2612  OG1 THR A 388     2850   3016   3114    489     11    148       O  
ATOM   2613  CG2 THR A 388     -41.155 -35.746  -5.525  1.00 25.70           C  
ANISOU 2613  CG2 THR A 388     3146   3333   3286    409    -72    245       C  
ATOM   2614  N   LEU A 389     -44.605 -37.895  -2.848  1.00 25.43           N  
ANISOU 2614  N   LEU A 389     2973   3298   3391    501     -3    116       N  
ATOM   2615  CA  LEU A 389     -45.287 -38.931  -2.077  1.00 27.70           C  
ANISOU 2615  CA  LEU A 389     3233   3610   3683    499     29     77       C  
ATOM   2616  C   LEU A 389     -46.740 -38.478  -1.982  1.00 29.66           C  
ANISOU 2616  C   LEU A 389     3411   3854   4003    526      4     86       C  
ATOM   2617  O   LEU A 389     -47.057 -37.317  -2.260  1.00 32.52           O  
ANISOU 2617  O   LEU A 389     3748   4180   4427    556    -30    113       O  
ATOM   2618  CB  LEU A 389     -44.633 -39.147  -0.662  1.00 31.01           C  
ANISOU 2618  CB  LEU A 389     3664   4020   4097    506     92     30       C  
ATOM   2619  CG  LEU A 389     -44.382 -37.911   0.246  1.00 36.65           C  
ANISOU 2619  CG  LEU A 389     4369   4698   4857    542    119      9       C  
ATOM   2620  CD1 LEU A 389     -45.601 -37.177   0.442  1.00 39.16           C  
ANISOU 2620  CD1 LEU A 389     4622   5004   5251    576    108      1       C  
ATOM   2621  CD2 LEU A 389     -43.960 -38.297   1.652  1.00 39.56           C  
ANISOU 2621  CD2 LEU A 389     4744   5080   5207    532    177    -35       C  
ATOM   2622  N   GLY A 390     -47.622 -39.370  -1.555  1.00 27.62           N  
ANISOU 2622  N   GLY A 390     3116   3629   3749    515     19     64       N  
ATOM   2623  CA  GLY A 390     -48.984 -38.966  -1.306  1.00 27.32           C  
ANISOU 2623  CA  GLY A 390     3000   3593   3787    542      7     60       C  
ATOM   2624  C   GLY A 390     -49.400 -39.463   0.071  1.00 27.16           C  
ANISOU 2624  C   GLY A 390     2945   3602   3774    539     71      5       C  
ATOM   2625  O   GLY A 390     -49.132 -40.617   0.414  1.00 26.25           O  
ANISOU 2625  O   GLY A 390     2856   3518   3601    498     93     -3       O  
ATOM   2626  N   ARG A 391     -49.992 -38.600   0.883  1.00 25.12           N  
ANISOU 2626  N   ARG A 391     2626   3334   3584    576    100    -35       N  
ATOM   2627  CA  ARG A 391     -50.625 -39.008   2.129  1.00 27.60           C  
ANISOU 2627  CA  ARG A 391     2890   3698   3900    562    162    -90       C  
ATOM   2628  C   ARG A 391     -52.054 -38.482   2.069  1.00 29.47           C  
ANISOU 2628  C   ARG A 391     3027   3940   4231    595    149   -110       C  
ATOM   2629  O   ARG A 391     -52.257 -37.294   1.793  1.00 29.00           O  
ANISOU 2629  O   ARG A 391     2931   3827   4260    648    124   -117       O  
ATOM   2630  CB  ARG A 391     -49.837 -38.431   3.351  1.00 30.31           C  
ANISOU 2630  CB  ARG A 391     3250   4038   4230    567    226   -146       C  
ATOM   2631  CG  ARG A 391     -48.352 -38.726   3.227  1.00 33.35           C  
ANISOU 2631  CG  ARG A 391     3728   4401   4543    545    223   -118       C  
ATOM   2632  CD  ARG A 391     -47.626 -38.896   4.544  1.00 37.51           C  
ANISOU 2632  CD  ARG A 391     4278   4955   5019    515    283   -156       C  
ATOM   2633  NE  ARG A 391     -47.927 -37.849   5.521  1.00 38.61           N  
ANISOU 2633  NE  ARG A 391     4369   5100   5200    539    332   -227       N  
ATOM   2634  CZ  ARG A 391     -47.246 -36.712   5.609  1.00 40.38           C  
ANISOU 2634  CZ  ARG A 391     4612   5272   5458    576    337   -252       C  
ATOM   2635  NH1 ARG A 391     -46.230 -36.509   4.796  1.00 41.31           N  
ANISOU 2635  NH1 ARG A 391     4796   5338   5564    587    296   -202       N  
ATOM   2636  NH2 ARG A 391     -47.568 -35.803   6.534  1.00 41.54           N  
ANISOU 2636  NH2 ARG A 391     4708   5425   5650    596    385   -333       N  
ATOM   2637  N   ILE A 392     -53.063 -39.350   2.242  1.00 27.91           N  
ANISOU 2637  N   ILE A 392     2778   3800   4027    564    157   -113       N  
ATOM   2638  CA  ILE A 392     -54.457 -38.917   2.085  1.00 29.46           C  
ANISOU 2638  CA  ILE A 392     2870   4003   4321    596    140   -130       C  
ATOM   2639  C   ILE A 392     -55.178 -39.071   3.419  1.00 30.03           C  
ANISOU 2639  C   ILE A 392     2865   4144   4401    578    221   -208       C  
ATOM   2640  O   ILE A 392     -54.979 -40.082   4.108  1.00 29.07           O  
ANISOU 2640  O   ILE A 392     2771   4084   4190    515    262   -210       O  
ATOM   2641  CB  ILE A 392     -55.178 -39.730   0.989  1.00 29.83           C  
ANISOU 2641  CB  ILE A 392     2908   4065   4360    570     71    -65       C  
ATOM   2642  CG1 ILE A 392     -54.554 -39.439  -0.407  1.00 28.13           C  
ANISOU 2642  CG1 ILE A 392     2758   3798   4134    578    -10      7       C  
ATOM   2643  CG2 ILE A 392     -56.734 -39.528   1.058  1.00 29.77           C  
ANISOU 2643  CG2 ILE A 392     2778   4083   4449    590     63    -87       C  
ATOM   2644  CD1 ILE A 392     -54.932 -40.490  -1.444  1.00 25.98           C  
ANISOU 2644  CD1 ILE A 392     2505   3555   3812    531    -68     61       C  
ATOM   2645  N   ARG A 393     -56.013 -38.085   3.782  1.00 29.39           N  
ANISOU 2645  N   ARG A 393     2684   4054   4429    629    242   -273       N  
ATOM   2646  CA  ARG A 393     -56.934 -38.241   4.908  1.00 32.14           C  
ANISOU 2646  CA  ARG A 393     2936   4485   4789    607    320   -356       C  
ATOM   2647  C   ARG A 393     -58.203 -37.434   4.634  1.00 34.85           C  
ANISOU 2647  C   ARG A 393     3152   4807   5283    669    300   -398       C  
ATOM   2648  O   ARG A 393     -58.216 -36.576   3.745  1.00 36.33           O  
ANISOU 2648  O   ARG A 393     3331   4903   5571    732    227   -366       O  
ATOM   2649  CB  ARG A 393     -56.268 -37.777   6.222  1.00 33.27           C  
ANISOU 2649  CB  ARG A 393     3090   4660   4893    595    409   -444       C  
ATOM   2650  CG  ARG A 393     -55.854 -36.312   6.216  1.00 35.20           C  
ANISOU 2650  CG  ARG A 393     3322   4817   5236    672    406   -498       C  
ATOM   2651  CD  ARG A 393     -55.159 -35.881   7.519  1.00 39.38           C  
ANISOU 2651  CD  ARG A 393     3865   5383   5716    652    495   -591       C  
ATOM   2652  NE  ARG A 393     -54.652 -34.511   7.399  1.00 43.48           N  
ANISOU 2652  NE  ARG A 393     4385   5803   6334    724    480   -634       N  
ATOM   2653  CZ  ARG A 393     -55.310 -33.410   7.768  1.00 51.54           C  
ANISOU 2653  CZ  ARG A 393     5301   6792   7491    784    506   -741       C  
ATOM   2654  NH1 ARG A 393     -56.545 -33.445   8.319  1.00 52.97           N  
ANISOU 2654  NH1 ARG A 393     5357   7041   7727    784    560   -831       N  
ATOM   2655  NH2 ARG A 393     -54.711 -32.244   7.588  1.00 55.55           N  
ANISOU 2655  NH2 ARG A 393     5823   7194   8087    844    478   -764       N  
ATOM   2656  N   PRO A 394     -59.284 -37.665   5.388  1.00 35.48           N  
ANISOU 2656  N   PRO A 394     3124   4969   5389    649    360   -469       N  
ATOM   2657  CA  PRO A 394     -60.519 -36.906   5.121  1.00 38.14           C  
ANISOU 2657  CA  PRO A 394     3324   5280   5886    712    339   -515       C  
ATOM   2658  C   PRO A 394     -60.357 -35.420   5.422  1.00 40.59           C  
ANISOU 2658  C   PRO A 394     3582   5511   6329    795    355   -604       C  
ATOM   2659  O   PRO A 394     -59.550 -35.017   6.268  1.00 43.01           O  
ANISOU 2659  O   PRO A 394     3928   5824   6591    790    421   -672       O  
ATOM   2660  CB  PRO A 394     -61.556 -37.557   6.051  1.00 38.73           C  
ANISOU 2660  CB  PRO A 394     3298   5481   5936    658    422   -586       C  
ATOM   2661  CG  PRO A 394     -60.754 -38.107   7.192  1.00 38.47           C  
ANISOU 2661  CG  PRO A 394     3334   5532   5752    581    509   -618       C  
ATOM   2662  CD  PRO A 394     -59.475 -38.638   6.472  1.00 36.47           C  
ANISOU 2662  CD  PRO A 394     3238   5215   5401    562    442   -502       C  
ATOM   2663  N   LYS A 395     -61.099 -34.589   4.677  1.00 39.40           N  
ANISOU 2663  N   LYS A 395     3344   5276   6348    870    282   -597       N  
ATOM   2664  CA  LYS A 395     -61.025 -33.144   4.914  1.00 45.37           C  
ANISOU 2664  CA  LYS A 395     4038   5937   7263    954    282   -682       C  
ATOM   2665  C   LYS A 395     -61.457 -32.781   6.338  1.00 48.42           C  
ANISOU 2665  C   LYS A 395     4320   6395   7682    957    411   -859       C  
ATOM   2666  O   LYS A 395     -60.903 -31.858   6.943  1.00 49.74           O  
ANISOU 2666  O   LYS A 395     4485   6518   7898    992    453   -952       O  
ATOM   2667  CB  LYS A 395     -61.891 -32.376   3.897  1.00 50.76           C  
ANISOU 2667  CB  LYS A 395     4627   6515   8145   1029    170   -637       C  
ATOM   2668  CG  LYS A 395     -61.603 -30.859   3.852  1.00 52.84           C  
ANISOU 2668  CG  LYS A 395     4851   6640   8586   1117    130   -684       C  
ATOM   2669  CD  LYS A 395     -60.261 -30.620   3.121  1.00 55.55           C  
ANISOU 2669  CD  LYS A 395     5347   6905   8854   1106     58   -568       C  
ATOM   2670  CE  LYS A 395     -59.448 -29.384   3.617  1.00 57.33           C  
ANISOU 2670  CE  LYS A 395     5584   7033   9164   1157     75   -642       C  
ATOM   2671  NZ  LYS A 395     -60.176 -28.073   3.480  1.00 60.26           N  
ANISOU 2671  NZ  LYS A 395     5821   7277   9797   1251     15   -697       N  
ATOM   2672  N   ILE A 396     -62.447 -33.475   6.885  1.00 50.05           N  
ANISOU 2672  N   ILE A 396     4435   6719   7862    914    476   -914       N  
ATOM   2673  CA  ILE A 396     -62.895 -33.249   8.259  1.00 53.91           C  
ANISOU 2673  CA  ILE A 396     4821   7309   8354    895    610  -1087       C  
ATOM   2674  C   ILE A 396     -62.291 -34.349   9.127  1.00 55.81           C  
ANISOU 2674  C   ILE A 396     5154   7688   8364    778    693  -1075       C  
ATOM   2675  O   ILE A 396     -62.631 -35.524   8.934  1.00 55.67           O  
ANISOU 2675  O   ILE A 396     5160   7748   8244    708    680   -990       O  
ATOM   2676  CB  ILE A 396     -64.435 -33.219   8.383  1.00 54.67           C  
ANISOU 2676  CB  ILE A 396     4737   7457   8579    916    635  -1167       C  
ATOM   2677  N   PRO A 397     -61.417 -34.021  10.081  1.00 58.79           N  
ANISOU 2677  N   PRO A 397     5580   8095   8660    751    769  -1153       N  
ATOM   2678  CA  PRO A 397     -60.690 -35.061  10.831  1.00 59.83           C  
ANISOU 2678  CA  PRO A 397     5815   8343   8575    635    824  -1113       C  
ATOM   2679  C   PRO A 397     -61.627 -36.019  11.560  1.00 62.94           C  
ANISOU 2679  C   PRO A 397     6131   8902   8881    540    898  -1144       C  
ATOM   2680  O   PRO A 397     -62.577 -35.602  12.223  1.00 63.25           O  
ANISOU 2680  O   PRO A 397     6028   9016   8987    544    978  -1282       O  
ATOM   2681  CB  PRO A 397     -59.838 -34.256  11.817  1.00 60.05           C  
ANISOU 2681  CB  PRO A 397     5867   8377   8571    633    898  -1227       C  
ATOM   2682  CG  PRO A 397     -59.706 -32.901  11.197  1.00 60.05           C  
ANISOU 2682  CG  PRO A 397     5838   8218   8761    755    844  -1268       C  
ATOM   2683  CD  PRO A 397     -60.990 -32.661  10.448  1.00 59.78           C  
ANISOU 2683  CD  PRO A 397     5677   8137   8899    824    793  -1270       C  
ATOM   2684  N   ASN A 398     -61.327 -37.321  11.436  1.00 64.50           N  
ANISOU 2684  N   ASN A 398     6421   9155   8930    451    869  -1016       N  
ATOM   2685  CA  ASN A 398     -62.151 -38.413  11.973  1.00 66.42           C  
ANISOU 2685  CA  ASN A 398     6611   9545   9081    346    914  -1003       C  
ATOM   2686  C   ASN A 398     -63.549 -38.453  11.346  1.00 68.32           C  
ANISOU 2686  C   ASN A 398     6724   9786   9449    386    888  -1011       C  
ATOM   2687  O   ASN A 398     -64.486 -38.974  11.952  1.00 69.75           O  
ANISOU 2687  O   ASN A 398     6808  10098   9595    316    951  -1054       O  
ATOM   2688  CB  ASN A 398     -62.246 -38.351  13.506  1.00 67.58           C  
ANISOU 2688  CB  ASN A 398     6700   9849   9127    255   1044  -1128       C  
ATOM   2689  N   ASN A 399     -63.706 -37.920  10.128  1.00 68.20           N  
ANISOU 2689  N   ASN A 399     6705   9632   9578    491    791   -962       N  
ATOM   2690  CA  ASN A 399     -65.000 -37.958   9.437  1.00 67.45           C  
ANISOU 2690  CA  ASN A 399     6492   9527   9610    530    747   -953       C  
ATOM   2691  C   ASN A 399     -65.468 -39.402   9.285  1.00 65.97           C  
ANISOU 2691  C   ASN A 399     6325   9428   9313    431    727   -851       C  
ATOM   2692  O   ASN A 399     -64.794 -40.219   8.647  1.00 64.24           O  
ANISOU 2692  O   ASN A 399     6235   9168   9005    398    653   -720       O  
ATOM   2693  CB  ASN A 399     -64.884 -37.280   8.063  1.00 67.03           C  
ANISOU 2693  CB  ASN A 399     6463   9307   9698    638    623   -879       C  
ATOM   2694  CG  ASN A 399     -66.224 -37.139   7.330  1.00 68.48           C  
ANISOU 2694  CG  ASN A 399     6513   9467  10038    688    565   -871       C  
ATOM   2695  OD1 ASN A 399     -67.184 -37.908   7.528  1.00 69.01           O  
ANISOU 2695  OD1 ASN A 399     6502   9636  10081    630    592   -873       O  
ATOM   2696  ND2 ASN A 399     -66.283 -36.148   6.458  1.00 68.89           N  
ANISOU 2696  ND2 ASN A 399     6538   9383  10253    789    477   -853       N  
ATOM   2697  N   LEU A 400     -66.650 -39.697   9.840  1.00 65.87           N  
ANISOU 2697  N   LEU A 400     6177   9534   9317    386    790   -917       N  
ATOM   2698  CA  LEU A 400     -67.179 -41.056   9.833  1.00 63.85           C  
ANISOU 2698  CA  LEU A 400     5927   9372   8961    280    778   -829       C  
ATOM   2699  C   LEU A 400     -67.490 -41.572   8.424  1.00 61.78           C  
ANISOU 2699  C   LEU A 400     5700   9019   8755    312    649   -698       C  
ATOM   2700  O   LEU A 400     -67.432 -42.786   8.210  1.00 61.40           O  
ANISOU 2700  O   LEU A 400     5720   9005   8604    228    610   -594       O  
ATOM   2701  CB  LEU A 400     -68.431 -41.126  10.730  1.00 65.02           C  
ANISOU 2701  CB  LEU A 400     5905   9673   9126    225    879   -939       C  
ATOM   2702  N   LYS A 401     -67.818 -40.699   7.451  1.00 61.74           N  
ANISOU 2702  N   LYS A 401     5648   8899   8911    423    575   -698       N  
ATOM   2703  CA  LYS A 401     -68.112 -41.153   6.079  1.00 62.38           C  
ANISOU 2703  CA  LYS A 401     5764   8905   9034    443    448   -573       C  
ATOM   2704  C   LYS A 401     -66.851 -41.341   5.202  1.00 62.18           C  
ANISOU 2704  C   LYS A 401     5912   8774   8939    455    362   -464       C  
ATOM   2705  O   LYS A 401     -66.965 -41.584   3.985  1.00 61.83           O  
ANISOU 2705  O   LYS A 401     5905   8664   8924    473    255   -368       O  
ATOM   2706  CB  LYS A 401     -69.080 -40.188   5.378  1.00 63.65           C  
ANISOU 2706  CB  LYS A 401     5792   8996   9397    543    392   -604       C  
ATOM   2707  N   TYR A 402     -65.656 -41.219   5.772  1.00 60.64           N  
ANISOU 2707  N   TYR A 402     5819   8569   8651    442    407   -480       N  
ATOM   2708  CA  TYR A 402     -64.434 -41.484   5.008  1.00 58.44           C  
ANISOU 2708  CA  TYR A 402     5699   8205   8300    445    336   -385       C  
ATOM   2709  C   TYR A 402     -64.319 -42.985   4.759  1.00 57.84           C  
ANISOU 2709  C   TYR A 402     5700   8171   8107    352    303   -293       C  
ATOM   2710  O   TYR A 402     -64.364 -43.772   5.711  1.00 57.80           O  
ANISOU 2710  O   TYR A 402     5693   8257   8011    266    365   -305       O  
ATOM   2711  CB  TYR A 402     -63.244 -40.971   5.795  1.00 56.11           C  
ANISOU 2711  CB  TYR A 402     5478   7896   7945    452    398   -434       C  
ATOM   2712  CG  TYR A 402     -61.890 -41.258   5.222  1.00 56.16           C  
ANISOU 2712  CG  TYR A 402     5639   7831   7870    448    345   -352       C  
ATOM   2713  CD1 TYR A 402     -61.562 -40.854   3.927  1.00 54.11           C  
ANISOU 2713  CD1 TYR A 402     5429   7468   7661    505    250   -286       C  
ATOM   2714  CD2 TYR A 402     -60.906 -41.888   5.993  1.00 55.64           C  
ANISOU 2714  CD2 TYR A 402     5664   7802   7674    381    390   -343       C  
ATOM   2715  CE1 TYR A 402     -60.317 -41.067   3.413  1.00 51.13           C  
ANISOU 2715  CE1 TYR A 402     5183   7036   7210    499    211   -225       C  
ATOM   2716  CE2 TYR A 402     -59.614 -42.108   5.473  1.00 52.85           C  
ANISOU 2716  CE2 TYR A 402     5443   7378   7259    383    345   -279       C  
ATOM   2717  CZ  TYR A 402     -59.349 -41.685   4.178  1.00 51.08           C  
ANISOU 2717  CZ  TYR A 402     5260   7060   7088    443    261   -227       C  
ATOM   2718  OH  TYR A 402     -58.114 -41.904   3.632  1.00 48.35           O  
ANISOU 2718  OH  TYR A 402     5033   6656   6680    441    223   -174       O  
ATOM   2719  N   ASP A 403     -64.179 -43.393   3.491  1.00 56.80           N  
ANISOU 2719  N   ASP A 403     5632   7973   7977    360    202   -202       N  
ATOM   2720  CA  ASP A 403     -64.180 -44.811   3.106  1.00 54.65           C  
ANISOU 2720  CA  ASP A 403     5420   7725   7619    278    159   -124       C  
ATOM   2721  C   ASP A 403     -62.902 -45.165   2.345  1.00 51.82           C  
ANISOU 2721  C   ASP A 403     5206   7291   7191    277    103    -63       C  
ATOM   2722  O   ASP A 403     -62.892 -45.198   1.101  1.00 51.51           O  
ANISOU 2722  O   ASP A 403     5201   7198   7172    298     18    -11       O  
ATOM   2723  CB  ASP A 403     -65.422 -45.142   2.278  1.00 54.60           C  
ANISOU 2723  CB  ASP A 403     5334   7733   7680    272     93    -88       C  
ATOM   2724  CG  ASP A 403     -65.510 -46.625   1.908  1.00 56.89           C  
ANISOU 2724  CG  ASP A 403     5678   8046   7892    183     48    -18       C  
ATOM   2725  OD1 ASP A 403     -64.642 -47.408   2.337  1.00 57.16           O  
ANISOU 2725  OD1 ASP A 403     5803   8083   7832    128     67      1       O  
ATOM   2726  OD2 ASP A 403     -66.455 -47.021   1.192  1.00 59.42           O  
ANISOU 2726  OD2 ASP A 403     5945   8378   8254    167    -12     17       O  
ATOM   2727  N   PRO A 404     -61.808 -45.463   3.051  1.00 48.77           N  
ANISOU 2727  N   PRO A 404     4904   6905   6720    246    147    -69       N  
ATOM   2728  CA  PRO A 404     -60.541 -45.700   2.340  1.00 45.27           C  
ANISOU 2728  CA  PRO A 404     4587   6389   6226    254    101    -26       C  
ATOM   2729  C   PRO A 404     -60.554 -46.958   1.484  1.00 43.51           C  
ANISOU 2729  C   PRO A 404     4415   6152   5964    200     32     35       C  
ATOM   2730  O   PRO A 404     -59.750 -47.053   0.546  1.00 42.39           O  
ANISOU 2730  O   PRO A 404     4356   5952   5799    215    -19     62       O  
ATOM   2731  CB  PRO A 404     -59.497 -45.770   3.463  1.00 46.12           C  
ANISOU 2731  CB  PRO A 404     4752   6510   6263    227    166    -50       C  
ATOM   2732  CG  PRO A 404     -60.305 -46.030   4.740  1.00 48.18           C  
ANISOU 2732  CG  PRO A 404     4928   6870   6508    170    238    -87       C  
ATOM   2733  CD  PRO A 404     -61.662 -45.448   4.520  1.00 48.87           C  
ANISOU 2733  CD  PRO A 404     4893   6989   6687    206    242   -122       C  
ATOM   2734  N   LYS A 405     -61.474 -47.900   1.723  1.00 41.11           N  
ANISOU 2734  N   LYS A 405     4059   5903   5656    135     26     52       N  
ATOM   2735  CA  LYS A 405     -61.556 -49.055   0.836  1.00 40.55           C  
ANISOU 2735  CA  LYS A 405     4031   5812   5565     87    -46    101       C  
ATOM   2736  C   LYS A 405     -62.049 -48.658  -0.555  1.00 37.51           C  
ANISOU 2736  C   LYS A 405     3630   5397   5223    126   -120    120       C  
ATOM   2737  O   LYS A 405     -61.556 -49.174  -1.568  1.00 35.77           O  
ANISOU 2737  O   LYS A 405     3482   5137   4972    112   -179    144       O  
ATOM   2738  CB  LYS A 405     -62.459 -50.135   1.443  1.00 44.76           C  
ANISOU 2738  CB  LYS A 405     4509   6408   6090      2    -39    120       C  
ATOM   2739  CG  LYS A 405     -61.961 -50.649   2.778  1.00 48.06           C  
ANISOU 2739  CG  LYS A 405     4947   6862   6453    -59     19    121       C  
ATOM   2740  N   ALA A 406     -63.034 -47.760  -0.644  1.00 35.11           N  
ANISOU 2740  N   ALA A 406     3230   5115   4995    171   -122    108       N  
ATOM   2741  CA  ALA A 406     -63.497 -47.387  -1.974  1.00 35.03           C  
ANISOU 2741  CA  ALA A 406     3205   5078   5027    198   -207    143       C  
ATOM   2742  C   ALA A 406     -62.439 -46.546  -2.669  1.00 35.32           C  
ANISOU 2742  C   ALA A 406     3319   5052   5048    249   -233    152       C  
ATOM   2743  O   ALA A 406     -62.217 -46.673  -3.883  1.00 34.60           O  
ANISOU 2743  O   ALA A 406     3278   4939   4931    238   -306    190       O  
ATOM   2744  CB  ALA A 406     -64.840 -46.642  -1.889  1.00 32.68           C  
ANISOU 2744  CB  ALA A 406     2773   4811   4835    234   -214    133       C  
ATOM   2745  N   ILE A 407     -61.734 -45.727  -1.890  1.00 35.28           N  
ANISOU 2745  N   ILE A 407     3328   5026   5050    295   -171    116       N  
ATOM   2746  CA  ILE A 407     -60.672 -44.900  -2.440  1.00 33.37           C  
ANISOU 2746  CA  ILE A 407     3159   4726   4794    339   -190    126       C  
ATOM   2747  C   ILE A 407     -59.538 -45.776  -2.980  1.00 33.26           C  
ANISOU 2747  C   ILE A 407     3261   4695   4682    295   -206    142       C  
ATOM   2748  O   ILE A 407     -59.117 -45.633  -4.131  1.00 32.77           O  
ANISOU 2748  O   ILE A 407     3250   4611   4592    293   -265    173       O  
ATOM   2749  CB  ILE A 407     -60.186 -43.914  -1.362  1.00 31.59           C  
ANISOU 2749  CB  ILE A 407     2919   4484   4599    390   -115     75       C  
ATOM   2750  CG1 ILE A 407     -61.340 -42.953  -1.031  1.00 36.75           C  
ANISOU 2750  CG1 ILE A 407     3447   5145   5373    442   -108     46       C  
ATOM   2751  CG2 ILE A 407     -58.900 -43.217  -1.822  1.00 29.87           C  
ANISOU 2751  CG2 ILE A 407     2791   4206   4352    423   -129     89       C  
ATOM   2752  CD1 ILE A 407     -60.889 -41.670  -0.315  1.00 39.31           C  
ANISOU 2752  CD1 ILE A 407     3751   5431   5754    508    -58     -8       C  
ATOM   2753  N   ILE A 408     -59.070 -46.746  -2.183  1.00 32.12           N  
ANISOU 2753  N   ILE A 408     3154   4564   4488    252   -158    120       N  
ATOM   2754  CA  ILE A 408     -57.916 -47.483  -2.640  1.00 32.26           C  
ANISOU 2754  CA  ILE A 408     3270   4552   4436    223   -171    122       C  
ATOM   2755  C   ILE A 408     -58.259 -48.331  -3.877  1.00 31.83           C  
ANISOU 2755  C   ILE A 408     3233   4503   4358    178   -243    142       C  
ATOM   2756  O   ILE A 408     -57.440 -48.427  -4.816  1.00 30.66           O  
ANISOU 2756  O   ILE A 408     3153   4334   4163    171   -273    140       O  
ATOM   2757  CB  ILE A 408     -57.266 -48.289  -1.496  1.00 35.87           C  
ANISOU 2757  CB  ILE A 408     3760   5008   4860    189   -117    103       C  
ATOM   2758  CG1 ILE A 408     -56.043 -49.030  -2.046  1.00 38.55           C  
ANISOU 2758  CG1 ILE A 408     4192   5304   5151    167   -137     97       C  
ATOM   2759  CG2 ILE A 408     -58.168 -49.263  -0.953  1.00 39.09           C  
ANISOU 2759  CG2 ILE A 408     4118   5455   5278    132   -116    113       C  
ATOM   2760  CD1 ILE A 408     -54.835 -49.005  -1.050  1.00 38.99           C  
ANISOU 2760  CD1 ILE A 408     4297   5334   5184    173    -85     81       C  
ATOM   2761  N   ALA A 409     -59.477 -48.888  -3.942  1.00 31.77           N  
ANISOU 2761  N   ALA A 409     3160   4530   4380    144   -271    157       N  
ATOM   2762  CA  ALA A 409     -59.906 -49.618  -5.138  1.00 33.23           C  
ANISOU 2762  CA  ALA A 409     3354   4725   4545     98   -344    173       C  
ATOM   2763  C   ALA A 409     -59.904 -48.732  -6.380  1.00 35.75           C  
ANISOU 2763  C   ALA A 409     3683   5045   4855    120   -403    200       C  
ATOM   2764  O   ALA A 409     -59.532 -49.173  -7.485  1.00 35.18           O  
ANISOU 2764  O   ALA A 409     3663   4978   4726     82   -450    198       O  
ATOM   2765  CB  ALA A 409     -61.316 -50.191  -4.927  1.00 32.88           C  
ANISOU 2765  CB  ALA A 409     3225   4723   4545     62   -365    190       C  
ATOM   2766  N   ASN A 410     -60.355 -47.486  -6.240  1.00 33.70           N  
ANISOU 2766  N   ASN A 410     3368   4784   4654    175   -406    225       N  
ATOM   2767  CA  ASN A 410     -60.307 -46.636  -7.422  1.00 31.26           C  
ANISOU 2767  CA  ASN A 410     3069   4470   4338    186   -476    269       C  
ATOM   2768  C   ASN A 410     -58.894 -46.205  -7.798  1.00 29.93           C  
ANISOU 2768  C   ASN A 410     2992   4275   4105    195   -462    262       C  
ATOM   2769  O   ASN A 410     -58.698 -45.697  -8.909  1.00 30.78           O  
ANISOU 2769  O   ASN A 410     3124   4391   4178    179   -524    302       O  
ATOM   2770  CB  ASN A 410     -61.175 -45.398  -7.225  1.00 32.92           C  
ANISOU 2770  CB  ASN A 410     3188   4669   4652    244   -499    302       C  
ATOM   2771  CG  ASN A 410     -62.600 -45.606  -7.735  1.00 38.70           C  
ANISOU 2771  CG  ASN A 410     3833   5434   5438    220   -568    340       C  
ATOM   2772  OD1 ASN A 410     -63.114 -46.734  -7.713  1.00 36.19           O  
ANISOU 2772  OD1 ASN A 410     3504   5151   5094    168   -569    326       O  
ATOM   2773  ND2 ASN A 410     -63.234 -44.544  -8.194  1.00 45.47           N  
ANISOU 2773  ND2 ASN A 410     4625   6274   6376    256   -633    390       N  
ATOM   2774  N   LEU A 411     -57.914 -46.387  -6.922  1.00 27.15           N  
ANISOU 2774  N   LEU A 411     2687   3898   3732    213   -388    218       N  
ATOM   2775  CA  LEU A 411     -56.543 -45.972  -7.205  1.00 27.62           C  
ANISOU 2775  CA  LEU A 411     2825   3933   3736    223   -369    208       C  
ATOM   2776  C   LEU A 411     -55.622 -47.146  -7.557  1.00 28.48           C  
ANISOU 2776  C   LEU A 411     3006   4046   3768    174   -354    162       C  
ATOM   2777  O   LEU A 411     -54.410 -46.942  -7.752  1.00 28.73           O  
ANISOU 2777  O   LEU A 411     3100   4062   3752    178   -330    142       O  
ATOM   2778  CB  LEU A 411     -55.956 -45.228  -5.991  1.00 24.94           C  
ANISOU 2778  CB  LEU A 411     2486   3557   3434    280   -299    187       C  
ATOM   2779  CG  LEU A 411     -56.564 -43.888  -5.515  1.00 26.77           C  
ANISOU 2779  CG  LEU A 411     2648   3768   3754    342   -299    207       C  
ATOM   2780  CD1 LEU A 411     -55.924 -43.537  -4.165  1.00 28.13           C  
ANISOU 2780  CD1 LEU A 411     2828   3916   3943    380   -215    161       C  
ATOM   2781  CD2 LEU A 411     -56.192 -42.847  -6.555  1.00 26.85           C  
ANISOU 2781  CD2 LEU A 411     2683   3757   3762    354   -360    258       C  
ATOM   2782  N   THR A 412     -56.160 -48.348  -7.658  1.00 28.56           N  
ANISOU 2782  N   THR A 412     3005   4073   3774    127   -369    141       N  
ATOM   2783  CA  THR A 412     -55.369 -49.556  -7.834  1.00 29.09           C  
ANISOU 2783  CA  THR A 412     3126   4126   3799     86   -356     86       C  
ATOM   2784  C   THR A 412     -55.415 -49.973  -9.308  1.00 30.92           C  
ANISOU 2784  C   THR A 412     3381   4397   3969     30   -412     70       C  
ATOM   2785  O   THR A 412     -56.487 -50.276  -9.825  1.00 33.00           O  
ANISOU 2785  O   THR A 412     3606   4694   4240     -4   -465     92       O  
ATOM   2786  CB  THR A 412     -55.918 -50.657  -6.919  1.00 30.55           C  
ANISOU 2786  CB  THR A 412     3280   4297   4029     64   -341     72       C  
ATOM   2787  OG1 THR A 412     -55.624 -50.351  -5.548  1.00 30.83           O  
ANISOU 2787  OG1 THR A 412     3307   4309   4098    100   -282     78       O  
ATOM   2788  CG2 THR A 412     -55.330 -52.017  -7.248  1.00 29.35           C  
ANISOU 2788  CG2 THR A 412     3171   4120   3861     17   -350     17       C  
ATOM   2789  N   CYS A 413     -54.252 -49.991  -9.970  1.00 31.46           N  
ANISOU 2789  N   CYS A 413     3510   4469   3974     15   -399     29       N  
ATOM   2790  CA  CYS A 413     -54.084 -50.503 -11.328  1.00 36.25           C  
ANISOU 2790  CA  CYS A 413     4144   5123   4505    -50   -437    -11       C  
ATOM   2791  C   CYS A 413     -55.184 -50.000 -12.265  1.00 36.57           C  
ANISOU 2791  C   CYS A 413     4152   5225   4520    -85   -512     52       C  
ATOM   2792  O   CYS A 413     -55.815 -50.778 -12.972  1.00 36.86           O  
ANISOU 2792  O   CYS A 413     4176   5297   4532   -144   -556     31       O  
ATOM   2793  CB  CYS A 413     -54.038 -52.044 -11.348  1.00 39.01           C  
ANISOU 2793  CB  CYS A 413     4501   5452   4871    -90   -434    -92       C  
ATOM   2794  SG  CYS A 413     -52.792 -52.728 -10.166  1.00 40.18           S  
ANISOU 2794  SG  CYS A 413     4677   5513   5076    -51   -365   -151       S  
ATOM   2795  N   LYS A 414     -55.430 -48.690 -12.273  1.00 34.16           N  
ANISOU 2795  N   LYS A 414     3827   4926   4227    -52   -534    133       N  
ATOM   2796  CA  LYS A 414     -56.510 -48.227 -13.139  1.00 35.88           C  
ANISOU 2796  CA  LYS A 414     4005   5193   4436    -87   -620    204       C  
ATOM   2797  C   LYS A 414     -56.049 -47.727 -14.494  1.00 39.44           C  
ANISOU 2797  C   LYS A 414     4494   5710   4781   -150   -668    230       C  
ATOM   2798  O   LYS A 414     -56.862 -47.681 -15.426  1.00 41.69           O  
ANISOU 2798  O   LYS A 414     4756   6051   5032   -208   -749    278       O  
ATOM   2799  CB  LYS A 414     -57.309 -47.150 -12.435  1.00 36.68           C  
ANISOU 2799  CB  LYS A 414     4042   5260   4636    -20   -637    282       C  
ATOM   2800  CG  LYS A 414     -58.102 -47.774 -11.298  1.00 40.54           C  
ANISOU 2800  CG  LYS A 414     4476   5717   5211     12   -602    259       C  
ATOM   2801  CD  LYS A 414     -59.233 -48.659 -11.806  1.00 44.14           C  
ANISOU 2801  CD  LYS A 414     4891   6211   5668    -43   -658    263       C  
ATOM   2802  CE  LYS A 414     -60.048 -49.085 -10.634  1.00 47.68           C  
ANISOU 2802  CE  LYS A 414     5276   6636   6205    -14   -624    255       C  
ATOM   2803  NZ  LYS A 414     -61.090 -49.973 -11.104  1.00 51.12           N  
ANISOU 2803  NZ  LYS A 414     5673   7106   6644    -71   -677    258       N  
ATOM   2804  N   LYS A 415     -54.783 -47.384 -14.652  1.00 38.63           N  
ANISOU 2804  N   LYS A 415     4448   5611   4620   -150   -625    203       N  
ATOM   2805  CA  LYS A 415     -54.291 -46.855 -15.911  1.00 42.72           C  
ANISOU 2805  CA  LYS A 415     5001   6205   5025   -222   -667    232       C  
ATOM   2806  C   LYS A 415     -53.043 -47.623 -16.308  1.00 43.77           C  
ANISOU 2806  C   LYS A 415     5191   6371   5067   -264   -602    119       C  
ATOM   2807  O   LYS A 415     -52.264 -48.015 -15.445  1.00 42.21           O  
ANISOU 2807  O   LYS A 415     5011   6114   4913   -211   -526     51       O  
ATOM   2808  CB  LYS A 415     -53.965 -45.361 -15.803  1.00 45.39           C  
ANISOU 2808  CB  LYS A 415     5342   6521   5385   -186   -687    329       C  
ATOM   2809  CG  LYS A 415     -55.179 -44.527 -15.442  1.00 49.97           C  
ANISOU 2809  CG  LYS A 415     5854   7058   6076   -139   -755    431       C  
ATOM   2810  CD  LYS A 415     -54.921 -43.042 -15.655  1.00 54.51           C  
ANISOU 2810  CD  LYS A 415     6427   7613   6671   -124   -803    534       C  
ATOM   2811  CE  LYS A 415     -56.202 -42.282 -15.974  1.00 56.43           C  
ANISOU 2811  CE  LYS A 415     6600   7844   6997   -120   -913    648       C  
ATOM   2812  NZ  LYS A 415     -57.379 -42.730 -15.164  1.00 57.72           N  
ANISOU 2812  NZ  LYS A 415     6689   7966   7276    -62   -907    625       N  
ATOM   2813  N   PRO A 416     -52.815 -47.833 -17.601  1.00 47.47           N  
ANISOU 2813  N   PRO A 416     5686   6940   5412   -363   -632     95       N  
ATOM   2814  CA  PRO A 416     -51.794 -48.832 -18.000  1.00 49.86           C  
ANISOU 2814  CA  PRO A 416     6025   7277   5643   -407   -566    -47       C  
ATOM   2815  C   PRO A 416     -50.380 -48.554 -17.490  1.00 49.66           C  
ANISOU 2815  C   PRO A 416     6032   7216   5620   -362   -483    -95       C  
ATOM   2816  O   PRO A 416     -49.692 -49.481 -17.055  1.00 52.45           O  
ANISOU 2816  O   PRO A 416     6394   7527   6008   -337   -418   -209       O  
ATOM   2817  CB  PRO A 416     -51.862 -48.802 -19.541  1.00 51.47           C  
ANISOU 2817  CB  PRO A 416     6244   7617   5696   -532   -617    -49       C  
ATOM   2818  CG  PRO A 416     -53.157 -48.136 -19.877  1.00 52.10           C  
ANISOU 2818  CG  PRO A 416     6290   7719   5787   -555   -723     90       C  
ATOM   2819  CD  PRO A 416     -53.457 -47.188 -18.756  1.00 50.59           C  
ANISOU 2819  CD  PRO A 416     6073   7424   5727   -446   -728    191       C  
ATOM   2820  N   ASP A 417     -49.888 -47.336 -17.545  1.00 46.61           N  
ANISOU 2820  N   ASP A 417     5663   6842   5206   -353   -489    -12       N  
ATOM   2821  CA  ASP A 417     -48.541 -47.111 -17.025  1.00 45.91           C  
ANISOU 2821  CA  ASP A 417     5602   6718   5124   -312   -411    -60       C  
ATOM   2822  C   ASP A 417     -48.568 -46.243 -15.762  1.00 41.21           C  
ANISOU 2822  C   ASP A 417     4997   6020   4640   -210   -399     19       C  
ATOM   2823  O   ASP A 417     -47.664 -45.447 -15.518  1.00 43.08           O  
ANISOU 2823  O   ASP A 417     5256   6242   4870   -187   -369     42       O  
ATOM   2824  CB  ASP A 417     -47.640 -46.505 -18.100  1.00 49.26           C  
ANISOU 2824  CB  ASP A 417     6058   7245   5413   -395   -407    -56       C  
ATOM   2825  N   GLN A 418     -49.586 -46.445 -14.934  1.00 33.94           N  
ANISOU 2825  N   GLN A 418     4040   5033   3821   -153   -419     48       N  
ATOM   2826  CA  GLN A 418     -49.894 -45.591 -13.794  1.00 29.92           C  
ANISOU 2826  CA  GLN A 418     3508   4443   3416    -67   -415    119       C  
ATOM   2827  C   GLN A 418     -48.654 -45.280 -12.970  1.00 28.74           C  
ANISOU 2827  C   GLN A 418     3388   4242   3289    -15   -342     87       C  
ATOM   2828  O   GLN A 418     -47.895 -46.195 -12.645  1.00 29.87           O  
ANISOU 2828  O   GLN A 418     3549   4368   3432    -10   -285     -5       O  
ATOM   2829  CB  GLN A 418     -50.916 -46.333 -12.942  1.00 31.73           C  
ANISOU 2829  CB  GLN A 418     3695   4624   3737    -27   -415    105       C  
ATOM   2830  CG  GLN A 418     -51.492 -45.566 -11.834  1.00 32.20           C  
ANISOU 2830  CG  GLN A 418     3716   4619   3899     49   -412    163       C  
ATOM   2831  CD  GLN A 418     -52.583 -46.362 -11.100  1.00 29.53           C  
ANISOU 2831  CD  GLN A 418     3329   4257   3634     69   -412    148       C  
ATOM   2832  OE1 GLN A 418     -53.516 -46.861 -11.717  1.00 30.02           O  
ANISOU 2832  OE1 GLN A 418     3364   4355   3687     27   -463    159       O  
ATOM   2833  NE2 GLN A 418     -52.467 -46.446  -9.786  1.00 27.63           N  
ANISOU 2833  NE2 GLN A 418     3076   3961   3462    124   -357    129       N  
ATOM   2834  N   HIS A 419     -48.422 -44.000 -12.618  1.00 25.65           N  
ANISOU 2834  N   HIS A 419     2999   3819   2927     23   -350    160       N  
ATOM   2835  CA  HIS A 419     -47.096 -43.636 -12.078  1.00 24.32           C  
ANISOU 2835  CA  HIS A 419     2866   3619   2757     54   -287    131       C  
ATOM   2836  C   HIS A 419     -47.083 -43.440 -10.553  1.00 25.16           C  
ANISOU 2836  C   HIS A 419     2957   3638   2965    139   -243    126       C  
ATOM   2837  O   HIS A 419     -46.264 -42.675 -10.018  1.00 23.84           O  
ANISOU 2837  O   HIS A 419     2809   3435   2815    173   -212    137       O  
ATOM   2838  CB  HIS A 419     -46.556 -42.408 -12.792  1.00 24.51           C  
ANISOU 2838  CB  HIS A 419     2912   3675   2727     22   -318    204       C  
ATOM   2839  CG  HIS A 419     -46.467 -42.605 -14.274  1.00 26.01           C  
ANISOU 2839  CG  HIS A 419     3118   3970   2793    -80   -357    208       C  
ATOM   2840  ND1 HIS A 419     -45.455 -43.335 -14.862  1.00 26.68           N  
ANISOU 2840  ND1 HIS A 419     3232   4119   2787   -135   -305    114       N  
ATOM   2841  CD2 HIS A 419     -47.314 -42.248 -15.277  1.00 26.88           C  
ANISOU 2841  CD2 HIS A 419     3214   4140   2857   -144   -442    287       C  
ATOM   2842  CE1 HIS A 419     -45.623 -43.333 -16.182  1.00 28.10           C  
ANISOU 2842  CE1 HIS A 419     3419   4405   2854   -234   -350    132       C  
ATOM   2843  NE2 HIS A 419     -46.763 -42.709 -16.455  1.00 28.62           N  
ANISOU 2843  NE2 HIS A 419     3462   4470   2942   -244   -438    243       N  
ATOM   2844  N   PHE A 420     -47.956 -44.149  -9.835  1.00 24.13           N  
ANISOU 2844  N   PHE A 420     2793   3480   2897    166   -238    106       N  
ATOM   2845  CA  PHE A 420     -47.928 -44.202  -8.385  1.00 23.71           C  
ANISOU 2845  CA  PHE A 420     2725   3364   2920    226   -190     89       C  
ATOM   2846  C   PHE A 420     -48.650 -45.478  -8.026  1.00 24.20           C  
ANISOU 2846  C   PHE A 420     2761   3424   3008    214   -188     51       C  
ATOM   2847  O   PHE A 420     -49.344 -46.081  -8.872  1.00 22.41           O  
ANISOU 2847  O   PHE A 420     2521   3237   2756    171   -229     48       O  
ATOM   2848  CB  PHE A 420     -48.633 -43.010  -7.711  1.00 23.77           C  
ANISOU 2848  CB  PHE A 420     2694   3337   3001    279   -204    147       C  
ATOM   2849  CG  PHE A 420     -50.096 -42.921  -8.032  1.00 26.76           C  
ANISOU 2849  CG  PHE A 420     3017   3733   3420    276   -261    190       C  
ATOM   2850  CD1 PHE A 420     -51.063 -43.590  -7.260  1.00 26.38           C  
ANISOU 2850  CD1 PHE A 420     2921   3679   3424    290   -247    170       C  
ATOM   2851  CD2 PHE A 420     -50.531 -42.190  -9.160  1.00 28.72           C  
ANISOU 2851  CD2 PHE A 420     3255   4007   3651    249   -335    258       C  
ATOM   2852  CE1 PHE A 420     -52.467 -43.488  -7.588  1.00 28.81           C  
ANISOU 2852  CE1 PHE A 420     3166   4005   3776    286   -302    209       C  
ATOM   2853  CE2 PHE A 420     -51.899 -42.116  -9.496  1.00 30.78           C  
ANISOU 2853  CE2 PHE A 420     3456   4281   3957    244   -397    302       C  
ATOM   2854  CZ  PHE A 420     -52.877 -42.773  -8.694  1.00 29.06           C  
ANISOU 2854  CZ  PHE A 420     3186   4056   3801    267   -378    273       C  
ATOM   2855  N   LYS A 421     -48.486 -45.884  -6.765  1.00 22.35           N  
ANISOU 2855  N   LYS A 421     2520   3148   2823    245   -144     27       N  
ATOM   2856  CA  LYS A 421     -49.164 -47.109  -6.277  1.00 23.46           C  
ANISOU 2856  CA  LYS A 421     2636   3282   2997    227   -145      4       C  
ATOM   2857  C   LYS A 421     -49.717 -46.834  -4.874  1.00 22.68           C  
ANISOU 2857  C   LYS A 421     2500   3162   2956    260   -116     26       C  
ATOM   2858  O   LYS A 421     -48.971 -46.323  -4.003  1.00 25.49           O  
ANISOU 2858  O   LYS A 421     2872   3492   3321    290    -74     22       O  
ATOM   2859  CB  LYS A 421     -48.194 -48.304  -6.262  1.00 23.24           C  
ANISOU 2859  CB  LYS A 421     2640   3229   2961    202   -125    -60       C  
ATOM   2860  CG  LYS A 421     -48.984 -49.677  -5.956  1.00 24.02           C  
ANISOU 2860  CG  LYS A 421     2711   3315   3101    170   -146    -77       C  
ATOM   2861  CD  LYS A 421     -48.013 -50.911  -5.888  1.00 21.73           C  
ANISOU 2861  CD  LYS A 421     2444   2978   2833    150   -138   -141       C  
ATOM   2862  CE  LYS A 421     -47.385 -51.127  -7.257  1.00 23.08           C  
ANISOU 2862  CE  LYS A 421     2640   3175   2955    125   -146   -206       C  
ATOM   2863  NZ  LYS A 421     -48.457 -51.404  -8.276  1.00 25.87           N  
ANISOU 2863  NZ  LYS A 421     2973   3578   3277     83   -191   -208       N  
ATOM   2864  N   PRO A 422     -50.992 -47.124  -4.610  1.00 21.89           N  
ANISOU 2864  N   PRO A 422     2347   3080   2890    252   -134     44       N  
ATOM   2865  CA  PRO A 422     -51.532 -46.883  -3.259  1.00 21.56           C  
ANISOU 2865  CA  PRO A 422     2263   3037   2893    273    -97     53       C  
ATOM   2866  C   PRO A 422     -51.204 -48.029  -2.322  1.00 25.79           C  
ANISOU 2866  C   PRO A 422     2810   3559   3432    240    -73     37       C  
ATOM   2867  O   PRO A 422     -51.180 -49.205  -2.721  1.00 25.49           O  
ANISOU 2867  O   PRO A 422     2784   3511   3391    200   -101     24       O  
ATOM   2868  CB  PRO A 422     -53.050 -46.804  -3.471  1.00 22.16           C  
ANISOU 2868  CB  PRO A 422     2269   3146   3004    268   -129     78       C  
ATOM   2869  CG  PRO A 422     -53.334 -47.660  -4.729  1.00 22.47           C  
ANISOU 2869  CG  PRO A 422     2322   3202   3015    223   -186     79       C  
ATOM   2870  CD  PRO A 422     -52.026 -47.582  -5.565  1.00 22.18           C  
ANISOU 2870  CD  PRO A 422     2355   3151   2922    218   -189     57       C  
ATOM   2871  N   TYR A 423     -51.067 -47.687  -1.035  1.00 22.57           N  
ANISOU 2871  N   TYR A 423     2388   3151   3035    252    -27     39       N  
ATOM   2872  CA  TYR A 423     -50.879 -48.683   0.014  1.00 22.78           C  
ANISOU 2872  CA  TYR A 423     2418   3173   3064    209    -12     43       C  
ATOM   2873  C   TYR A 423     -51.585 -48.201   1.250  1.00 25.73           C  
ANISOU 2873  C   TYR A 423     2740   3591   3445    206     32     51       C  
ATOM   2874  O   TYR A 423     -51.419 -47.036   1.638  1.00 27.13           O  
ANISOU 2874  O   TYR A 423     2910   3776   3623    247     69     35       O  
ATOM   2875  CB  TYR A 423     -49.401 -48.864   0.399  1.00 22.04           C  
ANISOU 2875  CB  TYR A 423     2382   3036   2956    211      4     32       C  
ATOM   2876  CG  TYR A 423     -48.463 -49.537  -0.601  1.00 22.83           C  
ANISOU 2876  CG  TYR A 423     2528   3092   3055    207    -27      7       C  
ATOM   2877  CD1 TYR A 423     -47.873 -48.805  -1.658  1.00 21.50           C  
ANISOU 2877  CD1 TYR A 423     2389   2921   2860    239    -28    -16       C  
ATOM   2878  CD2 TYR A 423     -48.109 -50.897  -0.457  1.00 23.42           C  
ANISOU 2878  CD2 TYR A 423     2613   3127   3159    166    -55      1       C  
ATOM   2879  CE1 TYR A 423     -46.958 -49.430  -2.554  1.00 21.77           C  
ANISOU 2879  CE1 TYR A 423     2457   2927   2886    229    -44    -56       C  
ATOM   2880  CE2 TYR A 423     -47.197 -51.526  -1.348  1.00 23.85           C  
ANISOU 2880  CE2 TYR A 423     2699   3137   3226    166    -76    -44       C  
ATOM   2881  CZ  TYR A 423     -46.607 -50.781  -2.357  1.00 24.27           C  
ANISOU 2881  CZ  TYR A 423     2778   3203   3242    197    -64    -78       C  
ATOM   2882  OH  TYR A 423     -45.757 -51.427  -3.237  1.00 25.62           O  
ANISOU 2882  OH  TYR A 423     2970   3345   3419    189    -76   -137       O  
ATOM   2883  N   MET A 424     -52.290 -49.095   1.923  1.00 27.54           N  
ANISOU 2883  N   MET A 424     2934   3850   3679    150     29     70       N  
ATOM   2884  CA  MET A 424     -52.445 -48.921   3.365  1.00 26.28           C  
ANISOU 2884  CA  MET A 424     2746   3738   3501    121     79     74       C  
ATOM   2885  C   MET A 424     -51.083 -49.046   4.054  1.00 25.20           C  
ANISOU 2885  C   MET A 424     2669   3569   3338    109     92     81       C  
ATOM   2886  O   MET A 424     -50.228 -49.881   3.682  1.00 25.66           O  
ANISOU 2886  O   MET A 424     2775   3569   3404     95     53     95       O  
ATOM   2887  CB  MET A 424     -53.452 -49.929   3.934  1.00 31.31           C  
ANISOU 2887  CB  MET A 424     3333   4422   4139     47     69    105       C  
ATOM   2888  CG  MET A 424     -54.861 -49.843   3.321  1.00 33.51           C  
ANISOU 2888  CG  MET A 424     3544   4739   4450     54     55    100       C  
ATOM   2889  SD  MET A 424     -55.578 -48.193   3.468  1.00 38.61           S  
ANISOU 2889  SD  MET A 424     4121   5428   5122    124    109     52       S  
ATOM   2890  CE  MET A 424     -55.824 -48.180   5.236  1.00 38.65           C  
ANISOU 2890  CE  MET A 424     4080   5519   5087     64    184     37       C  
ATOM   2891  N   LYS A 425     -50.834 -48.169   5.051  1.00 22.67           N  
ANISOU 2891  N   LYS A 425     2340   3283   2992    117    147     63       N  
ATOM   2892  CA  LYS A 425     -49.439 -47.973   5.468  1.00 22.90           C  
ANISOU 2892  CA  LYS A 425     2428   3274   2998    124    156     63       C  
ATOM   2893  C   LYS A 425     -48.836 -49.262   6.046  1.00 23.72           C  
ANISOU 2893  C   LYS A 425     2560   3357   3094     54    120    113       C  
ATOM   2894  O   LYS A 425     -47.619 -49.485   5.922  1.00 21.51           O  
ANISOU 2894  O   LYS A 425     2332   3018   2822     64     98    120       O  
ATOM   2895  CB  LYS A 425     -49.317 -46.839   6.498  1.00 24.23           C  
ANISOU 2895  CB  LYS A 425     2581   3489   3137    135    220     30       C  
ATOM   2896  CG  LYS A 425     -50.084 -47.120   7.844  1.00 24.55           C  
ANISOU 2896  CG  LYS A 425     2570   3622   3138     59    258     35       C  
ATOM   2897  CD  LYS A 425     -49.951 -45.897   8.757  1.00 22.81           C  
ANISOU 2897  CD  LYS A 425     2330   3448   2888     74    328    -22       C  
ATOM   2898  CE  LYS A 425     -50.693 -46.105  10.097  1.00 22.90           C  
ANISOU 2898  CE  LYS A 425     2285   3572   2843    -12    377    -31       C  
ATOM   2899  NZ  LYS A 425     -50.308 -44.883  10.902  1.00 23.60           N  
ANISOU 2899  NZ  LYS A 425     2366   3695   2905      7    444   -103       N  
ATOM   2900  N   GLN A 426     -49.666 -50.132   6.649  1.00 24.90           N  
ANISOU 2900  N   GLN A 426     2672   3550   3237    -20    106    151       N  
ATOM   2901  CA  GLN A 426     -49.108 -51.387   7.152  1.00 25.68           C  
ANISOU 2901  CA  GLN A 426     2796   3616   3346    -91     54    212       C  
ATOM   2902  C   GLN A 426     -48.632 -52.307   6.012  1.00 27.78           C  
ANISOU 2902  C   GLN A 426     3093   3785   3676    -70    -11    213       C  
ATOM   2903  O   GLN A 426     -47.900 -53.268   6.280  1.00 26.76           O  
ANISOU 2903  O   GLN A 426     2988   3598   3583   -109    -63    252       O  
ATOM   2904  CB  GLN A 426     -50.120 -52.151   8.017  1.00 25.66           C  
ANISOU 2904  CB  GLN A 426     2746   3683   3322   -188     46    264       C  
ATOM   2905  CG  GLN A 426     -51.348 -52.716   7.268  1.00 31.39           C  
ANISOU 2905  CG  GLN A 426     3428   4417   4082   -196     21    265       C  
ATOM   2906  CD  GLN A 426     -52.523 -51.699   7.102  1.00 35.86           C  
ANISOU 2906  CD  GLN A 426     3933   5061   4631   -158     82    213       C  
ATOM   2907  OE1 GLN A 426     -52.349 -50.478   7.309  1.00 36.60           O  
ANISOU 2907  OE1 GLN A 426     4021   5182   4703   -104    139    163       O  
ATOM   2908  NE2 GLN A 426     -53.727 -52.216   6.802  1.00 34.36           N  
ANISOU 2908  NE2 GLN A 426     3690   4905   4461   -189     65    225       N  
ATOM   2909  N   HIS A 427     -49.015 -52.031   4.761  1.00 26.94           N  
ANISOU 2909  N   HIS A 427     2983   3662   3590    -13    -14    168       N  
ATOM   2910  CA  HIS A 427     -48.552 -52.839   3.637  1.00 25.95           C  
ANISOU 2910  CA  HIS A 427     2885   3460   3517      3    -66    148       C  
ATOM   2911  C   HIS A 427     -47.379 -52.234   2.890  1.00 24.29           C  
ANISOU 2911  C   HIS A 427     2718   3206   3306     67    -53    100       C  
ATOM   2912  O   HIS A 427     -46.895 -52.839   1.921  1.00 24.29           O  
ANISOU 2912  O   HIS A 427     2736   3151   3342     80    -86     65       O  
ATOM   2913  CB  HIS A 427     -49.734 -53.094   2.698  1.00 28.82           C  
ANISOU 2913  CB  HIS A 427     3215   3844   3893      3    -86    132       C  
ATOM   2914  CG  HIS A 427     -50.829 -53.868   3.372  1.00 31.63           C  
ANISOU 2914  CG  HIS A 427     3525   4237   4257    -69   -105    181       C  
ATOM   2915  ND1 HIS A 427     -52.171 -53.673   3.104  1.00 33.52           N  
ANISOU 2915  ND1 HIS A 427     3712   4536   4487    -76    -97    180       N  
ATOM   2916  CD2 HIS A 427     -50.767 -54.831   4.325  1.00 32.45           C  
ANISOU 2916  CD2 HIS A 427     3623   4329   4377   -145   -137    239       C  
ATOM   2917  CE1 HIS A 427     -52.883 -54.491   3.863  1.00 35.62           C  
ANISOU 2917  CE1 HIS A 427     3943   4832   4759   -154   -115    230       C  
ATOM   2918  NE2 HIS A 427     -52.051 -55.203   4.611  1.00 35.36           N  
ANISOU 2918  NE2 HIS A 427     3940   4757   4740   -200   -142    271       N  
ATOM   2919  N   LEU A 428     -46.909 -51.048   3.278  1.00 22.26           N  
ANISOU 2919  N   LEU A 428     2475   2974   3010    104     -5     90       N  
ATOM   2920  CA  LEU A 428     -45.652 -50.576   2.677  1.00 24.26           C  
ANISOU 2920  CA  LEU A 428     2770   3184   3263    152      3     54       C  
ATOM   2921  C   LEU A 428     -44.513 -51.570   2.923  1.00 23.49           C  
ANISOU 2921  C   LEU A 428     2696   3017   3212    130    -32     61       C  
ATOM   2922  O   LEU A 428     -44.521 -52.293   3.951  1.00 20.35           O  
ANISOU 2922  O   LEU A 428     2289   2609   2835     77    -58    111       O  
ATOM   2923  CB  LEU A 428     -45.261 -49.219   3.265  1.00 22.94           C  
ANISOU 2923  CB  LEU A 428     2614   3047   3055    185     55     50       C  
ATOM   2924  CG  LEU A 428     -46.230 -48.104   2.819  1.00 22.84           C  
ANISOU 2924  CG  LEU A 428     2575   3081   3023    223     82     33       C  
ATOM   2925  CD1 LEU A 428     -45.970 -46.829   3.693  1.00 25.59           C  
ANISOU 2925  CD1 LEU A 428     2923   3453   3346    248    132     24       C  
ATOM   2926  CD2 LEU A 428     -45.962 -47.686   1.353  1.00 19.57           C  
ANISOU 2926  CD2 LEU A 428     2181   2646   2608    264     67      6       C  
ATOM   2927  N   PRO A 429     -43.503 -51.594   2.026  1.00 20.85           N  
ANISOU 2927  N   PRO A 429     2387   2637   2899    166    -37     12       N  
ATOM   2928  CA  PRO A 429     -42.287 -52.408   2.266  1.00 23.28           C  
ANISOU 2928  CA  PRO A 429     2707   2871   3267    157    -68      7       C  
ATOM   2929  C   PRO A 429     -41.733 -52.165   3.668  1.00 23.11           C  
ANISOU 2929  C   PRO A 429     2694   2851   3237    134    -64     65       C  
ATOM   2930  O   PRO A 429     -41.591 -51.015   4.099  1.00 20.33           O  
ANISOU 2930  O   PRO A 429     2355   2544   2825    154    -18     69       O  
ATOM   2931  CB  PRO A 429     -41.294 -51.907   1.194  1.00 20.33           C  
ANISOU 2931  CB  PRO A 429     2355   2484   2887    206    -44    -62       C  
ATOM   2932  CG  PRO A 429     -42.244 -51.505   0.004  1.00 19.71           C  
ANISOU 2932  CG  PRO A 429     2271   2457   2763    219    -31    -95       C  
ATOM   2933  CD  PRO A 429     -43.450 -50.854   0.723  1.00 19.65           C  
ANISOU 2933  CD  PRO A 429     2247   2506   2714    209    -16    -40       C  
ATOM   2934  N   LYS A 430     -41.458 -53.249   4.402  1.00 22.43           N  
ANISOU 2934  N   LYS A 430     2598   2714   3211     86   -119    112       N  
ATOM   2935  CA  LYS A 430     -41.022 -53.059   5.804  1.00 24.68           C  
ANISOU 2935  CA  LYS A 430     2889   3014   3473     45   -124    180       C  
ATOM   2936  C   LYS A 430     -39.700 -52.266   5.895  1.00 25.70           C  
ANISOU 2936  C   LYS A 430     3045   3127   3592     85    -98    157       C  
ATOM   2937  O   LYS A 430     -39.465 -51.556   6.886  1.00 24.04           O  
ANISOU 2937  O   LYS A 430     2847   2961   3326     66    -74    191       O  
ATOM   2938  CB  LYS A 430     -40.874 -54.417   6.474  1.00 24.08           C  
ANISOU 2938  CB  LYS A 430     2797   2877   3475    -21   -205    248       C  
ATOM   2939  CG  LYS A 430     -42.229 -55.170   6.416  1.00 26.20           C  
ANISOU 2939  CG  LYS A 430     3038   3166   3750    -70   -232    277       C  
ATOM   2940  CD  LYS A 430     -43.312 -54.426   7.262  1.00 26.33           C  
ANISOU 2940  CD  LYS A 430     3044   3301   3661   -111   -181    314       C  
ATOM   2941  CE  LYS A 430     -43.155 -54.837   8.762  1.00 26.30           C  
ANISOU 2941  CE  LYS A 430     3035   3322   3635   -206   -218    414       C  
ATOM   2942  NZ  LYS A 430     -44.281 -54.178   9.598  1.00 25.40           N  
ANISOU 2942  NZ  LYS A 430     2899   3340   3413   -257   -159    434       N  
ATOM   2943  N   ARG A 431     -38.826 -52.385   4.888  1.00 19.80           N  
ANISOU 2943  N   ARG A 431     2303   2323   2895    135   -100     94       N  
ATOM   2944  CA  ARG A 431     -37.568 -51.621   4.901  1.00 21.93           C  
ANISOU 2944  CA  ARG A 431     2594   2582   3156    171    -73     71       C  
ATOM   2945  C   ARG A 431     -37.781 -50.117   4.990  1.00 22.26           C  
ANISOU 2945  C   ARG A 431     2658   2697   3102    198     -7     61       C  
ATOM   2946  O   ARG A 431     -36.852 -49.405   5.366  1.00 25.09           O  
ANISOU 2946  O   ARG A 431     3035   3057   3443    212     13     61       O  
ATOM   2947  CB  ARG A 431     -36.748 -51.884   3.634  1.00 24.85           C  
ANISOU 2947  CB  ARG A 431     2958   2903   3580    218    -71    -12       C  
ATOM   2948  CG  ARG A 431     -37.494 -51.356   2.354  1.00 22.44           C  
ANISOU 2948  CG  ARG A 431     2659   2649   3219    247    -29    -71       C  
ATOM   2949  CD  ARG A 431     -36.703 -51.812   1.050  1.00 21.33           C  
ANISOU 2949  CD  ARG A 431     2506   2473   3125    275    -26   -164       C  
ATOM   2950  NE  ARG A 431     -37.550 -51.629  -0.107  1.00 21.24           N  
ANISOU 2950  NE  ARG A 431     2496   2511   3063    279     -7   -207       N  
ATOM   2951  CZ  ARG A 431     -37.791 -50.439  -0.686  1.00 23.30           C  
ANISOU 2951  CZ  ARG A 431     2777   2840   3236    297     36   -211       C  
ATOM   2952  NH1 ARG A 431     -37.174 -49.331  -0.271  1.00 21.06           N  
ANISOU 2952  NH1 ARG A 431     2515   2576   2912    316     67   -187       N  
ATOM   2953  NH2 ARG A 431     -38.640 -50.365  -1.735  1.00 19.60           N  
ANISOU 2953  NH2 ARG A 431     2306   2417   2725    291     39   -238       N  
ATOM   2954  N   LEU A 432     -38.973 -49.595   4.654  1.00 20.06           N  
ANISOU 2954  N   LEU A 432     2373   2475   2772    205     24     51       N  
ATOM   2955  CA  LEU A 432     -39.195 -48.147   4.842  1.00 19.81           C  
ANISOU 2955  CA  LEU A 432     2355   2500   2672    232     78     42       C  
ATOM   2956  C   LEU A 432     -39.456 -47.781   6.317  1.00 23.80           C  
ANISOU 2956  C   LEU A 432     2857   3050   3137    190     94     83       C  
ATOM   2957  O   LEU A 432     -39.361 -46.599   6.663  1.00 23.37           O  
ANISOU 2957  O   LEU A 432     2812   3028   3039    210    137     67       O  
ATOM   2958  CB  LEU A 432     -40.390 -47.652   4.013  1.00 18.53           C  
ANISOU 2958  CB  LEU A 432     2179   2378   2486    256     99     18       C  
ATOM   2959  CG  LEU A 432     -40.304 -47.909   2.485  1.00 23.47           C  
ANISOU 2959  CG  LEU A 432     2807   2983   3127    283     86    -24       C  
ATOM   2960  CD1 LEU A 432     -41.588 -47.498   1.781  1.00 21.91           C  
ANISOU 2960  CD1 LEU A 432     2592   2828   2907    294     91    -29       C  
ATOM   2961  CD2 LEU A 432     -39.085 -47.188   1.885  1.00 24.46           C  
ANISOU 2961  CD2 LEU A 432     2960   3093   3241    316    106    -55       C  
ATOM   2962  N   HIS A 433     -39.842 -48.753   7.165  1.00 21.44           N  
ANISOU 2962  N   HIS A 433     2541   2758   2846    127     59    134       N  
ATOM   2963  CA  HIS A 433     -40.135 -48.476   8.606  1.00 21.64           C  
ANISOU 2963  CA  HIS A 433     2560   2849   2815     67     76    174       C  
ATOM   2964  C   HIS A 433     -41.037 -47.265   8.748  1.00 22.51           C  
ANISOU 2964  C   HIS A 433     2654   3030   2868     89    142    131       C  
ATOM   2965  O   HIS A 433     -40.763 -46.338   9.543  1.00 22.81           O  
ANISOU 2965  O   HIS A 433     2700   3109   2859     83    182    115       O  
ATOM   2966  CB  HIS A 433     -38.823 -48.250   9.371  1.00 20.83           C  
ANISOU 2966  CB  HIS A 433     2483   2727   2704     50     65    197       C  
ATOM   2967  CG  HIS A 433     -37.979 -49.478   9.416  1.00 23.06           C  
ANISOU 2967  CG  HIS A 433     2768   2934   3060     22    -10    245       C  
ATOM   2968  ND1 HIS A 433     -38.324 -50.550  10.205  1.00 26.47           N  
ANISOU 2968  ND1 HIS A 433     3182   3368   3506    -58    -67    321       N  
ATOM   2969  CD2 HIS A 433     -36.900 -49.856   8.695  1.00 21.07           C  
ANISOU 2969  CD2 HIS A 433     2523   2599   2883     63    -41    226       C  
ATOM   2970  CE1 HIS A 433     -37.447 -51.528  10.015  1.00 25.50           C  
ANISOU 2970  CE1 HIS A 433     3057   3153   3477    -62   -138    351       C  
ATOM   2971  NE2 HIS A 433     -36.584 -51.135   9.091  1.00 24.27           N  
ANISOU 2971  NE2 HIS A 433     2913   2946   3361     15   -119    285       N  
ATOM   2972  N   TYR A 434     -42.110 -47.222   7.938  1.00 23.05           N  
ANISOU 2972  N   TYR A 434     2697   3112   2949    119    153    105       N  
ATOM   2973  CA  TYR A 434     -42.931 -45.992   7.851  1.00 25.37           C  
ANISOU 2973  CA  TYR A 434     2967   3452   3219    158    208     57       C  
ATOM   2974  C   TYR A 434     -44.396 -46.292   8.138  1.00 28.14           C  
ANISOU 2974  C   TYR A 434     3266   3866   3559    125    221     59       C  
ATOM   2975  O   TYR A 434     -45.255 -46.169   7.252  1.00 28.49           O  
ANISOU 2975  O   TYR A 434     3285   3909   3632    161    219     40       O  
ATOM   2976  CB  TYR A 434     -42.746 -45.320   6.451  1.00 23.99           C  
ANISOU 2976  CB  TYR A 434     2808   3232   3076    235    207     22       C  
ATOM   2977  CG  TYR A 434     -43.294 -43.883   6.378  1.00 24.77           C  
ANISOU 2977  CG  TYR A 434     2887   3355   3172    283    249    -20       C  
ATOM   2978  CD1 TYR A 434     -42.629 -42.840   7.033  1.00 25.15           C  
ANISOU 2978  CD1 TYR A 434     2950   3403   3203    296    283    -45       C  
ATOM   2979  CD2 TYR A 434     -44.451 -43.574   5.661  1.00 23.09           C  
ANISOU 2979  CD2 TYR A 434     2635   3154   2984    312    248    -34       C  
ATOM   2980  CE1 TYR A 434     -43.125 -41.520   7.025  1.00 24.88           C  
ANISOU 2980  CE1 TYR A 434     2891   3376   3187    341    316    -90       C  
ATOM   2981  CE2 TYR A 434     -44.934 -42.201   5.619  1.00 24.45           C  
ANISOU 2981  CE2 TYR A 434     2780   3332   3179    361    277    -72       C  
ATOM   2982  CZ  TYR A 434     -44.243 -41.212   6.333  1.00 25.62           C  
ANISOU 2982  CZ  TYR A 434     2942   3473   3318    374    311   -102       C  
ATOM   2983  OH  TYR A 434     -44.618 -39.884   6.320  1.00 26.37           O  
ANISOU 2983  OH  TYR A 434     3010   3557   3454    423    332   -144       O  
ATOM   2984  N   ALA A 435     -44.717 -46.597   9.395  1.00 20.42           N  
ANISOU 2984  N   ALA A 435     2268   2955   2537     50    236     82       N  
ATOM   2985  CA  ALA A 435     -46.105 -46.908   9.697  1.00 21.91           C  
ANISOU 2985  CA  ALA A 435     2399   3214   2712      9    253     83       C  
ATOM   2986  C   ALA A 435     -46.491 -46.648  11.164  1.00 21.66           C  
ANISOU 2986  C   ALA A 435     2336   3287   2608    -67    302     75       C  
ATOM   2987  O   ALA A 435     -47.618 -46.244  11.418  1.00 22.16           O  
ANISOU 2987  O   ALA A 435     2340   3422   2658    -73    350     32       O  
ATOM   2988  CB  ALA A 435     -46.414 -48.388   9.371  1.00 21.16           C  
ANISOU 2988  CB  ALA A 435     2302   3093   2646    -39    189    146       C  
ATOM   2989  N   ASN A 436     -45.580 -46.841  12.114  1.00 21.77           N  
ANISOU 2989  N   ASN A 436     2382   3316   2574   -127    293    111       N  
ATOM   2990  CA  ASN A 436     -45.949 -46.877  13.540  1.00 25.76           C  
ANISOU 2990  CA  ASN A 436     2858   3938   2992   -231    328    120       C  
ATOM   2991  C   ASN A 436     -45.923 -45.470  14.147  1.00 26.63           C  
ANISOU 2991  C   ASN A 436     2953   4107   3060   -207    410     25       C  
ATOM   2992  O   ASN A 436     -45.177 -45.183  15.066  1.00 28.61           O  
ANISOU 2992  O   ASN A 436     3228   4394   3250   -257    423     27       O  
ATOM   2993  CB  ASN A 436     -45.039 -47.813  14.314  1.00 25.19           C  
ANISOU 2993  CB  ASN A 436     2825   3861   2886   -324    266    216       C  
ATOM   2994  CG  ASN A 436     -45.490 -47.953  15.771  1.00 28.49           C  
ANISOU 2994  CG  ASN A 436     3213   4417   3197   -455    296    240       C  
ATOM   2995  OD1 ASN A 436     -46.645 -47.838  16.021  1.00 27.23           O  
ANISOU 2995  OD1 ASN A 436     2996   4347   3003   -485    346    204       O  
ATOM   2996  ND2 ASN A 436     -44.561 -48.098  16.716  1.00 25.00           N  
ANISOU 2996  ND2 ASN A 436     2804   4000   2696   -533    268    294       N  
ATOM   2997  N   ASN A 437     -46.772 -44.598  13.616  1.00 25.53           N  
ANISOU 2997  N   ASN A 437     2767   3971   2961   -132    460    -58       N  
ATOM   2998  CA  ASN A 437     -46.938 -43.250  14.165  1.00 24.00           C  
ANISOU 2998  CA  ASN A 437     2542   3826   2753   -104    537   -164       C  
ATOM   2999  C   ASN A 437     -48.317 -42.732  13.774  1.00 27.01           C  
ANISOU 2999  C   ASN A 437     2842   4236   3187    -55    582   -238       C  
ATOM   3000  O   ASN A 437     -48.715 -42.811  12.609  1.00 25.70           O  
ANISOU 3000  O   ASN A 437     2670   3998   3098     17    546   -223       O  
ATOM   3001  CB  ASN A 437     -45.846 -42.283  13.687  1.00 22.52           C  
ANISOU 3001  CB  ASN A 437     2406   3545   2606    -20    531   -195       C  
ATOM   3002  CG  ASN A 437     -45.734 -41.054  14.595  1.00 28.99           C  
ANISOU 3002  CG  ASN A 437     3204   4416   3393    -21    603   -295       C  
ATOM   3003  OD1 ASN A 437     -46.661 -40.202  14.657  1.00 28.76           O  
ANISOU 3003  OD1 ASN A 437     3108   4419   3402     17    661   -392       O  
ATOM   3004  ND2 ASN A 437     -44.658 -41.001  15.364  1.00 23.02           N  
ANISOU 3004  ND2 ASN A 437     2496   3675   2574    -73    599   -278       N  
ATOM   3005  N   ARG A 438     -49.035 -42.171  14.748  1.00 26.27           N  
ANISOU 3005  N   ARG A 438     2680   4249   3051    -96    660   -325       N  
ATOM   3006  CA  ARG A 438     -50.357 -41.645  14.477  1.00 27.66           C  
ANISOU 3006  CA  ARG A 438     2764   4456   3291    -49    706   -406       C  
ATOM   3007  C   ARG A 438     -50.361 -40.440  13.532  1.00 29.28           C  
ANISOU 3007  C   ARG A 438     2957   4554   3613     83    702   -469       C  
ATOM   3008  O   ARG A 438     -51.442 -40.049  13.071  1.00 28.01           O  
ANISOU 3008  O   ARG A 438     2720   4390   3533    136    717   -519       O  
ATOM   3009  CB  ARG A 438     -51.020 -41.245  15.786  1.00 29.62           C  
ANISOU 3009  CB  ARG A 438     2934   4848   3470   -124    800   -505       C  
ATOM   3010  CG  ARG A 438     -50.325 -40.026  16.424  1.00 32.30           C  
ANISOU 3010  CG  ARG A 438     3284   5188   3799   -100    853   -607       C  
ATOM   3011  CD  ARG A 438     -50.807 -39.837  17.906  1.00 37.42           C  
ANISOU 3011  CD  ARG A 438     3867   6009   4343   -211    949   -704       C  
ATOM   3012  NE  ARG A 438     -50.218 -38.645  18.495  1.00 41.22           N  
ANISOU 3012  NE  ARG A 438     4351   6491   4821   -187   1003   -819       N  
ATOM   3013  CZ  ARG A 438     -50.092 -38.461  19.802  1.00 48.55           C  
ANISOU 3013  CZ  ARG A 438     5259   7554   5631   -294   1072   -890       C  
ATOM   3014  NH1 ARG A 438     -50.515 -39.406  20.649  1.00 51.91           N  
ANISOU 3014  NH1 ARG A 438     5663   8131   5928   -436   1093   -845       N  
ATOM   3015  NH2 ARG A 438     -49.567 -37.337  20.277  1.00 49.13           N  
ANISOU 3015  NH2 ARG A 438     5335   7620   5713   -267   1119  -1007       N  
ATOM   3016  N   ARG A 439     -49.207 -39.830  13.264  1.00 28.32           N  
ANISOU 3016  N   ARG A 439     2905   4347   3508    132    679   -465       N  
ATOM   3017  CA  ARG A 439     -49.124 -38.751  12.292  1.00 29.80           C  
ANISOU 3017  CA  ARG A 439     3091   4427   3806    246    659   -499       C  
ATOM   3018  C   ARG A 439     -48.969 -39.263  10.864  1.00 30.27           C  
ANISOU 3018  C   ARG A 439     3193   4394   3913    295    577   -406       C  
ATOM   3019  O   ARG A 439     -48.979 -38.443   9.943  1.00 30.25           O  
ANISOU 3019  O   ARG A 439     3189   4308   3997    378    549   -415       O  
ATOM   3020  CB  ARG A 439     -47.918 -37.833  12.627  1.00 29.08           C  
ANISOU 3020  CB  ARG A 439     3054   4288   3707    268    669   -533       C  
ATOM   3021  CG  ARG A 439     -48.022 -37.256  14.057  1.00 31.03           C  
ANISOU 3021  CG  ARG A 439     3259   4631   3900    214    753   -642       C  
ATOM   3022  CD  ARG A 439     -46.668 -36.659  14.468  1.00 27.52           C  
ANISOU 3022  CD  ARG A 439     2884   4150   3421    210    752   -652       C  
ATOM   3023  NE  ARG A 439     -46.752 -36.273  15.862  1.00 30.23           N  
ANISOU 3023  NE  ARG A 439     3192   4602   3691    139    830   -752       N  
ATOM   3024  CZ  ARG A 439     -45.713 -35.881  16.623  1.00 28.28           C  
ANISOU 3024  CZ  ARG A 439     2995   4370   3381     98    845   -774       C  
ATOM   3025  NH1 ARG A 439     -44.488 -35.889  16.149  1.00 25.02           N  
ANISOU 3025  NH1 ARG A 439     2667   3869   2971    121    786   -697       N  
ATOM   3026  NH2 ARG A 439     -45.933 -35.516  17.880  1.00 29.75           N  
ANISOU 3026  NH2 ARG A 439     3139   4672   3494     25    921   -879       N  
ATOM   3027  N   ILE A 440     -48.763 -40.570  10.659  1.00 26.18           N  
ANISOU 3027  N   ILE A 440     2717   3887   3342    240    535   -317       N  
ATOM   3028  CA  ILE A 440     -48.678 -41.134   9.313  1.00 24.87           C  
ANISOU 3028  CA  ILE A 440     2585   3647   3216    277    464   -245       C  
ATOM   3029  C   ILE A 440     -50.074 -41.604   8.904  1.00 26.14           C  
ANISOU 3029  C   ILE A 440     2677   3843   3412    274    456   -241       C  
ATOM   3030  O   ILE A 440     -50.667 -42.469   9.572  1.00 25.66           O  
ANISOU 3030  O   ILE A 440     2585   3860   3305    200    473   -226       O  
ATOM   3031  CB  ILE A 440     -47.671 -42.296   9.250  1.00 25.39           C  
ANISOU 3031  CB  ILE A 440     2727   3693   3228    226    419   -165       C  
ATOM   3032  CG1 ILE A 440     -46.249 -41.813   9.621  1.00 24.09           C  
ANISOU 3032  CG1 ILE A 440     2626   3492   3036    231    423   -167       C  
ATOM   3033  CG2 ILE A 440     -47.688 -42.908   7.828  1.00 26.12           C  
ANISOU 3033  CG2 ILE A 440     2843   3719   3361    260    355   -113       C  
ATOM   3034  CD1 ILE A 440     -45.222 -42.941   9.819  1.00 25.06           C  
ANISOU 3034  CD1 ILE A 440     2808   3599   3116    175    382    -95       C  
ATOM   3035  N   GLU A 441     -50.630 -41.000   7.848  1.00 25.68           N  
ANISOU 3035  N   GLU A 441     2589   3732   3435    347    427   -249       N  
ATOM   3036  CA  GLU A 441     -51.990 -41.355   7.418  1.00 28.60           C  
ANISOU 3036  CA  GLU A 441     2886   4133   3849    348    414   -245       C  
ATOM   3037  C   GLU A 441     -52.047 -42.813   6.957  1.00 25.06           C  
ANISOU 3037  C   GLU A 441     2471   3692   3359    293    366   -168       C  
ATOM   3038  O   GLU A 441     -51.073 -43.315   6.389  1.00 24.95           O  
ANISOU 3038  O   GLU A 441     2534   3625   3321    290    322   -119       O  
ATOM   3039  CB  GLU A 441     -52.403 -40.439   6.257  1.00 32.07           C  
ANISOU 3039  CB  GLU A 441     3299   4501   4385    433    371   -249       C  
ATOM   3040  CG  GLU A 441     -52.756 -38.993   6.666  1.00 32.73           C  
ANISOU 3040  CG  GLU A 441     3317   4568   4552    494    410   -333       C  
ATOM   3041  CD  GLU A 441     -51.502 -38.131   6.944  1.00 39.57           C  
ANISOU 3041  CD  GLU A 441     4245   5381   5408    519    423   -355       C  
ATOM   3042  OE1 GLU A 441     -50.346 -38.628   6.831  1.00 40.14           O  
ANISOU 3042  OE1 GLU A 441     4408   5435   5408    491    405   -304       O  
ATOM   3043  OE2 GLU A 441     -51.672 -36.934   7.306  1.00 43.79           O  
ANISOU 3043  OE2 GLU A 441     4731   5890   6017    568    452   -430       O  
ATOM   3044  N   ASP A 442     -53.184 -43.478   7.213  1.00 24.46           N  
ANISOU 3044  N   ASP A 442     2330   3681   3281    249    374   -165       N  
ATOM   3045  CA  ASP A 442     -53.335 -44.890   6.849  1.00 26.76           C  
ANISOU 3045  CA  ASP A 442     2645   3977   3544    190    325    -95       C  
ATOM   3046  C   ASP A 442     -53.132 -45.071   5.355  1.00 26.95           C  
ANISOU 3046  C   ASP A 442     2710   3924   3606    236    255    -58       C  
ATOM   3047  O   ASP A 442     -52.539 -46.056   4.920  1.00 27.83           O  
ANISOU 3047  O   ASP A 442     2878   4001   3693    205    211    -13       O  
ATOM   3048  CB  ASP A 442     -54.740 -45.430   7.205  1.00 29.50           C  
ANISOU 3048  CB  ASP A 442     2905   4406   3898    140    341    -98       C  
ATOM   3049  CG  ASP A 442     -54.996 -45.406   8.668  1.00 36.37           C  
ANISOU 3049  CG  ASP A 442     3731   5376   4713     73    413   -133       C  
ATOM   3050  OD1 ASP A 442     -54.034 -45.281   9.414  1.00 38.87           O  
ANISOU 3050  OD1 ASP A 442     4096   5698   4974     47    437   -136       O  
ATOM   3051  OD2 ASP A 442     -56.144 -45.460   9.077  1.00 38.90           O  
ANISOU 3051  OD2 ASP A 442     3963   5777   5041     42    448   -162       O  
ATOM   3052  N   LEU A 443     -53.645 -44.138   4.549  1.00 25.47           N  
ANISOU 3052  N   LEU A 443     2487   3708   3481    303    239    -78       N  
ATOM   3053  CA  LEU A 443     -53.561 -44.264   3.086  1.00 26.11           C  
ANISOU 3053  CA  LEU A 443     2601   3735   3585    332    169    -40       C  
ATOM   3054  C   LEU A 443     -52.352 -43.514   2.539  1.00 28.18           C  
ANISOU 3054  C   LEU A 443     2933   3934   3841    377    156    -37       C  
ATOM   3055  O   LEU A 443     -52.213 -42.298   2.749  1.00 27.54           O  
ANISOU 3055  O   LEU A 443     2835   3832   3796    426    177    -67       O  
ATOM   3056  CB  LEU A 443     -54.845 -43.737   2.476  1.00 30.29           C  
ANISOU 3056  CB  LEU A 443     3050   4274   4185    367    144    -44       C  
ATOM   3057  CG  LEU A 443     -54.952 -43.817   0.938  1.00 34.61           C  
ANISOU 3057  CG  LEU A 443     3621   4783   4748    383     65      1       C  
ATOM   3058  CD1 LEU A 443     -54.552 -45.171   0.390  1.00 33.39           C  
ANISOU 3058  CD1 LEU A 443     3525   4626   4536    328     30     33       C  
ATOM   3059  CD2 LEU A 443     -56.482 -43.526   0.603  1.00 34.44           C  
ANISOU 3059  CD2 LEU A 443     3497   4786   4801    400     39      3       C  
ATOM   3060  N   HIS A 444     -51.478 -44.226   1.822  1.00 21.43           N  
ANISOU 3060  N   HIS A 444     2149   3047   2948    358    119     -7       N  
ATOM   3061  CA  HIS A 444     -50.211 -43.683   1.360  1.00 24.70           C  
ANISOU 3061  CA  HIS A 444     2630   3413   3343    386    112     -5       C  
ATOM   3062  C   HIS A 444     -50.090 -43.950  -0.130  1.00 26.30           C  
ANISOU 3062  C   HIS A 444     2861   3595   3535    385     54     22       C  
ATOM   3063  O   HIS A 444     -50.638 -44.940  -0.622  1.00 29.09           O  
ANISOU 3063  O   HIS A 444     3205   3967   3882    350     23     33       O  
ATOM   3064  CB  HIS A 444     -49.036 -44.334   2.070  1.00 23.72           C  
ANISOU 3064  CB  HIS A 444     2561   3278   3174    354    136     -7       C  
ATOM   3065  CG  HIS A 444     -47.771 -43.574   1.905  1.00 25.58           C  
ANISOU 3065  CG  HIS A 444     2849   3473   3396    384    144    -14       C  
ATOM   3066  ND1 HIS A 444     -47.482 -42.453   2.658  1.00 25.09           N  
ANISOU 3066  ND1 HIS A 444     2782   3406   3346    414    183    -38       N  
ATOM   3067  CD2 HIS A 444     -46.736 -43.739   1.037  1.00 25.04           C  
ANISOU 3067  CD2 HIS A 444     2837   3372   3307    387    120     -6       C  
ATOM   3068  CE1 HIS A 444     -46.304 -41.979   2.287  1.00 25.78           C  
ANISOU 3068  CE1 HIS A 444     2923   3455   3419    432    178    -34       C  
ATOM   3069  NE2 HIS A 444     -45.833 -42.733   1.299  1.00 25.11           N  
ANISOU 3069  NE2 HIS A 444     2873   3357   3312    415    143    -15       N  
ATOM   3070  N   LEU A 445     -49.439 -43.046  -0.854  1.00 24.12           N  
ANISOU 3070  N   LEU A 445     2617   3290   3257    415     37     32       N  
ATOM   3071  CA  LEU A 445     -49.113 -43.279  -2.269  1.00 23.90           C  
ANISOU 3071  CA  LEU A 445     2625   3260   3197    399    -13     54       C  
ATOM   3072  C   LEU A 445     -47.596 -43.268  -2.423  1.00 25.80           C  
ANISOU 3072  C   LEU A 445     2932   3478   3393    395      5     42       C  
ATOM   3073  O   LEU A 445     -46.952 -42.279  -2.038  1.00 26.07           O  
ANISOU 3073  O   LEU A 445     2981   3487   3435    424     26     42       O  
ATOM   3074  CB  LEU A 445     -49.739 -42.216  -3.170  1.00 24.35           C  
ANISOU 3074  CB  LEU A 445     2655   3315   3284    422    -61     91       C  
ATOM   3075  CG  LEU A 445     -51.207 -41.894  -3.009  1.00 26.19           C  
ANISOU 3075  CG  LEU A 445     2807   3559   3584    441    -82    103       C  
ATOM   3076  CD1 LEU A 445     -51.645 -40.758  -4.011  1.00 27.83           C  
ANISOU 3076  CD1 LEU A 445     2991   3748   3835    463   -149    155       C  
ATOM   3077  CD2 LEU A 445     -52.148 -43.131  -3.154  1.00 25.01           C  
ANISOU 3077  CD2 LEU A 445     2628   3450   3426    401    -97    102       C  
ATOM   3078  N   LEU A 446     -47.023 -44.378  -2.937  1.00 23.37           N  
ANISOU 3078  N   LEU A 446     2657   3174   3047    358     -3     23       N  
ATOM   3079  CA  LEU A 446     -45.621 -44.437  -3.357  1.00 25.00           C  
ANISOU 3079  CA  LEU A 446     2917   3367   3216    351      8      3       C  
ATOM   3080  C   LEU A 446     -45.542 -43.966  -4.802  1.00 24.72           C  
ANISOU 3080  C   LEU A 446     2896   3359   3138    335    -28     18       C  
ATOM   3081  O   LEU A 446     -46.097 -44.614  -5.691  1.00 25.13           O  
ANISOU 3081  O   LEU A 446     2938   3441   3167    301    -61     13       O  
ATOM   3082  CB  LEU A 446     -45.058 -45.859  -3.273  1.00 27.98           C  
ANISOU 3082  CB  LEU A 446     3310   3731   3589    321     14    -37       C  
ATOM   3083  CG  LEU A 446     -44.592 -46.427  -1.917  1.00 32.78           C  
ANISOU 3083  CG  LEU A 446     3921   4307   4228    320     41    -44       C  
ATOM   3084  CD1 LEU A 446     -43.739 -47.686  -2.152  1.00 30.84           C  
ANISOU 3084  CD1 LEU A 446     3693   4031   3995    295     32    -83       C  
ATOM   3085  CD2 LEU A 446     -43.747 -45.379  -1.093  1.00 31.23           C  
ANISOU 3085  CD2 LEU A 446     3744   4095   4028    350     78    -35       C  
ATOM   3086  N   VAL A 447     -44.863 -42.869  -5.049  1.00 24.15           N  
ANISOU 3086  N   VAL A 447     2846   3280   3051    349    -25     40       N  
ATOM   3087  CA  VAL A 447     -44.844 -42.275  -6.382  1.00 23.11           C  
ANISOU 3087  CA  VAL A 447     2726   3183   2873    321    -67     74       C  
ATOM   3088  C   VAL A 447     -43.611 -42.734  -7.167  1.00 23.46           C  
ANISOU 3088  C   VAL A 447     2811   3257   2847    281    -50     34       C  
ATOM   3089  O   VAL A 447     -42.509 -42.825  -6.618  1.00 22.09           O  
ANISOU 3089  O   VAL A 447     2659   3058   2675    294     -7      1       O  
ATOM   3090  CB  VAL A 447     -44.871 -40.747  -6.274  1.00 24.59           C  
ANISOU 3090  CB  VAL A 447     2908   3343   3091    351    -86    131       C  
ATOM   3091  CG1 VAL A 447     -44.854 -40.095  -7.682  1.00 24.13           C  
ANISOU 3091  CG1 VAL A 447     2862   3323   2983    308   -144    188       C  
ATOM   3092  CG2 VAL A 447     -46.062 -40.314  -5.456  1.00 25.71           C  
ANISOU 3092  CG2 VAL A 447     2997   3456   3317    396    -94    147       C  
ATOM   3093  N   GLU A 448     -43.787 -42.972  -8.473  1.00 23.35           N  
ANISOU 3093  N   GLU A 448     2801   3301   2769    227    -83     36       N  
ATOM   3094  CA  GLU A 448     -42.661 -43.375  -9.307  1.00 22.60           C  
ANISOU 3094  CA  GLU A 448     2735   3252   2601    181    -60    -17       C  
ATOM   3095  C   GLU A 448     -41.639 -42.253  -9.372  1.00 22.92           C  
ANISOU 3095  C   GLU A 448     2801   3292   2615    181    -46     17       C  
ATOM   3096  O   GLU A 448     -42.009 -41.086  -9.477  1.00 23.91           O  
ANISOU 3096  O   GLU A 448     2925   3410   2750    188    -84     97       O  
ATOM   3097  CB  GLU A 448     -43.149 -43.684 -10.722  1.00 21.99           C  
ANISOU 3097  CB  GLU A 448     2655   3255   2445    110   -100    -18       C  
ATOM   3098  CG  GLU A 448     -42.031 -44.273 -11.653  1.00 31.66           C  
ANISOU 3098  CG  GLU A 448     3898   4544   3585     51    -65   -101       C  
ATOM   3099  CD  GLU A 448     -42.564 -44.635 -13.052  1.00 38.32           C  
ANISOU 3099  CD  GLU A 448     4738   5484   4337    -33   -103   -115       C  
ATOM   3100  OE1 GLU A 448     -43.756 -44.932 -13.163  1.00 38.10           O  
ANISOU 3100  OE1 GLU A 448     4691   5457   4328    -37   -149    -87       O  
ATOM   3101  OE2 GLU A 448     -41.798 -44.610 -14.039  1.00 45.55           O  
ANISOU 3101  OE2 GLU A 448     5668   6483   5156   -100    -86   -153       O  
ATOM   3102  N   ARG A 449     -40.362 -42.597  -9.297  1.00 23.49           N  
ANISOU 3102  N   ARG A 449     2892   3367   2667    175      4    -44       N  
ATOM   3103  CA  ARG A 449     -39.306 -41.583  -9.452  1.00 24.64           C  
ANISOU 3103  CA  ARG A 449     3061   3523   2780    165     19    -15       C  
ATOM   3104  C   ARG A 449     -39.543 -40.799 -10.742  1.00 24.86           C  
ANISOU 3104  C   ARG A 449     3097   3624   2725     98    -29     50       C  
ATOM   3105  O   ARG A 449     -39.953 -41.360 -11.754  1.00 23.56           O  
ANISOU 3105  O   ARG A 449     2926   3530   2495     40    -49     30       O  
ATOM   3106  CB  ARG A 449     -37.911 -42.232  -9.522  1.00 24.81           C  
ANISOU 3106  CB  ARG A 449     3089   3559   2777    150     77   -102       C  
ATOM   3107  CG  ARG A 449     -37.776 -43.303 -10.653  1.00 27.24           C  
ANISOU 3107  CG  ARG A 449     3386   3942   3021     90     89   -189       C  
ATOM   3108  CD  ARG A 449     -36.351 -43.935 -10.754  1.00 27.34           C  
ANISOU 3108  CD  ARG A 449     3391   3967   3028     80    150   -292       C  
ATOM   3109  NE  ARG A 449     -35.370 -42.945 -11.118  1.00 30.74           N  
ANISOU 3109  NE  ARG A 449     3838   4442   3401     49    170   -264       N  
ATOM   3110  CZ  ARG A 449     -34.994 -42.684 -12.380  1.00 33.84           C  
ANISOU 3110  CZ  ARG A 449     4232   4942   3683    -33    177   -277       C  
ATOM   3111  NH1 ARG A 449     -35.489 -43.393 -13.408  1.00 34.38           N  
ANISOU 3111  NH1 ARG A 449     4288   5090   3685    -93    169   -332       N  
ATOM   3112  NH2 ARG A 449     -34.121 -41.719 -12.611  1.00 32.69           N  
ANISOU 3112  NH2 ARG A 449     4100   4832   3488    -64    190   -235       N  
ATOM   3113  N   ARG A 450     -39.304 -39.497 -10.685  1.00 24.32           N  
ANISOU 3113  N   ARG A 450     3041   3537   2663    101    -53    131       N  
ATOM   3114  CA  ARG A 450     -39.407 -38.533 -11.769  1.00 22.57           C  
ANISOU 3114  CA  ARG A 450     2829   3370   2376     34   -112    221       C  
ATOM   3115  C   ARG A 450     -40.848 -38.027 -11.920  1.00 24.87           C  
ANISOU 3115  C   ARG A 450     3097   3637   2714     45   -193    308       C  
ATOM   3116  O   ARG A 450     -41.104 -37.180 -12.827  1.00 26.09           O  
ANISOU 3116  O   ARG A 450     3255   3829   2830    -13   -264    405       O  
ATOM   3117  CB  ARG A 450     -38.902 -39.062 -13.125  1.00 28.32           C  
ANISOU 3117  CB  ARG A 450     3567   4222   2973    -66   -102    184       C  
ATOM   3118  CG  ARG A 450     -37.403 -39.500 -13.099  1.00 28.80           C  
ANISOU 3118  CG  ARG A 450     3638   4314   2991    -82    -20     90       C  
ATOM   3119  CD  ARG A 450     -37.047 -40.213 -14.456  1.00 32.61           C  
ANISOU 3119  CD  ARG A 450     4116   4930   3343   -184      0     20       C  
ATOM   3120  NE  ARG A 450     -36.754 -39.222 -15.478  1.00 39.22           N  
ANISOU 3120  NE  ARG A 450     4969   5858   4075   -280    -37    107       N  
ATOM   3121  CZ  ARG A 450     -37.433 -39.008 -16.619  1.00 46.24           C  
ANISOU 3121  CZ  ARG A 450     5860   6841   4868   -373   -100    171       C  
ATOM   3122  NH1 ARG A 450     -38.505 -39.721 -16.963  1.00 47.82           N  
ANISOU 3122  NH1 ARG A 450     6047   7061   5061   -382   -133    152       N  
ATOM   3123  NH2 ARG A 450     -36.995 -38.061 -17.449  1.00 48.51           N  
ANISOU 3123  NH2 ARG A 450     6163   7209   5060   -468   -135    261       N  
ATOM   3124  N   TRP A 451     -41.794 -38.480 -11.096  1.00 25.63           N  
ANISOU 3124  N   TRP A 451     3166   3677   2896    111   -191    284       N  
ATOM   3125  CA  TRP A 451     -43.193 -38.078 -11.251  1.00 27.95           C  
ANISOU 3125  CA  TRP A 451     3425   3951   3244    123   -265    356       C  
ATOM   3126  C   TRP A 451     -43.671 -37.312 -10.038  1.00 27.59           C  
ANISOU 3126  C   TRP A 451     3352   3804   3326    210   -267    377       C  
ATOM   3127  O   TRP A 451     -43.085 -37.419  -8.952  1.00 28.11           O  
ANISOU 3127  O   TRP A 451     3426   3823   3431    261   -202    320       O  
ATOM   3128  CB  TRP A 451     -44.119 -39.308 -11.461  1.00 24.81           C  
ANISOU 3128  CB  TRP A 451     3004   3588   2834    112   -268    307       C  
ATOM   3129  CG  TRP A 451     -44.059 -39.718 -12.868  1.00 23.80           C  
ANISOU 3129  CG  TRP A 451     2891   3563   2589     16   -298    311       C  
ATOM   3130  CD1 TRP A 451     -43.066 -40.440 -13.460  1.00 24.56           C  
ANISOU 3130  CD1 TRP A 451     3015   3732   2587    -41   -248    233       C  
ATOM   3131  CD2 TRP A 451     -45.012 -39.415 -13.892  1.00 26.77           C  
ANISOU 3131  CD2 TRP A 451     3250   3991   2930    -43   -387    393       C  
ATOM   3132  NE1 TRP A 451     -43.327 -40.592 -14.815  1.00 28.33           N  
ANISOU 3132  NE1 TRP A 451     3496   4313   2955   -139   -294    254       N  
ATOM   3133  CE2 TRP A 451     -44.516 -39.968 -15.099  1.00 29.70           C  
ANISOU 3133  CE2 TRP A 451     3646   4477   3162   -145   -384    360       C  
ATOM   3134  CE3 TRP A 451     -46.229 -38.712 -13.913  1.00 29.20           C  
ANISOU 3134  CE3 TRP A 451     3519   4261   3315    -23   -473    490       C  
ATOM   3135  CZ2 TRP A 451     -45.195 -39.849 -16.326  1.00 31.66           C  
ANISOU 3135  CZ2 TRP A 451     3888   4811   3329   -237   -466    428       C  
ATOM   3136  CZ3 TRP A 451     -46.914 -38.587 -15.148  1.00 30.06           C  
ANISOU 3136  CZ3 TRP A 451     3619   4444   3358   -108   -563    567       C  
ATOM   3137  CH2 TRP A 451     -46.398 -39.172 -16.326  1.00 32.44           C  
ANISOU 3137  CH2 TRP A 451     3952   4868   3505   -217   -559    538       C  
ATOM   3138  N   HIS A 452     -44.766 -36.554 -10.224  1.00 25.09           N  
ANISOU 3138  N   HIS A 452     2997   3457   3081    225   -343    454       N  
ATOM   3139  CA  HIS A 452     -45.512 -35.974  -9.113  1.00 24.69           C  
ANISOU 3139  CA  HIS A 452     2900   3318   3163    308   -343    451       C  
ATOM   3140  C   HIS A 452     -46.942 -36.504  -9.105  1.00 26.19           C  
ANISOU 3140  C   HIS A 452     3036   3516   3400    324   -373    450       C  
ATOM   3141  O   HIS A 452     -47.500 -36.842 -10.163  1.00 26.72           O  
ANISOU 3141  O   HIS A 452     3096   3639   3417    268   -432    493       O  
ATOM   3142  CB  HIS A 452     -45.648 -34.440  -9.223  1.00 27.53           C  
ANISOU 3142  CB  HIS A 452     3242   3610   3610    327   -413    539       C  
ATOM   3143  CG  HIS A 452     -44.478 -33.688  -8.680  1.00 26.91           C  
ANISOU 3143  CG  HIS A 452     3198   3486   3542    345   -377    529       C  
ATOM   3144  ND1 HIS A 452     -44.091 -32.469  -9.192  1.00 26.89           N  
ANISOU 3144  ND1 HIS A 452     3205   3447   3565    321   -443    618       N  
ATOM   3145  CD2 HIS A 452     -43.587 -33.995  -7.705  1.00 25.39           C  
ANISOU 3145  CD2 HIS A 452     3032   3279   3337    375   -288    449       C  
ATOM   3146  CE1 HIS A 452     -43.030 -32.035  -8.536  1.00 25.81           C  
ANISOU 3146  CE1 HIS A 452     3100   3274   3434    341   -392    587       C  
ATOM   3147  NE2 HIS A 452     -42.691 -32.954  -7.643  1.00 26.32           N  
ANISOU 3147  NE2 HIS A 452     3175   3355   3471    373   -298    484       N  
ATOM   3148  N   VAL A 453     -47.573 -36.484  -7.934  1.00 24.68           N  
ANISOU 3148  N   VAL A 453     2799   3272   3305    394   -337    404       N  
ATOM   3149  CA  VAL A 453     -49.024 -36.626  -7.854  1.00 27.78           C  
ANISOU 3149  CA  VAL A 453     3123   3659   3774    418   -374    414       C  
ATOM   3150  C   VAL A 453     -49.593 -35.302  -7.348  1.00 28.02           C  
ANISOU 3150  C   VAL A 453     3094   3606   3945    481   -410    443       C  
ATOM   3151  O   VAL A 453     -48.999 -34.643  -6.484  1.00 31.19           O  
ANISOU 3151  O   VAL A 453     3503   3955   4394    525   -366    407       O  
ATOM   3152  CB  VAL A 453     -49.436 -37.800  -6.951  1.00 29.89           C  
ANISOU 3152  CB  VAL A 453     3372   3948   4037    435   -304    331       C  
ATOM   3153  CG1 VAL A 453     -48.999 -37.509  -5.486  1.00 30.36           C  
ANISOU 3153  CG1 VAL A 453     3427   3962   4146    491   -225    266       C  
ATOM   3154  CG2 VAL A 453     -50.948 -37.901  -6.961  1.00 32.33           C  
ANISOU 3154  CG2 VAL A 453     3602   4259   4421    452   -345    346       C  
ATOM   3155  N   ALA A 454     -50.730 -34.921  -7.882  1.00 25.61           N  
ANISOU 3155  N   ALA A 454     2727   3287   3715    486   -492    501       N  
ATOM   3156  CA  ALA A 454     -51.427 -33.693  -7.533  1.00 27.11           C  
ANISOU 3156  CA  ALA A 454     2844   3390   4067    548   -542    527       C  
ATOM   3157  C   ALA A 454     -52.878 -34.041  -7.270  1.00 29.97           C  
ANISOU 3157  C   ALA A 454     3116   3757   4515    580   -555    504       C  
ATOM   3158  O   ALA A 454     -53.342 -35.092  -7.690  1.00 29.76           O  
ANISOU 3158  O   ALA A 454     3092   3801   4415    538   -557    504       O  
ATOM   3159  CB  ALA A 454     -51.388 -32.656  -8.656  1.00 27.93           C  
ANISOU 3159  CB  ALA A 454     2949   3458   4205    516   -663    652       C  
ATOM   3160  N   ARG A 455     -53.607 -33.133  -6.609  1.00 33.56           N  
ANISOU 3160  N   ARG A 455     3068   3988   5695    657  -1306    574       N  
ATOM   3161  CA  ARG A 455     -54.989 -33.428  -6.282  1.00 36.61           C  
ANISOU 3161  CA  ARG A 455     3291   4365   6253    681  -1324    588       C  
ATOM   3162  C   ARG A 455     -55.902 -33.267  -7.489  1.00 37.22           C  
ANISOU 3162  C   ARG A 455     3314   4417   6411    662  -1516    700       C  
ATOM   3163  O   ARG A 455     -56.645 -34.188  -7.841  1.00 37.49           O  
ANISOU 3163  O   ARG A 455     3296   4490   6459    616  -1591    726       O  
ATOM   3164  CB  ARG A 455     -55.481 -32.557  -5.117  1.00 40.75           C  
ANISOU 3164  CB  ARG A 455     3698   4828   6957    771  -1201    542       C  
ATOM   3165  CG  ARG A 455     -56.712 -33.190  -4.389  1.00 44.89           C  
ANISOU 3165  CG  ARG A 455     4062   5364   7628    787  -1152    515       C  
ATOM   3166  CD  ARG A 455     -57.066 -32.476  -3.079  1.00 48.43           C  
ANISOU 3166  CD  ARG A 455     4413   5762   8227    864   -991    445       C  
ATOM   3167  NE  ARG A 455     -57.166 -31.054  -3.372  1.00 51.30           N  
ANISOU 3167  NE  ARG A 455     4747   6033   8712    931  -1030    492       N  
ATOM   3168  CZ  ARG A 455     -58.294 -30.423  -3.640  1.00 52.66           C  
ANISOU 3168  CZ  ARG A 455     4781   6139   9089    980  -1097    552       C  
ATOM   3169  NH1 ARG A 455     -59.449 -31.078  -3.608  1.00 51.74           N  
ANISOU 3169  NH1 ARG A 455     4561   6047   9050    957  -1110    562       N  
ATOM   3170  NH2 ARG A 455     -58.252 -29.128  -3.954  1.00 54.95           N  
ANISOU 3170  NH2 ARG A 455     5088   6348   9441   1023  -1121    589       N  
ATOM   3171  N   LYS A 456     -55.864 -32.108  -8.138  1.00 34.14           N  
ANISOU 3171  N   LYS A 456     2936   3960   6074    692  -1604    773       N  
ATOM   3172  CA  LYS A 456     -56.764 -31.835  -9.243  1.00 35.20           C  
ANISOU 3172  CA  LYS A 456     3016   4063   6296    676  -1792    888       C  
ATOM   3173  C   LYS A 456     -56.220 -30.631  -9.989  1.00 38.38           C  
ANISOU 3173  C   LYS A 456     3510   4407   6666    685  -1857    949       C  
ATOM   3174  O   LYS A 456     -55.507 -29.822  -9.396  1.00 40.28           O  
ANISOU 3174  O   LYS A 456     3777   4605   6922    742  -1766    912       O  
ATOM   3175  CB  LYS A 456     -58.190 -31.522  -8.736  1.00 40.99           C  
ANISOU 3175  CB  LYS A 456     3582   4755   7238    724  -1754    889       C  
ATOM   3176  CG  LYS A 456     -58.260 -30.184  -7.991  1.00 42.86           C  
ANISOU 3176  CG  LYS A 456     3760   4906   7621    818  -1653    865       C  
ATOM   3177  CD  LYS A 456     -59.721 -29.823  -7.677  1.00 48.80           C  
ANISOU 3177  CD  LYS A 456     4355   5611   8575    857  -1633    877       C  
ATOM   3178  CE  LYS A 456     -59.863 -28.465  -6.986  1.00 51.56           C  
ANISOU 3178  CE  LYS A 456     4649   5868   9074    946  -1532    852       C  
ATOM   3179  NZ  LYS A 456     -61.285 -28.345  -6.529  1.00 53.84           N  
ANISOU 3179  NZ  LYS A 456     4779   6122   9554    979  -1491    847       N  
ATOM   3180  N   PRO A 457     -56.496 -30.501 -11.274  1.00 38.93           N  
ANISOU 3180  N   PRO A 457     3643   4473   6677    620  -2003   1037       N  
ATOM   3181  CA  PRO A 457     -56.182 -29.253 -11.962  1.00 44.56           C  
ANISOU 3181  CA  PRO A 457     4423   5120   7387    630  -2065   1103       C  
ATOM   3182  C   PRO A 457     -57.159 -28.169 -11.523  1.00 49.56           C  
ANISOU 3182  C   PRO A 457     4923   5668   8240    711  -2035   1120       C  
ATOM   3183  O   PRO A 457     -58.307 -28.453 -11.179  1.00 49.96           O  
ANISOU 3183  O   PRO A 457     4841   5715   8426    729  -2022   1114       O  
ATOM   3184  CB  PRO A 457     -56.369 -29.619 -13.443  1.00 43.84           C  
ANISOU 3184  CB  PRO A 457     4426   5058   7173    526  -2227   1186       C  
ATOM   3185  CG  PRO A 457     -57.371 -30.722 -13.415  1.00 43.05           C  
ANISOU 3185  CG  PRO A 457     4240   5007   7111    489  -2254   1178       C  
ATOM   3186  CD  PRO A 457     -57.143 -31.486 -12.153  1.00 41.54           C  
ANISOU 3186  CD  PRO A 457     3985   4857   6942    531  -2117   1080       C  
ATOM   3187  N   LEU A 458     -56.703 -26.914 -11.534  1.00 54.56           N  
ANISOU 3187  N   LEU A 458     5591   6228   8911    757  -2019   1140       N  
ATOM   3188  CA  LEU A 458     -57.615 -25.805 -11.228  1.00 60.77           C  
ANISOU 3188  CA  LEU A 458     6261   6924   9903    829  -1998   1161       C  
ATOM   3189  C   LEU A 458     -58.674 -25.628 -12.299  1.00 66.50           C  
ANISOU 3189  C   LEU A 458     6951   7629  10689    786  -2149   1262       C  
ATOM   3190  O   LEU A 458     -59.872 -25.483 -12.000  1.00 69.60           O  
ANISOU 3190  O   LEU A 458     7202   7987  11256    822  -2143   1270       O  
ATOM   3191  CB  LEU A 458     -56.849 -24.507 -11.078  1.00 64.27           C  
ANISOU 3191  CB  LEU A 458     6764   7293  10364    880  -1957   1163       C  
ATOM   3192  CG  LEU A 458     -56.245 -24.363  -9.700  1.00 65.82           C  
ANISOU 3192  CG  LEU A 458     6935   7475  10598    953  -1778   1056       C  
ATOM   3193  CD1 LEU A 458     -56.177 -22.871  -9.423  1.00 68.64           C  
ANISOU 3193  CD1 LEU A 458     7281   7728  11073   1022  -1732   1061       C  
ATOM   3194  CD2 LEU A 458     -57.052 -25.123  -8.642  1.00 65.57           C  
ANISOU 3194  CD2 LEU A 458     6768   7474  10671    985  -1669    978       C  
ATOM   3195  N   ASP A 459     -58.252 -25.556 -13.549  1.00 68.25           N  
ANISOU 3195  N   ASP A 459     7298   7863  10772    709  -2283   1339       N  
ATOM   3196  CA  ASP A 459     -59.174 -25.451 -14.675  1.00 69.79           C  
ANISOU 3196  CA  ASP A 459     7477   8041  10999    652  -2439   1439       C  
ATOM   3197  C   ASP A 459     -58.895 -26.612 -15.618  1.00 69.37           C  
ANISOU 3197  C   ASP A 459     7534   8074  10748    538  -2536   1462       C  
ATOM   3198  O   ASP A 459     -57.970 -26.543 -16.430  1.00 66.31           O  
ANISOU 3198  O   ASP A 459     7303   7706  10187    475  -2591   1491       O  
ATOM   3199  CB  ASP A 459     -59.026 -24.127 -15.406  1.00 72.16           C  
ANISOU 3199  CB  ASP A 459     7830   8262  11327    658  -2518   1520       C  
ATOM   3200  CG  ASP A 459     -60.033 -23.991 -16.544  1.00 76.64           C  
ANISOU 3200  CG  ASP A 459     8373   8807  11941    599  -2683   1627       C  
ATOM   3201  OD1 ASP A 459     -61.196 -23.651 -16.238  1.00 76.62           O  
ANISOU 3201  OD1 ASP A 459     8220   8754  12137    648  -2689   1647       O  
ATOM   3202  OD2 ASP A 459     -59.668 -24.256 -17.723  1.00 79.08           O  
ANISOU 3202  OD2 ASP A 459     8813   9149  12086    500  -2802   1688       O  
ATOM   3203  N   VAL A 460     -59.712 -27.663 -15.531  1.00 73.96           N  
ANISOU 3203  N   VAL A 460     8040   8705  11355    508  -2553   1448       N  
ATOM   3204  CA  VAL A 460     -59.505 -28.847 -16.363  1.00 78.96           C  
ANISOU 3204  CA  VAL A 460     8776   9420  11806    398  -2634   1459       C  
ATOM   3205  C   VAL A 460     -59.545 -28.497 -17.860  1.00 84.38           C  
ANISOU 3205  C   VAL A 460     9573  10091  12398    307  -2794   1560       C  
ATOM   3206  O   VAL A 460     -58.898 -29.168 -18.679  1.00 84.65           O  
ANISOU 3206  O   VAL A 460     9752  10180  12231    211  -2846   1566       O  
ATOM   3207  CB  VAL A 460     -60.545 -29.922 -15.965  1.00 80.52           C  
ANISOU 3207  CB  VAL A 460     8853   9660  12082    387  -2626   1432       C  
ATOM   3208  CG1 VAL A 460     -61.946 -29.299 -15.885  1.00 82.28           C  
ANISOU 3208  CG1 VAL A 460     8915   9816  12531    432  -2667   1485       C  
ATOM   3209  CG2 VAL A 460     -60.522 -31.121 -16.920  1.00 80.64           C  
ANISOU 3209  CG2 VAL A 460     8967   9748  11925    266  -2723   1451       C  
ATOM   3210  N   TYR A 461     -60.245 -27.412 -18.238  1.00 87.71           N  
ANISOU 3210  N   TYR A 461     9934  10434  12959    335  -2868   1638       N  
ATOM   3211  CA  TYR A 461     -60.468 -27.082 -19.648  1.00 90.67           C  
ANISOU 3211  CA  TYR A 461    10394  10788  13266    246  -3029   1742       C  
ATOM   3212  C   TYR A 461     -59.347 -26.271 -20.325  1.00 88.77           C  
ANISOU 3212  C   TYR A 461    10315  10526  12889    215  -3054   1774       C  
ATOM   3213  O   TYR A 461     -59.208 -26.367 -21.549  1.00 89.22           O  
ANISOU 3213  O   TYR A 461    10492  10596  12811    112  -3170   1838       O  
ATOM   3214  CB  TYR A 461     -61.817 -26.354 -19.793  1.00 96.05           C  
ANISOU 3214  CB  TYR A 461    10932  11396  14168    282  -3111   1819       C  
ATOM   3215  CG  TYR A 461     -62.965 -27.269 -19.446  1.00 98.77           C  
ANISOU 3215  CG  TYR A 461    11141  11769  14618    280  -3117   1804       C  
ATOM   3216  CD1 TYR A 461     -63.389 -28.239 -20.343  1.00100.37           C  
ANISOU 3216  CD1 TYR A 461    11392  12024  14720    172  -3230   1842       C  
ATOM   3217  CD2 TYR A 461     -63.590 -27.205 -18.202  1.00 99.58           C  
ANISOU 3217  CD2 TYR A 461    11076  11850  14911    381  -3002   1746       C  
ATOM   3218  CE1 TYR A 461     -64.425 -29.114 -20.022  1.00101.88           C  
ANISOU 3218  CE1 TYR A 461    11462  12243  15004    166  -3236   1828       C  
ATOM   3219  CE2 TYR A 461     -64.633 -28.076 -17.873  1.00100.84           C  
ANISOU 3219  CE2 TYR A 461    11113  12038  15164    374  -3002   1731       C  
ATOM   3220  CZ  TYR A 461     -65.043 -29.031 -18.790  1.00101.60           C  
ANISOU 3220  CZ  TYR A 461    11256  12186  15161    267  -3123   1774       C  
ATOM   3221  OH  TYR A 461     -66.069 -29.906 -18.496  1.00101.75           O  
ANISOU 3221  OH  TYR A 461    11158  12234  15269    255  -3127   1762       O  
ATOM   3222  N   LYS A 462     -58.522 -25.517 -19.591  1.00 85.93           N  
ANISOU 3222  N   LYS A 462     9968  10133  12549    293  -2946   1731       N  
ATOM   3223  CA  LYS A 462     -57.559 -24.608 -20.216  1.00 85.04           C  
ANISOU 3223  CA  LYS A 462     9992   9986  12331    269  -2973   1770       C  
ATOM   3224  C   LYS A 462     -56.459 -25.342 -21.010  1.00 84.37           C  
ANISOU 3224  C   LYS A 462    10099   9975  11981    160  -2989   1756       C  
ATOM   3225  O   LYS A 462     -56.142 -26.516 -20.779  1.00 81.62           O  
ANISOU 3225  O   LYS A 462     9783   9703  11524    126  -2940   1690       O  
ATOM   3226  CB  LYS A 462     -56.916 -23.715 -19.156  1.00 83.41           C  
ANISOU 3226  CB  LYS A 462     9754   9730  12209    377  -2843   1718       C  
ATOM   3227  N   LYS A 463     -55.821 -24.587 -21.907  1.00 87.34           N  
ANISOU 3227  N   LYS A 463    10606  10323  12255    108  -3048   1814       N  
ATOM   3228  CA  LYS A 463     -55.006 -25.110 -23.009  1.00 90.33           C  
ANISOU 3228  CA  LYS A 463    11174  10757  12391    -18  -3094   1826       C  
ATOM   3229  C   LYS A 463     -53.588 -25.452 -22.537  1.00 93.18           C  
ANISOU 3229  C   LYS A 463    11642  11164  12598    -15  -2969   1741       C  
ATOM   3230  O   LYS A 463     -53.238 -25.280 -21.358  1.00 92.50           O  
ANISOU 3230  O   LYS A 463    11486  11067  12592     83  -2854   1678       O  
ATOM   3231  CB  LYS A 463     -55.002 -24.083 -24.143  1.00 90.55           C  
ANISOU 3231  CB  LYS A 463    11286  10729  12392    -75  -3208   1926       C  
ATOM   3232  N   PRO A 464     -52.698 -25.967 -23.467  1.00 95.58           N  
ANISOU 3232  N   PRO A 464    12126  11521  12670   -128  -2982   1736       N  
ATOM   3233  CA  PRO A 464     -51.331 -26.338 -23.045  1.00 93.57           C  
ANISOU 3233  CA  PRO A 464    11975  11311  12268   -131  -2860   1656       C  
ATOM   3234  C   PRO A 464     -50.300 -25.220 -23.175  1.00 91.89           C  
ANISOU 3234  C   PRO A 464    11857  11054  12004   -120  -2825   1675       C  
ATOM   3235  O   PRO A 464     -49.823 -24.923 -24.280  1.00 93.40           O  
ANISOU 3235  O   PRO A 464    12187  11243  12057   -214  -2877   1720       O  
ATOM   3236  CB  PRO A 464     -50.990 -27.505 -23.986  1.00 94.75           C  
ANISOU 3236  CB  PRO A 464    12261  11536  12205   -260  -2883   1634       C  
ATOM   3237  CG  PRO A 464     -51.689 -27.157 -25.249  1.00 96.61           C  
ANISOU 3237  CG  PRO A 464    12537  11743  12426   -344  -3024   1728       C  
ATOM   3238  CD  PRO A 464     -52.967 -26.431 -24.847  1.00 97.47           C  
ANISOU 3238  CD  PRO A 464    12472  11786  12777   -260  -3096   1789       C  
ATOM   3239  N   SER A 465     -49.911 -24.620 -22.041  1.00 87.50           N  
ANISOU 3239  N   SER A 465    11232  10462  11553    -12  -2731   1637       N  
ATOM   3240  CA  SER A 465     -49.025 -23.464 -22.093  1.00 82.67           C  
ANISOU 3240  CA  SER A 465    10697   9796  10918      5  -2700   1660       C  
ATOM   3241  C   SER A 465     -47.552 -23.840 -22.135  1.00 76.64           C  
ANISOU 3241  C   SER A 465    10083   9082   9955    -44  -2609   1603       C  
ATOM   3242  O   SER A 465     -46.743 -23.095 -22.701  1.00 76.02           O  
ANISOU 3242  O   SER A 465    10121   8978   9785    -86  -2607   1634       O  
ATOM   3243  CB  SER A 465     -49.267 -22.555 -20.904  1.00 82.74           C  
ANISOU 3243  CB  SER A 465    10572   9732  11134    139  -2639   1646       C  
ATOM   3244  OG  SER A 465     -48.026 -22.029 -20.481  1.00 82.95           O  
ANISOU 3244  OG  SER A 465    10681   9742  11096    162  -2547   1612       O  
ATOM   3245  N   GLY A 466     -47.166 -24.958 -21.533  1.00 72.27           N  
ANISOU 3245  N   GLY A 466     9529   8597   9334    -41  -2528   1520       N  
ATOM   3246  CA  GLY A 466     -45.772 -25.334 -21.612  1.00 68.63           C  
ANISOU 3246  CA  GLY A 466     9210   8182   8685    -93  -2440   1467       C  
ATOM   3247  C   GLY A 466     -44.881 -24.547 -20.688  1.00 65.26           C  
ANISOU 3247  C   GLY A 466     8782   7714   8300    -15  -2347   1439       C  
ATOM   3248  O   GLY A 466     -43.675 -24.424 -20.943  1.00 65.66           O  
ANISOU 3248  O   GLY A 466     8964   7779   8204    -63  -2287   1420       O  
ATOM   3249  N   LYS A 467     -45.438 -23.984 -19.629  1.00 60.82           N  
ANISOU 3249  N   LYS A 467     8077   7095   7938    102  -2325   1433       N  
ATOM   3250  CA  LYS A 467     -44.650 -23.227 -18.675  1.00 57.32           C  
ANISOU 3250  CA  LYS A 467     7622   6612   7547    174  -2200   1379       C  
ATOM   3251  C   LYS A 467     -44.407 -24.105 -17.460  1.00 52.11           C  
ANISOU 3251  C   LYS A 467     6887   6010   6901    223  -2037   1246       C  
ATOM   3252  O   LYS A 467     -45.358 -24.625 -16.866  1.00 53.41           O  
ANISOU 3252  O   LYS A 467     6925   6185   7185    273  -2042   1225       O  
ATOM   3253  CB  LYS A 467     -45.349 -21.934 -18.271  1.00 60.29           C  
ANISOU 3253  CB  LYS A 467     7895   6879   8134    268  -2250   1441       C  
ATOM   3254  CG  LYS A 467     -44.601 -20.632 -18.683  1.00 60.99           C  
ANISOU 3254  CG  LYS A 467     8081   6895   8196    256  -2259   1495       C  
ATOM   3255  CD  LYS A 467     -45.569 -19.472 -18.712  1.00 60.95           C  
ANISOU 3255  CD  LYS A 467     7979   6797   8384    316  -2319   1558       C  
ATOM   3256  CE  LYS A 467     -45.005 -18.294 -19.461  1.00 62.34           C  
ANISOU 3256  CE  LYS A 467     8260   6912   8512    276  -2355   1624       C  
ATOM   3257  NZ  LYS A 467     -44.321 -17.368 -18.534  1.00 61.76           N  
ANISOU 3257  NZ  LYS A 467     8183   6766   8519    352  -2261   1593       N  
ATOM   3258  N   CYS A 468     -43.141 -24.267 -17.096  1.00 44.98           N  
ANISOU 3258  N   CYS A 468     6063   5145   5881    203  -1896   1162       N  
ATOM   3259  CA  CYS A 468     -42.816 -25.011 -15.903  1.00 42.12           C  
ANISOU 3259  CA  CYS A 468     5639   4833   5533    247  -1743   1042       C  
ATOM   3260  C   CYS A 468     -41.678 -24.274 -15.220  1.00 38.48           C  
ANISOU 3260  C   CYS A 468     5215   4350   5056    275  -1613    985       C  
ATOM   3261  O   CYS A 468     -40.689 -23.923 -15.866  1.00 37.74           O  
ANISOU 3261  O   CYS A 468     5243   4258   4839    215  -1603   1001       O  
ATOM   3262  CB  CYS A 468     -42.446 -26.466 -16.222  1.00 40.46           C  
ANISOU 3262  CB  CYS A 468     5485   4717   5170    175  -1710    988       C  
ATOM   3263  SG  CYS A 468     -42.435 -27.425 -14.684  1.00 44.36           S  
ANISOU 3263  SG  CYS A 468     5870   5262   5722    240  -1556    861       S  
ATOM   3264  N   PHE A 469     -41.838 -23.986 -13.930  1.00 33.13           N  
ANISOU 3264  N   PHE A 469     4436   3648   4505    360  -1517    920       N  
ATOM   3265  CA  PHE A 469     -40.827 -23.231 -13.217  1.00 32.33           C  
ANISOU 3265  CA  PHE A 469     4365   3520   4399    385  -1401    867       C  
ATOM   3266  C   PHE A 469     -39.978 -24.096 -12.299  1.00 31.71           C  
ANISOU 3266  C   PHE A 469     4289   3514   4247    381  -1255    754       C  
ATOM   3267  O   PHE A 469     -39.301 -23.566 -11.407  1.00 28.98           O  
ANISOU 3267  O   PHE A 469     3939   3150   3924    413  -1151    697       O  
ATOM   3268  CB  PHE A 469     -41.492 -22.096 -12.449  1.00 32.88           C  
ANISOU 3268  CB  PHE A 469     4339   3497   4657    475  -1394    877       C  
ATOM   3269  CG  PHE A 469     -42.096 -21.059 -13.359  1.00 33.65           C  
ANISOU 3269  CG  PHE A 469     4448   3509   4829    479  -1534    994       C  
ATOM   3270  CD1 PHE A 469     -41.330 -19.959 -13.782  1.00 32.95           C  
ANISOU 3270  CD1 PHE A 469     4451   3363   4704    458  -1542   1036       C  
ATOM   3271  CD2 PHE A 469     -43.393 -21.175 -13.802  1.00 34.55           C  
ANISOU 3271  CD2 PHE A 469     4481   3599   5049    500  -1660   1068       C  
ATOM   3272  CE1 PHE A 469     -41.884 -18.988 -14.645  1.00 34.76           C  
ANISOU 3272  CE1 PHE A 469     4696   3509   5004    459  -1680   1153       C  
ATOM   3273  CE2 PHE A 469     -43.947 -20.217 -14.646  1.00 36.54           C  
ANISOU 3273  CE2 PHE A 469     4741   3768   5375    503  -1800   1186       C  
ATOM   3274  CZ  PHE A 469     -43.187 -19.124 -15.088  1.00 36.08           C  
ANISOU 3274  CZ  PHE A 469     4781   3650   5277    481  -1812   1231       C  
ATOM   3275  N   PHE A 470     -39.982 -25.425 -12.483  1.00 27.10           N  
ANISOU 3275  N   PHE A 470     3712   3009   3575    341  -1247    722       N  
ATOM   3276  CA  PHE A 470     -39.102 -26.258 -11.651  1.00 25.85           C  
ANISOU 3276  CA  PHE A 470     3561   2915   3347    335  -1115    624       C  
ATOM   3277  C   PHE A 470     -38.693 -27.447 -12.483  1.00 29.22           C  
ANISOU 3277  C   PHE A 470     4061   3413   3627    258  -1129    618       C  
ATOM   3278  O   PHE A 470     -39.402 -27.818 -13.426  1.00 26.25           O  
ANISOU 3278  O   PHE A 470     3702   3044   3228    221  -1236    675       O  
ATOM   3279  CB  PHE A 470     -39.754 -26.775 -10.354  1.00 30.49           C  
ANISOU 3279  CB  PHE A 470     4030   3518   4038    399  -1047    557       C  
ATOM   3280  CG  PHE A 470     -41.012 -27.615 -10.591  1.00 31.90           C  
ANISOU 3280  CG  PHE A 470     4135   3717   4269    403  -1123    581       C  
ATOM   3281  CD1 PHE A 470     -40.918 -28.999 -10.793  1.00 30.64           C  
ANISOU 3281  CD1 PHE A 470     3994   3632   4016    357  -1113    549       C  
ATOM   3282  CD2 PHE A 470     -42.280 -27.003 -10.616  1.00 32.85           C  
ANISOU 3282  CD2 PHE A 470     4164   3779   4539    453  -1206    637       C  
ATOM   3283  CE1 PHE A 470     -42.057 -29.755 -11.004  1.00 30.41           C  
ANISOU 3283  CE1 PHE A 470     3899   3620   4033    355  -1184    571       C  
ATOM   3284  CE2 PHE A 470     -43.453 -27.751 -10.845  1.00 31.49           C  
ANISOU 3284  CE2 PHE A 470     3916   3625   4423    454  -1282    664       C  
ATOM   3285  CZ  PHE A 470     -43.334 -29.127 -11.025  1.00 30.26           C  
ANISOU 3285  CZ  PHE A 470     3785   3547   4166    402  -1271    630       C  
ATOM   3286  N   GLN A 471     -37.529 -28.023 -12.146  1.00 26.87           N  
ANISOU 3286  N   GLN A 471     3811   3165   3233    232  -1022    548       N  
ATOM   3287  CA  GLN A 471     -37.009 -29.185 -12.861  1.00 24.77           C  
ANISOU 3287  CA  GLN A 471     3618   2963   2833    162  -1011    529       C  
ATOM   3288  C   GLN A 471     -36.494 -30.275 -11.950  1.00 23.27           C  
ANISOU 3288  C   GLN A 471     3393   2828   2621    173   -902    441       C  
ATOM   3289  O   GLN A 471     -36.195 -31.358 -12.461  1.00 26.77           O  
ANISOU 3289  O   GLN A 471     3882   3319   2971    123   -890    419       O  
ATOM   3290  CB  GLN A 471     -35.843 -28.811 -13.812  1.00 28.08           C  
ANISOU 3290  CB  GLN A 471     4162   3382   3124     92   -997    548       C  
ATOM   3291  CG  GLN A 471     -36.222 -27.791 -14.854  1.00 37.66           C  
ANISOU 3291  CG  GLN A 471     5433   4543   4332     63  -1109    643       C  
ATOM   3292  CD  GLN A 471     -36.921 -28.451 -16.025  1.00 50.04           C  
ANISOU 3292  CD  GLN A 471     7049   6131   5831      0  -1218    694       C  
ATOM   3293  OE1 GLN A 471     -38.054 -28.063 -16.394  1.00 56.45           O  
ANISOU 3293  OE1 GLN A 471     7826   6907   6716     13  -1341    767       O  
ATOM   3294  NE2 GLN A 471     -36.247 -29.440 -16.650  1.00 50.67           N  
ANISOU 3294  NE2 GLN A 471     7213   6266   5773    -72  -1177    659       N  
ATOM   3295  N   GLY A 472     -36.462 -30.085 -10.637  1.00 22.70           N  
ANISOU 3295  N   GLY A 472     3243   2750   2633    234   -827    392       N  
ATOM   3296  CA  GLY A 472     -35.991 -31.151  -9.735  1.00 22.26           C  
ANISOU 3296  CA  GLY A 472     3155   2745   2556    242   -732    316       C  
ATOM   3297  C   GLY A 472     -36.898 -31.297  -8.512  1.00 25.14           C  
ANISOU 3297  C   GLY A 472     3411   3106   3036    304   -709    285       C  
ATOM   3298  O   GLY A 472     -37.561 -30.339  -8.063  1.00 25.31           O  
ANISOU 3298  O   GLY A 472     3377   3077   3161    353   -727    303       O  
ATOM   3299  N   ASP A 473     -36.897 -32.493  -7.940  1.00 22.81           N  
ANISOU 3299  N   ASP A 473     3084   2859   2723    302   -660    235       N  
ATOM   3300  CA  ASP A 473     -37.573 -32.680  -6.658  1.00 22.83           C  
ANISOU 3300  CA  ASP A 473     2991   2863   2819    353   -616    196       C  
ATOM   3301  C   ASP A 473     -37.090 -33.983  -6.029  1.00 20.93           C  
ANISOU 3301  C   ASP A 473     2746   2678   2529    337   -547    140       C  
ATOM   3302  O   ASP A 473     -36.394 -34.783  -6.655  1.00 22.12           O  
ANISOU 3302  O   ASP A 473     2955   2861   2588    293   -541    133       O  
ATOM   3303  CB  ASP A 473     -39.105 -32.665  -6.843  1.00 23.84           C  
ANISOU 3303  CB  ASP A 473     3045   2970   3044    378   -695    234       C  
ATOM   3304  CG  ASP A 473     -39.867 -32.336  -5.533  1.00 25.69           C  
ANISOU 3304  CG  ASP A 473     3178   3182   3400    439   -644    201       C  
ATOM   3305  OD1 ASP A 473     -39.197 -32.051  -4.466  1.00 26.00           O  
ANISOU 3305  OD1 ASP A 473     3217   3222   3441    457   -550    149       O  
ATOM   3306  OD2 ASP A 473     -41.128 -32.371  -5.582  1.00 23.61           O  
ANISOU 3306  OD2 ASP A 473     2839   2902   3230    463   -696    226       O  
ATOM   3307  N   HIS A 474     -37.440 -34.164  -4.752  1.00 23.31           N  
ANISOU 3307  N   HIS A 474     2978   2987   2894    372   -489     99       N  
ATOM   3308  CA  HIS A 474     -36.979 -35.282  -3.925  1.00 20.91           C  
ANISOU 3308  CA  HIS A 474     2663   2728   2554    362   -421     48       C  
ATOM   3309  C   HIS A 474     -38.150 -35.695  -3.004  1.00 23.95           C  
ANISOU 3309  C   HIS A 474     2959   3117   3023    391   -407     29       C  
ATOM   3310  O   HIS A 474     -39.115 -34.944  -2.825  1.00 23.08           O  
ANISOU 3310  O   HIS A 474     2794   2971   3004    426   -429     44       O  
ATOM   3311  CB  HIS A 474     -35.724 -34.898  -3.117  1.00 19.82           C  
ANISOU 3311  CB  HIS A 474     2553   2594   2383    362   -343     13       C  
ATOM   3312  CG  HIS A 474     -35.907 -33.674  -2.285  1.00 20.28           C  
ANISOU 3312  CG  HIS A 474     2582   2612   2509    398   -314      3       C  
ATOM   3313  ND1 HIS A 474     -36.399 -33.713  -1.002  1.00 21.86           N  
ANISOU 3313  ND1 HIS A 474     2726   2813   2766    423   -261    -36       N  
ATOM   3314  CD2 HIS A 474     -35.734 -32.356  -2.590  1.00 19.06           C  
ANISOU 3314  CD2 HIS A 474     2452   2410   2379    410   -330     26       C  
ATOM   3315  CE1 HIS A 474     -36.485 -32.472  -0.533  1.00 23.83           C  
ANISOU 3315  CE1 HIS A 474     2968   3017   3070    449   -239    -42       C  
ATOM   3316  NE2 HIS A 474     -36.101 -31.643  -1.491  1.00 20.82           N  
ANISOU 3316  NE2 HIS A 474     2633   2605   2674    444   -284     -3       N  
ATOM   3317  N   GLY A 475     -38.071 -36.887  -2.430  1.00 23.77           N  
ANISOU 3317  N   GLY A 475     2922   3135   2974    377   -368     -4       N  
ATOM   3318  CA  GLY A 475     -39.142 -37.356  -1.547  1.00 24.08           C  
ANISOU 3318  CA  GLY A 475     2883   3183   3085    396   -347    -24       C  
ATOM   3319  C   GLY A 475     -39.460 -38.835  -1.794  1.00 27.08           C  
ANISOU 3319  C   GLY A 475     3256   3600   3432    366   -364    -28       C  
ATOM   3320  O   GLY A 475     -40.073 -39.486  -0.947  1.00 27.53           O  
ANISOU 3320  O   GLY A 475     3259   3673   3526    370   -331    -51       O  
ATOM   3321  N   PHE A 476     -38.998 -39.375  -2.929  1.00 20.50           N  
ANISOU 3321  N   PHE A 476     2483   2778   2526    330   -408     -8       N  
ATOM   3322  CA  PHE A 476     -39.237 -40.742  -3.372  1.00 19.60           C  
ANISOU 3322  CA  PHE A 476     2379   2692   2375    295   -430    -12       C  
ATOM   3323  C   PHE A 476     -38.639 -41.775  -2.394  1.00 21.43           C  
ANISOU 3323  C   PHE A 476     2610   2953   2581    287   -356    -53       C  
ATOM   3324  O   PHE A 476     -37.775 -41.475  -1.570  1.00 21.71           O  
ANISOU 3324  O   PHE A 476     2656   2992   2604    299   -296    -75       O  
ATOM   3325  CB  PHE A 476     -38.589 -40.938  -4.766  1.00 20.11           C  
ANISOU 3325  CB  PHE A 476     2530   2758   2354    254   -473      8       C  
ATOM   3326  CG  PHE A 476     -39.124 -39.978  -5.800  1.00 22.94           C  
ANISOU 3326  CG  PHE A 476     2902   3089   2726    251   -557     58       C  
ATOM   3327  CD1 PHE A 476     -40.434 -40.069  -6.229  1.00 20.32           C  
ANISOU 3327  CD1 PHE A 476     2523   2749   2448    248   -636     91       C  
ATOM   3328  CD2 PHE A 476     -38.304 -38.969  -6.308  1.00 21.46           C  
ANISOU 3328  CD2 PHE A 476     2773   2881   2501    250   -558     76       C  
ATOM   3329  CE1 PHE A 476     -40.955 -39.190  -7.204  1.00 22.23           C  
ANISOU 3329  CE1 PHE A 476     2778   2963   2707    243   -727    147       C  
ATOM   3330  CE2 PHE A 476     -38.816 -38.058  -7.273  1.00 20.31           C  
ANISOU 3330  CE2 PHE A 476     2645   2705   2367    244   -643    130       C  
ATOM   3331  CZ  PHE A 476     -40.115 -38.160  -7.726  1.00 21.85           C  
ANISOU 3331  CZ  PHE A 476     2796   2892   2616    241   -731    168       C  
ATOM   3332  N   ASP A 477     -39.048 -43.030  -2.590  1.00 22.91           N  
ANISOU 3332  N   ASP A 477     2792   3159   2754    260   -370    -59       N  
ATOM   3333  CA  ASP A 477     -38.494 -44.241  -1.977  1.00 23.49           C  
ANISOU 3333  CA  ASP A 477     2876   3254   2796    244   -318    -88       C  
ATOM   3334  C   ASP A 477     -36.977 -44.097  -1.775  1.00 22.77           C  
ANISOU 3334  C   ASP A 477     2836   3164   2652    244   -267   -103       C  
ATOM   3335  O   ASP A 477     -36.256 -43.700  -2.708  1.00 22.22           O  
ANISOU 3335  O   ASP A 477     2821   3085   2536    234   -281    -94       O  
ATOM   3336  CB  ASP A 477     -38.869 -45.434  -2.912  1.00 24.23           C  
ANISOU 3336  CB  ASP A 477     2994   3354   2857    204   -361    -84       C  
ATOM   3337  CG  ASP A 477     -38.353 -46.808  -2.423  1.00 25.70           C  
ANISOU 3337  CG  ASP A 477     3194   3553   3017    185   -314   -112       C  
ATOM   3338  OD1 ASP A 477     -37.438 -46.875  -1.531  1.00 25.03           O  
ANISOU 3338  OD1 ASP A 477     3112   3473   2923    199   -254   -128       O  
ATOM   3339  OD2 ASP A 477     -38.912 -47.836  -2.933  1.00 25.32           O  
ANISOU 3339  OD2 ASP A 477     3152   3508   2960    154   -343   -113       O  
ATOM   3340  N   ASN A 478     -36.470 -44.382  -0.567  1.00 23.07           N  
ANISOU 3340  N   ASN A 478     2856   3214   2696    253   -209   -124       N  
ATOM   3341  CA  ASN A 478     -35.080 -44.071  -0.267  1.00 22.45           C  
ANISOU 3341  CA  ASN A 478     2811   3135   2582    256   -168   -132       C  
ATOM   3342  C   ASN A 478     -34.119 -45.076  -0.883  1.00 27.12           C  
ANISOU 3342  C   ASN A 478     3447   3729   3126    233   -155   -139       C  
ATOM   3343  O   ASN A 478     -32.904 -44.940  -0.697  1.00 27.95           O  
ANISOU 3343  O   ASN A 478     3575   3835   3211    234   -121   -144       O  
ATOM   3344  CB  ASN A 478     -34.830 -43.968   1.273  1.00 22.45           C  
ANISOU 3344  CB  ASN A 478     2781   3146   2601    265   -119   -148       C  
ATOM   3345  CG  ASN A 478     -35.093 -45.271   2.021  1.00 23.39           C  
ANISOU 3345  CG  ASN A 478     2879   3282   2725    251   -100   -156       C  
ATOM   3346  OD1 ASN A 478     -35.879 -46.111   1.561  1.00 23.47           O  
ANISOU 3346  OD1 ASN A 478     2878   3294   2745    239   -125   -154       O  
ATOM   3347  ND2 ASN A 478     -34.479 -45.424   3.204  1.00 21.33           N  
ANISOU 3347  ND2 ASN A 478     2614   3031   2457    246    -61   -164       N  
ATOM   3348  N   LYS A 479     -34.579 -46.038  -1.680  1.00 26.89           N  
ANISOU 3348  N   LYS A 479     3435   3700   3084    211   -181   -140       N  
ATOM   3349  CA  LYS A 479     -33.550 -46.818  -2.350  1.00 29.06           C  
ANISOU 3349  CA  LYS A 479     3757   3968   3315    192   -157   -152       C  
ATOM   3350  C   LYS A 479     -33.308 -46.378  -3.788  1.00 29.41           C  
ANISOU 3350  C   LYS A 479     3862   4001   3313    171   -180   -146       C  
ATOM   3351  O   LYS A 479     -32.470 -46.956  -4.455  1.00 29.27           O  
ANISOU 3351  O   LYS A 479     3888   3974   3258    152   -152   -161       O  
ATOM   3352  CB  LYS A 479     -33.861 -48.309  -2.299  1.00 28.07           C  
ANISOU 3352  CB  LYS A 479     3629   3843   3195    174   -152   -165       C  
ATOM   3353  CG  LYS A 479     -34.936 -48.804  -3.156  1.00 30.72           C  
ANISOU 3353  CG  LYS A 479     3976   4175   3521    148   -200   -163       C  
ATOM   3354  CD  LYS A 479     -34.858 -50.351  -2.933  1.00 34.35           C  
ANISOU 3354  CD  LYS A 479     4439   4628   3985    130   -176   -182       C  
ATOM   3355  CE  LYS A 479     -35.940 -51.134  -3.598  1.00 36.62           C  
ANISOU 3355  CE  LYS A 479     4735   4911   4267     97   -220   -184       C  
ATOM   3356  NZ  LYS A 479     -35.660 -51.273  -5.033  1.00 39.31           N  
ANISOU 3356  NZ  LYS A 479     5148   5238   4550     63   -236   -195       N  
ATOM   3357  N   VAL A 480     -34.018 -45.362  -4.252  1.00 27.53           N  
ANISOU 3357  N   VAL A 480     3624   3759   3078    174   -229   -124       N  
ATOM   3358  CA  VAL A 480     -33.828 -44.805  -5.590  1.00 25.95           C  
ANISOU 3358  CA  VAL A 480     3487   3548   2827    148   -259   -109       C  
ATOM   3359  C   VAL A 480     -32.473 -44.097  -5.658  1.00 24.28           C  
ANISOU 3359  C   VAL A 480     3306   3329   2589    153   -212   -113       C  
ATOM   3360  O   VAL A 480     -32.137 -43.307  -4.768  1.00 25.18           O  
ANISOU 3360  O   VAL A 480     3387   3445   2736    182   -191   -109       O  
ATOM   3361  CB  VAL A 480     -35.020 -43.853  -5.846  1.00 27.05           C  
ANISOU 3361  CB  VAL A 480     3602   3680   2995    157   -332    -75       C  
ATOM   3362  CG1 VAL A 480     -34.697 -42.836  -6.856  1.00 29.64           C  
ANISOU 3362  CG1 VAL A 480     3986   3992   3282    141   -362    -50       C  
ATOM   3363  CG2 VAL A 480     -36.389 -44.735  -6.217  1.00 26.38           C  
ANISOU 3363  CG2 VAL A 480     3497   3601   2927    134   -393    -67       C  
ATOM   3364  N   ASN A 481     -31.702 -44.340  -6.716  1.00 23.11           N  
ANISOU 3364  N   ASN A 481     3225   3174   2381    120   -192   -122       N  
ATOM   3365  CA  ASN A 481     -30.314 -43.835  -6.801  1.00 21.89           C  
ANISOU 3365  CA  ASN A 481     3095   3014   2207    119   -135   -130       C  
ATOM   3366  C   ASN A 481     -30.237 -42.299  -6.695  1.00 22.16           C  
ANISOU 3366  C   ASN A 481     3129   3043   2250    134   -155   -102       C  
ATOM   3367  O   ASN A 481     -29.341 -41.763  -6.031  1.00 22.12           O  
ANISOU 3367  O   ASN A 481     3104   3037   2263    150   -115   -106       O  
ATOM   3368  CB  ASN A 481     -29.676 -44.259  -8.118  1.00 27.65           C  
ANISOU 3368  CB  ASN A 481     3903   3735   2869     74   -108   -145       C  
ATOM   3369  CG  ASN A 481     -28.967 -45.604  -8.036  1.00 34.94           C  
ANISOU 3369  CG  ASN A 481     4826   4654   3796     69    -43   -184       C  
ATOM   3370  OD1 ASN A 481     -28.829 -46.211  -6.956  1.00 38.26           O  
ANISOU 3370  OD1 ASN A 481     5187   5079   4271    100    -21   -193       O  
ATOM   3371  ND2 ASN A 481     -28.520 -46.084  -9.200  1.00 37.24           N  
ANISOU 3371  ND2 ASN A 481     5188   4933   4029     26    -11   -206       N  
ATOM   3372  N   SER A 482     -31.137 -41.583  -7.371  1.00 18.45           N  
ANISOU 3372  N   SER A 482     2680   2562   1767    124   -222    -72       N  
ATOM   3373  CA  SER A 482     -31.110 -40.097  -7.331  1.00 21.06           C  
ANISOU 3373  CA  SER A 482     3013   2877   2112    138   -244    -42       C  
ATOM   3374  C   SER A 482     -31.336 -39.495  -5.942  1.00 20.30           C  
ANISOU 3374  C   SER A 482     2846   2779   2087    184   -233    -45       C  
ATOM   3375  O   SER A 482     -31.017 -38.308  -5.729  1.00 21.44           O  
ANISOU 3375  O   SER A 482     2993   2907   2246    197   -231    -31       O  
ATOM   3376  CB  SER A 482     -32.196 -39.535  -8.270  1.00 24.51           C  
ANISOU 3376  CB  SER A 482     3477   3298   2538    122   -331     -2       C  
ATOM   3377  OG  SER A 482     -33.489 -40.038  -7.950  1.00 24.97           O  
ANISOU 3377  OG  SER A 482     3483   3362   2643    137   -380      4       O  
ATOM   3378  N   MET A 483     -31.938 -40.244  -5.014  1.00 19.57           N  
ANISOU 3378  N   MET A 483     2697   2701   2038    206   -227    -62       N  
ATOM   3379  CA  MET A 483     -32.202 -39.819  -3.626  1.00 17.99           C  
ANISOU 3379  CA  MET A 483     2437   2502   1897    241   -207    -72       C  
ATOM   3380  C   MET A 483     -30.997 -40.009  -2.685  1.00 19.62           C  
ANISOU 3380  C   MET A 483     2634   2722   2100    244   -144    -95       C  
ATOM   3381  O   MET A 483     -30.984 -39.413  -1.583  1.00 17.57           O  
ANISOU 3381  O   MET A 483     2343   2460   1873    262   -125   -103       O  
ATOM   3382  CB  MET A 483     -33.432 -40.593  -3.067  1.00 17.20           C  
ANISOU 3382  CB  MET A 483     2282   2413   1840    254   -226    -79       C  
ATOM   3383  CG  MET A 483     -34.819 -40.254  -3.767  1.00 17.96           C  
ANISOU 3383  CG  MET A 483     2363   2494   1966    258   -298    -50       C  
ATOM   3384  SD  MET A 483     -35.142 -38.465  -3.694  1.00 23.06           S  
ANISOU 3384  SD  MET A 483     2997   3104   2662    288   -323    -24       S  
ATOM   3385  CE  MET A 483     -34.569 -37.932  -5.370  1.00 20.28           C  
ANISOU 3385  CE  MET A 483     2732   2734   2238    252   -371     13       C  
ATOM   3386  N   GLN A 484     -29.982 -40.786  -3.101  1.00 18.96           N  
ANISOU 3386  N   GLN A 484     2578   2647   1979    222   -112   -106       N  
ATOM   3387  CA  GLN A 484     -28.816 -41.054  -2.255  1.00 20.65           C  
ANISOU 3387  CA  GLN A 484     2775   2872   2199    224    -62   -120       C  
ATOM   3388  C   GLN A 484     -28.023 -39.753  -2.057  1.00 20.74           C  
ANISOU 3388  C   GLN A 484     2798   2873   2210    224    -48   -112       C  
ATOM   3389  O   GLN A 484     -28.070 -38.850  -2.894  1.00 23.34           O  
ANISOU 3389  O   GLN A 484     3163   3184   2520    216    -67    -97       O  
ATOM   3390  CB  GLN A 484     -27.914 -42.108  -2.913  1.00 20.30           C  
ANISOU 3390  CB  GLN A 484     2753   2831   2129    204    -29   -132       C  
ATOM   3391  CG  GLN A 484     -28.709 -43.439  -3.259  1.00 20.33           C  
ANISOU 3391  CG  GLN A 484     2756   2838   2129    198    -43   -142       C  
ATOM   3392  CD  GLN A 484     -29.597 -43.861  -2.097  1.00 23.61           C  
ANISOU 3392  CD  GLN A 484     3121   3265   2585    216    -58   -144       C  
ATOM   3393  OE1 GLN A 484     -29.100 -44.181  -1.030  1.00 26.00           O  
ANISOU 3393  OE1 GLN A 484     3392   3577   2911    225    -33   -148       O  
ATOM   3394  NE2 GLN A 484     -30.908 -43.827  -2.283  1.00 21.84           N  
ANISOU 3394  NE2 GLN A 484     2888   3041   2370    219   -101   -137       N  
ATOM   3395  N   THR A 485     -27.338 -39.635  -0.931  1.00 19.76           N  
ANISOU 3395  N   THR A 485     2646   2757   2104    227    -22   -120       N  
ATOM   3396  CA  THR A 485     -26.645 -38.373  -0.627  1.00 20.85           C  
ANISOU 3396  CA  THR A 485     2794   2884   2243    223    -11   -115       C  
ATOM   3397  C   THR A 485     -25.211 -38.695  -0.204  1.00 22.78           C  
ANISOU 3397  C   THR A 485     3027   3141   2487    207     23   -118       C  
ATOM   3398  O   THR A 485     -24.660 -39.734  -0.579  1.00 24.54           O  
ANISOU 3398  O   THR A 485     3243   3372   2707    201     43   -121       O  
ATOM   3399  CB  THR A 485     -27.465 -37.553   0.382  1.00 24.05           C  
ANISOU 3399  CB  THR A 485     3180   3281   2677    240    -23   -121       C  
ATOM   3400  OG1 THR A 485     -26.822 -36.255   0.583  1.00 25.79           O  
ANISOU 3400  OG1 THR A 485     3418   3483   2897    232    -14   -118       O  
ATOM   3401  CG2 THR A 485     -27.608 -38.319   1.705  1.00 21.37           C  
ANISOU 3401  CG2 THR A 485     2803   2964   2353    242     -9   -136       C  
ATOM   3402  N   VAL A 486     -24.523 -37.749   0.486  1.00 25.81           N  
ANISOU 3402  N   VAL A 486     3407   3521   2878    197     32   -116       N  
ATOM   3403  CA  VAL A 486     -23.061 -37.819   0.609  1.00 26.10           C  
ANISOU 3403  CA  VAL A 486     3433   3565   2918    176     58   -111       C  
ATOM   3404  C   VAL A 486     -22.670 -38.048   2.053  1.00 24.17           C  
ANISOU 3404  C   VAL A 486     3153   3338   2693    170     55   -112       C  
ATOM   3405  O   VAL A 486     -23.340 -37.598   2.972  1.00 27.01           O  
ANISOU 3405  O   VAL A 486     3513   3698   3052    172     42   -120       O  
ATOM   3406  CB  VAL A 486     -22.308 -36.555   0.066  1.00 24.73           C  
ANISOU 3406  CB  VAL A 486     3289   3375   2733    157     68   -102       C  
ATOM   3407  CG1 VAL A 486     -22.444 -36.483  -1.499  1.00 28.87           C  
ANISOU 3407  CG1 VAL A 486     3856   3884   3227    151     75    -96       C  
ATOM   3408  CG2 VAL A 486     -22.830 -35.210   0.727  1.00 21.06           C  
ANISOU 3408  CG2 VAL A 486     2840   2892   2271    158     49   -105       C  
ATOM   3409  N   PHE A 487     -21.542 -38.708   2.245  1.00 23.41           N  
ANISOU 3409  N   PHE A 487     3028   3252   2614    158     69   -102       N  
ATOM   3410  CA  PHE A 487     -20.910 -38.716   3.554  1.00 23.17           C  
ANISOU 3410  CA  PHE A 487     2969   3236   2598    139     56    -93       C  
ATOM   3411  C   PHE A 487     -19.383 -38.626   3.422  1.00 23.11           C  
ANISOU 3411  C   PHE A 487     2936   3229   2615    118     69    -77       C  
ATOM   3412  O   PHE A 487     -18.778 -39.417   2.697  1.00 20.92           O  
ANISOU 3412  O   PHE A 487     2637   2949   2363    126     93    -72       O  
ATOM   3413  CB  PHE A 487     -21.237 -39.978   4.339  1.00 22.67           C  
ANISOU 3413  CB  PHE A 487     2878   3188   2548    146     43    -88       C  
ATOM   3414  CG  PHE A 487     -20.369 -40.112   5.583  1.00 23.40           C  
ANISOU 3414  CG  PHE A 487     2943   3295   2654    119     22    -68       C  
ATOM   3415  CD1 PHE A 487     -20.698 -39.389   6.716  1.00 22.98           C  
ANISOU 3415  CD1 PHE A 487     2908   3250   2574     95      4    -73       C  
ATOM   3416  CD2 PHE A 487     -19.222 -40.905   5.575  1.00 24.40           C  
ANISOU 3416  CD2 PHE A 487     3026   3424   2822    115     21    -43       C  
ATOM   3417  CE1 PHE A 487     -19.911 -39.495   7.897  1.00 23.24           C  
ANISOU 3417  CE1 PHE A 487     2925   3298   2607     58    -25    -52       C  
ATOM   3418  CE2 PHE A 487     -18.429 -40.987   6.698  1.00 29.24           C  
ANISOU 3418  CE2 PHE A 487     3612   4049   3450     86    -11    -16       C  
ATOM   3419  CZ  PHE A 487     -18.767 -40.273   7.861  1.00 26.31           C  
ANISOU 3419  CZ  PHE A 487     3268   3691   3038     54    -39    -19       C  
ATOM   3420  N   VAL A 488     -18.760 -37.697   4.156  1.00 21.79           N  
ANISOU 3420  N   VAL A 488     2768   3065   2446     89     56    -70       N  
ATOM   3421  CA  VAL A 488     -17.296 -37.636   4.281  1.00 20.27           C  
ANISOU 3421  CA  VAL A 488     2539   2877   2287     63     58    -49       C  
ATOM   3422  C   VAL A 488     -16.985 -37.402   5.753  1.00 19.94           C  
ANISOU 3422  C   VAL A 488     2484   2850   2242     31     18    -36       C  
ATOM   3423  O   VAL A 488     -17.598 -36.520   6.375  1.00 18.00           O  
ANISOU 3423  O   VAL A 488     2278   2601   1958     15      6    -52       O  
ATOM   3424  CB  VAL A 488     -16.697 -36.499   3.443  1.00 21.88           C  
ANISOU 3424  CB  VAL A 488     2764   3066   2485     46     83    -51       C  
ATOM   3425  CG1 VAL A 488     -15.167 -36.400   3.654  1.00 19.06           C  
ANISOU 3425  CG1 VAL A 488     2358   2714   2171     15     85    -29       C  
ATOM   3426  CG2 VAL A 488     -17.029 -36.692   1.897  1.00 21.47           C  
ANISOU 3426  CG2 VAL A 488     2738   2998   2421     68    122    -63       C  
ATOM   3427  N   GLY A 489     -16.002 -38.132   6.286  1.00 21.33           N  
ANISOU 3427  N   GLY A 489     2608   3038   2459     16     -2     -6       N  
ATOM   3428  CA  GLY A 489     -15.529 -37.882   7.654  1.00 21.15           C  
ANISOU 3428  CA  GLY A 489     2576   3031   2428    -28    -51     14       C  
ATOM   3429  C   GLY A 489     -14.034 -37.613   7.563  1.00 23.59           C  
ANISOU 3429  C   GLY A 489     2836   3340   2786    -56    -60     43       C  
ATOM   3430  O   GLY A 489     -13.295 -38.404   6.959  1.00 25.62           O  
ANISOU 3430  O   GLY A 489     3037   3592   3105    -36    -42     61       O  
ATOM   3431  N   TYR A 490     -13.583 -36.473   8.090  1.00 19.00           N  
ANISOU 3431  N   TYR A 490     2275   2761   2182   -103    -81     43       N  
ATOM   3432  CA  TYR A 490     -12.194 -36.065   7.990  1.00 19.78           C  
ANISOU 3432  CA  TYR A 490     2327   2860   2327   -137    -90     69       C  
ATOM   3433  C   TYR A 490     -11.723 -35.695   9.378  1.00 23.01           C  
ANISOU 3433  C   TYR A 490     2738   3287   2719   -198   -157     92       C  
ATOM   3434  O   TYR A 490     -12.371 -34.874  10.047  1.00 26.49           O  
ANISOU 3434  O   TYR A 490     3245   3727   3092   -227   -169     66       O  
ATOM   3435  CB  TYR A 490     -12.014 -34.852   7.031  1.00 22.04           C  
ANISOU 3435  CB  TYR A 490     2644   3128   2601   -144    -46     46       C  
ATOM   3436  CG  TYR A 490     -10.582 -34.363   6.906  1.00 22.23           C  
ANISOU 3436  CG  TYR A 490     2618   3152   2675   -185    -50     71       C  
ATOM   3437  CD1 TYR A 490     -10.091 -33.373   7.769  1.00 23.04           C  
ANISOU 3437  CD1 TYR A 490     2737   3260   2758   -246    -93     79       C  
ATOM   3438  CD2 TYR A 490      -9.761 -34.810   5.893  1.00 23.46           C  
ANISOU 3438  CD2 TYR A 490     2717   3302   2896   -166     -5     83       C  
ATOM   3439  CE1 TYR A 490      -8.780 -32.869   7.685  1.00 25.47           C  
ANISOU 3439  CE1 TYR A 490     2996   3568   3113   -290   -102    104       C  
ATOM   3440  CE2 TYR A 490      -8.393 -34.311   5.794  1.00 25.58           C  
ANISOU 3440  CE2 TYR A 490     2929   3570   3219   -208     -5    107       C  
ATOM   3441  CZ  TYR A 490      -7.949 -33.337   6.686  1.00 28.24           C  
ANISOU 3441  CZ  TYR A 490     3279   3914   3537   -269    -56    119       C  
ATOM   3442  OH  TYR A 490      -6.674 -32.827   6.662  1.00 32.52           O  
ANISOU 3442  OH  TYR A 490     3766   4458   4133   -315    -63    144       O  
ATOM   3443  N   GLY A 491     -10.561 -36.226   9.783  1.00 24.14           N  
ANISOU 3443  N   GLY A 491     2809   3440   2923   -222   -199    139       N  
ATOM   3444  CA  GLY A 491      -9.983 -35.889  11.065  1.00 24.52           C  
ANISOU 3444  CA  GLY A 491     2856   3506   2954   -291   -274    169       C  
ATOM   3445  C   GLY A 491      -9.154 -36.965  11.736  1.00 27.36           C  
ANISOU 3445  C   GLY A 491     3140   3879   3378   -304   -340    231       C  
ATOM   3446  O   GLY A 491      -8.970 -38.065  11.200  1.00 28.96           O  
ANISOU 3446  O   GLY A 491     3280   4073   3650   -252   -322    251       O  
ATOM   3447  N   PRO A 492      -8.639 -36.666  12.958  1.00 27.45           N  
ANISOU 3447  N   PRO A 492     3158   3909   3365   -377   -422    265       N  
ATOM   3448  CA  PRO A 492      -7.813 -37.654  13.654  1.00 23.52           C  
ANISOU 3448  CA  PRO A 492     2585   3421   2931   -395   -501    335       C  
ATOM   3449  C   PRO A 492      -8.541 -38.944  13.922  1.00 26.14           C  
ANISOU 3449  C   PRO A 492     2917   3752   3262   -354   -509    350       C  
ATOM   3450  O   PRO A 492      -7.915 -40.013  13.888  1.00 28.91           O  
ANISOU 3450  O   PRO A 492     3186   4095   3704   -329   -540    402       O  
ATOM   3451  CB  PRO A 492      -7.422 -36.936  14.960  1.00 28.29           C  
ANISOU 3451  CB  PRO A 492     3230   4047   3474   -493   -588    359       C  
ATOM   3452  CG  PRO A 492      -8.507 -35.943  15.167  1.00 29.72           C  
ANISOU 3452  CG  PRO A 492     3525   4227   3540   -512   -546    290       C  
ATOM   3453  CD  PRO A 492      -8.883 -35.479  13.790  1.00 28.23           C  
ANISOU 3453  CD  PRO A 492     3339   4015   3372   -447   -448    239       C  
ATOM   3454  N   THR A 493      -9.835 -38.904  14.213  1.00 25.76           N  
ANISOU 3454  N   THR A 493     2956   3709   3122   -347   -484    307       N  
ATOM   3455  CA  THR A 493     -10.478 -40.161  14.592  1.00 26.89           C  
ANISOU 3455  CA  THR A 493     3100   3854   3265   -320   -500    328       C  
ATOM   3456  C   THR A 493     -10.949 -40.976  13.394  1.00 27.70           C  
ANISOU 3456  C   THR A 493     3171   3934   3421   -233   -426    305       C  
ATOM   3457  O   THR A 493     -11.109 -42.192  13.520  1.00 27.30           O  
ANISOU 3457  O   THR A 493     3090   3874   3408   -204   -442    334       O  
ATOM   3458  CB  THR A 493     -11.641 -39.881  15.549  1.00 28.49           C  
ANISOU 3458  CB  THR A 493     3404   4073   3349   -359   -506    297       C  
ATOM   3459  OG1 THR A 493     -11.204 -38.909  16.509  1.00 29.37           O  
ANISOU 3459  OG1 THR A 493     3560   4201   3400   -445   -559    303       O  
ATOM   3460  CG2 THR A 493     -12.026 -41.150  16.329  1.00 28.37           C  
ANISOU 3460  CG2 THR A 493     3389   4064   3327   -362   -552    339       C  
ATOM   3461  N   PHE A 494     -11.154 -40.354  12.232  1.00 26.12           N  
ANISOU 3461  N   PHE A 494     2979   3720   3224   -195   -349    255       N  
ATOM   3462  CA  PHE A 494     -11.515 -41.098  11.045  1.00 24.70           C  
ANISOU 3462  CA  PHE A 494     2775   3519   3090   -123   -281    232       C  
ATOM   3463  C   PHE A 494     -10.266 -41.689  10.400  1.00 23.99           C  
ANISOU 3463  C   PHE A 494     2587   3410   3116    -99   -272    266       C  
ATOM   3464  O   PHE A 494      -9.155 -41.199  10.588  1.00 26.08           O  
ANISOU 3464  O   PHE A 494     2803   3679   3426   -133   -301    296       O  
ATOM   3465  CB  PHE A 494     -12.248 -40.196  10.031  1.00 22.83           C  
ANISOU 3465  CB  PHE A 494     2594   3275   2805   -100   -207    170       C  
ATOM   3466  CG  PHE A 494     -13.651 -39.879  10.416  1.00 25.29           C  
ANISOU 3466  CG  PHE A 494     2986   3594   3029   -100   -198    132       C  
ATOM   3467  CD1 PHE A 494     -14.005 -38.617  10.945  1.00 22.31           C  
ANISOU 3467  CD1 PHE A 494     2671   3223   2581   -142   -204    105       C  
ATOM   3468  CD2 PHE A 494     -14.649 -40.835  10.268  1.00 23.85           C  
ANISOU 3468  CD2 PHE A 494     2816   3407   2836    -61   -180    120       C  
ATOM   3469  CE1 PHE A 494     -15.319 -38.338  11.264  1.00 18.49           C  
ANISOU 3469  CE1 PHE A 494     2254   2742   2032   -137   -185     67       C  
ATOM   3470  CE2 PHE A 494     -15.974 -40.545  10.620  1.00 23.09           C  
ANISOU 3470  CE2 PHE A 494     2786   3318   2669    -62   -168     85       C  
ATOM   3471  CZ  PHE A 494     -16.298 -39.275  11.113  1.00 21.25           C  
ANISOU 3471  CZ  PHE A 494     2608   3091   2377    -98   -167     57       C  
ATOM   3472  N   LYS A 495     -10.463 -42.726   9.598  1.00 22.28           N  
ANISOU 3472  N   LYS A 495     2341   3172   2953    -41   -224    258       N  
ATOM   3473  CA  LYS A 495      -9.349 -43.320   8.847  1.00 25.79           C  
ANISOU 3473  CA  LYS A 495     2694   3591   3516    -10   -192    278       C  
ATOM   3474  C   LYS A 495      -8.864 -42.377   7.740  1.00 26.37           C  
ANISOU 3474  C   LYS A 495     2764   3658   3596     -9   -121    242       C  
ATOM   3475  O   LYS A 495      -9.557 -41.436   7.361  1.00 27.48           O  
ANISOU 3475  O   LYS A 495     2980   3810   3653    -19    -91    199       O  
ATOM   3476  CB  LYS A 495      -9.784 -44.645   8.227  1.00 25.02           C  
ANISOU 3476  CB  LYS A 495     2581   3464   3463     49   -148    266       C  
ATOM   3477  CG  LYS A 495      -9.978 -45.736   9.326  1.00 25.19           C  
ANISOU 3477  CG  LYS A 495     2584   3481   3504     48   -223    318       C  
ATOM   3478  CD  LYS A 495     -10.343 -47.065   8.652  1.00 26.22           C  
ANISOU 3478  CD  LYS A 495     2697   3575   3689    106   -174    305       C  
ATOM   3479  CE  LYS A 495     -10.146 -48.231   9.645  1.00 33.76           C  
ANISOU 3479  CE  LYS A 495     3609   4514   4703    107   -249    370       C  
ATOM   3480  NZ  LYS A 495     -10.808 -49.375   8.990  1.00 37.89           N  
ANISOU 3480  NZ  LYS A 495     4143   5003   5250    158   -196    343       N  
ATOM   3481  N   TYR A 496      -7.665 -42.672   7.223  1.00 25.12           N  
ANISOU 3481  N   TYR A 496     2517   3482   3548      2    -93    262       N  
ATOM   3482  CA  TYR A 496      -6.947 -41.861   6.243  1.00 24.85           C  
ANISOU 3482  CA  TYR A 496     2463   3442   3538     -6    -26    238       C  
ATOM   3483  C   TYR A 496      -7.152 -42.448   4.842  1.00 28.11           C  
ANISOU 3483  C   TYR A 496     2880   3826   3973     44     80    192       C  
ATOM   3484  O   TYR A 496      -6.971 -43.650   4.655  1.00 28.30           O  
ANISOU 3484  O   TYR A 496     2854   3824   4075     84    101    200       O  
ATOM   3485  CB  TYR A 496      -5.456 -41.848   6.600  1.00 22.82           C  
ANISOU 3485  CB  TYR A 496     2095   3180   3395    -30    -58    290       C  
ATOM   3486  CG  TYR A 496      -4.506 -41.191   5.577  1.00 24.83           C  
ANISOU 3486  CG  TYR A 496     2307   3425   3704    -39     21    271       C  
ATOM   3487  CD1 TYR A 496      -3.532 -41.933   4.883  1.00 24.29           C  
ANISOU 3487  CD1 TYR A 496     2137   3326   3766     -7     85    278       C  
ATOM   3488  CD2 TYR A 496      -4.557 -39.822   5.349  1.00 27.52           C  
ANISOU 3488  CD2 TYR A 496     2705   3783   3968    -83     33    247       C  
ATOM   3489  CE1 TYR A 496      -2.593 -41.284   4.004  1.00 27.13           C  
ANISOU 3489  CE1 TYR A 496     2453   3679   4177    -24    162    262       C  
ATOM   3490  CE2 TYR A 496      -3.673 -39.194   4.476  1.00 27.00           C  
ANISOU 3490  CE2 TYR A 496     2603   3709   3947   -100    102    235       C  
ATOM   3491  CZ  TYR A 496      -2.718 -39.925   3.809  1.00 28.97           C  
ANISOU 3491  CZ  TYR A 496     2753   3934   4321    -72    168    242       C  
ATOM   3492  OH  TYR A 496      -1.865 -39.256   2.964  1.00 33.10           O  
ANISOU 3492  OH  TYR A 496     3243   4450   4882    -96    243    227       O  
ATOM   3493  N   ARG A 497      -7.554 -41.615   3.870  1.00 23.73           N  
ANISOU 3493  N   ARG A 497     2392   3274   3349     38    143    145       N  
ATOM   3494  CA  ARG A 497      -7.673 -42.055   2.477  1.00 24.87           C  
ANISOU 3494  CA  ARG A 497     2553   3394   3502     70    245    100       C  
ATOM   3495  C   ARG A 497      -8.371 -43.411   2.363  1.00 25.09           C  
ANISOU 3495  C   ARG A 497     2588   3402   3543    117    256     88       C  
ATOM   3496  O   ARG A 497      -7.826 -44.351   1.793  1.00 26.54           O  
ANISOU 3496  O   ARG A 497     2717   3554   3812    147    315     81       O  
ATOM   3497  CB  ARG A 497      -6.309 -42.152   1.785  1.00 27.78           C  
ANISOU 3497  CB  ARG A 497     2837   3742   3977     68    315    103       C  
ATOM   3498  CG  ARG A 497      -5.523 -40.834   1.625  1.00 30.88           C  
ANISOU 3498  CG  ARG A 497     3220   4149   4363     19    325    109       C  
ATOM   3499  CD  ARG A 497      -4.272 -41.072   0.768  1.00 34.88           C  
ANISOU 3499  CD  ARG A 497     3643   4632   4979     21    417    104       C  
ATOM   3500  NE  ARG A 497      -3.516 -39.844   0.514  1.00 38.79           N  
ANISOU 3500  NE  ARG A 497     4129   5139   5470    -30    437    108       N  
ATOM   3501  CZ  ARG A 497      -3.756 -39.033  -0.524  1.00 40.86           C  
ANISOU 3501  CZ  ARG A 497     4469   5402   5655    -53    506     69       C  
ATOM   3502  NH1 ARG A 497      -4.753 -39.333  -1.357  1.00 42.84           N  
ANISOU 3502  NH1 ARG A 497     4810   5644   5824    -30    553     27       N  
ATOM   3503  NH2 ARG A 497      -3.039 -37.923  -0.726  1.00 39.33           N  
ANISOU 3503  NH2 ARG A 497     4267   5216   5462   -103    523     77       N  
ATOM   3504  N   THR A 498      -9.555 -43.523   2.929  1.00 24.89           N  
ANISOU 3504  N   THR A 498     2625   3391   3440    121    204     85       N  
ATOM   3505  CA  THR A 498     -10.254 -44.811   3.043  1.00 24.58           C  
ANISOU 3505  CA  THR A 498     2592   3336   3413    158    199     82       C  
ATOM   3506  C   THR A 498     -11.660 -44.709   2.449  1.00 27.14           C  
ANISOU 3506  C   THR A 498     3013   3666   3634    167    219     38       C  
ATOM   3507  O   THR A 498     -12.400 -43.738   2.702  1.00 26.73           O  
ANISOU 3507  O   THR A 498     3021   3638   3496    145    187     30       O  
ATOM   3508  CB  THR A 498     -10.314 -45.245   4.525  1.00 25.71           C  
ANISOU 3508  CB  THR A 498     2703   3491   3574    150    103    134       C  
ATOM   3509  OG1 THR A 498      -8.980 -45.572   4.938  1.00 27.38           O  
ANISOU 3509  OG1 THR A 498     2814   3688   3900    148     82    181       O  
ATOM   3510  CG2 THR A 498     -11.249 -46.508   4.741  1.00 26.35           C  
ANISOU 3510  CG2 THR A 498     2805   3556   3650    182     90    132       C  
ATOM   3511  N   LYS A 499     -12.020 -45.678   1.616  1.00 24.15           N  
ANISOU 3511  N   LYS A 499     2648   3262   3268    197    273      8       N  
ATOM   3512  CA  LYS A 499     -13.361 -45.733   1.056  1.00 26.09           C  
ANISOU 3512  CA  LYS A 499     2977   3511   3424    203    283    -29       C  
ATOM   3513  C   LYS A 499     -14.088 -46.843   1.805  1.00 26.31           C  
ANISOU 3513  C   LYS A 499     3000   3533   3463    223    239    -15       C  
ATOM   3514  O   LYS A 499     -13.499 -47.908   2.004  1.00 28.56           O  
ANISOU 3514  O   LYS A 499     3227   3790   3833    245    247      2       O  
ATOM   3515  CB  LYS A 499     -13.290 -46.011  -0.447  1.00 28.47           C  
ANISOU 3515  CB  LYS A 499     3311   3788   3719    209    372    -74       C  
ATOM   3516  CG  LYS A 499     -14.698 -46.182  -1.073  1.00 31.57           C  
ANISOU 3516  CG  LYS A 499     3789   4183   4022    211    372   -108       C  
ATOM   3517  CD  LYS A 499     -14.650 -46.148  -2.603  1.00 37.64           C  
ANISOU 3517  CD  LYS A 499     4611   4934   4756    199    452   -151       C  
ATOM   3518  CE  LYS A 499     -14.486 -47.534  -3.183  1.00 45.46           C  
ANISOU 3518  CE  LYS A 499     5592   5887   5795    219    512   -180       C  
ATOM   3519  NZ  LYS A 499     -14.253 -47.568  -4.709  1.00 50.36           N  
ANISOU 3519  NZ  LYS A 499     6267   6486   6381    198    605   -229       N  
ATOM   3520  N   VAL A 500     -15.317 -46.587   2.260  1.00 23.11           N  
ANISOU 3520  N   VAL A 500     2648   3150   2981    217    194    -19       N  
ATOM   3521  CA  VAL A 500     -16.122 -47.599   2.952  1.00 22.58           C  
ANISOU 3521  CA  VAL A 500     2584   3080   2915    230    156     -8       C  
ATOM   3522  C   VAL A 500     -17.401 -47.827   2.163  1.00 24.20           C  
ANISOU 3522  C   VAL A 500     2854   3283   3058    237    177    -47       C  
ATOM   3523  O   VAL A 500     -17.839 -46.951   1.420  1.00 25.24           O  
ANISOU 3523  O   VAL A 500     3034   3426   3131    227    194    -73       O  
ATOM   3524  CB  VAL A 500     -16.458 -47.178   4.407  1.00 24.74           C  
ANISOU 3524  CB  VAL A 500     2857   3383   3159    207     82     27       C  
ATOM   3525  CG1 VAL A 500     -15.172 -46.854   5.195  1.00 26.15           C  
ANISOU 3525  CG1 VAL A 500     2976   3567   3392    189     49     70       C  
ATOM   3526  CG2 VAL A 500     -17.389 -45.973   4.427  1.00 22.69           C  
ANISOU 3526  CG2 VAL A 500     2658   3152   2813    189     71      4       C  
ATOM   3527  N   PRO A 501     -18.049 -48.980   2.326  1.00 26.61           N  
ANISOU 3527  N   PRO A 501     3162   3573   3375    252    169    -49       N  
ATOM   3528  CA  PRO A 501     -19.297 -49.252   1.529  1.00 25.14           C  
ANISOU 3528  CA  PRO A 501     3036   3385   3132    254    183    -85       C  
ATOM   3529  C   PRO A 501     -20.423 -48.314   1.943  1.00 21.74           C  
ANISOU 3529  C   PRO A 501     2643   2989   2629    239    141    -87       C  
ATOM   3530  O   PRO A 501     -20.422 -47.799   3.081  1.00 25.39           O  
ANISOU 3530  O   PRO A 501     3090   3473   3085    228    101    -61       O  
ATOM   3531  CB  PRO A 501     -19.646 -50.724   1.855  1.00 26.70           C  
ANISOU 3531  CB  PRO A 501     3219   3558   3369    268    176    -79       C  
ATOM   3532  CG  PRO A 501     -18.629 -51.232   2.891  1.00 29.98           C  
ANISOU 3532  CG  PRO A 501     3567   3960   3863    276    152    -33       C  
ATOM   3533  CD  PRO A 501     -17.627 -50.109   3.208  1.00 28.06           C  
ANISOU 3533  CD  PRO A 501     3294   3738   3630    263    143    -12       C  
ATOM   3534  N   PRO A 502     -21.412 -48.114   1.065  1.00 21.58           N  
ANISOU 3534  N   PRO A 502     2673   2970   2557    236    150   -115       N  
ATOM   3535  CA  PRO A 502     -22.601 -47.293   1.405  1.00 20.47           C  
ANISOU 3535  CA  PRO A 502     2560   2854   2363    229    112   -117       C  
ATOM   3536  C   PRO A 502     -23.248 -47.755   2.694  1.00 20.06           C  
ANISOU 3536  C   PRO A 502     2488   2816   2318    228     76    -99       C  
ATOM   3537  O   PRO A 502     -23.256 -48.951   3.021  1.00 20.20           O  
ANISOU 3537  O   PRO A 502     2488   2821   2367    232     74    -90       O  
ATOM   3538  CB  PRO A 502     -23.566 -47.515   0.207  1.00 23.62           C  
ANISOU 3538  CB  PRO A 502     3005   3245   2725    227    121   -145       C  
ATOM   3539  CG  PRO A 502     -22.677 -48.092  -0.941  1.00 25.57           C  
ANISOU 3539  CG  PRO A 502     3265   3464   2986    226    174   -164       C  
ATOM   3540  CD  PRO A 502     -21.470 -48.722  -0.300  1.00 24.04           C  
ANISOU 3540  CD  PRO A 502     3017   3256   2860    238    195   -148       C  
ATOM   3541  N   PHE A 503     -23.852 -46.819   3.410  1.00 18.12           N  
ANISOU 3541  N   PHE A 503     2250   2592   2042    219     51    -96       N  
ATOM   3542  CA  PHE A 503     -24.521 -47.180   4.665  1.00 17.87           C  
ANISOU 3542  CA  PHE A 503     2207   2575   2008    209     25    -83       C  
ATOM   3543  C   PHE A 503     -25.673 -46.200   4.870  1.00 20.01           C  
ANISOU 3543  C   PHE A 503     2498   2861   2243    206     16    -99       C  
ATOM   3544  O   PHE A 503     -25.796 -45.223   4.134  1.00 21.24           O  
ANISOU 3544  O   PHE A 503     2673   3014   2384    212     22   -113       O  
ATOM   3545  CB  PHE A 503     -23.513 -47.189   5.829  1.00 18.34           C  
ANISOU 3545  CB  PHE A 503     2240   2642   2085    193      7    -52       C  
ATOM   3546  CG  PHE A 503     -22.975 -45.801   6.139  1.00 21.54           C  
ANISOU 3546  CG  PHE A 503     2653   3061   2471    179      3    -51       C  
ATOM   3547  CD1 PHE A 503     -23.717 -44.926   6.923  1.00 20.57           C  
ANISOU 3547  CD1 PHE A 503     2551   2955   2310    163     -7    -62       C  
ATOM   3548  CD2 PHE A 503     -21.761 -45.375   5.598  1.00 25.39           C  
ANISOU 3548  CD2 PHE A 503     3127   3540   2981    180     16    -45       C  
ATOM   3549  CE1 PHE A 503     -23.240 -43.640   7.204  1.00 23.02           C  
ANISOU 3549  CE1 PHE A 503     2874   3271   2602    147     -8    -65       C  
ATOM   3550  CE2 PHE A 503     -21.272 -44.092   5.835  1.00 26.03           C  
ANISOU 3550  CE2 PHE A 503     3217   3630   3044    163     12    -45       C  
ATOM   3551  CZ  PHE A 503     -22.023 -43.211   6.621  1.00 23.57           C  
ANISOU 3551  CZ  PHE A 503     2932   3332   2692    146     -2    -56       C  
ATOM   3552  N   GLU A 504     -26.532 -46.481   5.864  1.00 22.52           N  
ANISOU 3552  N   GLU A 504     2811   3193   2554    196      5    -97       N  
ATOM   3553  CA  GLU A 504     -27.758 -45.728   6.091  1.00 22.43           C  
ANISOU 3553  CA  GLU A 504     2807   3189   2524    196      6   -116       C  
ATOM   3554  C   GLU A 504     -27.525 -44.618   7.109  1.00 21.47           C  
ANISOU 3554  C   GLU A 504     2695   3080   2385    179      9   -119       C  
ATOM   3555  O   GLU A 504     -26.784 -44.787   8.082  1.00 21.52           O  
ANISOU 3555  O   GLU A 504     2698   3095   2382    155      2   -101       O  
ATOM   3556  CB  GLU A 504     -28.896 -46.643   6.614  1.00 24.32           C  
ANISOU 3556  CB  GLU A 504     3036   3436   2768    189      4   -119       C  
ATOM   3557  CG  GLU A 504     -29.204 -47.771   5.653  1.00 25.31           C  
ANISOU 3557  CG  GLU A 504     3159   3548   2910    200     -1   -119       C  
ATOM   3558  CD  GLU A 504     -30.494 -48.561   5.991  1.00 28.36           C  
ANISOU 3558  CD  GLU A 504     3533   3939   3302    191     -4   -124       C  
ATOM   3559  OE1 GLU A 504     -30.861 -48.652   7.205  1.00 28.44           O  
ANISOU 3559  OE1 GLU A 504     3535   3964   3306    172      2   -118       O  
ATOM   3560  OE2 GLU A 504     -31.127 -49.087   5.017  1.00 29.69           O  
ANISOU 3560  OE2 GLU A 504     3704   4098   3480    198    -12   -133       O  
ATOM   3561  N   ASN A 505     -28.199 -43.487   6.906  1.00 21.27           N  
ANISOU 3561  N   ASN A 505     2679   3048   2353    189     18   -139       N  
ATOM   3562  CA  ASN A 505     -27.951 -42.344   7.774  1.00 21.97           C  
ANISOU 3562  CA  ASN A 505     2782   3140   2425    172     28   -149       C  
ATOM   3563  C   ASN A 505     -28.431 -42.580   9.219  1.00 24.91           C  
ANISOU 3563  C   ASN A 505     3157   3529   2779    142     39   -155       C  
ATOM   3564  O   ASN A 505     -27.967 -41.873  10.139  1.00 23.49           O  
ANISOU 3564  O   ASN A 505     2997   3354   2573    113     45   -160       O  
ATOM   3565  CB  ASN A 505     -28.591 -41.060   7.172  1.00 20.50           C  
ANISOU 3565  CB  ASN A 505     2607   2935   2249    193     37   -169       C  
ATOM   3566  CG  ASN A 505     -30.129 -41.068   7.233  1.00 25.03           C  
ANISOU 3566  CG  ASN A 505     3163   3504   2844    209     47   -188       C  
ATOM   3567  OD1 ASN A 505     -30.794 -42.128   7.434  1.00 24.94           O  
ANISOU 3567  OD1 ASN A 505     3133   3505   2839    207     46   -185       O  
ATOM   3568  ND2 ASN A 505     -30.724 -39.858   7.071  1.00 24.70           N  
ANISOU 3568  ND2 ASN A 505     3124   3440   2821    226     57   -205       N  
ATOM   3569  N   ILE A 506     -29.303 -43.574   9.475  1.00 23.47           N  
ANISOU 3569  N   ILE A 506     2960   3354   2603    141     43   -154       N  
ATOM   3570  CA  ILE A 506     -29.638 -43.871  10.881  1.00 19.60           C  
ANISOU 3570  CA  ILE A 506     2480   2882   2086    103     58   -157       C  
ATOM   3571  C   ILE A 506     -28.409 -44.309  11.680  1.00 20.10           C  
ANISOU 3571  C   ILE A 506     2558   2958   2123     66     32   -124       C  
ATOM   3572  O   ILE A 506     -28.454 -44.311  12.914  1.00 20.11           O  
ANISOU 3572  O   ILE A 506     2581   2973   2086     22     37   -123       O  
ATOM   3573  CB  ILE A 506     -30.734 -44.993  11.014  1.00 22.73           C  
ANISOU 3573  CB  ILE A 506     2857   3285   2495    102     66   -156       C  
ATOM   3574  CG1 ILE A 506     -30.266 -46.297  10.360  1.00 19.74           C  
ANISOU 3574  CG1 ILE A 506     2464   2901   2134    112     36   -126       C  
ATOM   3575  CG2 ILE A 506     -32.109 -44.567  10.435  1.00 22.43           C  
ANISOU 3575  CG2 ILE A 506     2796   3237   2490    131     88   -185       C  
ATOM   3576  CD1 ILE A 506     -31.221 -47.526  10.568  1.00 19.41           C  
ANISOU 3576  CD1 ILE A 506     2408   2864   2103    102     39   -121       C  
ATOM   3577  N   GLU A 507     -27.328 -44.760  11.015  1.00 21.08           N  
ANISOU 3577  N   GLU A 507     2667   3074   2267     80      3    -96       N  
ATOM   3578  CA  GLU A 507     -26.146 -45.263  11.737  1.00 18.90           C  
ANISOU 3578  CA  GLU A 507     2392   2806   1984     49    -31    -57       C  
ATOM   3579  C   GLU A 507     -25.226 -44.144  12.232  1.00 21.84           C  
ANISOU 3579  C   GLU A 507     2782   3184   2332     21    -41    -55       C  
ATOM   3580  O   GLU A 507     -24.322 -44.390  13.050  1.00 20.87           O  
ANISOU 3580  O   GLU A 507     2663   3071   2197    -16    -76    -21       O  
ATOM   3581  CB  GLU A 507     -25.328 -46.174  10.801  1.00 19.91           C  
ANISOU 3581  CB  GLU A 507     2488   2918   2159     78    -49    -30       C  
ATOM   3582  CG  GLU A 507     -26.090 -47.343  10.168  1.00 22.35           C  
ANISOU 3582  CG  GLU A 507     2782   3215   2493    103    -41    -32       C  
ATOM   3583  CD  GLU A 507     -26.580 -48.379  11.239  1.00 27.87           C  
ANISOU 3583  CD  GLU A 507     3486   3922   3181     72    -53    -10       C  
ATOM   3584  OE1 GLU A 507     -25.879 -48.604  12.299  1.00 27.16           O  
ANISOU 3584  OE1 GLU A 507     3403   3841   3076     36    -83     26       O  
ATOM   3585  OE2 GLU A 507     -27.651 -49.000  10.980  1.00 29.95           O  
ANISOU 3585  OE2 GLU A 507     3747   4183   3450     81    -38    -24       O  
ATOM   3586  N   LEU A 508     -25.438 -42.909  11.789  1.00 22.22           N  
ANISOU 3586  N   LEU A 508     2844   3223   2375     35    -17    -89       N  
ATOM   3587  CA  LEU A 508     -24.448 -41.867  12.048  1.00 20.79           C  
ANISOU 3587  CA  LEU A 508     2678   3042   2180     10    -29    -87       C  
ATOM   3588  C   LEU A 508     -24.443 -41.429  13.502  1.00 21.24           C  
ANISOU 3588  C   LEU A 508     2774   3113   2182    -49    -32    -92       C  
ATOM   3589  O   LEU A 508     -23.384 -41.054  14.030  1.00 23.53           O  
ANISOU 3589  O   LEU A 508     3074   3410   2455    -88    -64    -72       O  
ATOM   3590  CB  LEU A 508     -24.719 -40.639  11.184  1.00 24.99           C  
ANISOU 3590  CB  LEU A 508     3219   3553   2721     38     -2   -120       C  
ATOM   3591  CG  LEU A 508     -23.896 -40.641   9.886  1.00 35.59           C  
ANISOU 3591  CG  LEU A 508     4540   4884   4100     69    -10   -104       C  
ATOM   3592  CD1 LEU A 508     -23.927 -39.258   9.124  1.00 37.66           C  
ANISOU 3592  CD1 LEU A 508     4820   5125   4363     83      8   -127       C  
ATOM   3593  CD2 LEU A 508     -22.435 -41.058  10.171  1.00 35.46           C  
ANISOU 3593  CD2 LEU A 508     4501   4876   4096     44    -42    -66       C  
ATOM   3594  N   TYR A 509     -25.626 -41.379  14.130  1.00 19.76           N  
ANISOU 3594  N   TYR A 509     2610   2930   1967    -60      3   -123       N  
ATOM   3595  CA  TYR A 509     -25.728 -40.869  15.508  1.00 21.43           C  
ANISOU 3595  CA  TYR A 509     2871   3154   2118   -124     14   -140       C  
ATOM   3596  C   TYR A 509     -24.783 -41.634  16.463  1.00 23.35           C  
ANISOU 3596  C   TYR A 509     3126   3419   2326   -181    -42    -89       C  
ATOM   3597  O   TYR A 509     -24.105 -41.036  17.301  1.00 24.43           O  
ANISOU 3597  O   TYR A 509     3300   3564   2417   -239    -64    -84       O  
ATOM   3598  CB  TYR A 509     -27.210 -40.954  15.950  1.00 18.07           C  
ANISOU 3598  CB  TYR A 509     2459   2728   1679   -123     70   -180       C  
ATOM   3599  CG  TYR A 509     -27.432 -40.742  17.466  1.00 20.59           C  
ANISOU 3599  CG  TYR A 509     2836   3063   1926   -198     92   -198       C  
ATOM   3600  CD1 TYR A 509     -27.546 -39.487  18.003  1.00 18.45           C  
ANISOU 3600  CD1 TYR A 509     2610   2780   1622   -227    132   -245       C  
ATOM   3601  CD2 TYR A 509     -27.586 -41.832  18.308  1.00 20.73           C  
ANISOU 3601  CD2 TYR A 509     2868   3104   1906   -241     77   -169       C  
ATOM   3602  CE1 TYR A 509     -27.792 -39.300  19.399  1.00 22.46           C  
ANISOU 3602  CE1 TYR A 509     3181   3299   2053   -304    162   -269       C  
ATOM   3603  CE2 TYR A 509     -27.844 -41.653  19.688  1.00 23.27           C  
ANISOU 3603  CE2 TYR A 509     3252   3440   2149   -319    102   -187       C  
ATOM   3604  CZ  TYR A 509     -27.926 -40.382  20.205  1.00 23.17           C  
ANISOU 3604  CZ  TYR A 509     3288   3417   2099   -351    146   -239       C  
ATOM   3605  OH  TYR A 509     -28.152 -40.250  21.533  1.00 24.72           O  
ANISOU 3605  OH  TYR A 509     3555   3627   2212   -434    175   -260       O  
ATOM   3606  N   ASN A 510     -24.737 -42.967  16.348  1.00 21.65           N  
ANISOU 3606  N   ASN A 510     2881   3210   2135   -169    -71    -47       N  
ATOM   3607  CA  ASN A 510     -23.808 -43.782  17.133  1.00 22.77           C  
ANISOU 3607  CA  ASN A 510     3024   3366   2262   -216   -135     13       C  
ATOM   3608  C   ASN A 510     -22.357 -43.380  16.881  1.00 23.18           C  
ANISOU 3608  C   ASN A 510     3052   3414   2340   -221   -184     46       C  
ATOM   3609  O   ASN A 510     -21.542 -43.380  17.803  1.00 23.54           O  
ANISOU 3609  O   ASN A 510     3116   3473   2354   -281   -238     84       O  
ATOM   3610  CB  ASN A 510     -23.935 -45.276  16.783  1.00 20.23           C  
ANISOU 3610  CB  ASN A 510     2662   3038   1984   -186   -155     52       C  
ATOM   3611  CG  ASN A 510     -25.137 -45.913  17.424  1.00 20.98           C  
ANISOU 3611  CG  ASN A 510     2784   3143   2044   -207   -126     41       C  
ATOM   3612  OD1 ASN A 510     -25.625 -45.429  18.440  1.00 20.00           O  
ANISOU 3612  OD1 ASN A 510     2712   3034   1852   -262   -103     19       O  
ATOM   3613  ND2 ASN A 510     -25.638 -47.058  16.819  1.00 20.32           N  
ANISOU 3613  ND2 ASN A 510     2667   3048   2006   -167   -122     54       N  
ATOM   3614  N   VAL A 511     -22.005 -43.119  15.627  1.00 23.65           N  
ANISOU 3614  N   VAL A 511     3070   3457   2460   -163   -170     36       N  
ATOM   3615  CA  VAL A 511     -20.628 -42.741  15.312  1.00 23.89           C  
ANISOU 3615  CA  VAL A 511     3070   3482   2524   -167   -208     65       C  
ATOM   3616  C   VAL A 511     -20.305 -41.398  15.928  1.00 21.36           C  
ANISOU 3616  C   VAL A 511     2794   3169   2153   -218   -210     43       C  
ATOM   3617  O   VAL A 511     -19.205 -41.190  16.438  1.00 23.10           O  
ANISOU 3617  O   VAL A 511     3010   3398   2371   -263   -263     78       O  
ATOM   3618  CB  VAL A 511     -20.387 -42.693  13.788  1.00 25.43           C  
ANISOU 3618  CB  VAL A 511     3221   3657   2786   -100   -179     53       C  
ATOM   3619  CG1 VAL A 511     -19.034 -42.072  13.537  1.00 27.42           C  
ANISOU 3619  CG1 VAL A 511     3446   3905   3067   -112   -205     74       C  
ATOM   3620  CG2 VAL A 511     -20.436 -44.078  13.179  1.00 25.44           C  
ANISOU 3620  CG2 VAL A 511     3178   3646   2841    -57   -181     78       C  
ATOM   3621  N   MET A 512     -21.236 -40.438  15.818  1.00 22.86           N  
ANISOU 3621  N   MET A 512     3024   3351   2311   -210   -154    -17       N  
ATOM   3622  CA  MET A 512     -20.994 -39.118  16.415  1.00 22.25           C  
ANISOU 3622  CA  MET A 512     2996   3272   2187   -259   -147    -46       C  
ATOM   3623  C   MET A 512     -20.871 -39.239  17.928  1.00 25.16           C  
ANISOU 3623  C   MET A 512     3416   3663   2481   -344   -180    -32       C  
ATOM   3624  O   MET A 512     -20.027 -38.569  18.555  1.00 25.35           O  
ANISOU 3624  O   MET A 512     3469   3693   2471   -406   -216    -22       O  
ATOM   3625  CB  MET A 512     -22.131 -38.172  16.023  1.00 22.17           C  
ANISOU 3625  CB  MET A 512     3013   3240   2169   -227    -76   -112       C  
ATOM   3626  CG  MET A 512     -22.059 -37.910  14.449  1.00 27.01           C  
ANISOU 3626  CG  MET A 512     3583   3831   2850   -154    -58   -116       C  
ATOM   3627  SD  MET A 512     -23.275 -36.634  13.952  1.00 30.08           S  
ANISOU 3627  SD  MET A 512     4001   4186   3243   -118      9   -181       S  
ATOM   3628  CE  MET A 512     -24.776 -37.601  14.141  1.00 27.95           C  
ANISOU 3628  CE  MET A 512     3721   3923   2975    -90     42   -197       C  
ATOM   3629  N   CYS A 513     -21.682 -40.113  18.530  1.00 23.09           N  
ANISOU 3629  N   CYS A 513     3171   3414   2190   -356   -170    -28       N  
ATOM   3630  CA  CYS A 513     -21.490 -40.392  19.966  1.00 24.76           C  
ANISOU 3630  CA  CYS A 513     3437   3648   2324   -445   -209     -4       C  
ATOM   3631  C   CYS A 513     -20.108 -40.962  20.247  1.00 28.57           C  
ANISOU 3631  C   CYS A 513     3889   4143   2825   -480   -306     75       C  
ATOM   3632  O   CYS A 513     -19.450 -40.526  21.195  1.00 28.71           O  
ANISOU 3632  O   CYS A 513     3949   4174   2784   -561   -354     93       O  
ATOM   3633  CB  CYS A 513     -22.558 -41.355  20.492  1.00 22.83           C  
ANISOU 3633  CB  CYS A 513     3210   3414   2049   -452   -183     -5       C  
ATOM   3634  SG  CYS A 513     -24.133 -40.463  20.637  1.00 26.60           S  
ANISOU 3634  SG  CYS A 513     3736   3880   2492   -443    -70   -100       S  
ATOM   3635  N   ASP A 514     -19.646 -41.938  19.441  1.00 28.05           N  
ANISOU 3635  N   ASP A 514     3746   4069   2842   -421   -336    122       N  
ATOM   3636  CA  ASP A 514     -18.292 -42.474  19.633  1.00 25.39           C  
ANISOU 3636  CA  ASP A 514     3364   3736   2547   -445   -426    199       C  
ATOM   3637  C   ASP A 514     -17.229 -41.373  19.500  1.00 26.34           C  
ANISOU 3637  C   ASP A 514     3475   3855   2677   -470   -452    198       C  
ATOM   3638  O   ASP A 514     -16.292 -41.306  20.303  1.00 29.13           O  
ANISOU 3638  O   ASP A 514     3834   4222   3011   -539   -529    247       O  
ATOM   3639  CB  ASP A 514     -17.982 -43.565  18.595  1.00 26.42           C  
ANISOU 3639  CB  ASP A 514     3410   3848   2782   -366   -432    234       C  
ATOM   3640  CG  ASP A 514     -18.783 -44.889  18.842  1.00 35.71           C  
ANISOU 3640  CG  ASP A 514     4588   5022   3957   -352   -430    255       C  
ATOM   3641  OD1 ASP A 514     -19.239 -45.172  19.984  1.00 37.26           O  
ANISOU 3641  OD1 ASP A 514     4841   5236   4080   -415   -451    270       O  
ATOM   3642  OD2 ASP A 514     -18.991 -45.635  17.853  1.00 39.14           O  
ANISOU 3642  OD2 ASP A 514     4972   5436   4463   -280   -402    254       O  
ATOM   3643  N   LEU A 515     -17.356 -40.502  18.490  1.00 23.50           N  
ANISOU 3643  N   LEU A 515     3102   3479   2347   -420   -392    147       N  
ATOM   3644  CA  LEU A 515     -16.368 -39.428  18.309  1.00 25.13           C  
ANISOU 3644  CA  LEU A 515     3301   3682   2566   -445   -411    145       C  
ATOM   3645  C   LEU A 515     -16.313 -38.484  19.487  1.00 27.04           C  
ANISOU 3645  C   LEU A 515     3624   3937   2715   -539   -431    126       C  
ATOM   3646  O   LEU A 515     -15.311 -37.800  19.657  1.00 28.22           O  
ANISOU 3646  O   LEU A 515     3768   4088   2866   -584   -475    143       O  
ATOM   3647  CB  LEU A 515     -16.697 -38.617  17.063  1.00 25.80           C  
ANISOU 3647  CB  LEU A 515     3373   3743   2685   -381   -338     91       C  
ATOM   3648  CG  LEU A 515     -16.592 -39.395  15.767  1.00 27.94           C  
ANISOU 3648  CG  LEU A 515     3572   4000   3044   -298   -315    106       C  
ATOM   3649  CD1 LEU A 515     -17.239 -38.581  14.610  1.00 27.75           C  
ANISOU 3649  CD1 LEU A 515     3558   3955   3031   -243   -242     49       C  
ATOM   3650  CD2 LEU A 515     -15.141 -39.687  15.460  1.00 28.61           C  
ANISOU 3650  CD2 LEU A 515     3585   4085   3203   -301   -365    162       C  
ATOM   3651  N   LEU A 516     -17.372 -38.405  20.289  1.00 27.79           N  
ANISOU 3651  N   LEU A 516     3794   4038   2727   -572   -395     86       N  
ATOM   3652  CA  LEU A 516     -17.404 -37.501  21.433  1.00 27.65           C  
ANISOU 3652  CA  LEU A 516     3867   4029   2611   -667   -401     56       C  
ATOM   3653  C   LEU A 516     -17.258 -38.216  22.775  1.00 29.61           C  
ANISOU 3653  C   LEU A 516     4162   4306   2784   -756   -468    104       C  
ATOM   3654  O   LEU A 516     -17.323 -37.567  23.832  1.00 26.66           O  
ANISOU 3654  O   LEU A 516     3877   3942   2312   -848   -472     78       O  
ATOM   3655  CB  LEU A 516     -18.715 -36.700  21.391  1.00 23.96           C  
ANISOU 3655  CB  LEU A 516     3458   3542   2102   -647   -296    -33       C  
ATOM   3656  CG  LEU A 516     -18.726 -35.700  20.215  1.00 25.20           C  
ANISOU 3656  CG  LEU A 516     3587   3667   2319   -581   -245    -76       C  
ATOM   3657  CD1 LEU A 516     -20.184 -35.185  19.981  1.00 24.55           C  
ANISOU 3657  CD1 LEU A 516     3539   3561   2230   -536   -144   -153       C  
ATOM   3658  CD2 LEU A 516     -17.697 -34.517  20.404  1.00 23.39           C  
ANISOU 3658  CD2 LEU A 516     3383   3429   2074   -640   -276    -81       C  
ATOM   3659  N   GLY A 517     -17.115 -39.541  22.771  1.00 27.70           N  
ANISOU 3659  N   GLY A 517     3871   4074   2581   -734   -516    169       N  
ATOM   3660  CA  GLY A 517     -17.042 -40.221  24.046  1.00 27.19           C  
ANISOU 3660  CA  GLY A 517     3857   4033   2440   -822   -583    219       C  
ATOM   3661  C   GLY A 517     -18.355 -40.403  24.757  1.00 28.69           C  
ANISOU 3661  C   GLY A 517     4128   4231   2541   -852   -516    173       C  
ATOM   3662  O   GLY A 517     -18.374 -40.480  25.995  1.00 30.66           O  
ANISOU 3662  O   GLY A 517     4459   4501   2688   -954   -552    189       O  
ATOM   3663  N   LEU A 518     -19.466 -40.457  24.026  1.00 29.03           N  
ANISOU 3663  N   LEU A 518     4155   4259   2618   -772   -419    115       N  
ATOM   3664  CA  LEU A 518     -20.801 -40.420  24.605  1.00 27.93           C  
ANISOU 3664  CA  LEU A 518     4084   4123   2406   -794   -335     55       C  
ATOM   3665  C   LEU A 518     -21.438 -41.802  24.495  1.00 26.08           C  
ANISOU 3665  C   LEU A 518     3817   3893   2199   -757   -333     91       C  
ATOM   3666  O   LEU A 518     -21.267 -42.481  23.482  1.00 26.89           O  
ANISOU 3666  O   LEU A 518     3835   3983   2399   -672   -347    121       O  
ATOM   3667  CB  LEU A 518     -21.680 -39.401  23.856  1.00 28.99           C  
ANISOU 3667  CB  LEU A 518     4217   4230   2567   -730   -226    -37       C  
ATOM   3668  CG  LEU A 518     -21.247 -37.922  23.849  1.00 27.72           C  
ANISOU 3668  CG  LEU A 518     4092   4054   2387   -755   -208    -86       C  
ATOM   3669  CD1 LEU A 518     -22.175 -37.158  22.886  1.00 25.58           C  
ANISOU 3669  CD1 LEU A 518     3798   3749   2172   -669   -109   -161       C  
ATOM   3670  CD2 LEU A 518     -21.413 -37.368  25.235  1.00 26.73           C  
ANISOU 3670  CD2 LEU A 518     4078   3939   2140   -870   -193   -120       C  
ATOM   3671  N   LYS A 519     -22.178 -42.200  25.510  1.00 25.65           N  
ANISOU 3671  N   LYS A 519     3832   3855   2059   -823   -310     84       N  
ATOM   3672  CA  LYS A 519     -23.050 -43.390  25.388  1.00 27.45           C  
ANISOU 3672  CA  LYS A 519     4036   4083   2310   -788   -285    100       C  
ATOM   3673  C   LYS A 519     -24.301 -42.998  24.603  1.00 27.71           C  
ANISOU 3673  C   LYS A 519     4045   4099   2385   -710   -170     18       C  
ATOM   3674  O   LYS A 519     -25.019 -42.089  25.030  1.00 27.78           O  
ANISOU 3674  O   LYS A 519     4109   4104   2340   -739    -89    -56       O  
ATOM   3675  CB  LYS A 519     -23.464 -43.930  26.752  1.00 32.00           C  
ANISOU 3675  CB  LYS A 519     4700   4683   2776   -892   -292    120       C  
ATOM   3676  CG  LYS A 519     -24.304 -45.167  26.599  1.00 36.62           C  
ANISOU 3676  CG  LYS A 519     5257   5266   3391   -858   -270    142       C  
ATOM   3677  CD  LYS A 519     -24.624 -45.824  27.949  1.00 45.18           C  
ANISOU 3677  CD  LYS A 519     6428   6372   4364   -967   -287    176       C  
ATOM   3678  CE  LYS A 519     -25.608 -47.034  27.790  1.00 48.85           C  
ANISOU 3678  CE  LYS A 519     6868   6833   4859   -936   -250    190       C  
ATOM   3679  NZ  LYS A 519     -25.912 -47.692  29.136  1.00 53.01           N  
ANISOU 3679  NZ  LYS A 519     7487   7381   5272  -1052   -266    228       N  
ATOM   3680  N   PRO A 520     -24.576 -43.617  23.456  1.00 25.28           N  
ANISOU 3680  N   PRO A 520     3655   3775   2174   -614   -160     27       N  
ATOM   3681  CA  PRO A 520     -25.786 -43.253  22.689  1.00 26.64           C  
ANISOU 3681  CA  PRO A 520     3802   3932   2390   -544    -64    -44       C  
ATOM   3682  C   PRO A 520     -27.059 -43.544  23.455  1.00 28.25           C  
ANISOU 3682  C   PRO A 520     4049   4145   2541   -582      9    -80       C  
ATOM   3683  O   PRO A 520     -27.130 -44.486  24.243  1.00 28.85           O  
ANISOU 3683  O   PRO A 520     4156   4238   2569   -638    -18    -38       O  
ATOM   3684  CB  PRO A 520     -25.706 -44.135  21.428  1.00 26.47           C  
ANISOU 3684  CB  PRO A 520     3693   3896   2469   -453    -88    -10       C  
ATOM   3685  CG  PRO A 520     -24.298 -44.660  21.397  1.00 26.48           C  
ANISOU 3685  CG  PRO A 520     3668   3899   2494   -464   -186     66       C  
ATOM   3686  CD  PRO A 520     -23.861 -44.750  22.856  1.00 24.18           C  
ANISOU 3686  CD  PRO A 520     3447   3630   2110   -570   -235    103       C  
ATOM   3687  N   ALA A 521     -28.078 -42.730  23.210  1.00 26.03           N  
ANISOU 3687  N   ALA A 521     3768   3848   2273   -551    103   -158       N  
ATOM   3688  CA  ALA A 521     -29.434 -43.096  23.629  1.00 27.26           C  
ANISOU 3688  CA  ALA A 521     3935   4008   2413   -563    185   -196       C  
ATOM   3689  C   ALA A 521     -29.957 -44.245  22.740  1.00 24.02           C  
ANISOU 3689  C   ALA A 521     3451   3595   2082   -494    173   -165       C  
ATOM   3690  O   ALA A 521     -29.460 -44.441  21.633  1.00 24.63           O  
ANISOU 3690  O   ALA A 521     3468   3659   2232   -424    126   -138       O  
ATOM   3691  CB  ALA A 521     -30.362 -41.880  23.499  1.00 28.32           C  
ANISOU 3691  CB  ALA A 521     4074   4120   2566   -537    288   -286       C  
ATOM   3692  N   PRO A 522     -30.915 -45.046  23.227  1.00 24.40           N  
ANISOU 3692  N   PRO A 522     3506   3653   2111   -520    214   -167       N  
ATOM   3693  CA  PRO A 522     -31.461 -46.160  22.408  1.00 24.92           C  
ANISOU 3693  CA  PRO A 522     3506   3713   2250   -462    202   -140       C  
ATOM   3694  C   PRO A 522     -31.915 -45.663  21.034  1.00 24.14           C  
ANISOU 3694  C   PRO A 522     3334   3591   2246   -365    226   -176       C  
ATOM   3695  O   PRO A 522     -32.651 -44.683  20.929  1.00 26.53           O  
ANISOU 3695  O   PRO A 522     3632   3883   2567   -345    296   -238       O  
ATOM   3696  CB  PRO A 522     -32.654 -46.672  23.245  1.00 24.20           C  
ANISOU 3696  CB  PRO A 522     3440   3634   2120   -514    273   -162       C  
ATOM   3697  CG  PRO A 522     -32.313 -46.235  24.700  1.00 26.48           C  
ANISOU 3697  CG  PRO A 522     3827   3943   2292   -621    288   -169       C  
ATOM   3698  CD  PRO A 522     -31.632 -44.882  24.519  1.00 25.60           C  
ANISOU 3698  CD  PRO A 522     3731   3820   2176   -607    285   -204       C  
ATOM   3699  N   ASN A 523     -31.421 -46.284  19.968  1.00 21.70           N  
ANISOU 3699  N   ASN A 523     2973   3271   1999   -306    167   -136       N  
ATOM   3700  CA  ASN A 523     -31.793 -45.769  18.638  1.00 20.94           C  
ANISOU 3700  CA  ASN A 523     2820   3154   1982   -224    183   -166       C  
ATOM   3701  C   ASN A 523     -31.816 -46.929  17.651  1.00 22.59           C  
ANISOU 3701  C   ASN A 523     2979   3355   2249   -177    142   -129       C  
ATOM   3702  O   ASN A 523     -31.696 -48.092  18.052  1.00 22.06           O  
ANISOU 3702  O   ASN A 523     2919   3294   2168   -206    113    -87       O  
ATOM   3703  CB  ASN A 523     -30.837 -44.636  18.222  1.00 19.88           C  
ANISOU 3703  CB  ASN A 523     2693   3010   1852   -203    161   -175       C  
ATOM   3704  CG  ASN A 523     -29.379 -45.135  18.040  1.00 23.22           C  
ANISOU 3704  CG  ASN A 523     3114   3435   2273   -208     79   -114       C  
ATOM   3705  OD1 ASN A 523     -28.980 -45.491  16.907  1.00 21.95           O  
ANISOU 3705  OD1 ASN A 523     2909   3261   2171   -152     48    -94       O  
ATOM   3706  ND2 ASN A 523     -28.605 -45.184  19.135  1.00 21.37           N  
ANISOU 3706  ND2 ASN A 523     2927   3216   1975   -277     46    -85       N  
ATOM   3707  N   ASN A 524     -31.995 -46.618  16.345  1.00 21.94           N  
ANISOU 3707  N   ASN A 524     2852   3255   2230   -109    140   -145       N  
ATOM   3708  CA  ASN A 524     -32.142 -47.668  15.328  1.00 23.73           C  
ANISOU 3708  CA  ASN A 524     3038   3471   2508    -69    111   -121       C  
ATOM   3709  C   ASN A 524     -30.864 -48.011  14.588  1.00 23.93           C  
ANISOU 3709  C   ASN A 524     3054   3485   2555    -43     55    -84       C  
ATOM   3710  O   ASN A 524     -30.882 -48.948  13.773  1.00 25.58           O  
ANISOU 3710  O   ASN A 524     3237   3680   2803    -15     35    -66       O  
ATOM   3711  CB  ASN A 524     -33.266 -47.273  14.356  1.00 23.13           C  
ANISOU 3711  CB  ASN A 524     2920   3382   2484    -20    141   -158       C  
ATOM   3712  CG  ASN A 524     -34.537 -47.032  15.140  1.00 26.22           C  
ANISOU 3712  CG  ASN A 524     3309   3783   2870    -45    203   -194       C  
ATOM   3713  OD1 ASN A 524     -35.177 -45.968  15.060  1.00 23.56           O  
ANISOU 3713  OD1 ASN A 524     2960   3438   2555    -26    245   -235       O  
ATOM   3714  ND2 ASN A 524     -34.887 -48.033  15.968  1.00 29.33           N  
ANISOU 3714  ND2 ASN A 524     3716   4191   3237    -91    213   -176       N  
ATOM   3715  N   GLY A 525     -29.738 -47.338  14.875  1.00 20.87           N  
ANISOU 3715  N   GLY A 525     2686   3099   2144    -56     32    -72       N  
ATOM   3716  CA  GLY A 525     -28.475 -47.793  14.321  1.00 20.52           C  
ANISOU 3716  CA  GLY A 525     2626   3044   2128    -38    -17    -32       C  
ATOM   3717  C   GLY A 525     -28.078 -49.125  14.969  1.00 24.46           C  
ANISOU 3717  C   GLY A 525     3126   3541   2625    -68    -55     20       C  
ATOM   3718  O   GLY A 525     -28.667 -49.583  15.971  1.00 24.47           O  
ANISOU 3718  O   GLY A 525     3153   3556   2588   -113    -48     29       O  
ATOM   3719  N   THR A 526     -27.100 -49.784  14.377  1.00 23.31           N  
ANISOU 3719  N   THR A 526     2955   3377   2526    -43    -92     55       N  
ATOM   3720  CA  THR A 526     -26.594 -51.048  14.925  1.00 22.39           C  
ANISOU 3720  CA  THR A 526     2834   3250   2424    -64   -134    112       C  
ATOM   3721  C   THR A 526     -25.175 -50.701  15.366  1.00 23.41           C  
ANISOU 3721  C   THR A 526     2958   3380   2556    -83   -183    152       C  
ATOM   3722  O   THR A 526     -24.297 -50.465  14.535  1.00 24.12           O  
ANISOU 3722  O   THR A 526     3016   3455   2694    -45   -190    154       O  
ATOM   3723  CB  THR A 526     -26.638 -52.183  13.904  1.00 25.02           C  
ANISOU 3723  CB  THR A 526     3133   3550   2823    -19   -134    119       C  
ATOM   3724  OG1 THR A 526     -28.025 -52.494  13.609  1.00 25.54           O  
ANISOU 3724  OG1 THR A 526     3204   3619   2881    -13    -97     85       O  
ATOM   3725  CG2 THR A 526     -25.869 -53.448  14.440  1.00 24.18           C  
ANISOU 3725  CG2 THR A 526     3016   3421   2751    -34   -184    185       C  
ATOM   3726  N   HIS A 527     -24.997 -50.535  16.681  1.00 24.15           N  
ANISOU 3726  N   HIS A 527     3090   3495   2592   -147   -212    180       N  
ATOM   3727  CA  HIS A 527     -23.776 -49.945  17.218  1.00 21.25           C  
ANISOU 3727  CA  HIS A 527     2726   3136   2213   -178   -262    213       C  
ATOM   3728  C   HIS A 527     -22.605 -50.904  17.021  1.00 25.41           C  
ANISOU 3728  C   HIS A 527     3205   3636   2815   -160   -322    279       C  
ATOM   3729  O   HIS A 527     -22.609 -52.022  17.549  1.00 24.27           O  
ANISOU 3729  O   HIS A 527     3061   3479   2683   -179   -359    329       O  
ATOM   3730  CB  HIS A 527     -23.954 -49.628  18.697  1.00 23.04           C  
ANISOU 3730  CB  HIS A 527     3014   3391   2349   -263   -281    227       C  
ATOM   3731  CG  HIS A 527     -22.983 -48.593  19.215  1.00 25.40           C  
ANISOU 3731  CG  HIS A 527     3331   3704   2614   -304   -317    236       C  
ATOM   3732  ND1 HIS A 527     -22.938 -48.219  20.550  1.00 28.62           N  
ANISOU 3732  ND1 HIS A 527     3804   4138   2933   -390   -342    250       N  
ATOM   3733  CD2 HIS A 527     -22.006 -47.890  18.591  1.00 25.14           C  
ANISOU 3733  CD2 HIS A 527     3265   3665   2623   -277   -332    235       C  
ATOM   3734  CE1 HIS A 527     -21.980 -47.323  20.724  1.00 29.72           C  
ANISOU 3734  CE1 HIS A 527     3948   4285   3061   -415   -376    257       C  
ATOM   3735  NE2 HIS A 527     -21.405 -47.091  19.552  1.00 28.24           N  
ANISOU 3735  NE2 HIS A 527     3697   4078   2954   -346   -370    248       N  
ATOM   3736  N   GLY A 528     -21.568 -50.447  16.319  1.00 22.85           N  
ANISOU 3736  N   GLY A 528     2838   3300   2544   -128   -332    282       N  
ATOM   3737  CA  GLY A 528     -20.473 -51.298  15.923  1.00 21.84           C  
ANISOU 3737  CA  GLY A 528     2650   3139   2508    -97   -372    334       C  
ATOM   3738  C   GLY A 528     -20.453 -51.596  14.428  1.00 21.11           C  
ANISOU 3738  C   GLY A 528     2515   3016   2490    -23   -319    298       C  
ATOM   3739  O   GLY A 528     -19.411 -51.995  13.919  1.00 26.12           O  
ANISOU 3739  O   GLY A 528     3095   3623   3208      8   -333    325       O  
ATOM   3740  N   SER A 529     -21.575 -51.411  13.717  1.00 19.78           N  
ANISOU 3740  N   SER A 529     2370   2852   2294      3   -259    237       N  
ATOM   3741  CA  SER A 529     -21.588 -51.691  12.276  1.00 21.92           C  
ANISOU 3741  CA  SER A 529     2613   3095   2620     62   -212    202       C  
ATOM   3742  C   SER A 529     -20.753 -50.708  11.431  1.00 24.62           C  
ANISOU 3742  C   SER A 529     2933   3437   2985     85   -190    180       C  
ATOM   3743  O   SER A 529     -20.457 -51.015  10.260  1.00 25.60           O  
ANISOU 3743  O   SER A 529     3032   3535   3161    127   -154    159       O  
ATOM   3744  CB  SER A 529     -23.052 -51.705  11.779  1.00 23.24           C  
ANISOU 3744  CB  SER A 529     2813   3270   2748     74   -166    150       C  
ATOM   3745  OG  SER A 529     -23.574 -50.401  11.691  1.00 26.13           O  
ANISOU 3745  OG  SER A 529     3205   3663   3060     67   -140    108       O  
ATOM   3746  N   LEU A 530     -20.378 -49.536  11.975  1.00 22.89           N  
ANISOU 3746  N   LEU A 530     2727   3245   2724     53   -207    180       N  
ATOM   3747  CA  LEU A 530     -19.510 -48.568  11.286  1.00 22.64           C  
ANISOU 3747  CA  LEU A 530     2676   3213   2713     66   -191    165       C  
ATOM   3748  C   LEU A 530     -18.151 -48.415  11.990  1.00 24.65           C  
ANISOU 3748  C   LEU A 530     2895   3471   3002     37   -245    218       C  
ATOM   3749  O   LEU A 530     -17.447 -47.410  11.809  1.00 23.28           O  
ANISOU 3749  O   LEU A 530     2712   3306   2828     26   -244    211       O  
ATOM   3750  CB  LEU A 530     -20.188 -47.193  11.177  1.00 24.22           C  
ANISOU 3750  CB  LEU A 530     2922   3437   2845     54   -162    117       C  
ATOM   3751  CG  LEU A 530     -21.506 -47.078  10.389  1.00 24.10           C  
ANISOU 3751  CG  LEU A 530     2935   3420   2802     82   -115     66       C  
ATOM   3752  CD1 LEU A 530     -21.954 -45.604  10.274  1.00 23.71           C  
ANISOU 3752  CD1 LEU A 530     2920   3384   2704     74    -93     27       C  
ATOM   3753  CD2 LEU A 530     -21.342 -47.732   9.021  1.00 25.48           C  
ANISOU 3753  CD2 LEU A 530     3086   3567   3028    128    -83     53       C  
ATOM   3754  N   ASN A 531     -17.712 -49.440  12.726  1.00 26.83           N  
ANISOU 3754  N   ASN A 531     3143   3734   3316     24   -297    276       N  
ATOM   3755  CA  ASN A 531     -16.377 -49.380  13.338  1.00 26.82           C  
ANISOU 3755  CA  ASN A 531     3096   3731   3363     -3   -360    336       C  
ATOM   3756  C   ASN A 531     -15.284 -49.249  12.275  1.00 27.29           C  
ANISOU 3756  C   ASN A 531     3088   3766   3514     38   -330    332       C  
ATOM   3757  O   ASN A 531     -14.215 -48.670  12.535  1.00 27.72           O  
ANISOU 3757  O   ASN A 531     3106   3828   3599     15   -365    361       O  
ATOM   3758  CB  ASN A 531     -16.101 -50.638  14.194  1.00 24.63           C  
ANISOU 3758  CB  ASN A 531     2795   3435   3128    -17   -426    407       C  
ATOM   3759  CG  ASN A 531     -16.702 -50.533  15.589  1.00 26.64           C  
ANISOU 3759  CG  ASN A 531     3113   3721   3286    -86   -479    433       C  
ATOM   3760  OD1 ASN A 531     -17.156 -49.479  15.974  1.00 26.44           O  
ANISOU 3760  OD1 ASN A 531     3143   3731   3173   -124   -467    397       O  
ATOM   3761  ND2 ASN A 531     -16.663 -51.646  16.377  1.00 25.31           N  
ANISOU 3761  ND2 ASN A 531     2941   3538   3137   -106   -538    496       N  
ATOM   3762  N   HIS A 532     -15.522 -49.777  11.078  1.00 26.55           N  
ANISOU 3762  N   HIS A 532     2980   3643   3464     93   -264    295       N  
ATOM   3763  CA  HIS A 532     -14.508 -49.704  10.035  1.00 25.99           C  
ANISOU 3763  CA  HIS A 532     2850   3547   3477    128   -221    285       C  
ATOM   3764  C   HIS A 532     -14.346 -48.285   9.478  1.00 27.47           C  
ANISOU 3764  C   HIS A 532     3059   3758   3620    117   -185    244       C  
ATOM   3765  O   HIS A 532     -13.509 -48.105   8.607  1.00 30.39           O  
ANISOU 3765  O   HIS A 532     3387   4111   4050    138   -143    233       O  
ATOM   3766  CB  HIS A 532     -14.847 -50.662   8.886  1.00 25.89           C  
ANISOU 3766  CB  HIS A 532     2831   3496   3511    182   -152    249       C  
ATOM   3767  CG  HIS A 532     -16.195 -50.423   8.272  1.00 27.27           C  
ANISOU 3767  CG  HIS A 532     3076   3683   3600    189   -107    189       C  
ATOM   3768  ND1 HIS A 532     -17.374 -50.798   8.874  1.00 28.07           N  
ANISOU 3768  ND1 HIS A 532     3225   3798   3642    175   -129    187       N  
ATOM   3769  CD2 HIS A 532     -16.543 -49.855   7.088  1.00 26.24           C  
ANISOU 3769  CD2 HIS A 532     2977   3555   3440    206    -43    133       C  
ATOM   3770  CE1 HIS A 532     -18.399 -50.433   8.113  1.00 27.32           C  
ANISOU 3770  CE1 HIS A 532     3179   3713   3490    186    -84    133       C  
ATOM   3771  NE2 HIS A 532     -17.918 -49.859   7.021  1.00 27.17           N  
ANISOU 3771  NE2 HIS A 532     3152   3686   3484    204    -36    102       N  
ATOM   3772  N   LEU A 533     -15.151 -47.308   9.901  1.00 24.75           N  
ANISOU 3772  N   LEU A 533     2780   3448   3177     85   -194    218       N  
ATOM   3773  CA  LEU A 533     -14.882 -45.914   9.532  1.00 26.23           C  
ANISOU 3773  CA  LEU A 533     2986   3652   3329     68   -172    190       C  
ATOM   3774  C   LEU A 533     -13.770 -45.289  10.373  1.00 25.68           C  
ANISOU 3774  C   LEU A 533     2885   3597   3277     22   -229    233       C  
ATOM   3775  O   LEU A 533     -13.196 -44.261   9.972  1.00 27.88           O  
ANISOU 3775  O   LEU A 533     3158   3880   3554      8   -212    218       O  
ATOM   3776  CB  LEU A 533     -16.152 -45.062   9.694  1.00 23.71           C  
ANISOU 3776  CB  LEU A 533     2744   3354   2910     53   -158    146       C  
ATOM   3777  CG  LEU A 533     -17.108 -45.029   8.500  1.00 26.25           C  
ANISOU 3777  CG  LEU A 533     3099   3665   3209     93    -96     94       C  
ATOM   3778  CD1 LEU A 533     -17.670 -46.453   8.168  1.00 27.32           C  
ANISOU 3778  CD1 LEU A 533     3224   3781   3374    126    -82     95       C  
ATOM   3779  CD2 LEU A 533     -18.258 -44.095   8.834  1.00 26.16           C  
ANISOU 3779  CD2 LEU A 533     3150   3672   3117     76    -92     61       C  
ATOM   3780  N   LEU A 534     -13.498 -45.840  11.553  1.00 23.99           N  
ANISOU 3780  N   LEU A 534     2655   3390   3071    -10   -303    287       N  
ATOM   3781  CA  LEU A 534     -12.744 -45.144  12.586  1.00 23.93           C  
ANISOU 3781  CA  LEU A 534     2644   3404   3046    -73   -373    326       C  
ATOM   3782  C   LEU A 534     -11.371 -45.759  12.780  1.00 27.15           C  
ANISOU 3782  C   LEU A 534     2958   3795   3563    -74   -425    394       C  
ATOM   3783  O   LEU A 534     -11.205 -46.990  12.720  1.00 28.45           O  
ANISOU 3783  O   LEU A 534     3075   3933   3803    -40   -436    428       O  
ATOM   3784  CB  LEU A 534     -13.497 -45.203  13.922  1.00 28.45           C  
ANISOU 3784  CB  LEU A 534     3280   4000   3528   -125   -427    342       C  
ATOM   3785  CG  LEU A 534     -14.864 -44.571  13.850  1.00 29.00           C  
ANISOU 3785  CG  LEU A 534     3433   4084   3501   -125   -374    276       C  
ATOM   3786  CD1 LEU A 534     -15.575 -44.678  15.186  1.00 28.73           C  
ANISOU 3786  CD1 LEU A 534     3462   4073   3383   -181   -415    288       C  
ATOM   3787  CD2 LEU A 534     -14.759 -43.139  13.366  1.00 26.48           C  
ANISOU 3787  CD2 LEU A 534     3139   3771   3150   -134   -338    231       C  
ATOM   3788  N   ARG A 535     -10.395 -44.900  13.046  1.00 25.28           N  
ANISOU 3788  N   ARG A 535     2693   3570   3341   -115   -460    415       N  
ATOM   3789  CA  ARG A 535      -9.059 -45.376  13.367  1.00 32.75           C  
ANISOU 3789  CA  ARG A 535     3543   4504   4398   -126   -523    487       C  
ATOM   3790  C   ARG A 535      -8.946 -45.755  14.845  1.00 37.39           C  
ANISOU 3790  C   ARG A 535     4143   5107   4956   -186   -637    557       C  
ATOM   3791  O   ARG A 535      -8.104 -46.579  15.187  1.00 38.04           O  
ANISOU 3791  O   ARG A 535     4147   5170   5137   -183   -701    629       O  
ATOM   3792  CB  ARG A 535      -8.034 -44.296  12.971  1.00 34.60           C  
ANISOU 3792  CB  ARG A 535     3736   4745   4666   -148   -513    482       C  
ATOM   3793  CG  ARG A 535      -6.772 -44.258  13.783  1.00 42.01           C  
ANISOU 3793  CG  ARG A 535     4601   5689   5674   -198   -611    559       C  
ATOM   3794  CD  ARG A 535      -5.994 -42.930  13.690  1.00 43.68           C  
ANISOU 3794  CD  ARG A 535     4801   5917   5877   -247   -615    550       C  
ATOM   3795  NE  ARG A 535      -5.872 -42.532  12.309  1.00 46.89           N  
ANISOU 3795  NE  ARG A 535     5188   6308   6321   -198   -506    494       N  
ATOM   3796  CZ  ARG A 535      -4.952 -42.999  11.458  1.00 48.68           C  
ANISOU 3796  CZ  ARG A 535     5312   6506   6679   -155   -461    507       C  
ATOM   3797  NH1 ARG A 535      -4.043 -43.898  11.851  1.00 50.52           N  
ANISOU 3797  NH1 ARG A 535     5440   6719   7034   -146   -519    577       N  
ATOM   3798  NH2 ARG A 535      -4.965 -42.575  10.203  1.00 46.78           N  
ANISOU 3798  NH2 ARG A 535     5074   6254   6447   -121   -355    449       N  
ATOM   3799  N   THR A 536      -9.793 -45.193  15.714  1.00 40.21           N  
ANISOU 3799  N   THR A 536     4599   5496   5182   -243   -662    538       N  
ATOM   3800  CA  THR A 536      -9.804 -45.457  17.168  1.00 42.29           C  
ANISOU 3800  CA  THR A 536     4900   5779   5388   -316   -765    598       C  
ATOM   3801  C   THR A 536     -11.177 -45.067  17.720  1.00 41.12           C  
ANISOU 3801  C   THR A 536     4871   5656   5097   -349   -735    544       C  
ATOM   3802  O   THR A 536     -12.064 -44.635  16.981  1.00 37.96           O  
ANISOU 3802  O   THR A 536     4510   5254   4657   -309   -645    469       O  
ATOM   3803  CB  THR A 536      -8.666 -44.700  17.883  1.00 45.26           C  
ANISOU 3803  CB  THR A 536     5252   6175   5771   -392   -854    647       C  
ATOM   3804  OG1 THR A 536      -8.646 -45.085  19.259  1.00 49.86           O  
ANISOU 3804  OG1 THR A 536     5872   6774   6297   -468   -961    712       O  
ATOM   3805  CG2 THR A 536      -8.840 -43.157  17.812  1.00 43.13           C  
ANISOU 3805  CG2 THR A 536     5048   5929   5410   -434   -815    581       C  
ATOM   3806  N   ASN A 537     -11.366 -45.207  19.040  1.00 44.82           N  
ANISOU 3806  N   ASN A 537     5397   6146   5485   -425   -812    584       N  
ATOM   3807  CA  ASN A 537     -12.666 -44.918  19.678  1.00 46.57           C  
ANISOU 3807  CA  ASN A 537     5731   6390   5575   -462   -778    535       C  
ATOM   3808  C   ASN A 537     -13.752 -45.850  19.140  1.00 42.81           C  
ANISOU 3808  C   ASN A 537     5260   5897   5110   -395   -712    506       C  
ATOM   3809  O   ASN A 537     -14.925 -45.485  19.105  1.00 41.99           O  
ANISOU 3809  O   ASN A 537     5224   5803   4928   -392   -644    441       O  
ATOM   3810  CB  ASN A 537     -13.130 -43.454  19.475  1.00 52.50           C  
ANISOU 3810  CB  ASN A 537     6545   7155   6246   -480   -712    451       C  
ATOM   3811  CG  ASN A 537     -12.428 -42.441  20.396  1.00 55.83           C  
ANISOU 3811  CG  ASN A 537     7007   7600   6607   -576   -776    466       C  
ATOM   3812  OD1 ASN A 537     -11.520 -42.777  21.147  1.00 59.01           O  
ANISOU 3812  OD1 ASN A 537     7385   8011   7027   -633   -878    543       O  
ATOM   3813  ND2 ASN A 537     -12.876 -41.197  20.337  1.00 55.49           N  
ANISOU 3813  ND2 ASN A 537     7028   7563   6493   -597   -719    394       N  
ATOM   3814  N   THR A 538     -13.381 -47.030  18.662  1.00 40.23           N  
ANISOU 3814  N   THR A 538     4859   5540   4887   -340   -726    551       N  
ATOM   3815  CA  THR A 538     -14.422 -47.923  18.225  1.00 41.85           C  
ANISOU 3815  CA  THR A 538     5077   5729   5096   -287   -669    525       C  
ATOM   3816  C   THR A 538     -15.158 -48.469  19.452  1.00 43.22           C  
ANISOU 3816  C   THR A 538     5321   5918   5182   -349   -712    554       C  
ATOM   3817  O   THR A 538     -14.730 -48.341  20.603  1.00 43.80           O  
ANISOU 3817  O   THR A 538     5427   6012   5205   -429   -794    607       O  
ATOM   3818  CB  THR A 538     -13.867 -49.060  17.366  1.00 40.67           C  
ANISOU 3818  CB  THR A 538     4836   5536   5081   -213   -664    558       C  
ATOM   3819  OG1 THR A 538     -12.815 -49.699  18.065  1.00 42.20           O  
ANISOU 3819  OG1 THR A 538     4977   5717   5342   -241   -764    651       O  
ATOM   3820  CG2 THR A 538     -13.346 -48.586  15.996  1.00 40.07           C  
ANISOU 3820  CG2 THR A 538     4701   5442   5080   -150   -595    513       C  
ATOM   3821  N   PHE A 539     -16.322 -49.028  19.196  1.00 42.54           N  
ANISOU 3821  N   PHE A 539     5266   5826   5072   -317   -652    517       N  
ATOM   3822  CA  PHE A 539     -17.173 -49.535  20.255  1.00 39.46           C  
ANISOU 3822  CA  PHE A 539     4947   5452   4596   -374   -672    534       C  
ATOM   3823  C   PHE A 539     -16.971 -51.025  20.200  1.00 38.43           C  
ANISOU 3823  C   PHE A 539     4769   5286   4548   -343   -712    600       C  
ATOM   3824  O   PHE A 539     -16.987 -51.599  19.105  1.00 41.25           O  
ANISOU 3824  O   PHE A 539     5068   5609   4995   -263   -667    582       O  
ATOM   3825  CB  PHE A 539     -18.630 -49.145  19.989  1.00 37.56           C  
ANISOU 3825  CB  PHE A 539     4763   5224   4285   -359   -575    449       C  
ATOM   3826  CG  PHE A 539     -19.626 -49.916  20.803  1.00 35.73           C  
ANISOU 3826  CG  PHE A 539     4587   5000   3989   -398   -572    460       C  
ATOM   3827  CD1 PHE A 539     -19.803 -49.636  22.156  1.00 34.81           C  
ANISOU 3827  CD1 PHE A 539     4549   4913   3765   -495   -608    479       C  
ATOM   3828  CD2 PHE A 539     -20.412 -50.909  20.203  1.00 32.93           C  
ANISOU 3828  CD2 PHE A 539     4212   4622   3677   -345   -531    449       C  
ATOM   3829  CE1 PHE A 539     -20.750 -50.355  22.914  1.00 34.58           C  
ANISOU 3829  CE1 PHE A 539     4576   4891   3672   -538   -597    488       C  
ATOM   3830  CE2 PHE A 539     -21.349 -51.642  20.966  1.00 33.19           C  
ANISOU 3830  CE2 PHE A 539     4296   4662   3653   -386   -526    462       C  
ATOM   3831  CZ  PHE A 539     -21.507 -51.358  22.317  1.00 32.92           C  
ANISOU 3831  CZ  PHE A 539     4338   4659   3512   -482   -557    482       C  
ATOM   3832  N   ARG A 540     -16.758 -51.642  21.330  1.00 32.65           N  
ANISOU 3832  N   ARG A 540     4062   4556   3785   -408   -796    675       N  
ATOM   3833  CA  ARG A 540     -16.592 -53.098  21.255  1.00 32.57           C  
ANISOU 3833  CA  ARG A 540     4007   4504   3864   -375   -835    741       C  
ATOM   3834  C   ARG A 540     -17.952 -53.801  21.408  1.00 34.98           C  
ANISOU 3834  C   ARG A 540     4369   4808   4112   -377   -784    714       C  
ATOM   3835  O   ARG A 540     -18.492 -53.858  22.516  1.00 37.03           O  
ANISOU 3835  O   ARG A 540     4707   5094   4270   -457   -811    735       O  
ATOM   3836  CB  ARG A 540     -15.602 -53.568  22.345  1.00 35.01           C  
ANISOU 3836  CB  ARG A 540     4306   4808   4189   -439   -966    853       C  
ATOM   3837  N   PRO A 541     -18.570 -54.316  20.350  1.00 36.50           N  
ANISOU 3837  N   PRO A 541     4533   4974   4362   -301   -708    666       N  
ATOM   3838  CA  PRO A 541     -19.910 -54.903  20.506  1.00 37.45           C  
ANISOU 3838  CA  PRO A 541     4705   5096   4426   -311   -659    637       C  
ATOM   3839  C   PRO A 541     -19.811 -56.312  21.077  1.00 40.15           C  
ANISOU 3839  C   PRO A 541     5044   5404   4807   -328   -723    721       C  
ATOM   3840  O   PRO A 541     -18.781 -56.975  20.965  1.00 41.50           O  
ANISOU 3840  O   PRO A 541     5153   5533   5080   -302   -786    789       O  
ATOM   3841  CB  PRO A 541     -20.479 -54.921  19.074  1.00 36.94           C  
ANISOU 3841  CB  PRO A 541     4606   5013   4417   -225   -566    560       C  
ATOM   3842  CG  PRO A 541     -19.256 -55.034  18.197  1.00 38.75           C  
ANISOU 3842  CG  PRO A 541     4752   5207   4764   -164   -582    579       C  
ATOM   3843  CD  PRO A 541     -18.088 -54.364  18.964  1.00 37.39           C  
ANISOU 3843  CD  PRO A 541     4567   5053   4584   -211   -661    633       C  
ATOM   3844  N   THR A 542     -20.915 -56.768  21.688  1.00 41.55           N  
ANISOU 3844  N   THR A 542     5287   5594   4908   -373   -702    716       N  
ATOM   3845  CA  THR A 542     -21.014 -58.130  22.230  1.00 43.54           C  
ANISOU 3845  CA  THR A 542     5547   5809   5185   -394   -754    793       C  
ATOM   3846  C   THR A 542     -22.310 -58.812  21.784  1.00 38.88           C  
ANISOU 3846  C   THR A 542     4977   5207   4589   -371   -677    745       C  
ATOM   3847  O   THR A 542     -23.338 -58.151  21.616  1.00 37.30           O  
ANISOU 3847  O   THR A 542     4811   5043   4318   -378   -598    666       O  
ATOM   3848  CB  THR A 542     -20.991 -58.120  23.759  1.00 45.57           C  
ANISOU 3848  CB  THR A 542     5882   6097   5337   -505   -828    859       C  
ATOM   3849  OG1 THR A 542     -21.966 -57.160  24.185  1.00 45.76           O  
ANISOU 3849  OG1 THR A 542     5980   6176   5231   -557   -759    786       O  
ATOM   3850  CG2 THR A 542     -19.588 -57.750  24.296  1.00 47.17           C  
ANISOU 3850  CG2 THR A 542     6059   6301   5561   -537   -935    934       C  
ATOM   3851  N   LEU A 543     -22.241 -60.141  21.629  1.00 36.11           N  
ANISOU 3851  N   LEU A 543     4601   4801   4318   -347   -705    796       N  
ATOM   3852  CA  LEU A 543     -23.386 -60.952  21.192  1.00 35.54           C  
ANISOU 3852  CA  LEU A 543     4542   4708   4252   -328   -643    760       C  
ATOM   3853  C   LEU A 543     -24.555 -60.786  22.151  1.00 33.39           C  
ANISOU 3853  C   LEU A 543     4352   4482   3852   -411   -615    746       C  
ATOM   3854  O   LEU A 543     -24.357 -60.821  23.358  1.00 37.06           O  
ANISOU 3854  O   LEU A 543     4869   4965   4246   -492   -674    808       O  
ATOM   3855  CB  LEU A 543     -23.025 -62.442  21.170  1.00 36.32           C  
ANISOU 3855  CB  LEU A 543     4615   4737   4449   -308   -693    835       C  
ATOM   3856  CG  LEU A 543     -22.278 -63.046  19.995  1.00 36.65           C  
ANISOU 3856  CG  LEU A 543     4576   4712   4638   -214   -685    831       C  
ATOM   3857  CD1 LEU A 543     -22.091 -64.534  20.195  1.00 38.00           C  
ANISOU 3857  CD1 LEU A 543     4735   4810   4894   -208   -733    907       C  
ATOM   3858  CD2 LEU A 543     -23.112 -62.779  18.797  1.00 33.09           C  
ANISOU 3858  CD2 LEU A 543     4117   4268   4188   -163   -583    728       C  
ATOM   3859  N   PRO A 544     -25.784 -60.657  21.665  1.00 33.31           N  
ANISOU 3859  N   PRO A 544     4355   4489   3813   -398   -526    668       N  
ATOM   3860  CA  PRO A 544     -26.929 -60.684  22.592  1.00 33.62           C  
ANISOU 3860  CA  PRO A 544     4465   4564   3747   -477   -492    658       C  
ATOM   3861  C   PRO A 544     -27.053 -62.051  23.231  1.00 34.51           C  
ANISOU 3861  C   PRO A 544     4604   4639   3869   -520   -541    738       C  
ATOM   3862  O   PRO A 544     -26.830 -63.078  22.574  1.00 32.46           O  
ANISOU 3862  O   PRO A 544     4302   4322   3710   -468   -559    764       O  
ATOM   3863  CB  PRO A 544     -28.148 -60.406  21.706  1.00 33.08           C  
ANISOU 3863  CB  PRO A 544     4378   4507   3682   -436   -393    563       C  
ATOM   3864  CG  PRO A 544     -27.641 -60.148  20.346  1.00 33.69           C  
ANISOU 3864  CG  PRO A 544     4390   4562   3850   -343   -378    523       C  
ATOM   3865  CD  PRO A 544     -26.186 -60.479  20.261  1.00 33.36           C  
ANISOU 3865  CD  PRO A 544     4313   4483   3880   -315   -455    588       C  
ATOM   3866  N   GLU A 545     -27.441 -62.061  24.512  1.00 31.66           N  
ANISOU 3866  N   GLU A 545     4319   4310   3402   -619   -556    773       N  
ATOM   3867  CA  GLU A 545     -27.472 -63.307  25.252  1.00 33.90           C  
ANISOU 3867  CA  GLU A 545     4638   4559   3683   -673   -614    862       C  
ATOM   3868  C   GLU A 545     -28.713 -64.089  24.908  1.00 32.69           C  
ANISOU 3868  C   GLU A 545     4489   4391   3543   -669   -544    828       C  
ATOM   3869  O   GLU A 545     -29.817 -63.552  24.828  1.00 32.43           O  
ANISOU 3869  O   GLU A 545     4471   4398   3454   -684   -454    749       O  
ATOM   3870  CB  GLU A 545     -27.433 -63.076  26.777  1.00 38.68           C  
ANISOU 3870  CB  GLU A 545     5335   5204   4158   -793   -658    918       C  
ATOM   3871  CG  GLU A 545     -26.130 -62.422  27.215  1.00 45.80           C  
ANISOU 3871  CG  GLU A 545     6237   6117   5048   -810   -747    968       C  
ATOM   3872  CD  GLU A 545     -25.933 -62.359  28.776  1.00 51.65           C  
ANISOU 3872  CD  GLU A 545     7078   6889   5657   -943   -816   1044       C  
ATOM   3873  OE1 GLU A 545     -26.678 -63.030  29.574  1.00 53.88           O  
ANISOU 3873  OE1 GLU A 545     7431   7175   5865  -1024   -808   1076       O  
ATOM   3874  OE2 GLU A 545     -25.019 -61.599  29.182  1.00 53.41           O  
ANISOU 3874  OE2 GLU A 545     7311   7135   5847   -971   -879   1068       O  
ATOM   3875  N   GLU A 546     -28.520 -65.381  24.761  1.00 33.65           N  
ANISOU 3875  N   GLU A 546     4596   4449   3742   -654   -590    891       N  
ATOM   3876  CA  GLU A 546     -29.581 -66.277  24.403  1.00 36.45           C  
ANISOU 3876  CA  GLU A 546     4951   4777   4120   -652   -538    869       C  
ATOM   3877  C   GLU A 546     -30.352 -66.642  25.657  1.00 39.98           C  
ANISOU 3877  C   GLU A 546     5481   5250   4461   -764   -533    909       C  
ATOM   3878  O   GLU A 546     -29.765 -66.863  26.716  1.00 42.55           O  
ANISOU 3878  O   GLU A 546     5859   5574   4734   -834   -610    996       O  
ATOM   3879  CB  GLU A 546     -28.964 -67.503  23.736  1.00 39.87           C  
ANISOU 3879  CB  GLU A 546     5339   5125   4685   -590   -588    920       C  
ATOM   3880  CG  GLU A 546     -29.929 -68.477  23.204  1.00 43.47           C  
ANISOU 3880  CG  GLU A 546     5791   5543   5182   -580   -540    895       C  
ATOM   3881  CD  GLU A 546     -29.215 -69.688  22.635  1.00 50.37           C  
ANISOU 3881  CD  GLU A 546     6627   6324   6188   -524   -591    948       C  
ATOM   3882  OE1 GLU A 546     -28.016 -69.906  22.950  1.00 51.76           O  
ANISOU 3882  OE1 GLU A 546     6787   6463   6416   -509   -675   1026       O  
ATOM   3883  OE2 GLU A 546     -29.850 -70.422  21.859  1.00 52.82           O  
ANISOU 3883  OE2 GLU A 546     6921   6593   6554   -494   -547    911       O  
ATOM   3884  N   VAL A 547     -31.672 -66.666  25.543  1.00 41.58           N  
ANISOU 3884  N   VAL A 547     5695   5476   4627   -787   -443    845       N  
ATOM   3885  CA  VAL A 547     -32.587 -66.721  26.680  1.00 43.98           C  
ANISOU 3885  CA  VAL A 547     6075   5818   4815   -896   -404    854       C  
ATOM   3886  C   VAL A 547     -33.235 -68.102  26.768  1.00 46.44           C  
ANISOU 3886  C   VAL A 547     6403   6084   5158   -928   -405    898       C  
ATOM   3887  O   VAL A 547     -33.674 -68.534  27.831  1.00 50.75           O  
ANISOU 3887  O   VAL A 547     7021   6642   5621  -1028   -407    946       O  
ATOM   3888  CB  VAL A 547     -33.678 -65.635  26.525  1.00 45.91           C  
ANISOU 3888  CB  VAL A 547     6313   6127   5005   -901   -288    744       C  
ATOM   3889  CG1 VAL A 547     -34.665 -65.695  27.629  1.00 44.29           C  
ANISOU 3889  CG1 VAL A 547     6179   5958   4690  -1011   -229    743       C  
ATOM   3890  CG2 VAL A 547     -33.073 -64.217  26.356  1.00 48.63           C  
ANISOU 3890  CG2 VAL A 547     6641   6510   5325   -865   -281    694       C  
ATOM   3891  N   SER A 548     -33.401 -68.748  25.637  1.00 44.57           N  
ANISOU 3891  N   SER A 548     6104   5798   5032   -850   -394    873       N  
ATOM   3892  CA  SER A 548     -34.056 -70.040  25.517  1.00 43.82           C  
ANISOU 3892  CA  SER A 548     6016   5652   4981   -869   -388    900       C  
ATOM   3893  C   SER A 548     -33.084 -71.042  24.918  1.00 43.48           C  
ANISOU 3893  C   SER A 548     5940   5522   5059   -804   -468    961       C  
ATOM   3894  O   SER A 548     -32.391 -70.724  23.944  1.00 48.42           O  
ANISOU 3894  O   SER A 548     6505   6127   5765   -712   -477    928       O  
ATOM   3895  CB  SER A 548     -35.247 -69.945  24.585  1.00 48.27           C  
ANISOU 3895  CB  SER A 548     6534   6230   5577   -835   -294    803       C  
ATOM   3896  OG  SER A 548     -36.444 -69.618  25.253  1.00 52.81           O  
ANISOU 3896  OG  SER A 548     7141   6860   6063   -914   -216    767       O  
ATOM   3897  N   ARG A 549     -33.099 -72.242  25.391  1.00 35.76           N  
ANISOU 3897  N   ARG A 549     4997   4488   4102   -848   -514   1042       N  
ATOM   3898  CA  ARG A 549     -32.293 -73.245  24.714  1.00 31.49           C  
ANISOU 3898  CA  ARG A 549     4418   3852   3695   -778   -574   1088       C  
ATOM   3899  C   ARG A 549     -33.205 -74.273  24.060  1.00 31.61           C  
ANISOU 3899  C   ARG A 549     4424   3817   3769   -771   -528   1059       C  
ATOM   3900  O   ARG A 549     -34.274 -74.589  24.618  1.00 27.54           O  
ANISOU 3900  O   ARG A 549     3953   3324   3187   -851   -488   1059       O  
ATOM   3901  CB  ARG A 549     -31.346 -73.982  25.687  1.00 30.63           C  
ANISOU 3901  CB  ARG A 549     4348   3692   3598   -820   -686   1222       C  
ATOM   3902  CG  ARG A 549     -30.385 -73.076  26.526  1.00 35.32           C  
ANISOU 3902  CG  ARG A 549     4962   4333   4125   -848   -754   1272       C  
ATOM   3903  CD  ARG A 549     -29.711 -72.047  25.635  1.00 42.34           C  
ANISOU 3903  CD  ARG A 549     5780   5246   5061   -755   -735   1201       C  
ATOM   3904  NE  ARG A 549     -29.062 -70.864  26.286  1.00 47.00           N  
ANISOU 3904  NE  ARG A 549     6387   5903   5569   -784   -769   1211       N  
ATOM   3905  CZ  ARG A 549     -27.848 -70.932  26.782  1.00 50.08           C  
ANISOU 3905  CZ  ARG A 549     6772   6268   5989   -787   -875   1303       C  
ATOM   3906  NH1 ARG A 549     -27.248 -69.881  27.331  1.00 50.86           N  
ANISOU 3906  NH1 ARG A 549     6885   6423   6015   -817   -910   1310       N  
ATOM   3907  NH2 ARG A 549     -27.249 -72.114  26.741  1.00 53.84           N  
ANISOU 3907  NH2 ARG A 549     7228   6655   6574   -763   -951   1392       N  
ATOM   3908  N   PRO A 550     -32.749 -74.920  22.979  1.00 30.69           N  
ANISOU 3908  N   PRO A 550     4258   3623   3779   -686   -538   1044       N  
ATOM   3909  CA  PRO A 550     -33.623 -75.858  22.250  1.00 30.56           C  
ANISOU 3909  CA  PRO A 550     4235   3557   3818   -680   -492   1005       C  
ATOM   3910  C   PRO A 550     -33.698 -77.201  22.936  1.00 29.93           C  
ANISOU 3910  C   PRO A 550     4204   3404   3764   -738   -540   1100       C  
ATOM   3911  O   PRO A 550     -32.759 -77.653  23.593  1.00 30.34           O  
ANISOU 3911  O   PRO A 550     4274   3408   3845   -745   -625   1200       O  
ATOM   3912  CB  PRO A 550     -32.942 -76.014  20.879  1.00 29.80           C  
ANISOU 3912  CB  PRO A 550     4079   3401   3843   -571   -485    956       C  
ATOM   3913  CG  PRO A 550     -31.515 -75.679  21.113  1.00 31.83           C  
ANISOU 3913  CG  PRO A 550     4313   3640   4140   -526   -553   1012       C  
ATOM   3914  CD  PRO A 550     -31.452 -74.708  22.280  1.00 32.54           C  
ANISOU 3914  CD  PRO A 550     4437   3818   4110   -590   -578   1047       C  
ATOM   3915  N   ASN A 551     -34.841 -77.831  22.780  1.00 28.19           N  
ANISOU 3915  N   ASN A 551     4002   3173   3534   -781   -490   1071       N  
ATOM   3916  CA  ASN A 551     -34.923 -79.264  23.000  1.00 32.50           C  
ANISOU 3916  CA  ASN A 551     4583   3626   4141   -814   -527   1142       C  
ATOM   3917  C   ASN A 551     -34.507 -80.019  21.720  1.00 30.81           C  
ANISOU 3917  C   ASN A 551     4325   3314   4068   -723   -524   1106       C  
ATOM   3918  O   ASN A 551     -34.609 -79.499  20.617  1.00 28.15           O  
ANISOU 3918  O   ASN A 551     3942   2996   3759   -658   -472   1010       O  
ATOM   3919  CB  ASN A 551     -36.362 -79.616  23.379  1.00 34.37           C  
ANISOU 3919  CB  ASN A 551     4858   3894   4308   -907   -469   1124       C  
ATOM   3920  CG  ASN A 551     -36.505 -81.030  23.781  1.00 41.83           C  
ANISOU 3920  CG  ASN A 551     5848   4748   5296   -958   -507   1205       C  
ATOM   3921  OD1 ASN A 551     -35.747 -81.542  24.618  1.00 46.33           O  
ANISOU 3921  OD1 ASN A 551     6457   5271   5874   -984   -588   1315       O  
ATOM   3922  ND2 ASN A 551     -37.478 -81.712  23.173  1.00 45.16           N  
ANISOU 3922  ND2 ASN A 551     6267   5141   5752   -974   -456   1156       N  
ATOM   3923  N   TYR A 552     -34.089 -81.269  21.872  1.00 30.83           N  
ANISOU 3923  N   TYR A 552     4348   3209   4158   -724   -576   1183       N  
ATOM   3924  CA  TYR A 552     -33.673 -82.101  20.745  1.00 30.47           C  
ANISOU 3924  CA  TYR A 552     4270   3056   4251   -645   -568   1152       C  
ATOM   3925  C   TYR A 552     -34.468 -83.389  20.829  1.00 32.63           C  
ANISOU 3925  C   TYR A 552     4588   3256   4554   -702   -561   1177       C  
ATOM   3926  O   TYR A 552     -33.963 -84.394  21.332  1.00 33.84           O  
ANISOU 3926  O   TYR A 552     4768   3315   4776   -714   -623   1273       O  
ATOM   3927  CB  TYR A 552     -32.167 -82.399  20.768  1.00 30.42           C  
ANISOU 3927  CB  TYR A 552     4235   2968   4357   -573   -639   1223       C  
ATOM   3928  CG  TYR A 552     -31.324 -81.180  20.629  1.00 31.24           C  
ANISOU 3928  CG  TYR A 552     4291   3137   4443   -516   -647   1199       C  
ATOM   3929  CD1 TYR A 552     -30.810 -80.539  21.766  1.00 31.64           C  
ANISOU 3929  CD1 TYR A 552     4356   3246   4421   -556   -713   1278       C  
ATOM   3930  CD2 TYR A 552     -31.045 -80.642  19.386  1.00 28.96           C  
ANISOU 3930  CD2 TYR A 552     3948   2854   4201   -432   -590   1098       C  
ATOM   3931  CE1 TYR A 552     -30.036 -79.423  21.650  1.00 32.38           C  
ANISOU 3931  CE1 TYR A 552     4407   3396   4499   -510   -722   1256       C  
ATOM   3932  CE2 TYR A 552     -30.245 -79.488  19.260  1.00 29.04           C  
ANISOU 3932  CE2 TYR A 552     3914   2924   4195   -383   -597   1077       C  
ATOM   3933  CZ  TYR A 552     -29.757 -78.907  20.404  1.00 32.70           C  
ANISOU 3933  CZ  TYR A 552     4389   3440   4594   -422   -663   1157       C  
ATOM   3934  OH  TYR A 552     -28.977 -77.786  20.326  1.00 34.06           O  
ANISOU 3934  OH  TYR A 552     4522   3670   4750   -381   -673   1140       O  
ATOM   3935  N   PRO A 553     -35.725 -83.385  20.384  1.00 31.19           N  
ANISOU 3935  N   PRO A 553     4414   3114   4325   -743   -491   1098       N  
ATOM   3936  CA  PRO A 553     -36.583 -84.553  20.593  1.00 31.09           C  
ANISOU 3936  CA  PRO A 553     4445   3041   4325   -815   -484   1126       C  
ATOM   3937  C   PRO A 553     -36.185 -85.744  19.738  1.00 34.65           C  
ANISOU 3937  C   PRO A 553     4895   3354   4914   -763   -491   1120       C  
ATOM   3938  O   PRO A 553     -35.916 -85.608  18.550  1.00 34.99           O  
ANISOU 3938  O   PRO A 553     4901   3373   5021   -687   -455   1035       O  
ATOM   3939  CB  PRO A 553     -37.969 -84.049  20.183  1.00 30.47           C  
ANISOU 3939  CB  PRO A 553     4358   3051   4170   -861   -405   1030       C  
ATOM   3940  CG  PRO A 553     -37.678 -83.020  19.148  1.00 29.43           C  
ANISOU 3940  CG  PRO A 553     4169   2969   4045   -776   -371    933       C  
ATOM   3941  CD  PRO A 553     -36.451 -82.282  19.732  1.00 32.20           C  
ANISOU 3941  CD  PRO A 553     4507   3345   4384   -732   -421    988       C  
ATOM   3942  N   GLY A 554     -36.224 -86.927  20.331  1.00 35.60           N  
ANISOU 3942  N   GLY A 554     5062   3384   5079   -812   -532   1207       N  
ATOM   3943  CA  GLY A 554     -36.169 -88.164  19.577  1.00 36.50           C  
ANISOU 3943  CA  GLY A 554     5187   3365   5316   -785   -525   1194       C  
ATOM   3944  C   GLY A 554     -37.561 -88.628  19.173  1.00 38.65           C  
ANISOU 3944  C   GLY A 554     5486   3647   5553   -856   -467   1130       C  
ATOM   3945  O   GLY A 554     -38.556 -87.907  19.293  1.00 37.94           O  
ANISOU 3945  O   GLY A 554     5389   3669   5357   -911   -425   1082       O  
ATOM   3946  N   ILE A 555     -37.622 -89.855  18.654  1.00 37.43           N  
ANISOU 3946  N   ILE A 555     5356   3367   5499   -854   -464   1127       N  
ATOM   3947  CA  ILE A 555     -38.896 -90.442  18.283  1.00 39.62           C  
ANISOU 3947  CA  ILE A 555     5661   3638   5756   -928   -418   1076       C  
ATOM   3948  C   ILE A 555     -39.655 -90.771  19.553  1.00 43.86           C  
ANISOU 3948  C   ILE A 555     6245   4206   6215  -1042   -440   1164       C  
ATOM   3949  O   ILE A 555     -39.170 -91.533  20.389  1.00 44.02           O  
ANISOU 3949  O   ILE A 555     6306   4148   6271  -1067   -499   1276       O  
ATOM   3950  CB  ILE A 555     -38.692 -91.706  17.441  1.00 40.98           C  
ANISOU 3950  CB  ILE A 555     5857   3658   6057   -900   -410   1052       C  
ATOM   3951  CG1 ILE A 555     -38.110 -91.323  16.067  1.00 42.89           C  
ANISOU 3951  CG1 ILE A 555     6059   3880   6359   -799   -369    943       C  
ATOM   3952  CG2 ILE A 555     -40.001 -92.441  17.374  1.00 40.34           C  
ANISOU 3952  CG2 ILE A 555     5814   3563   5949   -999   -381   1030       C  
ATOM   3953  CD1 ILE A 555     -37.904 -92.508  15.169  1.00 47.24           C  
ANISOU 3953  CD1 ILE A 555     6638   4279   7032   -772   -347    903       C  
ATOM   3954  N   MET A 556     -40.853 -90.221  19.706  1.00 47.69           N  
ANISOU 3954  N   MET A 556     6723   4801   6597  -1116   -392   1118       N  
ATOM   3955  CA  MET A 556     -41.571 -90.426  20.957  1.00 51.65           C  
ANISOU 3955  CA  MET A 556     7268   5343   7013  -1230   -399   1198       C  
ATOM   3956  C   MET A 556     -43.006 -90.852  20.816  1.00 49.52           C  
ANISOU 3956  C   MET A 556     7008   5094   6712  -1324   -346   1155       C  
ATOM   3957  O   MET A 556     -43.601 -91.228  21.826  1.00 51.32           O  
ANISOU 3957  O   MET A 556     7279   5336   6884  -1426   -347   1225       O  
ATOM   3958  CB  MET A 556     -41.534 -89.157  21.803  1.00 58.42           C  
ANISOU 3958  CB  MET A 556     8111   6334   7753  -1247   -395   1214       C  
ATOM   3959  CG  MET A 556     -40.239 -89.023  22.530  1.00 66.30           C  
ANISOU 3959  CG  MET A 556     9126   7304   8761  -1207   -470   1310       C  
ATOM   3960  SD  MET A 556     -40.125 -87.351  23.127  1.00 72.19           S  
ANISOU 3960  SD  MET A 556     9844   8207   9377  -1205   -453   1289       S  
ATOM   3961  CE  MET A 556     -40.495 -86.395  21.636  1.00 70.49           C  
ANISOU 3961  CE  MET A 556     9547   8055   9179  -1120   -379   1131       C  
ATOM   3962  N   TYR A 557     -43.571 -90.839  19.612  1.00 45.38           N  
ANISOU 3962  N   TYR A 557     6448   4570   6223  -1300   -302   1048       N  
ATOM   3963  CA  TYR A 557     -44.976 -91.134  19.390  1.00 42.20           C  
ANISOU 3963  CA  TYR A 557     6041   4198   5795  -1388   -254   1000       C  
ATOM   3964  C   TYR A 557     -45.115 -92.150  18.274  1.00 42.24           C  
ANISOU 3964  C   TYR A 557     6061   4092   5898  -1375   -252    947       C  
ATOM   3965  O   TYR A 557     -44.196 -92.368  17.481  1.00 42.56           O  
ANISOU 3965  O   TYR A 557     6102   4051   6016  -1286   -270    919       O  
ATOM   3966  CB  TYR A 557     -45.751 -89.850  19.038  1.00 40.30           C  
ANISOU 3966  CB  TYR A 557     5732   4098   5481  -1386   -202    911       C  
ATOM   3967  CG  TYR A 557     -45.723 -88.854  20.152  1.00 40.88           C  
ANISOU 3967  CG  TYR A 557     5798   4280   5456  -1409   -191    953       C  
ATOM   3968  CD1 TYR A 557     -46.632 -88.938  21.207  1.00 43.16           C  
ANISOU 3968  CD1 TYR A 557     6106   4621   5672  -1521   -160    997       C  
ATOM   3969  CD2 TYR A 557     -44.784 -87.843  20.178  1.00 40.16           C  
ANISOU 3969  CD2 TYR A 557     5682   4235   5341  -1326   -208    947       C  
ATOM   3970  CE1 TYR A 557     -46.592 -87.995  22.265  1.00 43.71           C  
ANISOU 3970  CE1 TYR A 557     6177   4789   5642  -1548   -142   1030       C  
ATOM   3971  CE2 TYR A 557     -44.726 -86.928  21.207  1.00 41.01           C  
ANISOU 3971  CE2 TYR A 557     5791   4438   5354  -1351   -198    982       C  
ATOM   3972  CZ  TYR A 557     -45.632 -87.022  22.255  1.00 44.29           C  
ANISOU 3972  CZ  TYR A 557     6232   4902   5693  -1464   -164   1022       C  
ATOM   3973  OH  TYR A 557     -45.571 -86.106  23.276  1.00 47.70           O  
ANISOU 3973  OH  TYR A 557     6674   5426   6026  -1495   -146   1050       O  
ATOM   3974  N   LEU A 558     -46.273 -92.796  18.248  1.00 44.77           N  
ANISOU 3974  N   LEU A 558     6394   4403   6212  -1471   -227    934       N  
ATOM   3975  CA  LEU A 558     -46.676 -93.701  17.186  1.00 45.98           C  
ANISOU 3975  CA  LEU A 558     6563   4467   6441  -1483   -218    873       C  
ATOM   3976  C   LEU A 558     -47.500 -92.929  16.174  1.00 45.88           C  
ANISOU 3976  C   LEU A 558     6490   4545   6398  -1480   -180    758       C  
ATOM   3977  O   LEU A 558     -48.178 -91.963  16.524  1.00 43.45           O  
ANISOU 3977  O   LEU A 558     6131   4365   6015  -1507   -154    742       O  
ATOM   3978  CB  LEU A 558     -47.516 -94.848  17.754  1.00 47.22           C  
ANISOU 3978  CB  LEU A 558     6768   4564   6609  -1600   -218    928       C  
ATOM   3979  CG  LEU A 558     -46.813 -95.879  18.635  1.00 48.59           C  
ANISOU 3979  CG  LEU A 558     7014   4620   6829  -1617   -263   1045       C  
ATOM   3980  CD1 LEU A 558     -47.756 -97.023  18.994  1.00 49.43           C  
ANISOU 3980  CD1 LEU A 558     7168   4664   6950  -1738   -257   1085       C  
ATOM   3981  CD2 LEU A 558     -45.571 -96.379  17.902  1.00 48.99           C  
ANISOU 3981  CD2 LEU A 558     7085   4542   6989  -1510   -295   1036       C  
ATOM   3982  N   GLN A 559     -47.445 -93.362  14.919  1.00 48.42           N  
ANISOU 3982  N   GLN A 559     6819   4797   6779  -1449   -179    680       N  
ATOM   3983  CA  GLN A 559     -48.396 -92.861  13.935  1.00 52.98           C  
ANISOU 3983  CA  GLN A 559     7352   5448   7332  -1471   -155    581       C  
ATOM   3984  C   GLN A 559     -49.834 -92.905  14.463  1.00 51.13           C  
ANISOU 3984  C   GLN A 559     7087   5285   7054  -1588   -134    593       C  
ATOM   3985  O   GLN A 559     -50.567 -91.910  14.390  1.00 49.02           O  
ANISOU 3985  O   GLN A 559     6752   5139   6735  -1600   -112    553       O  
ATOM   3986  CB  GLN A 559     -48.244 -93.667  12.650  1.00 60.80           C  
ANISOU 3986  CB  GLN A 559     8381   6330   8391  -1456   -159    509       C  
ATOM   3987  CG  GLN A 559     -47.012 -93.242  11.852  1.00 67.16           C  
ANISOU 3987  CG  GLN A 559     9190   7102   9226  -1337   -160    462       C  
ATOM   3988  CD  GLN A 559     -47.294 -92.009  11.037  1.00 72.30           C  
ANISOU 3988  CD  GLN A 559     9783   7866   9820  -1302   -148    380       C  
ATOM   3989  OE1 GLN A 559     -48.402 -91.482  11.093  1.00 74.74           O  
ANISOU 3989  OE1 GLN A 559    10045   8275  10076  -1363   -142    361       O  
ATOM   3990  NE2 GLN A 559     -46.313 -91.548  10.253  1.00 74.97           N  
ANISOU 3990  NE2 GLN A 559    10124   8188  10174  -1207   -143    331       N  
ATOM   3991  N   SER A 560     -50.238 -94.025  15.056  1.00 50.73           N  
ANISOU 3991  N   SER A 560     7084   5160   7029  -1674   -138    652       N  
ATOM   3992  CA  SER A 560     -51.604 -94.172  15.564  1.00 48.38           C  
ANISOU 3992  CA  SER A 560     6761   4923   6699  -1792   -112    665       C  
ATOM   3993  C   SER A 560     -51.941 -93.184  16.677  1.00 47.48           C  
ANISOU 3993  C   SER A 560     6599   4935   6505  -1814    -80    706       C  
ATOM   3994  O   SER A 560     -53.111 -93.097  17.075  1.00 47.29           O  
ANISOU 3994  O   SER A 560     6535   4978   6453  -1906    -45    706       O  
ATOM   3995  CB  SER A 560     -51.824 -95.604  16.081  1.00 50.27           C  
ANISOU 3995  CB  SER A 560     7071   5047   6980  -1880   -122    732       C  
ATOM   3996  OG  SER A 560     -51.073 -95.824  17.275  1.00 52.10           O  
ANISOU 3996  OG  SER A 560     7351   5248   7198  -1874   -137    837       O  
ATOM   3997  N   ASP A 561     -50.968 -92.440  17.206  1.00 45.61           N  
ANISOU 3997  N   ASP A 561     6365   4732   6232  -1738    -89    740       N  
ATOM   3998  CA  ASP A 561     -51.323 -91.436  18.200  1.00 44.53           C  
ANISOU 3998  CA  ASP A 561     6189   4718   6014  -1763    -52    766       C  
ATOM   3999  C   ASP A 561     -51.916 -90.169  17.593  1.00 43.15           C  
ANISOU 3999  C   ASP A 561     5922   4662   5812  -1729    -21    680       C  
ATOM   4000  O   ASP A 561     -52.376 -89.309  18.353  1.00 44.25           O  
ANISOU 4000  O   ASP A 561     6020   4904   5891  -1755     22    688       O  
ATOM   4001  CB  ASP A 561     -50.104 -91.025  19.022  1.00 46.84           C  
ANISOU 4001  CB  ASP A 561     6516   5009   6270  -1702    -76    834       C  
ATOM   4002  CG  ASP A 561     -49.508 -92.180  19.796  1.00 52.36           C  
ANISOU 4002  CG  ASP A 561     7302   5598   6993  -1738   -115    937       C  
ATOM   4003  OD1 ASP A 561     -50.282 -92.995  20.357  1.00 52.85           O  
ANISOU 4003  OD1 ASP A 561     7397   5634   7051  -1845   -100    981       O  
ATOM   4004  OD2 ASP A 561     -48.257 -92.260  19.849  1.00 53.96           O  
ANISOU 4004  OD2 ASP A 561     7539   5740   7224  -1660   -162    977       O  
ATOM   4005  N   PHE A 562     -51.890 -90.009  16.269  1.00 39.85           N  
ANISOU 4005  N   PHE A 562     5475   4231   5436  -1674    -39    599       N  
ATOM   4006  CA  PHE A 562     -52.219 -88.728  15.643  1.00 38.46           C  
ANISOU 4006  CA  PHE A 562     5217   4158   5236  -1624    -24    526       C  
ATOM   4007  C   PHE A 562     -53.599 -88.812  14.999  1.00 41.73           C  
ANISOU 4007  C   PHE A 562     5572   4610   5675  -1695    -11    471       C  
ATOM   4008  O   PHE A 562     -53.916 -89.800  14.323  1.00 42.90           O  
ANISOU 4008  O   PHE A 562     5749   4681   5871  -1737    -35    452       O  
ATOM   4009  CB  PHE A 562     -51.172 -88.331  14.603  1.00 35.89           C  
ANISOU 4009  CB  PHE A 562     4902   3804   4931  -1512    -57    476       C  
ATOM   4010  CG  PHE A 562     -49.835 -87.998  15.197  1.00 34.35           C  
ANISOU 4010  CG  PHE A 562     4743   3592   4716  -1435    -70    525       C  
ATOM   4011  CD1 PHE A 562     -48.931 -89.017  15.496  1.00 34.35           C  
ANISOU 4011  CD1 PHE A 562     4817   3479   4755  -1423   -100    584       C  
ATOM   4012  CD2 PHE A 562     -49.507 -86.695  15.524  1.00 32.62           C  
ANISOU 4012  CD2 PHE A 562     4481   3468   4444  -1379    -55    518       C  
ATOM   4013  CE1 PHE A 562     -47.688 -88.719  16.062  1.00 33.93           C  
ANISOU 4013  CE1 PHE A 562     4790   3410   4693  -1354   -121    637       C  
ATOM   4014  CE2 PHE A 562     -48.263 -86.378  16.071  1.00 33.67           C  
ANISOU 4014  CE2 PHE A 562     4646   3588   4560  -1314    -74    564       C  
ATOM   4015  CZ  PHE A 562     -47.357 -87.385  16.361  1.00 34.37           C  
ANISOU 4015  CZ  PHE A 562     4802   3567   4690  -1302   -109    627       C  
ATOM   4016  N   ASP A 563     -54.427 -87.793  15.253  1.00 42.15           N  
ANISOU 4016  N   ASP A 563     5539   4775   5700  -1710     27    448       N  
ATOM   4017  CA  ASP A 563     -55.764 -87.657  14.654  1.00 45.56           C  
ANISOU 4017  CA  ASP A 563     5890   5257   6163  -1769     36    397       C  
ATOM   4018  C   ASP A 563     -55.875 -86.254  14.070  1.00 43.22           C  
ANISOU 4018  C   ASP A 563     5513   5054   5856  -1697     37    340       C  
ATOM   4019  O   ASP A 563     -56.679 -85.438  14.514  1.00 45.01           O  
ANISOU 4019  O   ASP A 563     5657   5371   6075  -1718     80    332       O  
ATOM   4020  CB  ASP A 563     -56.873 -87.908  15.687  1.00 52.21           C  
ANISOU 4020  CB  ASP A 563     6696   6140   7000  -1878     92    436       C  
ATOM   4021  CG  ASP A 563     -58.260 -88.019  15.062  1.00 58.16           C  
ANISOU 4021  CG  ASP A 563     7366   6927   7805  -1951     93    393       C  
ATOM   4022  OD1 ASP A 563     -58.355 -88.271  13.846  1.00 60.35           O  
ANISOU 4022  OD1 ASP A 563     7641   7170   8121  -1938     38    344       O  
ATOM   4023  OD2 ASP A 563     -59.268 -87.890  15.803  1.00 61.04           O  
ANISOU 4023  OD2 ASP A 563     7669   7349   8173  -2028    150    409       O  
ATOM   4024  N   LEU A 564     -55.001 -85.957  13.111  1.00 37.96           N  
ANISOU 4024  N   LEU A 564     4872   4361   5190  -1608     -7    302       N  
ATOM   4025  CA  LEU A 564     -54.869 -84.620  12.551  1.00 38.82           C  
ANISOU 4025  CA  LEU A 564     4920   4546   5283  -1529    -12    255       C  
ATOM   4026  C   LEU A 564     -55.731 -84.435  11.324  1.00 37.73           C  
ANISOU 4026  C   LEU A 564     4725   4430   5181  -1547    -49    195       C  
ATOM   4027  O   LEU A 564     -55.803 -83.335  10.802  1.00 37.86           O  
ANISOU 4027  O   LEU A 564     4683   4511   5191  -1492    -59    158       O  
ATOM   4028  CB  LEU A 564     -53.404 -84.336  12.184  1.00 37.63           C  
ANISOU 4028  CB  LEU A 564     4830   4356   5110  -1426    -37    248       C  
ATOM   4029  CG  LEU A 564     -52.359 -84.535  13.307  1.00 38.25           C  
ANISOU 4029  CG  LEU A 564     4971   4403   5158  -1400    -19    314       C  
ATOM   4030  CD1 LEU A 564     -50.932 -84.228  12.803  1.00 37.04           C  
ANISOU 4030  CD1 LEU A 564     4862   4213   5000  -1296    -47    302       C  
ATOM   4031  CD2 LEU A 564     -52.636 -83.695  14.563  1.00 37.46           C  
ANISOU 4031  CD2 LEU A 564     4832   4391   5012  -1416     32    349       C  
ATOM   4032  N   GLY A 565     -56.390 -85.474  10.857  1.00 32.66           N  
ANISOU 4032  N   GLY A 565     4098   3736   4576  -1626    -74    187       N  
ATOM   4033  CA  GLY A 565     -57.138 -85.352   9.621  1.00 37.77           C  
ANISOU 4033  CA  GLY A 565     4701   4399   5252  -1649   -123    132       C  
ATOM   4034  C   GLY A 565     -56.256 -85.298   8.394  1.00 40.49           C  
ANISOU 4034  C   GLY A 565     5108   4698   5580  -1584   -172     85       C  
ATOM   4035  O   GLY A 565     -56.699 -84.855   7.335  1.00 40.82           O  
ANISOU 4035  O   GLY A 565     5114   4768   5626  -1584   -218     39       O  
ATOM   4036  N   CYS A 566     -55.015 -85.740   8.504  1.00 40.96           N  
ANISOU 4036  N   CYS A 566     5257   4683   5622  -1530   -165     96       N  
ATOM   4037  CA  CYS A 566     -54.088 -85.667   7.388  1.00 44.69           C  
ANISOU 4037  CA  CYS A 566     5790   5110   6081  -1465   -195     48       C  
ATOM   4038  C   CYS A 566     -54.062 -86.998   6.627  1.00 42.96           C  
ANISOU 4038  C   CYS A 566     5654   4782   5887  -1520   -220     20       C  
ATOM   4039  O   CYS A 566     -54.404 -88.048   7.171  1.00 42.15           O  
ANISOU 4039  O   CYS A 566     5580   4623   5814  -1589   -209     53       O  
ATOM   4040  CB  CYS A 566     -52.705 -85.265   7.905  1.00 47.11           C  
ANISOU 4040  CB  CYS A 566     6135   5401   6364  -1367   -169     72       C  
ATOM   4041  SG  CYS A 566     -52.724 -83.512   8.617  1.00 51.00           S  
ANISOU 4041  SG  CYS A 566     6533   6025   6818  -1301   -142     88       S  
ATOM   4042  N   THR A 567     -53.714 -86.941   5.331  1.00 40.52           N  
ANISOU 4042  N   THR A 567     5387   4444   5564  -1497   -252    -43       N  
ATOM   4043  CA  THR A 567     -53.531 -88.170   4.565  1.00 41.11           C  
ANISOU 4043  CA  THR A 567     5555   4406   5658  -1541   -266    -79       C  
ATOM   4044  C   THR A 567     -52.239 -88.080   3.774  1.00 38.31           C  
ANISOU 4044  C   THR A 567     5276   3994   5288  -1458   -256   -124       C  
ATOM   4045  O   THR A 567     -51.757 -86.982   3.462  1.00 34.64           O  
ANISOU 4045  O   THR A 567     4784   3591   4788  -1385   -257   -141       O  
ATOM   4046  CB  THR A 567     -54.694 -88.465   3.592  1.00 45.99           C  
ANISOU 4046  CB  THR A 567     6162   5034   6276  -1639   -317   -124       C  
ATOM   4047  OG1 THR A 567     -54.837 -87.376   2.685  1.00 47.63           O  
ANISOU 4047  OG1 THR A 567     6333   5318   6446  -1609   -354   -165       O  
ATOM   4048  CG2 THR A 567     -55.997 -88.641   4.334  1.00 48.55           C  
ANISOU 4048  CG2 THR A 567     6407   5409   6630  -1727   -322    -81       C  
ATOM   4049  N   CYS A 568     -51.668 -89.249   3.475  1.00 37.79           N  
ANISOU 4049  N   CYS A 568     5302   3804   5251  -1470   -241   -142       N  
ATOM   4050  CA  CYS A 568     -50.496 -89.333   2.614  1.00 42.08           C  
ANISOU 4050  CA  CYS A 568     5921   4277   5791  -1403   -221   -196       C  
ATOM   4051  C   CYS A 568     -50.485 -90.691   1.950  1.00 47.42           C  
ANISOU 4051  C   CYS A 568     6694   4825   6500  -1463   -216   -240       C  
ATOM   4052  O   CYS A 568     -50.649 -91.724   2.613  1.00 47.72           O  
ANISOU 4052  O   CYS A 568     6757   4789   6587  -1506   -206   -202       O  
ATOM   4053  CB  CYS A 568     -49.169 -89.117   3.360  1.00 44.55           C  
ANISOU 4053  CB  CYS A 568     6239   4561   6127  -1297   -181   -154       C  
ATOM   4054  SG  CYS A 568     -47.737 -88.907   2.201  1.00 46.29           S  
ANISOU 4054  SG  CYS A 568     6528   4718   6342  -1205   -148   -228       S  
ATOM   4055  N   ASP A 569     -50.319 -90.683   0.640  1.00 51.53           N  
ANISOU 4055  N   ASP A 569     7274   5319   6988  -1472   -222   -322       N  
ATOM   4056  CA  ASP A 569     -50.363 -91.942  -0.103  1.00 55.52           C  
ANISOU 4056  CA  ASP A 569     7878   5700   7515  -1539   -214   -378       C  
ATOM   4057  C   ASP A 569     -49.083 -92.734   0.115  1.00 56.83           C  
ANISOU 4057  C   ASP A 569     8113   5735   7746  -1470   -152   -379       C  
ATOM   4058  O   ASP A 569     -48.045 -92.376  -0.439  1.00 58.06           O  
ANISOU 4058  O   ASP A 569     8300   5865   7895  -1391   -115   -421       O  
ATOM   4059  CB  ASP A 569     -50.560 -91.656  -1.570  1.00 58.74           C  
ANISOU 4059  CB  ASP A 569     8337   6121   7859  -1577   -237   -468       C  
ATOM   4060  CG  ASP A 569     -50.982 -92.863  -2.334  1.00 64.09           C  
ANISOU 4060  CG  ASP A 569     9112   6697   8544  -1677   -243   -527       C  
ATOM   4061  OD1 ASP A 569     -50.522 -93.971  -1.988  1.00 67.38           O  
ANISOU 4061  OD1 ASP A 569     9586   6990   9026  -1676   -199   -523       O  
ATOM   4062  OD2 ASP A 569     -51.784 -92.694  -3.275  1.00 64.42           O  
ANISOU 4062  OD2 ASP A 569     9170   6779   8528  -1760   -294   -575       O  
ATOM   4063  N   SER A 586     -24.637 -85.262   9.601  1.00 79.91           N  
ANISOU 4063  N   SER A 586    10120   8399  11842    277   -118    600       N  
ATOM   4064  CA  SER A 586     -24.031 -84.252   8.731  1.00 80.69           C  
ANISOU 4064  CA  SER A 586    10180   8553  11926    326    -53    518       C  
ATOM   4065  C   SER A 586     -25.050 -83.161   8.372  1.00 80.29           C  
ANISOU 4065  C   SER A 586    10173   8649  11685    270    -34    446       C  
ATOM   4066  O   SER A 586     -24.775 -82.261   7.572  1.00 79.47           O  
ANISOU 4066  O   SER A 586    10053   8602  11538    295     21    370       O  
ATOM   4067  CB  SER A 586     -23.464 -84.895   7.457  1.00 80.87           C  
ANISOU 4067  CB  SER A 586    10200   8456  12070    384     59    420       C  
ATOM   4068  OG  SER A 586     -24.468 -85.602   6.755  1.00 80.66           O  
ANISOU 4068  OG  SER A 586    10258   8390  11998    337    113    339       O  
ATOM   4069  N   THR A 587     -26.233 -83.269   8.979  1.00 80.72           N  
ANISOU 4069  N   THR A 587    10280   8758  11631    192    -81    474       N  
ATOM   4070  CA  THR A 587     -27.292 -82.286   8.766  1.00 79.80           C  
ANISOU 4070  CA  THR A 587    10198   8776  11346    137    -73    417       C  
ATOM   4071  C   THR A 587     -26.847 -80.886   9.206  1.00 80.95           C  
ANISOU 4071  C   THR A 587    10296   9039  11422    152   -105    443       C  
ATOM   4072  O   THR A 587     -26.957 -79.919   8.443  1.00 79.71           O  
ANISOU 4072  O   THR A 587    10137   8955  11192    160    -60    366       O  
ATOM   4073  CB  THR A 587     -28.557 -82.728   9.521  1.00 76.71           C  
ANISOU 4073  CB  THR A 587     9858   8415  10874     52   -120    458       C  
ATOM   4074  OG1 THR A 587     -28.951 -84.040   9.086  1.00 76.73           O  
ANISOU 4074  OG1 THR A 587     9906   8304  10944     35    -90    433       O  
ATOM   4075  CG2 THR A 587     -29.691 -81.741   9.325  1.00 73.85           C  
ANISOU 4075  CG2 THR A 587     9520   8185  10355     -2   -110    403       C  
ATOM   4076  N   GLU A 588     -26.321 -80.760  10.437  1.00 82.10           N  
ANISOU 4076  N   GLU A 588    10407   9199  11589    151   -186    554       N  
ATOM   4077  CA  GLU A 588     -25.854 -79.451  10.902  1.00 80.28           C  
ANISOU 4077  CA  GLU A 588    10136   9072  11294    160   -220    580       C  
ATOM   4078  C   GLU A 588     -24.636 -78.984  10.097  1.00 75.70           C  
ANISOU 4078  C   GLU A 588     9497   8468  10798    239   -173    539       C  
ATOM   4079  O   GLU A 588     -24.572 -77.820   9.665  1.00 73.38           O  
ANISOU 4079  O   GLU A 588     9190   8261  10429    247   -145    486       O  
ATOM   4080  CB  GLU A 588     -25.547 -79.499  12.405  1.00 83.77           C  
ANISOU 4080  CB  GLU A 588    10563   9529  11736    132   -322    710       C  
ATOM   4081  CG  GLU A 588     -26.070 -78.298  13.188  1.00 85.73           C  
ANISOU 4081  CG  GLU A 588    10825   9915  11833     77   -361    729       C  
ATOM   4082  CD  GLU A 588     -25.231 -77.950  14.432  1.00 89.14           C  
ANISOU 4082  CD  GLU A 588    11225  10369  12273     69   -453    842       C  
ATOM   4083  OE1 GLU A 588     -24.769 -76.779  14.556  1.00 90.02           O  
ANISOU 4083  OE1 GLU A 588    11307  10561  12335     80   -464    836       O  
ATOM   4084  OE2 GLU A 588     -25.044 -78.844  15.288  1.00 90.48           O  
ANISOU 4084  OE2 GLU A 588    11405  10476  12498     47   -521    940       O  
ATOM   4085  N   GLU A 589     -23.681 -79.898   9.847  1.00 71.39           N  
ANISOU 4085  N   GLU A 589     8914   7797  10414    297   -156    558       N  
ATOM   4086  CA  GLU A 589     -22.516 -79.570   9.024  1.00 65.06           C  
ANISOU 4086  CA  GLU A 589     8052   6960   9709    372    -96    513       C  
ATOM   4087  C   GLU A 589     -22.930 -78.950   7.678  1.00 59.30           C  
ANISOU 4087  C   GLU A 589     7356   6275   8899    372      3    381       C  
ATOM   4088  O   GLU A 589     -22.306 -77.996   7.203  1.00 60.00           O  
ANISOU 4088  O   GLU A 589     7409   6413   8975    404     37    344       O  
ATOM   4089  CB  GLU A 589     -21.659 -80.830   8.832  1.00 63.82           C  
ANISOU 4089  CB  GLU A 589     7859   6645   9745    430    -74    537       C  
ATOM   4090  N   ARG A 590     -24.009 -79.439   7.075  1.00 52.57           N  
ANISOU 4090  N   ARG A 590     6577   5412   7984    330     44    312       N  
ATOM   4091  CA  ARG A 590     -24.365 -79.053   5.714  1.00 47.11           C  
ANISOU 4091  CA  ARG A 590     5926   4744   7231    327    134    190       C  
ATOM   4092  C   ARG A 590     -25.380 -77.911   5.643  1.00 39.10           C  
ANISOU 4092  C   ARG A 590     4946   3867   6044    274    117    157       C  
ATOM   4093  O   ARG A 590     -25.219 -76.980   4.823  1.00 35.60           O  
ANISOU 4093  O   ARG A 590     4503   3480   5545    285    163     91       O  
ATOM   4094  CB  ARG A 590     -24.902 -80.283   4.970  1.00 50.76           C  
ANISOU 4094  CB  ARG A 590     6449   5103   7732    310    191    128       C  
ATOM   4095  CG  ARG A 590     -23.845 -81.347   4.795  1.00 55.72           C  
ANISOU 4095  CG  ARG A 590     7044   5585   8543    372    233    138       C  
ATOM   4096  CD  ARG A 590     -24.275 -82.504   3.926  1.00 60.11           C  
ANISOU 4096  CD  ARG A 590     7666   6033   9142    357    305     61       C  
ATOM   4097  NE  ARG A 590     -25.202 -83.397   4.605  1.00 63.28           N  
ANISOU 4097  NE  ARG A 590     8111   6402   9530    304    247    110       N  
ATOM   4098  CZ  ARG A 590     -26.447 -83.617   4.185  1.00 64.28           C  
ANISOU 4098  CZ  ARG A 590     8315   6557   9551    234    255     54       C  
ATOM   4099  NH1 ARG A 590     -26.876 -82.991   3.088  1.00 65.54           N  
ANISOU 4099  NH1 ARG A 590     8517   6775   9610    210    313    -49       N  
ATOM   4100  NH2 ARG A 590     -27.259 -84.452   4.842  1.00 62.26           N  
ANISOU 4100  NH2 ARG A 590     8095   6270   9291    183    204    104       N  
ATOM   4101  N   HIS A 591     -26.400 -77.928   6.510  1.00 34.59           N  
ANISOU 4101  N   HIS A 591     4401   3350   5391    215     51    205       N  
ATOM   4102  CA  HIS A 591     -27.558 -77.065   6.304  1.00 32.43           C  
ANISOU 4102  CA  HIS A 591     4163   3187   4971    162     47    162       C  
ATOM   4103  C   HIS A 591     -27.637 -75.897   7.238  1.00 32.79           C  
ANISOU 4103  C   HIS A 591     4179   3344   4936    148    -10    215       C  
ATOM   4104  O   HIS A 591     -28.318 -74.927   6.918  1.00 30.71           O  
ANISOU 4104  O   HIS A 591     3929   3171   4567    124     -2    171       O  
ATOM   4105  CB  HIS A 591     -28.851 -77.886   6.386  1.00 30.30           C  
ANISOU 4105  CB  HIS A 591     3949   2903   4660     98     35    153       C  
ATOM   4106  CG  HIS A 591     -28.925 -78.892   5.281  1.00 31.24           C  
ANISOU 4106  CG  HIS A 591     4111   2923   4835    101     98     80       C  
ATOM   4107  ND1 HIS A 591     -28.788 -78.525   3.940  1.00 29.11           N  
ANISOU 4107  ND1 HIS A 591     3865   2654   4541    115    168    -18       N  
ATOM   4108  CD2 HIS A 591     -28.998 -80.242   5.306  1.00 31.58           C  
ANISOU 4108  CD2 HIS A 591     4182   2857   4962     92    107     89       C  
ATOM   4109  CE1 HIS A 591     -28.804 -79.615   3.194  1.00 31.81           C  
ANISOU 4109  CE1 HIS A 591     4250   2892   4943    111    219    -70       C  
ATOM   4110  NE2 HIS A 591     -28.915 -80.671   3.995  1.00 35.08           N  
ANISOU 4110  NE2 HIS A 591     4666   3235   5429    101    184     -8       N  
ATOM   4111  N   LEU A 592     -26.954 -75.948   8.355  1.00 29.95           N  
ANISOU 4111  N   LEU A 592     3808   3779   3794    324   -174    117       N  
ATOM   4112  CA  LEU A 592     -26.799 -74.813   9.249  1.00 30.99           C  
ANISOU 4112  CA  LEU A 592     3924   3966   3883    286   -201    145       C  
ATOM   4113  C   LEU A 592     -25.328 -74.403   9.201  1.00 30.27           C  
ANISOU 4113  C   LEU A 592     3762   3923   3818    319   -220    151       C  
ATOM   4114  O   LEU A 592     -24.472 -75.058   9.808  1.00 31.54           O  
ANISOU 4114  O   LEU A 592     3901   4074   4010    360   -257    186       O  
ATOM   4115  CB  LEU A 592     -27.213 -75.238  10.647  1.00 34.62           C  
ANISOU 4115  CB  LEU A 592     4428   4407   4320    269   -241    198       C  
ATOM   4116  CG  LEU A 592     -27.713 -74.239  11.651  1.00 38.31           C  
ANISOU 4116  CG  LEU A 592     4913   4918   4725    213   -257    213       C  
ATOM   4117  CD1 LEU A 592     -28.910 -73.470  11.048  1.00 33.56           C  
ANISOU 4117  CD1 LEU A 592     4333   4323   4097    168   -213    171       C  
ATOM   4118  CD2 LEU A 592     -28.117 -75.074  12.879  1.00 42.29           C  
ANISOU 4118  CD2 LEU A 592     5463   5396   5207    205   -290    270       C  
ATOM   4119  N   LEU A 593     -25.028 -73.333   8.493  1.00 27.63           N  
ANISOU 4119  N   LEU A 593     3386   3638   3472    298   -196    122       N  
ATOM   4120  CA  LEU A 593     -23.637 -73.034   8.195  1.00 28.96           C  
ANISOU 4120  CA  LEU A 593     3478   3852   3672    328   -202    122       C  
ATOM   4121  C   LEU A 593     -23.020 -72.046   9.159  1.00 31.41           C  
ANISOU 4121  C   LEU A 593     3757   4213   3964    295   -246    150       C  
ATOM   4122  O   LEU A 593     -21.793 -71.970   9.238  1.00 31.70           O  
ANISOU 4122  O   LEU A 593     3727   4286   4030    320   -268    163       O  
ATOM   4123  CB  LEU A 593     -23.517 -72.441   6.787  1.00 30.45           C  
ANISOU 4123  CB  LEU A 593     3632   4074   3862    320   -149     80       C  
ATOM   4124  CG  LEU A 593     -23.844 -73.388   5.635  1.00 31.44           C  
ANISOU 4124  CG  LEU A 593     3775   4168   4005    355   -102     38       C  
ATOM   4125  CD1 LEU A 593     -23.474 -72.673   4.390  1.00 29.93           C  
ANISOU 4125  CD1 LEU A 593     3537   4033   3802    345    -57      8       C  
ATOM   4126  CD2 LEU A 593     -23.008 -74.662   5.782  1.00 33.81           C  
ANISOU 4126  CD2 LEU A 593     4053   4432   4362    429   -113     41       C  
ATOM   4127  N   TYR A 594     -23.829 -71.227   9.826  1.00 30.78           N  
ANISOU 4127  N   TYR A 594     3718   4141   3837    237   -257    152       N  
ATOM   4128  CA  TYR A 594     -23.308 -70.174  10.704  1.00 30.83           C  
ANISOU 4128  CA  TYR A 594     3699   4193   3821    197   -297    164       C  
ATOM   4129  C   TYR A 594     -23.800 -70.346  12.145  1.00 29.70           C  
ANISOU 4129  C   TYR A 594     3606   4046   3633    174   -340    190       C  
ATOM   4130  O   TYR A 594     -24.024 -69.354  12.839  1.00 29.67           O  
ANISOU 4130  O   TYR A 594     3613   4069   3590    124   -356    179       O  
ATOM   4131  CB  TYR A 594     -23.704 -68.784  10.157  1.00 30.78           C  
ANISOU 4131  CB  TYR A 594     3687   4205   3801    144   -267    132       C  
ATOM   4132  CG  TYR A 594     -23.729 -68.771   8.641  1.00 30.24           C  
ANISOU 4132  CG  TYR A 594     3597   4136   3759    160   -213    111       C  
ATOM   4133  CD1 TYR A 594     -22.534 -68.794   7.924  1.00 28.67           C  
ANISOU 4133  CD1 TYR A 594     3326   3972   3595    186   -203    111       C  
ATOM   4134  CD2 TYR A 594     -24.964 -68.818   7.927  1.00 33.45           C  
ANISOU 4134  CD2 TYR A 594     4050   4511   4147    148   -172     91       C  
ATOM   4135  CE1 TYR A 594     -22.533 -68.847   6.501  1.00 27.52           C  
ANISOU 4135  CE1 TYR A 594     3160   3837   3461    200   -149     90       C  
ATOM   4136  CE2 TYR A 594     -24.973 -68.865   6.506  1.00 33.26           C  
ANISOU 4136  CE2 TYR A 594     4006   4497   4135    160   -125     71       C  
ATOM   4137  CZ  TYR A 594     -23.750 -68.898   5.814  1.00 30.82           C  
ANISOU 4137  CZ  TYR A 594     3630   4227   3854    186   -113     70       C  
ATOM   4138  OH  TYR A 594     -23.702 -68.964   4.436  1.00 29.95           O  
ANISOU 4138  OH  TYR A 594     3499   4138   3743    196    -64     50       O  
ATOM   4139  N   GLY A 595     -24.012 -71.586  12.590  1.00 27.02           N  
ANISOU 4139  N   GLY A 595     3299   3672   3296    209   -356    224       N  
ATOM   4140  CA  GLY A 595     -24.588 -71.839  13.906  1.00 27.43           C  
ANISOU 4140  CA  GLY A 595     3403   3722   3295    184   -391    257       C  
ATOM   4141  C   GLY A 595     -26.108 -71.692  13.907  1.00 30.31           C  
ANISOU 4141  C   GLY A 595     3833   4060   3623    145   -350    235       C  
ATOM   4142  O   GLY A 595     -26.728 -71.130  12.987  1.00 27.04           O  
ANISOU 4142  O   GLY A 595     3422   3633   3217    130   -303    193       O  
ATOM   4143  N   ARG A 596     -26.744 -72.261  14.940  1.00 29.95           N  
ANISOU 4143  N   ARG A 596     3839   4006   3535    130   -369    271       N  
ATOM   4144  CA  ARG A 596     -28.171 -72.023  15.016  1.00 28.74           C  
ANISOU 4144  CA  ARG A 596     3737   3837   3345     90   -328    249       C  
ATOM   4145  C   ARG A 596     -28.443 -70.563  15.382  1.00 27.57           C  
ANISOU 4145  C   ARG A 596     3586   3735   3156     41   -319    206       C  
ATOM   4146  O   ARG A 596     -27.666 -69.929  16.104  1.00 26.66           O  
ANISOU 4146  O   ARG A 596     3449   3666   3016     25   -358    205       O  
ATOM   4147  CB  ARG A 596     -28.831 -72.919  16.051  1.00 31.28           C  
ANISOU 4147  CB  ARG A 596     4112   4147   3626     77   -343    299       C  
ATOM   4148  CG  ARG A 596     -28.326 -72.678  17.428  1.00 35.25           C  
ANISOU 4148  CG  ARG A 596     4618   4707   4068     55   -394    332       C  
ATOM   4149  CD  ARG A 596     -29.220 -73.461  18.380  1.00 38.90           C  
ANISOU 4149  CD  ARG A 596     5137   5163   4479     31   -396    382       C  
ATOM   4150  NE  ARG A 596     -28.537 -73.624  19.630  1.00 43.51           N  
ANISOU 4150  NE  ARG A 596     5724   5799   5009     22   -456    436       N  
ATOM   4151  CZ  ARG A 596     -28.553 -72.707  20.557  1.00 46.00           C  
ANISOU 4151  CZ  ARG A 596     6045   6187   5246    -24   -471    414       C  
ATOM   4152  NH1 ARG A 596     -29.266 -71.626  20.306  1.00 47.12           N  
ANISOU 4152  NH1 ARG A 596     6192   6341   5371    -57   -423    339       N  
ATOM   4153  NH2 ARG A 596     -27.909 -72.879  21.711  1.00 48.87           N  
ANISOU 4153  NH2 ARG A 596     6411   6608   5550    -36   -532    464       N  
ATOM   4154  N   PRO A 597     -29.568 -70.028  14.940  1.00 26.46           N  
ANISOU 4154  N   PRO A 597     3465   3578   3009     16   -272    169       N  
ATOM   4155  CA  PRO A 597     -29.968 -68.682  15.394  1.00 26.83           C  
ANISOU 4155  CA  PRO A 597     3515   3655   3023    -27   -260    126       C  
ATOM   4156  C   PRO A 597     -30.233 -68.721  16.892  1.00 27.30           C  
ANISOU 4156  C   PRO A 597     3609   3752   3010    -57   -283    138       C  
ATOM   4157  O   PRO A 597     -30.728 -69.721  17.407  1.00 29.57           O  
ANISOU 4157  O   PRO A 597     3932   4033   3271    -56   -284    179       O  
ATOM   4158  CB  PRO A 597     -31.252 -68.404  14.599  1.00 26.16           C  
ANISOU 4158  CB  PRO A 597     3446   3539   2956    -36   -205     97       C  
ATOM   4159  CG  PRO A 597     -31.155 -69.406  13.329  1.00 26.22           C  
ANISOU 4159  CG  PRO A 597     3442   3507   3013      3   -192    114       C  
ATOM   4160  CD  PRO A 597     -30.478 -70.629  13.950  1.00 23.36           C  
ANISOU 4160  CD  PRO A 597     3091   3139   2648     29   -229    162       C  
ATOM   4161  N   ALA A 598     -29.826 -67.687  17.624  1.00 22.54           N  
ANISOU 4161  N   ALA A 598     2998   3192   2374    -88   -303    105       N  
ATOM   4162  CA  ALA A 598     -30.230 -67.618  19.042  1.00 21.31           C  
ANISOU 4162  CA  ALA A 598     2880   3082   2134   -125   -315    104       C  
ATOM   4163  C   ALA A 598     -31.662 -67.067  19.137  1.00 24.87           C  
ANISOU 4163  C   ALA A 598     3361   3524   2564   -150   -255     58       C  
ATOM   4164  O   ALA A 598     -32.043 -66.167  18.383  1.00 28.62           O  
ANISOU 4164  O   ALA A 598     3820   3971   3085   -150   -221     11       O  
ATOM   4165  CB  ALA A 598     -29.262 -66.741  19.855  1.00 21.33           C  
ANISOU 4165  CB  ALA A 598     2864   3138   2101   -153   -363     76       C  
ATOM   4166  N   VAL A 599     -32.478 -67.660  20.004  1.00 25.09           N  
ANISOU 4166  N   VAL A 599     3429   3575   2530   -169   -241     80       N  
ATOM   4167  CA  VAL A 599     -33.797 -67.145  20.333  1.00 25.53           C  
ANISOU 4167  CA  VAL A 599     3507   3638   2556   -195   -184     36       C  
ATOM   4168  C   VAL A 599     -33.651 -66.223  21.547  1.00 26.29           C  
ANISOU 4168  C   VAL A 599     3617   3796   2578   -233   -193    -16       C  
ATOM   4169  O   VAL A 599     -33.190 -66.639  22.621  1.00 27.20           O  
ANISOU 4169  O   VAL A 599     3751   3967   2615   -253   -231     14       O  
ATOM   4170  CB  VAL A 599     -34.770 -68.296  20.608  1.00 28.50           C  
ANISOU 4170  CB  VAL A 599     3914   4012   2903   -201   -158     88       C  
ATOM   4171  CG1 VAL A 599     -36.132 -67.758  20.974  1.00 28.95           C  
ANISOU 4171  CG1 VAL A 599     3984   4086   2929   -227    -96     43       C  
ATOM   4172  CG2 VAL A 599     -34.888 -69.117  19.337  1.00 26.61           C  
ANISOU 4172  CG2 VAL A 599     3662   3707   2742   -167   -151    123       C  
ATOM   4173  N   LEU A 600     -33.975 -64.946  21.362  1.00 22.86           N  
ANISOU 4173  N   LEU A 600     3170   3348   2167   -242   -162    -94       N  
ATOM   4174  CA  LEU A 600     -33.674 -63.943  22.371  1.00 24.83           C  
ANISOU 4174  CA  LEU A 600     3429   3644   2362   -278   -173   -162       C  
ATOM   4175  C   LEU A 600     -34.868 -63.667  23.298  1.00 27.86           C  
ANISOU 4175  C   LEU A 600     3844   4067   2676   -304   -118   -209       C  
ATOM   4176  O   LEU A 600     -34.969 -62.562  23.836  1.00 28.02           O  
ANISOU 4176  O   LEU A 600     3869   4102   2676   -326   -102   -295       O  
ATOM   4177  CB  LEU A 600     -33.249 -62.645  21.683  1.00 23.38           C  
ANISOU 4177  CB  LEU A 600     3214   3415   2254   -275   -173   -225       C  
ATOM   4178  CG  LEU A 600     -32.063 -62.766  20.701  1.00 26.11           C  
ANISOU 4178  CG  LEU A 600     3521   3730   2671   -253   -219   -184       C  
ATOM   4179  CD1 LEU A 600     -31.629 -61.314  20.286  1.00 26.05           C  
ANISOU 4179  CD1 LEU A 600     3487   3687   2725   -268   -220   -250       C  
ATOM   4180  CD2 LEU A 600     -30.897 -63.457  21.483  1.00 26.18           C  
ANISOU 4180  CD2 LEU A 600     3529   3796   2621   -264   -288   -139       C  
ATOM   4181  N   TYR A 601     -35.770 -64.628  23.490  1.00 28.16           N  
ANISOU 4181  N   TYR A 601     3901   4119   2680   -303    -86   -161       N  
ATOM   4182  CA  TYR A 601     -36.866 -64.471  24.464  1.00 28.76           C  
ANISOU 4182  CA  TYR A 601     4002   4247   2678   -332    -30   -199       C  
ATOM   4183  C   TYR A 601     -37.211 -65.857  25.007  1.00 30.37           C  
ANISOU 4183  C   TYR A 601     4232   4492   2815   -347    -32   -108       C  
ATOM   4184  O   TYR A 601     -36.742 -66.878  24.482  1.00 27.78           O  
ANISOU 4184  O   TYR A 601     3902   4131   2521   -327    -71    -25       O  
ATOM   4185  CB  TYR A 601     -38.075 -63.777  23.802  1.00 29.45           C  
ANISOU 4185  CB  TYR A 601     4067   4288   2833   -314     43   -255       C  
ATOM   4186  CG  TYR A 601     -38.619 -64.520  22.576  1.00 29.96           C  
ANISOU 4186  CG  TYR A 601     4112   4293   2979   -283     57   -194       C  
ATOM   4187  CD1 TYR A 601     -38.083 -64.342  21.309  1.00 29.25           C  
ANISOU 4187  CD1 TYR A 601     3993   4136   2983   -252     32   -181       C  
ATOM   4188  CD2 TYR A 601     -39.667 -65.445  22.730  1.00 30.99           C  
ANISOU 4188  CD2 TYR A 601     4251   4441   3084   -293     96   -149       C  
ATOM   4189  CE1 TYR A 601     -38.588 -65.078  20.165  1.00 27.74           C  
ANISOU 4189  CE1 TYR A 601     3786   3898   2856   -228     43   -130       C  
ATOM   4190  CE2 TYR A 601     -40.165 -66.164  21.659  1.00 31.99           C  
ANISOU 4190  CE2 TYR A 601     4360   4515   3278   -273    105    -99       C  
ATOM   4191  CZ  TYR A 601     -39.642 -65.978  20.365  1.00 30.27           C  
ANISOU 4191  CZ  TYR A 601     4117   4233   3150   -240     78    -93       C  
ATOM   4192  OH  TYR A 601     -40.216 -66.716  19.334  1.00 28.97           O  
ANISOU 4192  OH  TYR A 601     3938   4026   3042   -226     89    -52       O  
ATOM   4193  N   ARG A 602     -38.038 -65.909  26.068  1.00 30.04           N  
ANISOU 4193  N   ARG A 602     4215   4519   2679   -381     12   -125       N  
ATOM   4194  CA  ARG A 602     -38.339 -67.191  26.703  1.00 31.94           C  
ANISOU 4194  CA  ARG A 602     4483   4803   2848   -405      8    -30       C  
ATOM   4195  C   ARG A 602     -39.396 -67.937  25.913  1.00 30.64           C  
ANISOU 4195  C   ARG A 602     4307   4586   2748   -392     55     15       C  
ATOM   4196  O   ARG A 602     -40.451 -67.371  25.623  1.00 31.67           O  
ANISOU 4196  O   ARG A 602     4417   4706   2910   -389    121    -42       O  
ATOM   4197  CB  ARG A 602     -38.815 -66.988  28.142  1.00 35.76           C  
ANISOU 4197  CB  ARG A 602     4997   5393   3196   -454     41    -59       C  
ATOM   4198  CG  ARG A 602     -37.710 -66.450  29.017  1.00 43.55           C  
ANISOU 4198  CG  ARG A 602     6001   6444   4102   -477    -18    -93       C  
ATOM   4199  CD  ARG A 602     -38.188 -65.712  30.248  1.00 50.10           C  
ANISOU 4199  CD  ARG A 602     6853   7372   4811   -521     26   -178       C  
ATOM   4200  NE  ARG A 602     -37.027 -65.139  30.938  1.00 55.17           N  
ANISOU 4200  NE  ARG A 602     7508   8067   5387   -544    -41   -218       N  
ATOM   4201  CZ  ARG A 602     -36.259 -65.864  31.737  1.00 57.17           C  
ANISOU 4201  CZ  ARG A 602     7785   8393   5544   -572   -109   -138       C  
ATOM   4202  NH1 ARG A 602     -36.569 -67.149  31.912  1.00 60.14           N  
ANISOU 4202  NH1 ARG A 602     8177   8785   5889   -578   -114    -15       N  
ATOM   4203  NH2 ARG A 602     -35.215 -65.330  32.363  1.00 55.74           N  
ANISOU 4203  NH2 ARG A 602     7610   8268   5301   -597   -176   -176       N  
ATOM   4204  N   THR A 603     -39.134 -69.205  25.571  1.00 30.57           N  
ANISOU 4204  N   THR A 603     4308   4542   2764   -385     19    115       N  
ATOM   4205  CA  THR A 603     -40.100 -69.981  24.769  1.00 30.89           C  
ANISOU 4205  CA  THR A 603     4339   4528   2872   -378     56    156       C  
ATOM   4206  C   THR A 603     -39.648 -71.438  24.728  1.00 32.41           C  
ANISOU 4206  C   THR A 603     4554   4687   3072   -378      9    268       C  
ATOM   4207  O   THR A 603     -38.497 -71.753  25.030  1.00 31.86           O  
ANISOU 4207  O   THR A 603     4498   4623   2985   -367    -57    310       O  
ATOM   4208  CB  THR A 603     -40.234 -69.417  23.338  1.00 30.62           C  
ANISOU 4208  CB  THR A 603     4266   4415   2952   -337     69    106       C  
ATOM   4209  OG1 THR A 603     -41.488 -69.784  22.759  1.00 29.15           O  
ANISOU 4209  OG1 THR A 603     4063   4202   2810   -343    121    114       O  
ATOM   4210  CG2 THR A 603     -39.047 -69.901  22.408  1.00 29.27           C  
ANISOU 4210  CG2 THR A 603     4089   4179   2853   -298      3    145       C  
ATOM   4211  N   SER A 604     -40.552 -72.323  24.326  1.00 32.41           N  
ANISOU 4211  N   SER A 604     4557   4650   3108   -390     40    315       N  
ATOM   4212  CA  SER A 604     -40.217 -73.747  24.227  1.00 33.25           C  
ANISOU 4212  CA  SER A 604     4687   4706   3239   -390     -1    418       C  
ATOM   4213  C   SER A 604     -40.150 -74.076  22.749  1.00 28.52           C  
ANISOU 4213  C   SER A 604     4067   4010   2760   -350     -9    407       C  
ATOM   4214  O   SER A 604     -41.144 -73.873  22.034  1.00 28.56           O  
ANISOU 4214  O   SER A 604     4049   3992   2810   -356     39    368       O  
ATOM   4215  CB  SER A 604     -41.276 -74.630  24.882  1.00 36.65           C  
ANISOU 4215  CB  SER A 604     5140   5160   3624   -443     37    486       C  
ATOM   4216  OG  SER A 604     -41.198 -74.451  26.260  1.00 41.95           O  
ANISOU 4216  OG  SER A 604     5836   5929   4175   -481     39    508       O  
ATOM   4217  N   TYR A 605     -39.007 -74.586  22.289  1.00 25.34           N  
ANISOU 4217  N   TYR A 605     3667   3555   2406   -310    -69    440       N  
ATOM   4218  CA  TYR A 605     -38.932 -74.967  20.891  1.00 23.97           C  
ANISOU 4218  CA  TYR A 605     3475   3295   2336   -274    -73    425       C  
ATOM   4219  C   TYR A 605     -38.008 -76.165  20.734  1.00 28.03           C  
ANISOU 4219  C   TYR A 605     4008   3748   2895   -245   -128    497       C  
ATOM   4220  O   TYR A 605     -37.231 -76.486  21.637  1.00 26.98           O  
ANISOU 4220  O   TYR A 605     3892   3641   2717   -243   -173    555       O  
ATOM   4221  CB  TYR A 605     -38.500 -73.812  20.011  1.00 21.41           C  
ANISOU 4221  CB  TYR A 605     3114   2968   2053   -239    -70    342       C  
ATOM   4222  CG  TYR A 605     -37.017 -73.464  20.064  1.00 28.84           C  
ANISOU 4222  CG  TYR A 605     4044   3918   2997   -203   -125    339       C  
ATOM   4223  CD1 TYR A 605     -36.458 -72.780  21.158  1.00 29.16           C  
ANISOU 4223  CD1 TYR A 605     4089   4030   2962   -218   -148    331       C  
ATOM   4224  CD2 TYR A 605     -36.185 -73.790  18.996  1.00 29.12           C  
ANISOU 4224  CD2 TYR A 605     4059   3895   3110   -157   -153    338       C  
ATOM   4225  CE1 TYR A 605     -35.068 -72.434  21.170  1.00 28.57           C  
ANISOU 4225  CE1 TYR A 605     3995   3966   2895   -189   -203    327       C  
ATOM   4226  CE2 TYR A 605     -34.835 -73.450  18.999  1.00 30.47           C  
ANISOU 4226  CE2 TYR A 605     4209   4079   3289   -125   -199    334       C  
ATOM   4227  CZ  TYR A 605     -34.282 -72.776  20.077  1.00 30.10           C  
ANISOU 4227  CZ  TYR A 605     4163   4101   3174   -142   -227    331       C  
ATOM   4228  OH  TYR A 605     -32.930 -72.481  20.009  1.00 28.49           O  
ANISOU 4228  OH  TYR A 605     3930   3909   2986   -113   -277    330       O  
ATOM   4229  N   ASP A 606     -38.168 -76.862  19.586  1.00 25.45           N  
ANISOU 4229  N   ASP A 606     3677   3338   2656   -224   -123    494       N  
ATOM   4230  CA  ASP A 606     -37.457 -78.111  19.296  1.00 28.01           C  
ANISOU 4230  CA  ASP A 606     4018   3584   3041   -192   -165    552       C  
ATOM   4231  C   ASP A 606     -36.578 -77.890  18.088  1.00 25.65           C  
ANISOU 4231  C   ASP A 606     3687   3243   2814   -134   -181    498       C  
ATOM   4232  O   ASP A 606     -37.012 -77.250  17.121  1.00 28.96           O  
ANISOU 4232  O   ASP A 606     4083   3662   3259   -131   -148    428       O  
ATOM   4233  CB  ASP A 606     -38.382 -79.245  18.911  1.00 31.57           C  
ANISOU 4233  CB  ASP A 606     4493   3962   3541   -219   -144    585       C  
ATOM   4234  CG  ASP A 606     -39.327 -79.681  20.027  1.00 38.60           C  
ANISOU 4234  CG  ASP A 606     5413   4883   4368   -284   -124    652       C  
ATOM   4235  OD1 ASP A 606     -38.928 -79.792  21.201  1.00 38.83           O  
ANISOU 4235  OD1 ASP A 606     5463   4959   4331   -296   -150    717       O  
ATOM   4236  OD2 ASP A 606     -40.478 -80.024  19.677  1.00 41.57           O  
ANISOU 4236  OD2 ASP A 606     5792   5235   4766   -325    -83    645       O  
ATOM   4237  N   ILE A 607     -35.391 -78.470  18.074  1.00 22.87           N  
ANISOU 4237  N   ILE A 607     3333   2857   2499    -86   -229    534       N  
ATOM   4238  CA  ILE A 607     -34.613 -78.499  16.841  1.00 22.87           C  
ANISOU 4238  CA  ILE A 607     3302   2811   2574    -30   -236    486       C  
ATOM   4239  C   ILE A 607     -34.826 -79.853  16.180  1.00 25.40           C  
ANISOU 4239  C   ILE A 607     3646   3031   2973    -15   -234    506       C  
ATOM   4240  O   ILE A 607     -34.730 -80.905  16.843  1.00 24.74           O  
ANISOU 4240  O   ILE A 607     3594   2901   2904    -15   -262    583       O  
ATOM   4241  CB  ILE A 607     -33.126 -78.191  17.095  1.00 27.26           C  
ANISOU 4241  CB  ILE A 607     3829   3397   3134     18   -284    498       C  
ATOM   4242  CG1 ILE A 607     -33.020 -76.634  17.252  1.00 27.59           C  
ANISOU 4242  CG1 ILE A 607     3840   3525   3119     -1   -273    441       C  
ATOM   4243  CG2 ILE A 607     -32.239 -78.665  15.853  1.00 24.61           C  
ANISOU 4243  CG2 ILE A 607     3462   2998   2889     83   -290    466       C  
ATOM   4244  CD1 ILE A 607     -31.675 -76.141  17.556  1.00 29.35           C  
ANISOU 4244  CD1 ILE A 607     4028   3789   3336     30   -318    445       C  
ATOM   4245  N   LEU A 608     -35.135 -79.821  14.879  1.00 25.40           N  
ANISOU 4245  N   LEU A 608     3633   2997   3022     -4   -203    436       N  
ATOM   4246  CA  LEU A 608     -35.540 -81.000  14.110  1.00 24.88           C  
ANISOU 4246  CA  LEU A 608     3590   2836   3026     -1   -193    430       C  
ATOM   4247  C   LEU A 608     -34.564 -81.139  12.939  1.00 24.88           C  
ANISOU 4247  C   LEU A 608     3563   2802   3089     63   -197    374       C  
ATOM   4248  O   LEU A 608     -34.346 -80.166  12.212  1.00 23.98           O  
ANISOU 4248  O   LEU A 608     3412   2740   2959     74   -179    313       O  
ATOM   4249  CB  LEU A 608     -36.983 -80.841  13.575  1.00 21.14           C  
ANISOU 4249  CB  LEU A 608     3124   2366   2540    -59   -149    389       C  
ATOM   4250  CG  LEU A 608     -38.097 -80.521  14.595  1.00 22.29           C  
ANISOU 4250  CG  LEU A 608     3286   2563   2622   -125   -130    428       C  
ATOM   4251  CD1 LEU A 608     -39.495 -80.400  13.890  1.00 22.44           C  
ANISOU 4251  CD1 LEU A 608     3298   2583   2645   -176    -88    383       C  
ATOM   4252  CD2 LEU A 608     -38.032 -81.639  15.667  1.00 22.45           C  
ANISOU 4252  CD2 LEU A 608     3347   2537   2644   -140   -157    524       C  
ATOM   4253  N   TYR A 609     -33.960 -82.326  12.779  1.00 23.12           N  
ANISOU 4253  N   TYR A 609     3355   2492   2938    107   -218    396       N  
ATOM   4254  CA  TYR A 609     -32.947 -82.583  11.759  1.00 24.59           C  
ANISOU 4254  CA  TYR A 609     3512   2644   3187    175   -218    343       C  
ATOM   4255  C   TYR A 609     -33.566 -83.429  10.665  1.00 24.96           C  
ANISOU 4255  C   TYR A 609     3584   2612   3290    168   -189    284       C  
ATOM   4256  O   TYR A 609     -34.365 -84.321  10.947  1.00 24.36           O  
ANISOU 4256  O   TYR A 609     3552   2466   3239    132   -191    315       O  
ATOM   4257  CB  TYR A 609     -31.718 -83.339  12.302  1.00 28.64           C  
ANISOU 4257  CB  TYR A 609     4017   3111   3754    241   -262    401       C  
ATOM   4258  CG  TYR A 609     -30.964 -82.589  13.389  1.00 32.12           C  
ANISOU 4258  CG  TYR A 609     4431   3634   4141    250   -301    459       C  
ATOM   4259  CD1 TYR A 609     -30.233 -81.472  13.067  1.00 35.66           C  
ANISOU 4259  CD1 TYR A 609     4825   4163   4560    268   -297    416       C  
ATOM   4260  CD2 TYR A 609     -30.968 -83.024  14.718  1.00 34.79           C  
ANISOU 4260  CD2 TYR A 609     4796   3968   4456    234   -342    559       C  
ATOM   4261  CE1 TYR A 609     -29.521 -80.769  14.030  1.00 38.18           C  
ANISOU 4261  CE1 TYR A 609     5118   4558   4832    270   -336    460       C  
ATOM   4262  CE2 TYR A 609     -30.269 -82.326  15.717  1.00 37.59           C  
ANISOU 4262  CE2 TYR A 609     5125   4407   4751    236   -382    606       C  
ATOM   4263  CZ  TYR A 609     -29.550 -81.182  15.346  1.00 38.72           C  
ANISOU 4263  CZ  TYR A 609     5214   4628   4869    253   -379    551       C  
ATOM   4264  OH  TYR A 609     -28.842 -80.421  16.225  1.00 39.30           O  
ANISOU 4264  OH  TYR A 609     5259   4786   4887    250   -418    582       O  
ATOM   4265  N   HIS A 610     -33.141 -83.193   9.432  1.00 24.57           N  
ANISOU 4265  N   HIS A 610     3504   2572   3259    201   -165    202       N  
ATOM   4266  CA  HIS A 610     -33.545 -84.033   8.314  1.00 26.29           C  
ANISOU 4266  CA  HIS A 610     3744   2719   3528    202   -141    132       C  
ATOM   4267  C   HIS A 610     -32.374 -84.081   7.346  1.00 27.73           C  
ANISOU 4267  C   HIS A 610     3887   2900   3748    275   -128     67       C  
ATOM   4268  O   HIS A 610     -31.489 -83.217   7.394  1.00 24.63           O  
ANISOU 4268  O   HIS A 610     3447   2583   3330    308   -131     71       O  
ATOM   4269  CB  HIS A 610     -34.780 -83.455   7.597  1.00 24.77           C  
ANISOU 4269  CB  HIS A 610     3554   2572   3284    134   -110     80       C  
ATOM   4270  CG  HIS A 610     -35.820 -82.873   8.519  1.00 26.90           C  
ANISOU 4270  CG  HIS A 610     3835   2888   3496     67   -113    135       C  
ATOM   4271  ND1 HIS A 610     -35.678 -81.634   9.131  1.00 25.31           N  
ANISOU 4271  ND1 HIS A 610     3605   2780   3232     61   -115    162       N  
ATOM   4272  CD2 HIS A 610     -37.046 -83.336   8.879  1.00 22.91           C  
ANISOU 4272  CD2 HIS A 610     3364   2354   2988      2   -108    160       C  
ATOM   4273  CE1 HIS A 610     -36.737 -81.394   9.884  1.00 22.38           C  
ANISOU 4273  CE1 HIS A 610     3250   2432   2820      1   -110    200       C  
ATOM   4274  NE2 HIS A 610     -37.591 -82.401   9.737  1.00 25.65           N  
ANISOU 4274  NE2 HIS A 610     3699   2778   3269    -36   -105    203       N  
ATOM   4275  N   THR A 611     -32.460 -84.995   6.362  1.00 25.37           N  
ANISOU 4275  N   THR A 611     3607   2527   3504    291   -107     -3       N  
ATOM   4276  CA  THR A 611     -31.398 -85.084   5.337  1.00 26.33           C  
ANISOU 4276  CA  THR A 611     3691   2655   3658    361    -84    -79       C  
ATOM   4277  C   THR A 611     -31.133 -83.763   4.634  1.00 24.34           C  
ANISOU 4277  C   THR A 611     3388   2526   3333    354    -58   -118       C  
ATOM   4278  O   THR A 611     -29.972 -83.415   4.383  1.00 25.51           O  
ANISOU 4278  O   THR A 611     3486   2716   3491    411    -51   -131       O  
ATOM   4279  CB  THR A 611     -31.762 -86.154   4.306  1.00 28.38           C  
ANISOU 4279  CB  THR A 611     3985   2829   3970    363    -58   -167       C  
ATOM   4280  OG1 THR A 611     -31.895 -87.380   5.020  1.00 30.14           O  
ANISOU 4280  OG1 THR A 611     4253   2924   4274    373    -85   -120       O  
ATOM   4281  CG2 THR A 611     -30.644 -86.313   3.202  1.00 30.30           C  
ANISOU 4281  CG2 THR A 611     4188   3081   4243    439    -24   -257       C  
ATOM   4282  N   ASP A 612     -32.191 -83.015   4.293  1.00 24.81           N  
ANISOU 4282  N   ASP A 612     3457   2645   3325    285    -45   -134       N  
ATOM   4283  CA  ASP A 612     -32.063 -81.839   3.423  1.00 23.47           C  
ANISOU 4283  CA  ASP A 612     3244   2580   3092    274    -19   -175       C  
ATOM   4284  C   ASP A 612     -32.264 -80.500   4.140  1.00 20.89           C  
ANISOU 4284  C   ASP A 612     2894   2335   2707    240    -33   -116       C  
ATOM   4285  O   ASP A 612     -32.146 -79.451   3.484  1.00 19.84           O  
ANISOU 4285  O   ASP A 612     2726   2284   2529    229    -15   -138       O  
ATOM   4286  CB  ASP A 612     -33.087 -81.905   2.248  1.00 24.75           C  
ANISOU 4286  CB  ASP A 612     3426   2756   3221    225      6   -246       C  
ATOM   4287  CG  ASP A 612     -32.882 -83.123   1.345  1.00 29.65           C  
ANISOU 4287  CG  ASP A 612     4069   3306   3890    253     26   -328       C  
ATOM   4288  OD1 ASP A 612     -33.876 -83.529   0.681  1.00 31.36           O  
ANISOU 4288  OD1 ASP A 612     4318   3505   4094    203     34   -378       O  
ATOM   4289  OD2 ASP A 612     -31.745 -83.650   1.300  1.00 28.09           O  
ANISOU 4289  OD2 ASP A 612     3854   3073   3746    324     33   -346       O  
ATOM   4290  N   PHE A 613     -32.620 -80.482   5.434  1.00 19.94           N  
ANISOU 4290  N   PHE A 613     2795   2197   2584    218    -62    -45       N  
ATOM   4291  CA  PHE A 613     -32.873 -79.193   6.097  1.00 22.91           C  
ANISOU 4291  CA  PHE A 613     3152   2649   2903    184    -70     -4       C  
ATOM   4292  C   PHE A 613     -32.936 -79.408   7.611  1.00 25.94           C  
ANISOU 4292  C   PHE A 613     3559   3011   3286    175   -103     71       C  
ATOM   4293  O   PHE A 613     -33.111 -80.540   8.111  1.00 26.84           O  
ANISOU 4293  O   PHE A 613     3710   3050   3438    179   -118    102       O  
ATOM   4294  CB  PHE A 613     -34.199 -78.523   5.600  1.00 20.39           C  
ANISOU 4294  CB  PHE A 613     2841   2369   2538    122    -50    -26       C  
ATOM   4295  CG  PHE A 613     -35.487 -79.322   5.929  1.00 22.02           C  
ANISOU 4295  CG  PHE A 613     3093   2523   2752     74    -52    -14       C  
ATOM   4296  CD1 PHE A 613     -35.842 -80.417   5.199  1.00 24.08           C  
ANISOU 4296  CD1 PHE A 613     3380   2721   3048     69    -44    -56       C  
ATOM   4297  CD2 PHE A 613     -36.338 -78.911   6.964  1.00 21.33           C  
ANISOU 4297  CD2 PHE A 613     3018   2453   2635     30    -59     35       C  
ATOM   4298  CE1 PHE A 613     -37.009 -81.137   5.484  1.00 25.10           C  
ANISOU 4298  CE1 PHE A 613     3547   2800   3188     17    -47    -44       C  
ATOM   4299  CE2 PHE A 613     -37.488 -79.570   7.245  1.00 24.67           C  
ANISOU 4299  CE2 PHE A 613     3472   2838   3062    -19    -56     49       C  
ATOM   4300  CZ  PHE A 613     -37.840 -80.697   6.530  1.00 26.15           C  
ANISOU 4300  CZ  PHE A 613     3686   2959   3291    -28    -53     14       C  
ATOM   4301  N   GLU A 614     -32.799 -78.306   8.335  1.00 22.55           N  
ANISOU 4301  N   GLU A 614     3109   2648   2812    159   -114    102       N  
ATOM   4302  CA  GLU A 614     -32.886 -78.305   9.796  1.00 22.79           C  
ANISOU 4302  CA  GLU A 614     3158   2681   2819    142   -143    169       C  
ATOM   4303  C   GLU A 614     -33.844 -77.180  10.188  1.00 23.88           C  
ANISOU 4303  C   GLU A 614     3297   2879   2897     87   -128    168       C  
ATOM   4304  O   GLU A 614     -33.953 -76.193   9.441  1.00 22.64           O  
ANISOU 4304  O   GLU A 614     3111   2766   2725     79   -108    127       O  
ATOM   4305  CB  GLU A 614     -31.499 -78.124  10.366  1.00 26.76           C  
ANISOU 4305  CB  GLU A 614     3630   3208   3332    188   -176    199       C  
ATOM   4306  CG  GLU A 614     -31.395 -78.199  11.853  1.00 36.61           C  
ANISOU 4306  CG  GLU A 614     4894   4466   4548    174   -214    270       C  
ATOM   4307  CD  GLU A 614     -29.920 -78.182  12.353  1.00 41.53           C  
ANISOU 4307  CD  GLU A 614     5480   5111   5189    224   -257    303       C  
ATOM   4308  OE1 GLU A 614     -28.981 -78.645  11.631  1.00 41.52           O  
ANISOU 4308  OE1 GLU A 614     5446   5083   5247    282   -258    284       O  
ATOM   4309  OE2 GLU A 614     -29.731 -77.681  13.482  1.00 43.56           O  
ANISOU 4309  OE2 GLU A 614     5736   5417   5397    203   -288    346       O  
ATOM   4310  N   SER A 615     -34.582 -77.332  11.315  1.00 19.49           N  
ANISOU 4310  N   SER A 615     2772   2324   2310     49   -135    213       N  
ATOM   4311  CA  SER A 615     -35.552 -76.284  11.678  1.00 20.41           C  
ANISOU 4311  CA  SER A 615     2886   2495   2375      1   -114    203       C  
ATOM   4312  C   SER A 615     -35.625 -76.131  13.208  1.00 22.52           C  
ANISOU 4312  C   SER A 615     3172   2794   2592    -23   -130    254       C  
ATOM   4313  O   SER A 615     -35.247 -77.031  13.967  1.00 22.89           O  
ANISOU 4313  O   SER A 615     3242   2813   2641    -15   -158    309       O  
ATOM   4314  CB  SER A 615     -36.936 -76.620  11.121  1.00 23.94           C  
ANISOU 4314  CB  SER A 615     3348   2921   2828    -39    -83    184       C  
ATOM   4315  OG  SER A 615     -37.458 -77.777  11.792  1.00 25.68           O  
ANISOU 4315  OG  SER A 615     3608   3093   3057    -62    -89    230       O  
ATOM   4316  N   GLY A 616     -36.090 -74.959  13.649  1.00 22.40           N  
ANISOU 4316  N   GLY A 616     3144   2838   2530    -51   -114    234       N  
ATOM   4317  CA  GLY A 616     -36.336 -74.711  15.054  1.00 22.47           C  
ANISOU 4317  CA  GLY A 616     3171   2889   2477    -81   -119    267       C  
ATOM   4318  C   GLY A 616     -37.855 -74.562  15.180  1.00 25.09           C  
ANISOU 4318  C   GLY A 616     3513   3233   2788   -128    -76    256       C  
ATOM   4319  O   GLY A 616     -38.417 -73.569  14.706  1.00 26.03           O  
ANISOU 4319  O   GLY A 616     3607   3377   2907   -136    -47    208       O  
ATOM   4320  N   TYR A 617     -38.523 -75.533  15.785  1.00 24.87           N  
ANISOU 4320  N   TYR A 617     3516   3185   2746   -158    -70    304       N  
ATOM   4321  CA  TYR A 617     -39.983 -75.675  15.720  1.00 22.70           C  
ANISOU 4321  CA  TYR A 617     3245   2914   2467   -203    -28    299       C  
ATOM   4322  C   TYR A 617     -40.596 -75.112  17.004  1.00 23.93           C  
ANISOU 4322  C   TYR A 617     3406   3137   2549   -241     -4    311       C  
ATOM   4323  O   TYR A 617     -40.262 -75.582  18.106  1.00 24.46           O  
ANISOU 4323  O   TYR A 617     3501   3223   2569   -255    -22    366       O  
ATOM   4324  CB  TYR A 617     -40.353 -77.158  15.532  1.00 23.63           C  
ANISOU 4324  CB  TYR A 617     3392   2963   2624   -221    -35    345       C  
ATOM   4325  CG  TYR A 617     -41.857 -77.369  15.472  1.00 27.12           C  
ANISOU 4325  CG  TYR A 617     3831   3409   3064   -275      6    344       C  
ATOM   4326  CD1 TYR A 617     -42.565 -77.137  14.289  1.00 25.77           C  
ANISOU 4326  CD1 TYR A 617     3633   3227   2933   -280     25    292       C  
ATOM   4327  CD2 TYR A 617     -42.573 -77.787  16.605  1.00 27.30           C  
ANISOU 4327  CD2 TYR A 617     3874   3456   3042   -324     24    399       C  
ATOM   4328  CE1 TYR A 617     -43.959 -77.320  14.245  1.00 24.89           C  
ANISOU 4328  CE1 TYR A 617     3508   3126   2823   -332     59    294       C  
ATOM   4329  CE2 TYR A 617     -43.949 -77.956  16.570  1.00 25.93           C  
ANISOU 4329  CE2 TYR A 617     3688   3294   2869   -377     64    399       C  
ATOM   4330  CZ  TYR A 617     -44.636 -77.715  15.379  1.00 26.52           C  
ANISOU 4330  CZ  TYR A 617     3730   3356   2991   -379     80    345       C  
ATOM   4331  OH  TYR A 617     -46.023 -77.874  15.312  1.00 26.42           O  
ANISOU 4331  OH  TYR A 617     3695   3359   2984   -433    116    346       O  
ATOM   4332  N   SER A 618     -41.421 -74.054  16.879  1.00 23.19           N  
ANISOU 4332  N   SER A 618     3283   3085   2443   -254     36    259       N  
ATOM   4333  CA  SER A 618     -42.014 -73.394  18.039  1.00 24.14           C  
ANISOU 4333  CA  SER A 618     3404   3274   2494   -285     68    251       C  
ATOM   4334  C   SER A 618     -43.262 -74.117  18.563  1.00 27.91           C  
ANISOU 4334  C   SER A 618     3890   3765   2949   -336    106    289       C  
ATOM   4335  O   SER A 618     -44.230 -74.291  17.816  1.00 28.40           O  
ANISOU 4335  O   SER A 618     3930   3807   3055   -351    133    276       O  
ATOM   4336  CB  SER A 618     -42.440 -71.967  17.696  1.00 25.92           C  
ANISOU 4336  CB  SER A 618     3591   3530   2729   -273    100    178       C  
ATOM   4337  OG  SER A 618     -43.310 -71.532  18.765  1.00 23.34           O  
ANISOU 4337  OG  SER A 618     3261   3264   2342   -305    145    166       O  
ATOM   4338  N   GLU A 619     -43.272 -74.480  19.868  1.00 26.60           N  
ANISOU 4338  N   GLU A 619     3753   3643   2710   -368    110    337       N  
ATOM   4339  CA  GLU A 619     -44.464 -75.107  20.423  1.00 30.77           C  
ANISOU 4339  CA  GLU A 619     4286   4195   3211   -424    152    377       C  
ATOM   4340  C   GLU A 619     -45.605 -74.111  20.556  1.00 33.30           C  
ANISOU 4340  C   GLU A 619     4565   4575   3513   -440    216    317       C  
ATOM   4341  O   GLU A 619     -46.767 -74.507  20.510  1.00 33.50           O  
ANISOU 4341  O   GLU A 619     4571   4609   3550   -478    257    332       O  
ATOM   4342  CB  GLU A 619     -44.201 -75.704  21.825  1.00 35.75           C  
ANISOU 4342  CB  GLU A 619     4958   4870   3757   -459    143    451       C  
ATOM   4343  CG  GLU A 619     -43.286 -76.877  21.856  1.00 38.27           C  
ANISOU 4343  CG  GLU A 619     5317   5127   4098   -449     83    532       C  
ATOM   4344  CD  GLU A 619     -43.221 -77.509  23.268  1.00 42.70           C  
ANISOU 4344  CD  GLU A 619     5917   5737   4570   -492     76    621       C  
ATOM   4345  OE1 GLU A 619     -43.713 -76.892  24.255  1.00 41.89           O  
ANISOU 4345  OE1 GLU A 619     5811   5731   4374   -526    116    608       O  
ATOM   4346  OE2 GLU A 619     -42.682 -78.637  23.360  1.00 45.26           O  
ANISOU 4346  OE2 GLU A 619     6274   6003   4920   -490     30    706       O  
ATOM   4347  N   ILE A 620     -45.297 -72.828  20.773  1.00 31.65           N  
ANISOU 4347  N   ILE A 620     4338   4407   3279   -412    226    249       N  
ATOM   4348  CA  ILE A 620     -46.360 -71.842  20.923  1.00 32.48           C  
ANISOU 4348  CA  ILE A 620     4402   4562   3377   -418    289    187       C  
ATOM   4349  C   ILE A 620     -47.039 -71.568  19.585  1.00 30.49           C  
ANISOU 4349  C   ILE A 620     4103   4265   3217   -397    299    155       C  
ATOM   4350  O   ILE A 620     -48.254 -71.516  19.525  1.00 34.23           O  
ANISOU 4350  O   ILE A 620     4539   4763   3704   -419    347    146       O  
ATOM   4351  CB  ILE A 620     -45.825 -70.533  21.543  1.00 39.40           C  
ANISOU 4351  CB  ILE A 620     5277   5483   4210   -394    296    117       C  
ATOM   4352  CG1 ILE A 620     -45.051 -70.845  22.823  1.00 44.86           C  
ANISOU 4352  CG1 ILE A 620     6016   6225   4803   -417    274    151       C  
ATOM   4353  CG2 ILE A 620     -46.993 -69.702  21.973  1.00 40.73           C  
ANISOU 4353  CG2 ILE A 620     5408   5707   4363   -403    369     59       C  
ATOM   4354  CD1 ILE A 620     -45.893 -71.641  23.791  1.00 46.75           C  
ANISOU 4354  CD1 ILE A 620     6270   6522   4972   -473    314    207       C  
ATOM   4355  N   PHE A 621     -46.265 -71.380  18.485  1.00 26.85           N  
ANISOU 4355  N   PHE A 621     3639   3746   2816   -357    254    140       N  
ATOM   4356  CA  PHE A 621     -46.830 -71.027  17.181  1.00 28.60           C  
ANISOU 4356  CA  PHE A 621     3817   3935   3113   -337    257    111       C  
ATOM   4357  C   PHE A 621     -47.212 -72.236  16.342  1.00 26.89           C  
ANISOU 4357  C   PHE A 621     3604   3675   2940   -360    240    153       C  
ATOM   4358  O   PHE A 621     -47.888 -72.075  15.324  1.00 28.69           O  
ANISOU 4358  O   PHE A 621     3793   3889   3220   -356    244    134       O  
ATOM   4359  CB  PHE A 621     -45.840 -70.171  16.375  1.00 33.32           C  
ANISOU 4359  CB  PHE A 621     4409   4502   3749   -288    222     74       C  
ATOM   4360  CG  PHE A 621     -45.614 -68.758  16.942  1.00 38.78           C  
ANISOU 4360  CG  PHE A 621     5088   5225   4423   -265    240     18       C  
ATOM   4361  CD1 PHE A 621     -46.609 -68.096  17.637  1.00 38.96           C  
ANISOU 4361  CD1 PHE A 621     5084   5292   4426   -275    295    -18       C  
ATOM   4362  CD2 PHE A 621     -44.381 -68.092  16.749  1.00 43.89           C  
ANISOU 4362  CD2 PHE A 621     5745   5852   5077   -235    203     -4       C  
ATOM   4363  CE1 PHE A 621     -46.419 -66.781  18.130  1.00 39.43           C  
ANISOU 4363  CE1 PHE A 621     5134   5369   4478   -253    314    -82       C  
ATOM   4364  CE2 PHE A 621     -44.170 -66.757  17.219  1.00 43.68           C  
ANISOU 4364  CE2 PHE A 621     5709   5843   5045   -218    217    -63       C  
ATOM   4365  CZ  PHE A 621     -45.210 -66.121  17.936  1.00 41.61           C  
ANISOU 4365  CZ  PHE A 621     5426   5618   4765   -227    273   -104       C  
ATOM   4366  N   LEU A 622     -46.803 -73.430  16.735  1.00 24.62           N  
ANISOU 4366  N   LEU A 622     3360   3362   2634   -384    218    208       N  
ATOM   4367  CA  LEU A 622     -47.118 -74.656  15.996  1.00 25.19           C  
ANISOU 4367  CA  LEU A 622     3442   3378   2752   -409    200    243       C  
ATOM   4368  C   LEU A 622     -46.480 -74.675  14.609  1.00 23.30           C  
ANISOU 4368  C   LEU A 622     3199   3086   2569   -371    161    215       C  
ATOM   4369  O   LEU A 622     -47.028 -75.284  13.685  1.00 25.10           O  
ANISOU 4369  O   LEU A 622     3415   3280   2840   -389    155    212       O  
ATOM   4370  CB  LEU A 622     -48.653 -74.864  15.900  1.00 22.24           C  
ANISOU 4370  CB  LEU A 622     3029   3029   2393   -457    242    247       C  
ATOM   4371  CG  LEU A 622     -49.417 -74.834  17.224  1.00 27.49           C  
ANISOU 4371  CG  LEU A 622     3688   3758   2999   -499    293    272       C  
ATOM   4372  CD1 LEU A 622     -50.952 -74.912  17.063  1.00 29.06           C  
ANISOU 4372  CD1 LEU A 622     3831   3989   3220   -544    339    270       C  
ATOM   4373  CD2 LEU A 622     -48.984 -75.984  18.133  1.00 28.54           C  
ANISOU 4373  CD2 LEU A 622     3878   3875   3092   -535    278    346       C  
ATOM   4374  N   MET A 623     -45.336 -74.027  14.429  1.00 23.84           N  
ANISOU 4374  N   MET A 623     3274   3150   2635   -323    135    192       N  
ATOM   4375  CA  MET A 623     -44.623 -74.019  13.146  1.00 22.77           C  
ANISOU 4375  CA  MET A 623     3133   2974   2544   -287    104    167       C  
ATOM   4376  C   MET A 623     -43.174 -73.590  13.404  1.00 24.55           C  
ANISOU 4376  C   MET A 623     3375   3198   2755   -244     75    163       C  
ATOM   4377  O   MET A 623     -42.841 -73.146  14.520  1.00 22.76           O  
ANISOU 4377  O   MET A 623     3158   3005   2483   -245     78    171       O  
ATOM   4378  CB  MET A 623     -45.294 -73.048  12.134  1.00 21.67           C  
ANISOU 4378  CB  MET A 623     2945   2856   2433   -277    117    123       C  
ATOM   4379  CG  MET A 623     -45.132 -71.508  12.571  1.00 21.22           C  
ANISOU 4379  CG  MET A 623     2862   2842   2359   -250    134     93       C  
ATOM   4380  SD  MET A 623     -46.174 -70.412  11.534  1.00 23.19           S  
ANISOU 4380  SD  MET A 623     3049   3112   2651   -241    152     60       S  
ATOM   4381  CE  MET A 623     -47.844 -70.941  12.032  1.00 21.31           C  
ANISOU 4381  CE  MET A 623     2785   2902   2410   -290    192     75       C  
ATOM   4382  N   PRO A 624     -42.276 -73.691  12.388  1.00 21.57           N  
ANISOU 4382  N   PRO A 624     2995   2788   2411   -209     47    146       N  
ATOM   4383  CA  PRO A 624     -40.886 -73.289  12.632  1.00 21.27           C  
ANISOU 4383  CA  PRO A 624     2963   2753   2364   -171     20    145       C  
ATOM   4384  C   PRO A 624     -40.777 -71.778  12.848  1.00 23.10           C  
ANISOU 4384  C   PRO A 624     3168   3031   2580   -161     32    112       C  
ATOM   4385  O   PRO A 624     -41.507 -70.970  12.235  1.00 22.51           O  
ANISOU 4385  O   PRO A 624     3062   2969   2522   -164     53     83       O  
ATOM   4386  CB  PRO A 624     -40.126 -73.741  11.354  1.00 20.42           C  
ANISOU 4386  CB  PRO A 624     2851   2608   2301   -139     -1    130       C  
ATOM   4387  CG  PRO A 624     -40.951 -74.972  10.869  1.00 18.85           C  
ANISOU 4387  CG  PRO A 624     2670   2365   2127   -166      5    138       C  
ATOM   4388  CD  PRO A 624     -42.395 -74.529  11.159  1.00 20.19           C  
ANISOU 4388  CD  PRO A 624     2822   2568   2279   -209     37    136       C  
ATOM   4389  N   LEU A 625     -39.880 -71.409  13.749  1.00 19.37           N  
ANISOU 4389  N   LEU A 625     2706   2579   2076   -151     14    117       N  
ATOM   4390  CA  LEU A 625     -39.359 -70.028  13.770  1.00 23.69           C  
ANISOU 4390  CA  LEU A 625     3228   3150   2621   -136     12     80       C  
ATOM   4391  C   LEU A 625     -38.369 -69.762  12.617  1.00 23.35           C  
ANISOU 4391  C   LEU A 625     3164   3089   2620   -104    -10     69       C  
ATOM   4392  O   LEU A 625     -38.207 -68.610  12.161  1.00 20.63           O  
ANISOU 4392  O   LEU A 625     2792   2753   2294    -96     -5     41       O  
ATOM   4393  CB  LEU A 625     -38.641 -69.776  15.101  1.00 25.22           C  
ANISOU 4393  CB  LEU A 625     3441   3378   2765   -142     -6     87       C  
ATOM   4394  CG  LEU A 625     -39.509 -69.951  16.359  1.00 27.21           C  
ANISOU 4394  CG  LEU A 625     3716   3665   2958   -177     19     97       C  
ATOM   4395  CD1 LEU A 625     -38.665 -69.669  17.659  1.00 27.19           C  
ANISOU 4395  CD1 LEU A 625     3733   3707   2892   -186     -7    101       C  
ATOM   4396  CD2 LEU A 625     -40.794 -69.058  16.352  1.00 25.71           C  
ANISOU 4396  CD2 LEU A 625     3503   3494   2770   -192     70     54       C  
ATOM   4397  N   TRP A 626     -37.663 -70.807  12.178  1.00 21.09           N  
ANISOU 4397  N   TRP A 626     2887   2774   2350    -85    -32     92       N  
ATOM   4398  CA  TRP A 626     -36.651 -70.726  11.140  1.00 20.41           C  
ANISOU 4398  CA  TRP A 626     2778   2678   2298    -54    -48     82       C  
ATOM   4399  C   TRP A 626     -36.474 -72.119  10.575  1.00 22.68           C  
ANISOU 4399  C   TRP A 626     3083   2926   2609    -38    -56     96       C  
ATOM   4400  O   TRP A 626     -36.666 -73.116  11.282  1.00 19.88           O  
ANISOU 4400  O   TRP A 626     2760   2548   2247    -46    -64    127       O  
ATOM   4401  CB  TRP A 626     -35.275 -70.249  11.681  1.00 23.04           C  
ANISOU 4401  CB  TRP A 626     3099   3031   2624    -36    -77     86       C  
ATOM   4402  CG  TRP A 626     -34.676 -71.052  12.842  1.00 20.43           C  
ANISOU 4402  CG  TRP A 626     2793   2702   2268    -32   -108    123       C  
ATOM   4403  CD1 TRP A 626     -34.717 -70.711  14.171  1.00 22.09           C  
ANISOU 4403  CD1 TRP A 626     3019   2945   2429    -55   -119    133       C  
ATOM   4404  CD2 TRP A 626     -33.842 -72.250  12.775  1.00 19.23           C  
ANISOU 4404  CD2 TRP A 626     2648   2521   2138     -1   -135    156       C  
ATOM   4405  NE1 TRP A 626     -34.034 -71.624  14.919  1.00 21.45           N  
ANISOU 4405  NE1 TRP A 626     2956   2862   2333    -44   -155    179       N  
ATOM   4406  CE2 TRP A 626     -33.462 -72.559  14.099  1.00 21.27           C  
ANISOU 4406  CE2 TRP A 626     2925   2797   2360     -7   -167    195       C  
ATOM   4407  CE3 TRP A 626     -33.351 -73.047  11.715  1.00 19.30           C  
ANISOU 4407  CE3 TRP A 626     2646   2493   2195     35   -136    152       C  
ATOM   4408  CZ2 TRP A 626     -32.683 -73.675  14.424  1.00 22.11           C  
ANISOU 4408  CZ2 TRP A 626     3041   2878   2482     22   -202    243       C  
ATOM   4409  CZ3 TRP A 626     -32.569 -74.176  12.032  1.00 20.36           C  
ANISOU 4409  CZ3 TRP A 626     2789   2595   2351     67   -165    188       C  
ATOM   4410  CH2 TRP A 626     -32.238 -74.465  13.376  1.00 20.70           C  
ANISOU 4410  CH2 TRP A 626     2850   2651   2364     62   -200    238       C  
ATOM   4411  N   THR A 627     -36.060 -72.168   9.321  1.00 19.96           N  
ANISOU 4411  N   THR A 627     2718   2574   2293    -17    -52     75       N  
ATOM   4412  CA  THR A 627     -35.783 -73.419   8.650  1.00 21.95           C  
ANISOU 4412  CA  THR A 627     2983   2785   2572      4    -56     72       C  
ATOM   4413  C   THR A 627     -34.559 -73.135   7.794  1.00 21.30           C  
ANISOU 4413  C   THR A 627     2867   2717   2508     41    -60     53       C  
ATOM   4414  O   THR A 627     -34.550 -72.122   7.093  1.00 21.11           O  
ANISOU 4414  O   THR A 627     2814   2728   2478     35    -48     35       O  
ATOM   4415  CB  THR A 627     -36.977 -73.808   7.743  1.00 25.71           C  
ANISOU 4415  CB  THR A 627     3467   3246   3054    -22    -35     50       C  
ATOM   4416  OG1 THR A 627     -38.079 -74.211   8.583  1.00 26.77           O  
ANISOU 4416  OG1 THR A 627     3627   3367   3176    -58    -29     72       O  
ATOM   4417  CG2 THR A 627     -36.574 -74.963   6.792  1.00 23.57           C  
ANISOU 4417  CG2 THR A 627     3207   2935   2814      1    -36     27       C  
ATOM   4418  N   SER A 628     -33.530 -73.973   7.860  1.00 19.77           N  
ANISOU 4418  N   SER A 628     2673   2498   2339     79    -76     61       N  
ATOM   4419  CA  SER A 628     -32.254 -73.679   7.215  1.00 19.23           C  
ANISOU 4419  CA  SER A 628     2565   2454   2289    115    -78     46       C  
ATOM   4420  C   SER A 628     -31.850 -74.827   6.297  1.00 23.76           C  
ANISOU 4420  C   SER A 628     3140   2991   2898    152    -67     19       C  
ATOM   4421  O   SER A 628     -32.024 -75.999   6.666  1.00 24.37           O  
ANISOU 4421  O   SER A 628     3250   3011   2999    164    -77     29       O  
ATOM   4422  CB  SER A 628     -31.166 -73.470   8.303  1.00 24.10           C  
ANISOU 4422  CB  SER A 628     3164   3085   2908    135   -111     80       C  
ATOM   4423  OG  SER A 628     -29.931 -73.114   7.728  1.00 27.62           O  
ANISOU 4423  OG  SER A 628     3561   3561   3374    165   -112     68       O  
ATOM   4424  N   TYR A 629     -31.398 -74.497   5.075  1.00 20.50           N  
ANISOU 4424  N   TYR A 629     2694   2610   2485    166    -43    -18       N  
ATOM   4425  CA  TYR A 629     -30.940 -75.545   4.170  1.00 22.35           C  
ANISOU 4425  CA  TYR A 629     2927   2816   2748    203    -26    -58       C  
ATOM   4426  C   TYR A 629     -29.950 -74.935   3.192  1.00 22.76           C  
ANISOU 4426  C   TYR A 629     2926   2926   2795    225     -4    -83       C  
ATOM   4427  O   TYR A 629     -30.003 -73.732   2.915  1.00 23.07           O  
ANISOU 4427  O   TYR A 629     2940   3022   2805    197      3    -73       O  
ATOM   4428  CB  TYR A 629     -32.138 -76.158   3.424  1.00 20.60           C  
ANISOU 4428  CB  TYR A 629     2744   2567   2517    174     -9    -94       C  
ATOM   4429  CG  TYR A 629     -33.039 -75.157   2.654  1.00 20.61           C  
ANISOU 4429  CG  TYR A 629     2735   2623   2471    128      7   -106       C  
ATOM   4430  CD1 TYR A 629     -34.035 -74.449   3.286  1.00 21.12           C  
ANISOU 4430  CD1 TYR A 629     2811   2698   2515     86     -3    -74       C  
ATOM   4431  CD2 TYR A 629     -32.887 -74.993   1.249  1.00 22.76           C  
ANISOU 4431  CD2 TYR A 629     2987   2939   2721    129     33   -149       C  
ATOM   4432  CE1 TYR A 629     -34.900 -73.594   2.554  1.00 23.82           C  
ANISOU 4432  CE1 TYR A 629     3141   3084   2826     50      7    -80       C  
ATOM   4433  CE2 TYR A 629     -33.722 -74.193   0.531  1.00 24.52           C  
ANISOU 4433  CE2 TYR A 629     3203   3210   2904     88     40   -150       C  
ATOM   4434  CZ  TYR A 629     -34.714 -73.463   1.178  1.00 26.32           C  
ANISOU 4434  CZ  TYR A 629     3438   3441   3123     51     25   -113       C  
ATOM   4435  OH  TYR A 629     -35.553 -72.673   0.419  1.00 27.01           O  
ANISOU 4435  OH  TYR A 629     3512   3574   3178     17     29   -109       O  
ATOM   4436  N   THR A 630     -29.074 -75.770   2.647  1.00 22.73           N  
ANISOU 4436  N   THR A 630     2905   2908   2825    275     11   -116       N  
ATOM   4437  CA  THR A 630     -28.068 -75.326   1.697  1.00 23.25           C  
ANISOU 4437  CA  THR A 630     2914   3034   2884    299     40   -142       C  
ATOM   4438  C   THR A 630     -28.335 -75.996   0.349  1.00 24.55           C  
ANISOU 4438  C   THR A 630     3091   3201   3036    306     80   -211       C  
ATOM   4439  O   THR A 630     -28.544 -77.222   0.290  1.00 25.50           O  
ANISOU 4439  O   THR A 630     3246   3255   3190    331     83   -246       O  
ATOM   4440  CB  THR A 630     -26.647 -75.669   2.186  1.00 26.94           C  
ANISOU 4440  CB  THR A 630     3336   3498   3401    358     29   -128       C  
ATOM   4441  OG1 THR A 630     -26.386 -74.973   3.418  1.00 27.24           O  
ANISOU 4441  OG1 THR A 630     3363   3547   3441    343    -12    -68       O  
ATOM   4442  CG2 THR A 630     -25.594 -75.265   1.150  1.00 29.16           C  
ANISOU 4442  CG2 THR A 630     3552   3848   3678    381     68   -158       C  
ATOM   4443  N   ILE A 631     -28.308 -75.209  -0.728  1.00 21.33           N  
ANISOU 4443  N   ILE A 631     2655   2868   2581    282    110   -229       N  
ATOM   4444  CA  ILE A 631     -28.596 -75.720  -2.090  1.00 23.69           C  
ANISOU 4444  CA  ILE A 631     2964   3190   2847    280    148   -297       C  
ATOM   4445  C   ILE A 631     -27.315 -75.509  -2.876  1.00 27.65           C  
ANISOU 4445  C   ILE A 631     3404   3759   3343    315    188   -322       C  
ATOM   4446  O   ILE A 631     -26.862 -74.361  -2.991  1.00 27.33           O  
ANISOU 4446  O   ILE A 631     3319   3786   3278    294    192   -280       O  
ATOM   4447  CB  ILE A 631     -29.762 -74.963  -2.784  1.00 23.46           C  
ANISOU 4447  CB  ILE A 631     2954   3209   2753    215    149   -291       C  
ATOM   4448  CG1 ILE A 631     -31.051 -75.115  -1.980  1.00 23.81           C  
ANISOU 4448  CG1 ILE A 631     3048   3195   2805    179    114   -265       C  
ATOM   4449  CG2 ILE A 631     -29.980 -75.485  -4.266  1.00 22.37           C  
ANISOU 4449  CG2 ILE A 631     2823   3111   2566    208    186   -365       C  
ATOM   4450  CD1 ILE A 631     -31.417 -76.612  -1.813  1.00 23.04           C  
ANISOU 4450  CD1 ILE A 631     2997   3013   2744    197    110   -311       C  
ATOM   4451  N   SER A 632     -26.698 -76.594  -3.361  1.00 25.44           N  
ANISOU 4451  N   SER A 632     3118   3456   3091    368    218   -388       N  
ATOM   4452  CA  SER A 632     -25.435 -76.408  -4.049  1.00 27.94           C  
ANISOU 4452  CA  SER A 632     3368   3843   3406    405    262   -412       C  
ATOM   4453  C   SER A 632     -25.646 -75.972  -5.512  1.00 26.56           C  
ANISOU 4453  C   SER A 632     3183   3762   3147    369    308   -453       C  
ATOM   4454  O   SER A 632     -26.730 -76.089  -6.073  1.00 24.51           O  
ANISOU 4454  O   SER A 632     2972   3504   2838    326    306   -479       O  
ATOM   4455  CB  SER A 632     -24.601 -77.696  -4.025  1.00 34.43           C  
ANISOU 4455  CB  SER A 632     4177   4607   4296    485    282   -471       C  
ATOM   4456  OG  SER A 632     -25.031 -78.491  -5.103  1.00 37.48           O  
ANISOU 4456  OG  SER A 632     4596   4989   4655    488    321   -562       O  
ATOM   4457  N   LYS A 633     -24.561 -75.490  -6.127  1.00 27.54           N  
ANISOU 4457  N   LYS A 633     3239   3971   3254    386    350   -456       N  
ATOM   4458  CA  LYS A 633     -24.644 -74.938  -7.479  1.00 29.16           C  
ANISOU 4458  CA  LYS A 633     3427   4283   3369    346    395   -478       C  
ATOM   4459  C   LYS A 633     -25.192 -75.956  -8.469  1.00 35.49           C  
ANISOU 4459  C   LYS A 633     4273   5083   4130    351    427   -578       C  
ATOM   4460  O   LYS A 633     -25.902 -75.581  -9.407  1.00 38.90           O  
ANISOU 4460  O   LYS A 633     4724   5581   4474    297    437   -588       O  
ATOM   4461  CB  LYS A 633     -23.244 -74.460  -7.925  1.00 27.84           C  
ANISOU 4461  CB  LYS A 633     3173   4204   3199    371    443   -471       C  
ATOM   4462  CG  LYS A 633     -23.167 -74.088  -9.428  1.00 29.39           C  
ANISOU 4462  CG  LYS A 633     3348   4522   3296    337    502   -502       C  
ATOM   4463  CD  LYS A 633     -21.744 -73.559  -9.811  1.00 34.21           C  
ANISOU 4463  CD  LYS A 633     3864   5226   3906    355    554   -485       C  
ATOM   4464  CE  LYS A 633     -21.857 -72.926 -11.249  1.00 36.68           C  
ANISOU 4464  CE  LYS A 633     4163   5672   4103    299    605   -487       C  
ATOM   4465  NZ  LYS A 633     -20.638 -72.267 -11.652  1.00 41.93           N  
ANISOU 4465  NZ  LYS A 633     4738   6435   4757    298    654   -456       N  
ATOM   4466  N   GLN A 634     -24.883 -77.243  -8.263  1.00 37.27           N  
ANISOU 4466  N   GLN A 634     4513   5229   4417    413    439   -651       N  
ATOM   4467  CA  GLN A 634     -25.317 -78.316  -9.146  1.00 41.15           C  
ANISOU 4467  CA  GLN A 634     5048   5703   4883    422    470   -761       C  
ATOM   4468  C   GLN A 634     -26.622 -79.002  -8.705  1.00 40.33           C  
ANISOU 4468  C   GLN A 634     5027   5498   4800    393    421   -774       C  
ATOM   4469  O   GLN A 634     -26.971 -80.028  -9.277  1.00 41.93           O  
ANISOU 4469  O   GLN A 634     5269   5661   5000    401    440   -870       O  
ATOM   4470  CB  GLN A 634     -24.200 -79.372  -9.251  1.00 45.07           C  
ANISOU 4470  CB  GLN A 634     5513   6163   5448    511    516   -842       C  
ATOM   4471  CG  GLN A 634     -22.796 -78.834  -9.671  1.00 46.93           C  
ANISOU 4471  CG  GLN A 634     5655   6501   5676    548    572   -837       C  
ATOM   4472  CD  GLN A 634     -21.958 -78.304  -8.488  1.00 49.11           C  
ANISOU 4472  CD  GLN A 634     5874   6754   6030    579    538   -741       C  
ATOM   4473  OE1 GLN A 634     -22.344 -78.427  -7.302  1.00 49.62           O  
ANISOU 4473  OE1 GLN A 634     5972   6724   6157    582    474   -683       O  
ATOM   4474  NE2 GLN A 634     -20.818 -77.701  -8.811  1.00 48.37           N  
ANISOU 4474  NE2 GLN A 634     5694   6755   5928    597    580   -723       N  
ATOM   4475  N   ALA A 635     -27.334 -78.484  -7.701  1.00 38.60           N  
ANISOU 4475  N   ALA A 635     4830   5234   4601    357    363   -686       N  
ATOM   4476  CA  ALA A 635     -28.539 -79.152  -7.196  1.00 38.24           C  
ANISOU 4476  CA  ALA A 635     4855   5094   4582    329    321   -692       C  
ATOM   4477  C   ALA A 635     -29.588 -79.311  -8.284  1.00 38.14           C  
ANISOU 4477  C   ALA A 635     4880   5122   4488    270    327   -752       C  
ATOM   4478  O   ALA A 635     -29.663 -78.515  -9.227  1.00 38.33           O  
ANISOU 4478  O   ALA A 635     4881   5258   4423    232    346   -748       O  
ATOM   4479  CB  ALA A 635     -29.161 -78.386  -6.045  1.00 37.62           C  
ANISOU 4479  CB  ALA A 635     4786   4988   4521    294    266   -588       C  
ATOM   4480  N   GLU A 636     -30.411 -80.350  -8.147  1.00 37.58           N  
ANISOU 4480  N   GLU A 636     4868   4961   4450    257    307   -802       N  
ATOM   4481  CA  GLU A 636     -31.445 -80.653  -9.130  1.00 37.73           C  
ANISOU 4481  CA  GLU A 636     4925   5011   4399    197    306   -868       C  
ATOM   4482  C   GLU A 636     -32.809 -80.239  -8.588  1.00 36.29           C  
ANISOU 4482  C   GLU A 636     4771   4809   4207    130    250   -799       C  
ATOM   4483  O   GLU A 636     -33.126 -80.483  -7.407  1.00 39.60           O  
ANISOU 4483  O   GLU A 636     5211   5137   4699    136    217   -747       O  
ATOM   4484  CB  GLU A 636     -31.431 -82.151  -9.492  1.00 38.95           C  
ANISOU 4484  CB  GLU A 636     5124   5078   4598    223    326   -988       C  
ATOM   4485  N   VAL A 637     -33.604 -79.584  -9.429  1.00 32.26           N  
ANISOU 4485  N   VAL A 637     4259   4394   3607     68    240   -793       N  
ATOM   4486  CA  VAL A 637     -34.989 -79.262  -9.099  1.00 31.08           C  
ANISOU 4486  CA  VAL A 637     4129   4235   3446      3    191   -742       C  
ATOM   4487  C   VAL A 637     -35.839 -80.403  -9.614  1.00 34.73           C  
ANISOU 4487  C   VAL A 637     4640   4654   3903    -35    180   -833       C  
ATOM   4488  O   VAL A 637     -35.647 -80.816 -10.754  1.00 36.91           O  
ANISOU 4488  O   VAL A 637     4922   4981   4120    -42    207   -924       O  
ATOM   4489  CB  VAL A 637     -35.429 -77.937  -9.746  1.00 30.95           C  
ANISOU 4489  CB  VAL A 637     4079   4341   3342    -42    179   -680       C  
ATOM   4490  CG1 VAL A 637     -36.850 -77.602  -9.310  1.00 28.05           C  
ANISOU 4490  CG1 VAL A 637     3722   3958   2977    -98    128   -624       C  
ATOM   4491  CG2 VAL A 637     -34.522 -76.790  -9.341  1.00 34.29           C  
ANISOU 4491  CG2 VAL A 637     4454   4804   3772    -10    192   -597       C  
ATOM   4492  N   SER A 638     -36.758 -80.935  -8.789  1.00 33.22           N  
ANISOU 4492  N   SER A 638     4482   4371   3771    -63    144   -813       N  
ATOM   4493  CA  SER A 638     -37.648 -82.010  -9.276  1.00 38.48           C  
ANISOU 4493  CA  SER A 638     5192   4991   4437   -112    129   -898       C  
ATOM   4494  C   SER A 638     -39.118 -81.649  -9.013  1.00 39.91           C  
ANISOU 4494  C   SER A 638     5375   5187   4603   -187     80   -841       C  
ATOM   4495  O   SER A 638     -39.418 -80.669  -8.334  1.00 42.43           O  
ANISOU 4495  O   SER A 638     5664   5532   4924   -191     62   -741       O  
ATOM   4496  CB  SER A 638     -37.289 -83.381  -8.686  1.00 40.58           C  
ANISOU 4496  CB  SER A 638     5501   5112   4804    -75    138   -954       C  
ATOM   4497  OG  SER A 638     -37.225 -83.328  -7.274  1.00 44.99           O  
ANISOU 4497  OG  SER A 638     6061   5590   5444    -50    120   -862       O  
ATOM   4498  N   SER A 639     -40.040 -82.390  -9.620  1.00 38.91           N  
ANISOU 4498  N   SER A 639     5276   5050   4457   -248     59   -911       N  
ATOM   4499  CA  SER A 639     -41.483 -82.193  -9.478  1.00 42.52           C  
ANISOU 4499  CA  SER A 639     5728   5524   4903   -323     13   -870       C  
ATOM   4500  C   SER A 639     -42.025 -82.854  -8.229  1.00 42.77           C  
ANISOU 4500  C   SER A 639     5785   5433   5033   -335     -5   -833       C  
ATOM   4501  O   SER A 639     -41.477 -83.840  -7.742  1.00 45.75           O  
ANISOU 4501  O   SER A 639     6200   5699   5485   -302     12   -869       O  
ATOM   4502  CB  SER A 639     -42.260 -82.830 -10.634  1.00 46.32           C  
ANISOU 4502  CB  SER A 639     6229   6044   5326   -393     -7   -967       C  
ATOM   4503  OG  SER A 639     -41.762 -82.424 -11.861  1.00 51.03           O  
ANISOU 4503  OG  SER A 639     6811   6755   5822   -388     11  -1015       O  
ATOM   4504  N   ILE A 640     -43.188 -82.382  -7.784  1.00 41.07           N  
ANISOU 4504  N   ILE A 640     5548   5240   4817   -388    -39   -763       N  
ATOM   4505  CA  ILE A 640     -43.949 -83.133  -6.779  1.00 39.14           C  
ANISOU 4505  CA  ILE A 640     5327   4893   4652   -423    -56   -738       C  
ATOM   4506  C   ILE A 640     -44.798 -84.191  -7.478  1.00 40.39           C  
ANISOU 4506  C   ILE A 640     5514   5021   4812   -496    -78   -826       C  
ATOM   4507  O   ILE A 640     -45.671 -83.846  -8.292  1.00 39.23           O  
ANISOU 4507  O   ILE A 640     5342   4964   4600   -556   -107   -841       O  
ATOM   4508  CB  ILE A 640     -44.824 -82.203  -5.943  1.00 40.02           C  
ANISOU 4508  CB  ILE A 640     5397   5041   4767   -446    -75   -631       C  
ATOM   4509  CG1 ILE A 640     -43.939 -81.221  -5.187  1.00 40.22           C  
ANISOU 4509  CG1 ILE A 640     5400   5083   4798   -377    -53   -556       C  
ATOM   4510  CG2 ILE A 640     -45.789 -83.009  -5.028  1.00 41.36           C  
ANISOU 4510  CG2 ILE A 640     5585   5123   5006   -499    -91   -607       C  
ATOM   4511  CD1 ILE A 640     -44.757 -80.180  -4.405  1.00 41.36           C  
ANISOU 4511  CD1 ILE A 640     5503   5270   4943   -393    -66   -461       C  
ATOM   4512  N   PRO A 641     -44.567 -85.475  -7.230  1.00 42.15           N  
ANISOU 4512  N   PRO A 641     5789   5119   5107   -496    -70   -885       N  
ATOM   4513  CA  PRO A 641     -45.409 -86.513  -7.849  1.00 45.56           C  
ANISOU 4513  CA  PRO A 641     6251   5509   5549   -575    -94   -973       C  
ATOM   4514  C   PRO A 641     -46.889 -86.273  -7.585  1.00 47.02           C  
ANISOU 4514  C   PRO A 641     6405   5731   5730   -662   -134   -918       C  
ATOM   4515  O   PRO A 641     -47.281 -85.751  -6.531  1.00 43.78           O  
ANISOU 4515  O   PRO A 641     5968   5316   5350   -660   -137   -812       O  
ATOM   4516  CB  PRO A 641     -44.931 -87.805  -7.178  1.00 45.55           C  
ANISOU 4516  CB  PRO A 641     6308   5341   5658   -552    -79  -1005       C  
ATOM   4517  CG  PRO A 641     -43.561 -87.488  -6.712  1.00 41.82           C  
ANISOU 4517  CG  PRO A 641     5835   4849   5206   -448    -43   -972       C  
ATOM   4518  CD  PRO A 641     -43.584 -86.043  -6.299  1.00 41.01           C  
ANISOU 4518  CD  PRO A 641     5677   4859   5048   -427    -44   -866       C  
ATOM   4519  N   GLU A 642     -47.716 -86.639  -8.571  1.00 49.18           N  
ANISOU 4519  N   GLU A 642     6678   6048   5961   -740   -165   -993       N  
ATOM   4520  CA  GLU A 642     -49.113 -86.231  -8.533  1.00 48.69           C  
ANISOU 4520  CA  GLU A 642     6567   6053   5878   -821   -207   -941       C  
ATOM   4521  C   GLU A 642     -49.823 -86.884  -7.358  1.00 48.40           C  
ANISOU 4521  C   GLU A 642     6540   5910   5939   -864   -213   -886       C  
ATOM   4522  O   GLU A 642     -50.689 -86.254  -6.746  1.00 48.44           O  
ANISOU 4522  O   GLU A 642     6495   5961   5948   -892   -226   -796       O  
ATOM   4523  CB  GLU A 642     -49.816 -86.551  -9.857  1.00 48.82           C  
ANISOU 4523  CB  GLU A 642     6580   6143   5826   -901   -245  -1037       C  
ATOM   4524  N   HIS A 643     -49.394 -88.094  -6.972  1.00 47.76           N  
ANISOU 4524  N   HIS A 643     6522   5684   5940   -861   -198   -932       N  
ATOM   4525  CA  HIS A 643     -49.941 -88.797  -5.819  1.00 49.41           C  
ANISOU 4525  CA  HIS A 643     6747   5781   6244   -900   -200   -872       C  
ATOM   4526  C   HIS A 643     -49.477 -88.227  -4.476  1.00 47.40           C  
ANISOU 4526  C   HIS A 643     6481   5505   6022   -834   -172   -752       C  
ATOM   4527  O   HIS A 643     -49.945 -88.726  -3.446  1.00 49.38           O  
ANISOU 4527  O   HIS A 643     6743   5679   6341   -868   -171   -688       O  
ATOM   4528  CB  HIS A 643     -49.621 -90.305  -5.869  1.00 51.78           C  
ANISOU 4528  CB  HIS A 643     7122   5922   6631   -918   -196   -956       C  
ATOM   4529  CG  HIS A 643     -48.201 -90.649  -5.555  1.00 55.37           C  
ANISOU 4529  CG  HIS A 643     7623   6286   7130   -816   -160   -970       C  
ATOM   4530  ND1 HIS A 643     -47.162 -90.419  -6.436  1.00 57.38           N  
ANISOU 4530  ND1 HIS A 643     7886   6582   7333   -746   -138  -1050       N  
ATOM   4531  CD2 HIS A 643     -47.639 -91.214  -4.457  1.00 57.15           C  
ANISOU 4531  CD2 HIS A 643     7884   6385   7447   -773   -143   -910       C  
ATOM   4532  CE1 HIS A 643     -46.021 -90.800  -5.885  1.00 57.74           C  
ANISOU 4532  CE1 HIS A 643     7965   6532   7441   -659   -109  -1040       C  
ATOM   4533  NE2 HIS A 643     -46.282 -91.292  -4.686  1.00 58.02           N  
ANISOU 4533  NE2 HIS A 643     8019   6463   7564   -673   -114   -953       N  
ATOM   4534  N   LEU A 644     -48.603 -87.206  -4.438  1.00 42.83           N  
ANISOU 4534  N   LEU A 644     5882   4997   5395   -749   -151   -719       N  
ATOM   4535  CA  LEU A 644     -48.183 -86.576  -3.180  1.00 40.21           C  
ANISOU 4535  CA  LEU A 644     5536   4658   5083   -692   -129   -611       C  
ATOM   4536  C   LEU A 644     -48.610 -85.121  -3.086  1.00 38.43           C  
ANISOU 4536  C   LEU A 644     5244   4564   4793   -683   -130   -543       C  
ATOM   4537  O   LEU A 644     -48.233 -84.440  -2.127  1.00 35.29           O  
ANISOU 4537  O   LEU A 644     4832   4175   4401   -635   -112   -465       O  
ATOM   4538  CB  LEU A 644     -46.661 -86.651  -2.996  1.00 40.46           C  
ANISOU 4538  CB  LEU A 644     5600   4640   5131   -594   -101   -621       C  
ATOM   4539  CG  LEU A 644     -46.116 -88.084  -2.953  1.00 44.65           C  
ANISOU 4539  CG  LEU A 644     6196   5024   5743   -585    -96   -680       C  
ATOM   4540  CD1 LEU A 644     -44.581 -88.172  -2.746  1.00 44.76           C  
ANISOU 4540  CD1 LEU A 644     6233   4990   5783   -480    -70   -686       C  
ATOM   4541  CD2 LEU A 644     -46.836 -88.839  -1.866  1.00 47.05           C  
ANISOU 4541  CD2 LEU A 644     6523   5231   6124   -639   -106   -613       C  
ATOM   4542  N   THR A 645     -49.365 -84.616  -4.070  1.00 39.61           N  
ANISOU 4542  N   THR A 645     5353   4815   4884   -727   -155   -572       N  
ATOM   4543  CA  THR A 645     -49.763 -83.204  -4.074  1.00 41.80           C  
ANISOU 4543  CA  THR A 645     5564   5210   5109   -712   -159   -507       C  
ATOM   4544  C   THR A 645     -50.313 -82.763  -2.715  1.00 40.00           C  
ANISOU 4544  C   THR A 645     5308   4973   4919   -714   -145   -411       C  
ATOM   4545  O   THR A 645     -49.991 -81.669  -2.208  1.00 39.10           O  
ANISOU 4545  O   THR A 645     5164   4906   4786   -660   -129   -351       O  
ATOM   4546  CB  THR A 645     -50.824 -82.993  -5.156  1.00 48.56           C  
ANISOU 4546  CB  THR A 645     6377   6159   5915   -779   -198   -539       C  
ATOM   4547  OG1 THR A 645     -50.348 -83.546  -6.386  1.00 50.05           O  
ANISOU 4547  OG1 THR A 645     6599   6356   6062   -788   -209   -640       O  
ATOM   4548  CG2 THR A 645     -51.135 -81.526  -5.327  1.00 50.58           C  
ANISOU 4548  CG2 THR A 645     6565   6532   6121   -754   -206   -475       C  
ATOM   4549  N   ASN A 646     -51.107 -83.624  -2.085  1.00 35.38           N  
ANISOU 4549  N   ASN A 646     4732   4324   4386   -777   -149   -396       N  
ATOM   4550  CA  ASN A 646     -51.811 -83.262  -0.864  1.00 36.46           C  
ANISOU 4550  CA  ASN A 646     4836   4469   4550   -793   -133   -310       C  
ATOM   4551  C   ASN A 646     -51.361 -84.116   0.321  1.00 36.32           C  
ANISOU 4551  C   ASN A 646     4871   4339   4588   -786   -110   -273       C  
ATOM   4552  O   ASN A 646     -52.104 -84.295   1.293  1.00 36.32           O  
ANISOU 4552  O   ASN A 646     4857   4326   4617   -829    -98   -213       O  
ATOM   4553  CB  ASN A 646     -53.319 -83.355  -1.093  1.00 42.52           C  
ANISOU 4553  CB  ASN A 646     5549   5284   5323   -881   -156   -303       C  
ATOM   4554  CG  ASN A 646     -53.789 -82.307  -2.072  1.00 51.03           C  
ANISOU 4554  CG  ASN A 646     6562   6482   6344   -878   -181   -312       C  
ATOM   4555  OD1 ASN A 646     -54.418 -82.617  -3.072  1.00 56.82           O  
ANISOU 4555  OD1 ASN A 646     7277   7253   7058   -935   -218   -361       O  
ATOM   4556  ND2 ASN A 646     -53.440 -81.051  -1.809  1.00 54.00           N  
ANISOU 4556  ND2 ASN A 646     6906   6919   6693   -810   -164   -264       N  
ATOM   4557  N   CYS A 647     -50.150 -84.650   0.237  1.00 33.67           N  
ANISOU 4557  N   CYS A 647     4594   3930   4269   -733   -104   -306       N  
ATOM   4558  CA  CYS A 647     -49.591 -85.416   1.339  1.00 34.18           C  
ANISOU 4558  CA  CYS A 647     4709   3891   4388   -716    -88   -262       C  
ATOM   4559  C   CYS A 647     -49.225 -84.487   2.504  1.00 31.72           C  
ANISOU 4559  C   CYS A 647     4378   3619   4054   -664    -64   -178       C  
ATOM   4560  O   CYS A 647     -48.546 -83.468   2.311  1.00 30.39           O  
ANISOU 4560  O   CYS A 647     4189   3514   3843   -600    -58   -180       O  
ATOM   4561  CB  CYS A 647     -48.357 -86.167   0.825  1.00 37.80           C  
ANISOU 4561  CB  CYS A 647     5225   4265   4873   -662    -90   -325       C  
ATOM   4562  SG  CYS A 647     -47.280 -86.899   2.091  1.00 42.21           S  
ANISOU 4562  SG  CYS A 647     5840   4704   5495   -606    -77   -264       S  
ATOM   4563  N   VAL A 648     -49.712 -84.796   3.704  1.00 29.04           N  
ANISOU 4563  N   VAL A 648     4043   3250   3740   -698    -51   -106       N  
ATOM   4564  CA  VAL A 648     -49.185 -84.201   4.932  1.00 28.76           C  
ANISOU 4564  CA  VAL A 648     4009   3233   3687   -651    -30    -33       C  
ATOM   4565  C   VAL A 648     -48.975 -85.320   5.956  1.00 31.99           C  
ANISOU 4565  C   VAL A 648     4471   3541   4144   -670    -27     24       C  
ATOM   4566  O   VAL A 648     -49.859 -86.169   6.132  1.00 32.08           O  
ANISOU 4566  O   VAL A 648     4490   3506   4192   -747    -30     41       O  
ATOM   4567  CB  VAL A 648     -50.119 -83.124   5.516  1.00 29.53           C  
ANISOU 4567  CB  VAL A 648     4045   3430   3744   -672     -9     12       C  
ATOM   4568  CG1 VAL A 648     -49.439 -82.499   6.734  1.00 31.06           C  
ANISOU 4568  CG1 VAL A 648     4247   3644   3912   -621     13     71       C  
ATOM   4569  CG2 VAL A 648     -50.372 -81.998   4.494  1.00 28.85           C  
ANISOU 4569  CG2 VAL A 648     3904   3437   3620   -652    -16    -32       C  
ATOM   4570  N   ARG A 649     -47.832 -85.319   6.635  1.00 29.27           N  
ANISOU 4570  N   ARG A 649     4159   3164   3800   -605    -26     59       N  
ATOM   4571  CA  ARG A 649     -47.429 -86.466   7.453  1.00 30.61           C  
ANISOU 4571  CA  ARG A 649     4384   3226   4022   -611    -33    114       C  
ATOM   4572  C   ARG A 649     -47.207 -86.046   8.901  1.00 31.37           C  
ANISOU 4572  C   ARG A 649     4481   3358   4082   -596    -20    208       C  
ATOM   4573  O   ARG A 649     -46.443 -85.101   9.154  1.00 30.96           O  
ANISOU 4573  O   ARG A 649     4412   3367   3985   -533    -16    211       O  
ATOM   4574  CB  ARG A 649     -46.105 -87.125   6.895  1.00 31.39           C  
ANISOU 4574  CB  ARG A 649     4525   3234   4166   -540    -52     68       C  
ATOM   4575  CG  ARG A 649     -46.238 -87.852   5.514  1.00 34.96           C  
ANISOU 4575  CG  ARG A 649     4994   3628   4662   -558    -64    -33       C  
ATOM   4576  CD  ARG A 649     -44.851 -88.351   4.953  1.00 37.79           C  
ANISOU 4576  CD  ARG A 649     5386   3913   5061   -474    -73    -88       C  
ATOM   4577  NE  ARG A 649     -44.178 -89.238   5.921  1.00 40.44           N  
ANISOU 4577  NE  ARG A 649     5766   4140   5460   -445    -83    -18       N  
ATOM   4578  CZ  ARG A 649     -43.019 -88.970   6.545  1.00 38.83           C  
ANISOU 4578  CZ  ARG A 649     5564   3938   5252   -365    -87     27       C  
ATOM   4579  NH1 ARG A 649     -42.339 -87.896   6.263  1.00 34.82           N  
ANISOU 4579  NH1 ARG A 649     5019   3524   4687   -307    -79      2       N  
ATOM   4580  NH2 ARG A 649     -42.531 -89.808   7.432  1.00 41.68           N  
ANISOU 4580  NH2 ARG A 649     5962   4203   5670   -345   -103    101       N  
ATOM   4581  N   PRO A 650     -47.818 -86.730   9.877  1.00 33.85           N  
ANISOU 4581  N   PRO A 650     4813   3636   4412   -656    -13    285       N  
ATOM   4582  CA  PRO A 650     -47.455 -86.496  11.283  1.00 32.72           C  
ANISOU 4582  CA  PRO A 650     4682   3522   4229   -641     -4    377       C  
ATOM   4583  C   PRO A 650     -45.960 -86.665  11.506  1.00 31.77           C  
ANISOU 4583  C   PRO A 650     4596   3353   4121   -557    -30    392       C  
ATOM   4584  O   PRO A 650     -45.298 -87.481  10.845  1.00 29.90           O  
ANISOU 4584  O   PRO A 650     4391   3018   3951   -524    -53    358       O  
ATOM   4585  CB  PRO A 650     -48.238 -87.572  12.052  1.00 34.28           C  
ANISOU 4585  CB  PRO A 650     4907   3659   4460   -724      1    457       C  
ATOM   4586  CG  PRO A 650     -49.421 -87.930  11.111  1.00 36.12           C  
ANISOU 4586  CG  PRO A 650     5116   3878   4731   -800      7    401       C  
ATOM   4587  CD  PRO A 650     -48.771 -87.850   9.725  1.00 34.36           C  
ANISOU 4587  CD  PRO A 650     4895   3626   4534   -744    -16    295       C  
ATOM   4588  N   ASP A 651     -45.432 -85.851  12.448  1.00 26.41           N  
ANISOU 4588  N   ASP A 651     3907   2749   3379   -521    -25    438       N  
ATOM   4589  CA  ASP A 651     -44.026 -85.913  12.878  1.00 29.38           C  
ANISOU 4589  CA  ASP A 651     4307   3099   3758   -445    -53    468       C  
ATOM   4590  C   ASP A 651     -43.955 -86.610  14.236  1.00 28.84           C  
ANISOU 4590  C   ASP A 651     4275   3000   3682   -470    -64    583       C  
ATOM   4591  O   ASP A 651     -44.400 -86.038  15.249  1.00 27.13           O  
ANISOU 4591  O   ASP A 651     4047   2871   3391   -504    -45    635       O  
ATOM   4592  CB  ASP A 651     -43.438 -84.493  12.983  1.00 28.32           C  
ANISOU 4592  CB  ASP A 651     4134   3071   3553   -393    -46    438       C  
ATOM   4593  CG  ASP A 651     -41.902 -84.489  13.168  1.00 30.05           C  
ANISOU 4593  CG  ASP A 651     4365   3269   3783   -311    -79    451       C  
ATOM   4594  OD1 ASP A 651     -41.379 -85.469  13.741  1.00 29.25           O  
ANISOU 4594  OD1 ASP A 651     4301   3093   3720   -299   -106    517       O  
ATOM   4595  OD2 ASP A 651     -41.224 -83.528  12.720  1.00 27.22           O  
ANISOU 4595  OD2 ASP A 651     3976   2967   3400   -260    -79    399       O  
ATOM   4596  N   VAL A 652     -43.368 -87.822  14.279  1.00 30.47           N  
ANISOU 4596  N   VAL A 652     4527   3086   3964   -452    -96    625       N  
ATOM   4597  CA  VAL A 652     -43.393 -88.663  15.503  1.00 31.05           C  
ANISOU 4597  CA  VAL A 652     4640   3115   4042   -485   -112    749       C  
ATOM   4598  C   VAL A 652     -42.464 -88.138  16.604  1.00 33.97           C  
ANISOU 4598  C   VAL A 652     5010   3554   4344   -439   -133    819       C  
ATOM   4599  O   VAL A 652     -42.409 -88.703  17.728  1.00 33.72           O  
ANISOU 4599  O   VAL A 652     5009   3509   4295   -464   -150    933       O  
ATOM   4600  CB  VAL A 652     -43.022 -90.132  15.208  1.00 31.68           C  
ANISOU 4600  CB  VAL A 652     4769   3031   4238   -474   -143    778       C  
ATOM   4601  CG1 VAL A 652     -44.162 -90.875  14.481  1.00 32.45           C  
ANISOU 4601  CG1 VAL A 652     4877   3054   4398   -553   -125    738       C  
ATOM   4602  CG2 VAL A 652     -41.666 -90.215  14.442  1.00 30.98           C  
ANISOU 4602  CG2 VAL A 652     4678   2886   4206   -369   -172    715       C  
ATOM   4603  N   ARG A 653     -41.701 -87.078  16.295  1.00 29.32           N  
ANISOU 4603  N   ARG A 653     4387   3039   3715   -375   -136    755       N  
ATOM   4604  CA  ARG A 653     -40.863 -86.426  17.299  1.00 27.84           C  
ANISOU 4604  CA  ARG A 653     4192   2931   3453   -339   -157    806       C  
ATOM   4605  C   ARG A 653     -41.619 -85.366  18.097  1.00 30.90           C  
ANISOU 4605  C   ARG A 653     4558   3453   3731   -389   -122    811       C  
ATOM   4606  O   ARG A 653     -41.067 -84.830  19.072  1.00 32.32           O  
ANISOU 4606  O   ARG A 653     4736   3708   3835   -375   -137    854       O  
ATOM   4607  CB  ARG A 653     -39.656 -85.753  16.605  1.00 25.33           C  
ANISOU 4607  CB  ARG A 653     3844   2632   3150   -251   -177    733       C  
ATOM   4608  CG  ARG A 653     -38.716 -86.736  15.861  1.00 26.55           C  
ANISOU 4608  CG  ARG A 653     4013   2664   3412   -185   -209    720       C  
ATOM   4609  CD  ARG A 653     -37.709 -85.955  14.986  1.00 24.74           C  
ANISOU 4609  CD  ARG A 653     3741   2468   3189   -109   -213    632       C  
ATOM   4610  NE  ARG A 653     -38.413 -85.295  13.888  1.00 24.38           N  
ANISOU 4610  NE  ARG A 653     3671   2458   3133   -131   -172    529       N  
ATOM   4611  CZ  ARG A 653     -37.834 -84.634  12.879  1.00 24.49           C  
ANISOU 4611  CZ  ARG A 653     3650   2500   3153    -84   -164    443       C  
ATOM   4612  NH1 ARG A 653     -36.488 -84.584  12.769  1.00 24.76           N  
ANISOU 4612  NH1 ARG A 653     3666   2528   3213     -8   -189    439       N  
ATOM   4613  NH2 ARG A 653     -38.614 -84.078  11.947  1.00 24.53           N  
ANISOU 4613  NH2 ARG A 653     3636   2540   3143   -114   -131    367       N  
ATOM   4614  N   VAL A 654     -42.810 -84.982  17.635  1.00 30.25           N  
ANISOU 4614  N   VAL A 654     4453   3404   3638   -442    -75    758       N  
ATOM   4615  CA  VAL A 654     -43.539 -83.817  18.123  1.00 29.26           C  
ANISOU 4615  CA  VAL A 654     4293   3401   3422   -475    -33    733       C  
ATOM   4616  C   VAL A 654     -44.951 -84.273  18.482  1.00 32.69           C  
ANISOU 4616  C   VAL A 654     4729   3846   3848   -564      7    771       C  
ATOM   4617  O   VAL A 654     -45.632 -84.892  17.657  1.00 33.32           O  
ANISOU 4617  O   VAL A 654     4806   3859   3995   -596     16    747       O  
ATOM   4618  CB  VAL A 654     -43.613 -82.700  17.058  1.00 27.86           C  
ANISOU 4618  CB  VAL A 654     4070   3266   3249   -442    -14    620       C  
ATOM   4619  CG1 VAL A 654     -44.529 -81.583  17.526  1.00 25.05           C  
ANISOU 4619  CG1 VAL A 654     3677   3020   2820   -477     34    594       C  
ATOM   4620  CG2 VAL A 654     -42.184 -82.113  16.725  1.00 26.98           C  
ANISOU 4620  CG2 VAL A 654     3949   3159   3141   -359    -49    582       C  
ATOM   4621  N   SER A 655     -45.416 -83.896  19.669  1.00 31.48           N  
ANISOU 4621  N   SER A 655     4573   3783   3605   -606     35    822       N  
ATOM   4622  CA  SER A 655     -46.718 -84.316  20.170  1.00 36.04           C  
ANISOU 4622  CA  SER A 655     5146   4385   4164   -694     79    870       C  
ATOM   4623  C   SER A 655     -47.898 -83.915  19.263  1.00 35.48           C  
ANISOU 4623  C   SER A 655     5024   4331   4124   -726    122    791       C  
ATOM   4624  O   SER A 655     -47.911 -82.824  18.655  1.00 35.53           O  
ANISOU 4624  O   SER A 655     4990   4389   4121   -687    135    702       O  
ATOM   4625  CB  SER A 655     -46.924 -83.699  21.556  1.00 39.32           C  
ANISOU 4625  CB  SER A 655     5558   4923   4460   -723    110    915       C  
ATOM   4626  OG  SER A 655     -48.281 -83.784  21.900  1.00 44.17           O  
ANISOU 4626  OG  SER A 655     6148   5587   5050   -802    169    934       O  
ATOM   4627  N   PRO A 656     -48.920 -84.774  19.163  1.00 34.29           N  
ANISOU 4627  N   PRO A 656     4872   4141   4014   -802    141    827       N  
ATOM   4628  CA  PRO A 656     -50.171 -84.356  18.468  1.00 35.16           C  
ANISOU 4628  CA  PRO A 656     4925   4291   4145   -842    183    763       C  
ATOM   4629  C   PRO A 656     -50.709 -83.011  18.965  1.00 35.38           C  
ANISOU 4629  C   PRO A 656     4899   4453   4092   -836    234    723       C  
ATOM   4630  O   PRO A 656     -51.133 -82.178  18.160  1.00 35.49           O  
ANISOU 4630  O   PRO A 656     4861   4501   4123   -814    249    640       O  
ATOM   4631  CB  PRO A 656     -51.171 -85.489  18.789  1.00 35.71           C  
ANISOU 4631  CB  PRO A 656     5002   4320   4245   -940    201    838       C  
ATOM   4632  CG  PRO A 656     -50.343 -86.681  19.091  1.00 38.10           C  
ANISOU 4632  CG  PRO A 656     5375   4512   4589   -938    154    920       C  
ATOM   4633  CD  PRO A 656     -48.968 -86.167  19.644  1.00 37.09           C  
ANISOU 4633  CD  PRO A 656     5277   4409   4408   -854    122    931       C  
ATOM   4634  N   GLY A 657     -50.635 -82.757  20.275  1.00 33.76           N  
ANISOU 4634  N   GLY A 657     4706   4325   3798   -851    260    777       N  
ATOM   4635  CA  GLY A 657     -51.108 -81.497  20.815  1.00 33.42           C  
ANISOU 4635  CA  GLY A 657     4615   4404   3678   -843    313    730       C  
ATOM   4636  C   GLY A 657     -50.258 -80.299  20.444  1.00 33.44           C  
ANISOU 4636  C   GLY A 657     4607   4431   3667   -758    295    646       C  
ATOM   4637  O   GLY A 657     -50.717 -79.167  20.588  1.00 34.11           O  
ANISOU 4637  O   GLY A 657     4647   4598   3716   -743    337    586       O  
ATOM   4638  N   PHE A 658     -49.032 -80.511  19.955  1.00 30.83           N  
ANISOU 4638  N   PHE A 658     4315   4029   3370   -702    235    641       N  
ATOM   4639  CA  PHE A 658     -48.214 -79.398  19.486  1.00 28.87           C  
ANISOU 4639  CA  PHE A 658     4052   3799   3118   -627    217    564       C  
ATOM   4640  C   PHE A 658     -48.031 -79.425  17.961  1.00 28.40           C  
ANISOU 4640  C   PHE A 658     3977   3668   3146   -591    188    505       C  
ATOM   4641  O   PHE A 658     -47.036 -78.888  17.462  1.00 30.38           O  
ANISOU 4641  O   PHE A 658     4231   3904   3409   -529    157    463       O  
ATOM   4642  CB  PHE A 658     -46.841 -79.394  20.182  1.00 30.37           C  
ANISOU 4642  CB  PHE A 658     4287   3988   3264   -587    173    597       C  
ATOM   4643  CG  PHE A 658     -46.878 -78.968  21.647  1.00 33.86           C  
ANISOU 4643  CG  PHE A 658     4739   4528   3598   -612    199    630       C  
ATOM   4644  CD1 PHE A 658     -47.535 -77.807  22.046  1.00 36.93           C  
ANISOU 4644  CD1 PHE A 658     5089   5010   3931   -617    254    568       C  
ATOM   4645  CD2 PHE A 658     -46.245 -79.730  22.608  1.00 38.48           C  
ANISOU 4645  CD2 PHE A 658     5373   5111   4136   -628    168    721       C  
ATOM   4646  CE1 PHE A 658     -47.539 -77.405  23.378  1.00 40.58           C  
ANISOU 4646  CE1 PHE A 658     5564   5568   4287   -641    281    585       C  
ATOM   4647  CE2 PHE A 658     -46.260 -79.363  23.952  1.00 41.66           C  
ANISOU 4647  CE2 PHE A 658     5789   5614   4426   -656    189    752       C  
ATOM   4648  CZ  PHE A 658     -46.922 -78.182  24.333  1.00 42.89           C  
ANISOU 4648  CZ  PHE A 658     5907   5869   4520   -664    249    677       C  
ATOM   4649  N   SER A 659     -48.956 -80.063  17.234  1.00 26.63           N  
ANISOU 4649  N   SER A 659     3735   3405   2979   -634    197    503       N  
ATOM   4650  CA  SER A 659     -48.983 -80.125  15.770  1.00 29.14           C  
ANISOU 4650  CA  SER A 659     4034   3669   3368   -613    174    444       C  
ATOM   4651  C   SER A 659     -50.148 -79.308  15.232  1.00 27.95           C  
ANISOU 4651  C   SER A 659     3816   3578   3224   -630    209    393       C  
ATOM   4652  O   SER A 659     -51.191 -79.203  15.891  1.00 31.19           O  
ANISOU 4652  O   SER A 659     4196   4047   3610   -678    254    414       O  
ATOM   4653  CB  SER A 659     -49.155 -81.573  15.281  1.00 29.57           C  
ANISOU 4653  CB  SER A 659     4122   3627   3488   -654    149    476       C  
ATOM   4654  OG  SER A 659     -48.118 -82.384  15.786  1.00 31.97           O  
ANISOU 4654  OG  SER A 659     4484   3866   3798   -634    115    531       O  
ATOM   4655  N   GLN A 660     -49.977 -78.736  14.034  1.00 25.95           N  
ANISOU 4655  N   GLN A 660     3538   3318   3006   -590    190    329       N  
ATOM   4656  CA  GLN A 660     -51.119 -78.245  13.256  1.00 27.00           C  
ANISOU 4656  CA  GLN A 660     3606   3488   3163   -610    208    290       C  
ATOM   4657  C   GLN A 660     -52.001 -79.424  12.871  1.00 30.14           C  
ANISOU 4657  C   GLN A 660     4002   3846   3605   -682    203    312       C  
ATOM   4658  O   GLN A 660     -51.629 -80.577  13.058  1.00 30.63           O  
ANISOU 4658  O   GLN A 660     4116   3836   3685   -708    183    349       O  
ATOM   4659  CB  GLN A 660     -50.639 -77.539  11.979  1.00 27.28           C  
ANISOU 4659  CB  GLN A 660     3623   3517   3224   -556    179    230       C  
ATOM   4660  CG  GLN A 660     -49.839 -76.306  12.271  1.00 28.06           C  
ANISOU 4660  CG  GLN A 660     3718   3653   3291   -492    183    207       C  
ATOM   4661  CD  GLN A 660     -49.251 -75.733  11.003  1.00 27.92           C  
ANISOU 4661  CD  GLN A 660     3688   3623   3298   -445    152    162       C  
ATOM   4662  OE1 GLN A 660     -49.930 -75.676  10.017  1.00 30.36           O  
ANISOU 4662  OE1 GLN A 660     3961   3941   3634   -459    144    140       O  
ATOM   4663  NE2 GLN A 660     -47.993 -75.313  11.030  1.00 26.55           N  
ANISOU 4663  NE2 GLN A 660     3540   3436   3111   -393    134    151       N  
ATOM   4664  N   ASN A 661     -53.162 -79.143  12.284  1.00 33.12           N  
ANISOU 4664  N   ASN A 661     4316   4264   4005   -714    217    288       N  
ATOM   4665  CA  ASN A 661     -53.989 -80.231  11.799  1.00 33.78           C  
ANISOU 4665  CA  ASN A 661     4393   4310   4133   -788    206    299       C  
ATOM   4666  C   ASN A 661     -54.618 -79.857  10.459  1.00 33.02           C  
ANISOU 4666  C   ASN A 661     4242   4236   4069   -790    184    245       C  
ATOM   4667  O   ASN A 661     -54.841 -78.673  10.157  1.00 32.12           O  
ANISOU 4667  O   ASN A 661     4075   4187   3943   -748    193    216       O  
ATOM   4668  CB  ASN A 661     -55.033 -80.617  12.835  1.00 37.84           C  
ANISOU 4668  CB  ASN A 661     4882   4860   4635   -860    251    355       C  
ATOM   4669  CG  ASN A 661     -56.122 -79.600  12.941  1.00 39.60           C  
ANISOU 4669  CG  ASN A 661     5017   5182   4846   -863    293    337       C  
ATOM   4670  OD1 ASN A 661     -57.098 -79.683  12.210  1.00 40.54           O  
ANISOU 4670  OD1 ASN A 661     5078   5321   5004   -902    288    319       O  
ATOM   4671  ND2 ASN A 661     -55.977 -78.641  13.865  1.00 38.64           N  
ANISOU 4671  ND2 ASN A 661     4883   5125   4675   -822    335    338       N  
ATOM   4672  N   CYS A 662     -54.875 -80.889   9.636  1.00 29.81           N  
ANISOU 4672  N   CYS A 662     3850   3772   3705   -841    151    231       N  
ATOM   4673  CA  CYS A 662     -55.370 -80.640   8.281  1.00 31.64           C  
ANISOU 4673  CA  CYS A 662     4036   4027   3957   -847    120    177       C  
ATOM   4674  C   CYS A 662     -56.840 -80.231   8.238  1.00 31.85           C  
ANISOU 4674  C   CYS A 662     3972   4133   3995   -896    139    185       C  
ATOM   4675  O   CYS A 662     -57.268 -79.605   7.259  1.00 33.66           O  
ANISOU 4675  O   CYS A 662     4148   4411   4231   -883    116    150       O  
ATOM   4676  CB  CYS A 662     -55.162 -81.892   7.408  1.00 35.71           C  
ANISOU 4676  CB  CYS A 662     4600   4458   4511   -889     78    147       C  
ATOM   4677  SG  CYS A 662     -53.368 -82.179   7.107  1.00 41.76           S  
ANISOU 4677  SG  CYS A 662     5455   5140   5272   -810     52    119       S  
ATOM   4678  N   LEU A 663     -57.654 -80.693   9.197  1.00 30.82           N  
ANISOU 4678  N   LEU A 663     3822   4017   3872   -958    177    233       N  
ATOM   4679  CA  LEU A 663     -59.055 -80.292   9.231  1.00 31.11           C  
ANISOU 4679  CA  LEU A 663     3761   4136   3922  -1002    201    242       C  
ATOM   4680  C   LEU A 663     -59.218 -78.771   9.247  1.00 28.82           C  
ANISOU 4680  C   LEU A 663     3407   3930   3612   -928    224    224       C  
ATOM   4681  O   LEU A 663     -60.052 -78.231   8.513  1.00 29.80           O  
ANISOU 4681  O   LEU A 663     3452   4112   3760   -930    210    205       O  
ATOM   4682  CB  LEU A 663     -59.743 -80.900  10.459  1.00 34.46           C  
ANISOU 4682  CB  LEU A 663     4176   4573   4345  -1071    252    303       C  
ATOM   4683  CG  LEU A 663     -61.240 -80.633  10.545  1.00 39.48           C  
ANISOU 4683  CG  LEU A 663     4704   5296   5002  -1125    284    315       C  
ATOM   4684  CD1 LEU A 663     -61.911 -80.880   9.212  1.00 40.02           C  
ANISOU 4684  CD1 LEU A 663     4723   5368   5115  -1165    230    278       C  
ATOM   4685  CD2 LEU A 663     -61.885 -81.589  11.631  1.00 43.33           C  
ANISOU 4685  CD2 LEU A 663     5192   5780   5492  -1218    329    381       C  
ATOM   4686  N   ALA A 664     -58.448 -78.067  10.086  1.00 25.21           N  
ANISOU 4686  N   ALA A 664     2982   3481   3117   -863    255    231       N  
ATOM   4687  CA  ALA A 664     -58.555 -76.603  10.144  1.00 28.28           C  
ANISOU 4687  CA  ALA A 664     3315   3934   3497   -792    278    209       C  
ATOM   4688  C   ALA A 664     -58.303 -75.968   8.773  1.00 28.27           C  
ANISOU 4688  C   ALA A 664     3295   3934   3514   -746    226    170       C  
ATOM   4689  O   ALA A 664     -58.985 -74.994   8.382  1.00 26.60           O  
ANISOU 4689  O   ALA A 664     3004   3780   3323   -717    229    160       O  
ATOM   4690  CB  ALA A 664     -57.559 -76.029  11.164  1.00 28.85           C  
ANISOU 4690  CB  ALA A 664     3440   4000   3523   -734    308    211       C  
ATOM   4691  N   TYR A 665     -57.350 -76.509   8.005  1.00 26.92           N  
ANISOU 4691  N   TYR A 665     3189   3700   3337   -738    178    152       N  
ATOM   4692  CA  TYR A 665     -57.128 -75.920   6.673  1.00 24.37           C  
ANISOU 4692  CA  TYR A 665     2848   3390   3022   -701    131    119       C  
ATOM   4693  C   TYR A 665     -58.291 -76.203   5.719  1.00 25.44           C  
ANISOU 4693  C   TYR A 665     2916   3566   3186   -756     99    113       C  
ATOM   4694  O   TYR A 665     -58.606 -75.370   4.884  1.00 23.06           O  
ANISOU 4694  O   TYR A 665     2559   3311   2891   -727     74    104       O  
ATOM   4695  CB  TYR A 665     -55.805 -76.426   6.071  1.00 24.17           C  
ANISOU 4695  CB  TYR A 665     2906   3300   2979   -678     95     95       C  
ATOM   4696  CG  TYR A 665     -54.615 -75.794   6.738  1.00 24.02           C  
ANISOU 4696  CG  TYR A 665     2933   3260   2934   -609    113     97       C  
ATOM   4697  CD1 TYR A 665     -54.256 -74.480   6.462  1.00 25.80           C  
ANISOU 4697  CD1 TYR A 665     3133   3519   3153   -544    113     87       C  
ATOM   4698  CD2 TYR A 665     -53.864 -76.507   7.656  1.00 25.57           C  
ANISOU 4698  CD2 TYR A 665     3196   3404   3115   -613    128    115       C  
ATOM   4699  CE1 TYR A 665     -53.179 -73.883   7.078  1.00 23.42           C  
ANISOU 4699  CE1 TYR A 665     2869   3199   2829   -489    127     86       C  
ATOM   4700  CE2 TYR A 665     -52.782 -75.921   8.290  1.00 26.70           C  
ANISOU 4700  CE2 TYR A 665     3376   3536   3232   -555    140    118       C  
ATOM   4701  CZ  TYR A 665     -52.439 -74.620   7.977  1.00 25.63           C  
ANISOU 4701  CZ  TYR A 665     3212   3435   3089   -495    139     99       C  
ATOM   4702  OH  TYR A 665     -51.380 -74.051   8.612  1.00 29.15           O  
ANISOU 4702  OH  TYR A 665     3692   3870   3512   -446    148     99       O  
ATOM   4703  N   LYS A 666     -58.899 -77.386   5.770  1.00 25.50           N  
ANISOU 4703  N   LYS A 666     2928   3552   3211   -839     94    120       N  
ATOM   4704  CA  LYS A 666     -60.095 -77.622   4.951  1.00 27.20           C  
ANISOU 4704  CA  LYS A 666     3068   3814   3453   -901     63    114       C  
ATOM   4705  C   LYS A 666     -61.237 -76.680   5.324  1.00 28.02           C  
ANISOU 4705  C   LYS A 666     3063   4004   3579   -889     94    140       C  
ATOM   4706  O   LYS A 666     -61.984 -76.224   4.449  1.00 27.40           O  
ANISOU 4706  O   LYS A 666     2908   3984   3519   -893     59    136       O  
ATOM   4707  CB  LYS A 666     -60.605 -79.061   5.115  1.00 31.35           C  
ANISOU 4707  CB  LYS A 666     3614   4297   4002  -1001     58    120       C  
ATOM   4708  CG  LYS A 666     -59.821 -80.085   4.364  1.00 37.22           C  
ANISOU 4708  CG  LYS A 666     4442   4959   4742  -1026     13     80       C  
ATOM   4709  CD  LYS A 666     -60.567 -81.427   4.553  1.00 43.40           C  
ANISOU 4709  CD  LYS A 666     5229   5698   5562  -1134      9     89       C  
ATOM   4710  CE  LYS A 666     -59.595 -82.593   4.559  1.00 48.02           C  
ANISOU 4710  CE  LYS A 666     5923   6168   6156  -1149     -4     70       C  
ATOM   4711  NZ  LYS A 666     -60.403 -83.860   4.705  1.00 53.45           N  
ANISOU 4711  NZ  LYS A 666     6612   6806   6890  -1262    -11     81       N  
ATOM   4712  N   ASN A 667     -61.468 -76.480   6.625  1.00 27.11           N  
ANISOU 4712  N   ASN A 667     2935   3902   3463   -883    159    167       N  
ATOM   4713  CA  ASN A 667     -62.603 -75.648   7.059  1.00 29.21           C  
ANISOU 4713  CA  ASN A 667     3093   4250   3755   -872    199    185       C  
ATOM   4714  C   ASN A 667     -62.384 -74.181   6.692  1.00 28.91           C  
ANISOU 4714  C   ASN A 667     3017   4243   3723   -775    194    172       C  
ATOM   4715  O   ASN A 667     -63.347 -73.446   6.479  1.00 30.50           O  
ANISOU 4715  O   ASN A 667     3117   4510   3963   -758    198    180       O  
ATOM   4716  CB  ASN A 667     -62.817 -75.751   8.583  1.00 26.77           C  
ANISOU 4716  CB  ASN A 667     2785   3953   3432   -885    278    210       C  
ATOM   4717  CG  ASN A 667     -63.261 -77.136   8.992  1.00 32.53           C  
ANISOU 4717  CG  ASN A 667     3534   4659   4167   -989    287    238       C  
ATOM   4718  OD1 ASN A 667     -63.752 -77.896   8.159  1.00 32.28           O  
ANISOU 4718  OD1 ASN A 667     3484   4617   4162  -1056    241    235       O  
ATOM   4719  ND2 ASN A 667     -63.072 -77.482  10.284  1.00 35.79           N  
ANISOU 4719  ND2 ASN A 667     3986   5062   4549  -1007    346    268       N  
ATOM   4720  N   ASP A 668     -61.138 -73.737   6.664  1.00 26.89           N  
ANISOU 4720  N   ASP A 668     2837   3942   3439   -712    186    156       N  
ATOM   4721  CA  ASP A 668     -60.869 -72.317   6.399  1.00 24.56           C  
ANISOU 4721  CA  ASP A 668     2511   3665   3154   -624    184    148       C  
ATOM   4722  C   ASP A 668     -60.874 -72.133   4.889  1.00 25.05           C  
ANISOU 4722  C   ASP A 668     2552   3740   3224   -618    111    146       C  
ATOM   4723  O   ASP A 668     -59.939 -72.566   4.210  1.00 24.83           O  
ANISOU 4723  O   ASP A 668     2597   3672   3165   -621     71    130       O  
ATOM   4724  CB  ASP A 668     -59.546 -71.942   7.026  1.00 23.05           C  
ANISOU 4724  CB  ASP A 668     2407   3424   2928   -569    205    134       C  
ATOM   4725  CG  ASP A 668     -59.280 -70.434   7.010  1.00 27.52           C  
ANISOU 4725  CG  ASP A 668     2945   4000   3513   -482    215    125       C  
ATOM   4726  OD1 ASP A 668     -59.606 -69.774   5.990  1.00 27.36           O  
ANISOU 4726  OD1 ASP A 668     2871   4003   3523   -455    175    133       O  
ATOM   4727  OD2 ASP A 668     -58.706 -69.936   8.021  1.00 26.18           O  
ANISOU 4727  OD2 ASP A 668     2809   3813   3325   -445    260    111       O  
ATOM   4728  N   LYS A 669     -61.925 -71.543   4.347  1.00 25.49           N  
ANISOU 4728  N   LYS A 669     2508   3857   3320   -612     93    162       N  
ATOM   4729  CA  LYS A 669     -61.995 -71.420   2.888  1.00 25.00           C  
ANISOU 4729  CA  LYS A 669     2423   3820   3256   -616     18    167       C  
ATOM   4730  C   LYS A 669     -61.129 -70.305   2.337  1.00 26.67           C  
ANISOU 4730  C   LYS A 669     2656   4017   3459   -535     -4    172       C  
ATOM   4731  O   LYS A 669     -61.138 -70.087   1.118  1.00 26.37           O  
ANISOU 4731  O   LYS A 669     2600   4007   3411   -534    -65    184       O  
ATOM   4732  CB  LYS A 669     -63.425 -71.171   2.384  1.00 28.11           C  
ANISOU 4732  CB  LYS A 669     2694   4291   3695   -638     -8    193       C  
ATOM   4733  CG  LYS A 669     -64.370 -72.051   2.983  1.00 36.46           C  
ANISOU 4733  CG  LYS A 669     3711   5372   4772   -713     20    195       C  
ATOM   4734  CD  LYS A 669     -64.136 -73.488   2.625  1.00 33.36           C  
ANISOU 4734  CD  LYS A 669     3384   4945   4344   -803    -12    173       C  
ATOM   4735  CE  LYS A 669     -65.123 -74.193   3.540  1.00 32.98           C  
ANISOU 4735  CE  LYS A 669     3288   4918   4326   -873     35    186       C  
ATOM   4736  NZ  LYS A 669     -64.678 -75.555   3.885  1.00 31.55           N  
ANISOU 4736  NZ  LYS A 669     3196   4671   4120   -948     42    171       N  
ATOM   4737  N   GLN A 670     -60.407 -69.572   3.176  1.00 26.40           N  
ANISOU 4737  N   GLN A 670     2659   3944   3428   -473     43    166       N  
ATOM   4738  CA  GLN A 670     -59.493 -68.595   2.599  1.00 29.44           C  
ANISOU 4738  CA  GLN A 670     3072   4308   3807   -408     19    172       C  
ATOM   4739  C   GLN A 670     -58.053 -69.022   2.680  1.00 29.14           C  
ANISOU 4739  C   GLN A 670     3141   4212   3717   -405     19    147       C  
ATOM   4740  O   GLN A 670     -57.228 -68.509   1.918  1.00 29.82           O  
ANISOU 4740  O   GLN A 670     3256   4288   3787   -371    -12    153       O  
ATOM   4741  CB  GLN A 670     -59.604 -67.245   3.322  1.00 34.24           C  
ANISOU 4741  CB  GLN A 670     3640   4908   4463   -332     61    179       C  
ATOM   4742  CG  GLN A 670     -60.873 -66.464   3.088  1.00 42.15           C  
ANISOU 4742  CG  GLN A 670     4525   5959   5530   -306     56    208       C  
ATOM   4743  CD  GLN A 670     -60.713 -65.125   3.817  1.00 54.22           C  
ANISOU 4743  CD  GLN A 670     6036   7457   7109   -223    102    202       C  
ATOM   4744  OE1 GLN A 670     -60.839 -65.057   5.055  1.00 56.94           O  
ANISOU 4744  OE1 GLN A 670     6383   7790   7460   -213    170    170       O  
ATOM   4745  NE2 GLN A 670     -60.333 -64.074   3.070  1.00 57.73           N  
ANISOU 4745  NE2 GLN A 670     6471   7882   7581   -168     65    229       N  
ATOM   4746  N   MET A 671     -57.723 -69.944   3.574  1.00 28.25           N  
ANISOU 4746  N   MET A 671     3086   4066   3582   -438     53    126       N  
ATOM   4747  CA  MET A 671     -56.330 -70.245   3.886  1.00 25.43           C  
ANISOU 4747  CA  MET A 671     2823   3653   3187   -422     61    107       C  
ATOM   4748  C   MET A 671     -55.936 -71.606   3.318  1.00 23.86           C  
ANISOU 4748  C   MET A 671     2681   3429   2955   -477     30     89       C  
ATOM   4749  O   MET A 671     -56.594 -72.605   3.613  1.00 23.05           O  
ANISOU 4749  O   MET A 671     2575   3325   2857   -537     37     87       O  
ATOM   4750  CB  MET A 671     -56.138 -70.270   5.442  1.00 25.64           C  
ANISOU 4750  CB  MET A 671     2878   3656   3210   -414    122    100       C  
ATOM   4751  CG  MET A 671     -54.686 -70.288   5.925  1.00 22.81           C  
ANISOU 4751  CG  MET A 671     2604   3247   2817   -384    129     86       C  
ATOM   4752  SD  MET A 671     -53.705 -68.869   5.303  1.00 24.18           S  
ANISOU 4752  SD  MET A 671     2780   3409   2998   -311    109     84       S  
ATOM   4753  CE  MET A 671     -54.662 -67.488   5.952  1.00 24.86           C  
ANISOU 4753  CE  MET A 671     2788   3522   3134   -268    148     88       C  
ATOM   4754  N   SER A 672     -54.793 -71.678   2.658  1.00 23.95           N  
ANISOU 4754  N   SER A 672     2749   3414   2937   -456      5     74       N  
ATOM   4755  CA  SER A 672     -54.190 -72.962   2.308  1.00 24.38           C  
ANISOU 4755  CA  SER A 672     2870   3428   2965   -494    -13     46       C  
ATOM   4756  C   SER A 672     -52.900 -73.139   3.131  1.00 24.63           C  
ANISOU 4756  C   SER A 672     2974   3402   2982   -461     12     38       C  
ATOM   4757  O   SER A 672     -52.762 -72.570   4.224  1.00 22.68           O  
ANISOU 4757  O   SER A 672     2726   3149   2742   -432     48     54       O  
ATOM   4758  CB  SER A 672     -53.971 -73.006   0.763  1.00 25.02           C  
ANISOU 4758  CB  SER A 672     2949   3537   3020   -501    -63     28       C  
ATOM   4759  OG  SER A 672     -53.466 -74.273   0.332  1.00 25.45           O  
ANISOU 4759  OG  SER A 672     3064   3551   3053   -538    -79    -13       O  
ATOM   4760  N   TYR A 673     -51.987 -73.981   2.659  1.00 24.63           N  
ANISOU 4760  N   TYR A 673     3034   3361   2963   -466     -5     12       N  
ATOM   4761  CA  TYR A 673     -50.731 -74.144   3.383  1.00 22.39           C  
ANISOU 4761  CA  TYR A 673     2810   3027   2669   -430     12     10       C  
ATOM   4762  C   TYR A 673     -49.593 -74.299   2.381  1.00 22.50           C  
ANISOU 4762  C   TYR A 673     2859   3027   2662   -403    -11    -20       C  
ATOM   4763  O   TYR A 673     -49.808 -74.720   1.255  1.00 24.38           O  
ANISOU 4763  O   TYR A 673     3094   3281   2889   -428    -38    -47       O  
ATOM   4764  CB  TYR A 673     -50.757 -75.359   4.342  1.00 24.03           C  
ANISOU 4764  CB  TYR A 673     3063   3181   2888   -465     28     16       C  
ATOM   4765  CG  TYR A 673     -50.957 -76.685   3.624  1.00 27.31           C  
ANISOU 4765  CG  TYR A 673     3505   3558   3313   -516      4    -12       C  
ATOM   4766  CD1 TYR A 673     -49.854 -77.387   3.118  1.00 27.77           C  
ANISOU 4766  CD1 TYR A 673     3619   3565   3366   -496    -11    -44       C  
ATOM   4767  CD2 TYR A 673     -52.232 -77.221   3.443  1.00 27.89           C  
ANISOU 4767  CD2 TYR A 673     3546   3647   3404   -582     -3    -10       C  
ATOM   4768  CE1 TYR A 673     -50.011 -78.613   2.458  1.00 30.54           C  
ANISOU 4768  CE1 TYR A 673     4000   3872   3732   -540    -31    -82       C  
ATOM   4769  CE2 TYR A 673     -52.424 -78.486   2.761  1.00 31.80           C  
ANISOU 4769  CE2 TYR A 673     4070   4099   3913   -637    -28    -45       C  
ATOM   4770  CZ  TYR A 673     -51.293 -79.156   2.277  1.00 32.87           C  
ANISOU 4770  CZ  TYR A 673     4268   4176   4044   -613    -41    -84       C  
ATOM   4771  OH  TYR A 673     -51.412 -80.344   1.622  1.00 34.95           O  
ANISOU 4771  OH  TYR A 673     4565   4390   4325   -660    -63   -129       O  
ATOM   4772  N   GLY A 674     -48.377 -73.904   2.798  1.00 21.64           N  
ANISOU 4772  N   GLY A 674     2780   2897   2545   -354      0    -17       N  
ATOM   4773  CA  GLY A 674     -47.164 -74.177   2.050  1.00 22.25           C  
ANISOU 4773  CA  GLY A 674     2891   2957   2606   -326    -13    -44       C  
ATOM   4774  C   GLY A 674     -46.142 -74.829   2.965  1.00 22.86           C  
ANISOU 4774  C   GLY A 674     3019   2975   2692   -303     -1    -43       C  
ATOM   4775  O   GLY A 674     -46.438 -75.139   4.131  1.00 25.40           O  
ANISOU 4775  O   GLY A 674     3353   3271   3026   -316     14    -18       O  
ATOM   4776  N   PHE A 675     -44.952 -75.045   2.416  1.00 21.81           N  
ANISOU 4776  N   PHE A 675     2910   2827   2551   -270     -7    -67       N  
ATOM   4777  CA  PHE A 675     -43.825 -75.665   3.128  1.00 22.61           C  
ANISOU 4777  CA  PHE A 675     3052   2873   2665   -238     -2    -65       C  
ATOM   4778  C   PHE A 675     -42.634 -74.709   3.185  1.00 23.98           C  
ANISOU 4778  C   PHE A 675     3214   3070   2827   -187      1    -57       C  
ATOM   4779  O   PHE A 675     -42.354 -74.011   2.201  1.00 23.77           O  
ANISOU 4779  O   PHE A 675     3163   3087   2783   -174     -1    -70       O  
ATOM   4780  CB  PHE A 675     -43.426 -76.990   2.441  1.00 23.70           C  
ANISOU 4780  CB  PHE A 675     3227   2961   2818   -242    -10   -108       C  
ATOM   4781  CG  PHE A 675     -44.514 -78.059   2.588  1.00 26.38           C  
ANISOU 4781  CG  PHE A 675     3584   3259   3179   -299    -15   -113       C  
ATOM   4782  CD1 PHE A 675     -44.788 -78.611   3.858  1.00 26.03           C  
ANISOU 4782  CD1 PHE A 675     3563   3168   3159   -316     -9    -71       C  
ATOM   4783  CD2 PHE A 675     -45.285 -78.435   1.524  1.00 28.40           C  
ANISOU 4783  CD2 PHE A 675     3832   3531   3429   -341    -27   -154       C  
ATOM   4784  CE1 PHE A 675     -45.779 -79.544   4.037  1.00 26.46           C  
ANISOU 4784  CE1 PHE A 675     3631   3185   3237   -375    -12    -67       C  
ATOM   4785  CE2 PHE A 675     -46.331 -79.386   1.690  1.00 29.16           C  
ANISOU 4785  CE2 PHE A 675     3940   3589   3550   -402    -34   -158       C  
ATOM   4786  CZ  PHE A 675     -46.573 -79.925   2.953  1.00 26.96           C  
ANISOU 4786  CZ  PHE A 675     3683   3258   3302   -420    -24   -112       C  
ATOM   4787  N   LEU A 676     -41.934 -74.670   4.344  1.00 20.53           N  
ANISOU 4787  N   LEU A 676     2794   2609   2398   -164      5    -31       N  
ATOM   4788  CA  LEU A 676     -40.734 -73.824   4.439  1.00 22.88           C  
ANISOU 4788  CA  LEU A 676     3078   2927   2688   -121      4    -25       C  
ATOM   4789  C   LEU A 676     -39.525 -74.411   3.696  1.00 21.52           C  
ANISOU 4789  C   LEU A 676     2915   2738   2523    -87      0    -52       C  
ATOM   4790  O   LEU A 676     -38.856 -73.687   2.960  1.00 22.82           O  
ANISOU 4790  O   LEU A 676     3053   2940   2675    -66      3    -63       O  
ATOM   4791  CB  LEU A 676     -40.367 -73.564   5.921  1.00 22.10           C  
ANISOU 4791  CB  LEU A 676     2991   2818   2589   -111      4      8       C  
ATOM   4792  CG  LEU A 676     -41.387 -72.635   6.575  1.00 22.58           C  
ANISOU 4792  CG  LEU A 676     3033   2910   2638   -135     17     24       C  
ATOM   4793  CD1 LEU A 676     -41.024 -72.436   8.039  1.00 20.57           C  
ANISOU 4793  CD1 LEU A 676     2794   2654   2370   -130     19     48       C  
ATOM   4794  CD2 LEU A 676     -41.429 -71.232   5.869  1.00 21.94           C  
ANISOU 4794  CD2 LEU A 676     2911   2871   2556   -124     21     16       C  
ATOM   4795  N   PHE A 677     -39.184 -75.735   3.916  1.00 19.77           N  
ANISOU 4795  N   PHE A 677     2729   2458   2326    -78     -5    -63       N  
ATOM   4796  CA  PHE A 677     -38.270 -76.377   3.006  1.00 21.70           C  
ANISOU 4796  CA  PHE A 677     2977   2685   2582    -45     -3   -104       C  
ATOM   4797  C   PHE A 677     -39.040 -76.880   1.786  1.00 24.23           C  
ANISOU 4797  C   PHE A 677     3303   3012   2893    -76      2   -152       C  
ATOM   4798  O   PHE A 677     -39.963 -77.675   1.926  1.00 23.65           O  
ANISOU 4798  O   PHE A 677     3254   2898   2833   -113     -4   -158       O  
ATOM   4799  CB  PHE A 677     -37.490 -77.566   3.653  1.00 21.49           C  
ANISOU 4799  CB  PHE A 677     2983   2586   2598    -13    -11    -98       C  
ATOM   4800  CG  PHE A 677     -36.655 -78.311   2.628  1.00 24.12           C  
ANISOU 4800  CG  PHE A 677     3318   2897   2951     24     -2   -154       C  
ATOM   4801  CD1 PHE A 677     -35.445 -77.774   2.180  1.00 22.96           C  
ANISOU 4801  CD1 PHE A 677     3136   2790   2797     69      8   -167       C  
ATOM   4802  CD2 PHE A 677     -37.114 -79.508   2.034  1.00 26.31           C  
ANISOU 4802  CD2 PHE A 677     3626   3116   3252      9      1   -201       C  
ATOM   4803  CE1 PHE A 677     -34.702 -78.405   1.125  1.00 23.77           C  
ANISOU 4803  CE1 PHE A 677     3233   2885   2912    104     26   -228       C  
ATOM   4804  CE2 PHE A 677     -36.373 -80.139   1.039  1.00 24.90           C  
ANISOU 4804  CE2 PHE A 677     3449   2922   3089     44     16   -266       C  
ATOM   4805  CZ  PHE A 677     -35.141 -79.575   0.581  1.00 22.42           C  
ANISOU 4805  CZ  PHE A 677     3098   2658   2763     95     31   -280       C  
ATOM   4806  N   PRO A 678     -38.669 -76.490   0.579  1.00 26.98           N  
ANISOU 4806  N   PRO A 678     3629   3409   3212    -66     11   -188       N  
ATOM   4807  CA  PRO A 678     -39.484 -76.869  -0.596  1.00 25.39           C  
ANISOU 4807  CA  PRO A 678     3432   3229   2988   -103     10   -235       C  
ATOM   4808  C   PRO A 678     -39.280 -78.319  -1.015  1.00 28.11           C  
ANISOU 4808  C   PRO A 678     3813   3510   3357    -99     14   -296       C  
ATOM   4809  O   PRO A 678     -38.145 -78.750  -1.279  1.00 29.13           O  
ANISOU 4809  O   PRO A 678     3947   3619   3501    -52     28   -328       O  
ATOM   4810  CB  PRO A 678     -38.980 -75.917  -1.694  1.00 27.34           C  
ANISOU 4810  CB  PRO A 678     3643   3558   3187    -91     20   -245       C  
ATOM   4811  CG  PRO A 678     -37.571 -75.720  -1.373  1.00 27.23           C  
ANISOU 4811  CG  PRO A 678     3619   3539   3189    -38     33   -237       C  
ATOM   4812  CD  PRO A 678     -37.532 -75.636   0.218  1.00 27.51           C  
ANISOU 4812  CD  PRO A 678     3664   3524   3264    -28     21   -184       C  
ATOM   4813  N   PRO A 679     -40.370 -79.082  -1.193  1.00 30.47           N  
ANISOU 4813  N   PRO A 679     4136   3778   3664   -150      3   -320       N  
ATOM   4814  CA  PRO A 679     -40.244 -80.442  -1.771  1.00 32.07           C  
ANISOU 4814  CA  PRO A 679     4377   3916   3894   -153      6   -392       C  
ATOM   4815  C   PRO A 679     -39.516 -80.490  -3.100  1.00 30.41           C  
ANISOU 4815  C   PRO A 679     4158   3750   3646   -128     24   -466       C  
ATOM   4816  O   PRO A 679     -38.873 -81.511  -3.401  1.00 31.97           O  
ANISOU 4816  O   PRO A 679     4383   3887   3876    -99     37   -529       O  
ATOM   4817  CB  PRO A 679     -41.694 -80.881  -1.951  1.00 32.38           C  
ANISOU 4817  CB  PRO A 679     4426   3946   3930   -227    -13   -404       C  
ATOM   4818  CG  PRO A 679     -42.456 -80.029  -0.907  1.00 32.85           C  
ANISOU 4818  CG  PRO A 679     4461   4032   3989   -249    -21   -319       C  
ATOM   4819  CD  PRO A 679     -41.766 -78.723  -0.869  1.00 30.85           C  
ANISOU 4819  CD  PRO A 679     4172   3847   3703   -207    -12   -284       C  
ATOM   4820  N   TYR A 680     -39.615 -79.418  -3.906  1.00 27.53           N  
ANISOU 4820  N   TYR A 680     3757   3490   3215   -140     26   -460       N  
ATOM   4821  CA  TYR A 680     -38.939 -79.303  -5.213  1.00 29.77           C  
ANISOU 4821  CA  TYR A 680     4027   3839   3444   -124     47   -521       C  
ATOM   4822  C   TYR A 680     -37.420 -79.513  -5.149  1.00 29.45           C  
ANISOU 4822  C   TYR A 680     3982   3779   3430    -52     78   -542       C  
ATOM   4823  O   TYR A 680     -36.803 -79.815  -6.176  1.00 31.27           O  
ANISOU 4823  O   TYR A 680     4210   4044   3629    -34    104   -613       O  
ATOM   4824  CB  TYR A 680     -39.168 -77.880  -5.798  1.00 32.66           C  
ANISOU 4824  CB  TYR A 680     4349   4320   3743   -142     42   -474       C  
ATOM   4825  CG  TYR A 680     -40.621 -77.489  -5.906  1.00 37.02           C  
ANISOU 4825  CG  TYR A 680     4890   4905   4272   -203     10   -443       C  
ATOM   4826  CD1 TYR A 680     -41.442 -78.114  -6.853  1.00 38.92           C  
ANISOU 4826  CD1 TYR A 680     5144   5170   4475   -255     -6   -503       C  
ATOM   4827  CD2 TYR A 680     -41.182 -76.502  -5.073  1.00 36.81           C  
ANISOU 4827  CD2 TYR A 680     4836   4888   4261   -211     -5   -360       C  
ATOM   4828  CE1 TYR A 680     -42.775 -77.817  -6.955  1.00 39.89           C  
ANISOU 4828  CE1 TYR A 680     5249   5326   4582   -312    -39   -474       C  
ATOM   4829  CE2 TYR A 680     -42.544 -76.199  -5.183  1.00 40.39           C  
ANISOU 4829  CE2 TYR A 680     5272   5372   4702   -262    -33   -334       C  
ATOM   4830  CZ  TYR A 680     -43.312 -76.876  -6.148  1.00 42.16           C  
ANISOU 4830  CZ  TYR A 680     5506   5623   4892   -312    -51   -390       C  
ATOM   4831  OH  TYR A 680     -44.629 -76.678  -6.339  1.00 47.10           O  
ANISOU 4831  OH  TYR A 680     6108   6284   5506   -365    -82   -369       O  
ATOM   4832  N   LEU A 681     -36.790 -79.245  -4.004  1.00 26.95           N  
ANISOU 4832  N   LEU A 681     3656   3423   3161    -12     76   -481       N  
ATOM   4833  CA  LEU A 681     -35.345 -79.296  -3.873  1.00 28.98           C  
ANISOU 4833  CA  LEU A 681     3894   3672   3444     56     99   -488       C  
ATOM   4834  C   LEU A 681     -34.876 -80.506  -3.070  1.00 30.13           C  
ANISOU 4834  C   LEU A 681     4071   3705   3672     97     96   -500       C  
ATOM   4835  O   LEU A 681     -33.725 -80.544  -2.641  1.00 30.21           O  
ANISOU 4835  O   LEU A 681     4062   3699   3719    157    106   -485       O  
ATOM   4836  CB  LEU A 681     -34.828 -77.993  -3.240  1.00 28.19           C  
ANISOU 4836  CB  LEU A 681     3753   3624   3335     71     95   -407       C  
ATOM   4837  CG  LEU A 681     -35.188 -76.740  -4.096  1.00 28.89           C  
ANISOU 4837  CG  LEU A 681     3808   3818   3350     35     98   -387       C  
ATOM   4838  CD1 LEU A 681     -34.709 -75.439  -3.450  1.00 26.55           C  
ANISOU 4838  CD1 LEU A 681     3474   3557   3056     45     92   -311       C  
ATOM   4839  CD2 LEU A 681     -34.566 -76.801  -5.484  1.00 28.58           C  
ANISOU 4839  CD2 LEU A 681     3751   3848   3260     45    131   -448       C  
ATOM   4840  N   SER A 682     -35.737 -81.503  -2.867  1.00 29.03           N  
ANISOU 4840  N   SER A 682     3978   3486   3567     65     81   -523       N  
ATOM   4841  CA  SER A 682     -35.323 -82.687  -2.121  1.00 30.20           C  
ANISOU 4841  CA  SER A 682     4159   3516   3800    103     75   -526       C  
ATOM   4842  C   SER A 682     -34.177 -83.431  -2.819  1.00 31.58           C  
ANISOU 4842  C   SER A 682     4330   3662   4009    170    106   -605       C  
ATOM   4843  O   SER A 682     -34.034 -83.403  -4.047  1.00 31.22           O  
ANISOU 4843  O   SER A 682     4273   3672   3915    168    135   -686       O  
ATOM   4844  CB  SER A 682     -36.522 -83.610  -1.957  1.00 34.39           C  
ANISOU 4844  CB  SER A 682     4739   3969   4360     45     55   -540       C  
ATOM   4845  OG  SER A 682     -36.926 -84.070  -3.257  1.00 36.84           O  
ANISOU 4845  OG  SER A 682     5064   4294   4641     16     69   -640       O  
ATOM   4846  N   SER A 683     -33.318 -84.078  -2.018  1.00 32.50           N  
ANISOU 4846  N   SER A 683     4449   3695   4204    232    101   -580       N  
ATOM   4847  CA  SER A 683     -32.120 -84.707  -2.581  1.00 31.26           C  
ANISOU 4847  CA  SER A 683     4275   3511   4090    309    133   -650       C  
ATOM   4848  C   SER A 683     -32.374 -86.102  -3.133  1.00 33.94           C  
ANISOU 4848  C   SER A 683     4663   3746   4486    314    145   -745       C  
ATOM   4849  O   SER A 683     -31.498 -86.628  -3.822  1.00 35.58           O  
ANISOU 4849  O   SER A 683     4858   3939   4722    375    181   -827       O  
ATOM   4850  CB  SER A 683     -30.994 -84.815  -1.523  1.00 30.34           C  
ANISOU 4850  CB  SER A 683     4132   3353   4044    383    120   -582       C  
ATOM   4851  OG  SER A 683     -31.473 -85.516  -0.377  1.00 30.88           O  
ANISOU 4851  OG  SER A 683     4243   3314   4175    372     80   -517       O  
ATOM   4852  N   SER A 684     -33.499 -86.730  -2.821  1.00 34.48           N  
ANISOU 4852  N   SER A 684     4785   3738   4577    255    118   -739       N  
ATOM   4853  CA  SER A 684     -33.854 -88.035  -3.382  1.00 35.18           C  
ANISOU 4853  CA  SER A 684     4924   3720   4721    245    126   -835       C  
ATOM   4854  C   SER A 684     -35.357 -88.212  -3.227  1.00 36.17           C  
ANISOU 4854  C   SER A 684     5091   3822   4829    146     95   -818       C  
ATOM   4855  O   SER A 684     -35.978 -87.514  -2.411  1.00 34.51           O  
ANISOU 4855  O   SER A 684     4872   3650   4590    104     68   -719       O  
ATOM   4856  CB  SER A 684     -33.114 -89.179  -2.667  1.00 35.04           C  
ANISOU 4856  CB  SER A 684     4928   3555   4830    318    120   -823       C  
ATOM   4857  OG  SER A 684     -33.694 -89.355  -1.382  1.00 35.91           O  
ANISOU 4857  OG  SER A 684     5065   3597   4982    286     76   -710       O  
ATOM   4858  N   PRO A 685     -35.983 -89.107  -4.018  1.00 36.50           N  
ANISOU 4858  N   PRO A 685     5175   3806   4885    104    100   -918       N  
ATOM   4859  CA  PRO A 685     -37.409 -89.407  -3.767  1.00 38.56           C  
ANISOU 4859  CA  PRO A 685     5472   4031   5147      7     67   -896       C  
ATOM   4860  C   PRO A 685     -37.699 -89.793  -2.321  1.00 38.28           C  
ANISOU 4860  C   PRO A 685     5460   3898   5188     -2     35   -781       C  
ATOM   4861  O   PRO A 685     -38.746 -89.404  -1.801  1.00 41.32           O  
ANISOU 4861  O   PRO A 685     5845   4314   5543    -75     12   -713       O  
ATOM   4862  CB  PRO A 685     -37.723 -90.580  -4.740  1.00 39.04           C  
ANISOU 4862  CB  PRO A 685     5581   4011   5243    -20     77  -1033       C  
ATOM   4863  CG  PRO A 685     -36.672 -90.541  -5.746  1.00 38.95           C  
ANISOU 4863  CG  PRO A 685     5550   4048   5204     48    120  -1135       C  
ATOM   4864  CD  PRO A 685     -35.436 -89.887  -5.151  1.00 37.24           C  
ANISOU 4864  CD  PRO A 685     5284   3868   4996    140    137  -1060       C  
ATOM   4865  N   GLU A 686     -36.822 -90.552  -1.656  1.00 37.12           N  
ANISOU 4865  N   GLU A 686     5329   3638   5138     69     35   -755       N  
ATOM   4866  CA  GLU A 686     -37.062 -90.914  -0.260  1.00 36.70           C  
ANISOU 4866  CA  GLU A 686     5297   3500   5147     59      3   -634       C  
ATOM   4867  C   GLU A 686     -37.001 -89.690   0.649  1.00 35.45           C  
ANISOU 4867  C   GLU A 686     5097   3450   4923     60     -9   -518       C  
ATOM   4868  O   GLU A 686     -37.874 -89.491   1.497  1.00 37.96           O  
ANISOU 4868  O   GLU A 686     5424   3773   5225     -1    -31   -434       O  
ATOM   4869  CB  GLU A 686     -36.037 -91.960   0.202  1.00 39.29           C  
ANISOU 4869  CB  GLU A 686     5647   3688   5594    144      0   -625       C  
ATOM   4870  N   ALA A 687     -35.952 -88.881   0.522  1.00 32.79           N  
ANISOU 4870  N   ALA A 687     4712   3196   4549    128      6   -516       N  
ATOM   4871  CA  ALA A 687     -35.848 -87.643   1.300  1.00 32.94           C  
ANISOU 4871  CA  ALA A 687     4691   3319   4504    127     -5   -421       C  
ATOM   4872  C   ALA A 687     -37.017 -86.699   1.062  1.00 31.27           C  
ANISOU 4872  C   ALA A 687     4467   3210   4205     45     -6   -413       C  
ATOM   4873  O   ALA A 687     -37.305 -85.827   1.900  1.00 30.51           O  
ANISOU 4873  O   ALA A 687     4351   3174   4067     25    -18   -330       O  
ATOM   4874  CB  ALA A 687     -34.562 -86.895   0.947  1.00 32.20           C  
ANISOU 4874  CB  ALA A 687     4545   3305   4384    203     15   -438       C  
ATOM   4875  N   LYS A 688     -37.700 -86.830  -0.063  1.00 32.63           N  
ANISOU 4875  N   LYS A 688     4647   3405   4347     -1      6   -499       N  
ATOM   4876  CA  LYS A 688     -38.752 -85.848  -0.333  1.00 31.53           C  
ANISOU 4876  CA  LYS A 688     4484   3371   4126    -70      2   -484       C  
ATOM   4877  C   LYS A 688     -39.898 -85.988   0.655  1.00 30.69           C  
ANISOU 4877  C   LYS A 688     4394   3233   4032   -137    -20   -409       C  
ATOM   4878  O   LYS A 688     -40.603 -84.999   0.933  1.00 29.02           O  
ANISOU 4878  O   LYS A 688     4153   3108   3766   -175    -24   -361       O  
ATOM   4879  CB  LYS A 688     -39.240 -85.978  -1.785  1.00 34.61           C  
ANISOU 4879  CB  LYS A 688     4876   3801   4473   -108     12   -590       C  
ATOM   4880  CG  LYS A 688     -40.113 -84.768  -2.245  1.00 36.86           C  
ANISOU 4880  CG  LYS A 688     5121   4216   4667   -162      6   -572       C  
ATOM   4881  CD  LYS A 688     -40.913 -85.087  -3.499  1.00 39.11           C  
ANISOU 4881  CD  LYS A 688     5415   4533   4912   -222      2   -661       C  
ATOM   4882  CE  LYS A 688     -40.011 -85.358  -4.697  1.00 41.02           C  
ANISOU 4882  CE  LYS A 688     5660   4796   5129   -180     29   -765       C  
ATOM   4883  NZ  LYS A 688     -39.348 -84.065  -5.062  1.00 41.12           N  
ANISOU 4883  NZ  LYS A 688     5623   4931   5070   -143     45   -736       N  
ATOM   4884  N   TYR A 689     -40.112 -87.203   1.209  1.00 31.89           N  
ANISOU 4884  N   TYR A 689     4592   3261   4262   -152    -33   -394       N  
ATOM   4885  CA  TYR A 689     -41.184 -87.372   2.195  1.00 32.50           C  
ANISOU 4885  CA  TYR A 689     4683   3313   4351   -221    -49   -314       C  
ATOM   4886  C   TYR A 689     -40.987 -86.515   3.453  1.00 30.49           C  
ANISOU 4886  C   TYR A 689     4406   3113   4066   -203    -52   -208       C  
ATOM   4887  O   TYR A 689     -41.979 -86.177   4.106  1.00 30.38           O  
ANISOU 4887  O   TYR A 689     4383   3133   4025   -262    -55   -151       O  
ATOM   4888  CB  TYR A 689     -41.335 -88.846   2.604  1.00 35.67           C  
ANISOU 4888  CB  TYR A 689     5141   3566   4848   -240    -61   -306       C  
ATOM   4889  CG  TYR A 689     -41.940 -89.696   1.498  1.00 40.16           C  
ANISOU 4889  CG  TYR A 689     5735   4078   5444   -290    -61   -410       C  
ATOM   4890  CD1 TYR A 689     -43.317 -89.777   1.334  1.00 43.50           C  
ANISOU 4890  CD1 TYR A 689     6157   4520   5850   -389    -71   -414       C  
ATOM   4891  CD2 TYR A 689     -41.143 -90.388   0.610  1.00 40.84           C  
ANISOU 4891  CD2 TYR A 689     5843   4101   5573   -239    -51   -510       C  
ATOM   4892  CE1 TYR A 689     -43.887 -90.545   0.313  1.00 44.54           C  
ANISOU 4892  CE1 TYR A 689     6313   4607   6004   -443    -77   -515       C  
ATOM   4893  CE2 TYR A 689     -41.703 -91.148  -0.432  1.00 43.51           C  
ANISOU 4893  CE2 TYR A 689     6209   4394   5930   -290    -51   -619       C  
ATOM   4894  CZ  TYR A 689     -43.076 -91.211  -0.567  1.00 46.45           C  
ANISOU 4894  CZ  TYR A 689     6582   4785   6281   -394    -67   -619       C  
ATOM   4895  OH  TYR A 689     -43.642 -91.956  -1.585  1.00 51.94           O  
ANISOU 4895  OH  TYR A 689     7303   5440   6992   -452    -73   -730       O  
ATOM   4896  N   ASP A 690     -39.749 -86.152   3.797  1.00 28.85           N  
ANISOU 4896  N   ASP A 690     4185   2919   3859   -125    -51   -185       N  
ATOM   4897  CA  ASP A 690     -39.504 -85.269   4.953  1.00 27.03           C  
ANISOU 4897  CA  ASP A 690     3932   2749   3590   -111    -58    -95       C  
ATOM   4898  C   ASP A 690     -40.115 -83.901   4.740  1.00 24.27           C  
ANISOU 4898  C   ASP A 690     3540   2521   3162   -141    -46    -97       C  
ATOM   4899  O   ASP A 690     -40.479 -83.216   5.718  1.00 23.42           O  
ANISOU 4899  O   ASP A 690     3419   2460   3020   -160    -47    -31       O  
ATOM   4900  CB  ASP A 690     -38.008 -85.024   5.175  1.00 29.89           C  
ANISOU 4900  CB  ASP A 690     4277   3117   3963    -24    -62    -83       C  
ATOM   4901  CG  ASP A 690     -37.228 -86.278   5.532  1.00 34.98           C  
ANISOU 4901  CG  ASP A 690     4954   3643   4694     25    -77    -66       C  
ATOM   4902  OD1 ASP A 690     -37.903 -87.225   5.965  1.00 34.76           O  
ANISOU 4902  OD1 ASP A 690     4968   3528   4710    -17    -89    -35       O  
ATOM   4903  OD2 ASP A 690     -35.934 -86.282   5.409  1.00 36.45           O  
ANISOU 4903  OD2 ASP A 690     5119   3823   4905    104    -79    -78       O  
ATOM   4904  N   ALA A 691     -40.171 -83.461   3.476  1.00 23.73           N  
ANISOU 4904  N   ALA A 691     3448   2504   3064   -141    -34   -172       N  
ATOM   4905  CA  ALA A 691     -40.671 -82.114   3.150  1.00 22.76           C  
ANISOU 4905  CA  ALA A 691     3281   2492   2874   -161    -26   -170       C  
ATOM   4906  C   ALA A 691     -42.162 -82.010   3.408  1.00 24.66           C  
ANISOU 4906  C   ALA A 691     3517   2753   3100   -236    -28   -147       C  
ATOM   4907  O   ALA A 691     -42.653 -80.904   3.660  1.00 24.84           O  
ANISOU 4907  O   ALA A 691     3504   2853   3081   -250    -23   -117       O  
ATOM   4908  CB  ALA A 691     -40.360 -81.777   1.644  1.00 22.12           C  
ANISOU 4908  CB  ALA A 691     3180   2464   2763   -146    -16   -250       C  
ATOM   4909  N   PHE A 692     -42.888 -83.141   3.409  1.00 23.93           N  
ANISOU 4909  N   PHE A 692     3457   2588   3048   -285    -35   -157       N  
ATOM   4910  CA  PHE A 692     -44.327 -83.146   3.697  1.00 25.87           C  
ANISOU 4910  CA  PHE A 692     3692   2852   3286   -363    -36   -131       C  
ATOM   4911  C   PHE A 692     -44.658 -83.331   5.182  1.00 26.14           C  
ANISOU 4911  C   PHE A 692     3739   2861   3333   -384    -32    -45       C  
ATOM   4912  O   PHE A 692     -45.826 -83.542   5.522  1.00 25.30           O  
ANISOU 4912  O   PHE A 692     3625   2759   3230   -451    -28    -19       O  
ATOM   4913  CB  PHE A 692     -45.012 -84.245   2.876  1.00 28.67           C  
ANISOU 4913  CB  PHE A 692     4070   3149   3676   -418    -46   -189       C  
ATOM   4914  CG  PHE A 692     -44.875 -84.005   1.394  1.00 30.49           C  
ANISOU 4914  CG  PHE A 692     4284   3425   3874   -410    -50   -277       C  
ATOM   4915  CD1 PHE A 692     -45.527 -82.945   0.807  1.00 33.21           C  
ANISOU 4915  CD1 PHE A 692     4581   3877   4162   -431    -52   -282       C  
ATOM   4916  CD2 PHE A 692     -44.030 -84.780   0.619  1.00 33.11           C  
ANISOU 4916  CD2 PHE A 692     4648   3699   4231   -376    -49   -350       C  
ATOM   4917  CE1 PHE A 692     -45.400 -82.689  -0.597  1.00 34.79           C  
ANISOU 4917  CE1 PHE A 692     4765   4132   4320   -428    -58   -354       C  
ATOM   4918  CE2 PHE A 692     -43.875 -84.513  -0.754  1.00 34.84           C  
ANISOU 4918  CE2 PHE A 692     4853   3977   4406   -371    -48   -432       C  
ATOM   4919  CZ  PHE A 692     -44.591 -83.488  -1.358  1.00 33.75           C  
ANISOU 4919  CZ  PHE A 692     4669   3952   4202   -402    -54   -430       C  
ATOM   4920  N   LEU A 693     -43.683 -83.216   6.075  1.00 25.91           N  
ANISOU 4920  N   LEU A 693     3723   2817   3305   -332    -33      2       N  
ATOM   4921  CA  LEU A 693     -44.005 -83.336   7.494  1.00 25.96           C  
ANISOU 4921  CA  LEU A 693     3742   2815   3306   -357    -30     87       C  
ATOM   4922  C   LEU A 693     -44.888 -82.172   7.938  1.00 25.80           C  
ANISOU 4922  C   LEU A 693     3677   2894   3230   -387    -10    109       C  
ATOM   4923  O   LEU A 693     -44.678 -81.018   7.534  1.00 25.94           O  
ANISOU 4923  O   LEU A 693     3659   2985   3212   -356     -4     82       O  
ATOM   4924  CB  LEU A 693     -42.732 -83.357   8.345  1.00 26.09           C  
ANISOU 4924  CB  LEU A 693     3778   2811   3326   -295    -42    133       C  
ATOM   4925  CG  LEU A 693     -42.014 -84.727   8.315  1.00 26.15           C  
ANISOU 4925  CG  LEU A 693     3831   2699   3404   -269    -61    139       C  
ATOM   4926  CD1 LEU A 693     -40.512 -84.663   8.794  1.00 23.74           C  
ANISOU 4926  CD1 LEU A 693     3531   2382   3109   -187    -79    167       C  
ATOM   4927  CD2 LEU A 693     -42.791 -85.757   9.089  1.00 26.09           C  
ANISOU 4927  CD2 LEU A 693     3860   2621   3431   -330    -66    202       C  
ATOM   4928  N   VAL A 694     -45.835 -82.465   8.830  1.00 24.83           N  
ANISOU 4928  N   VAL A 694     3557   2773   3104   -446      3    162       N  
ATOM   4929  CA  VAL A 694     -46.675 -81.405   9.389  1.00 25.60           C  
ANISOU 4929  CA  VAL A 694     3611   2964   3154   -469     29    182       C  
ATOM   4930  C   VAL A 694     -45.839 -80.318  10.100  1.00 25.32           C  
ANISOU 4930  C   VAL A 694     3566   2984   3072   -414     34    199       C  
ATOM   4931  O   VAL A 694     -46.295 -79.181  10.229  1.00 26.92           O  
ANISOU 4931  O   VAL A 694     3727   3261   3239   -412     54    188       O  
ATOM   4932  CB  VAL A 694     -47.716 -82.058  10.342  1.00 26.57           C  
ANISOU 4932  CB  VAL A 694     3740   3076   3279   -542     46    243       C  
ATOM   4933  CG1 VAL A 694     -47.073 -82.504  11.694  1.00 25.18           C  
ANISOU 4933  CG1 VAL A 694     3607   2873   3088   -532     44    319       C  
ATOM   4934  CG2 VAL A 694     -48.862 -81.136  10.593  1.00 28.68           C  
ANISOU 4934  CG2 VAL A 694     3952   3435   3512   -575     78    243       C  
ATOM   4935  N   THR A 695     -44.612 -80.628  10.528  1.00 23.22           N  
ANISOU 4935  N   THR A 695     3333   2679   2809   -367     15    221       N  
ATOM   4936  CA  THR A 695     -43.747 -79.643  11.209  1.00 23.14           C  
ANISOU 4936  CA  THR A 695     3313   2721   2756   -321     13    234       C  
ATOM   4937  C   THR A 695     -42.983 -78.718  10.250  1.00 22.85           C  
ANISOU 4937  C   THR A 695     3249   2715   2718   -268      6    177       C  
ATOM   4938  O   THR A 695     -42.269 -77.798  10.709  1.00 22.30           O  
ANISOU 4938  O   THR A 695     3167   2689   2619   -234      4    180       O  
ATOM   4939  CB  THR A 695     -42.757 -80.381  12.089  1.00 23.89           C  
ANISOU 4939  CB  THR A 695     3449   2771   2857   -296    -11    289       C  
ATOM   4940  OG1 THR A 695     -42.255 -81.525  11.368  1.00 24.86           O  
ANISOU 4940  OG1 THR A 695     3600   2802   3043   -278    -33    277       O  
ATOM   4941  CG2 THR A 695     -43.437 -80.859  13.411  1.00 23.81           C  
ANISOU 4941  CG2 THR A 695     3462   2768   2818   -349      0    364       C  
ATOM   4942  N   ASN A 696     -43.102 -78.944   8.942  1.00 22.33           N  
ANISOU 4942  N   ASN A 696     3174   2629   2682   -266      2    126       N  
ATOM   4943  CA  ASN A 696     -42.558 -78.100   7.892  1.00 21.61           C  
ANISOU 4943  CA  ASN A 696     3053   2573   2583   -228      0     77       C  
ATOM   4944  C   ASN A 696     -43.632 -77.210   7.240  1.00 24.14           C  
ANISOU 4944  C   ASN A 696     3331   2953   2887   -256     14     53       C  
ATOM   4945  O   ASN A 696     -43.313 -76.389   6.396  1.00 25.15           O  
ANISOU 4945  O   ASN A 696     3432   3119   3006   -231     13     23       O  
ATOM   4946  CB  ASN A 696     -41.894 -79.012   6.815  1.00 21.13           C  
ANISOU 4946  CB  ASN A 696     3011   2457   2559   -204    -14     35       C  
ATOM   4947  CG  ASN A 696     -41.130 -78.229   5.736  1.00 22.03           C  
ANISOU 4947  CG  ASN A 696     3096   2613   2660   -163    -14    -11       C  
ATOM   4948  OD1 ASN A 696     -40.438 -77.212   6.010  1.00 21.32           O  
ANISOU 4948  OD1 ASN A 696     2984   2568   2549   -131    -13      1       O  
ATOM   4949  ND2 ASN A 696     -41.194 -78.738   4.494  1.00 21.97           N  
ANISOU 4949  ND2 ASN A 696     3092   2592   2665   -167    -14    -64       N  
ATOM   4950  N   MET A 697     -44.886 -77.344   7.623  1.00 24.86           N  
ANISOU 4950  N   MET A 697     3412   3057   2977   -306     28     70       N  
ATOM   4951  CA  MET A 697     -46.000 -76.682   6.960  1.00 25.49           C  
ANISOU 4951  CA  MET A 697     3446   3188   3052   -333     37     51       C  
ATOM   4952  C   MET A 697     -46.323 -75.335   7.616  1.00 23.84           C  
ANISOU 4952  C   MET A 697     3200   3039   2820   -320     58     65       C  
ATOM   4953  O   MET A 697     -46.145 -75.139   8.832  1.00 22.67           O  
ANISOU 4953  O   MET A 697     3064   2896   2653   -316     73     93       O  
ATOM   4954  CB  MET A 697     -47.208 -77.641   7.025  1.00 31.00           C  
ANISOU 4954  CB  MET A 697     4145   3864   3769   -399     41     60       C  
ATOM   4955  CG  MET A 697     -48.575 -77.200   6.542  1.00 35.50           C  
ANISOU 4955  CG  MET A 697     4662   4486   4340   -439     48     52       C  
ATOM   4956  SD  MET A 697     -49.854 -78.570   6.879  1.00 39.97           S  
ANISOU 4956  SD  MET A 697     5234   5016   4935   -528     53     73       S  
ATOM   4957  CE  MET A 697     -49.579 -78.604   8.542  1.00 30.03           C  
ANISOU 4957  CE  MET A 697     4002   3750   3658   -523     81    130       C  
ATOM   4958  N   VAL A 698     -46.817 -74.402   6.807  1.00 22.28           N  
ANISOU 4958  N   VAL A 698     2957   2885   2623   -314     58     46       N  
ATOM   4959  CA  VAL A 698     -47.151 -73.069   7.310  1.00 21.21           C  
ANISOU 4959  CA  VAL A 698     2784   2796   2481   -296     78     53       C  
ATOM   4960  C   VAL A 698     -48.386 -72.566   6.593  1.00 22.48           C  
ANISOU 4960  C   VAL A 698     2888   2996   2657   -315     80     48       C  
ATOM   4961  O   VAL A 698     -48.641 -72.925   5.433  1.00 23.01           O  
ANISOU 4961  O   VAL A 698     2944   3067   2730   -331     57     34       O  
ATOM   4962  CB  VAL A 698     -45.983 -72.065   7.102  1.00 21.42           C  
ANISOU 4962  CB  VAL A 698     2810   2829   2500   -245     69     43       C  
ATOM   4963  CG1 VAL A 698     -44.825 -72.320   8.132  1.00 23.71           C  
ANISOU 4963  CG1 VAL A 698     3142   3094   2772   -224     68     53       C  
ATOM   4964  CG2 VAL A 698     -45.471 -72.095   5.656  1.00 20.38           C  
ANISOU 4964  CG2 VAL A 698     2673   2697   2373   -231     44     23       C  
ATOM   4965  N   PRO A 699     -49.173 -71.713   7.251  1.00 20.42           N  
ANISOU 4965  N   PRO A 699     2588   2770   2402   -313    107     56       N  
ATOM   4966  CA  PRO A 699     -50.408 -71.224   6.588  1.00 23.24           C  
ANISOU 4966  CA  PRO A 699     2881   3166   2783   -327    107     57       C  
ATOM   4967  C   PRO A 699     -50.067 -70.205   5.505  1.00 24.07           C  
ANISOU 4967  C   PRO A 699     2959   3287   2898   -289     83     53       C  
ATOM   4968  O   PRO A 699     -49.324 -69.247   5.761  1.00 23.41           O  
ANISOU 4968  O   PRO A 699     2881   3197   2816   -248     88     51       O  
ATOM   4969  CB  PRO A 699     -51.221 -70.569   7.732  1.00 23.64           C  
ANISOU 4969  CB  PRO A 699     2896   3245   2840   -325    151     63       C  
ATOM   4970  CG  PRO A 699     -50.354 -70.617   8.970  1.00 25.77           C  
ANISOU 4970  CG  PRO A 699     3217   3496   3080   -312    172     62       C  
ATOM   4971  CD  PRO A 699     -49.013 -71.224   8.639  1.00 22.09           C  
ANISOU 4971  CD  PRO A 699     2809   2988   2597   -300    140     62       C  
ATOM   4972  N   MET A 700     -50.665 -70.373   4.317  1.00 21.60           N  
ANISOU 4972  N   MET A 700     2615   2999   2592   -309     54     54       N  
ATOM   4973  CA  MET A 700     -50.479 -69.413   3.229  1.00 19.27           C  
ANISOU 4973  CA  MET A 700     2290   2728   2302   -280     28     63       C  
ATOM   4974  C   MET A 700     -51.757 -69.247   2.421  1.00 22.61           C  
ANISOU 4974  C   MET A 700     2649   3199   2743   -302      7     79       C  
ATOM   4975  O   MET A 700     -52.415 -70.238   2.065  1.00 21.29           O  
ANISOU 4975  O   MET A 700     2477   3044   2567   -351     -8     70       O  
ATOM   4976  CB  MET A 700     -49.358 -69.865   2.246  1.00 19.69           C  
ANISOU 4976  CB  MET A 700     2386   2772   2323   -276      1     49       C  
ATOM   4977  CG  MET A 700     -47.995 -69.871   2.883  1.00 24.16           C  
ANISOU 4977  CG  MET A 700     3002   3299   2878   -246     15     39       C  
ATOM   4978  SD  MET A 700     -46.708 -70.231   1.685  1.00 24.35           S  
ANISOU 4978  SD  MET A 700     3059   3323   2871   -234     -8     20       S  
ATOM   4979  CE  MET A 700     -45.270 -69.793   2.703  1.00 25.13           C  
ANISOU 4979  CE  MET A 700     3190   3385   2973   -191     10     22       C  
ATOM   4980  N   TYR A 701     -52.093 -68.002   2.131  1.00 23.21           N  
ANISOU 4980  N   TYR A 701     2675   3298   2847   -268      2    104       N  
ATOM   4981  CA  TYR A 701     -53.140 -67.723   1.163  1.00 23.36           C  
ANISOU 4981  CA  TYR A 701     2629   3367   2881   -281    -31    129       C  
ATOM   4982  C   TYR A 701     -52.761 -68.275  -0.213  1.00 22.26           C  
ANISOU 4982  C   TYR A 701     2509   3254   2695   -307    -77    126       C  
ATOM   4983  O   TYR A 701     -51.607 -68.144  -0.647  1.00 22.91           O  
ANISOU 4983  O   TYR A 701     2634   3322   2748   -288    -83    120       O  
ATOM   4984  CB  TYR A 701     -53.384 -66.221   1.049  1.00 21.98           C  
ANISOU 4984  CB  TYR A 701     2402   3200   2751   -229    -33    164       C  
ATOM   4985  CG  TYR A 701     -53.912 -65.559   2.288  1.00 23.18           C  
ANISOU 4985  CG  TYR A 701     2523   3332   2952   -199     14    158       C  
ATOM   4986  CD1 TYR A 701     -55.232 -65.809   2.744  1.00 24.75           C  
ANISOU 4986  CD1 TYR A 701     2664   3561   3180   -218     32    159       C  
ATOM   4987  CD2 TYR A 701     -53.095 -64.699   3.027  1.00 21.35           C  
ANISOU 4987  CD2 TYR A 701     2319   3056   2736   -156     42    147       C  
ATOM   4988  CE1 TYR A 701     -55.752 -65.156   3.862  1.00 25.57           C  
ANISOU 4988  CE1 TYR A 701     2734   3655   3327   -188     83    147       C  
ATOM   4989  CE2 TYR A 701     -53.560 -64.073   4.150  1.00 23.48           C  
ANISOU 4989  CE2 TYR A 701     2565   3312   3045   -129     88    130       C  
ATOM   4990  CZ  TYR A 701     -54.894 -64.310   4.573  1.00 30.39           C  
ANISOU 4990  CZ  TYR A 701     3380   4221   3947   -143    111    128       C  
ATOM   4991  OH  TYR A 701     -55.356 -63.677   5.703  1.00 36.28           O  
ANISOU 4991  OH  TYR A 701     4099   4958   4727   -114    165    103       O  
ATOM   4992  N   PRO A 702     -53.728 -68.856  -0.942  1.00 24.63           N  
ANISOU 4992  N   PRO A 702     2773   3599   2986   -353   -109    127       N  
ATOM   4993  CA  PRO A 702     -53.503 -69.206  -2.370  1.00 22.44           C  
ANISOU 4993  CA  PRO A 702     2504   3363   2657   -379   -157    122       C  
ATOM   4994  C   PRO A 702     -52.813 -68.113  -3.190  1.00 24.99           C  
ANISOU 4994  C   PRO A 702     2821   3709   2963   -339   -176    158       C  
ATOM   4995  O   PRO A 702     -51.924 -68.438  -3.966  1.00 24.52           O  
ANISOU 4995  O   PRO A 702     2805   3661   2852   -346   -188    140       O  
ATOM   4996  CB  PRO A 702     -54.936 -69.451  -2.887  1.00 24.47           C  
ANISOU 4996  CB  PRO A 702     2694   3679   2925   -424   -192    136       C  
ATOM   4997  CG  PRO A 702     -55.691 -69.984  -1.641  1.00 25.06           C  
ANISOU 4997  CG  PRO A 702     2754   3723   3043   -446   -154    123       C  
ATOM   4998  CD  PRO A 702     -55.098 -69.174  -0.477  1.00 23.15           C  
ANISOU 4998  CD  PRO A 702     2530   3434   2833   -386   -103    133       C  
ATOM   4999  N   ALA A 703     -53.201 -66.831  -3.067  1.00 24.19           N  
ANISOU 4999  N   ALA A 703     2668   3616   2909   -297   -178    210       N  
ATOM   5000  CA  ALA A 703     -52.520 -65.796  -3.865  1.00 25.15           C  
ANISOU 5000  CA  ALA A 703     2785   3752   3018   -264   -198    255       C  
ATOM   5001  C   ALA A 703     -51.047 -65.719  -3.500  1.00 24.01           C  
ANISOU 5001  C   ALA A 703     2706   3560   2857   -240   -167    232       C  
ATOM   5002  O   ALA A 703     -50.183 -65.530  -4.369  1.00 24.34           O  
ANISOU 5002  O   ALA A 703     2770   3624   2855   -238   -181    244       O  
ATOM   5003  CB  ALA A 703     -53.174 -64.425  -3.655  1.00 25.57           C  
ANISOU 5003  CB  ALA A 703     2773   3801   3142   -218   -202    314       C  
ATOM   5004  N   PHE A 704     -50.732 -65.933  -2.217  1.00 23.43           N  
ANISOU 5004  N   PHE A 704     2662   3427   2812   -225   -124    198       N  
ATOM   5005  CA  PHE A 704     -49.346 -65.861  -1.795  1.00 22.26           C  
ANISOU 5005  CA  PHE A 704     2569   3237   2652   -203    -98    179       C  
ATOM   5006  C   PHE A 704     -48.576 -67.090  -2.233  1.00 20.58           C  
ANISOU 5006  C   PHE A 704     2409   3028   2381   -230   -100    135       C  
ATOM   5007  O   PHE A 704     -47.381 -66.990  -2.503  1.00 18.65           O  
ANISOU 5007  O   PHE A 704     2196   2776   2113   -215    -94    129       O  
ATOM   5008  CB  PHE A 704     -49.212 -65.732  -0.249  1.00 19.61           C  
ANISOU 5008  CB  PHE A 704     2251   2845   2356   -182    -56    156       C  
ATOM   5009  CG  PHE A 704     -47.774 -65.532   0.187  1.00 22.14           C  
ANISOU 5009  CG  PHE A 704     2619   3128   2667   -159    -38    142       C  
ATOM   5010  CD1 PHE A 704     -47.173 -64.282   0.029  1.00 24.16           C  
ANISOU 5010  CD1 PHE A 704     2862   3371   2946   -128    -40    171       C  
ATOM   5011  CD2 PHE A 704     -47.022 -66.568   0.705  1.00 23.25           C  
ANISOU 5011  CD2 PHE A 704     2811   3244   2779   -170    -24    104       C  
ATOM   5012  CE1 PHE A 704     -45.806 -64.082   0.393  1.00 24.22           C  
ANISOU 5012  CE1 PHE A 704     2908   3350   2947   -113    -27    159       C  
ATOM   5013  CE2 PHE A 704     -45.691 -66.378   1.044  1.00 24.71           C  
ANISOU 5013  CE2 PHE A 704     3030   3403   2957   -148    -13     94       C  
ATOM   5014  CZ  PHE A 704     -45.093 -65.112   0.921  1.00 24.39           C  
ANISOU 5014  CZ  PHE A 704     2974   3356   2938   -122    -14    120       C  
ATOM   5015  N   LYS A 705     -49.211 -68.262  -2.229  1.00 20.43           N  
ANISOU 5015  N   LYS A 705     2399   3014   2348   -270   -106    101       N  
ATOM   5016  CA  LYS A 705     -48.474 -69.437  -2.715  1.00 21.50           C  
ANISOU 5016  CA  LYS A 705     2587   3145   2438   -292   -107     53       C  
ATOM   5017  C   LYS A 705     -47.978 -69.258  -4.143  1.00 21.19           C  
ANISOU 5017  C   LYS A 705     2546   3162   2344   -297   -132     55       C  
ATOM   5018  O   LYS A 705     -46.993 -69.895  -4.518  1.00 24.19           O  
ANISOU 5018  O   LYS A 705     2968   3535   2688   -295   -122     16       O  
ATOM   5019  CB  LYS A 705     -49.344 -70.703  -2.651  1.00 20.44           C  
ANISOU 5019  CB  LYS A 705     2461   3005   2302   -342   -115     17       C  
ATOM   5020  CG  LYS A 705     -49.767 -70.978  -1.177  1.00 19.85           C  
ANISOU 5020  CG  LYS A 705     2391   2879   2273   -342    -85     18       C  
ATOM   5021  CD  LYS A 705     -50.730 -72.191  -1.086  1.00 23.42           C  
ANISOU 5021  CD  LYS A 705     2845   3323   2731   -401    -93     -7       C  
ATOM   5022  CE  LYS A 705     -50.181 -73.447  -1.762  1.00 31.14           C  
ANISOU 5022  CE  LYS A 705     3875   4278   3678   -429   -105    -60       C  
ATOM   5023  NZ  LYS A 705     -51.271 -74.475  -1.505  1.00 35.36           N  
ANISOU 5023  NZ  LYS A 705     4404   4797   4234   -492   -112    -75       N  
ATOM   5024  N   ARG A 706     -48.655 -68.453  -4.970  1.00 23.36           N  
ANISOU 5024  N   ARG A 706     2772   3496   2608   -303   -163    102       N  
ATOM   5025  CA  ARG A 706     -48.080 -68.182  -6.302  1.00 22.46           C  
ANISOU 5025  CA  ARG A 706     2659   3445   2432   -308   -184    114       C  
ATOM   5026  C   ARG A 706     -46.687 -67.584  -6.181  1.00 22.59           C  
ANISOU 5026  C   ARG A 706     2698   3439   2446   -270   -156    126       C  
ATOM   5027  O   ARG A 706     -45.764 -67.979  -6.918  1.00 23.83           O  
ANISOU 5027  O   ARG A 706     2882   3623   2548   -275   -148     98       O  
ATOM   5028  CB  ARG A 706     -48.977 -67.239  -7.119  1.00 23.38           C  
ANISOU 5028  CB  ARG A 706     2715   3627   2542   -316   -226    183       C  
ATOM   5029  CG  ARG A 706     -50.383 -67.814  -7.419  1.00 24.79           C  
ANISOU 5029  CG  ARG A 706     2858   3845   2716   -360   -263    175       C  
ATOM   5030  CD  ARG A 706     -51.230 -66.921  -8.333  1.00 24.84           C  
ANISOU 5030  CD  ARG A 706     2799   3926   2711   -366   -314    249       C  
ATOM   5031  NE  ARG A 706     -50.592 -66.682  -9.647  1.00 27.61           N  
ANISOU 5031  NE  ARG A 706     3161   4351   2980   -379   -338    271       N  
ATOM   5032  CZ  ARG A 706     -50.918 -65.662 -10.447  1.00 28.10           C  
ANISOU 5032  CZ  ARG A 706     3177   4473   3029   -372   -378    356       C  
ATOM   5033  NH1 ARG A 706     -51.859 -64.778 -10.092  1.00 25.95           N  
ANISOU 5033  NH1 ARG A 706     2843   4189   2830   -347   -399    424       N  
ATOM   5034  NH2 ARG A 706     -50.306 -65.508 -11.594  1.00 30.76           N  
ANISOU 5034  NH2 ARG A 706     3526   4880   3280   -389   -394    377       N  
ATOM   5035  N   VAL A 707     -46.517 -66.611  -5.279  1.00 21.02           N  
ANISOU 5035  N   VAL A 707     2486   3194   2307   -234   -140    164       N  
ATOM   5036  CA  VAL A 707     -45.213 -65.973  -5.081  1.00 21.52           C  
ANISOU 5036  CA  VAL A 707     2566   3234   2377   -204   -116    177       C  
ATOM   5037  C   VAL A 707     -44.221 -66.973  -4.504  1.00 22.36           C  
ANISOU 5037  C   VAL A 707     2721   3300   2473   -197    -87    115       C  
ATOM   5038  O   VAL A 707     -43.091 -67.125  -5.004  1.00 24.20           O  
ANISOU 5038  O   VAL A 707     2972   3551   2674   -189    -74    100       O  
ATOM   5039  CB  VAL A 707     -45.358 -64.751  -4.143  1.00 22.42           C  
ANISOU 5039  CB  VAL A 707     2657   3299   2563   -172   -107    219       C  
ATOM   5040  CG1 VAL A 707     -44.011 -64.100  -3.788  1.00 22.26           C  
ANISOU 5040  CG1 VAL A 707     2653   3246   2558   -148    -86    227       C  
ATOM   5041  CG2 VAL A 707     -46.360 -63.708  -4.704  1.00 20.07           C  
ANISOU 5041  CG2 VAL A 707     2305   3029   2291   -170   -138    286       C  
ATOM   5042  N   TRP A 708     -44.629 -67.640  -3.427  1.00 21.35           N  
ANISOU 5042  N   TRP A 708     2612   3123   2379   -198    -75     84       N  
ATOM   5043  CA  TRP A 708     -43.737 -68.507  -2.659  1.00 22.30           C  
ANISOU 5043  CA  TRP A 708     2776   3195   2504   -185    -51     40       C  
ATOM   5044  C   TRP A 708     -43.270 -69.707  -3.495  1.00 22.03           C  
ANISOU 5044  C   TRP A 708     2771   3176   2425   -199    -51    -12       C  
ATOM   5045  O   TRP A 708     -42.102 -70.093  -3.429  1.00 22.68           O  
ANISOU 5045  O   TRP A 708     2876   3240   2500   -177    -33    -38       O  
ATOM   5046  CB  TRP A 708     -44.473 -68.992  -1.400  1.00 21.83           C  
ANISOU 5046  CB  TRP A 708     2726   3086   2481   -191    -42     28       C  
ATOM   5047  CG  TRP A 708     -43.589 -69.714  -0.385  1.00 23.73           C  
ANISOU 5047  CG  TRP A 708     3009   3273   2733   -175    -23      2       C  
ATOM   5048  CD1 TRP A 708     -43.668 -71.057  -0.015  1.00 24.19           C  
ANISOU 5048  CD1 TRP A 708     3103   3295   2793   -190    -19    -31       C  
ATOM   5049  CD2 TRP A 708     -42.546 -69.138   0.406  1.00 21.93           C  
ANISOU 5049  CD2 TRP A 708     2789   3021   2522   -143    -10     13       C  
ATOM   5050  NE1 TRP A 708     -42.682 -71.336   0.931  1.00 23.02           N  
ANISOU 5050  NE1 TRP A 708     2983   3104   2658   -164     -6    -35       N  
ATOM   5051  CE2 TRP A 708     -41.983 -70.174   1.192  1.00 23.42           C  
ANISOU 5051  CE2 TRP A 708     3017   3167   2716   -136     -1    -11       C  
ATOM   5052  CE3 TRP A 708     -41.995 -67.835   0.497  1.00 24.87           C  
ANISOU 5052  CE3 TRP A 708     3140   3402   2909   -122     -7     42       C  
ATOM   5053  CZ2 TRP A 708     -40.909 -69.945   2.096  1.00 22.10           C  
ANISOU 5053  CZ2 TRP A 708     2863   2976   2560   -109      6     -6       C  
ATOM   5054  CZ3 TRP A 708     -40.950 -67.604   1.413  1.00 22.94           C  
ANISOU 5054  CZ3 TRP A 708     2909   3128   2678    -99      2     39       C  
ATOM   5055  CH2 TRP A 708     -40.415 -68.651   2.185  1.00 24.35           C  
ANISOU 5055  CH2 TRP A 708     3122   3275   2853    -93      7     16       C  
ATOM   5056  N   THR A 709     -44.177 -70.315  -4.249  1.00 21.25           N  
ANISOU 5056  N   THR A 709     2668   3109   2298   -236    -71    -33       N  
ATOM   5057  CA  THR A 709     -43.796 -71.418  -5.146  1.00 23.81           C  
ANISOU 5057  CA  THR A 709     3021   3450   2577   -253    -71    -94       C  
ATOM   5058  C   THR A 709     -42.780 -70.996  -6.198  1.00 24.56           C  
ANISOU 5058  C   THR A 709     3111   3602   2620   -238    -62    -95       C  
ATOM   5059  O   THR A 709     -41.832 -71.738  -6.467  1.00 24.37           O  
ANISOU 5059  O   THR A 709     3114   3569   2578   -224    -40   -147       O  
ATOM   5060  CB  THR A 709     -45.026 -71.996  -5.826  1.00 28.17           C  
ANISOU 5060  CB  THR A 709     3565   4035   3104   -303   -100   -115       C  
ATOM   5061  OG1 THR A 709     -45.811 -72.626  -4.822  1.00 32.43           O  
ANISOU 5061  OG1 THR A 709     4114   4516   3692   -320   -100   -123       O  
ATOM   5062  CG2 THR A 709     -44.680 -73.062  -6.891  1.00 31.18           C  
ANISOU 5062  CG2 THR A 709     3976   4440   3430   -326   -101   -190       C  
ATOM   5063  N   TYR A 710     -42.965 -69.818  -6.822  1.00 22.52           N  
ANISOU 5063  N   TYR A 710     2815   3404   2339   -242    -77    -35       N  
ATOM   5064  CA  TYR A 710     -42.004 -69.368  -7.824  1.00 21.82           C  
ANISOU 5064  CA  TYR A 710     2717   3377   2196   -235    -65    -25       C  
ATOM   5065  C   TYR A 710     -40.642 -69.135  -7.176  1.00 23.84           C  
ANISOU 5065  C   TYR A 710     2982   3593   2484   -194    -31    -25       C  
ATOM   5066  O   TYR A 710     -39.598 -69.521  -7.718  1.00 28.00           O  
ANISOU 5066  O   TYR A 710     3517   4145   2976   -182     -6    -60       O  
ATOM   5067  CB  TYR A 710     -42.528 -68.084  -8.488  1.00 21.48           C  
ANISOU 5067  CB  TYR A 710     2632   3395   2135   -248    -92     57       C  
ATOM   5068  CG  TYR A 710     -41.706 -67.634  -9.662  1.00 24.65           C  
ANISOU 5068  CG  TYR A 710     3022   3876   2467   -254    -84     79       C  
ATOM   5069  CD1 TYR A 710     -40.771 -66.639  -9.514  1.00 26.23           C  
ANISOU 5069  CD1 TYR A 710     3207   4072   2689   -231    -65    131       C  
ATOM   5070  CD2 TYR A 710     -41.852 -68.217 -10.920  1.00 23.82           C  
ANISOU 5070  CD2 TYR A 710     2923   3855   2272   -287    -92     43       C  
ATOM   5071  CE1 TYR A 710     -39.987 -66.217 -10.595  1.00 24.65           C  
ANISOU 5071  CE1 TYR A 710     2993   3951   2423   -242    -52    158       C  
ATOM   5072  CE2 TYR A 710     -41.072 -67.800 -11.966  1.00 24.44           C  
ANISOU 5072  CE2 TYR A 710     2992   4016   2280   -295    -78     65       C  
ATOM   5073  CZ  TYR A 710     -40.145 -66.790 -11.786  1.00 25.54           C  
ANISOU 5073  CZ  TYR A 710     3111   4149   2443   -272    -57    127       C  
ATOM   5074  OH  TYR A 710     -39.328 -66.353 -12.840  1.00 27.65           O  
ANISOU 5074  OH  TYR A 710     3364   4505   2637   -285    -38    156       O  
ATOM   5075  N   PHE A 711     -40.633 -68.517  -6.001  1.00 21.66           N  
ANISOU 5075  N   PHE A 711     2700   3259   2273   -173    -30     11       N  
ATOM   5076  CA  PHE A 711     -39.395 -68.391  -5.244  1.00 20.70           C  
ANISOU 5076  CA  PHE A 711     2584   3097   2182   -139     -5      7       C  
ATOM   5077  C   PHE A 711     -38.743 -69.769  -5.027  1.00 23.18           C  
ANISOU 5077  C   PHE A 711     2933   3378   2495   -123     14    -63       C  
ATOM   5078  O   PHE A 711     -37.585 -69.968  -5.351  1.00 22.80           O  
ANISOU 5078  O   PHE A 711     2883   3345   2434   -102     37    -85       O  
ATOM   5079  CB  PHE A 711     -39.689 -67.727  -3.883  1.00 18.90           C  
ANISOU 5079  CB  PHE A 711     2353   2809   2019   -126    -10     39       C  
ATOM   5080  CG  PHE A 711     -38.545 -67.783  -2.940  1.00 20.92           C  
ANISOU 5080  CG  PHE A 711     2620   3023   2306    -97      7     28       C  
ATOM   5081  CD1 PHE A 711     -37.344 -67.178  -3.268  1.00 22.61           C  
ANISOU 5081  CD1 PHE A 711     2815   3261   2515    -84     20     45       C  
ATOM   5082  CD2 PHE A 711     -38.651 -68.437  -1.701  1.00 22.90           C  
ANISOU 5082  CD2 PHE A 711     2897   3214   2589    -86      8      6       C  
ATOM   5083  CE1 PHE A 711     -36.228 -67.267  -2.387  1.00 20.88           C  
ANISOU 5083  CE1 PHE A 711     2600   3008   2326    -59     30     35       C  
ATOM   5084  CE2 PHE A 711     -37.549 -68.513  -0.798  1.00 24.48           C  
ANISOU 5084  CE2 PHE A 711     3105   3382   2814    -60     16      1       C  
ATOM   5085  CZ  PHE A 711     -36.352 -67.938  -1.145  1.00 23.07           C  
ANISOU 5085  CZ  PHE A 711     2905   3229   2633    -46     25     13       C  
ATOM   5086  N   GLN A 712     -39.506 -70.746  -4.504  1.00 21.57           N  
ANISOU 5086  N   GLN A 712     2758   3128   2311   -133      5    -97       N  
ATOM   5087  CA  GLN A 712     -38.905 -72.032  -4.116  1.00 19.84           C  
ANISOU 5087  CA  GLN A 712     2572   2855   2109   -114     20   -154       C  
ATOM   5088  C   GLN A 712     -38.476 -72.876  -5.305  1.00 23.70           C  
ANISOU 5088  C   GLN A 712     3073   3377   2554   -115     34   -218       C  
ATOM   5089  O   GLN A 712     -37.413 -73.530  -5.263  1.00 25.02           O  
ANISOU 5089  O   GLN A 712     3252   3520   2734    -80     57   -258       O  
ATOM   5090  CB  GLN A 712     -39.923 -72.792  -3.276  1.00 19.86           C  
ANISOU 5090  CB  GLN A 712     2601   2798   2145   -133      6   -163       C  
ATOM   5091  CG  GLN A 712     -39.970 -72.146  -1.863  1.00 19.83           C  
ANISOU 5091  CG  GLN A 712     2592   2756   2185   -120      4   -114       C  
ATOM   5092  CD  GLN A 712     -40.728 -73.009  -0.870  1.00 24.16           C  
ANISOU 5092  CD  GLN A 712     3168   3245   2765   -136     -1   -119       C  
ATOM   5093  OE1 GLN A 712     -41.671 -73.655  -1.244  1.00 24.00           O  
ANISOU 5093  OE1 GLN A 712     3158   3223   2739   -170    -11   -140       O  
ATOM   5094  NE2 GLN A 712     -40.267 -73.042   0.395  1.00 26.42           N  
ANISOU 5094  NE2 GLN A 712     3469   3488   3082   -114      3    -98       N  
ATOM   5095  N   ARG A 713     -39.303 -72.906  -6.367  1.00 18.54           N  
ANISOU 5095  N   ARG A 713     2415   2780   1848   -155     20   -233       N  
ATOM   5096  CA  ARG A 713     -39.103 -73.803  -7.493  1.00 21.95           C  
ANISOU 5096  CA  ARG A 713     2865   3246   2229   -166     32   -309       C  
ATOM   5097  C   ARG A 713     -38.150 -73.204  -8.520  1.00 25.72           C  
ANISOU 5097  C   ARG A 713     3317   3809   2647   -154     57   -307       C  
ATOM   5098  O   ARG A 713     -37.429 -73.954  -9.184  1.00 26.74           O  
ANISOU 5098  O   ARG A 713     3458   3955   2747   -139     86   -377       O  
ATOM   5099  CB  ARG A 713     -40.468 -74.125  -8.176  1.00 25.48           C  
ANISOU 5099  CB  ARG A 713     3317   3726   2638   -222      1   -328       C  
ATOM   5100  CG  ARG A 713     -40.368 -75.045  -9.421  1.00 31.76           C  
ANISOU 5100  CG  ARG A 713     4134   4565   3369   -244      9   -419       C  
ATOM   5101  CD  ARG A 713     -41.724 -75.302 -10.101  1.00 36.17           C  
ANISOU 5101  CD  ARG A 713     4693   5165   3884   -308    -30   -437       C  
ATOM   5102  NE  ARG A 713     -42.070 -74.178 -10.978  1.00 36.44           N  
ANISOU 5102  NE  ARG A 713     4687   5309   3848   -332    -52   -376       N  
ATOM   5103  CZ  ARG A 713     -41.553 -74.016 -12.199  1.00 38.69           C  
ANISOU 5103  CZ  ARG A 713     4967   5690   4045   -341    -39   -400       C  
ATOM   5104  NH1 ARG A 713     -40.679 -74.909 -12.691  1.00 38.67           N  
ANISOU 5104  NH1 ARG A 713     4992   5686   4013   -325     -1   -494       N  
ATOM   5105  NH2 ARG A 713     -41.903 -72.950 -12.928  1.00 37.09           N  
ANISOU 5105  NH2 ARG A 713     4727   5584   3782   -364    -64   -327       N  
ATOM   5106  N   VAL A 714     -38.139 -71.871  -8.680  1.00 23.12           N  
ANISOU 5106  N   VAL A 714     2950   3533   2300   -160     48   -227       N  
ATOM   5107  CA  VAL A 714     -37.368 -71.219  -9.729  1.00 21.37           C  
ANISOU 5107  CA  VAL A 714     2701   3402   2015   -162     70   -210       C  
ATOM   5108  C   VAL A 714     -36.205 -70.421  -9.146  1.00 22.57           C  
ANISOU 5108  C   VAL A 714     2827   3540   2207   -127     92   -162       C  
ATOM   5109  O   VAL A 714     -35.063 -70.551  -9.604  1.00 23.35           O  
ANISOU 5109  O   VAL A 714     2912   3676   2283   -106    129   -188       O  
ATOM   5110  CB  VAL A 714     -38.268 -70.320 -10.608  1.00 21.98           C  
ANISOU 5110  CB  VAL A 714     2756   3562   2034   -206     38   -149       C  
ATOM   5111  CG1 VAL A 714     -37.503 -69.693 -11.784  1.00 23.33           C  
ANISOU 5111  CG1 VAL A 714     2901   3837   2126   -216     60   -123       C  
ATOM   5112  CG2 VAL A 714     -39.509 -71.132 -11.138  1.00 22.33           C  
ANISOU 5112  CG2 VAL A 714     2821   3624   2040   -248      7   -197       C  
ATOM   5113  N   LEU A 715     -36.483 -69.546  -8.182  1.00 20.12           N  
ANISOU 5113  N   LEU A 715     2505   3185   1955   -123     71    -95       N  
ATOM   5114  CA  LEU A 715     -35.461 -68.535  -7.858  1.00 22.05           C  
ANISOU 5114  CA  LEU A 715     2718   3434   2226   -106     86    -42       C  
ATOM   5115  C   LEU A 715     -34.334 -69.089  -6.974  1.00 21.54           C  
ANISOU 5115  C   LEU A 715     2657   3315   2211    -63    108    -77       C  
ATOM   5116  O   LEU A 715     -33.177 -68.719  -7.159  1.00 24.03           O  
ANISOU 5116  O   LEU A 715     2943   3662   2526    -48    133    -66       O  
ATOM   5117  CB  LEU A 715     -36.139 -67.324  -7.196  1.00 19.70           C  
ANISOU 5117  CB  LEU A 715     2407   3106   1974   -117     56     35       C  
ATOM   5118  CG  LEU A 715     -37.093 -66.531  -8.145  1.00 21.60           C  
ANISOU 5118  CG  LEU A 715     2629   3405   2172   -153     31     92       C  
ATOM   5119  CD1 LEU A 715     -37.729 -65.288  -7.313  1.00 19.55           C  
ANISOU 5119  CD1 LEU A 715     2353   3095   1981   -153      5    164       C  
ATOM   5120  CD2 LEU A 715     -36.391 -66.072  -9.454  1.00 21.92           C  
ANISOU 5120  CD2 LEU A 715     2646   3541   2143   -171     49    121       C  
ATOM   5121  N   VAL A 716     -34.638 -69.962  -6.014  1.00 19.98           N  
ANISOU 5121  N   VAL A 716     2491   3041   2058    -45     98   -113       N  
ATOM   5122  CA  VAL A 716     -33.591 -70.520  -5.153  1.00 22.11           C  
ANISOU 5122  CA  VAL A 716     2763   3262   2377     -3    111   -137       C  
ATOM   5123  C   VAL A 716     -32.511 -71.196  -5.997  1.00 23.38           C  
ANISOU 5123  C   VAL A 716     2909   3462   2512     24    149   -190       C  
ATOM   5124  O   VAL A 716     -31.317 -70.967  -5.806  1.00 23.93           O  
ANISOU 5124  O   VAL A 716     2947   3543   2602     52    168   -182       O  
ATOM   5125  CB  VAL A 716     -34.184 -71.504  -4.131  1.00 21.25           C  
ANISOU 5125  CB  VAL A 716     2694   3068   2310      7     93   -163       C  
ATOM   5126  CG1 VAL A 716     -33.050 -72.273  -3.435  1.00 22.48           C  
ANISOU 5126  CG1 VAL A 716     2852   3179   2511     55    104   -188       C  
ATOM   5127  CG2 VAL A 716     -34.938 -70.704  -3.069  1.00 19.76           C  
ANISOU 5127  CG2 VAL A 716     2509   2847   2153    -10     66   -108       C  
ATOM   5128  N   LYS A 717     -32.927 -72.003  -6.975  1.00 23.49           N  
ANISOU 5128  N   LYS A 717     2943   3503   2478     13    161   -250       N  
ATOM   5129  CA  LYS A 717     -31.965 -72.702  -7.826  1.00 25.85           C  
ANISOU 5129  CA  LYS A 717     3231   3842   2750     40    205   -316       C  
ATOM   5130  C   LYS A 717     -31.184 -71.719  -8.692  1.00 26.47           C  
ANISOU 5130  C   LYS A 717     3261   4021   2777     29    233   -281       C  
ATOM   5131  O   LYS A 717     -29.985 -71.906  -8.950  1.00 26.21           O  
ANISOU 5131  O   LYS A 717     3195   4017   2746     63    273   -307       O  
ATOM   5132  CB  LYS A 717     -32.719 -73.709  -8.710  1.00 29.43           C  
ANISOU 5132  CB  LYS A 717     3722   4305   3156     21    209   -395       C  
ATOM   5133  CG  LYS A 717     -31.877 -74.332  -9.834  1.00 35.34           C  
ANISOU 5133  CG  LYS A 717     4459   5114   3856     41    260   -476       C  
ATOM   5134  CD  LYS A 717     -30.587 -74.915  -9.235  1.00 43.15           C  
ANISOU 5134  CD  LYS A 717     5429   6053   4914    109    290   -506       C  
ATOM   5135  CE  LYS A 717     -29.673 -75.476 -10.367  1.00 49.57           C  
ANISOU 5135  CE  LYS A 717     6220   6932   5681    137    350   -591       C  
ATOM   5136  NZ  LYS A 717     -28.448 -75.986  -9.716  1.00 50.97           N  
ANISOU 5136  NZ  LYS A 717     6369   7058   5939    208    375   -611       N  
ATOM   5137  N   LYS A 718     -31.857 -70.680  -9.178  1.00 27.16           N  
ANISOU 5137  N   LYS A 718     3338   4161   2819    -17    214   -218       N  
ATOM   5138  CA  LYS A 718     -31.164 -69.669  -9.956  1.00 27.62           C  
ANISOU 5138  CA  LYS A 718     3351   4310   2832    -35    238   -167       C  
ATOM   5139  C   LYS A 718     -30.073 -69.002  -9.118  1.00 26.56           C  
ANISOU 5139  C   LYS A 718     3178   4150   2762    -12    245   -121       C  
ATOM   5140  O   LYS A 718     -28.968 -68.754  -9.607  1.00 26.64           O  
ANISOU 5140  O   LYS A 718     3145   4221   2755     -5    284   -117       O  
ATOM   5141  CB  LYS A 718     -32.161 -68.611 -10.437  1.00 28.38           C  
ANISOU 5141  CB  LYS A 718     3447   4448   2889    -87    206    -90       C  
ATOM   5142  CG  LYS A 718     -31.452 -67.619 -11.363  1.00 31.18           C  
ANISOU 5142  CG  LYS A 718     3757   4900   3191   -112    231    -30       C  
ATOM   5143  CD  LYS A 718     -32.428 -66.599 -11.923  1.00 35.76           C  
ANISOU 5143  CD  LYS A 718     4334   5519   3732   -159    195     54       C  
ATOM   5144  CE  LYS A 718     -32.772 -65.607 -10.819  1.00 39.46           C  
ANISOU 5144  CE  LYS A 718     4798   5905   4291   -158    158    127       C  
ATOM   5145  NZ  LYS A 718     -33.530 -64.516 -11.483  1.00 41.83           N  
ANISOU 5145  NZ  LYS A 718     5085   6247   4561   -198    129    219       N  
ATOM   5146  N   TYR A 719     -30.418 -68.597  -7.890  1.00 22.42           N  
ANISOU 5146  N   TYR A 719     2666   3547   2307     -9    208    -82       N  
ATOM   5147  CA  TYR A 719     -29.423 -67.967  -7.014  1.00 25.60           C  
ANISOU 5147  CA  TYR A 719     3034   3923   2769      7    207    -44       C  
ATOM   5148  C   TYR A 719     -28.262 -68.938  -6.723  1.00 24.47           C  
ANISOU 5148  C   TYR A 719     2873   3768   2656     59    234   -101       C  
ATOM   5149  O   TYR A 719     -27.083 -68.561  -6.700  1.00 25.71           O  
ANISOU 5149  O   TYR A 719     2980   3958   2832     70    255    -84       O  
ATOM   5150  CB  TYR A 719     -30.096 -67.544  -5.690  1.00 25.15           C  
ANISOU 5150  CB  TYR A 719     3001   3783   2772      3    163    -10       C  
ATOM   5151  CG  TYR A 719     -31.219 -66.567  -5.841  1.00 29.03           C  
ANISOU 5151  CG  TYR A 719     3503   4274   3253    -37    136     44       C  
ATOM   5152  CD1 TYR A 719     -31.309 -65.755  -6.972  1.00 32.37           C  
ANISOU 5152  CD1 TYR A 719     3904   4768   3629    -70    145     91       C  
ATOM   5153  CD2 TYR A 719     -32.228 -66.452  -4.834  1.00 30.24           C  
ANISOU 5153  CD2 TYR A 719     3686   4357   3445    -40    103     54       C  
ATOM   5154  CE1 TYR A 719     -32.366 -64.846  -7.131  1.00 34.22           C  
ANISOU 5154  CE1 TYR A 719     4143   4997   3861   -101    116    149       C  
ATOM   5155  CE2 TYR A 719     -33.271 -65.539  -4.983  1.00 33.63           C  
ANISOU 5155  CE2 TYR A 719     4118   4786   3874    -69     80    103       C  
ATOM   5156  CZ  TYR A 719     -33.338 -64.742  -6.139  1.00 37.14           C  
ANISOU 5156  CZ  TYR A 719     4538   5294   4279    -97     85    152       C  
ATOM   5157  OH  TYR A 719     -34.377 -63.825  -6.313  1.00 42.25           O  
ANISOU 5157  OH  TYR A 719     5183   5936   4935   -120     58    208       O  
ATOM   5158  N   ALA A 720     -28.592 -70.200  -6.491  1.00 24.08           N  
ANISOU 5158  N   ALA A 720     2861   3669   2620     90    233   -166       N  
ATOM   5159  CA  ALA A 720     -27.543 -71.195  -6.287  1.00 23.84           C  
ANISOU 5159  CA  ALA A 720     2813   3619   2625    146    258   -220       C  
ATOM   5160  C   ALA A 720     -26.601 -71.264  -7.484  1.00 25.78           C  
ANISOU 5160  C   ALA A 720     3013   3957   2826    157    314   -253       C  
ATOM   5161  O   ALA A 720     -25.377 -71.389  -7.311  1.00 27.17           O  
ANISOU 5161  O   ALA A 720     3139   4148   3037    196    339   -261       O  
ATOM   5162  CB  ALA A 720     -28.162 -72.573  -6.009  1.00 22.75           C  
ANISOU 5162  CB  ALA A 720     2729   3406   2508    173    248   -285       C  
ATOM   5163  N   SER A 721     -27.151 -71.231  -8.716  1.00 25.76           N  
ANISOU 5163  N   SER A 721     3024   4023   2742    124    337   -276       N  
ATOM   5164  CA  SER A 721     -26.276 -71.366  -9.862  1.00 29.55           C  
ANISOU 5164  CA  SER A 721     3462   4598   3167    133    397   -315       C  
ATOM   5165  C   SER A 721     -25.461 -70.098 -10.068  1.00 28.51           C  
ANISOU 5165  C   SER A 721     3267   4541   3024    106    413   -236       C  
ATOM   5166  O   SER A 721     -24.321 -70.176 -10.492  1.00 28.75           O  
ANISOU 5166  O   SER A 721     3242   4631   3049    129    462   -255       O  
ATOM   5167  CB  SER A 721     -27.063 -71.738 -11.138  1.00 36.80           C  
ANISOU 5167  CB  SER A 721     4414   5581   3989    101    416   -366       C  
ATOM   5168  OG  SER A 721     -27.941 -70.689 -11.489  1.00 44.69           O  
ANISOU 5168  OG  SER A 721     5423   6621   4937     39    385   -289       O  
ATOM   5169  N   GLU A 722     -25.990 -68.951  -9.718  1.00 28.16           N  
ANISOU 5169  N   GLU A 722     3228   4487   2987     60    373   -149       N  
ATOM   5170  CA  GLU A 722     -25.271 -67.691  -9.921  1.00 28.42           C  
ANISOU 5170  CA  GLU A 722     3204   4578   3016     25    385    -68       C  
ATOM   5171  C   GLU A 722     -24.264 -67.387  -8.805  1.00 30.00           C  
ANISOU 5171  C   GLU A 722     3361   4733   3304     49    373    -43       C  
ATOM   5172  O   GLU A 722     -23.276 -66.690  -9.046  1.00 31.44           O  
ANISOU 5172  O   GLU A 722     3482   4974   3491     33    398     -2       O  
ATOM   5173  CB  GLU A 722     -26.291 -66.546 -10.030  1.00 29.47           C  
ANISOU 5173  CB  GLU A 722     3360   4708   3129    -33    345     15       C  
ATOM   5174  CG  GLU A 722     -27.152 -66.666 -11.327  1.00 34.14           C  
ANISOU 5174  CG  GLU A 722     3978   5374   3620    -66    355      8       C  
ATOM   5175  CD  GLU A 722     -28.273 -65.614 -11.526  1.00 38.17           C  
ANISOU 5175  CD  GLU A 722     4508   5882   4111   -117    310     94       C  
ATOM   5176  OE1 GLU A 722     -28.568 -64.852 -10.578  1.00 39.94           O  
ANISOU 5176  OE1 GLU A 722     4737   6031   4407   -123    270    148       O  
ATOM   5177  OE2 GLU A 722     -28.877 -65.590 -12.646  1.00 39.57           O  
ANISOU 5177  OE2 GLU A 722     4697   6137   4200   -149    314    103       O  
ATOM   5178  N   ARG A 723     -24.490 -67.869  -7.580  1.00 24.15           N  
ANISOU 5178  N   ARG A 723     2649   3896   2629     82    332    -61       N  
ATOM   5179  CA  ARG A 723     -23.666 -67.503  -6.445  1.00 23.47           C  
ANISOU 5179  CA  ARG A 723     2528   3770   2618     95    308    -31       C  
ATOM   5180  C   ARG A 723     -22.784 -68.645  -5.999  1.00 27.78           C  
ANISOU 5180  C   ARG A 723     3051   4295   3209    163    321    -89       C  
ATOM   5181  O   ARG A 723     -22.067 -68.496  -4.985  1.00 27.27           O  
ANISOU 5181  O   ARG A 723     2955   4200   3207    180    294    -67       O  
ATOM   5182  CB  ARG A 723     -24.575 -67.047  -5.267  1.00 20.95           C  
ANISOU 5182  CB  ARG A 723     2258   3364   2339     77    247      3       C  
ATOM   5183  CG  ARG A 723     -25.214 -65.712  -5.619  1.00 22.63           C  
ANISOU 5183  CG  ARG A 723     2476   3593   2530     16    234     71       C  
ATOM   5184  CD  ARG A 723     -26.400 -65.284  -4.709  1.00 26.86           C  
ANISOU 5184  CD  ARG A 723     3065   4049   3093     -2    184     93       C  
ATOM   5185  NE  ARG A 723     -25.997 -65.202  -3.310  1.00 29.38           N  
ANISOU 5185  NE  ARG A 723     3382   4309   3473     13    151     94       N  
ATOM   5186  CZ  ARG A 723     -26.735 -64.587  -2.374  1.00 27.77           C  
ANISOU 5186  CZ  ARG A 723     3210   4044   3298     -6    113    115       C  
ATOM   5187  NH1 ARG A 723     -27.934 -64.004  -2.726  1.00 24.24           N  
ANISOU 5187  NH1 ARG A 723     2793   3583   2832    -35    105    140       N  
ATOM   5188  NH2 ARG A 723     -26.266 -64.531  -1.117  1.00 24.34           N  
ANISOU 5188  NH2 ARG A 723     2772   3570   2908      3     85    111       N  
ATOM   5189  N   ASN A 724     -22.796 -69.759  -6.756  1.00 26.70           N  
ANISOU 5189  N   ASN A 724     2926   4176   3043    201    361   -163       N  
ATOM   5190  CA  ASN A 724     -22.066 -70.987  -6.436  1.00 26.26           C  
ANISOU 5190  CA  ASN A 724     2853   4087   3037    275    376   -225       C  
ATOM   5191  C   ASN A 724     -22.573 -71.585  -5.116  1.00 27.68           C  
ANISOU 5191  C   ASN A 724     3083   4155   3278    301    319   -223       C  
ATOM   5192  O   ASN A 724     -21.839 -71.697  -4.150  1.00 28.88           O  
ANISOU 5192  O   ASN A 724     3205   4275   3493    333    293   -203       O  
ATOM   5193  CB  ASN A 724     -20.565 -70.723  -6.379  1.00 25.89           C  
ANISOU 5193  CB  ASN A 724     2714   4095   3028    300    403   -210       C  
ATOM   5194  CG  ASN A 724     -19.720 -72.003  -6.387  1.00 29.99           C  
ANISOU 5194  CG  ASN A 724     3201   4599   3594    385    434   -282       C  
ATOM   5195  OD1 ASN A 724     -20.240 -73.124  -6.413  1.00 29.29           O  
ANISOU 5195  OD1 ASN A 724     3166   4449   3516    425    435   -345       O  
ATOM   5196  ND2 ASN A 724     -18.421 -71.827  -6.305  1.00 29.69           N  
ANISOU 5196  ND2 ASN A 724     3075   4611   3596    412    456   -269       N  
ATOM   5197  N   GLY A 725     -23.843 -71.970  -5.107  1.00 28.42           N  
ANISOU 5197  N   GLY A 725     3252   4199   3348    283    298   -241       N  
ATOM   5198  CA  GLY A 725     -24.552 -72.478  -3.925  1.00 25.96           C  
ANISOU 5198  CA  GLY A 725     2996   3789   3081    293    247   -232       C  
ATOM   5199  C   GLY A 725     -25.068 -71.349  -3.048  1.00 26.42           C  
ANISOU 5199  C   GLY A 725     3066   3830   3141    244    201   -160       C  
ATOM   5200  O   GLY A 725     -24.533 -70.245  -3.018  1.00 26.52           O  
ANISOU 5200  O   GLY A 725     3035   3889   3152    217    199   -114       O  
ATOM   5201  N   VAL A 726     -26.159 -71.624  -2.319  1.00 23.13           N  
ANISOU 5201  N   VAL A 726     2711   3347   2732    231    165   -153       N  
ATOM   5202  CA  VAL A 726     -26.652 -70.672  -1.338  1.00 24.27           C  
ANISOU 5202  CA  VAL A 726     2868   3468   2884    193    124    -98       C  
ATOM   5203  C   VAL A 726     -27.142 -71.435  -0.108  1.00 26.69           C  
ANISOU 5203  C   VAL A 726     3221   3697   3224    210     88    -96       C  
ATOM   5204  O   VAL A 726     -27.610 -72.578  -0.199  1.00 28.96           O  
ANISOU 5204  O   VAL A 726     3547   3939   3517    232     91   -132       O  
ATOM   5205  CB  VAL A 726     -27.796 -69.764  -1.876  1.00 21.85           C  
ANISOU 5205  CB  VAL A 726     2585   3183   2535    138    123    -75       C  
ATOM   5206  CG1 VAL A 726     -27.279 -68.838  -3.023  1.00 22.10           C  
ANISOU 5206  CG1 VAL A 726     2569   3295   2531    113    154    -55       C  
ATOM   5207  CG2 VAL A 726     -29.052 -70.630  -2.318  1.00 21.16           C  
ANISOU 5207  CG2 VAL A 726     2553   3067   2420    131    126   -113       C  
ATOM   5208  N   ASN A 727     -27.043 -70.775   1.036  1.00 23.56           N  
ANISOU 5208  N   ASN A 727     2822   3284   2845    195     52    -54       N  
ATOM   5209  CA  ASN A 727     -27.695 -71.210   2.265  1.00 21.60           C  
ANISOU 5209  CA  ASN A 727     2621   2977   2611    194     17    -40       C  
ATOM   5210  C   ASN A 727     -28.921 -70.338   2.439  1.00 23.36           C  
ANISOU 5210  C   ASN A 727     2873   3196   2805    144     10    -23       C  
ATOM   5211  O   ASN A 727     -28.829 -69.114   2.252  1.00 22.14           O  
ANISOU 5211  O   ASN A 727     2693   3075   2643    114     12     -2       O  
ATOM   5212  CB  ASN A 727     -26.756 -71.064   3.469  1.00 21.08           C  
ANISOU 5212  CB  ASN A 727     2530   2906   2574    210    -18    -10       C  
ATOM   5213  CG  ASN A 727     -27.461 -71.406   4.776  1.00 24.75           C  
ANISOU 5213  CG  ASN A 727     3045   3323   3037    201    -53     12       C  
ATOM   5214  OD1 ASN A 727     -27.937 -70.516   5.469  1.00 24.10           O  
ANISOU 5214  OD1 ASN A 727     2975   3246   2936    162    -70     31       O  
ATOM   5215  ND2 ASN A 727     -27.590 -72.708   5.069  1.00 22.07           N  
ANISOU 5215  ND2 ASN A 727     2736   2934   2717    233    -61      7       N  
ATOM   5216  N   VAL A 728     -30.080 -70.965   2.695  1.00 20.71           N  
ANISOU 5216  N   VAL A 728     2589   2819   2462    133      5    -32       N  
ATOM   5217  CA  VAL A 728     -31.349 -70.241   2.806  1.00 21.18           C  
ANISOU 5217  CA  VAL A 728     2671   2877   2500     91      3    -19       C  
ATOM   5218  C   VAL A 728     -31.846 -70.452   4.238  1.00 21.04           C  
ANISOU 5218  C   VAL A 728     2686   2819   2488     83    -22     -1       C  
ATOM   5219  O   VAL A 728     -31.831 -71.591   4.739  1.00 22.22           O  
ANISOU 5219  O   VAL A 728     2862   2930   2649    102    -31     -4       O  
ATOM   5220  CB  VAL A 728     -32.394 -70.750   1.783  1.00 21.49           C  
ANISOU 5220  CB  VAL A 728     2733   2917   2518     76     21    -44       C  
ATOM   5221  CG1 VAL A 728     -33.759 -70.078   1.983  1.00 20.67           C  
ANISOU 5221  CG1 VAL A 728     2644   2809   2400     37     14    -27       C  
ATOM   5222  CG2 VAL A 728     -31.912 -70.570   0.285  1.00 24.34           C  
ANISOU 5222  CG2 VAL A 728     3062   3330   2854     79     47    -64       C  
ATOM   5223  N   ILE A 729     -32.264 -69.381   4.901  1.00 19.10           N  
ANISOU 5223  N   ILE A 729     2440   2581   2236     55    -31     17       N  
ATOM   5224  CA  ILE A 729     -33.034 -69.500   6.152  1.00 20.85           C  
ANISOU 5224  CA  ILE A 729     2695   2777   2449     39    -44     27       C  
ATOM   5225  C   ILE A 729     -34.380 -68.786   5.953  1.00 21.87           C  
ANISOU 5225  C   ILE A 729     2832   2910   2569      8    -29     25       C  
ATOM   5226  O   ILE A 729     -34.396 -67.600   5.596  1.00 24.41           O  
ANISOU 5226  O   ILE A 729     3129   3250   2897     -4    -24     28       O  
ATOM   5227  CB  ILE A 729     -32.273 -68.871   7.335  1.00 23.07           C  
ANISOU 5227  CB  ILE A 729     2967   3068   2729     37    -68     41       C  
ATOM   5228  CG1 ILE A 729     -30.850 -69.430   7.455  1.00 26.13           C  
ANISOU 5228  CG1 ILE A 729     3332   3463   3133     70    -88     49       C  
ATOM   5229  CG2 ILE A 729     -33.134 -69.005   8.626  1.00 20.82           C  
ANISOU 5229  CG2 ILE A 729     2721   2770   2422     17    -76     49       C  
ATOM   5230  CD1 ILE A 729     -30.019 -68.778   8.647  1.00 27.19           C  
ANISOU 5230  CD1 ILE A 729     3452   3618   3262     62   -121     64       C  
ATOM   5231  N   SER A 730     -35.496 -69.488   6.157  1.00 18.62           N  
ANISOU 5231  N   SER A 730     2450   2478   2149     -5    -23     22       N  
ATOM   5232  CA  SER A 730     -36.815 -68.936   5.884  1.00 18.80           C  
ANISOU 5232  CA  SER A 730     2469   2506   2168    -31     -9     21       C  
ATOM   5233  C   SER A 730     -37.680 -69.093   7.122  1.00 23.01           C  
ANISOU 5233  C   SER A 730     3027   3026   2691    -49     -6     27       C  
ATOM   5234  O   SER A 730     -37.478 -70.006   7.929  1.00 23.58           O  
ANISOU 5234  O   SER A 730     3126   3080   2754    -47    -14     36       O  
ATOM   5235  CB  SER A 730     -37.550 -69.673   4.711  1.00 18.41           C  
ANISOU 5235  CB  SER A 730     2423   2457   2114    -39      0      9       C  
ATOM   5236  OG  SER A 730     -36.821 -69.511   3.473  1.00 24.13           O  
ANISOU 5236  OG  SER A 730     3125   3208   2836    -26      3      0       O  
ATOM   5237  N   GLY A 731     -38.696 -68.252   7.225  1.00 20.07           N  
ANISOU 5237  N   GLY A 731     2641   2664   2321    -66      8     24       N  
ATOM   5238  CA  GLY A 731     -39.606 -68.359   8.341  1.00 18.95           C  
ANISOU 5238  CA  GLY A 731     2515   2519   2166    -84     21     25       C  
ATOM   5239  C   GLY A 731     -40.759 -67.369   8.348  1.00 20.64           C  
ANISOU 5239  C   GLY A 731     2704   2745   2393    -95     41     18       C  
ATOM   5240  O   GLY A 731     -40.825 -66.441   7.535  1.00 21.73           O  
ANISOU 5240  O   GLY A 731     2814   2889   2556    -87     41     17       O  
ATOM   5241  N   PRO A 732     -41.616 -67.490   9.356  1.00 20.07           N  
ANISOU 5241  N   PRO A 732     2642   2679   2307   -112     61     14       N  
ATOM   5242  CA  PRO A 732     -42.759 -66.593   9.510  1.00 19.31           C  
ANISOU 5242  CA  PRO A 732     2517   2594   2228   -117     86      2       C  
ATOM   5243  C   PRO A 732     -42.410 -65.347  10.319  1.00 22.49           C  
ANISOU 5243  C   PRO A 732     2914   2996   2635   -106     95    -23       C  
ATOM   5244  O   PRO A 732     -41.516 -65.355  11.158  1.00 21.18           O  
ANISOU 5244  O   PRO A 732     2773   2832   2441   -107     85    -32       O  
ATOM   5245  CB  PRO A 732     -43.768 -67.449  10.295  1.00 19.64           C  
ANISOU 5245  CB  PRO A 732     2570   2647   2246   -144    108      8       C  
ATOM   5246  CG  PRO A 732     -42.892 -68.295  11.189  1.00 21.78           C  
ANISOU 5246  CG  PRO A 732     2885   2913   2479   -150     96     20       C  
ATOM   5247  CD  PRO A 732     -41.664 -68.623  10.307  1.00 20.83           C  
ANISOU 5247  CD  PRO A 732     2773   2771   2371   -129     62     27       C  
ATOM   5248  N   ILE A 733     -43.213 -64.301  10.102  1.00 21.44           N  
ANISOU 5248  N   ILE A 733     2747   2860   2538    -96    114    -36       N  
ATOM   5249  CA  ILE A 733     -43.141 -63.085  10.885  1.00 20.49           C  
ANISOU 5249  CA  ILE A 733     2622   2731   2434    -87    130    -72       C  
ATOM   5250  C   ILE A 733     -44.560 -62.711  11.287  1.00 21.31           C  
ANISOU 5250  C   ILE A 733     2698   2845   2555    -84    169    -90       C  
ATOM   5251  O   ILE A 733     -45.484 -62.782  10.462  1.00 19.81           O  
ANISOU 5251  O   ILE A 733     2473   2658   2397    -79    173    -69       O  
ATOM   5252  CB  ILE A 733     -42.457 -61.957  10.069  1.00 19.80           C  
ANISOU 5252  CB  ILE A 733     2514   2614   2394    -69    110    -68       C  
ATOM   5253  CG1 ILE A 733     -40.933 -62.104  10.170  1.00 19.09           C  
ANISOU 5253  CG1 ILE A 733     2449   2522   2283    -74     80    -65       C  
ATOM   5254  CG2 ILE A 733     -42.920 -60.552  10.516  1.00 19.35           C  
ANISOU 5254  CG2 ILE A 733     2437   2531   2385    -54    132   -103       C  
ATOM   5255  CD1 ILE A 733     -40.216 -61.255   9.117  1.00 19.88           C  
ANISOU 5255  CD1 ILE A 733     2526   2600   2427    -65     60    -46       C  
ATOM   5256  N   PHE A 734     -44.726 -62.270  12.537  1.00 15.59           N  
ANISOU 5256  N   PHE A 734     1984   2131   1810    -87    198   -133       N  
ATOM   5257  CA  PHE A 734     -46.000 -61.758  13.045  1.00 18.14           C  
ANISOU 5257  CA  PHE A 734     2275   2465   2152    -79    245   -164       C  
ATOM   5258  C   PHE A 734     -45.792 -60.303  13.459  1.00 22.41           C  
ANISOU 5258  C   PHE A 734     2807   2973   2733    -55    259   -217       C  
ATOM   5259  O   PHE A 734     -45.202 -60.048  14.529  1.00 21.32           O  
ANISOU 5259  O   PHE A 734     2702   2844   2554    -66    267   -261       O  
ATOM   5260  CB  PHE A 734     -46.453 -62.556  14.279  1.00 21.31           C  
ANISOU 5260  CB  PHE A 734     2698   2914   2485   -107    279   -177       C  
ATOM   5261  CG  PHE A 734     -46.555 -64.022  13.987  1.00 22.22           C  
ANISOU 5261  CG  PHE A 734     2829   3047   2565   -135    263   -124       C  
ATOM   5262  CD1 PHE A 734     -47.729 -64.538  13.485  1.00 21.17           C  
ANISOU 5262  CD1 PHE A 734     2661   2929   2455   -145    280   -101       C  
ATOM   5263  CD2 PHE A 734     -45.425 -64.849  14.155  1.00 24.17           C  
ANISOU 5263  CD2 PHE A 734     3124   3292   2769   -150    227    -99       C  
ATOM   5264  CE1 PHE A 734     -47.795 -65.911  13.127  1.00 19.19           C  
ANISOU 5264  CE1 PHE A 734     2428   2683   2181   -176    261    -56       C  
ATOM   5265  CE2 PHE A 734     -45.463 -66.218  13.820  1.00 22.25           C  
ANISOU 5265  CE2 PHE A 734     2897   3049   2506   -172    210    -53       C  
ATOM   5266  CZ  PHE A 734     -46.673 -66.730  13.275  1.00 20.00           C  
ANISOU 5266  CZ  PHE A 734     2582   2772   2245   -187    228    -34       C  
ATOM   5267  N   ASP A 735     -46.437 -59.378  12.751  1.00 22.07           N  
ANISOU 5267  N   ASP A 735     2720   2897   2768    -24    267   -216       N  
ATOM   5268  CA  ASP A 735     -46.327 -57.954  13.149  1.00 20.43           C  
ANISOU 5268  CA  ASP A 735     2503   2643   2615      1    283   -271       C  
ATOM   5269  C   ASP A 735     -47.660 -57.268  12.865  1.00 21.29           C  
ANISOU 5269  C   ASP A 735     2555   2735   2800     38    316   -279       C  
ATOM   5270  O   ASP A 735     -47.769 -56.316  12.067  1.00 23.59           O  
ANISOU 5270  O   ASP A 735     2814   2973   3175     69    301   -261       O  
ATOM   5271  CB  ASP A 735     -45.148 -57.287  12.430  1.00 17.83           C  
ANISOU 5271  CB  ASP A 735     2186   2263   2323      3    237   -251       C  
ATOM   5272  CG  ASP A 735     -44.875 -55.839  12.973  1.00 22.58           C  
ANISOU 5272  CG  ASP A 735     2790   2807   2982     19    250   -314       C  
ATOM   5273  OD1 ASP A 735     -45.284 -55.557  14.139  1.00 19.21           O  
ANISOU 5273  OD1 ASP A 735     2373   2391   2535     21    292   -387       O  
ATOM   5274  OD2 ASP A 735     -44.279 -54.989  12.250  1.00 20.28           O  
ANISOU 5274  OD2 ASP A 735     2491   2459   2754     28    222   -293       O  
ATOM   5275  N   TYR A 736     -48.698 -57.701  13.597  1.00 19.86           N  
ANISOU 5275  N   TYR A 736     2354   2600   2590     35    364   -304       N  
ATOM   5276  CA  TYR A 736     -50.061 -57.196  13.380  1.00 21.24           C  
ANISOU 5276  CA  TYR A 736     2462   2772   2836     72    400   -310       C  
ATOM   5277  C   TYR A 736     -50.199 -55.725  13.766  1.00 25.61           C  
ANISOU 5277  C   TYR A 736     2998   3265   3468    116    428   -374       C  
ATOM   5278  O   TYR A 736     -51.078 -55.036  13.255  1.00 24.49           O  
ANISOU 5278  O   TYR A 736     2796   3092   3416    160    440   -365       O  
ATOM   5279  CB  TYR A 736     -51.043 -58.026  14.206  1.00 22.02           C  
ANISOU 5279  CB  TYR A 736     2544   2941   2880     52    452   -327       C  
ATOM   5280  CG  TYR A 736     -51.381 -59.285  13.448  1.00 24.80           C  
ANISOU 5280  CG  TYR A 736     2887   3334   3204     21    424   -254       C  
ATOM   5281  CD1 TYR A 736     -50.590 -60.402  13.518  1.00 24.01           C  
ANISOU 5281  CD1 TYR A 736     2842   3256   3026    -24    395   -224       C  
ATOM   5282  CD2 TYR A 736     -52.477 -59.283  12.548  1.00 25.94           C  
ANISOU 5282  CD2 TYR A 736     2962   3486   3410     38    420   -214       C  
ATOM   5283  CE1 TYR A 736     -50.970 -61.602  12.804  1.00 24.34           C  
ANISOU 5283  CE1 TYR A 736     2874   3325   3048    -54    371   -165       C  
ATOM   5284  CE2 TYR A 736     -52.803 -60.371  11.829  1.00 25.67           C  
ANISOU 5284  CE2 TYR A 736     2917   3485   3352      5    392   -156       C  
ATOM   5285  CZ  TYR A 736     -52.054 -61.528  11.935  1.00 25.89           C  
ANISOU 5285  CZ  TYR A 736     3005   3530   3303    -41    369   -135       C  
ATOM   5286  OH  TYR A 736     -52.443 -62.589  11.115  1.00 29.09           O  
ANISOU 5286  OH  TYR A 736     3397   3958   3696    -74    340    -84       O  
ATOM   5287  N   ASN A 737     -49.361 -55.230  14.679  1.00 23.71           N  
ANISOU 5287  N   ASN A 737     2806   3005   3199    106    438   -442       N  
ATOM   5288  CA  ASN A 737     -49.450 -53.817  15.037  1.00 22.97           C  
ANISOU 5288  CA  ASN A 737     2700   2842   3186    145    464   -513       C  
ATOM   5289  C   ASN A 737     -48.395 -52.999  14.311  1.00 24.05           C  
ANISOU 5289  C   ASN A 737     2857   2897   3384    148    410   -489       C  
ATOM   5290  O   ASN A 737     -48.131 -51.863  14.701  1.00 23.94           O  
ANISOU 5290  O   ASN A 737     2851   2815   3429    167    422   -553       O  
ATOM   5291  CB  ASN A 737     -49.331 -53.639  16.579  1.00 23.38           C  
ANISOU 5291  CB  ASN A 737     2788   2924   3172    130    516   -619       C  
ATOM   5292  CG  ASN A 737     -48.013 -54.125  17.131  1.00 25.65           C  
ANISOU 5292  CG  ASN A 737     3145   3238   3361     76    481   -628       C  
ATOM   5293  OD1 ASN A 737     -47.167 -54.659  16.420  1.00 23.64           O  
ANISOU 5293  OD1 ASN A 737     2912   2981   3088     53    423   -558       O  
ATOM   5294  ND2 ASN A 737     -47.793 -53.868  18.438  1.00 28.08           N  
ANISOU 5294  ND2 ASN A 737     3489   3575   3606     58    516   -720       N  
ATOM   5295  N   TYR A 738     -47.787 -53.567  13.244  1.00 22.96           N  
ANISOU 5295  N   TYR A 738     2726   2765   3232    128    353   -400       N  
ATOM   5296  CA  TYR A 738     -46.891 -52.855  12.337  1.00 23.03           C  
ANISOU 5296  CA  TYR A 738     2742   2707   3300    128    303   -357       C  
ATOM   5297  C   TYR A 738     -45.899 -51.965  13.069  1.00 25.25           C  
ANISOU 5297  C   TYR A 738     3064   2935   3596    114    301   -426       C  
ATOM   5298  O   TYR A 738     -45.654 -50.830  12.623  1.00 27.08           O  
ANISOU 5298  O   TYR A 738     3285   3081   3923    132    286   -423       O  
ATOM   5299  CB  TYR A 738     -47.658 -52.016  11.272  1.00 21.59           C  
ANISOU 5299  CB  TYR A 738     2502   2467   3234    175    293   -304       C  
ATOM   5300  CG  TYR A 738     -48.788 -51.090  11.769  1.00 23.54           C  
ANISOU 5300  CG  TYR A 738     2705   2668   3570    229    343   -361       C  
ATOM   5301  CD1 TYR A 738     -48.541 -49.750  12.116  1.00 26.72           C  
ANISOU 5301  CD1 TYR A 738     3114   2974   4064    255    354   -418       C  
ATOM   5302  CD2 TYR A 738     -50.079 -51.545  11.835  1.00 24.10           C  
ANISOU 5302  CD2 TYR A 738     2725   2789   3642    255    378   -357       C  
ATOM   5303  CE1 TYR A 738     -49.558 -48.919  12.567  1.00 27.18           C  
ANISOU 5303  CE1 TYR A 738     3131   2985   4211    311    403   -477       C  
ATOM   5304  CE2 TYR A 738     -51.124 -50.734  12.280  1.00 28.02           C  
ANISOU 5304  CE2 TYR A 738     3173   3250   4223    310    427   -411       C  
ATOM   5305  CZ  TYR A 738     -50.846 -49.431  12.645  1.00 30.84           C  
ANISOU 5305  CZ  TYR A 738     3539   3509   4669    341    441   -472       C  
ATOM   5306  OH  TYR A 738     -51.848 -48.646  13.067  1.00 35.81           O  
ANISOU 5306  OH  TYR A 738     4119   4097   5389    401    493   -531       O  
ATOM   5307  N   ASN A 739     -45.292 -52.442  14.173  1.00 21.77           N  
ANISOU 5307  N   ASN A 739     2669   2540   3062     78    311   -485       N  
ATOM   5308  CA  ASN A 739     -44.256 -51.621  14.806  1.00 21.07           C  
ANISOU 5308  CA  ASN A 739     2618   2406   2981     56    298   -550       C  
ATOM   5309  C   ASN A 739     -42.870 -52.129  14.480  1.00 22.93           C  
ANISOU 5309  C   ASN A 739     2884   2664   3165     11    242   -503       C  
ATOM   5310  O   ASN A 739     -41.906 -51.685  15.114  1.00 25.75           O  
ANISOU 5310  O   ASN A 739     3273   3005   3506    -19    225   -554       O  
ATOM   5311  CB  ASN A 739     -44.406 -51.522  16.355  1.00 23.03           C  
ANISOU 5311  CB  ASN A 739     2897   2689   3166     43    343   -663       C  
ATOM   5312  CG  ASN A 739     -44.217 -52.875  17.089  1.00 23.74           C  
ANISOU 5312  CG  ASN A 739     3016   2886   3117      6    345   -655       C  
ATOM   5313  OD1 ASN A 739     -44.031 -53.906  16.478  1.00 20.37           O  
ANISOU 5313  OD1 ASN A 739     2588   2500   2650     -7    316   -573       O  
ATOM   5314  ND2 ASN A 739     -44.217 -52.835  18.449  1.00 25.73           N  
ANISOU 5314  ND2 ASN A 739     3300   3183   3295    -15    377   -745       N  
ATOM   5315  N   GLY A 740     -42.745 -53.106  13.569  1.00 19.69           N  
ANISOU 5315  N   GLY A 740     2463   2295   2722      6    215   -414       N  
ATOM   5316  CA  GLY A 740     -41.429 -53.548  13.214  1.00 18.89           C  
ANISOU 5316  CA  GLY A 740     2383   2212   2582    -28    168   -372       C  
ATOM   5317  C   GLY A 740     -40.801 -54.504  14.225  1.00 22.86           C  
ANISOU 5317  C   GLY A 740     2924   2786   2977    -61    160   -400       C  
ATOM   5318  O   GLY A 740     -39.633 -54.896  14.038  1.00 22.24           O  
ANISOU 5318  O   GLY A 740     2859   2725   2866    -87    120   -370       O  
ATOM   5319  N   LEU A 741     -41.532 -54.900  15.271  1.00 22.90           N  
ANISOU 5319  N   LEU A 741     2943   2835   2924    -61    198   -449       N  
ATOM   5320  CA  LEU A 741     -41.036 -55.756  16.345  1.00 21.17           C  
ANISOU 5320  CA  LEU A 741     2761   2685   2598    -93    192   -470       C  
ATOM   5321  C   LEU A 741     -41.912 -57.001  16.438  1.00 22.45           C  
ANISOU 5321  C   LEU A 741     2922   2907   2702    -89    216   -432       C  
ATOM   5322  O   LEU A 741     -43.145 -56.922  16.294  1.00 22.93           O  
ANISOU 5322  O   LEU A 741     2955   2965   2793    -66    258   -437       O  
ATOM   5323  CB  LEU A 741     -41.092 -55.019  17.723  1.00 20.65           C  
ANISOU 5323  CB  LEU A 741     2720   2626   2501   -107    220   -574       C  
ATOM   5324  CG  LEU A 741     -40.531 -53.590  17.759  1.00 21.77           C  
ANISOU 5324  CG  LEU A 741     2862   2692   2717   -110    209   -635       C  
ATOM   5325  CD1 LEU A 741     -40.677 -53.082  19.231  1.00 20.36           C  
ANISOU 5325  CD1 LEU A 741     2714   2538   2485   -129    241   -750       C  
ATOM   5326  CD2 LEU A 741     -39.038 -53.706  17.353  1.00 23.42           C  
ANISOU 5326  CD2 LEU A 741     3080   2899   2921   -142    144   -592       C  
ATOM   5327  N   ARG A 742     -41.257 -58.143  16.653  1.00 21.42           N  
ANISOU 5327  N   ARG A 742     2816   2825   2496   -113    187   -391       N  
ATOM   5328  CA  ARG A 742     -41.914 -59.421  16.878  1.00 23.63           C  
ANISOU 5328  CA  ARG A 742     3103   3158   2716   -120    204   -352       C  
ATOM   5329  C   ARG A 742     -43.147 -59.227  17.764  1.00 25.37           C  
ANISOU 5329  C   ARG A 742     3318   3409   2914   -119    265   -403       C  
ATOM   5330  O   ARG A 742     -43.081 -58.567  18.812  1.00 23.64           O  
ANISOU 5330  O   ARG A 742     3116   3205   2662   -129    287   -475       O  
ATOM   5331  CB  ARG A 742     -40.896 -60.358  17.560  1.00 26.80           C  
ANISOU 5331  CB  ARG A 742     3543   3606   3034   -149    167   -327       C  
ATOM   5332  CG  ARG A 742     -41.461 -61.347  18.536  1.00 36.80           C  
ANISOU 5332  CG  ARG A 742     4833   4934   4215   -170    190   -316       C  
ATOM   5333  CD  ARG A 742     -40.310 -62.095  19.314  1.00 38.00           C  
ANISOU 5333  CD  ARG A 742     5023   5128   4287   -197    144   -289       C  
ATOM   5334  NE  ARG A 742     -40.035 -61.497  20.605  1.00 38.57           N  
ANISOU 5334  NE  ARG A 742     5119   5243   4292   -221    149   -352       N  
ATOM   5335  CZ  ARG A 742     -40.711 -61.786  21.734  1.00 38.81           C  
ANISOU 5335  CZ  ARG A 742     5170   5336   4240   -245    186   -372       C  
ATOM   5336  NH1 ARG A 742     -41.736 -62.650  21.750  1.00 37.39           N  
ANISOU 5336  NH1 ARG A 742     4987   5179   4041   -248    224   -331       N  
ATOM   5337  NH2 ARG A 742     -40.347 -61.206  22.839  1.00 38.02           N  
ANISOU 5337  NH2 ARG A 742     5094   5279   4074   -269    186   -435       N  
ATOM   5338  N   ASP A 743     -44.284 -59.753  17.358  1.00 28.64           N  
ANISOU 5338  N   ASP A 743     3705   3834   3344   -108    296   -372       N  
ATOM   5339  CA  ASP A 743     -45.273 -59.310  18.320  1.00 36.00           C  
ANISOU 5339  CA  ASP A 743     4626   4795   4256   -106    358   -435       C  
ATOM   5340  C   ASP A 743     -45.518 -60.388  19.426  1.00 34.40           C  
ANISOU 5340  C   ASP A 743     4453   4674   3944   -144    380   -424       C  
ATOM   5341  O   ASP A 743     -45.000 -61.513  19.398  1.00 29.25           O  
ANISOU 5341  O   ASP A 743     3828   4045   3243   -168    345   -361       O  
ATOM   5342  CB  ASP A 743     -46.478 -58.671  17.555  1.00 43.60           C  
ANISOU 5342  CB  ASP A 743     5531   5722   5314    -66    393   -441       C  
ATOM   5343  CG  ASP A 743     -47.191 -59.602  16.746  1.00 42.83           C  
ANISOU 5343  CG  ASP A 743     5405   5639   5229    -67    390   -371       C  
ATOM   5344  OD1 ASP A 743     -47.985 -59.214  15.812  1.00 34.98           O  
ANISOU 5344  OD1 ASP A 743     4360   4616   4316    -37    396   -351       O  
ATOM   5345  OD2 ASP A 743     -46.913 -60.767  17.135  1.00 46.56           O  
ANISOU 5345  OD2 ASP A 743     5910   6157   5625   -102    378   -334       O  
ATOM   5346  N   ILE A 744     -46.192 -59.944  20.480  1.00 36.84           N  
ANISOU 5346  N   ILE A 744     4759   5023   4214   -148    439   -492       N  
ATOM   5347  CA  ILE A 744     -46.091 -60.484  21.833  1.00 50.27           C  
ANISOU 5347  CA  ILE A 744     6499   6805   5795   -189    459   -508       C  
ATOM   5348  C   ILE A 744     -47.473 -60.447  22.487  1.00 57.38           C  
ANISOU 5348  C   ILE A 744     7370   7760   6673   -190    542   -545       C  
ATOM   5349  O   ILE A 744     -48.336 -59.661  22.094  1.00 59.13           O  
ANISOU 5349  O   ILE A 744     7542   7949   6975   -152    584   -588       O  
ATOM   5350  CB  ILE A 744     -45.073 -59.638  22.641  1.00 52.77           C  
ANISOU 5350  CB  ILE A 744     6853   7125   6071   -200    438   -582       C  
ATOM   5351  CG1 ILE A 744     -43.668 -59.958  22.173  1.00 56.43           C  
ANISOU 5351  CG1 ILE A 744     7344   7561   6537   -210    356   -531       C  
ATOM   5352  CG2 ILE A 744     -45.102 -59.968  24.025  1.00 57.53           C  
ANISOU 5352  CG2 ILE A 744     7491   7818   6550   -239    464   -612       C  
ATOM   5353  CD1 ILE A 744     -42.576 -59.044  22.746  1.00 61.20           C  
ANISOU 5353  CD1 ILE A 744     7975   8158   7121   -223    323   -599       C  
ATOM   5354  N   GLU A 745     -47.703 -61.348  23.439  1.00 63.88           N  
ANISOU 5354  N   GLU A 745     8217   8665   7389   -233    566   -520       N  
ATOM   5355  CA  GLU A 745     -48.823 -61.265  24.401  1.00 63.51           C  
ANISOU 5355  CA  GLU A 745     8150   8694   7287   -246    652   -568       C  
ATOM   5356  C   GLU A 745     -50.164 -60.876  23.761  1.00 60.12           C  
ANISOU 5356  C   GLU A 745     7646   8242   6954   -208    709   -585       C  
ATOM   5357  O   GLU A 745     -50.713 -59.814  24.049  1.00 63.41           O  
ANISOU 5357  O   GLU A 745     8032   8653   7407   -174    764   -676       O  
ATOM   5358  CB  GLU A 745     -48.470 -60.261  25.505  1.00 67.30           C  
ANISOU 5358  CB  GLU A 745     8656   9207   7706   -248    680   -680       C  
ATOM   5359  N   ASP A 746     -50.695 -61.715  22.878  1.00 48.73           N  
ANISOU 5359  N   ASP A 746     6173   6784   5559   -211    694   -500       N  
ATOM   5360  CA  ASP A 746     -52.050 -61.483  22.345  1.00 46.71           C  
ANISOU 5360  CA  ASP A 746     5839   6524   5383   -183    746   -505       C  
ATOM   5361  C   ASP A 746     -52.140 -60.381  21.286  1.00 39.22           C  
ANISOU 5361  C   ASP A 746     4847   5489   4565   -120    728   -535       C  
ATOM   5362  O   ASP A 746     -53.259 -59.958  20.946  1.00 37.95           O  
ANISOU 5362  O   ASP A 746     4615   5325   4477    -87    772   -552       O  
ATOM   5363  CB  ASP A 746     -53.072 -61.176  23.452  1.00 50.50           C  
ANISOU 5363  CB  ASP A 746     6287   7085   5816   -188    843   -573       C  
ATOM   5364  N   GLU A 747     -51.016 -59.940  20.699  1.00 31.62           N  
ANISOU 5364  N   GLU A 747     3920   4458   3638   -104    661   -532       N  
ATOM   5365  CA  GLU A 747     -51.095 -59.013  19.569  1.00 30.75           C  
ANISOU 5365  CA  GLU A 747     3769   4264   3650    -51    637   -536       C  
ATOM   5366  C   GLU A 747     -51.451 -59.698  18.244  1.00 28.96           C  
ANISOU 5366  C   GLU A 747     3508   4016   3479    -49    596   -445       C  
ATOM   5367  O   GLU A 747     -51.845 -59.007  17.306  1.00 27.52           O  
ANISOU 5367  O   GLU A 747     3279   3784   3396     -7    584   -437       O  
ATOM   5368  CB  GLU A 747     -49.754 -58.244  19.441  1.00 31.52           C  
ANISOU 5368  CB  GLU A 747     3914   4299   3764    -42    585   -564       C  
ATOM   5369  CG  GLU A 747     -49.592 -57.289  20.639  1.00 33.11           C  
ANISOU 5369  CG  GLU A 747     4137   4510   3934    -37    629   -675       C  
ATOM   5370  CD  GLU A 747     -48.175 -56.739  20.726  1.00 35.13           C  
ANISOU 5370  CD  GLU A 747     4446   4721   4181    -48    573   -701       C  
ATOM   5371  OE1 GLU A 747     -47.995 -55.714  21.428  1.00 35.32           O  
ANISOU 5371  OE1 GLU A 747     4482   4725   4211    -38    599   -799       O  
ATOM   5372  OE2 GLU A 747     -47.267 -57.350  20.103  1.00 35.36           O  
ANISOU 5372  OE2 GLU A 747     4501   4736   4199    -67    507   -629       O  
ATOM   5373  N   ILE A 748     -51.379 -61.024  18.151  1.00 28.87           N  
ANISOU 5373  N   ILE A 748     3519   4042   3409    -95    574   -377       N  
ATOM   5374  CA  ILE A 748     -51.712 -61.714  16.912  1.00 31.27           C  
ANISOU 5374  CA  ILE A 748     3794   4328   3759    -99    534   -302       C  
ATOM   5375  C   ILE A 748     -53.224 -61.756  16.742  1.00 30.27           C  
ANISOU 5375  C   ILE A 748     3590   4234   3676    -91    581   -297       C  
ATOM   5376  O   ILE A 748     -53.950 -62.240  17.613  1.00 27.60           O  
ANISOU 5376  O   ILE A 748     3239   3959   3290   -120    636   -306       O  
ATOM   5377  CB  ILE A 748     -51.123 -63.131  16.903  1.00 32.24           C  
ANISOU 5377  CB  ILE A 748     3969   4469   3813   -149    497   -240       C  
ATOM   5378  CG1 ILE A 748     -49.598 -63.055  16.814  1.00 32.60           C  
ANISOU 5378  CG1 ILE A 748     4075   4477   3835   -147    441   -236       C  
ATOM   5379  CG2 ILE A 748     -51.816 -64.002  15.724  1.00 31.03           C  
ANISOU 5379  CG2 ILE A 748     3778   4310   3701   -164    471   -174       C  
ATOM   5380  CD1 ILE A 748     -48.928 -64.376  16.954  1.00 34.04           C  
ANISOU 5380  CD1 ILE A 748     4308   4672   3954   -187    407   -181       C  
ATOM   5381  N   LYS A 749     -53.710 -61.307  15.584  1.00 29.83           N  
ANISOU 5381  N   LYS A 749     3480   4144   3712    -57    557   -273       N  
ATOM   5382  CA  LYS A 749     -55.141 -61.077  15.448  1.00 30.26           C  
ANISOU 5382  CA  LYS A 749     3447   4227   3823    -38    601   -277       C  
ATOM   5383  C   LYS A 749     -55.826 -62.044  14.502  1.00 31.59           C  
ANISOU 5383  C   LYS A 749     3577   4417   4008    -69    570   -206       C  
ATOM   5384  O   LYS A 749     -57.046 -61.953  14.363  1.00 30.78           O  
ANISOU 5384  O   LYS A 749     3394   4348   3952    -60    601   -201       O  
ATOM   5385  CB  LYS A 749     -55.433 -59.642  14.965  1.00 29.36           C  
ANISOU 5385  CB  LYS A 749     3281   4060   3813     32    604   -309       C  
ATOM   5386  CG  LYS A 749     -54.968 -58.540  15.910  1.00 29.67           C  
ANISOU 5386  CG  LYS A 749     3348   4070   3855     66    643   -395       C  
ATOM   5387  CD  LYS A 749     -55.627 -58.714  17.327  1.00 33.20           C  
ANISOU 5387  CD  LYS A 749     3786   4590   4240     50    730   -458       C  
ATOM   5388  CE  LYS A 749     -55.041 -57.694  18.356  1.00 37.70           C  
ANISOU 5388  CE  LYS A 749     4396   5138   4792     73    767   -558       C  
ATOM   5389  NZ  LYS A 749     -55.564 -57.986  19.745  1.00 40.96           N  
ANISOU 5389  NZ  LYS A 749     4810   5636   5117     47    849   -617       N  
ATOM   5390  N   GLN A 750     -55.092 -62.943  13.818  1.00 25.51           N  
ANISOU 5390  N   GLN A 750     2856   3630   3205   -104    509   -155       N  
ATOM   5391  CA  GLN A 750     -55.763 -63.881  12.920  1.00 25.89           C  
ANISOU 5391  CA  GLN A 750     2871   3699   3269   -139    479    -99       C  
ATOM   5392  C   GLN A 750     -55.201 -65.286  13.126  1.00 24.87           C  
ANISOU 5392  C   GLN A 750     2808   3577   3066   -201    459    -66       C  
ATOM   5393  O   GLN A 750     -53.974 -65.457  13.202  1.00 25.40           O  
ANISOU 5393  O   GLN A 750     2946   3610   3094   -202    428    -66       O  
ATOM   5394  CB  GLN A 750     -55.597 -63.451  11.402  1.00 24.84           C  
ANISOU 5394  CB  GLN A 750     2714   3528   3197   -110    414    -65       C  
ATOM   5395  N   TYR A 751     -56.093 -66.286  13.122  1.00 25.99           N  
ANISOU 5395  N   TYR A 751     2920   3756   3198   -252    471    -35       N  
ATOM   5396  CA  TYR A 751     -55.766 -67.709  13.229  1.00 26.85           C  
ANISOU 5396  CA  TYR A 751     3084   3862   3256   -314    451      3       C  
ATOM   5397  C   TYR A 751     -56.483 -68.482  12.112  1.00 27.06           C  
ANISOU 5397  C   TYR A 751     3071   3890   3318   -351    414     39       C  
ATOM   5398  O   TYR A 751     -57.500 -68.035  11.609  1.00 24.67           O  
ANISOU 5398  O   TYR A 751     2688   3616   3068   -340    420     39       O  
ATOM   5399  CB  TYR A 751     -56.211 -68.252  14.601  1.00 26.28           C  
ANISOU 5399  CB  TYR A 751     3020   3838   3128   -357    512      5       C  
ATOM   5400  CG  TYR A 751     -55.387 -67.655  15.725  1.00 25.10           C  
ANISOU 5400  CG  TYR A 751     2921   3693   2923   -332    541    -32       C  
ATOM   5401  CD1 TYR A 751     -55.695 -66.399  16.248  1.00 27.25           C  
ANISOU 5401  CD1 TYR A 751     3156   3987   3211   -285    588    -90       C  
ATOM   5402  CD2 TYR A 751     -54.299 -68.335  16.237  1.00 24.83           C  
ANISOU 5402  CD2 TYR A 751     2970   3639   2825   -355    516    -12       C  
ATOM   5403  CE1 TYR A 751     -54.938 -65.843  17.264  1.00 28.76           C  
ANISOU 5403  CE1 TYR A 751     3395   4184   3348   -269    611   -134       C  
ATOM   5404  CE2 TYR A 751     -53.512 -67.788  17.243  1.00 27.94           C  
ANISOU 5404  CE2 TYR A 751     3408   4044   3162   -337    533    -46       C  
ATOM   5405  CZ  TYR A 751     -53.854 -66.557  17.754  1.00 31.66           C  
ANISOU 5405  CZ  TYR A 751     3845   4541   3643   -298    581   -109       C  
ATOM   5406  OH  TYR A 751     -53.096 -66.038  18.754  1.00 36.28           O  
ANISOU 5406  OH  TYR A 751     4475   5140   4168   -288    596   -150       O  
ATOM   5407  N   VAL A 752     -55.912 -69.619  11.696  1.00 24.38           N  
ANISOU 5407  N   VAL A 752     2789   3519   2955   -392    372     66       N  
ATOM   5408  CA  VAL A 752     -56.617 -70.514  10.797  1.00 25.66           C  
ANISOU 5408  CA  VAL A 752     2923   3685   3143   -441    340     92       C  
ATOM   5409  C   VAL A 752     -57.927 -70.935  11.452  1.00 28.39           C  
ANISOU 5409  C   VAL A 752     3209   4082   3495   -491    389    107       C  
ATOM   5410  O   VAL A 752     -57.989 -71.202  12.670  1.00 28.57           O  
ANISOU 5410  O   VAL A 752     3252   4126   3477   -514    440    113       O  
ATOM   5411  CB  VAL A 752     -55.737 -71.728  10.452  1.00 23.02           C  
ANISOU 5411  CB  VAL A 752     2667   3297   2781   -476    297    109       C  
ATOM   5412  CG1 VAL A 752     -56.390 -72.528   9.334  1.00 23.63           C  
ANISOU 5412  CG1 VAL A 752     2718   3372   2888   -524    257    120       C  
ATOM   5413  CG2 VAL A 752     -54.331 -71.231   9.934  1.00 19.55           C  
ANISOU 5413  CG2 VAL A 752     2282   2815   2332   -421    259     92       C  
ATOM   5414  N   GLU A 753     -58.994 -70.937  10.652  1.00 28.54           N  
ANISOU 5414  N   GLU A 753     3150   4133   3562   -509    375    116       N  
ATOM   5415  CA  GLU A 753     -60.361 -71.109  11.168  1.00 32.41           C  
ANISOU 5415  CA  GLU A 753     3558   4684   4071   -549    424    128       C  
ATOM   5416  C   GLU A 753     -60.493 -72.242  12.185  1.00 34.70           C  
ANISOU 5416  C   GLU A 753     3885   4980   4318   -622    461    155       C  
ATOM   5417  O   GLU A 753     -60.136 -73.387  11.901  1.00 35.86           O  
ANISOU 5417  O   GLU A 753     4089   5084   4452   -676    425    180       O  
ATOM   5418  CB  GLU A 753     -61.294 -71.380   9.992  1.00 38.76           C  
ANISOU 5418  CB  GLU A 753     4289   5510   4926   -580    379    144       C  
ATOM   5419  CG  GLU A 753     -62.528 -72.046  10.366  1.00 47.76           C  
ANISOU 5419  CG  GLU A 753     5362   6702   6082   -650    412    166       C  
ATOM   5420  CD  GLU A 753     -63.457 -71.084  10.975  1.00 55.00           C  
ANISOU 5420  CD  GLU A 753     6184   7685   7031   -612    475    154       C  
ATOM   5421  OE1 GLU A 753     -63.182 -69.872  10.811  1.00 56.07           O  
ANISOU 5421  OE1 GLU A 753     6302   7814   7188   -528    475    128       O  
ATOM   5422  OE2 GLU A 753     -64.440 -71.523  11.616  1.00 58.88           O  
ANISOU 5422  OE2 GLU A 753     6615   8230   7526   -664    526    170       O  
ATOM   5423  N   GLY A 754     -61.058 -71.924  13.355  1.00 35.14           N  
ANISOU 5423  N   GLY A 754     3907   5092   4354   -625    537    151       N  
ATOM   5424  CA  GLY A 754     -61.345 -72.921  14.380  1.00 35.57           C  
ANISOU 5424  CA  GLY A 754     3984   5167   4363   -699    581    188       C  
ATOM   5425  C   GLY A 754     -60.149 -73.477  15.121  1.00 38.53           C  
ANISOU 5425  C   GLY A 754     4470   5498   4670   -708    575    205       C  
ATOM   5426  O   GLY A 754     -60.295 -74.495  15.775  1.00 40.47           O  
ANISOU 5426  O   GLY A 754     4745   5746   4884   -777    593    251       O  
ATOM   5427  N   SER A 755     -58.957 -72.858  15.021  1.00 34.63           N  
ANISOU 5427  N   SER A 755     4037   4963   4158   -643    545    176       N  
ATOM   5428  CA  SER A 755     -57.712 -73.461  15.473  1.00 29.72           C  
ANISOU 5428  CA  SER A 755     3517   4291   3484   -648    519    197       C  
ATOM   5429  C   SER A 755     -56.917 -72.437  16.267  1.00 29.26           C  
ANISOU 5429  C   SER A 755     3489   4249   3379   -588    543    160       C  
ATOM   5430  O   SER A 755     -57.265 -71.255  16.312  1.00 29.78           O  
ANISOU 5430  O   SER A 755     3503   4348   3462   -538    574    112       O  
ATOM   5431  CB  SER A 755     -56.850 -73.947  14.291  1.00 28.18           C  
ANISOU 5431  CB  SER A 755     3371   4016   3319   -636    441    199       C  
ATOM   5432  OG  SER A 755     -56.063 -72.863  13.798  1.00 26.48           O  
ANISOU 5432  OG  SER A 755     3163   3785   3114   -559    417    157       O  
ATOM   5433  N   SER A 756     -55.797 -72.859  16.856  1.00 28.57           N  
ANISOU 5433  N   SER A 756     3486   4133   3238   -589    523    179       N  
ATOM   5434  CA  SER A 756     -54.886 -71.858  17.400  1.00 33.00           C  
ANISOU 5434  CA  SER A 756     4078   4700   3760   -531    527    137       C  
ATOM   5435  C   SER A 756     -53.596 -71.757  16.583  1.00 29.59           C  
ANISOU 5435  C   SER A 756     3697   4199   3349   -488    458    129       C  
ATOM   5436  O   SER A 756     -52.537 -71.396  17.085  1.00 29.26           O  
ANISOU 5436  O   SER A 756     3702   4147   3266   -459    444    115       O  
ATOM   5437  CB  SER A 756     -54.635 -72.089  18.893  1.00 41.33           C  
ANISOU 5437  CB  SER A 756     5176   5803   4725   -560    567    156       C  
ATOM   5438  OG  SER A 756     -54.149 -73.368  19.144  1.00 44.46           O  
ANISOU 5438  OG  SER A 756     5633   6167   5092   -607    536    225       O  
ATOM   5439  N   ILE A 757     -53.686 -72.022  15.289  1.00 25.08           N  
ANISOU 5439  N   ILE A 757     3107   3583   2837   -484    415    132       N  
ATOM   5440  CA  ILE A 757     -52.557 -71.811  14.383  1.00 22.44           C  
ANISOU 5440  CA  ILE A 757     2808   3194   2525   -440    357    118       C  
ATOM   5441  C   ILE A 757     -52.553 -70.338  13.979  1.00 23.91           C  
ANISOU 5441  C   ILE A 757     2952   3393   2741   -381    363     69       C  
ATOM   5442  O   ILE A 757     -53.474 -69.905  13.249  1.00 25.24           O  
ANISOU 5442  O   ILE A 757     3055   3576   2958   -374    368     59       O  
ATOM   5443  CB  ILE A 757     -52.687 -72.698  13.134  1.00 23.19           C  
ANISOU 5443  CB  ILE A 757     2903   3246   2664   -463    312    135       C  
ATOM   5444  CG1 ILE A 757     -52.866 -74.186  13.521  1.00 24.10           C  
ANISOU 5444  CG1 ILE A 757     3055   3336   2766   -527    309    183       C  
ATOM   5445  CG2 ILE A 757     -51.460 -72.448  12.189  1.00 20.44           C  
ANISOU 5445  CG2 ILE A 757     2587   2849   2330   -416    260    117       C  
ATOM   5446  CD1 ILE A 757     -53.552 -74.958  12.339  1.00 23.13           C  
ANISOU 5446  CD1 ILE A 757     2908   3187   2695   -566    281    187       C  
ATOM   5447  N   PRO A 758     -51.564 -69.554  14.408  1.00 23.34           N  
ANISOU 5447  N   PRO A 758     2910   3312   2645   -340    358     42       N  
ATOM   5448  CA  PRO A 758     -51.531 -68.115  14.071  1.00 23.46           C  
ANISOU 5448  CA  PRO A 758     2889   3327   2698   -287    364     -2       C  
ATOM   5449  C   PRO A 758     -51.178 -67.886  12.592  1.00 23.48           C  
ANISOU 5449  C   PRO A 758     2879   3290   2753   -261    312      3       C  
ATOM   5450  O   PRO A 758     -50.424 -68.655  11.999  1.00 22.82           O  
ANISOU 5450  O   PRO A 758     2834   3175   2661   -271    271     25       O  
ATOM   5451  CB  PRO A 758     -50.399 -67.587  14.969  1.00 23.10           C  
ANISOU 5451  CB  PRO A 758     2894   3277   2607   -266    363    -28       C  
ATOM   5452  CG  PRO A 758     -49.374 -68.804  15.014  1.00 24.24           C  
ANISOU 5452  CG  PRO A 758     3103   3395   2712   -291    320     15       C  
ATOM   5453  CD  PRO A 758     -50.332 -69.995  15.140  1.00 23.44           C  
ANISOU 5453  CD  PRO A 758     2995   3309   2604   -343    338     56       C  
ATOM   5454  N   VAL A 759     -51.670 -66.799  12.001  1.00 22.10           N  
ANISOU 5454  N   VAL A 759     2650   3117   2630   -225    316    -15       N  
ATOM   5455  CA  VAL A 759     -51.410 -66.503  10.580  1.00 18.53           C  
ANISOU 5455  CA  VAL A 759     2182   2640   2220   -203    269     -2       C  
ATOM   5456  C   VAL A 759     -50.308 -65.455  10.484  1.00 20.59           C  
ANISOU 5456  C   VAL A 759     2465   2869   2491   -160    252    -21       C  
ATOM   5457  O   VAL A 759     -50.476 -64.348  11.026  1.00 21.95           O  
ANISOU 5457  O   VAL A 759     2615   3038   2686   -130    281    -52       O  
ATOM   5458  CB  VAL A 759     -52.672 -66.021   9.859  1.00 18.18           C  
ANISOU 5458  CB  VAL A 759     2058   2617   2231   -194    273      6       C  
ATOM   5459  CG1 VAL A 759     -52.333 -65.603   8.353  1.00 19.33           C  
ANISOU 5459  CG1 VAL A 759     2189   2745   2410   -172    219     27       C  
ATOM   5460  CG2 VAL A 759     -53.811 -67.179   9.937  1.00 17.27           C  
ANISOU 5460  CG2 VAL A 759     1916   2539   2107   -250    287     27       C  
ATOM   5461  N   PRO A 760     -49.202 -65.731   9.797  1.00 21.88           N  
ANISOU 5461  N   PRO A 760     2665   3005   2642   -157    210     -8       N  
ATOM   5462  CA  PRO A 760     -48.131 -64.730   9.722  1.00 23.04           C  
ANISOU 5462  CA  PRO A 760     2828   3125   2801   -124    196    -22       C  
ATOM   5463  C   PRO A 760     -48.588 -63.533   8.902  1.00 22.93           C  
ANISOU 5463  C   PRO A 760     2762   3100   2849    -91    190    -17       C  
ATOM   5464  O   PRO A 760     -49.393 -63.666   7.980  1.00 21.47           O  
ANISOU 5464  O   PRO A 760     2537   2930   2689    -95    176      9       O  
ATOM   5465  CB  PRO A 760     -46.972 -65.463   9.033  1.00 19.96           C  
ANISOU 5465  CB  PRO A 760     2478   2719   2387   -131    155     -3       C  
ATOM   5466  CG  PRO A 760     -47.206 -66.974   9.357  1.00 23.92           C  
ANISOU 5466  CG  PRO A 760     3008   3229   2851   -168    157     10       C  
ATOM   5467  CD  PRO A 760     -48.744 -67.095   9.428  1.00 22.49           C  
ANISOU 5467  CD  PRO A 760     2782   3076   2687   -188    184     14       C  
ATOM   5468  N   THR A 761     -48.008 -62.355   9.210  1.00 22.04           N  
ANISOU 5468  N   THR A 761     2653   2958   2763    -62    194    -40       N  
ATOM   5469  CA  THR A 761     -48.240 -61.186   8.362  1.00 19.18           C  
ANISOU 5469  CA  THR A 761     2249   2572   2468    -30    181    -24       C  
ATOM   5470  C   THR A 761     -47.212 -61.080   7.235  1.00 21.58           C  
ANISOU 5470  C   THR A 761     2568   2861   2772    -30    137     11       C  
ATOM   5471  O   THR A 761     -47.486 -60.386   6.245  1.00 20.06           O  
ANISOU 5471  O   THR A 761     2339   2660   2624    -13    116     46       O  
ATOM   5472  CB  THR A 761     -48.181 -59.904   9.203  1.00 20.33           C  
ANISOU 5472  CB  THR A 761     2388   2682   2655     -1    209    -67       C  
ATOM   5473  OG1 THR A 761     -46.897 -59.820   9.875  1.00 21.75           O  
ANISOU 5473  OG1 THR A 761     2620   2844   2798    -11    203    -95       O  
ATOM   5474  CG2 THR A 761     -49.343 -59.884  10.232  1.00 18.82           C  
ANISOU 5474  CG2 THR A 761     2170   2514   2467      5    262   -107       C  
ATOM   5475  N   HIS A 762     -46.054 -61.754   7.369  1.00 19.39           N  
ANISOU 5475  N   HIS A 762     2337   2584   2444    -48    122      7       N  
ATOM   5476  CA  HIS A 762     -44.980 -61.735   6.388  1.00 18.85           C  
ANISOU 5476  CA  HIS A 762     2282   2511   2370    -49     89     34       C  
ATOM   5477  C   HIS A 762     -44.262 -63.082   6.447  1.00 21.65           C  
ANISOU 5477  C   HIS A 762     2677   2883   2667    -70     79     31       C  
ATOM   5478  O   HIS A 762     -44.401 -63.846   7.418  1.00 20.62           O  
ANISOU 5478  O   HIS A 762     2571   2757   2505    -83     94     11       O  
ATOM   5479  CB  HIS A 762     -43.954 -60.590   6.649  1.00 19.93           C  
ANISOU 5479  CB  HIS A 762     2428   2611   2535    -35     84     24       C  
ATOM   5480  CG  HIS A 762     -44.555 -59.203   6.640  1.00 20.92           C  
ANISOU 5480  CG  HIS A 762     2518   2700   2730    -10     94     25       C  
ATOM   5481  ND1 HIS A 762     -45.242 -58.691   7.723  1.00 20.33           N  
ANISOU 5481  ND1 HIS A 762     2436   2608   2680      3    127    -20       N  
ATOM   5482  CD2 HIS A 762     -44.521 -58.207   5.702  1.00 21.55           C  
ANISOU 5482  CD2 HIS A 762     2569   2755   2865      4     75     65       C  
ATOM   5483  CE1 HIS A 762     -45.661 -57.461   7.438  1.00 22.98           C  
ANISOU 5483  CE1 HIS A 762     2738   2902   3091     30    130    -13       C  
ATOM   5484  NE2 HIS A 762     -45.203 -57.128   6.234  1.00 22.99           N  
ANISOU 5484  NE2 HIS A 762     2727   2895   3114     30     96     44       N  
ATOM   5485  N   TYR A 763     -43.507 -63.372   5.399  1.00 20.16           N  
ANISOU 5485  N   TYR A 763     2493   2702   2464    -72     54     52       N  
ATOM   5486  CA  TYR A 763     -42.542 -64.477   5.403  1.00 22.27           C  
ANISOU 5486  CA  TYR A 763     2797   2975   2691    -81     44     45       C  
ATOM   5487  C   TYR A 763     -41.184 -63.915   4.991  1.00 23.66           C  
ANISOU 5487  C   TYR A 763     2973   3145   2870    -70     30     53       C  
ATOM   5488  O   TYR A 763     -41.111 -63.114   4.056  1.00 22.83           O  
ANISOU 5488  O   TYR A 763     2842   3045   2786    -66     22     78       O  
ATOM   5489  CB  TYR A 763     -42.940 -65.608   4.416  1.00 18.02           C  
ANISOU 5489  CB  TYR A 763     2260   2458   2129    -96     34     53       C  
ATOM   5490  CG  TYR A 763     -44.065 -66.450   5.023  1.00 18.12           C  
ANISOU 5490  CG  TYR A 763     2279   2472   2135   -117     47     44       C  
ATOM   5491  CD1 TYR A 763     -43.761 -67.502   5.909  1.00 18.97           C  
ANISOU 5491  CD1 TYR A 763     2425   2564   2219   -127     53     32       C  
ATOM   5492  CD2 TYR A 763     -45.394 -66.245   4.651  1.00 19.35           C  
ANISOU 5492  CD2 TYR A 763     2397   2646   2308   -128     50     54       C  
ATOM   5493  CE1 TYR A 763     -44.768 -68.276   6.480  1.00 20.11           C  
ANISOU 5493  CE1 TYR A 763     2574   2710   2357   -153     67     31       C  
ATOM   5494  CE2 TYR A 763     -46.440 -67.031   5.272  1.00 20.01           C  
ANISOU 5494  CE2 TYR A 763     2481   2736   2388   -153     66     47       C  
ATOM   5495  CZ  TYR A 763     -46.089 -68.049   6.147  1.00 21.42           C  
ANISOU 5495  CZ  TYR A 763     2701   2897   2541   -168     75     37       C  
ATOM   5496  OH  TYR A 763     -47.084 -68.826   6.721  1.00 23.08           O  
ANISOU 5496  OH  TYR A 763     2911   3113   2747   -200     91     38       O  
ATOM   5497  N   TYR A 764     -40.121 -64.346   5.667  1.00 20.45           N  
ANISOU 5497  N   TYR A 764     2593   2732   2445    -68     27     39       N  
ATOM   5498  CA  TYR A 764     -38.778 -63.878   5.344  1.00 20.34           C  
ANISOU 5498  CA  TYR A 764     2573   2719   2436    -60     14     46       C  
ATOM   5499  C   TYR A 764     -37.946 -65.009   4.745  1.00 20.82           C  
ANISOU 5499  C   TYR A 764     2645   2796   2470    -55      6     46       C  
ATOM   5500  O   TYR A 764     -38.243 -66.198   4.921  1.00 16.82           O  
ANISOU 5500  O   TYR A 764     2161   2287   1943    -56      8     36       O  
ATOM   5501  CB  TYR A 764     -38.069 -63.303   6.584  1.00 16.73           C  
ANISOU 5501  CB  TYR A 764     2127   2245   1986    -60     11     26       C  
ATOM   5502  CG  TYR A 764     -37.681 -64.355   7.594  1.00 18.65           C  
ANISOU 5502  CG  TYR A 764     2401   2492   2194    -61      6     12       C  
ATOM   5503  CD1 TYR A 764     -36.420 -64.976   7.524  1.00 21.53           C  
ANISOU 5503  CD1 TYR A 764     2770   2866   2546    -52    -11     18       C  
ATOM   5504  CD2 TYR A 764     -38.522 -64.683   8.659  1.00 16.42           C  
ANISOU 5504  CD2 TYR A 764     2140   2208   1892    -70     19     -2       C  
ATOM   5505  CE1 TYR A 764     -35.995 -65.949   8.467  1.00 20.43           C  
ANISOU 5505  CE1 TYR A 764     2656   2726   2379    -48    -23     17       C  
ATOM   5506  CE2 TYR A 764     -38.104 -65.679   9.630  1.00 16.79           C  
ANISOU 5506  CE2 TYR A 764     2217   2259   1902    -73     10     -1       C  
ATOM   5507  CZ  TYR A 764     -36.845 -66.318   9.487  1.00 20.26           C  
ANISOU 5507  CZ  TYR A 764     2662   2701   2335    -60    -15     11       C  
ATOM   5508  OH  TYR A 764     -36.374 -67.297  10.363  1.00 21.49           O  
ANISOU 5508  OH  TYR A 764     2844   2859   2463    -58    -30     23       O  
ATOM   5509  N   SER A 765     -36.899 -64.616   4.022  1.00 19.32           N  
ANISOU 5509  N   SER A 765     2435   2621   2284    -50      1     58       N  
ATOM   5510  CA  SER A 765     -35.799 -65.507   3.675  1.00 20.07           C  
ANISOU 5510  CA  SER A 765     2534   2731   2362    -37     -2     51       C  
ATOM   5511  C   SER A 765     -34.489 -64.715   3.681  1.00 22.84           C  
ANISOU 5511  C   SER A 765     2858   3091   2728    -34     -8     62       C  
ATOM   5512  O   SER A 765     -34.451 -63.536   3.327  1.00 22.34           O  
ANISOU 5512  O   SER A 765     2772   3029   2685    -47     -8     82       O  
ATOM   5513  CB  SER A 765     -36.009 -66.192   2.313  1.00 23.86           C  
ANISOU 5513  CB  SER A 765     3010   3238   2820    -36      5     50       C  
ATOM   5514  OG  SER A 765     -37.151 -67.040   2.442  1.00 28.30           O  
ANISOU 5514  OG  SER A 765     3596   3787   3371    -44      6     36       O  
ATOM   5515  N   ILE A 766     -33.438 -65.360   4.149  1.00 20.92           N  
ANISOU 5515  N   ILE A 766     2618   2851   2481    -19    -16     51       N  
ATOM   5516  CA  ILE A 766     -32.097 -64.801   4.218  1.00 20.71           C  
ANISOU 5516  CA  ILE A 766     2560   2840   2470    -18    -25     60       C  
ATOM   5517  C   ILE A 766     -31.258 -65.708   3.341  1.00 23.23           C  
ANISOU 5517  C   ILE A 766     2861   3187   2777      6    -14     55       C  
ATOM   5518  O   ILE A 766     -31.200 -66.915   3.593  1.00 24.75           O  
ANISOU 5518  O   ILE A 766     3074   3368   2962     29    -16     38       O  
ATOM   5519  CB  ILE A 766     -31.543 -64.797   5.666  1.00 20.42           C  
ANISOU 5519  CB  ILE A 766     2533   2789   2438    -17    -48     50       C  
ATOM   5520  CG1 ILE A 766     -32.317 -63.794   6.579  1.00 21.39           C  
ANISOU 5520  CG1 ILE A 766     2672   2887   2568    -41    -53     41       C  
ATOM   5521  CG2 ILE A 766     -30.042 -64.473   5.633  1.00 22.66           C  
ANISOU 5521  CG2 ILE A 766     2776   3096   2737    -15    -61     58       C  
ATOM   5522  CD1 ILE A 766     -32.186 -64.086   8.069  1.00 18.63           C  
ANISOU 5522  CD1 ILE A 766     2347   2531   2200    -43    -72     25       C  
ATOM   5523  N   ILE A 767     -30.589 -65.154   2.334  1.00 21.49           N  
ANISOU 5523  N   ILE A 767     2604   3003   2559     -1     -1     70       N  
ATOM   5524  CA  ILE A 767     -29.888 -65.984   1.364  1.00 21.11           C  
ANISOU 5524  CA  ILE A 767     2536   2990   2495     22     20     57       C  
ATOM   5525  C   ILE A 767     -28.409 -65.632   1.385  1.00 21.91           C  
ANISOU 5525  C   ILE A 767     2587   3121   2615     28     21     68       C  
ATOM   5526  O   ILE A 767     -28.022 -64.525   1.012  1.00 19.22           O  
ANISOU 5526  O   ILE A 767     2214   2803   2284      0     25     96       O  
ATOM   5527  CB  ILE A 767     -30.507 -65.832  -0.030  1.00 24.67           C  
ANISOU 5527  CB  ILE A 767     2983   3475   2914      7     42     64       C  
ATOM   5528  CG1 ILE A 767     -31.987 -66.245   0.077  1.00 27.25           C  
ANISOU 5528  CG1 ILE A 767     3353   3773   3228      0     35     53       C  
ATOM   5529  CG2 ILE A 767     -29.736 -66.681  -1.088  1.00 23.62           C  
ANISOU 5529  CG2 ILE A 767     2830   3388   2755     30     71     38       C  
ATOM   5530  CD1 ILE A 767     -32.729 -65.885  -1.147  1.00 29.55           C  
ANISOU 5530  CD1 ILE A 767     3638   4099   3488    -21     45     68       C  
ATOM   5531  N   THR A 768     -27.572 -66.560   1.871  1.00 22.50           N  
ANISOU 5531  N   THR A 768     2653   3194   2702     63     14     50       N  
ATOM   5532  CA  THR A 768     -26.172 -66.246   2.109  1.00 25.64           C  
ANISOU 5532  CA  THR A 768     2997   3621   3126     69      7     61       C  
ATOM   5533  C   THR A 768     -25.259 -67.099   1.214  1.00 24.06           C  
ANISOU 5533  C   THR A 768     2758   3460   2924    108     38     41       C  
ATOM   5534  O   THR A 768     -25.541 -68.276   0.965  1.00 23.42           O  
ANISOU 5534  O   THR A 768     2702   3361   2835    144     50     10       O  
ATOM   5535  CB  THR A 768     -25.810 -66.496   3.611  1.00 25.18           C  
ANISOU 5535  CB  THR A 768     2947   3533   3087     80    -35     62       C  
ATOM   5536  OG1 THR A 768     -26.855 -65.992   4.441  1.00 24.37           O  
ANISOU 5536  OG1 THR A 768     2891   3392   2975     52    -55     65       O  
ATOM   5537  CG2 THR A 768     -24.460 -65.860   3.982  1.00 25.54           C  
ANISOU 5537  CG2 THR A 768     2933   3612   3161     71    -54     79       C  
ATOM   5538  N   SER A 769     -24.148 -66.529   0.777  1.00 23.38           N  
ANISOU 5538  N   SER A 769     2609   3425   2851    100     52     57       N  
ATOM   5539  CA  SER A 769     -23.115 -67.313   0.076  1.00 21.82           C  
ANISOU 5539  CA  SER A 769     2360   3270   2658    143     85     35       C  
ATOM   5540  C   SER A 769     -21.760 -66.651   0.299  1.00 25.25           C  
ANISOU 5540  C   SER A 769     2718   3749   3125    133     79     61       C  
ATOM   5541  O   SER A 769     -21.631 -65.709   1.092  1.00 21.53           O  
ANISOU 5541  O   SER A 769     2240   3266   2673     94     43     90       O  
ATOM   5542  CB  SER A 769     -23.522 -67.414  -1.405  1.00 24.71           C  
ANISOU 5542  CB  SER A 769     2731   3680   2978    136    135     17       C  
ATOM   5543  OG  SER A 769     -23.617 -66.083  -1.969  1.00 25.79           O  
ANISOU 5543  OG  SER A 769     2848   3854   3097     79    144     62       O  
ATOM   5544  N   CYS A 770     -20.745 -67.069  -0.489  1.00 23.87           N  
ANISOU 5544  N   CYS A 770     2481   3632   2956    163    118     46       N  
ATOM   5545  CA  CYS A 770     -19.398 -66.580  -0.284  1.00 26.85           C  
ANISOU 5545  CA  CYS A 770     2774   4058   3371    157    114     70       C  
ATOM   5546  C   CYS A 770     -19.226 -65.326  -1.138  1.00 26.88           C  
ANISOU 5546  C   CYS A 770     2743   4115   3355     93    143    106       C  
ATOM   5547  O   CYS A 770     -19.625 -65.304  -2.308  1.00 28.98           O  
ANISOU 5547  O   CYS A 770     3019   4417   3577     83    189    102       O  
ATOM   5548  CB  CYS A 770     -18.374 -67.658  -0.654  1.00 28.44           C  
ANISOU 5548  CB  CYS A 770     2916   4295   3595    225    146     37       C  
ATOM   5549  SG  CYS A 770     -16.699 -67.460   0.055  1.00 35.30           S  
ANISOU 5549  SG  CYS A 770     3676   5209   4528    240    119     62       S  
ATOM   5550  N   LEU A 771     -18.649 -64.278  -0.556  1.00 30.29           N  
ANISOU 5550  N   LEU A 771     3168   4510   3830    202    495   -338       N  
ATOM   5551  CA  LEU A 771     -18.345 -63.096  -1.370  1.00 28.89           C  
ANISOU 5551  CA  LEU A 771     2951   4464   3562    108    573   -265       C  
ATOM   5552  C   LEU A 771     -17.435 -63.450  -2.552  1.00 32.07           C  
ANISOU 5552  C   LEU A 771     3227   5047   3913    122    674   -358       C  
ATOM   5553  O   LEU A 771     -17.654 -62.992  -3.680  1.00 33.51           O  
ANISOU 5553  O   LEU A 771     3401   5364   3965     64    750   -333       O  
ATOM   5554  CB  LEU A 771     -17.716 -62.026  -0.497  1.00 32.12           C  
ANISOU 5554  CB  LEU A 771     3335   4835   4034     45    539   -164       C  
ATOM   5555  CG  LEU A 771     -17.510 -60.725  -1.259  1.00 35.57           C  
ANISOU 5555  CG  LEU A 771     3743   5376   4398    -69    600    -60       C  
ATOM   5556  CD1 LEU A 771     -18.904 -60.121  -1.569  1.00 33.64           C  
ANISOU 5556  CD1 LEU A 771     3625   5085   4070   -116    580     22       C  
ATOM   5557  CD2 LEU A 771     -16.619 -59.772  -0.442  1.00 37.18           C  
ANISOU 5557  CD2 LEU A 771     3889   5544   4694   -127    565     13       C  
ATOM   5558  N   ASP A 772     -16.400 -64.253  -2.310  1.00 31.09           N  
ANISOU 5558  N   ASP A 772     2994   4935   3884    199    673   -467       N  
ATOM   5559  CA  ASP A 772     -15.624 -64.889  -3.374  1.00 33.11           C  
ANISOU 5559  CA  ASP A 772     3121   5357   4102    246    764   -606       C  
ATOM   5560  C   ASP A 772     -16.427 -66.073  -3.877  1.00 34.98           C  
ANISOU 5560  C   ASP A 772     3411   5562   4318    334    748   -736       C  
ATOM   5561  O   ASP A 772     -16.366 -67.159  -3.287  1.00 35.45           O  
ANISOU 5561  O   ASP A 772     3469   5496   4505    435    673   -832       O  
ATOM   5562  CB  ASP A 772     -14.257 -65.334  -2.854  1.00 31.11           C  
ANISOU 5562  CB  ASP A 772     2725   5111   3985    309    753   -687       C  
ATOM   5563  CG  ASP A 772     -13.457 -66.115  -3.873  1.00 38.08           C  
ANISOU 5563  CG  ASP A 772     3460   6160   4849    379    841   -864       C  
ATOM   5564  OD1 ASP A 772     -13.844 -66.195  -5.056  1.00 39.56           O  
ANISOU 5564  OD1 ASP A 772     3644   6491   4893    364    926   -919       O  
ATOM   5565  OD2 ASP A 772     -12.386 -66.637  -3.494  1.00 40.72           O  
ANISOU 5565  OD2 ASP A 772     3669   6495   5310    452    824   -957       O  
ATOM   5566  N   PHE A 773     -17.154 -65.881  -4.995  1.00 34.24           N  
ANISOU 5566  N   PHE A 773     3359   5582   4070    293    811   -740       N  
ATOM   5567  CA  PHE A 773     -18.033 -66.932  -5.524  1.00 35.24           C  
ANISOU 5567  CA  PHE A 773     3542   5677   4170    367    788   -865       C  
ATOM   5568  C   PHE A 773     -17.276 -68.053  -6.235  1.00 36.29           C  
ANISOU 5568  C   PHE A 773     3550   5911   4329    472    832  -1085       C  
ATOM   5569  O   PHE A 773     -17.924 -68.965  -6.756  1.00 39.63           O  
ANISOU 5569  O   PHE A 773     4006   6312   4738    537    811  -1214       O  
ATOM   5570  CB  PHE A 773     -19.060 -66.348  -6.502  1.00 37.61           C  
ANISOU 5570  CB  PHE A 773     3925   6074   4291    291    830   -803       C  
ATOM   5571  CG  PHE A 773     -18.426 -65.564  -7.611  1.00 45.52           C  
ANISOU 5571  CG  PHE A 773     4839   7321   5135    213    949   -773       C  
ATOM   5572  CD1 PHE A 773     -17.687 -66.195  -8.615  1.00 47.89           C  
ANISOU 5572  CD1 PHE A 773     5014   7819   5364    263   1039   -941       C  
ATOM   5573  CD2 PHE A 773     -18.512 -64.179  -7.623  1.00 49.96           C  
ANISOU 5573  CD2 PHE A 773     5435   7922   5627     88    968   -575       C  
ATOM   5574  CE1 PHE A 773     -17.072 -65.471  -9.619  1.00 51.83           C  
ANISOU 5574  CE1 PHE A 773     5423   8570   5702    179   1158   -901       C  
ATOM   5575  CE2 PHE A 773     -17.886 -63.439  -8.645  1.00 52.54           C  
ANISOU 5575  CE2 PHE A 773     5676   8478   5807     -1   1076   -520       C  
ATOM   5576  CZ  PHE A 773     -17.173 -64.089  -9.641  1.00 52.99           C  
ANISOU 5576  CZ  PHE A 773     5608   8752   5773     40   1176   -677       C  
ATOM   5577  N   THR A 774     -15.946 -68.001  -6.325  1.00 35.02           N  
ANISOU 5577  N   THR A 774     3236   5864   4204    491    892  -1143       N  
ATOM   5578  CA  THR A 774     -15.246 -69.196  -6.770  1.00 38.14           C  
ANISOU 5578  CA  THR A 774     3508   6314   4671    617    909  -1376       C  
ATOM   5579  C   THR A 774     -15.211 -70.250  -5.670  1.00 39.24           C  
ANISOU 5579  C   THR A 774     3669   6207   5034    728    773  -1437       C  
ATOM   5580  O   THR A 774     -14.841 -71.389  -5.947  1.00 41.63           O  
ANISOU 5580  O   THR A 774     3892   6492   5433    849    751  -1636       O  
ATOM   5581  CB  THR A 774     -13.807 -68.879  -7.257  1.00 43.37           C  
ANISOU 5581  CB  THR A 774     3977   7193   5308    611   1021  -1440       C  
ATOM   5582  OG1 THR A 774     -13.023 -68.367  -6.187  1.00 43.97           O  
ANISOU 5582  OG1 THR A 774     4011   7184   5512    585    980  -1329       O  
ATOM   5583  CG2 THR A 774     -13.814 -67.853  -8.395  1.00 44.68           C  
ANISOU 5583  CG2 THR A 774     4116   7620   5241    486   1158  -1359       C  
ATOM   5584  N   GLN A 775     -15.644 -69.907  -4.434  1.00 36.10           N  
ANISOU 5584  N   GLN A 775     3381   5617   4719    689    675  -1270       N  
ATOM   5585  CA  GLN A 775     -15.790 -70.889  -3.375  1.00 35.39           C  
ANISOU 5585  CA  GLN A 775     3335   5295   4817    775    537  -1291       C  
ATOM   5586  C   GLN A 775     -17.260 -71.241  -3.147  1.00 31.56           C  
ANISOU 5586  C   GLN A 775     3013   4659   4319    759    464  -1235       C  
ATOM   5587  O   GLN A 775     -18.128 -70.352  -3.081  1.00 31.24           O  
ANISOU 5587  O   GLN A 775     3079   4628   4163    660    482  -1091       O  
ATOM   5588  CB  GLN A 775     -15.177 -70.386  -2.062  1.00 35.70           C  
ANISOU 5588  CB  GLN A 775     3368   5238   4957    750    471  -1154       C  
ATOM   5589  CG  GLN A 775     -13.691 -70.019  -2.169  1.00 39.06           C  
ANISOU 5589  CG  GLN A 775     3622   5800   5419    761    531  -1200       C  
ATOM   5590  CD  GLN A 775     -13.008 -69.983  -0.793  1.00 44.54           C  
ANISOU 5590  CD  GLN A 775     4296   6362   6264    780    425  -1119       C  
ATOM   5591  OE1 GLN A 775     -13.522 -69.410   0.135  1.00 41.84           O  
ANISOU 5591  OE1 GLN A 775     4064   5919   5913    715    363   -962       O  
ATOM   5592  NE2 GLN A 775     -11.852 -70.626  -0.674  1.00 50.70           N  
ANISOU 5592  NE2 GLN A 775     4929   7150   7183    876    399  -1239       N  
ATOM   5593  N   PRO A 776     -17.573 -72.512  -2.985  1.00 31.13           N  
ANISOU 5593  N   PRO A 776     2976   4456   4394    852    373  -1342       N  
ATOM   5594  CA  PRO A 776     -18.974 -72.889  -2.757  1.00 32.03           C  
ANISOU 5594  CA  PRO A 776     3235   4428   4508    827    302  -1286       C  
ATOM   5595  C   PRO A 776     -19.454 -72.390  -1.388  1.00 31.88           C  
ANISOU 5595  C   PRO A 776     3321   4271   4521    759    228  -1078       C  
ATOM   5596  O   PRO A 776     -18.667 -72.235  -0.446  1.00 29.93           O  
ANISOU 5596  O   PRO A 776     3039   3976   4359    769    185  -1012       O  
ATOM   5597  CB  PRO A 776     -18.960 -74.426  -2.866  1.00 35.24           C  
ANISOU 5597  CB  PRO A 776     3610   4697   5083    946    212  -1456       C  
ATOM   5598  CG  PRO A 776     -17.574 -74.845  -2.700  1.00 36.95           C  
ANISOU 5598  CG  PRO A 776     3686   4926   5428   1038    199  -1560       C  
ATOM   5599  CD  PRO A 776     -16.667 -73.684  -3.112  1.00 35.69           C  
ANISOU 5599  CD  PRO A 776     3432   4993   5135    985    330  -1533       C  
ATOM   5600  N   ALA A 777     -20.765 -72.060  -1.311  1.00 31.26           N  
ANISOU 5600  N   ALA A 777     3367   4152   4360    687    219   -981       N  
ATOM   5601  CA  ALA A 777     -21.326 -71.507  -0.073  1.00 30.21           C  
ANISOU 5601  CA  ALA A 777     3329   3919   4230    619    164   -798       C  
ATOM   5602  C   ALA A 777     -21.018 -72.368   1.149  1.00 32.02           C  
ANISOU 5602  C   ALA A 777     3564   3979   4623    667     45   -760       C  
ATOM   5603  O   ALA A 777     -20.846 -71.823   2.255  1.00 31.23           O  
ANISOU 5603  O   ALA A 777     3493   3845   4528    627      8   -629       O  
ATOM   5604  CB  ALA A 777     -22.851 -71.303  -0.198  1.00 27.74           C  
ANISOU 5604  CB  ALA A 777     3133   3575   3834    554    161   -732       C  
ATOM   5605  N   ASP A 778     -20.914 -73.694   0.988  1.00 31.93           N  
ANISOU 5605  N   ASP A 778     3524   3859   4750    753    -26   -871       N  
ATOM   5606  CA  ASP A 778     -20.674 -74.526   2.171  1.00 35.67           C  
ANISOU 5606  CA  ASP A 778     4011   4156   5384    790   -156   -807       C  
ATOM   5607  C   ASP A 778     -19.196 -74.687   2.531  1.00 37.40           C  
ANISOU 5607  C   ASP A 778     4117   4381   5711    865   -189   -851       C  
ATOM   5608  O   ASP A 778     -18.886 -75.402   3.492  1.00 39.18           O  
ANISOU 5608  O   ASP A 778     4347   4463   6078    903   -311   -796       O  
ATOM   5609  CB  ASP A 778     -21.312 -75.907   2.007  1.00 39.76           C  
ANISOU 5609  CB  ASP A 778     4560   4512   6036    840   -248   -876       C  
ATOM   5610  CG  ASP A 778     -20.731 -76.659   0.875  1.00 48.05           C  
ANISOU 5610  CG  ASP A 778     5510   5587   7161    942   -232  -1099       C  
ATOM   5611  OD1 ASP A 778     -19.991 -76.032   0.096  1.00 51.38           O  
ANISOU 5611  OD1 ASP A 778     5845   6187   7492    960   -126  -1193       O  
ATOM   5612  OD2 ASP A 778     -20.997 -77.876   0.748  1.00 51.45           O  
ANISOU 5612  OD2 ASP A 778     5941   5865   7743   1004   -327  -1186       O  
ATOM   5613  N   LYS A 779     -18.276 -74.054   1.802  1.00 34.34           N  
ANISOU 5613  N   LYS A 779     3625   4157   5264    881    -90   -940       N  
ATOM   5614  CA  LYS A 779     -16.851 -74.176   2.074  1.00 35.92           C  
ANISOU 5614  CA  LYS A 779     3698   4380   5571    951   -113   -996       C  
ATOM   5615  C   LYS A 779     -16.198 -72.818   1.898  1.00 38.34           C  
ANISOU 5615  C   LYS A 779     3947   4868   5752    885     -4   -952       C  
ATOM   5616  O   LYS A 779     -15.236 -72.657   1.151  1.00 43.22           O  
ANISOU 5616  O   LYS A 779     4434   5621   6367    921     74  -1067       O  
ATOM   5617  CB  LYS A 779     -16.175 -75.206   1.166  1.00 40.07           C  
ANISOU 5617  CB  LYS A 779     4101   4910   6214   1075   -114  -1217       C  
ATOM   5618  CG  LYS A 779     -16.810 -76.593   1.253  1.00 47.33           C  
ANISOU 5618  CG  LYS A 779     5071   5628   7286   1143   -235  -1276       C  
ATOM   5619  CD  LYS A 779     -16.307 -77.510   0.144  1.00 56.64           C  
ANISOU 5619  CD  LYS A 779     6131   6831   8559   1264   -221  -1533       C  
ATOM   5620  CE  LYS A 779     -16.839 -78.938   0.285  1.00 62.05           C  
ANISOU 5620  CE  LYS A 779     6855   7282   9438   1339   -367  -1599       C  
ATOM   5621  NZ  LYS A 779     -16.808 -79.402   1.713  1.00 65.24           N  
ANISOU 5621  NZ  LYS A 779     7318   7474   9995   1335   -527  -1423       N  
ATOM   5622  N   CYS A 780     -16.711 -71.825   2.584  1.00 36.98           N  
ANISOU 5622  N   CYS A 780     3865   4703   5482    785      2   -789       N  
ATOM   5623  CA  CYS A 780     -16.341 -70.437   2.356  1.00 40.43           C  
ANISOU 5623  CA  CYS A 780     4271   5292   5798    702     99   -732       C  
ATOM   5624  C   CYS A 780     -15.337 -69.984   3.421  1.00 43.50           C  
ANISOU 5624  C   CYS A 780     4606   5668   6257    697     42   -660       C  
ATOM   5625  O   CYS A 780     -15.655 -69.994   4.614  1.00 42.45           O  
ANISOU 5625  O   CYS A 780     4552   5427   6152    679    -55   -550       O  
ATOM   5626  CB  CYS A 780     -17.598 -69.540   2.377  1.00 38.80           C  
ANISOU 5626  CB  CYS A 780     4196   5097   5449    598    135   -613       C  
ATOM   5627  SG  CYS A 780     -17.203 -67.750   2.111  1.00 43.11           S  
ANISOU 5627  SG  CYS A 780     4711   5799   5870    487    234   -526       S  
ATOM   5628  N   ASP A 781     -14.167 -69.515   2.980  1.00 50.00           N  
ANISOU 5628  N   ASP A 781     5291   6616   7090    702    106   -719       N  
ATOM   5629  CA  ASP A 781     -13.107 -69.047   3.874  1.00 55.45           C  
ANISOU 5629  CA  ASP A 781     5907   7310   7853    696     55   -669       C  
ATOM   5630  C   ASP A 781     -13.227 -67.579   4.301  1.00 56.91           C  
ANISOU 5630  C   ASP A 781     6134   7548   7940    577     84   -539       C  
ATOM   5631  O   ASP A 781     -12.805 -67.237   5.418  1.00 61.78           O  
ANISOU 5631  O   ASP A 781     6752   8114   8606    563     -1   -467       O  
ATOM   5632  CB  ASP A 781     -11.739 -69.248   3.220  1.00 63.31           C  
ANISOU 5632  CB  ASP A 781     6713   8419   8925    755    107   -800       C  
ATOM   5633  CG  ASP A 781     -11.368 -70.701   3.121  1.00 70.30           C  
ANISOU 5633  CG  ASP A 781     7532   9220   9958    893     38   -938       C  
ATOM   5634  OD1 ASP A 781     -11.698 -71.413   4.090  1.00 72.21           O  
ANISOU 5634  OD1 ASP A 781     7853   9291  10293    937    -98   -883       O  
ATOM   5635  OD2 ASP A 781     -10.784 -71.141   2.097  1.00 73.63           O  
ANISOU 5635  OD2 ASP A 781     7827   9745  10405    957    113  -1100       O  
ATOM   5636  N   GLY A 782     -13.765 -66.687   3.476  1.00 47.19           N  
ANISOU 5636  N   GLY A 782     4936   6412   6581    493    189   -508       N  
ATOM   5637  CA  GLY A 782     -13.661 -65.292   3.807  1.00 39.31           C  
ANISOU 5637  CA  GLY A 782     3949   5457   5529    388    207   -402       C  
ATOM   5638  C   GLY A 782     -14.984 -64.638   4.124  1.00 32.30           C  
ANISOU 5638  C   GLY A 782     3216   4511   4547    319    193   -301       C  
ATOM   5639  O   GLY A 782     -15.900 -65.228   4.688  1.00 31.01           O  
ANISOU 5639  O   GLY A 782     3159   4245   4379    348    131   -281       O  
ATOM   5640  N   PRO A 783     -15.103 -63.389   3.727  1.00 30.85           N  
ANISOU 5640  N   PRO A 783     3038   4393   4292    224    251   -235       N  
ATOM   5641  CA  PRO A 783     -16.348 -62.652   3.937  1.00 29.47           C  
ANISOU 5641  CA  PRO A 783     2994   4166   4036    162    239   -151       C  
ATOM   5642  C   PRO A 783     -17.532 -63.272   3.169  1.00 25.99           C  
ANISOU 5642  C   PRO A 783     2638   3719   3520    184    276   -177       C  
ATOM   5643  O   PRO A 783     -17.370 -63.939   2.142  1.00 25.38           O  
ANISOU 5643  O   PRO A 783     2511   3711   3421    220    338   -256       O  
ATOM   5644  CB  PRO A 783     -16.011 -61.248   3.401  1.00 32.21           C  
ANISOU 5644  CB  PRO A 783     3299   4591   4348     59    296    -84       C  
ATOM   5645  CG  PRO A 783     -14.482 -61.169   3.458  1.00 33.18           C  
ANISOU 5645  CG  PRO A 783     3272   4781   4554     60    306   -115       C  
ATOM   5646  CD  PRO A 783     -14.065 -62.566   3.071  1.00 33.68           C  
ANISOU 5646  CD  PRO A 783     3271   4874   4651    163    326   -229       C  
ATOM   5647  N   LEU A 784     -18.714 -63.053   3.712  1.00 24.62           N  
ANISOU 5647  N   LEU A 784     2583   3466   3307    163    234   -121       N  
ATOM   5648  CA  LEU A 784     -19.979 -63.576   3.234  1.00 23.53           C  
ANISOU 5648  CA  LEU A 784     2532   3300   3108    177    247   -134       C  
ATOM   5649  C   LEU A 784     -20.679 -62.536   2.352  1.00 27.30           C  
ANISOU 5649  C   LEU A 784     3048   3836   3491    103    304    -83       C  
ATOM   5650  O   LEU A 784     -20.360 -61.352   2.368  1.00 25.74           O  
ANISOU 5650  O   LEU A 784     2831   3665   3285     37    314    -18       O  
ATOM   5651  CB  LEU A 784     -20.875 -63.926   4.428  1.00 24.05           C  
ANISOU 5651  CB  LEU A 784     2694   3255   3190    191    165    -96       C  
ATOM   5652  CG  LEU A 784     -20.292 -64.937   5.387  1.00 27.62           C  
ANISOU 5652  CG  LEU A 784     3123   3640   3730    254     89   -115       C  
ATOM   5653  CD1 LEU A 784     -21.238 -65.188   6.629  1.00 27.96           C  
ANISOU 5653  CD1 LEU A 784     3264   3598   3762    247     13    -52       C  
ATOM   5654  CD2 LEU A 784     -20.069 -66.201   4.561  1.00 30.64           C  
ANISOU 5654  CD2 LEU A 784     3464   4019   4159    324    107   -207       C  
ATOM   5655  N   SER A 785     -21.641 -63.010   1.578  1.00 25.23           N  
ANISOU 5655  N   SER A 785     2837   3582   3165    115    330   -111       N  
ATOM   5656  CA  SER A 785     -22.505 -62.193   0.763  1.00 25.81           C  
ANISOU 5656  CA  SER A 785     2960   3698   3148     57    364    -60       C  
ATOM   5657  C   SER A 785     -23.953 -62.528   1.138  1.00 24.50           C  
ANISOU 5657  C   SER A 785     2897   3447   2966     70    319    -53       C  
ATOM   5658  O   SER A 785     -24.293 -63.711   1.270  1.00 23.29           O  
ANISOU 5658  O   SER A 785     2761   3249   2840    125    298   -114       O  
ATOM   5659  CB  SER A 785     -22.183 -62.527  -0.680  1.00 27.95           C  
ANISOU 5659  CB  SER A 785     3177   4096   3347     60    443   -115       C  
ATOM   5660  OG  SER A 785     -23.004 -61.841  -1.538  1.00 33.53           O  
ANISOU 5660  OG  SER A 785     3931   4852   3957      5    468    -61       O  
ATOM   5661  N   VAL A 786     -24.827 -61.522   1.288  1.00 22.42           N  
ANISOU 5661  N   VAL A 786     2692   3156   2670     21    300     18       N  
ATOM   5662  CA  VAL A 786     -26.201 -61.801   1.727  1.00 20.55           C  
ANISOU 5662  CA  VAL A 786     2536   2850   2424     32    261     20       C  
ATOM   5663  C   VAL A 786     -27.220 -60.976   0.936  1.00 22.89           C  
ANISOU 5663  C   VAL A 786     2876   3167   2656     -9    269     62       C  
ATOM   5664  O   VAL A 786     -26.955 -59.842   0.503  1.00 23.19           O  
ANISOU 5664  O   VAL A 786     2899   3237   2674    -59    278    123       O  
ATOM   5665  CB  VAL A 786     -26.424 -61.532   3.266  1.00 19.93           C  
ANISOU 5665  CB  VAL A 786     2487   2692   2393     33    201     49       C  
ATOM   5666  CG1 VAL A 786     -26.360 -60.004   3.566  1.00 19.01           C  
ANISOU 5666  CG1 VAL A 786     2371   2570   2283    -17    184    105       C  
ATOM   5667  CG2 VAL A 786     -27.837 -62.091   3.767  1.00 17.80           C  
ANISOU 5667  CG2 VAL A 786     2285   2369   2111     45    172     43       C  
ATOM   5668  N   SER A 787     -28.388 -61.581   0.689  1.00 21.51           N  
ANISOU 5668  N   SER A 787     2749   2971   2454      9    257     34       N  
ATOM   5669  CA  SER A 787     -29.581 -60.795   0.338  1.00 22.62           C  
ANISOU 5669  CA  SER A 787     2937   3103   2557    -21    237     75       C  
ATOM   5670  C   SER A 787     -30.773 -61.395   1.063  1.00 23.12           C  
ANISOU 5670  C   SER A 787     3043   3100   2642      1    203     49       C  
ATOM   5671  O   SER A 787     -30.822 -62.605   1.343  1.00 26.96           O  
ANISOU 5671  O   SER A 787     3530   3561   3151     32    200      2       O  
ATOM   5672  CB  SER A 787     -29.866 -60.749  -1.185  1.00 24.82           C  
ANISOU 5672  CB  SER A 787     3217   3465   2751    -38    266     75       C  
ATOM   5673  OG  SER A 787     -29.877 -62.074  -1.726  1.00 28.76           O  
ANISOU 5673  OG  SER A 787     3707   3994   3228      4    288    -14       O  
ATOM   5674  N   SER A 788     -31.749 -60.559   1.365  1.00 21.14           N  
ANISOU 5674  N   SER A 788     2821   2820   2392    -17    172     81       N  
ATOM   5675  CA  SER A 788     -32.888 -61.066   2.114  1.00 23.19           C  
ANISOU 5675  CA  SER A 788     3105   3036   2668     -4    149     58       C  
ATOM   5676  C   SER A 788     -34.150 -60.350   1.713  1.00 21.29           C  
ANISOU 5676  C   SER A 788     2885   2793   2413    -16    125     69       C  
ATOM   5677  O   SER A 788     -34.094 -59.256   1.178  1.00 20.03           O  
ANISOU 5677  O   SER A 788     2724   2641   2245    -34    110    108       O  
ATOM   5678  CB  SER A 788     -32.756 -60.791   3.618  1.00 23.62           C  
ANISOU 5678  CB  SER A 788     3157   3058   2759     -3    129     67       C  
ATOM   5679  OG  SER A 788     -31.478 -61.013   4.082  1.00 28.05           O  
ANISOU 5679  OG  SER A 788     3695   3621   3343      5    134     71       O  
ATOM   5680  N  APHE A 789     -35.294 -60.934   2.095  0.48 20.70           N  
ANISOU 5680  N  APHE A 789     2821   2699   2345     -9    113     42       N  
ATOM   5681  N  BPHE A 789     -35.286 -60.908   2.122  0.52 20.69           N  
ANISOU 5681  N  BPHE A 789     2820   2697   2345     -9    112     43       N  
ATOM   5682  CA APHE A 789     -36.608 -60.392   1.757  0.48 20.30           C  
ANISOU 5682  CA APHE A 789     2777   2646   2291    -13     85     39       C  
ATOM   5683  CA BPHE A 789     -36.520 -60.183   1.890  0.52 20.23           C  
ANISOU 5683  CA BPHE A 789     2766   2633   2286    -14     83     44       C  
ATOM   5684  C  APHE A 789     -37.543 -60.506   2.968  0.48 19.67           C  
ANISOU 5684  C  APHE A 789     2686   2548   2239    -11     77     17       C  
ATOM   5685  C  BPHE A 789     -37.515 -60.459   3.005  0.52 19.64           C  
ANISOU 5685  C  BPHE A 789     2682   2544   2236    -11     77     18       C  
ATOM   5686  O  APHE A 789     -37.434 -61.453   3.757  0.48 19.42           O  
ANISOU 5686  O  APHE A 789     2653   2513   2213    -15     95     11       O  
ATOM   5687  O  BPHE A 789     -37.434 -61.469   3.716  0.52 19.47           O  
ANISOU 5687  O  BPHE A 789     2659   2519   2219    -15     95     10       O  
ATOM   5688  CB APHE A 789     -37.248 -61.162   0.580  0.48 20.45           C  
ANISOU 5688  CB APHE A 789     2806   2688   2277    -13     82     14       C  
ATOM   5689  CB BPHE A 789     -37.137 -60.544   0.547  0.52 20.23           C  
ANISOU 5689  CB BPHE A 789     2777   2661   2248    -16     75     34       C  
ATOM   5690  CG APHE A 789     -36.399 -61.235  -0.689  0.48 21.45           C  
ANISOU 5690  CG APHE A 789     2936   2865   2348    -15     99     20       C  
ATOM   5691  CG BPHE A 789     -37.401 -62.025   0.363  0.52 19.95           C  
ANISOU 5691  CG BPHE A 789     2744   2626   2210     -9     88    -14       C  
ATOM   5692  CD1APHE A 789     -36.427 -60.197  -1.616  0.48 21.39           C  
ANISOU 5692  CD1APHE A 789     2935   2894   2299    -32     81     69       C  
ATOM   5693  CD1BPHE A 789     -38.418 -62.656   1.029  0.52 20.67           C  
ANISOU 5693  CD1BPHE A 789     2829   2690   2334    -15     78    -36       C  
ATOM   5694  CD2APHE A 789     -35.651 -62.383  -0.995  0.48 22.03           C  
ANISOU 5694  CD2APHE A 789     3002   2957   2410     -1    130    -26       C  
ATOM   5695  CD2BPHE A 789     -36.649 -62.762  -0.527  0.52 21.87           C  
ANISOU 5695  CD2BPHE A 789     2988   2900   2422     -1    108    -43       C  
ATOM   5696  CE1APHE A 789     -35.683 -60.253  -2.801  0.48 19.72           C  
ANISOU 5696  CE1APHE A 789     2722   2760   2013    -45    106     82       C  
ATOM   5697  CE1BPHE A 789     -38.668 -64.038   0.811  0.52 20.80           C  
ANISOU 5697  CE1BPHE A 789     2847   2688   2370    -17     77    -75       C  
ATOM   5698  CE2APHE A 789     -34.932 -62.475  -2.201  0.48 24.95           C  
ANISOU 5698  CE2APHE A 789     3363   3402   2715      0    155    -41       C  
ATOM   5699  CE2BPHE A 789     -36.891 -64.108  -0.728  0.52 22.16           C  
ANISOU 5699  CE2BPHE A 789     3025   2919   2477     10    106   -102       C  
ATOM   5700  CZ APHE A 789     -34.957 -61.415  -3.100  0.48 24.31           C  
ANISOU 5700  CZ APHE A 789     3288   3380   2570    -27    149     16       C  
ATOM   5701  CZ BPHE A 789     -37.915 -64.738  -0.058  0.52 19.16           C  
ANISOU 5701  CZ BPHE A 789     2645   2490   2146     -1     85   -112       C  
ATOM   5702  N   ILE A 790     -38.503 -59.579   3.083  1.00 18.19           N  
ANISOU 5702  N   ILE A 790     2486   2356   2070     -6     49      8       N  
ATOM   5703  CA  ILE A 790     -39.652 -59.737   3.980  1.00 19.05           C  
ANISOU 5703  CA  ILE A 790     2569   2476   2193     -5     51    -28       C  
ATOM   5704  C   ILE A 790     -40.904 -59.580   3.113  1.00 21.55           C  
ANISOU 5704  C   ILE A 790     2873   2795   2521      1     21    -46       C  
ATOM   5705  O   ILE A 790     -41.340 -58.447   2.825  1.00 18.85           O  
ANISOU 5705  O   ILE A 790     2519   2437   2207     20    -21    -50       O  
ATOM   5706  CB  ILE A 790     -39.644 -58.710   5.130  1.00 21.74           C  
ANISOU 5706  CB  ILE A 790     2886   2820   2554     10     42    -54       C  
ATOM   5707  CG1 ILE A 790     -38.318 -58.785   5.937  1.00 22.41           C  
ANISOU 5707  CG1 ILE A 790     2983   2906   2625      5     58    -36       C  
ATOM   5708  CG2 ILE A 790     -40.967 -58.859   6.026  1.00 19.63           C  
ANISOU 5708  CG2 ILE A 790     2575   2597   2286     11     55   -104       C  
ATOM   5709  CD1 ILE A 790     -38.059 -57.531   6.829  1.00 22.82           C  
ANISOU 5709  CD1 ILE A 790     3015   2953   2703     22     32    -72       C  
ATOM   5710  N   LEU A 791     -41.513 -60.681   2.743  1.00 21.05           N  
ANISOU 5710  N   LEU A 791     2807   2742   2448    -15     30    -57       N  
ATOM   5711  CA  LEU A 791     -42.633 -60.643   1.776  1.00 23.60           C  
ANISOU 5711  CA  LEU A 791     3118   3071   2779    -12     -7    -76       C  
ATOM   5712  C   LEU A 791     -43.956 -60.502   2.504  1.00 25.55           C  
ANISOU 5712  C   LEU A 791     3310   3335   3062    -12    -11   -115       C  
ATOM   5713  O   LEU A 791     -44.218 -61.269   3.449  1.00 22.61           O  
ANISOU 5713  O   LEU A 791     2915   2984   2692    -38     28   -123       O  
ATOM   5714  CB  LEU A 791     -42.669 -61.921   0.947  1.00 25.80           C  
ANISOU 5714  CB  LEU A 791     3414   3351   3038    -29     -5    -88       C  
ATOM   5715  CG  LEU A 791     -41.467 -62.124   0.021  1.00 30.93           C  
ANISOU 5715  CG  LEU A 791     4103   4007   3643    -23      2    -73       C  
ATOM   5716  CD1 LEU A 791     -41.567 -63.445  -0.798  1.00 28.37           C  
ANISOU 5716  CD1 LEU A 791     3787   3686   3307    -30     -2   -118       C  
ATOM   5717  CD2 LEU A 791     -41.386 -60.932  -0.910  1.00 34.94           C  
ANISOU 5717  CD2 LEU A 791     4622   4535   4117    -12    -32    -40       C  
ATOM   5718  N   PRO A 792     -44.798 -59.534   2.155  1.00 26.81           N  
ANISOU 5718  N   PRO A 792     3440   3492   3254     15    -58   -136       N  
ATOM   5719  CA  PRO A 792     -46.114 -59.451   2.831  1.00 25.58           C  
ANISOU 5719  CA  PRO A 792     3213   3368   3139     20    -56   -190       C  
ATOM   5720  C   PRO A 792     -47.007 -60.642   2.461  1.00 22.51           C  
ANISOU 5720  C   PRO A 792     2799   3000   2753    -16    -51   -202       C  
ATOM   5721  O   PRO A 792     -47.138 -61.010   1.298  1.00 22.34           O  
ANISOU 5721  O   PRO A 792     2802   2962   2724    -20    -90   -194       O  
ATOM   5722  CB  PRO A 792     -46.705 -58.114   2.354  1.00 28.76           C  
ANISOU 5722  CB  PRO A 792     3589   3744   3593     68   -126   -212       C  
ATOM   5723  CG  PRO A 792     -45.885 -57.715   1.152  1.00 33.42           C  
ANISOU 5723  CG  PRO A 792     4245   4293   4159     71   -172   -147       C  
ATOM   5724  CD  PRO A 792     -44.536 -58.392   1.253  1.00 30.76           C  
ANISOU 5724  CD  PRO A 792     3963   3961   3763     41   -117   -107       C  
ATOM   5725  N   HIS A 793     -47.614 -61.245   3.477  1.00 21.27           N  
ANISOU 5725  N   HIS A 793     2591   2886   2605    -49     -3   -220       N  
ATOM   5726  CA  HIS A 793     -48.506 -62.392   3.309  1.00 22.99           C  
ANISOU 5726  CA  HIS A 793     2773   3118   2845    -98      2   -224       C  
ATOM   5727  C   HIS A 793     -49.924 -61.873   3.038  1.00 25.26           C  
ANISOU 5727  C   HIS A 793     2978   3437   3182    -80    -33   -280       C  
ATOM   5728  O   HIS A 793     -50.737 -61.701   3.948  1.00 26.18           O  
ANISOU 5728  O   HIS A 793     3013   3616   3317    -90      2   -316       O  
ATOM   5729  CB  HIS A 793     -48.442 -63.252   4.571  1.00 20.81           C  
ANISOU 5729  CB  HIS A 793     2476   2878   2553   -155     68   -193       C  
ATOM   5730  CG  HIS A 793     -49.242 -64.510   4.473  1.00 21.32           C  
ANISOU 5730  CG  HIS A 793     2506   2941   2654   -221     70   -178       C  
ATOM   5731  ND1 HIS A 793     -49.841 -65.105   5.574  1.00 20.14           N  
ANISOU 5731  ND1 HIS A 793     2297   2852   2506   -287    122   -150       N  
ATOM   5732  CD2 HIS A 793     -49.564 -65.272   3.388  1.00 19.35           C  
ANISOU 5732  CD2 HIS A 793     2268   2640   2444   -238     22   -189       C  
ATOM   5733  CE1 HIS A 793     -50.502 -66.189   5.156  1.00 22.66           C  
ANISOU 5733  CE1 HIS A 793     2592   3140   2880   -346    102   -134       C  
ATOM   5734  NE2 HIS A 793     -50.331 -66.320   3.842  1.00 20.47           N  
ANISOU 5734  NE2 HIS A 793     2358   2790   2629   -313     39   -167       N  
ATOM   5735  N   ARG A 794     -50.240 -61.596   1.770  1.00 23.83           N  
ANISOU 5735  N   ARG A 794     2812   3225   3018    -53   -106   -292       N  
ATOM   5736  CA AARG A 794     -51.505 -60.945   1.496  0.25 23.37           C  
ANISOU 5736  CA AARG A 794     2674   3189   3017    -23   -156   -344       C  
ATOM   5737  CA BARG A 794     -51.504 -60.944   1.493  0.25 23.37           C  
ANISOU 5737  CA BARG A 794     2674   3188   3016    -22   -157   -344       C  
ATOM   5738  CA CARG A 794     -51.487 -60.922   1.429  0.50 23.15           C  
ANISOU 5738  CA CARG A 794     2649   3159   2989    -21   -160   -343       C  
ATOM   5739  C   ARG A 794     -52.471 -61.894   0.791  1.00 23.07           C  
ANISOU 5739  C   ARG A 794     2598   3160   3010    -61   -190   -364       C  
ATOM   5740  O   ARG A 794     -52.053 -62.805   0.095  1.00 23.66           O  
ANISOU 5740  O   ARG A 794     2728   3204   3057    -93   -203   -342       O  
ATOM   5741  CB AARG A 794     -51.283 -59.685   0.652  0.25 23.82           C  
ANISOU 5741  CB AARG A 794     2763   3204   3083     42   -237   -336       C  
ATOM   5742  CB BARG A 794     -51.275 -59.690   0.641  0.25 23.81           C  
ANISOU 5742  CB BARG A 794     2763   3203   3081     42   -237   -336       C  
ATOM   5743  CB CARG A 794     -51.218 -59.765   0.462  0.50 23.65           C  
ANISOU 5743  CB CARG A 794     2752   3178   3054     40   -243   -330       C  
ATOM   5744  CG AARG A 794     -50.501 -58.601   1.435  0.25 24.32           C  
ANISOU 5744  CG AARG A 794     2844   3248   3147     81   -217   -332       C  
ATOM   5745  CG BARG A 794     -50.421 -58.640   1.390  0.25 24.29           C  
ANISOU 5745  CG BARG A 794     2847   3243   3139     79   -217   -327       C  
ATOM   5746  CG CARG A 794     -50.177 -58.755   1.003  0.50 24.40           C  
ANISOU 5746  CG CARG A 794     2890   3244   3137     74   -228   -306       C  
ATOM   5747  CD AARG A 794     -50.296 -57.340   0.624  0.25 25.03           C  
ANISOU 5747  CD AARG A 794     2964   3280   3268    134   -308   -307       C  
ATOM   5748  CD BARG A 794     -50.209 -57.384   0.572  0.25 24.99           C  
ANISOU 5748  CD BARG A 794     2966   3273   3256    131   -307   -301       C  
ATOM   5749  CD CARG A 794     -50.806 -57.842   2.093  0.50 24.16           C  
ANISOU 5749  CD CARG A 794     2775   3236   3169    116   -218   -376       C  
ATOM   5750  NE AARG A 794     -51.565 -56.896   0.072  0.25 25.79           N  
ANISOU 5750  NE AARG A 794     2992   3373   3433    170   -390   -345       N  
ATOM   5751  NE BARG A 794     -51.482 -56.910   0.052  0.25 25.74           N  
ANISOU 5751  NE BARG A 794     2992   3365   3421    168   -388   -340       N  
ATOM   5752  NE CARG A 794     -52.150 -57.454   1.700  0.50 26.59           N  
ANISOU 5752  NE CARG A 794     2999   3554   3551    149   -281   -431       N  
ATOM   5753  CZ AARG A 794     -51.747 -55.739  -0.547  0.25 25.36           C  
ANISOU 5753  CZ AARG A 794     2939   3262   3434    221   -490   -327       C  
ATOM   5754  CZ BARG A 794     -51.657 -55.737  -0.537  0.25 25.27           C  
ANISOU 5754  CZ BARG A 794     2934   3250   3419    220   -487   -323       C  
ATOM   5755  CZ CARG A 794     -53.227 -57.471   2.483  0.50 29.75           C  
ANISOU 5755  CZ CARG A 794     3287   4018   3998    157   -251   -513       C  
ATOM   5756  NH1AARG A 794     -50.732 -54.904  -0.697  0.25 23.45           N  
ANISOU 5756  NH1AARG A 794     2763   2960   3186    234   -517   -265       N  
ATOM   5757  NH1BARG A 794     -50.634 -54.914  -0.682  0.25 23.39           N  
ANISOU 5757  NH1BARG A 794     2761   2952   3173    231   -512   -261       N  
ATOM   5758  NH1CARG A 794     -54.401 -57.162   1.956  0.50 32.98           N  
ANISOU 5758  NH1CARG A 794     3618   4430   4482    190   -320   -560       N  
ATOM   5759  NH2AARG A 794     -52.952 -55.437  -1.024  0.25 26.43           N  
ANISOU 5759  NH2AARG A 794     3005   3396   3639    256   -572   -364       N  
ATOM   5760  NH2BARG A 794     -52.864 -55.406  -0.987  0.25 26.49           N  
ANISOU 5760  NH2BARG A 794     3017   3401   3645    256   -569   -362       N  
ATOM   5761  NH2CARG A 794     -53.134 -57.795   3.772  0.50 28.67           N  
ANISOU 5761  NH2CARG A 794     3111   3952   3829    130   -154   -545       N  
ATOM   5762  N   PRO A 795     -53.782 -61.709   0.972  1.00 23.94           N  
ANISOU 5762  N   PRO A 795     2603   3311   3183    -59   -207   -417       N  
ATOM   5763  CA  PRO A 795     -54.747 -62.636   0.347  1.00 22.03           C  
ANISOU 5763  CA  PRO A 795     2312   3076   2981   -104   -244   -439       C  
ATOM   5764  C   PRO A 795     -54.964 -62.376  -1.133  1.00 23.91           C  
ANISOU 5764  C   PRO A 795     2583   3284   3218    -67   -353   -450       C  
ATOM   5765  O   PRO A 795     -55.684 -63.139  -1.751  1.00 22.63           O  
ANISOU 5765  O   PRO A 795     2388   3125   3085   -101   -397   -478       O  
ATOM   5766  CB  PRO A 795     -56.066 -62.402   1.151  1.00 22.70           C  
ANISOU 5766  CB  PRO A 795     2254   3235   3136   -111   -218   -496       C  
ATOM   5767  CG  PRO A 795     -55.939 -60.925   1.558  1.00 25.41           C  
ANISOU 5767  CG  PRO A 795     2580   3588   3487    -25   -227   -530       C  
ATOM   5768  CD  PRO A 795     -54.431 -60.806   1.957  1.00 24.13           C  
ANISOU 5768  CD  PRO A 795     2532   3390   3248    -23   -179   -471       C  
ATOM   5769  N   ASP A 796     -54.390 -61.316  -1.711  1.00 26.73           N  
ANISOU 5769  N   ASP A 796     3000   3615   3541     -5   -404   -424       N  
ATOM   5770  CA  ASP A 796     -54.526 -61.046  -3.135  1.00 28.00           C  
ANISOU 5770  CA  ASP A 796     3199   3763   3675     22   -510   -414       C  
ATOM   5771  C   ASP A 796     -53.191 -60.497  -3.627  1.00 25.22           C  
ANISOU 5771  C   ASP A 796     2958   3386   3238     43   -514   -345       C  
ATOM   5772  O   ASP A 796     -52.307 -60.134  -2.834  1.00 25.27           O  
ANISOU 5772  O   ASP A 796     2995   3374   3231     49   -448   -316       O  
ATOM   5773  CB  ASP A 796     -55.650 -60.049  -3.414  1.00 30.99           C  
ANISOU 5773  CB  ASP A 796     3498   4148   4129     76   -603   -443       C  
ATOM   5774  CG  ASP A 796     -55.415 -58.717  -2.652  1.00 37.83           C  
ANISOU 5774  CG  ASP A 796     4348   4988   5040    136   -595   -437       C  
ATOM   5775  OD1 ASP A 796     -54.324 -58.081  -2.754  1.00 35.98           O  
ANISOU 5775  OD1 ASP A 796     4199   4714   4759    155   -593   -376       O  
ATOM   5776  OD2 ASP A 796     -56.297 -58.362  -1.850  1.00 45.34           O  
ANISOU 5776  OD2 ASP A 796     5189   5961   6076    161   -581   -504       O  
ATOM   5777  N   ASN A 797     -53.042 -60.408  -4.940  1.00 23.70           N  
ANISOU 5777  N   ASN A 797     2819   3204   2982     52   -591   -318       N  
ATOM   5778  CA  ASN A 797     -51.830 -59.830  -5.517  1.00 23.31           C  
ANISOU 5778  CA  ASN A 797     2862   3150   2844     63   -595   -242       C  
ATOM   5779  C   ASN A 797     -52.170 -58.480  -6.140  1.00 24.95           C  
ANISOU 5779  C   ASN A 797     3070   3342   3069    106   -702   -185       C  
ATOM   5780  O   ASN A 797     -51.620 -58.104  -7.170  1.00 23.92           O  
ANISOU 5780  O   ASN A 797     3005   3233   2851    103   -752   -114       O  
ATOM   5781  CB  ASN A 797     -51.188 -60.787  -6.524  1.00 21.81           C  
ANISOU 5781  CB  ASN A 797     2738   3003   2545     31   -590   -247       C  
ATOM   5782  CG  ASN A 797     -50.493 -61.945  -5.820  1.00 28.30           C  
ANISOU 5782  CG  ASN A 797     3575   3811   3367     -3   -489   -284       C  
ATOM   5783  OD1 ASN A 797     -50.837 -63.143  -5.984  1.00 27.62           O  
ANISOU 5783  OD1 ASN A 797     3472   3728   3293    -32   -486   -348       O  
ATOM   5784  ND2 ASN A 797     -49.557 -61.600  -5.017  1.00 20.41           N  
ANISOU 5784  ND2 ASN A 797     2601   2787   2367      0   -420   -244       N  
ATOM   5785  N   ASP A 798     -53.069 -57.732  -5.500  1.00 25.80           N  
ANISOU 5785  N   ASP A 798     3098   3414   3291    147   -738   -215       N  
ATOM   5786  CA  ASP A 798     -53.426 -56.407  -6.001  1.00 26.70           C  
ANISOU 5786  CA  ASP A 798     3205   3486   3455    196   -856   -162       C  
ATOM   5787  C   ASP A 798     -52.224 -55.488  -6.113  1.00 27.38           C  
ANISOU 5787  C   ASP A 798     3369   3528   3504    198   -858    -61       C  
ATOM   5788  O   ASP A 798     -52.269 -54.511  -6.899  1.00 26.80           O  
ANISOU 5788  O   ASP A 798     3321   3422   3439    217   -970     26       O  
ATOM   5789  CB  ASP A 798     -54.468 -55.761  -5.087  1.00 27.81           C  
ANISOU 5789  CB  ASP A 798     3234   3588   3742    251   -881   -237       C  
ATOM   5790  CG  ASP A 798     -55.839 -56.443  -5.256  1.00 34.27           C  
ANISOU 5790  CG  ASP A 798     3959   4454   4610    250   -914   -319       C  
ATOM   5791  OD1 ASP A 798     -55.938 -57.352  -6.134  1.00 32.17           O  
ANISOU 5791  OD1 ASP A 798     3724   4234   4264    209   -933   -314       O  
ATOM   5792  OD2 ASP A 798     -56.786 -56.107  -4.511  1.00 38.58           O  
ANISOU 5792  OD2 ASP A 798     4394   4996   5271    289   -920   -399       O  
ATOM   5793  N   GLU A 799     -51.180 -55.745  -5.308  1.00 24.44           N  
ANISOU 5793  N   GLU A 799     3030   3150   3104    174   -746    -62       N  
ATOM   5794  CA  GLU A 799     -49.989 -54.908  -5.379  1.00 25.76           C  
ANISOU 5794  CA  GLU A 799     3263   3278   3246    166   -744     31       C  
ATOM   5795  C   GLU A 799     -49.282 -55.045  -6.740  1.00 28.25           C  
ANISOU 5795  C   GLU A 799     3659   3650   3426    124   -771    131       C  
ATOM   5796  O   GLU A 799     -48.654 -54.093  -7.209  1.00 27.03           O  
ANISOU 5796  O   GLU A 799     3547   3466   3257    114   -821    241       O  
ATOM   5797  CB  GLU A 799     -49.024 -55.268  -4.222  1.00 25.47           C  
ANISOU 5797  CB  GLU A 799     3238   3235   3203    148   -620     -1       C  
ATOM   5798  CG  GLU A 799     -47.733 -54.392  -4.176  1.00 24.35           C  
ANISOU 5798  CG  GLU A 799     3152   3049   3051    135   -614     87       C  
ATOM   5799  CD  GLU A 799     -46.797 -54.778  -2.997  1.00 29.77           C  
ANISOU 5799  CD  GLU A 799     3843   3735   3733    121   -502     48       C  
ATOM   5800  OE1 GLU A 799     -47.111 -55.754  -2.223  1.00 27.69           O  
ANISOU 5800  OE1 GLU A 799     3548   3508   3465    117   -428    -33       O  
ATOM   5801  OE2 GLU A 799     -45.741 -54.091  -2.874  1.00 31.80           O  
ANISOU 5801  OE2 GLU A 799     4134   3954   3992    108   -497    109       O  
ATOM   5802  N   SER A 800     -49.438 -56.186  -7.423  1.00 26.36           N  
ANISOU 5802  N   SER A 800     3434   3494   3089     98   -749     92       N  
ATOM   5803  CA  SER A 800     -48.730 -56.420  -8.680  1.00 26.64           C  
ANISOU 5803  CA  SER A 800     3537   3613   2974     60   -759    161       C  
ATOM   5804  C   SER A 800     -49.732 -56.297  -9.816  1.00 27.31           C  
ANISOU 5804  C   SER A 800     3614   3742   3020     69   -882    180       C  
ATOM   5805  O   SER A 800     -50.569 -57.195 -10.011  1.00 24.44           O  
ANISOU 5805  O   SER A 800     3216   3415   2655     74   -896     86       O  
ATOM   5806  CB  SER A 800     -48.062 -57.798  -8.699  1.00 22.53           C  
ANISOU 5806  CB  SER A 800     3037   3159   2365     32   -653     86       C  
ATOM   5807  OG  SER A 800     -47.303 -57.984  -7.540  1.00 21.52           O  
ANISOU 5807  OG  SER A 800     2904   2983   2288     29   -554     62       O  
ATOM   5808  N   CYS A 801     -49.656 -55.184 -10.573  1.00 25.31           N  
ANISOU 5808  N   CYS A 801     3392   3483   2741     66   -981    310       N  
ATOM   5809  CA  CYS A 801     -50.685 -54.945 -11.570  1.00 31.30           C  
ANISOU 5809  CA  CYS A 801     4140   4275   3477     80  -1120    340       C  
ATOM   5810  C   CYS A 801     -50.710 -55.981 -12.689  1.00 30.99           C  
ANISOU 5810  C   CYS A 801     4130   4377   3267     49  -1119    301       C  
ATOM   5811  O   CYS A 801     -51.742 -56.087 -13.387  1.00 28.05           O  
ANISOU 5811  O   CYS A 801     3734   4040   2882     65  -1229    281       O  
ATOM   5812  CB  CYS A 801     -50.559 -53.529 -12.180  1.00 38.14           C  
ANISOU 5812  CB  CYS A 801     5039   5100   4352     76  -1241    512       C  
ATOM   5813  SG  CYS A 801     -50.911 -52.203 -10.899  1.00 39.35           S  
ANISOU 5813  SG  CYS A 801     5135   5059   4759    137  -1292    520       S  
ATOM   5814  N   ASN A 802     -49.668 -56.775 -12.914  1.00 27.61           N  
ANISOU 5814  N   ASN A 802     3745   4035   2712     12  -1010    272       N  
ATOM   5815  CA  ASN A 802     -49.926 -57.780 -13.950  1.00 35.04           C  
ANISOU 5815  CA  ASN A 802     4698   5103   3513     -3  -1029    196       C  
ATOM   5816  C   ASN A 802     -49.804 -59.179 -13.400  1.00 33.26           C  
ANISOU 5816  C   ASN A 802     4449   4876   3313     -1   -927     35       C  
ATOM   5817  O   ASN A 802     -49.349 -60.110 -14.090  1.00 31.26           O  
ANISOU 5817  O   ASN A 802     4219   4724   2934    -18   -890    -40       O  
ATOM   5818  CB  ASN A 802     -49.045 -57.612 -15.185  1.00 45.05           C  
ANISOU 5818  CB  ASN A 802     6030   6520   4568    -46  -1031    286       C  
ATOM   5819  CG  ASN A 802     -47.830 -56.901 -14.892  1.00 52.46           C  
ANISOU 5819  CG  ASN A 802     7001   7444   5488    -76   -958    401       C  
ATOM   5820  OD1 ASN A 802     -47.533 -55.862 -15.519  1.00 57.69           O  
ANISOU 5820  OD1 ASN A 802     7697   8138   6083   -109  -1020    566       O  
ATOM   5821  ND2 ASN A 802     -47.126 -57.371 -13.872  1.00 52.15           N  
ANISOU 5821  ND2 ASN A 802     6948   7342   5523    -70   -835    329       N  
ATOM   5822  N   SER A 803     -50.294 -59.355 -12.177  1.00 30.15           N  
ANISOU 5822  N   SER A 803     4001   4368   3085     20   -891    -25       N  
ATOM   5823  CA  SER A 803     -50.213 -60.676 -11.569  1.00 31.30           C  
ANISOU 5823  CA  SER A 803     4124   4494   3273     12   -805   -153       C  
ATOM   5824  C   SER A 803     -51.153 -61.678 -12.241  1.00 32.90           C  
ANISOU 5824  C   SER A 803     4297   4741   3461      8   -868   -266       C  
ATOM   5825  O   SER A 803     -51.025 -62.885 -12.012  1.00 32.29           O  
ANISOU 5825  O   SER A 803     4209   4653   3406     -5   -815   -373       O  
ATOM   5826  CB  SER A 803     -50.523 -60.537 -10.068  1.00 26.99           C  
ANISOU 5826  CB  SER A 803     3527   3836   2894     25   -751   -169       C  
ATOM   5827  OG  SER A 803     -51.862 -60.089  -9.939  1.00 27.63           O  
ANISOU 5827  OG  SER A 803     3543   3882   3074     48   -840   -180       O  
ATOM   5828  N   SER A 804     -52.087 -61.232 -13.088  1.00 37.16           N  
ANISOU 5828  N   SER A 804     4822   5324   3972     19   -993   -245       N  
ATOM   5829  CA  SER A 804     -52.859 -62.253 -13.797  1.00 40.06           C  
ANISOU 5829  CA  SER A 804     5163   5743   4314     11  -1056   -365       C  
ATOM   5830  C   SER A 804     -52.019 -62.984 -14.851  1.00 40.36           C  
ANISOU 5830  C   SER A 804     5260   5902   4174     -4  -1035   -422       C  
ATOM   5831  O   SER A 804     -52.458 -63.986 -15.407  1.00 40.86           O  
ANISOU 5831  O   SER A 804     5305   6004   4214    -10  -1075   -549       O  
ATOM   5832  CB  SER A 804     -54.090 -61.615 -14.424  1.00 43.30           C  
ANISOU 5832  CB  SER A 804     5536   6174   4741     30  -1204   -334       C  
ATOM   5833  OG  SER A 804     -53.678 -60.798 -15.501  1.00 47.37           O  
ANISOU 5833  OG  SER A 804     6115   6786   5097     29  -1272   -224       O  
ATOM   5834  N   GLU A 805     -50.810 -62.532 -15.113  1.00 41.75           N  
ANISOU 5834  N   GLU A 805     5495   6139   4230    -12   -970   -344       N  
ATOM   5835  CA  GLU A 805     -49.936 -63.186 -16.068  1.00 41.74           C  
ANISOU 5835  CA  GLU A 805     5536   6273   4052    -23   -934   -410       C  
ATOM   5836  C   GLU A 805     -49.089 -64.249 -15.364  1.00 36.22           C  
ANISOU 5836  C   GLU A 805     4831   5518   3413    -20   -814   -518       C  
ATOM   5837  O   GLU A 805     -49.158 -64.427 -14.142  1.00 30.01           O  
ANISOU 5837  O   GLU A 805     4017   4596   2790    -18   -762   -518       O  
ATOM   5838  CB  GLU A 805     -49.064 -62.137 -16.748  1.00 46.36           C  
ANISOU 5838  CB  GLU A 805     6174   6968   4471    -41   -924   -261       C  
ATOM   5839  CG  GLU A 805     -49.855 -61.234 -17.673  1.00 55.47           C  
ANISOU 5839  CG  GLU A 805     7341   8195   5541    -48  -1063   -153       C  
ATOM   5840  CD  GLU A 805     -48.956 -60.407 -18.569  1.00 62.99           C  
ANISOU 5840  CD  GLU A 805     8349   9291   6294    -84  -1057     -6       C  
ATOM   5841  OE1 GLU A 805     -48.240 -59.534 -18.027  1.00 64.99           O  
ANISOU 5841  OE1 GLU A 805     8619   9485   6589   -100  -1004    129       O  
ATOM   5842  OE2 GLU A 805     -48.938 -60.645 -19.802  1.00 66.08           O  
ANISOU 5842  OE2 GLU A 805     8764   9861   6483   -101  -1103    -28       O  
ATOM   5843  N   ASP A 806     -48.241 -64.925 -16.144  1.00 37.14           N  
ANISOU 5843  N   ASP A 806     4972   5750   3391    -18   -772   -607       N  
ATOM   5844  CA  ASP A 806     -47.307 -65.898 -15.586  1.00 34.91           C  
ANISOU 5844  CA  ASP A 806     4682   5418   3163     -7   -669   -708       C  
ATOM   5845  C   ASP A 806     -46.384 -65.236 -14.578  1.00 33.44           C  
ANISOU 5845  C   ASP A 806     4508   5162   3035    -11   -572   -589       C  
ATOM   5846  O   ASP A 806     -45.968 -64.080 -14.737  1.00 31.56           O  
ANISOU 5846  O   ASP A 806     4295   4975   2721    -27   -562   -446       O  
ATOM   5847  CB  ASP A 806     -46.460 -66.539 -16.687  1.00 39.48           C  
ANISOU 5847  CB  ASP A 806     5276   6156   3567      6   -640   -826       C  
ATOM   5848  CG  ASP A 806     -45.667 -67.745 -16.177  1.00 43.05           C  
ANISOU 5848  CG  ASP A 806     5709   6539   4110     31   -563   -969       C  
ATOM   5849  OD1 ASP A 806     -46.238 -68.850 -16.137  1.00 44.93           O  
ANISOU 5849  OD1 ASP A 806     5922   6702   4449     44   -610  -1117       O  
ATOM   5850  OD2 ASP A 806     -44.502 -67.581 -15.760  1.00 43.14           O  
ANISOU 5850  OD2 ASP A 806     5727   6553   4112     38   -464   -929       O  
ATOM   5851  N   GLU A 807     -46.053 -65.995 -13.529  1.00 30.58           N  
ANISOU 5851  N   GLU A 807     4126   4677   2815     -2   -509   -647       N  
ATOM   5852  CA  GLU A 807     -45.164 -65.490 -12.478  1.00 28.94           C  
ANISOU 5852  CA  GLU A 807     3925   4400   2671     -5   -421   -552       C  
ATOM   5853  C   GLU A 807     -43.838 -64.939 -13.022  1.00 26.77           C  
ANISOU 5853  C   GLU A 807     3676   4243   2253     -8   -354   -496       C  
ATOM   5854  O   GLU A 807     -43.229 -64.041 -12.412  1.00 26.35           O  
ANISOU 5854  O   GLU A 807     3632   4159   2220    -21   -308   -374       O  
ATOM   5855  CB  GLU A 807     -44.915 -66.609 -11.445  1.00 28.99           C  
ANISOU 5855  CB  GLU A 807     3909   4281   2826      5   -373   -635       C  
ATOM   5856  CG  GLU A 807     -46.150 -66.873 -10.524  1.00 28.75           C  
ANISOU 5856  CG  GLU A 807     3844   4123   2955    -12   -416   -632       C  
ATOM   5857  CD  GLU A 807     -47.263 -67.744 -11.188  1.00 33.65           C  
ANISOU 5857  CD  GLU A 807     4438   4743   3603    -19   -503   -748       C  
ATOM   5858  OE1 GLU A 807     -47.095 -68.167 -12.350  1.00 34.72           O  
ANISOU 5858  OE1 GLU A 807     4587   4974   3630     -4   -537   -843       O  
ATOM   5859  OE2 GLU A 807     -48.317 -67.982 -10.549  1.00 34.40           O  
ANISOU 5859  OE2 GLU A 807     4494   4753   3824    -41   -539   -747       O  
ATOM   5860  N   SER A 808     -43.402 -65.407 -14.185  1.00 29.90           N  
ANISOU 5860  N   SER A 808     4078   4786   2498     -1   -349   -583       N  
ATOM   5861  CA  SER A 808     -42.150 -64.907 -14.724  1.00 30.98           C  
ANISOU 5861  CA  SER A 808     4225   5058   2490    -14   -275   -529       C  
ATOM   5862  C   SER A 808     -42.206 -63.401 -14.992  1.00 34.36           C  
ANISOU 5862  C   SER A 808     4679   5536   2839    -56   -302   -330       C  
ATOM   5863  O   SER A 808     -41.165 -62.757 -15.090  1.00 36.36           O  
ANISOU 5863  O   SER A 808     4937   5859   3021    -82   -236   -236       O  
ATOM   5864  CB  SER A 808     -41.810 -65.699 -16.004  1.00 28.28           C  
ANISOU 5864  CB  SER A 808     3873   4893   1980      3   -268   -677       C  
ATOM   5865  OG  SER A 808     -42.767 -65.474 -17.032  1.00 29.41           O  
ANISOU 5865  OG  SER A 808     4033   5139   2003    -12   -364   -675       O  
ATOM   5866  N   LYS A 809     -43.396 -62.816 -15.024  1.00 36.13           N  
ANISOU 5866  N   LYS A 809     4915   5709   3103    -64   -402   -260       N  
ATOM   5867  CA  LYS A 809     -43.581 -61.427 -15.414  1.00 34.60           C  
ANISOU 5867  CA  LYS A 809     4747   5552   2848    -99   -458    -76       C  
ATOM   5868  C   LYS A 809     -43.785 -60.487 -14.226  1.00 33.93           C  
ANISOU 5868  C   LYS A 809     4658   5297   2935   -100   -469     38       C  
ATOM   5869  O   LYS A 809     -43.920 -59.282 -14.434  1.00 34.86           O  
ANISOU 5869  O   LYS A 809     4795   5411   3041   -125   -527    192       O  
ATOM   5870  CB  LYS A 809     -44.785 -61.335 -16.380  1.00 37.49           C  
ANISOU 5870  CB  LYS A 809     5123   5986   3137   -100   -584    -78       C  
ATOM   5871  CG  LYS A 809     -44.605 -62.031 -17.777  1.00 41.76           C  
ANISOU 5871  CG  LYS A 809     5672   6736   3459   -106   -592   -177       C  
ATOM   5872  CD  LYS A 809     -45.708 -61.484 -18.701  1.00 45.59           C  
ANISOU 5872  CD  LYS A 809     6175   7291   3856   -119   -733   -107       C  
ATOM   5873  CE  LYS A 809     -45.802 -62.189 -20.003  1.00 49.99           C  
ANISOU 5873  CE  LYS A 809     6738   8050   4207   -120   -765   -223       C  
ATOM   5874  NZ  LYS A 809     -46.732 -61.453 -20.951  1.00 53.66           N  
ANISOU 5874  NZ  LYS A 809     7227   8603   4558   -142   -911   -111       N  
ATOM   5875  N   TRP A 810     -43.806 -60.980 -12.986  1.00 31.46           N  
ANISOU 5875  N   TRP A 810     4321   4848   2783    -73   -422    -31       N  
ATOM   5876  CA  TRP A 810     -44.120 -60.063 -11.881  1.00 29.62           C  
ANISOU 5876  CA  TRP A 810     4079   4475   2701    -69   -440     57       C  
ATOM   5877  C   TRP A 810     -43.575 -60.490 -10.522  1.00 27.03           C  
ANISOU 5877  C   TRP A 810     3732   4043   2498    -54   -355      9       C  
ATOM   5878  O   TRP A 810     -43.329 -59.629  -9.663  1.00 24.34           O  
ANISOU 5878  O   TRP A 810     3387   3619   2241    -56   -344     86       O  
ATOM   5879  CB  TRP A 810     -45.639 -59.849 -11.772  1.00 28.83           C  
ANISOU 5879  CB  TRP A 810     3956   4307   2689    -48   -544     46       C  
ATOM   5880  CG  TRP A 810     -46.452 -61.117 -11.500  1.00 23.74           C  
ANISOU 5880  CG  TRP A 810     3278   3632   2109    -29   -547   -103       C  
ATOM   5881  CD1 TRP A 810     -46.952 -62.007 -12.444  1.00 24.60           C  
ANISOU 5881  CD1 TRP A 810     3386   3820   2142    -28   -590   -201       C  
ATOM   5882  CD2 TRP A 810     -46.890 -61.588 -10.229  1.00 22.75           C  
ANISOU 5882  CD2 TRP A 810     3114   3393   2138    -16   -513   -161       C  
ATOM   5883  NE1 TRP A 810     -47.671 -63.007 -11.830  1.00 24.20           N  
ANISOU 5883  NE1 TRP A 810     3295   3692   2208    -19   -590   -313       N  
ATOM   5884  CE2 TRP A 810     -47.631 -62.789 -10.462  1.00 23.08           C  
ANISOU 5884  CE2 TRP A 810     3129   3437   2201    -16   -537   -282       C  
ATOM   5885  CE3 TRP A 810     -46.726 -61.120  -8.898  1.00 23.04           C  
ANISOU 5885  CE3 TRP A 810     3132   3332   2290    -10   -466   -124       C  
ATOM   5886  CZ2 TRP A 810     -48.190 -63.516  -9.433  1.00 22.49           C  
ANISOU 5886  CZ2 TRP A 810     3011   3272   2260    -19   -513   -344       C  
ATOM   5887  CZ3 TRP A 810     -47.302 -61.862  -7.861  1.00 21.82           C  
ANISOU 5887  CZ3 TRP A 810     2934   3107   2250     -8   -437   -194       C  
ATOM   5888  CH2 TRP A 810     -48.015 -63.052  -8.139  1.00 21.56           C  
ANISOU 5888  CH2 TRP A 810     2877   3078   2236    -18   -458   -293       C  
ATOM   5889  N   VAL A 811     -43.364 -61.791 -10.276  1.00 24.11           N  
ANISOU 5889  N   VAL A 811     3348   3668   2146    -39   -302   -116       N  
ATOM   5890  CA  VAL A 811     -42.985 -62.190  -8.914  1.00 22.29           C  
ANISOU 5890  CA  VAL A 811     3100   3331   2038    -29   -240   -144       C  
ATOM   5891  C   VAL A 811     -41.626 -61.627  -8.534  1.00 23.67           C  
ANISOU 5891  C   VAL A 811     3284   3512   2196    -39   -171    -75       C  
ATOM   5892  O   VAL A 811     -41.453 -61.108  -7.429  1.00 25.04           O  
ANISOU 5892  O   VAL A 811     3450   3602   2462    -38   -152    -29       O  
ATOM   5893  CB  VAL A 811     -43.021 -63.727  -8.730  1.00 23.41           C  
ANISOU 5893  CB  VAL A 811     3226   3448   2221    -15   -214   -276       C  
ATOM   5894  CG1 VAL A 811     -42.396 -64.084  -7.380  1.00 20.94           C  
ANISOU 5894  CG1 VAL A 811     2902   3041   2013    -11   -151   -275       C  
ATOM   5895  CG2 VAL A 811     -44.478 -64.224  -8.852  1.00 21.66           C  
ANISOU 5895  CG2 VAL A 811     2982   3192   2054    -15   -287   -336       C  
ATOM   5896  N   GLU A 812     -40.628 -61.706  -9.428  1.00 24.66           N  
ANISOU 5896  N   GLU A 812     3420   3750   2202    -51   -130    -72       N  
ATOM   5897  CA  GLU A 812     -39.292 -61.258  -9.017  1.00 26.46           C  
ANISOU 5897  CA  GLU A 812     3641   3984   2427    -64    -60    -14       C  
ATOM   5898  C   GLU A 812     -39.279 -59.762  -8.721  1.00 25.59           C  
ANISOU 5898  C   GLU A 812     3542   3831   2349    -93    -93    130       C  
ATOM   5899  O   GLU A 812     -38.675 -59.335  -7.722  1.00 25.06           O  
ANISOU 5899  O   GLU A 812     3465   3689   2366    -95    -62    165       O  
ATOM   5900  CB  GLU A 812     -38.208 -61.623 -10.069  1.00 27.16           C  
ANISOU 5900  CB  GLU A 812     3721   4222   2375    -75     -1    -44       C  
ATOM   5901  CG  GLU A 812     -36.842 -61.708  -9.349  1.00 31.63           C  
ANISOU 5901  CG  GLU A 812     4260   4770   2987    -72     81    -43       C  
ATOM   5902  CD  GLU A 812     -35.679 -62.307 -10.199  1.00 38.24           C  
ANISOU 5902  CD  GLU A 812     5064   5754   3711    -69    156   -114       C  
ATOM   5903  OE1 GLU A 812     -35.900 -62.693 -11.384  1.00 37.03           O  
ANISOU 5903  OE1 GLU A 812     4912   5732   3427    -68    151   -174       O  
ATOM   5904  OE2 GLU A 812     -34.579 -62.478  -9.595  1.00 42.76           O  
ANISOU 5904  OE2 GLU A 812     5604   6309   4335    -59    218   -128       O  
ATOM   5905  N  AGLU A 813     -39.992 -58.974  -9.533  0.50 25.18           N  
ANISOU 5905  N  AGLU A 813     3509   3814   2245   -112   -168    209       N  
ATOM   5906  N  BGLU A 813     -39.992 -58.957  -9.518  0.50 25.19           N  
ANISOU 5906  N  BGLU A 813     3511   3814   2248   -112   -168    210       N  
ATOM   5907  CA AGLU A 813     -40.103 -57.534  -9.311  0.50 26.79           C  
ANISOU 5907  CA AGLU A 813     3723   3953   2505   -136   -224    345       C  
ATOM   5908  CA BGLU A 813     -40.026 -57.519  -9.251  0.50 26.74           C  
ANISOU 5908  CA BGLU A 813     3714   3943   2501   -136   -220    346       C  
ATOM   5909  C  AGLU A 813     -40.698 -57.224  -7.937  0.50 26.14           C  
ANISOU 5909  C  AGLU A 813     3623   3722   2587   -102   -247    318       C  
ATOM   5910  C  BGLU A 813     -40.691 -57.213  -7.907  0.50 26.11           C  
ANISOU 5910  C  BGLU A 813     3619   3716   2586   -102   -247    318       C  
ATOM   5911  O  AGLU A 813     -40.222 -56.330  -7.227  0.50 26.24           O  
ANISOU 5911  O  AGLU A 813     3631   3661   2679   -111   -249    379       O  
ATOM   5912  O  BGLU A 813     -40.257 -56.307  -7.186  0.50 26.18           O  
ANISOU 5912  O  BGLU A 813     3623   3649   2677   -110   -251    379       O  
ATOM   5913  CB AGLU A 813     -40.961 -56.939 -10.427  0.50 29.67           C  
ANISOU 5913  CB AGLU A 813     4108   4369   2796   -152   -322    422       C  
ATOM   5914  CB BGLU A 813     -40.744 -56.789 -10.386  0.50 29.73           C  
ANISOU 5914  CB BGLU A 813     4116   4375   2804   -159   -314    441       C  
ATOM   5915  CG AGLU A 813     -41.162 -55.438 -10.382  0.50 32.06           C  
ANISOU 5915  CG AGLU A 813     4422   4594   3167   -175   -408    572       C  
ATOM   5916  CG BGLU A 813     -39.886 -56.583 -11.642  0.50 32.97           C  
ANISOU 5916  CG BGLU A 813     4543   4945   3041   -216   -289    528       C  
ATOM   5917  CD AGLU A 813     -42.034 -54.922 -11.544  0.50 36.11           C  
ANISOU 5917  CD AGLU A 813     4956   5158   3604   -190   -521    659       C  
ATOM   5918  CD BGLU A 813     -38.578 -55.847 -11.357  0.50 35.13           C  
ANISOU 5918  CD BGLU A 813     4807   5216   3326   -264   -231    631       C  
ATOM   5919  OE1AGLU A 813     -42.300 -55.694 -12.493  0.50 36.78           O  
ANISOU 5919  OE1AGLU A 813     5052   5372   3552   -192   -520    609       O  
ATOM   5920  OE1BGLU A 813     -38.613 -54.761 -10.717  0.50 35.81           O  
ANISOU 5920  OE1BGLU A 813     4894   5176   3536   -276   -283    727       O  
ATOM   5921  OE2AGLU A 813     -42.435 -53.736 -11.510  0.50 37.48           O  
ANISOU 5921  OE2AGLU A 813     5137   5242   3862   -197   -619    775       O  
ATOM   5922  OE2BGLU A 813     -37.512 -56.382 -11.740  0.50 34.94           O  
ANISOU 5922  OE2BGLU A 813     4764   5312   3199   -286   -137    602       O  
ATOM   5923  N   LEU A 814     -41.725 -57.972  -7.544  1.00 23.19           N  
ANISOU 5923  N   LEU A 814     3234   3313   2264    -67   -264    220       N  
ATOM   5924  CA  LEU A 814     -42.344 -57.820  -6.218  1.00 25.02           C  
ANISOU 5924  CA  LEU A 814     3438   3437   2632    -38   -271    179       C  
ATOM   5925  C   LEU A 814     -41.334 -58.081  -5.108  1.00 23.92           C  
ANISOU 5925  C   LEU A 814     3291   3262   2536    -38   -191    157       C  
ATOM   5926  O   LEU A 814     -41.217 -57.316  -4.135  1.00 23.34           O  
ANISOU 5926  O   LEU A 814     3205   3118   2546    -30   -195    177       O  
ATOM   5927  CB  LEU A 814     -43.551 -58.790  -6.073  1.00 22.82           C  
ANISOU 5927  CB  LEU A 814     3135   3152   2385    -17   -287     80       C  
ATOM   5928  CG  LEU A 814     -44.196 -58.891  -4.669  1.00 25.75           C  
ANISOU 5928  CG  LEU A 814     3465   3448   2872      3   -271     27       C  
ATOM   5929  CD1 LEU A 814     -44.972 -57.483  -4.326  1.00 19.31           C  
ANISOU 5929  CD1 LEU A 814     2622   2572   2144     29   -346     66       C  
ATOM   5930  CD2 LEU A 814     -45.171 -60.110  -4.581  1.00 23.70           C  
ANISOU 5930  CD2 LEU A 814     3176   3195   2633      3   -269    -61       C  
ATOM   5931  N   MET A 815     -40.597 -59.174  -5.227  1.00 22.99           N  
ANISOU 5931  N   MET A 815     3178   3191   2366    -43   -125    105       N  
ATOM   5932  CA  MET A 815     -39.594 -59.503  -4.228  1.00 25.47           C  
ANISOU 5932  CA  MET A 815     3483   3474   2719    -40    -60     87       C  
ATOM   5933  C   MET A 815     -38.536 -58.423  -4.088  1.00 25.89           C  
ANISOU 5933  C   MET A 815     3539   3522   2777    -61    -49    171       C  
ATOM   5934  O   MET A 815     -38.088 -58.130  -2.979  1.00 23.12           O  
ANISOU 5934  O   MET A 815     3176   3114   2494    -56    -31    171       O  
ATOM   5935  CB  MET A 815     -38.961 -60.846  -4.602  1.00 25.57           C  
ANISOU 5935  CB  MET A 815     3495   3536   2684    -34     -8     16       C  
ATOM   5936  CG  MET A 815     -40.060 -61.919  -4.451  1.00 29.53           C  
ANISOU 5936  CG  MET A 815     3989   4008   3222    -20    -29    -66       C  
ATOM   5937  SD  MET A 815     -39.406 -63.547  -4.875  1.00 36.59           S  
ANISOU 5937  SD  MET A 815     4880   4927   4095     -4      8   -168       S  
ATOM   5938  CE  MET A 815     -37.896 -63.607  -3.900  1.00 39.43           C  
ANISOU 5938  CE  MET A 815     5229   5257   4495      4     69   -146       C  
ATOM   5939  N   LYS A 816     -38.103 -57.834  -5.200  1.00 24.42           N  
ANISOU 5939  N   LYS A 816     3365   3400   2514    -92    -60    245       N  
ATOM   5940  CA  LYS A 816     -37.084 -56.799  -5.109  1.00 23.07           C  
ANISOU 5940  CA  LYS A 816     3190   3219   2358   -126    -54    337       C  
ATOM   5941  C   LYS A 816     -37.616 -55.582  -4.358  1.00 25.19           C  
ANISOU 5941  C   LYS A 816     3456   3376   2739   -121   -123    382       C  
ATOM   5942  O   LYS A 816     -36.871 -54.943  -3.625  1.00 24.25           O  
ANISOU 5942  O   LYS A 816     3324   3203   2685   -133   -117    409       O  
ATOM   5943  CB  LYS A 816     -36.639 -56.405  -6.530  1.00 25.17           C  
ANISOU 5943  CB  LYS A 816     3465   3591   2506   -174    -55    426       C  
ATOM   5944  CG  LYS A 816     -35.894 -57.538  -7.262  1.00 24.97           C  
ANISOU 5944  CG  LYS A 816     3426   3696   2365   -175     25    360       C  
ATOM   5945  CD  LYS A 816     -35.575 -57.111  -8.754  1.00 29.96           C  
ANISOU 5945  CD  LYS A 816     4064   4471   2847   -229     26    450       C  
ATOM   5946  CE  LYS A 816     -34.611 -58.130  -9.366  1.00 34.23           C  
ANISOU 5946  CE  LYS A 816     4573   5154   3278   -225    120    366       C  
ATOM   5947  NZ  LYS A 816     -34.520 -57.938 -10.863  1.00 38.06           N  
ANISOU 5947  NZ  LYS A 816     5062   5815   3585   -272    126    423       N  
ATOM   5948  N   MET A 817     -38.909 -55.270  -4.516  1.00 24.42           N  
ANISOU 5948  N   MET A 817     3364   3241   2673    -99   -195    377       N  
ATOM   5949  CA  MET A 817     -39.521 -54.159  -3.779  1.00 23.26           C  
ANISOU 5949  CA  MET A 817     3204   2984   2648    -77   -268    389       C  
ATOM   5950  C   MET A 817     -39.482 -54.392  -2.259  1.00 22.07           C  
ANISOU 5950  C   MET A 817     3027   2782   2576    -44   -230    296       C  
ATOM   5951  O   MET A 817     -39.407 -53.419  -1.493  1.00 20.66           O  
ANISOU 5951  O   MET A 817     2834   2525   2492    -33   -268    297       O  
ATOM   5952  CB  MET A 817     -40.963 -53.976  -4.269  1.00 25.22           C  
ANISOU 5952  CB  MET A 817     3450   3218   2916    -49   -349    380       C  
ATOM   5953  CG  MET A 817     -41.609 -52.714  -3.788  1.00 29.62           C  
ANISOU 5953  CG  MET A 817     3986   3665   3604    -21   -441    395       C  
ATOM   5954  SD  MET A 817     -40.803 -51.131  -4.218  1.00 34.80           S  
ANISOU 5954  SD  MET A 817     4660   4240   4323    -65   -522    546       S  
ATOM   5955  CE  MET A 817     -42.015 -50.197  -3.361  1.00 37.02           C  
ANISOU 5955  CE  MET A 817     4898   4389   4779      7   -624    471       C  
ATOM   5956  N   HIS A 818     -39.531 -55.653  -1.823  1.00 18.95           N  
ANISOU 5956  N   HIS A 818     2626   2430   2142    -31   -164    218       N  
ATOM   5957  CA  HIS A 818     -39.555 -56.043  -0.415  1.00 19.96           C  
ANISOU 5957  CA  HIS A 818     2732   2533   2317     -9   -126    144       C  
ATOM   5958  C   HIS A 818     -38.225 -56.604   0.077  1.00 21.27           C  
ANISOU 5958  C   HIS A 818     2904   2720   2458    -24    -62    143       C  
ATOM   5959  O   HIS A 818     -38.187 -57.367   1.045  1.00 20.04           O  
ANISOU 5959  O   HIS A 818     2738   2569   2309    -13    -25     92       O  
ATOM   5960  CB  HIS A 818     -40.716 -57.027  -0.185  1.00 17.13           C  
ANISOU 5960  CB  HIS A 818     2359   2198   1953      9   -114     73       C  
ATOM   5961  CG  HIS A 818     -42.042 -56.363  -0.416  1.00 22.19           C  
ANISOU 5961  CG  HIS A 818     2976   2815   2641     33   -182     59       C  
ATOM   5962  ND1 HIS A 818     -42.648 -55.575   0.533  1.00 20.61           N  
ANISOU 5962  ND1 HIS A 818     2737   2573   2521     63   -209     14       N  
ATOM   5963  CD2 HIS A 818     -42.807 -56.262  -1.533  1.00 22.40           C  
ANISOU 5963  CD2 HIS A 818     3007   2854   2649     34   -237     82       C  
ATOM   5964  CE1 HIS A 818     -43.767 -55.072   0.030  1.00 23.77           C  
ANISOU 5964  CE1 HIS A 818     3113   2955   2964     87   -278      5       C  
ATOM   5965  NE2 HIS A 818     -43.875 -55.461  -1.228  1.00 24.41           N  
ANISOU 5965  NE2 HIS A 818     3223   3066   2985     68   -300     54       N  
ATOM   5966  N   THR A 819     -37.119 -56.245  -0.597  1.00 19.01           N  
ANISOU 5966  N   THR A 819     2627   2454   2142    -54    -51    208       N  
ATOM   5967  CA  THR A 819     -35.791 -56.557  -0.098  1.00 21.68           C  
ANISOU 5967  CA  THR A 819     2955   2805   2476    -65     -2    207       C  
ATOM   5968  C   THR A 819     -35.648 -56.002   1.334  1.00 22.42           C  
ANISOU 5968  C   THR A 819     3032   2840   2645    -50    -18    177       C  
ATOM   5969  O   THR A 819     -36.308 -55.037   1.695  1.00 22.60           O  
ANISOU 5969  O   THR A 819     3049   2811   2727    -39    -71    170       O  
ATOM   5970  CB  THR A 819     -34.750 -55.930  -1.062  1.00 22.74           C  
ANISOU 5970  CB  THR A 819     3086   2974   2579   -108      5    292       C  
ATOM   5971  OG1 THR A 819     -33.437 -56.345  -0.688  1.00 23.85           O  
ANISOU 5971  OG1 THR A 819     3204   3142   2717   -117     57    282       O  
ATOM   5972  CG2 THR A 819     -34.884 -54.366  -1.065  1.00 21.18           C  
ANISOU 5972  CG2 THR A 819     2888   2705   2453   -132    -67    365       C  
ATOM   5973  N   ALA A 820     -34.804 -56.627   2.156  1.00 20.25           N  
ANISOU 5973  N   ALA A 820     2748   2579   2369    -46     20    150       N  
ATOM   5974  CA  ALA A 820     -34.696 -56.190   3.560  1.00 18.45           C  
ANISOU 5974  CA  ALA A 820     2504   2317   2189    -32      3    111       C  
ATOM   5975  C   ALA A 820     -33.277 -56.447   4.095  1.00 20.11           C  
ANISOU 5975  C   ALA A 820     2700   2539   2402    -42     26    118       C  
ATOM   5976  O   ALA A 820     -32.491 -57.198   3.492  1.00 20.28           O  
ANISOU 5976  O   ALA A 820     2718   2596   2392    -50     64    139       O  
ATOM   5977  CB  ALA A 820     -35.707 -56.948   4.458  1.00 18.73           C  
ANISOU 5977  CB  ALA A 820     2539   2370   2208     -8     16     51       C  
ATOM   5978  N   ARG A 821     -32.974 -55.886   5.290  1.00 20.47           N  
ANISOU 5978  N   ARG A 821     2730   2561   2485    -35      0     87       N  
ATOM   5979  CA  ARG A 821     -31.713 -56.172   5.977  1.00 19.89           C  
ANISOU 5979  CA  ARG A 821     2640   2501   2418    -39      9     86       C  
ATOM   5980  C   ARG A 821     -31.915 -57.375   6.882  1.00 20.42           C  
ANISOU 5980  C   ARG A 821     2714   2602   2441    -18     30     56       C  
ATOM   5981  O   ARG A 821     -33.006 -57.605   7.379  1.00 21.03           O  
ANISOU 5981  O   ARG A 821     2804   2693   2495     -6     30     27       O  
ATOM   5982  CB  ARG A 821     -31.247 -54.984   6.841  1.00 18.01           C  
ANISOU 5982  CB  ARG A 821     2379   2224   2238    -44    -42     61       C  
ATOM   5983  CG  ARG A 821     -31.166 -53.607   6.078  1.00 18.14           C  
ANISOU 5983  CG  ARG A 821     2388   2178   2328    -73    -87    100       C  
ATOM   5984  CD  ARG A 821     -30.879 -52.417   7.033  1.00 21.30           C  
ANISOU 5984  CD  ARG A 821     2765   2518   2810    -72   -155     51       C  
ATOM   5985  NE  ARG A 821     -31.815 -52.481   8.167  1.00 22.76           N  
ANISOU 5985  NE  ARG A 821     2953   2721   2973    -26   -168    -47       N  
ATOM   5986  CZ  ARG A 821     -31.547 -52.104   9.420  1.00 24.01           C  
ANISOU 5986  CZ  ARG A 821     3093   2887   3145     -9   -202   -127       C  
ATOM   5987  NH1 ARG A 821     -30.336 -51.615   9.743  1.00 22.58           N  
ANISOU 5987  NH1 ARG A 821     2888   2678   3014    -32   -237   -123       N  
ATOM   5988  NH2 ARG A 821     -32.507 -52.216  10.344  1.00 20.33           N  
ANISOU 5988  NH2 ARG A 821     2623   2466   2634     29   -200   -215       N  
ATOM   5989  N   VAL A 822     -30.844 -58.130   7.136  1.00 22.37           N  
ANISOU 5989  N   VAL A 822     2950   2866   2685    -16     42     70       N  
ATOM   5990  CA  VAL A 822     -30.978 -59.193   8.143  1.00 18.76           C  
ANISOU 5990  CA  VAL A 822     2503   2429   2196     -2     42     61       C  
ATOM   5991  C   VAL A 822     -31.418 -58.589   9.462  1.00 21.52           C  
ANISOU 5991  C   VAL A 822     2851   2801   2526      0     14     27       C  
ATOM   5992  O   VAL A 822     -32.265 -59.145  10.185  1.00 20.15           O  
ANISOU 5992  O   VAL A 822     2689   2662   2304      0     22     20       O  
ATOM   5993  CB  VAL A 822     -29.657 -59.989   8.284  1.00 19.33           C  
ANISOU 5993  CB  VAL A 822     2555   2503   2287      8     40     81       C  
ATOM   5994  CG1 VAL A 822     -29.738 -61.006   9.446  1.00 17.36           C  
ANISOU 5994  CG1 VAL A 822     2319   2266   2012     17     19     94       C  
ATOM   5995  CG2 VAL A 822     -29.335 -60.761   6.964  1.00 16.25           C  
ANISOU 5995  CG2 VAL A 822     2157   2109   1910     16     76     88       C  
ATOM   5996  N   ARG A 823     -30.872 -57.421   9.785  1.00 20.50           N  
ANISOU 5996  N   ARG A 823     2702   2657   2430     -3    -20      0       N  
ATOM   5997  CA  ARG A 823     -31.260 -56.740  11.009  1.00 23.61           C  
ANISOU 5997  CA  ARG A 823     3088   3079   2804      6    -52    -61       C  
ATOM   5998  C   ARG A 823     -32.774 -56.521  11.083  1.00 23.66           C  
ANISOU 5998  C   ARG A 823     3099   3105   2786     16    -37   -103       C  
ATOM   5999  O   ARG A 823     -33.357 -56.582  12.175  1.00 22.28           O  
ANISOU 5999  O   ARG A 823     2916   2995   2553     24    -36   -150       O  
ATOM   6000  CB  ARG A 823     -30.459 -55.411  11.088  1.00 27.53           C  
ANISOU 6000  CB  ARG A 823     3559   3531   3372      1   -101    -93       C  
ATOM   6001  CG  ARG A 823     -30.385 -54.806  12.467  1.00 33.57           C  
ANISOU 6001  CG  ARG A 823     4307   4330   4118     14   -147   -173       C  
ATOM   6002  CD  ARG A 823     -29.274 -55.429  13.376  1.00 32.27           C  
ANISOU 6002  CD  ARG A 823     4134   4213   3914     11   -167   -158       C  
ATOM   6003  NE  ARG A 823     -29.483 -54.833  14.686  1.00 34.20           N  
ANISOU 6003  NE  ARG A 823     4366   4513   4113     25   -209   -249       N  
ATOM   6004  CZ  ARG A 823     -30.185 -55.392  15.675  1.00 37.99           C  
ANISOU 6004  CZ  ARG A 823     4857   5095   4484     32   -192   -271       C  
ATOM   6005  NH1 ARG A 823     -30.666 -56.626  15.536  1.00 36.49           N  
ANISOU 6005  NH1 ARG A 823     4693   4940   4233     21   -144   -193       N  
ATOM   6006  NH2 ARG A 823     -30.351 -54.755  16.821  1.00 38.99           N  
ANISOU 6006  NH2 ARG A 823     4965   5292   4558     47   -227   -370       N  
ATOM   6007  N   ASP A 824     -33.429 -56.182   9.952  1.00 18.55           N  
ANISOU 6007  N   ASP A 824     2457   2412   2177     17    -29    -91       N  
ATOM   6008  CA  ASP A 824     -34.880 -55.929   9.984  1.00 19.30           C  
ANISOU 6008  CA  ASP A 824     2544   2523   2264     32    -23   -138       C  
ATOM   6009  C   ASP A 824     -35.619 -57.197  10.417  1.00 21.09           C  
ANISOU 6009  C   ASP A 824     2778   2819   2418     22     23   -123       C  
ATOM   6010  O   ASP A 824     -36.612 -57.150  11.166  1.00 21.47           O  
ANISOU 6010  O   ASP A 824     2803   2927   2428     28     37   -174       O  
ATOM   6011  CB  ASP A 824     -35.391 -55.528   8.580  1.00 19.73           C  
ANISOU 6011  CB  ASP A 824     2608   2520   2370     32    -31   -108       C  
ATOM   6012  CG  ASP A 824     -34.842 -54.172   8.090  1.00 22.01           C  
ANISOU 6012  CG  ASP A 824     2889   2731   2743     30    -87   -102       C  
ATOM   6013  OD1 ASP A 824     -34.704 -53.262   8.905  1.00 23.74           O  
ANISOU 6013  OD1 ASP A 824     3085   2929   3004     45   -129   -166       O  
ATOM   6014  OD2 ASP A 824     -34.609 -53.989   6.850  1.00 26.22           O  
ANISOU 6014  OD2 ASP A 824     3436   3226   3301     10    -93    -33       O  
ATOM   6015  N   ILE A 825     -35.131 -58.344   9.931  1.00 18.96           N  
ANISOU 6015  N   ILE A 825     2532   2538   2134      4     45    -54       N  
ATOM   6016  CA  ILE A 825     -35.725 -59.632  10.268  1.00 19.55           C  
ANISOU 6016  CA  ILE A 825     2614   2652   2162    -15     75    -22       C  
ATOM   6017  C   ILE A 825     -35.478 -59.994  11.738  1.00 20.96           C  
ANISOU 6017  C   ILE A 825     2788   2899   2277    -28     73    -14       C  
ATOM   6018  O   ILE A 825     -36.371 -60.572  12.395  1.00 23.02           O  
ANISOU 6018  O   ILE A 825     3039   3224   2483    -53     97     -3       O  
ATOM   6019  CB  ILE A 825     -35.183 -60.710   9.329  1.00 16.03           C  
ANISOU 6019  CB  ILE A 825     2191   2158   1740    -22     84     33       C  
ATOM   6020  CG1 ILE A 825     -35.687 -60.464   7.887  1.00 16.43           C  
ANISOU 6020  CG1 ILE A 825     2247   2174   1823    -15     89     23       C  
ATOM   6021  CG2 ILE A 825     -35.682 -62.106   9.780  1.00 16.25           C  
ANISOU 6021  CG2 ILE A 825     2228   2202   1746    -47     96     76       C  
ATOM   6022  CD1 ILE A 825     -34.905 -61.306   6.836  1.00 20.18           C  
ANISOU 6022  CD1 ILE A 825     2736   2616   2317    -12     98     49       C  
ATOM   6023  N   GLU A 826     -34.301 -59.627  12.306  1.00 20.74           N  
ANISOU 6023  N   GLU A 826     2761   2873   2248    -19     42    -17       N  
ATOM   6024  CA  GLU A 826     -34.052 -59.920  13.732  1.00 20.43           C  
ANISOU 6024  CA  GLU A 826     2718   2914   2130    -32     30     -8       C  
ATOM   6025  C   GLU A 826     -35.049 -59.189  14.626  1.00 22.14           C  
ANISOU 6025  C   GLU A 826     2905   3225   2283    -30     44    -86       C  
ATOM   6026  O   GLU A 826     -35.602 -59.787  15.562  1.00 24.84           O  
ANISOU 6026  O   GLU A 826     3239   3665   2532    -59     66    -63       O  
ATOM   6027  CB  GLU A 826     -32.580 -59.540  14.102  1.00 20.02           C  
ANISOU 6027  CB  GLU A 826     2664   2844   2098    -18    -18    -10       C  
ATOM   6028  CG  GLU A 826     -31.538 -60.445  13.322  1.00 21.37           C  
ANISOU 6028  CG  GLU A 826     2848   2941   2330    -15    -28     62       C  
ATOM   6029  CD  GLU A 826     -30.056 -60.189  13.683  1.00 26.06           C  
ANISOU 6029  CD  GLU A 826     3426   3523   2953     -2    -75     63       C  
ATOM   6030  OE1 GLU A 826     -29.708 -59.024  13.925  1.00 29.16           O  
ANISOU 6030  OE1 GLU A 826     3798   3921   3361      4    -99      4       O  
ATOM   6031  OE2 GLU A 826     -29.224 -61.152  13.656  1.00 26.90           O  
ANISOU 6031  OE2 GLU A 826     3533   3605   3083      4    -95    119       O  
ATOM   6032  N   HIS A 827     -35.235 -57.857  14.402  1.00 21.32           N  
ANISOU 6032  N   HIS A 827     2777   3096   2226      3     27   -182       N  
ATOM   6033  CA  HIS A 827     -36.278 -57.082  15.116  1.00 21.58           C  
ANISOU 6033  CA  HIS A 827     2769   3211   2220     21     39   -289       C  
ATOM   6034  C   HIS A 827     -37.652 -57.794  15.086  1.00 19.84           C  
ANISOU 6034  C   HIS A 827     2529   3055   1953     -2     96   -271       C  
ATOM   6035  O   HIS A 827     -38.361 -57.874  16.097  1.00 21.33           O  
ANISOU 6035  O   HIS A 827     2682   3373   2049    -15    129   -312       O  
ATOM   6036  CB  HIS A 827     -36.430 -55.684  14.449  1.00 24.40           C  
ANISOU 6036  CB  HIS A 827     3106   3481   2685     63      0   -377       C  
ATOM   6037  CG  HIS A 827     -35.189 -54.807  14.493  1.00 27.96           C  
ANISOU 6037  CG  HIS A 827     3563   3862   3200     77    -62   -403       C  
ATOM   6038  ND1 HIS A 827     -34.246 -54.897  15.502  1.00 31.29           N  
ANISOU 6038  ND1 HIS A 827     3985   4338   3565     69    -86   -413       N  
ATOM   6039  CD2 HIS A 827     -34.798 -53.755  13.710  1.00 28.10           C  
ANISOU 6039  CD2 HIS A 827     3577   3765   3336     92   -112   -421       C  
ATOM   6040  CE1 HIS A 827     -33.310 -53.966  15.324  1.00 30.55           C  
ANISOU 6040  CE1 HIS A 827     3886   4162   3559     80   -146   -444       C  
ATOM   6041  NE2 HIS A 827     -33.625 -53.256  14.256  1.00 30.35           N  
ANISOU 6041  NE2 HIS A 827     3858   4033   3642     89   -161   -444       N  
ATOM   6042  N   LEU A 828     -38.049 -58.299  13.914  1.00 18.70           N  
ANISOU 6042  N   LEU A 828     2401   2833   1871    -12    110   -215       N  
ATOM   6043  CA  LEU A 828     -39.395 -58.849  13.683  1.00 20.56           C  
ANISOU 6043  CA  LEU A 828     2610   3109   2093    -33    154   -208       C  
ATOM   6044  C   LEU A 828     -39.569 -60.271  14.227  1.00 21.81           C  
ANISOU 6044  C   LEU A 828     2779   3329   2180    -94    188   -108       C  
ATOM   6045  O   LEU A 828     -40.703 -60.754  14.300  1.00 24.08           O  
ANISOU 6045  O   LEU A 828     3033   3673   2445   -127    228    -99       O  
ATOM   6046  CB  LEU A 828     -39.689 -58.858  12.153  1.00 17.69           C  
ANISOU 6046  CB  LEU A 828     2263   2636   1824    -21    141   -186       C  
ATOM   6047  CG  LEU A 828     -40.008 -57.440  11.645  1.00 19.31           C  
ANISOU 6047  CG  LEU A 828     2443   2792   2101     30    104   -275       C  
ATOM   6048  CD1 LEU A 828     -39.927 -57.289  10.076  1.00 18.98           C  
ANISOU 6048  CD1 LEU A 828     2431   2642   2140     40     74   -232       C  
ATOM   6049  CD2 LEU A 828     -41.503 -57.134  12.012  1.00 18.39           C  
ANISOU 6049  CD2 LEU A 828     2259   2751   1977     44    128   -358       C  
ATOM   6050  N   THR A 829     -38.479 -60.981  14.495  1.00 20.91           N  
ANISOU 6050  N   THR A 829     2708   3188   2048   -113    166    -25       N  
ATOM   6051  CA  THR A 829     -38.534 -62.384  14.938  1.00 22.48           C  
ANISOU 6051  CA  THR A 829     2924   3413   2206   -173    176     91       C  
ATOM   6052  C   THR A 829     -37.942 -62.601  16.322  1.00 24.67           C  
ANISOU 6052  C   THR A 829     3207   3789   2378   -198    163    135       C  
ATOM   6053  O   THR A 829     -38.262 -63.608  16.955  1.00 25.75           O  
ANISOU 6053  O   THR A 829     3347   3982   2457   -260    175    235       O  
ATOM   6054  CB  THR A 829     -37.777 -63.311  13.966  1.00 22.89           C  
ANISOU 6054  CB  THR A 829     3021   3331   2345   -171    144    165       C  
ATOM   6055  OG1 THR A 829     -36.424 -62.881  13.896  1.00 21.80           O  
ANISOU 6055  OG1 THR A 829     2906   3146   2232   -132    105    153       O  
ATOM   6056  CG2 THR A 829     -38.339 -63.226  12.520  1.00 18.93           C  
ANISOU 6056  CG2 THR A 829     2518   2745   1929   -151    153    128       C  
ATOM   6057  N   GLY A 830     -37.089 -61.709  16.811  1.00 23.14           N  
ANISOU 6057  N   GLY A 830     3015   3618   2160   -159    132     71       N  
ATOM   6058  CA  GLY A 830     -36.405 -61.977  18.078  1.00 22.39           C  
ANISOU 6058  CA  GLY A 830     2930   3616   1960   -182    105    118       C  
ATOM   6059  C   GLY A 830     -35.314 -63.033  17.966  1.00 25.00           C  
ANISOU 6059  C   GLY A 830     3306   3858   2333   -195     52    242       C  
ATOM   6060  O   GLY A 830     -34.938 -63.633  18.968  1.00 25.33           O  
ANISOU 6060  O   GLY A 830     3362   3971   2292   -230     23    326       O  
ATOM   6061  N   LEU A 831     -34.846 -63.316  16.749  1.00 23.41           N  
ANISOU 6061  N   LEU A 831     3124   3511   2258   -167     37    254       N  
ATOM   6062  CA  LEU A 831     -33.744 -64.230  16.484  1.00 23.29           C  
ANISOU 6062  CA  LEU A 831     3139   3400   2311   -160    -16    337       C  
ATOM   6063  C   LEU A 831     -32.469 -63.429  16.238  1.00 24.95           C  
ANISOU 6063  C   LEU A 831     3344   3567   2570   -108    -54    276       C  
ATOM   6064  O   LEU A 831     -32.527 -62.281  15.813  1.00 24.83           O  
ANISOU 6064  O   LEU A 831     3312   3548   2576    -80    -36    181       O  
ATOM   6065  CB  LEU A 831     -34.043 -65.058  15.248  1.00 20.76           C  
ANISOU 6065  CB  LEU A 831     2830   2962   2095   -160     -5    365       C  
ATOM   6066  CG  LEU A 831     -35.304 -65.938  15.302  1.00 23.15           C  
ANISOU 6066  CG  LEU A 831     3132   3281   2384   -218     25    428       C  
ATOM   6067  CD1 LEU A 831     -35.612 -66.555  13.863  1.00 21.39           C  
ANISOU 6067  CD1 LEU A 831     2916   2934   2278   -205     31    414       C  
ATOM   6068  CD2 LEU A 831     -35.071 -67.002  16.393  1.00 23.22           C  
ANISOU 6068  CD2 LEU A 831     3159   3318   2348   -271    -18    562       C  
ATOM   6069  N   ASP A 832     -31.317 -64.062  16.464  1.00 24.38           N  
ANISOU 6069  N   ASP A 832     3282   3452   2530    -97   -112    337       N  
ATOM   6070  CA  ASP A 832     -30.007 -63.432  16.231  1.00 23.46           C  
ANISOU 6070  CA  ASP A 832     3148   3295   2471    -54   -149    289       C  
ATOM   6071  C   ASP A 832     -29.215 -64.407  15.354  1.00 24.28           C  
ANISOU 6071  C   ASP A 832     3252   3288   2687    -29   -172    333       C  
ATOM   6072  O   ASP A 832     -28.971 -65.552  15.763  1.00 24.65           O  
ANISOU 6072  O   ASP A 832     3312   3306   2748    -37   -217    420       O  
ATOM   6073  CB  ASP A 832     -29.292 -63.151  17.598  1.00 22.49           C  
ANISOU 6073  CB  ASP A 832     3020   3259   2267    -57   -210    299       C  
ATOM   6074  CG  ASP A 832     -27.998 -62.309  17.451  1.00 31.60           C  
ANISOU 6074  CG  ASP A 832     4143   4381   3483    -20   -251    234       C  
ATOM   6075  OD1 ASP A 832     -28.135 -61.137  17.002  1.00 35.37           O  
ANISOU 6075  OD1 ASP A 832     4601   4851   3986    -10   -224    142       O  
ATOM   6076  OD2 ASP A 832     -26.848 -62.792  17.769  1.00 33.45           O  
ANISOU 6076  OD2 ASP A 832     4366   4593   3751     -4   -317    278       O  
ATOM   6077  N   PHE A 833     -28.875 -63.993  14.143  1.00 20.99           N  
ANISOU 6077  N   PHE A 833     2816   2811   2349      0   -142    274       N  
ATOM   6078  CA  PHE A 833     -28.194 -64.839  13.163  1.00 26.34           C  
ANISOU 6078  CA  PHE A 833     3480   3402   3126     31   -149    283       C  
ATOM   6079  C   PHE A 833     -26.663 -64.674  13.164  1.00 25.01           C  
ANISOU 6079  C   PHE A 833     3270   3217   3017     66   -189    266       C  
ATOM   6080  O   PHE A 833     -26.110 -63.736  13.732  1.00 25.54           O  
ANISOU 6080  O   PHE A 833     3317   3329   3058     64   -210    241       O  
ATOM   6081  CB  PHE A 833     -28.732 -64.525  11.756  1.00 19.54           C  
ANISOU 6081  CB  PHE A 833     2616   2512   2297     36    -86    228       C  
ATOM   6082  CG  PHE A 833     -30.208 -64.687  11.655  1.00 22.23           C  
ANISOU 6082  CG  PHE A 833     2987   2865   2595      6    -51    236       C  
ATOM   6083  CD1 PHE A 833     -30.765 -65.962  11.464  1.00 22.64           C  
ANISOU 6083  CD1 PHE A 833     3057   2868   2678     -6    -59    279       C  
ATOM   6084  CD2 PHE A 833     -31.052 -63.592  11.778  1.00 19.85           C  
ANISOU 6084  CD2 PHE A 833     2688   2617   2239    -12    -19    197       C  
ATOM   6085  CE1 PHE A 833     -32.106 -66.137  11.434  1.00 21.96           C  
ANISOU 6085  CE1 PHE A 833     2986   2797   2559    -42    -30    290       C  
ATOM   6086  CE2 PHE A 833     -32.448 -63.759  11.686  1.00 21.95           C  
ANISOU 6086  CE2 PHE A 833     2966   2901   2473    -38     12    198       C  
ATOM   6087  CZ  PHE A 833     -32.969 -65.038  11.518  1.00 21.94           C  
ANISOU 6087  CZ  PHE A 833     2980   2862   2495    -57     10    247       C  
ATOM   6088  N   TYR A 834     -25.990 -65.562  12.417  1.00 22.84           N  
ANISOU 6088  N   TYR A 834     2971   2876   2833    103   -200    264       N  
ATOM   6089  CA  TYR A 834     -24.528 -65.497  12.171  1.00 20.60           C  
ANISOU 6089  CA  TYR A 834     2626   2579   2624    142   -226    234       C  
ATOM   6090  C   TYR A 834     -23.743 -65.513  13.470  1.00 23.60           C  
ANISOU 6090  C   TYR A 834     2994   2981   2993    147   -310    276       C  
ATOM   6091  O   TYR A 834     -22.716 -64.833  13.606  1.00 21.15           O  
ANISOU 6091  O   TYR A 834     2633   2696   2707    158   -330    244       O  
ATOM   6092  CB  TYR A 834     -24.129 -64.271  11.366  1.00 20.32           C  
ANISOU 6092  CB  TYR A 834     2551   2578   2592    135   -171    171       C  
ATOM   6093  CG  TYR A 834     -24.828 -64.193  10.023  1.00 22.70           C  
ANISOU 6093  CG  TYR A 834     2862   2872   2890    129    -96    136       C  
ATOM   6094  CD1 TYR A 834     -24.732 -65.260   9.084  1.00 24.01           C  
ANISOU 6094  CD1 TYR A 834     3012   2999   3109    164    -78    110       C  
ATOM   6095  CD2 TYR A 834     -25.539 -63.043   9.670  1.00 25.64           C  
ANISOU 6095  CD2 TYR A 834     3254   3276   3213     93    -53    121       C  
ATOM   6096  CE1 TYR A 834     -25.361 -65.179   7.811  1.00 23.29           C  
ANISOU 6096  CE1 TYR A 834     2929   2919   3000    158    -13     70       C  
ATOM   6097  CE2 TYR A 834     -26.171 -62.939   8.421  1.00 25.53           C  
ANISOU 6097  CE2 TYR A 834     3249   3263   3190     86      5     99       C  
ATOM   6098  CZ  TYR A 834     -26.086 -64.035   7.491  1.00 25.01           C  
ANISOU 6098  CZ  TYR A 834     3172   3176   3156    116     27     74       C  
ATOM   6099  OH  TYR A 834     -26.669 -63.896   6.242  1.00 24.69           O  
ANISOU 6099  OH  TYR A 834     3139   3154   3089    108     79     46       O  
ATOM   6100  N   ARG A 835     -24.163 -66.374  14.393  1.00 24.52           N  
ANISOU 6100  N   ARG A 835     3152   3087   3078    135   -366    357       N  
ATOM   6101  CA  ARG A 835     -23.438 -66.413  15.657  1.00 27.91           C  
ANISOU 6101  CA  ARG A 835     3575   3552   3479    136   -455    409       C  
ATOM   6102  C   ARG A 835     -22.137 -67.203  15.622  1.00 29.93           C  
ANISOU 6102  C   ARG A 835     3778   3742   3850    192   -534    422       C  
ATOM   6103  O   ARG A 835     -21.278 -66.972  16.485  1.00 30.31           O  
ANISOU 6103  O   ARG A 835     3801   3827   3890    202   -609    440       O  
ATOM   6104  CB  ARG A 835     -24.385 -66.932  16.736  1.00 30.58           C  
ANISOU 6104  CB  ARG A 835     3974   3929   3715     89   -486    507       C  
ATOM   6105  CG  ARG A 835     -25.385 -65.773  17.037  1.00 30.57           C  
ANISOU 6105  CG  ARG A 835     3997   4029   3588     44   -417    460       C  
ATOM   6106  CD  ARG A 835     -26.401 -66.165  18.008  1.00 29.29           C  
ANISOU 6106  CD  ARG A 835     3881   3938   3310     -8   -422    540       C  
ATOM   6107  NE  ARG A 835     -25.892 -66.318  19.373  1.00 30.51           N  
ANISOU 6107  NE  ARG A 835     4043   4169   3380    -23   -507    610       N  
ATOM   6108  CZ  ARG A 835     -25.947 -65.368  20.315  1.00 27.74           C  
ANISOU 6108  CZ  ARG A 835     3691   3947   2903    -41   -513    566       C  
ATOM   6109  NH1 ARG A 835     -26.474 -64.170  20.056  1.00 22.43           N  
ANISOU 6109  NH1 ARG A 835     3006   3323   2195    -42   -443    449       N  
ATOM   6110  NH2 ARG A 835     -25.562 -65.649  21.529  1.00 24.29           N  
ANISOU 6110  NH2 ARG A 835     3265   3592   2372    -59   -593    640       N  
ATOM   6111  N   LYS A 836     -21.946 -68.134  14.678  1.00 29.87           N  
ANISOU 6111  N   LYS A 836     3747   3644   3957    235   -527    402       N  
ATOM   6112  CA  LYS A 836     -20.693 -68.917  14.597  1.00 31.10           C  
ANISOU 6112  CA  LYS A 836     3838   3733   4245    303   -605    393       C  
ATOM   6113  C   LYS A 836     -20.142 -68.752  13.182  1.00 31.48           C  
ANISOU 6113  C   LYS A 836     3814   3769   4379    347   -529    275       C  
ATOM   6114  O   LYS A 836     -20.504 -69.512  12.286  1.00 31.05           O  
ANISOU 6114  O   LYS A 836     3760   3653   4385    373   -498    237       O  
ATOM   6115  CB  LYS A 836     -20.919 -70.400  14.912  1.00 35.20           C  
ANISOU 6115  CB  LYS A 836     4388   4146   4840    323   -693    478       C  
ATOM   6116  CG  LYS A 836     -21.791 -70.647  16.107  1.00 43.52           C  
ANISOU 6116  CG  LYS A 836     5523   5226   5787    256   -742    613       C  
ATOM   6117  CD  LYS A 836     -20.968 -70.600  17.367  1.00 50.04           C  
ANISOU 6117  CD  LYS A 836     6340   6093   6581    259   -853    689       C  
ATOM   6118  CE  LYS A 836     -21.685 -71.199  18.579  1.00 55.12           C  
ANISOU 6118  CE  LYS A 836     7056   6757   7128    196   -925    851       C  
ATOM   6119  NZ  LYS A 836     -20.838 -70.934  19.794  1.00 59.85           N  
ANISOU 6119  NZ  LYS A 836     7645   7432   7664    197  -1029    910       N  
ATOM   6120  N   THR A 837     -19.290 -67.761  12.970  1.00 32.83           N  
ANISOU 6120  N   THR A 837     3919   4006   4550    348   -497    216       N  
ATOM   6121  CA  THR A 837     -18.550 -67.622  11.719  1.00 30.92           C  
ANISOU 6121  CA  THR A 837     3589   3777   4382    384   -429    116       C  
ATOM   6122  C   THR A 837     -17.084 -67.434  12.075  1.00 31.22           C  
ANISOU 6122  C   THR A 837     3526   3837   4497    420   -485     91       C  
ATOM   6123  O   THR A 837     -16.724 -67.268  13.242  1.00 29.86           O  
ANISOU 6123  O   THR A 837     3363   3673   4310    411   -575    147       O  
ATOM   6124  CB  THR A 837     -19.019 -66.406  10.920  1.00 28.80           C  
ANISOU 6124  CB  THR A 837     3328   3582   4034    329   -317     78       C  
ATOM   6125  OG1 THR A 837     -18.548 -65.241  11.577  1.00 27.59           O  
ANISOU 6125  OG1 THR A 837     3155   3483   3844    289   -334     91       O  
ATOM   6126  CG2 THR A 837     -20.566 -66.356  10.828  1.00 28.54           C  
ANISOU 6126  CG2 THR A 837     3396   3538   3909    285   -275    112       C  
ATOM   6127  N   SER A 838     -16.220 -67.424  11.068  1.00 30.09           N  
ANISOU 6127  N   SER A 838     3281   3721   4432    456   -431      2       N  
ATOM   6128  CA  SER A 838     -14.818 -67.102  11.308  1.00 31.09           C  
ANISOU 6128  CA  SER A 838     3292   3885   4635    481   -470    -31       C  
ATOM   6129  C   SER A 838     -14.512 -65.616  11.131  1.00 30.95           C  
ANISOU 6129  C   SER A 838     3238   3958   4563    409   -405    -42       C  
ATOM   6130  O   SER A 838     -13.344 -65.255  11.002  1.00 33.29           O  
ANISOU 6130  O   SER A 838     3420   4300   4930    417   -407    -83       O  
ATOM   6131  CB  SER A 838     -13.912 -67.920  10.387  1.00 36.57           C  
ANISOU 6131  CB  SER A 838     3869   4573   5455    563   -450   -130       C  
ATOM   6132  OG  SER A 838     -14.349 -67.764   9.040  1.00 39.42           O  
ANISOU 6132  OG  SER A 838     4220   4984   5774    548   -321   -198       O  
ATOM   6133  N   ARG A 839     -15.516 -64.746  11.126  1.00 28.32           N  
ANISOU 6133  N   ARG A 839     2993   3645   4122    338   -355     -7       N  
ATOM   6134  CA  ARG A 839     -15.293 -63.333  10.818  1.00 28.64           C  
ANISOU 6134  CA  ARG A 839     3000   3748   4133    267   -299    -15       C  
ATOM   6135  C   ARG A 839     -15.290 -62.497  12.097  1.00 31.31           C  
ANISOU 6135  C   ARG A 839     3373   4088   4436    228   -381     21       C  
ATOM   6136  O   ARG A 839     -15.831 -62.917  13.113  1.00 30.15           O  
ANISOU 6136  O   ARG A 839     3303   3914   4238    241   -453     60       O  
ATOM   6137  CB  ARG A 839     -16.402 -62.841   9.901  1.00 26.34           C  
ANISOU 6137  CB  ARG A 839     2776   3470   3762    220   -201    -10       C  
ATOM   6138  CG  ARG A 839     -16.630 -63.784   8.687  1.00 24.56           C  
ANISOU 6138  CG  ARG A 839     2536   3249   3547    263   -128    -54       C  
ATOM   6139  CD  ARG A 839     -15.327 -63.974   7.812  1.00 30.71           C  
ANISOU 6139  CD  ARG A 839     3173   4093   4404    292    -80   -123       C  
ATOM   6140  NE  ARG A 839     -14.710 -62.701   7.414  1.00 30.59           N  
ANISOU 6140  NE  ARG A 839     3087   4153   4381    218    -27   -110       N  
ATOM   6141  CZ  ARG A 839     -13.449 -62.603   7.065  1.00 33.34           C  
ANISOU 6141  CZ  ARG A 839     3300   4568   4801    223     -4   -150       C  
ATOM   6142  NH1 ARG A 839     -12.702 -63.693   7.044  1.00 34.79           N  
ANISOU 6142  NH1 ARG A 839     3402   4750   5068    310    -29   -219       N  
ATOM   6143  NH2 ARG A 839     -12.951 -61.431   6.729  1.00 35.42           N  
ANISOU 6143  NH2 ARG A 839     3502   4894   5062    140     40   -121       N  
ATOM   6144  N   SER A 840     -14.700 -61.291  12.053  1.00 27.98           N  
ANISOU 6144  N   SER A 840     2894   3702   4036    173   -371      5       N  
ATOM   6145  CA  SER A 840     -14.839 -60.504  13.264  1.00 30.06           C  
ANISOU 6145  CA  SER A 840     3198   3964   4259    140   -454     17       C  
ATOM   6146  C   SER A 840     -16.310 -60.124  13.465  1.00 29.76           C  
ANISOU 6146  C   SER A 840     3281   3912   4113    112   -428     36       C  
ATOM   6147  O   SER A 840     -17.120 -60.072  12.520  1.00 31.08           O  
ANISOU 6147  O   SER A 840     3488   4071   4252     96   -341     43       O  
ATOM   6148  CB  SER A 840     -13.963 -59.257  13.203  1.00 30.72           C  
ANISOU 6148  CB  SER A 840     3195   4070   4406     83   -462     -8       C  
ATOM   6149  OG  SER A 840     -14.565 -58.399  12.252  1.00 30.28           O  
ANISOU 6149  OG  SER A 840     3162   4012   4333     24   -373      1       O  
ATOM   6150  N   TYR A 841     -16.674 -59.802  14.705  1.00 27.30           N  
ANISOU 6150  N   TYR A 841     3024   3612   3738    103   -504     38       N  
ATOM   6151  CA  TYR A 841     -18.082 -59.513  14.946  1.00 26.98           C  
ANISOU 6151  CA  TYR A 841     3083   3573   3596     84   -476     44       C  
ATOM   6152  C   TYR A 841     -18.523 -58.175  14.310  1.00 27.88           C  
ANISOU 6152  C   TYR A 841     3200   3672   3724     32   -424     11       C  
ATOM   6153  O   TYR A 841     -19.632 -58.079  13.765  1.00 28.27           O  
ANISOU 6153  O   TYR A 841     3307   3706   3728     22   -362     19       O  
ATOM   6154  CB  TYR A 841     -18.364 -59.548  16.441  1.00 30.10           C  
ANISOU 6154  CB  TYR A 841     3527   4010   3902     89   -564     45       C  
ATOM   6155  CG  TYR A 841     -19.845 -59.426  16.802  1.00 32.93           C  
ANISOU 6155  CG  TYR A 841     3975   4392   4145     74   -531     46       C  
ATOM   6156  CD1 TYR A 841     -20.834 -60.066  16.053  1.00 36.36           C  
ANISOU 6156  CD1 TYR A 841     4458   4800   4556     78   -454     82       C  
ATOM   6157  CD2 TYR A 841     -20.230 -58.675  17.895  1.00 34.14           C  
ANISOU 6157  CD2 TYR A 841     4156   4602   4216     58   -579      0       C  
ATOM   6158  CE1 TYR A 841     -22.173 -59.950  16.396  1.00 37.16           C  
ANISOU 6158  CE1 TYR A 841     4628   4932   4561     62   -423     80       C  
ATOM   6159  CE2 TYR A 841     -21.534 -58.530  18.243  1.00 36.98           C  
ANISOU 6159  CE2 TYR A 841     4579   5000   4473     47   -544    -14       C  
ATOM   6160  CZ  TYR A 841     -22.504 -59.162  17.506  1.00 38.61           C  
ANISOU 6160  CZ  TYR A 841     4827   5181   4663     47   -466     31       C  
ATOM   6161  OH  TYR A 841     -23.783 -58.957  17.921  1.00 39.39           O  
ANISOU 6161  OH  TYR A 841     4974   5329   4664     35   -434     10       O  
ATOM   6162  N  ASER A 842     -17.688 -57.131  14.395  0.57 27.51           N  
ANISOU 6162  N  ASER A 842     3087   3618   3747     -4   -460    -21       N  
ATOM   6163  N  BSER A 842     -17.692 -57.132  14.378  0.43 27.46           N  
ANISOU 6163  N  BSER A 842     3081   3612   3741     -4   -459    -21       N  
ATOM   6164  CA ASER A 842     -18.047 -55.880  13.729  0.57 26.67           C  
ANISOU 6164  CA ASER A 842     2980   3476   3678    -58   -425    -35       C  
ATOM   6165  CA BSER A 842     -18.092 -55.893  13.714  0.43 26.57           C  
ANISOU 6165  CA BSER A 842     2970   3464   3663    -57   -422    -34       C  
ATOM   6166  C  ASER A 842     -18.286 -56.091  12.225  0.57 24.84           C  
ANISOU 6166  C  ASER A 842     2741   3235   3462    -73   -322     11       C  
ATOM   6167  C  BSER A 842     -18.305 -56.102  12.213  0.43 24.80           C  
ANISOU 6167  C  BSER A 842     2737   3230   3456    -73   -320     12       C  
ATOM   6168  O  ASER A 842     -19.159 -55.437  11.646  0.57 23.05           O  
ANISOU 6168  O  ASER A 842     2558   2980   3221   -102   -284     22       O  
ATOM   6169  O  BSER A 842     -19.160 -55.439  11.617  0.43 23.22           O  
ANISOU 6169  O  BSER A 842     2579   3001   3243   -102   -283     23       O  
ATOM   6170  CB ASER A 842     -16.958 -54.825  13.960  0.57 27.53           C  
ANISOU 6170  CB ASER A 842     3005   3568   3886   -103   -485    -64       C  
ATOM   6171  CB BSER A 842     -17.052 -54.806  13.934  0.43 27.55           C  
ANISOU 6171  CB BSER A 842     3014   3569   3885   -103   -481    -64       C  
ATOM   6172  OG ASER A 842     -16.799 -54.509  15.350  0.57 28.86           O  
ANISOU 6172  OG ASER A 842     3182   3752   4031    -90   -588   -125       O  
ATOM   6173  OG BSER A 842     -15.810 -55.241  13.447  0.43 29.18           O  
ANISOU 6173  OG BSER A 842     3124   3797   4165   -106   -467    -39       O  
ATOM   6174  N   GLU A 843     -17.555 -57.017  11.583  1.00 24.37           N  
ANISOU 6174  N   GLU A 843     2626   3203   3428    -49   -280     32       N  
ATOM   6175  CA  GLU A 843     -17.826 -57.304  10.166  1.00 25.27           C  
ANISOU 6175  CA  GLU A 843     2735   3333   3534    -58   -180     60       C  
ATOM   6176  C   GLU A 843     -19.212 -57.955   9.996  1.00 26.04           C  
ANISOU 6176  C   GLU A 843     2933   3416   3545    -27   -147     67       C  
ATOM   6177  O   GLU A 843     -19.953 -57.649   9.046  1.00 21.12           O  
ANISOU 6177  O   GLU A 843     2341   2791   2893    -52    -87     87       O  
ATOM   6178  CB  GLU A 843     -16.698 -58.159   9.555  1.00 28.55           C  
ANISOU 6178  CB  GLU A 843     3055   3794   3998    -30   -144     52       C  
ATOM   6179  CG  GLU A 843     -16.978 -58.559   8.077  1.00 33.48           C  
ANISOU 6179  CG  GLU A 843     3670   4459   4592    -32    -38     61       C  
ATOM   6180  CD  GLU A 843     -15.995 -59.590   7.529  1.00 37.60           C  
ANISOU 6180  CD  GLU A 843     4096   5034   5155     18     -1     21       C  
ATOM   6181  OE1 GLU A 843     -14.760 -59.360   7.592  1.00 38.10           O  
ANISOU 6181  OE1 GLU A 843     4048   5135   5292      5    -10      8       O  
ATOM   6182  OE2 GLU A 843     -16.469 -60.648   7.040  1.00 37.72           O  
ANISOU 6182  OE2 GLU A 843     4142   5052   5139     72     33     -7       O  
ATOM   6183  N   ILE A 844     -19.612 -58.816  10.937  1.00 24.73           N  
ANISOU 6183  N   ILE A 844     2816   3243   3337     19   -192     60       N  
ATOM   6184  CA  ILE A 844     -20.916 -59.445  10.845  1.00 22.53           C  
ANISOU 6184  CA  ILE A 844     2621   2952   2986     38   -164     71       C  
ATOM   6185  C   ILE A 844     -22.031 -58.401  11.067  1.00 22.25           C  
ANISOU 6185  C   ILE A 844     2644   2904   2905      5   -164     63       C  
ATOM   6186  O   ILE A 844     -23.088 -58.465  10.451  1.00 20.10           O  
ANISOU 6186  O   ILE A 844     2419   2623   2595      1   -118     71       O  
ATOM   6187  CB  ILE A 844     -20.988 -60.602  11.859  1.00 23.59           C  
ANISOU 6187  CB  ILE A 844     2785   3083   3094     82   -219     86       C  
ATOM   6188  CG1 ILE A 844     -20.039 -61.767  11.435  1.00 22.83           C  
ANISOU 6188  CG1 ILE A 844     2632   2977   3067    130   -222     86       C  
ATOM   6189  CG2 ILE A 844     -22.428 -61.026  12.083  1.00 22.73           C  
ANISOU 6189  CG2 ILE A 844     2761   2967   2906     81   -202    105       C  
ATOM   6190  CD1 ILE A 844     -20.285 -62.269   9.906  1.00 22.64           C  
ANISOU 6190  CD1 ILE A 844     2594   2950   3058    142   -133     66       C  
ATOM   6191  N   LEU A 845     -21.802 -57.416  11.938  1.00 25.33           N  
ANISOU 6191  N   LEU A 845     3024   3292   3308    -16   -222     35       N  
ATOM   6192  CA  LEU A 845     -22.801 -56.364  12.123  1.00 25.40           C  
ANISOU 6192  CA  LEU A 845     3074   3280   3296    -37   -230      5       C  
ATOM   6193  C   LEU A 845     -22.985 -55.532  10.845  1.00 22.99           C  
ANISOU 6193  C   LEU A 845     2758   2936   3041    -76   -187     30       C  
ATOM   6194  O   LEU A 845     -24.098 -55.158  10.512  1.00 23.02           O  
ANISOU 6194  O   LEU A 845     2806   2919   3021    -79   -169     27       O  
ATOM   6195  CB  LEU A 845     -22.397 -55.474  13.297  1.00 24.82           C  
ANISOU 6195  CB  LEU A 845     2981   3209   3239    -45   -312    -52       C  
ATOM   6196  CG  LEU A 845     -22.448 -56.149  14.677  1.00 25.66           C  
ANISOU 6196  CG  LEU A 845     3112   3376   3263    -14   -362    -73       C  
ATOM   6197  CD1 LEU A 845     -22.045 -55.174  15.783  1.00 26.22           C  
ANISOU 6197  CD1 LEU A 845     3160   3463   3340    -21   -446   -149       C  
ATOM   6198  CD2 LEU A 845     -23.865 -56.750  14.979  1.00 26.45           C  
ANISOU 6198  CD2 LEU A 845     3280   3511   3257      4   -325    -67       C  
ATOM   6199  N   THR A 846     -21.892 -55.197  10.154  1.00 23.84           N  
ANISOU 6199  N   THR A 846     2800   3040   3218   -110   -175     60       N  
ATOM   6200  CA  THR A 846     -21.990 -54.581   8.830  1.00 24.74           C  
ANISOU 6200  CA  THR A 846     2901   3139   3361   -156   -127    111       C  
ATOM   6201  C   THR A 846     -22.786 -55.461   7.844  1.00 22.80           C  
ANISOU 6201  C   THR A 846     2696   2923   3043   -135    -54    136       C  
ATOM   6202  O   THR A 846     -23.677 -54.984   7.148  1.00 22.16           O  
ANISOU 6202  O   THR A 846     2653   2822   2944   -153    -37    162       O  
ATOM   6203  CB  THR A 846     -20.553 -54.318   8.317  1.00 26.25           C  
ANISOU 6203  CB  THR A 846     2999   3354   3622   -201   -114    145       C  
ATOM   6204  OG1 THR A 846     -19.852 -53.450   9.260  1.00 28.70           O  
ANISOU 6204  OG1 THR A 846     3269   3626   4010   -226   -195    115       O  
ATOM   6205  CG2 THR A 846     -20.590 -53.625   7.005  1.00 25.65           C  
ANISOU 6205  CG2 THR A 846     2906   3279   3561   -265    -67    217       C  
ATOM   6206  N   LEU A 847     -22.452 -56.751   7.752  1.00 19.25           N  
ANISOU 6206  N   LEU A 847     2234   2516   2563    -93    -21    125       N  
ATOM   6207  CA  LEU A 847     -23.217 -57.674   6.911  1.00 22.01           C  
ANISOU 6207  CA  LEU A 847     2621   2887   2853    -67     36    129       C  
ATOM   6208  C   LEU A 847     -24.728 -57.647   7.252  1.00 21.71           C  
ANISOU 6208  C   LEU A 847     2664   2818   2767    -55     22    119       C  
ATOM   6209  O   LEU A 847     -25.590 -57.743   6.368  1.00 22.93           O  
ANISOU 6209  O   LEU A 847     2851   2977   2885    -59     57    132       O  
ATOM   6210  CB  LEU A 847     -22.630 -59.096   7.103  1.00 22.52           C  
ANISOU 6210  CB  LEU A 847     2662   2974   2922    -14     43    101       C  
ATOM   6211  CG  LEU A 847     -23.286 -60.226   6.307  1.00 24.62           C  
ANISOU 6211  CG  LEU A 847     2957   3250   3148     20     88     85       C  
ATOM   6212  CD1 LEU A 847     -22.885 -60.037   4.820  1.00 25.05           C  
ANISOU 6212  CD1 LEU A 847     2965   3366   3187     -3    159     86       C  
ATOM   6213  CD2 LEU A 847     -22.881 -61.626   6.840  1.00 24.27           C  
ANISOU 6213  CD2 LEU A 847     2901   3187   3133     79     61     57       C  
ATOM   6214  N   LYS A 848     -25.074 -57.579   8.540  1.00 18.31           N  
ANISOU 6214  N   LYS A 848     2260   2371   2328    -38    -29     92       N  
ATOM   6215  CA  LYS A 848     -26.495 -57.608   8.917  1.00 18.11           C  
ANISOU 6215  CA  LYS A 848     2292   2336   2252    -27    -33     76       C  
ATOM   6216  C   LYS A 848     -27.215 -56.303   8.601  1.00 18.02           C  
ANISOU 6216  C   LYS A 848     2293   2291   2262    -51    -46     68       C  
ATOM   6217  O   LYS A 848     -28.451 -56.264   8.605  1.00 19.88           O  
ANISOU 6217  O   LYS A 848     2565   2522   2466    -40    -41     51       O  
ATOM   6218  CB  LYS A 848     -26.629 -57.859  10.449  1.00 20.50           C  
ANISOU 6218  CB  LYS A 848     2609   2658   2521     -8    -78     47       C  
ATOM   6219  CG  LYS A 848     -26.262 -59.298  10.899  1.00 23.10           C  
ANISOU 6219  CG  LYS A 848     2943   3007   2827     17    -82     72       C  
ATOM   6220  CD  LYS A 848     -26.642 -59.485  12.370  1.00 28.42           C  
ANISOU 6220  CD  LYS A 848     3640   3719   3439     22   -124     65       C  
ATOM   6221  CE  LYS A 848     -26.058 -60.743  12.981  1.00 32.56           C  
ANISOU 6221  CE  LYS A 848     4165   4252   3954     39   -156    110       C  
ATOM   6222  NZ  LYS A 848     -26.735 -61.046  14.266  1.00 30.92           N  
ANISOU 6222  NZ  LYS A 848     3991   4099   3657     30   -184    128       N  
ATOM   6223  N   THR A 849     -26.480 -55.207   8.440  1.00 18.11           N  
ANISOU 6223  N   THR A 849     2269   2272   2338    -83    -75     78       N  
ATOM   6224  CA  THR A 849     -27.158 -53.975   8.061  1.00 17.86           C  
ANISOU 6224  CA  THR A 849     2249   2186   2349   -105   -104     82       C  
ATOM   6225  C   THR A 849     -27.202 -53.766   6.551  1.00 19.54           C  
ANISOU 6225  C   THR A 849     2462   2395   2567   -141    -68    157       C  
ATOM   6226  O   THR A 849     -27.857 -52.819   6.092  1.00 20.09           O  
ANISOU 6226  O   THR A 849     2547   2414   2674   -159   -100    180       O  
ATOM   6227  CB  THR A 849     -26.464 -52.748   8.704  1.00 20.34           C  
ANISOU 6227  CB  THR A 849     2529   2448   2752   -130   -174     56       C  
ATOM   6228  OG1 THR A 849     -25.119 -52.674   8.205  1.00 22.93           O  
ANISOU 6228  OG1 THR A 849     2804   2784   3123   -173   -162    110       O  
ATOM   6229  CG2 THR A 849     -26.424 -52.864  10.273  1.00 21.31           C  
ANISOU 6229  CG2 THR A 849     2651   2594   2851    -94   -218    -33       C  
ATOM   6230  N   TYR A 850     -26.529 -54.608   5.780  1.00 23.71           N  
ANISOU 6230  N   TYR A 850     2969   2981   3058   -148    -10    193       N  
ATOM   6231  CA  TYR A 850     -26.554 -54.536   4.317  1.00 22.04           C  
ANISOU 6231  CA  TYR A 850     2754   2802   2818   -183     34    259       C  
ATOM   6232  C   TYR A 850     -27.970 -54.693   3.762  1.00 20.19           C  
ANISOU 6232  C   TYR A 850     2576   2562   2535   -164     37    259       C  
ATOM   6233  O   TYR A 850     -28.707 -55.578   4.166  1.00 20.43           O  
ANISOU 6233  O   TYR A 850     2635   2602   2525   -120     48    208       O  
ATOM   6234  CB  TYR A 850     -25.685 -55.649   3.732  1.00 20.29           C  
ANISOU 6234  CB  TYR A 850     2495   2663   2552   -173    101    256       C  
ATOM   6235  CG  TYR A 850     -25.658 -55.652   2.202  1.00 21.81           C  
ANISOU 6235  CG  TYR A 850     2677   2923   2686   -209    156    310       C  
ATOM   6236  CD1 TYR A 850     -24.984 -54.661   1.506  1.00 25.04           C  
ANISOU 6236  CD1 TYR A 850     3045   3353   3116   -281    162    393       C  
ATOM   6237  CD2 TYR A 850     -26.373 -56.621   1.462  1.00 22.86           C  
ANISOU 6237  CD2 TYR A 850     2841   3104   2741   -176    196    282       C  
ATOM   6238  CE1 TYR A 850     -24.930 -54.654   0.093  1.00 24.68           C  
ANISOU 6238  CE1 TYR A 850     2987   3398   2992   -323    216    454       C  
ATOM   6239  CE2 TYR A 850     -26.331 -56.616   0.075  1.00 22.57           C  
ANISOU 6239  CE2 TYR A 850     2793   3152   2632   -208    243    322       C  
ATOM   6240  CZ  TYR A 850     -25.598 -55.657  -0.585  1.00 25.06           C  
ANISOU 6240  CZ  TYR A 850     3067   3508   2948   -280    257    409       C  
ATOM   6241  OH  TYR A 850     -25.554 -55.663  -1.953  1.00 30.81           O  
ANISOU 6241  OH  TYR A 850     3781   4344   3580   -319    307    457       O  
ATOM   6242  N   LEU A 851     -28.296 -53.884   2.748  1.00 20.63           N  
ANISOU 6242  N   LEU A 851     2639   2606   2592   -205     26    328       N  
ATOM   6243  CA  LEU A 851     -29.558 -53.965   2.019  1.00 19.62           C  
ANISOU 6243  CA  LEU A 851     2555   2480   2418   -192     21    340       C  
ATOM   6244  C   LEU A 851     -29.212 -54.177   0.541  1.00 21.60           C  
ANISOU 6244  C   LEU A 851     2798   2816   2595   -232     69    410       C  
ATOM   6245  O   LEU A 851     -28.597 -53.303  -0.094  1.00 19.50           O  
ANISOU 6245  O   LEU A 851     2507   2557   2344   -295     61    500       O  
ATOM   6246  CB  LEU A 851     -30.379 -52.672   2.196  1.00 19.24           C  
ANISOU 6246  CB  LEU A 851     2526   2339   2446   -200    -60    361       C  
ATOM   6247  CG  LEU A 851     -31.776 -52.666   1.498  1.00 20.81           C  
ANISOU 6247  CG  LEU A 851     2763   2532   2613   -181    -82    370       C  
ATOM   6248  CD1 LEU A 851     -32.735 -53.566   2.187  1.00 19.09           C  
ANISOU 6248  CD1 LEU A 851     2562   2328   2364   -122    -65    276       C  
ATOM   6249  CD2 LEU A 851     -32.394 -51.277   1.445  1.00 25.16           C  
ANISOU 6249  CD2 LEU A 851     3320   2982   3258   -191   -175    407       C  
ATOM   6250  N   HIS A 852     -29.651 -55.298  -0.037  1.00 20.04           N  
ANISOU 6250  N   HIS A 852     2616   2684   2313   -201    115    371       N  
ATOM   6251  CA  HIS A 852     -29.446 -55.456  -1.482  1.00 23.34           C  
ANISOU 6251  CA  HIS A 852     3026   3202   2639   -235    158    421       C  
ATOM   6252  C   HIS A 852     -30.485 -54.608  -2.231  1.00 24.70           C  
ANISOU 6252  C   HIS A 852     3238   3351   2794   -262    103    496       C  
ATOM   6253  O   HIS A 852     -31.700 -54.877  -2.171  1.00 23.52           O  
ANISOU 6253  O   HIS A 852     3127   3170   2639   -223     70    455       O  
ATOM   6254  CB  HIS A 852     -29.522 -56.940  -1.865  1.00 26.71           C  
ANISOU 6254  CB  HIS A 852     3453   3704   2993   -188    214    334       C  
ATOM   6255  CG  HIS A 852     -28.858 -57.216  -3.184  1.00 36.14           C  
ANISOU 6255  CG  HIS A 852     4613   5031   4087   -218    276    353       C  
ATOM   6256  ND1 HIS A 852     -29.519 -57.148  -4.383  1.00 41.88           N  
ANISOU 6256  ND1 HIS A 852     5366   5832   4717   -238    276    386       N  
ATOM   6257  CD2 HIS A 852     -27.558 -57.430  -3.496  1.00 41.09           C  
ANISOU 6257  CD2 HIS A 852     5174   5746   4692   -236    339    348       C  
ATOM   6258  CE1 HIS A 852     -28.683 -57.390  -5.376  1.00 41.87           C  
ANISOU 6258  CE1 HIS A 852     5319   5969   4621   -266    343    392       C  
ATOM   6259  NE2 HIS A 852     -27.482 -57.561  -4.865  1.00 43.11           N  
ANISOU 6259  NE2 HIS A 852     5415   6138   4826   -265    386    367       N  
ATOM   6260  N   THR A 853     -30.062 -53.536  -2.902  1.00 28.30           N  
ANISOU 6260  N   THR A 853     3682   3815   3254   -332     81    613       N  
ATOM   6261  CA  THR A 853     -31.096 -52.626  -3.400  1.00 29.70           C  
ANISOU 6261  CA  THR A 853     3900   3937   3449   -350      0    691       C  
ATOM   6262  C   THR A 853     -31.561 -52.905  -4.831  1.00 32.95           C  
ANISOU 6262  C   THR A 853     4333   4459   3728   -373     14    746       C  
ATOM   6263  O   THR A 853     -32.613 -52.344  -5.227  1.00 37.53           O  
ANISOU 6263  O   THR A 853     4950   4992   4317   -372    -64    796       O  
ATOM   6264  CB  THR A 853     -30.635 -51.173  -3.400  1.00 30.50           C  
ANISOU 6264  CB  THR A 853     3987   3957   3644   -419    -65    813       C  
ATOM   6265  OG1 THR A 853     -29.522 -51.074  -4.303  1.00 30.52           O  
ANISOU 6265  OG1 THR A 853     3952   4072   3573   -500     -6    913       O  
ATOM   6266  CG2 THR A 853     -30.265 -50.672  -1.944  1.00 30.60           C  
ANISOU 6266  CG2 THR A 853     3979   3845   3802   -397   -103    750       C  
ATOM   6267  N   TYR A 854     -30.789 -53.653  -5.649  1.00 30.61           N  
ANISOU 6267  N   TYR A 854     4008   4313   3308   -395    101    740       N  
ATOM   6268  CA  TYR A 854     -31.128 -53.943  -7.061  1.00 31.33           C  
ANISOU 6268  CA  TYR A 854     4115   4542   3247   -420    120    780       C  
ATOM   6269  C   TYR A 854     -31.005 -52.723  -7.963  1.00 35.90           C  
ANISOU 6269  C   TYR A 854     4700   5150   3790   -514     75    964       C  
ATOM   6270  O   TYR A 854     -31.529 -52.708  -9.083  1.00 36.63           O  
ANISOU 6270  O   TYR A 854     4817   5340   3760   -539     57   1025       O  
ATOM   6271  CB  TYR A 854     -32.532 -54.567  -7.201  1.00 29.99           C  
ANISOU 6271  CB  TYR A 854     3992   4351   3050   -356     77    700       C  
ATOM   6272  CG  TYR A 854     -32.620 -55.880  -6.402  1.00 30.74           C  
ANISOU 6272  CG  TYR A 854     4080   4425   3174   -279    123    535       C  
ATOM   6273  CD1 TYR A 854     -32.054 -57.055  -6.900  1.00 33.11           C  
ANISOU 6273  CD1 TYR A 854     4354   4842   3385   -257    201    443       C  
ATOM   6274  CD2 TYR A 854     -33.127 -55.900  -5.095  1.00 29.78           C  
ANISOU 6274  CD2 TYR A 854     3968   4168   3177   -232     87    477       C  
ATOM   6275  CE1 TYR A 854     -32.080 -58.264  -6.127  1.00 33.92           C  
ANISOU 6275  CE1 TYR A 854     4448   4902   3539   -190    228    307       C  
ATOM   6276  CE2 TYR A 854     -33.185 -57.087  -4.329  1.00 28.27           C  
ANISOU 6276  CE2 TYR A 854     3772   3957   3013   -175    122    354       C  
ATOM   6277  CZ  TYR A 854     -32.636 -58.266  -4.848  1.00 34.59           C  
ANISOU 6277  CZ  TYR A 854     4551   4849   3741   -156    187    278       C  
ATOM   6278  OH  TYR A 854     -32.662 -59.446  -4.084  1.00 38.21           O  
ANISOU 6278  OH  TYR A 854     5004   5267   4247   -103    206    171       O  
ATOM   6279  N   GLU A 855     -30.312 -51.694  -7.503  1.00 38.28           N  
ANISOU 6279  N   GLU A 855     4977   5369   4198   -571     47   1061       N  
ATOM   6280  CA  GLU A 855     -30.063 -50.508  -8.296  1.00 43.29           C  
ANISOU 6280  CA  GLU A 855     5610   6015   4821   -676     -2   1258       C  
ATOM   6281  C   GLU A 855     -28.673 -50.606  -8.933  1.00 46.26           C  
ANISOU 6281  C   GLU A 855     5919   6560   5096   -761    104   1324       C  
ATOM   6282  O   GLU A 855     -27.723 -51.114  -8.331  1.00 44.90           O  
ANISOU 6282  O   GLU A 855     5691   6414   4956   -743    181   1233       O  
ATOM   6283  CB  GLU A 855     -30.158 -49.248  -7.429  1.00 46.08           C  
ANISOU 6283  CB  GLU A 855     5971   6160   5376   -695   -110   1327       C  
ATOM   6284  CG  GLU A 855     -31.553 -48.948  -6.853  1.00 46.96           C  
ANISOU 6284  CG  GLU A 855     6134   6112   5596   -615   -221   1269       C  
ATOM   6285  CD  GLU A 855     -32.479 -48.297  -7.887  1.00 54.98           C  
ANISOU 6285  CD  GLU A 855     7195   7121   6575   -646   -319   1405       C  
ATOM   6286  OE1 GLU A 855     -33.481 -48.936  -8.288  1.00 58.36           O  
ANISOU 6286  OE1 GLU A 855     7656   7599   6921   -589   -328   1342       O  
ATOM   6287  OE2 GLU A 855     -32.210 -47.132  -8.302  1.00 56.45           O  
ANISOU 6287  OE2 GLU A 855     7382   7246   6823   -732   -397   1582       O  
ATOM   6288  N   SER A 856     -28.572 -50.122 -10.161  1.00 49.44           N  
ANISOU 6288  N   SER A 856     6322   7088   5374   -854    104   1484       N  
ATOM   6289  CA  SER A 856     -27.271 -49.978 -10.801  1.00 54.17           C  
ANISOU 6289  CA  SER A 856     6846   7855   5880   -958    200   1579       C  
ATOM   6290  C   SER A 856     -26.330 -49.139  -9.933  1.00 57.77           C  
ANISOU 6290  C   SER A 856     7251   8184   6515  -1015    182   1642       C  
ATOM   6291  O   SER A 856     -26.756 -48.367  -9.066  1.00 57.54           O  
ANISOU 6291  O   SER A 856     7256   7936   6671   -998     71   1660       O  
ATOM   6292  CB  SER A 856     -27.429 -49.335 -12.172  1.00 55.53           C  
ANISOU 6292  CB  SER A 856     7034   8162   5901  -1068    178   1784       C  
ATOM   6293  OG  SER A 856     -27.848 -47.992 -12.038  1.00 56.23           O  
ANISOU 6293  OG  SER A 856     7164   8070   6130  -1132     39   1967       O  
ATOM   6294  N   GLU A 857     -25.024 -49.327 -10.151  1.00 58.59           N  
ANISOU 6294  N   GLU A 857     7262   8432   6566  -1078    292   1655       N  
ATOM   6295  CA  GLU A 857     -24.025 -48.583  -9.399  1.00 56.96           C  
ANISOU 6295  CA  GLU A 857     6992   8126   6523  -1142    279   1712       C  
ATOM   6296  C   GLU A 857     -24.076 -47.110  -9.786  1.00 56.48           C  
ANISOU 6296  C   GLU A 857     6948   7971   6541  -1274    177   1956       C  
ATOM   6297  O   GLU A 857     -24.313 -46.758 -10.944  1.00 55.87           O  
ANISOU 6297  O   GLU A 857     6888   8009   6329  -1360    172   2121       O  
ATOM   6298  CB  GLU A 857     -22.623 -49.149  -9.654  1.00 58.03           C  
ANISOU 6298  CB  GLU A 857     7010   8460   6578  -1183    424   1672       C  
ATOM   6299  N   ILE A 858     -23.851 -46.251  -8.799  1.00 57.27           N  
ANISOU 6299  N   ILE A 858     7041   7858   6863  -1291     86   1979       N  
ATOM   6300  CA  ILE A 858     -23.884 -44.813  -9.011  1.00 58.14           C  
ANISOU 6300  CA  ILE A 858     7163   7828   7100  -1410    -36   2199       C  
ATOM   6301  C   ILE A 858     -22.552 -44.345  -9.597  1.00 60.85           C  
ANISOU 6301  C   ILE A 858     7408   8295   7417  -1549     33   2332       C  
ATOM   6302  O   ILE A 858     -22.533 -43.646 -10.618  1.00 63.01           O  
ANISOU 6302  O   ILE A 858     7688   8617   7636  -1621      1   2471       O  
ATOM   6303  CB  ILE A 858     -24.211 -44.072  -7.694  1.00 54.35           C  
ANISOU 6303  CB  ILE A 858     6710   7058   6882  -1356   -173   2129       C  
ATOM   6304  CG1 ILE A 858     -25.596 -44.474  -7.175  1.00 49.04           C  
ANISOU 6304  CG1 ILE A 858     6126   6278   6230  -1205   -239   1975       C  
ATOM   6305  CG2 ILE A 858     -24.101 -42.567  -7.892  1.00 55.31           C  
ANISOU 6305  CG2 ILE A 858     6831   7014   7169  -1484   -308   2350       C  
ATOM   6306  CD1 ILE A 858     -26.083 -43.587  -6.064  1.00 45.12           C  
ANISOU 6306  CD1 ILE A 858     5656   5513   5975  -1158   -385   1922       C  
TER    6307      ILE A 858                                                      
ATOM   6308  O5'  DC B2001     -34.799  -1.294 -24.076  1.00 95.62           O  
ANISOU 6308  O5'  DC B2001    13567   9285  13479  -1974  -3211   4575       O  
ATOM   6309  C5'  DC B2001     -35.515  -1.264 -22.834  1.00 94.34           C  
ANISOU 6309  C5'  DC B2001    13522   8878  13445  -1870  -3225   4399       C  
ATOM   6310  C4'  DC B2001     -36.146   0.109 -22.595  1.00 97.10           C  
ANISOU 6310  C4'  DC B2001    14025   8813  14056  -1764  -3306   4438       C  
ATOM   6311  O4'  DC B2001     -36.540   0.710 -23.865  1.00 99.11           O  
ANISOU 6311  O4'  DC B2001    14190   9102  14364  -1709  -3362   4656       O  
ATOM   6312  C3'  DC B2001     -37.415   0.081 -21.751  1.00 96.86           C  
ANISOU 6312  C3'  DC B2001    14084   8534  14183  -1526  -3253   4313       C  
ATOM   6313  O3'  DC B2001     -37.094   0.233 -20.391  1.00 97.53           O  
ANISOU 6313  O3'  DC B2001    14397   8360  14302  -1564  -3215   4104       O  
ATOM   6314  C2'  DC B2001     -38.200   1.277 -22.279  1.00 99.89           C  
ANISOU 6314  C2'  DC B2001    14502   8653  14799  -1369  -3289   4474       C  
ATOM   6315  C1'  DC B2001     -37.865   1.230 -23.767  1.00101.20           C  
ANISOU 6315  C1'  DC B2001    14482   9126  14844  -1475  -3371   4691       C  
ATOM   6316  N1   DC B2001     -38.816   0.356 -24.594  1.00101.05           N  
ANISOU 6316  N1   DC B2001    14260   9393  14742  -1369  -3383   4778       N  
ATOM   6317  C2   DC B2001     -40.099   0.826 -24.942  1.00103.35           C  
ANISOU 6317  C2   DC B2001    14470   9559  15238  -1163  -3424   4916       C  
ATOM   6318  O2   DC B2001     -40.456   1.954 -24.578  1.00106.20           O  
ANISOU 6318  O2   DC B2001    14936   9563  15851  -1033  -3404   4962       O  
ATOM   6319  N3   DC B2001     -40.917   0.021 -25.676  1.00102.91           N  
ANISOU 6319  N3   DC B2001    14229   9776  15097  -1120  -3478   5004       N  
ATOM   6320  C4   DC B2001     -40.503  -1.194 -26.051  1.00100.12           C  
ANISOU 6320  C4   DC B2001    13825   9770  14445  -1260  -3467   4933       C  
ATOM   6321  N4   DC B2001     -41.338  -1.947 -26.769  1.00 99.65           N  
ANISOU 6321  N4   DC B2001    13631   9944  14287  -1244  -3539   5011       N  
ATOM   6322  C5   DC B2001     -39.213  -1.688 -25.707  1.00 98.28           C  
ANISOU 6322  C5   DC B2001    13684   9653  14006  -1427  -3375   4789       C  
ATOM   6323  C6   DC B2001     -38.412  -0.891 -24.990  1.00 99.05           C  
ANISOU 6323  C6   DC B2001    13910   9513  14213  -1480  -3348   4730       C  
ATOM   6324  P    DC B2002     -37.910  -0.583 -19.275  1.00 97.64           P  
ANISOU 6324  P    DC B2002    14478   8288  14331  -1388  -3095   3889       P  
ATOM   6325  OP1  DC B2002     -37.359  -0.237 -17.949  1.00 99.11           O  
ANISOU 6325  OP1  DC B2002    14971   8180  14508  -1487  -3073   3669       O  
ATOM   6326  OP2  DC B2002     -37.969  -2.012 -19.666  1.00 93.35           O  
ANISOU 6326  OP2  DC B2002    13695   8176  13598  -1404  -3068   3892       O  
ATOM   6327  O5'  DC B2002     -39.361   0.064 -19.336  1.00101.37           O  
ANISOU 6327  O5'  DC B2002    14969   8473  15075  -1061  -3018   3958       O  
ATOM   6328  C5'  DC B2002     -39.617   1.309 -18.716  1.00106.22           C  
ANISOU 6328  C5'  DC B2002    15870   8600  15889   -947  -2943   3909       C  
ATOM   6329  C4'  DC B2002     -41.087   1.663 -18.843  1.00109.79           C  
ANISOU 6329  C4'  DC B2002    16249   8858  16609   -583  -2811   4018       C  
ATOM   6330  O4'  DC B2002     -41.428   1.750 -20.248  1.00110.55           O  
ANISOU 6330  O4'  DC B2002    16045   9221  16739   -577  -2937   4300       O  
ATOM   6331  C3'  DC B2002     -42.055   0.627 -18.283  1.00109.19           C  
ANISOU 6331  C3'  DC B2002    16041   8866  16580   -354  -2681   3928       C  
ATOM   6332  O3'  DC B2002     -42.244   0.808 -16.853  1.00111.31           O  
ANISOU 6332  O3'  DC B2002    16643   8735  16913   -208  -2468   3670       O  
ATOM   6333  C2'  DC B2002     -43.321   0.928 -19.077  1.00111.15           C  
ANISOU 6333  C2'  DC B2002    16026   9136  17070    -86  -2655   4189       C  
ATOM   6334  C1'  DC B2002     -42.758   1.296 -20.449  1.00111.28           C  
ANISOU 6334  C1'  DC B2002    15898   9398  16986   -309  -2874   4408       C  
ATOM   6335  N1   DC B2002     -42.741   0.154 -21.432  1.00108.61           N  
ANISOU 6335  N1   DC B2002    15250   9576  16440   -455  -3031   4509       N  
ATOM   6336  C2   DC B2002     -43.940  -0.263 -22.040  1.00109.22           C  
ANISOU 6336  C2   DC B2002    15037   9836  16626   -296  -3069   4686       C  
ATOM   6337  O2   DC B2002     -45.000   0.310 -21.745  1.00112.57           O  
ANISOU 6337  O2   DC B2002    15407  10014  17349    -14  -2959   4782       O  
ATOM   6338  N3   DC B2002     -43.904  -1.290 -22.938  1.00105.97           N  
ANISOU 6338  N3   DC B2002    14423   9861  15980   -465  -3212   4752       N  
ATOM   6339  C4   DC B2002     -42.740  -1.879 -23.234  1.00102.87           C  
ANISOU 6339  C4   DC B2002    14108   9708  15270   -730  -3261   4653       C  
ATOM   6340  N4   DC B2002     -42.751  -2.879 -24.123  1.00100.67           N  
ANISOU 6340  N4   DC B2002    13693   9814  14742   -871  -3350   4701       N  
ATOM   6341  C5   DC B2002     -41.511  -1.465 -22.630  1.00102.47           C  
ANISOU 6341  C5   DC B2002    14288   9503  15142   -868  -3206   4506       C  
ATOM   6342  C6   DC B2002     -41.558  -0.454 -21.748  1.00105.31           C  
ANISOU 6342  C6   DC B2002    14850   9442  15723   -747  -3121   4438       C  
ATOM   6343  P    DT B2003     -43.466   0.088 -16.080  1.00111.41           P  
ANISOU 6343  P    DT B2003    16577   8677  17077    143  -2237   3580       P  
ATOM   6344  OP1  DT B2003     -43.231   0.149 -14.619  1.00111.24           O  
ANISOU 6344  OP1  DT B2003    16974   8298  16994    182  -2042   3252       O  
ATOM   6345  OP2  DT B2003     -43.657  -1.240 -16.689  1.00108.21           O  
ANISOU 6345  OP2  DT B2003    15777   8776  16564     79  -2370   3668       O  
ATOM   6346  O5'  DT B2003     -44.724   1.017 -16.448  1.00116.38           O  
ANISOU 6346  O5'  DT B2003    17113   9058  18045    508  -2072   3811       O  
ATOM   6347  C5'  DT B2003     -45.924   0.941 -15.703  1.00117.98           C  
ANISOU 6347  C5'  DT B2003    17310   9041  18476    909  -1769   3780       C  
ATOM   6348  C4'  DT B2003     -47.022   0.214 -16.467  1.00116.87           C  
ANISOU 6348  C4'  DT B2003    16633   9282  18491   1070  -1827   4036       C  
ATOM   6349  O4'  DT B2003     -46.575  -0.177 -17.784  1.00114.18           O  
ANISOU 6349  O4'  DT B2003    16000   9390  17994    768  -2173   4226       O  
ATOM   6350  C3'  DT B2003     -47.477  -1.073 -15.806  1.00114.12           C  
ANISOU 6350  C3'  DT B2003    16109   9130  18122   1176  -1727   3901       C  
ATOM   6351  O3'  DT B2003     -48.592  -0.809 -14.987  1.00117.89           O  
ANISOU 6351  O3'  DT B2003    16613   9324  18855   1593  -1370   3880       O  
ATOM   6352  C2'  DT B2003     -47.836  -2.009 -16.976  1.00111.24           C  
ANISOU 6352  C2'  DT B2003    15243   9313  17710   1035  -2000   4140       C  
ATOM   6353  C1'  DT B2003     -47.403  -1.235 -18.224  1.00111.66           C  
ANISOU 6353  C1'  DT B2003    15260   9457  17709    825  -2248   4359       C  
ATOM   6354  N1   DT B2003     -46.666  -2.092 -19.238  1.00105.67           N  
ANISOU 6354  N1   DT B2003    14342   9173  16636    457  -2557   4406       N  
ATOM   6355  C2   DT B2003     -47.392  -2.747 -20.208  1.00103.77           C  
ANISOU 6355  C2   DT B2003    13735   9307  16388    413  -2726   4621       C  
ATOM   6356  O2   DT B2003     -48.599  -2.668 -20.301  1.00106.50           O  
ANISOU 6356  O2   DT B2003    13821   9647  16997    635  -2673   4802       O  
ATOM   6357  N3   DT B2003     -46.650  -3.493 -21.079  1.00 99.85           N  
ANISOU 6357  N3   DT B2003    13201   9186  15550     86  -2946   4620       N  
ATOM   6358  C4   DT B2003     -45.278  -3.662 -21.080  1.00 97.67           C  
ANISOU 6358  C4   DT B2003    13158   8979  14973   -173  -2990   4456       C  
ATOM   6359  O4   DT B2003     -44.704  -4.362 -21.913  1.00 95.56           O  
ANISOU 6359  O4   DT B2003    12849   9053  14405   -424  -3125   4471       O  
ATOM   6360  C5   DT B2003     -44.567  -2.958 -20.032  1.00 98.28           C  
ANISOU 6360  C5   DT B2003    13550   8688  15106   -137  -2844   4265       C  
ATOM   6361  C7   DT B2003     -43.069  -3.064 -19.927  1.00 95.15           C  
ANISOU 6361  C7   DT B2003    13370   8358  14425   -433  -2894   4112       C  
ATOM   6362  C6   DT B2003     -45.290  -2.215 -19.169  1.00102.04           C  
ANISOU 6362  C6   DT B2003    14124   8761  15884    161  -2647   4234       C  
ATOM   6363  P    DG B2004     -49.048  -1.883 -13.883  1.00117.42           P  
ANISOU 6363  P    DG B2004    16512   9306  18796   1780  -1129   3658       P  
ATOM   6364  OP1  DG B2004     -49.965  -1.153 -12.974  1.00122.66           O  
ANISOU 6364  OP1  DG B2004    17382   9557  19666   2198   -715   3594       O  
ATOM   6365  OP2  DG B2004     -47.852  -2.609 -13.361  1.00112.20           O  
ANISOU 6365  OP2  DG B2004    16091   8707  17832   1479  -1251   3368       O  
ATOM   6366  O5'  DG B2004     -49.922  -2.934 -14.716  1.00115.11           O  
ANISOU 6366  O5'  DG B2004    15593   9539  18605   1788  -1292   3919       O  
ATOM   6367  C5'  DG B2004     -50.991  -2.491 -15.564  1.00116.33           C  
ANISOU 6367  C5'  DG B2004    15377   9804  19020   1932  -1336   4271       C  
ATOM   6368  C4'  DG B2004     -51.534  -3.663 -16.358  1.00111.95           C  
ANISOU 6368  C4'  DG B2004    14312   9771  18452   1790  -1583   4466       C  
ATOM   6369  O4'  DG B2004     -50.599  -4.011 -17.408  1.00107.57           O  
ANISOU 6369  O4'  DG B2004    13754   9518  17601   1381  -1972   4508       O  
ATOM   6370  C3'  DG B2004     -51.746  -4.932 -15.528  1.00108.11           C  
ANISOU 6370  C3'  DG B2004    13720   9448  17908   1856  -1448   4274       C  
ATOM   6371  O3'  DG B2004     -53.102  -5.329 -15.600  1.00111.42           O  
ANISOU 6371  O3'  DG B2004    13699  10045  18592   2053  -1361   4490       O  
ATOM   6372  C2'  DG B2004     -50.797  -5.973 -16.144  1.00101.75           C  
ANISOU 6372  C2'  DG B2004    12891   9019  16749   1455  -1793   4204       C  
ATOM   6373  C1'  DG B2004     -50.531  -5.409 -17.532  1.00102.31           C  
ANISOU 6373  C1'  DG B2004    12896   9240  16739   1204  -2118   4448       C  
ATOM   6374  N9   DG B2004     -49.217  -5.757 -18.072  1.00 96.64           N  
ANISOU 6374  N9   DG B2004    12379   8705  15636    828  -2364   4336       N  
ATOM   6375  C8   DG B2004     -47.989  -5.375 -17.585  1.00 94.17           C  
ANISOU 6375  C8   DG B2004    12455   8184  15142    702  -2327   4112       C  
ATOM   6376  N7   DG B2004     -46.986  -5.841 -18.277  1.00 90.64           N  
ANISOU 6376  N7   DG B2004    12072   8012  14356    359  -2549   4084       N  
ATOM   6377  C5   DG B2004     -47.586  -6.573 -19.290  1.00 89.72           C  
ANISOU 6377  C5   DG B2004    11647   8279  14162    256  -2733   4273       C  
ATOM   6378  C6   DG B2004     -47.003  -7.300 -20.342  1.00 86.50           C  
ANISOU 6378  C6   DG B2004    11218   8251  13397    -68  -2950   4308       C  
ATOM   6379  O6   DG B2004     -45.801  -7.432 -20.597  1.00 84.83           O  
ANISOU 6379  O6   DG B2004    11212   8136  12885   -304  -2992   4200       O  
ATOM   6380  N1   DG B2004     -47.966  -7.905 -21.150  1.00 87.18           N  
ANISOU 6380  N1   DG B2004    11024   8611  13490   -110  -3100   4491       N  
ATOM   6381  C2   DG B2004     -49.334  -7.811 -20.955  1.00 90.78           C  
ANISOU 6381  C2   DG B2004    11186   9011  14294    123  -3063   4657       C  
ATOM   6382  N2   DG B2004     -50.119  -8.463 -21.832  1.00 90.97           N  
ANISOU 6382  N2   DG B2004    10966   9326  14272    -17  -3265   4837       N  
ATOM   6383  N3   DG B2004     -49.892  -7.125 -19.968  1.00 93.97           N  
ANISOU 6383  N3   DG B2004    11561   9085  15060    461  -2820   4648       N  
ATOM   6384  C4   DG B2004     -48.959  -6.530 -19.180  1.00 93.46           C  
ANISOU 6384  C4   DG B2004    11831   8719  14959    516  -2657   4436       C  
ATOM   6385  P    DG B2005     -53.656  -6.492 -14.637  1.00111.39           P  
ANISOU 6385  P    DG B2005    13530  10172  18620   2214  -1130   4333       P  
ATOM   6386  OP1  DG B2005     -55.098  -6.219 -14.414  1.00116.33           O  
ANISOU 6386  OP1  DG B2005    13827  10758  19616   2524   -885   4559       O  
ATOM   6387  OP2  DG B2005     -52.724  -6.654 -13.485  1.00109.24           O  
ANISOU 6387  OP2  DG B2005    13707   9656  18144   2256   -909   3926       O  
ATOM   6388  O5'  DG B2005     -53.529  -7.799 -15.544  1.00105.75           O  
ANISOU 6388  O5'  DG B2005    12511   9969  17700   1859  -1527   4433       O  
ATOM   6389  C5'  DG B2005     -53.985  -7.778 -16.887  1.00104.60           C  
ANISOU 6389  C5'  DG B2005    12063  10098  17583   1636  -1878   4767       C  
ATOM   6390  C4'  DG B2005     -53.675  -9.098 -17.538  1.00 98.70           C  
ANISOU 6390  C4'  DG B2005    11201   9776  16525   1282  -2200   4748       C  
ATOM   6391  O4'  DG B2005     -52.329  -9.059 -18.072  1.00 94.20           O  
ANISOU 6391  O4'  DG B2005    10960   9255  15577    987  -2411   4610       O  
ATOM   6392  C3'  DG B2005     -53.729 -10.291 -16.572  1.00 94.41           C  
ANISOU 6392  C3'  DG B2005    10616   9340  15916   1364  -2026   4522       C  
ATOM   6393  O3'  DG B2005     -54.571 -11.303 -17.104  1.00 95.95           O  
ANISOU 6393  O3'  DG B2005    10451   9885  16120   1209  -2216   4697       O  
ATOM   6394  C2'  DG B2005     -52.272 -10.748 -16.444  1.00 87.69           C  
ANISOU 6394  C2'  DG B2005    10130   8526  14663   1142  -2115   4239       C  
ATOM   6395  C1'  DG B2005     -51.661 -10.260 -17.753  1.00 86.60           C  
ANISOU 6395  C1'  DG B2005    10101   8497  14305    825  -2447   4382       C  
ATOM   6396  N9   DG B2005     -50.236  -9.970 -17.665  1.00 80.06           N  
ANISOU 6396  N9   DG B2005     9666   7558  13194    665  -2470   4179       N  
ATOM   6397  C8   DG B2005     -49.614  -9.146 -16.753  1.00 78.04           C  
ANISOU 6397  C8   DG B2005     9716   6917  13020    819  -2251   3997       C  
ATOM   6398  N7   DG B2005     -48.325  -9.056 -16.926  1.00 75.28           N  
ANISOU 6398  N7   DG B2005     9659   6615  12328    554  -2325   3807       N  
ATOM   6399  C5   DG B2005     -48.066  -9.882 -18.027  1.00 74.58           C  
ANISOU 6399  C5   DG B2005     9468   6916  11954    255  -2600   3933       C  
ATOM   6400  C6   DG B2005     -46.830 -10.203 -18.683  1.00 71.42           C  
ANISOU 6400  C6   DG B2005     9269   6725  11143    -79  -2734   3858       C  
ATOM   6401  O6   DG B2005     -45.685  -9.801 -18.414  1.00 70.69           O  
ANISOU 6401  O6   DG B2005     9434   6535  10889   -196  -2670   3693       O  
ATOM   6402  N1   DG B2005     -47.024 -11.076 -19.760  1.00 69.29           N  
ANISOU 6402  N1   DG B2005     8879   6817  10631   -294  -2930   3985       N  
ATOM   6403  C2   DG B2005     -48.254 -11.586 -20.151  1.00 71.32           C  
ANISOU 6403  C2   DG B2005     8851   7235  11012   -248  -3028   4137       C  
ATOM   6404  N2   DG B2005     -48.255 -12.412 -21.214  1.00 70.24           N  
ANISOU 6404  N2   DG B2005     8710   7420  10559   -522  -3204   4183       N  
ATOM   6405  N3   DG B2005     -49.407 -11.301 -19.545  1.00 74.78           N  
ANISOU 6405  N3   DG B2005     9040   7516  11857     39  -2933   4236       N  
ATOM   6406  C4   DG B2005     -49.238 -10.445 -18.496  1.00 76.49           C  
ANISOU 6406  C4   DG B2005     9375   7361  12327    305  -2700   4136       C  
ATOM   6407  P    DA B2006     -55.150 -12.467 -16.153  1.00 95.14           P  
ANISOU 6407  P    DA B2006    10153   9907  16088   1351  -2006   4570       P  
ATOM   6408  OP1  DA B2006     -56.599 -12.624 -16.464  1.00 98.72           O  
ANISOU 6408  OP1  DA B2006    10161  10490  16860   1384  -2040   4893       O  
ATOM   6409  OP2  DA B2006     -54.642 -12.220 -14.774  1.00 94.25           O  
ANISOU 6409  OP2  DA B2006    10311   9491  16008   1662  -1595   4250       O  
ATOM   6410  O5'  DA B2006     -54.375 -13.772 -16.655  1.00 87.52           O  
ANISOU 6410  O5'  DA B2006     9295   9287  14674    976  -2296   4431       O  
ATOM   6411  C5'  DA B2006     -54.266 -14.044 -18.052  1.00 83.85           C  
ANISOU 6411  C5'  DA B2006     8829   9080  13949    576  -2704   4596       C  
ATOM   6412  C4'  DA B2006     -53.216 -15.103 -18.291  1.00 74.72           C  
ANISOU 6412  C4'  DA B2006     7939   8157  12294    285  -2843   4368       C  
ATOM   6413  O4'  DA B2006     -51.922 -14.469 -18.284  1.00 71.93           O  
ANISOU 6413  O4'  DA B2006     7947   7657  11724    245  -2810   4212       O  
ATOM   6414  C3'  DA B2006     -53.188 -16.188 -17.216  1.00 69.58           C  
ANISOU 6414  C3'  DA B2006     7244   7585  11607    411  -2638   4146       C  
ATOM   6415  O3'  DA B2006     -53.446 -17.462 -17.787  1.00 66.03           O  
ANISOU 6415  O3'  DA B2006     6728   7465  10894    118  -2845   4157       O  
ATOM   6416  C2'  DA B2006     -51.784 -16.075 -16.584  1.00 65.76           C  
ANISOU 6416  C2'  DA B2006     7158   7029  10797    401  -2391   3710       C  
ATOM   6417  C1'  DA B2006     -50.993 -15.304 -17.634  1.00 66.69           C  
ANISOU 6417  C1'  DA B2006     7506   7106  10725    178  -2633   3836       C  
ATOM   6418  N9   DA B2006     -49.924 -14.471 -17.069  1.00 64.74           N  
ANISOU 6418  N9   DA B2006     7562   6635  10400    246  -2425   3586       N  
ATOM   6419  C8   DA B2006     -50.002 -13.663 -15.971  1.00 65.71           C  
ANISOU 6419  C8   DA B2006     7746   6432  10789    549  -2134   3447       C  
ATOM   6420  N7   DA B2006     -48.886 -13.017 -15.700  1.00 64.28           N  
ANISOU 6420  N7   DA B2006     7890   6093  10442    482  -2055   3246       N  
ATOM   6421  C5   DA B2006     -48.008 -13.438 -16.692  1.00 62.43           C  
ANISOU 6421  C5   DA B2006     7769   6113   9837    139  -2279   3276       C  
ATOM   6422  C6   DA B2006     -46.637 -13.135 -16.971  1.00 60.78           C  
ANISOU 6422  C6   DA B2006     7844   5911   9339    -86  -2316   3173       C  
ATOM   6423  N6   DA B2006     -45.889 -12.308 -16.230  1.00 60.29           N  
ANISOU 6423  N6   DA B2006     8010   5587   9309    -39  -2179   3004       N  
ATOM   6424  N1   DA B2006     -46.072 -13.725 -18.053  1.00 59.97           N  
ANISOU 6424  N1   DA B2006     7797   6080   8910   -372  -2498   3276       N  
ATOM   6425  C2   DA B2006     -46.813 -14.567 -18.789  1.00 60.95           C  
ANISOU 6425  C2   DA B2006     7764   6438   8956   -460  -2660   3434       C  
ATOM   6426  N3   DA B2006     -48.088 -14.938 -18.618  1.00 62.20           N  
ANISOU 6426  N3   DA B2006     7652   6627   9355   -316  -2699   3541       N  
ATOM   6427  C4   DA B2006     -48.635 -14.332 -17.546  1.00 62.81           C  
ANISOU 6427  C4   DA B2006     7618   6447   9799     -1  -2490   3468       C  
HETATM 6428  N1  OMC B2007     -48.014 -17.681 -15.300  1.00 54.97           N  
ANISOU 6428  N1  OMC B2007     6645   5993   8247      0  -1883   2593       N  
HETATM 6429  C2  OMC B2007     -46.896 -16.784 -15.625  1.00 52.63           C  
ANISOU 6429  C2  OMC B2007     6603   5572   7824   -123  -1935   2593       C  
HETATM 6430  N3  OMC B2007     -46.687 -15.567 -14.819  1.00 54.02           N  
ANISOU 6430  N3  OMC B2007     6903   5399   8225     60  -1807   2515       N  
HETATM 6431  C4  OMC B2007     -47.577 -15.260 -13.717  1.00 55.44           C  
ANISOU 6431  C4  OMC B2007     6994   5345   8725    389  -1584   2428       C  
HETATM 6432  C5  OMC B2007     -48.703 -16.139 -13.388  1.00 55.80           C  
ANISOU 6432  C5  OMC B2007     6756   5521   8923    554  -1490   2450       C  
HETATM 6433  C6  OMC B2007     -48.922 -17.377 -14.192  1.00 53.93           C  
ANISOU 6433  C6  OMC B2007     6352   5655   8483    339  -1667   2538       C  
HETATM 6434  O2  OMC B2007     -46.177 -17.045 -16.507  1.00 51.81           O  
ANISOU 6434  O2  OMC B2007     6624   5626   7436   -368  -2064   2662       O  
HETATM 6435  N4  OMC B2007     -47.340 -14.083 -12.959  1.00 57.20           N  
ANISOU 6435  N4  OMC B2007     7440   5185   9108    549  -1443   2337       N  
HETATM 6436  C1' OMC B2007     -48.222 -18.888 -16.105  1.00 55.94           C  
ANISOU 6436  C1' OMC B2007     6707   6428   8120   -221  -2036   2666       C  
HETATM 6437  C2' OMC B2007     -48.869 -20.026 -15.320  1.00 56.42           C  
ANISOU 6437  C2' OMC B2007     6592   6632   8214   -116  -1867   2506       C  
HETATM 6438  O2' OMC B2007     -47.942 -20.788 -14.554  1.00 59.38           O  
ANISOU 6438  O2' OMC B2007     7124   7123   8313   -143  -1605   2163       O  
HETATM 6439  CM2 OMC B2007     -46.842 -21.447 -15.137  1.00 58.00           C  
ANISOU 6439  CM2 OMC B2007     7174   7145   7717   -401  -1608   2081       C  
HETATM 6440  C3' OMC B2007     -49.720 -20.754 -16.386  1.00 58.93           C  
ANISOU 6440  C3' OMC B2007     6768   7143   8479   -313  -2169   2774       C  
HETATM 6441  C4' OMC B2007     -49.866 -19.733 -17.523  1.00 60.21           C  
ANISOU 6441  C4' OMC B2007     6954   7196   8726   -421  -2488   3120       C  
HETATM 6442  O4' OMC B2007     -49.143 -18.549 -17.113  1.00 58.84           O  
ANISOU 6442  O4' OMC B2007     6914   6784   8657   -281  -2349   3037       O  
HETATM 6443  O3' OMC B2007     -49.109 -21.950 -16.876  1.00 59.64           O  
ANISOU 6443  O3' OMC B2007     7059   7484   8118   -580  -2180   2644       O  
HETATM 6444  C5' OMC B2007     -51.280 -19.349 -17.890  1.00 66.33           C  
ANISOU 6444  C5' OMC B2007     7393   7903   9908   -339  -2736   3510       C  
HETATM 6445  O5' OMC B2007     -52.163 -19.399 -16.766  1.00 68.09           O  
ANISOU 6445  O5' OMC B2007     7316   8029  10528    -18  -2508   3480       O  
HETATM 6446  P   OMC B2007     -53.626 -18.751 -16.847  1.00 72.91           P  
ANISOU 6446  P   OMC B2007     7502   8493  11708    191  -2646   3928       P  
HETATM 6447  OP1 OMC B2007     -54.551 -19.723 -17.610  1.00 76.28           O  
ANISOU 6447  OP1 OMC B2007     7727   9171  12084    -82  -2924   4129       O  
HETATM 6448  OP2 OMC B2007     -53.912 -18.413 -15.422  1.00 70.21           O  
ANISOU 6448  OP2 OMC B2007     7049   7933  11693    609  -2209   3752       O  
ATOM   6449  P    DG B2008     -50.069 -23.120 -17.468  1.00 59.52           P  
ANISOU 6449  P    DG B2008     6933   7668   8014   -768  -2398   2791       P  
ATOM   6450  OP1  DG B2008     -49.149 -23.996 -18.233  1.00 62.83           O  
ANISOU 6450  OP1  DG B2008     7715   8258   7898  -1062  -2401   2680       O  
ATOM   6451  OP2  DG B2008     -51.255 -22.559 -18.061  1.00 54.26           O  
ANISOU 6451  OP2  DG B2008     6011   6929   7675   -775  -2733   3184       O  
ATOM   6452  O5'  DG B2008     -50.587 -23.839 -16.151  1.00 55.70           O  
ANISOU 6452  O5'  DG B2008     6215   7222   7725   -538  -2115   2576       O  
ATOM   6453  C5'  DG B2008     -49.737 -24.762 -15.490  1.00 45.48           C  
ANISOU 6453  C5'  DG B2008     5089   6054   6136   -546  -1812   2224       C  
ATOM   6454  C4'  DG B2008     -50.125 -24.899 -14.023  1.00 44.45           C  
ANISOU 6454  C4'  DG B2008     4743   5864   6280   -233  -1500   2023       C  
ATOM   6455  O4'  DG B2008     -49.789 -23.687 -13.311  1.00 44.75           O  
ANISOU 6455  O4'  DG B2008     4805   5663   6533      4  -1343   1954       O  
ATOM   6456  C3'  DG B2008     -51.619 -25.135 -13.720  1.00 46.64           C  
ANISOU 6456  C3'  DG B2008     4642   6129   6951    -87  -1567   2222       C  
ATOM   6457  O3'  DG B2008     -51.683 -25.956 -12.587  1.00 47.17           O  
ANISOU 6457  O3'  DG B2008     4630   6263   7030     73  -1253   1965       O  
ATOM   6458  C2'  DG B2008     -52.114 -23.724 -13.364  1.00 49.76           C  
ANISOU 6458  C2'  DG B2008     4874   6247   7786    198  -1538   2393       C  
ATOM   6459  C1'  DG B2008     -50.909 -23.269 -12.556  1.00 46.79           C  
ANISOU 6459  C1'  DG B2008     4781   5760   7237    306  -1245   2050       C  
ATOM   6460  N9   DG B2008     -50.784 -21.838 -12.339  1.00 48.60           N  
ANISOU 6460  N9   DG B2008     5075   5696   7694    487  -1205   2112       N  
ATOM   6461  C8   DG B2008     -51.382 -20.792 -13.037  1.00 52.39           C  
ANISOU 6461  C8   DG B2008     5441   6006   8459    532  -1423   2451       C  
ATOM   6462  N7   DG B2008     -51.019 -19.600 -12.594  1.00 52.95           N  
ANISOU 6462  N7   DG B2008     5664   5790   8665    705  -1295   2400       N  
ATOM   6463  C5   DG B2008     -50.140 -19.894 -11.541  1.00 54.50           C  
ANISOU 6463  C5   DG B2008     6094   5975   8639    751  -1008   2009       C  
ATOM   6464  C6   DG B2008     -49.414 -19.042 -10.669  1.00 50.13           C  
ANISOU 6464  C6   DG B2008     5822   5160   8065    871   -805   1788       C  
ATOM   6465  O6   DG B2008     -49.416 -17.803 -10.635  1.00 52.51           O  
ANISOU 6465  O6   DG B2008     6244   5155   8551    986   -807   1876       O  
ATOM   6466  N1   DG B2008     -48.597 -19.789  -9.773  1.00 47.11           N  
ANISOU 6466  N1   DG B2008     5611   4893   7397    823   -599   1441       N  
ATOM   6467  C2   DG B2008     -48.555 -21.168  -9.726  1.00 44.52           C  
ANISOU 6467  C2   DG B2008     5171   4880   6866    717   -553   1329       C  
ATOM   6468  N2   DG B2008     -47.769 -21.743  -8.792  1.00 42.04           N  
ANISOU 6468  N2   DG B2008     5016   4640   6318    699   -342   1024       N  
ATOM   6469  N3   DG B2008     -49.233 -21.944 -10.530  1.00 44.61           N  
ANISOU 6469  N3   DG B2008     4949   5108   6892    617   -716   1514       N  
ATOM   6470  C4   DG B2008     -49.992 -21.264 -11.397  1.00 47.50           C  
ANISOU 6470  C4   DG B2008     5162   5380   7506    625   -952   1846       C  
HETATM 6471  P   OMG B2009     -52.794 -27.097 -12.455  1.00 45.31           P  
ANISOU 6471  P   OMG B2009     4114   6177   6926     47  -1300   2068       P  
HETATM 6472  OP1 OMG B2009     -52.622 -28.127 -13.532  1.00 54.58           O  
ANISOU 6472  OP1 OMG B2009     5468   7558   7711   -346  -1558   2113       O  
HETATM 6473  OP2 OMG B2009     -54.148 -26.410 -12.408  1.00 49.16           O  
ANISOU 6473  OP2 OMG B2009     4202   6522   7953    244  -1423   2439       O  
HETATM 6474  O5' OMG B2009     -52.516 -27.657 -10.985  1.00 44.22           O  
ANISOU 6474  O5' OMG B2009     3964   6052   6787    297   -854   1715       O  
HETATM 6475  C5' OMG B2009     -51.262 -28.185 -10.554  1.00 39.10           C  
ANISOU 6475  C5' OMG B2009     3608   5498   5749    236   -622   1361       C  
HETATM 6476  C4' OMG B2009     -50.961 -27.833  -9.099  1.00 40.05           C  
ANISOU 6476  C4' OMG B2009     3746   5487   5985    547   -247   1102       C  
HETATM 6477  O4' OMG B2009     -50.670 -26.397  -9.004  1.00 39.32           O  
ANISOU 6477  O4' OMG B2009     3763   5142   6036    675   -257   1144       O  
HETATM 6478  C3' OMG B2009     -52.076 -28.091  -8.070  1.00 42.94           C  
ANISOU 6478  C3' OMG B2009     3821   5790   6703    848    -26   1117       C  
HETATM 6479  O3' OMG B2009     -51.474 -28.254  -6.780  1.00 44.89           O  
ANISOU 6479  O3' OMG B2009     4215   5997   6844   1030    335    788       O  
HETATM 6480  C2' OMG B2009     -52.772 -26.737  -8.045  1.00 47.30           C  
ANISOU 6480  C2' OMG B2009     4249   6064   7659   1080    -62   1351       C  
HETATM 6481  O2' OMG B2009     -53.606 -26.487  -6.931  1.00 49.10           O  
ANISOU 6481  O2' OMG B2009     4299   6113   8245   1458    248   1361       O  
HETATM 6482  CM2 OMG B2009     -54.768 -27.281  -6.892  1.00 50.70           C  
ANISOU 6482  CM2 OMG B2009     4123   6427   8713   1519    242   1572       C  
HETATM 6483  C1' OMG B2009     -51.565 -25.809  -8.081  1.00 41.41           C  
ANISOU 6483  C1' OMG B2009     3855   5185   6692   1024    -58   1187       C  
HETATM 6484  N9  OMG B2009     -51.866 -24.456  -8.507  1.00 46.65           N  
ANISOU 6484  N9  OMG B2009     4511   5600   7612   1118   -191   1416       N  
HETATM 6485  C8  OMG B2009     -52.760 -24.049  -9.456  1.00 48.65           C  
ANISOU 6485  C8  OMG B2009     4525   5825   8136   1083   -468   1802       C  
HETATM 6486  N7  OMG B2009     -52.728 -22.690  -9.478  1.00 49.52           N  
ANISOU 6486  N7  OMG B2009     4722   5650   8442   1233   -465   1907       N  
HETATM 6487  C5  OMG B2009     -51.875 -22.273  -8.544  1.00 48.14           C  
ANISOU 6487  C5  OMG B2009     4858   5317   8116   1343   -204   1586       C  
HETATM 6488  C6  OMG B2009     -51.381 -20.908  -8.057  1.00 50.22           C  
ANISOU 6488  C6  OMG B2009     5417   5226   8439   1495    -78   1497       C  
HETATM 6489  O6  OMG B2009     -51.764 -19.905  -8.550  1.00 52.36           O  
ANISOU 6489  O6  OMG B2009     5650   5294   8952   1572   -188   1740       O  
HETATM 6490  N1  OMG B2009     -50.409 -20.840  -7.000  1.00 47.78           N  
ANISOU 6490  N1  OMG B2009     5461   4819   7873   1515    153   1126       N  
HETATM 6491  C2  OMG B2009     -49.932 -22.031  -6.389  1.00 44.60           C  
ANISOU 6491  C2  OMG B2009     5089   4662   7194   1429    287    861       C  
HETATM 6492  N2  OMG B2009     -48.940 -21.993  -5.343  1.00 43.07           N  
ANISOU 6492  N2  OMG B2009     5234   4391   6740   1412    472    531       N  
HETATM 6493  N3  OMG B2009     -50.401 -23.316  -6.859  1.00 43.07           N  
ANISOU 6493  N3  OMG B2009     4604   4800   6963   1321    208    940       N  
HETATM 6494  C4  OMG B2009     -51.348 -23.392  -7.953  1.00 44.94           C  
ANISOU 6494  C4  OMG B2009     4530   5124   7423   1261    -51   1296       C  
ATOM   6495  P    DA B2010     -51.708 -29.543  -5.846  1.00 43.23           P  
ANISOU 6495  P    DA B2010     3898   5946   6581   1120    607    598       P  
ATOM   6496  OP1  DA B2010     -52.888 -30.302  -6.290  1.00 43.30           O  
ANISOU 6496  OP1  DA B2010     3578   6072   6800   1078    474    838       O  
ATOM   6497  OP2  DA B2010     -51.633 -29.047  -4.445  1.00 46.93           O  
ANISOU 6497  OP2  DA B2010     4462   6218   7151   1437    957    395       O  
ATOM   6498  O5'  DA B2010     -50.370 -30.388  -6.092  1.00 37.50           O  
ANISOU 6498  O5'  DA B2010     3434   5443   5372    845    614    371       O  
ATOM   6499  C5'  DA B2010     -49.113 -29.822  -5.790  1.00 33.25           C  
ANISOU 6499  C5'  DA B2010     3178   4845   4610    807    687    195       C  
ATOM   6500  C4'  DA B2010     -48.014 -30.421  -6.639  1.00 31.12           C  
ANISOU 6500  C4'  DA B2010     3088   4773   3963    503    587    171       C  
ATOM   6501  O4'  DA B2010     -48.302 -30.191  -8.030  1.00 32.70           O  
ANISOU 6501  O4'  DA B2010     3285   4987   4153    307    277    416       O  
ATOM   6502  C3'  DA B2010     -46.639 -29.807  -6.423  1.00 31.46           C  
ANISOU 6502  C3'  DA B2010     3377   4769   3808    430    629     66       C  
ATOM   6503  O3'  DA B2010     -46.003 -30.500  -5.388  1.00 31.09           O  
ANISOU 6503  O3'  DA B2010     3383   4822   3609    479    885   -151       O  
ATOM   6504  C2'  DA B2010     -45.943 -30.047  -7.767  1.00 29.54           C  
ANISOU 6504  C2'  DA B2010     3258   4656   3312    149    454    207       C  
ATOM   6505  C1'  DA B2010     -47.126 -30.040  -8.765  1.00 28.86           C  
ANISOU 6505  C1'  DA B2010     3039   4554   3374     94    204    427       C  
ATOM   6506  N9   DA B2010     -47.232 -28.809  -9.584  1.00 31.92           N  
ANISOU 6506  N9   DA B2010     3465   4781   3884     44    -59    637       N  
ATOM   6507  C8   DA B2010     -47.154 -28.727 -10.954  1.00 33.39           C  
ANISOU 6507  C8   DA B2010     3754   5008   3927   -188   -315    842       C  
ATOM   6508  N7   DA B2010     -47.313 -27.515 -11.432  1.00 35.30           N  
ANISOU 6508  N7   DA B2010     3995   5079   4338   -175   -518   1018       N  
ATOM   6509  C5   DA B2010     -47.494 -26.732 -10.307  1.00 36.17           C  
ANISOU 6509  C5   DA B2010     4021   5006   4717     84   -372    914       C  
ATOM   6510  C6   DA B2010     -47.713 -25.331 -10.157  1.00 39.37           C  
ANISOU 6510  C6   DA B2010     4422   5147   5390    229   -444   1011       C  
ATOM   6511  N6   DA B2010     -47.782 -24.478 -11.217  1.00 38.77           N  
ANISOU 6511  N6   DA B2010     4377   4980   5372    121   -713   1257       N  
ATOM   6512  N1   DA B2010     -47.877 -24.855  -8.878  1.00 39.56           N  
ANISOU 6512  N1   DA B2010     4444   4984   5603    490   -216    848       N  
ATOM   6513  C2   DA B2010     -47.819 -25.744  -7.848  1.00 37.14           C  
ANISOU 6513  C2   DA B2010     4116   4778   5217    587     43    615       C  
ATOM   6514  N3   DA B2010     -47.626 -27.091  -7.892  1.00 32.89           N  
ANISOU 6514  N3   DA B2010     3533   4508   4457    469    120    521       N  
ATOM   6515  C4   DA B2010     -47.449 -27.510  -9.149  1.00 32.74           C  
ANISOU 6515  C4   DA B2010     3540   4644   4256    219    -90    675       C  
ATOM   6516  P    DA B2011     -45.302 -29.715  -4.182  1.00 33.13           P  
ANISOU 6516  P    DA B2011     3808   4917   3863    584   1007   -315       P  
ATOM   6517  OP1  DA B2011     -44.902 -30.764  -3.196  1.00 36.93           O  
ANISOU 6517  OP1  DA B2011     4286   5552   4192    617   1252   -501       O  
ATOM   6518  OP2  DA B2011     -46.159 -28.685  -3.591  1.00 30.65           O  
ANISOU 6518  OP2  DA B2011     3503   4316   3825    818   1025   -325       O  
ATOM   6519  O5'  DA B2011     -44.025 -29.078  -4.892  1.00 32.00           O  
ANISOU 6519  O5'  DA B2011     3840   4773   3545    347    835   -210       O  
ATOM   6520  C5'  DA B2011     -42.881 -29.911  -5.236  1.00 28.83           C  
ANISOU 6520  C5'  DA B2011     3478   4604   2871    151    898   -186       C  
ATOM   6521  C4'  DA B2011     -41.640 -29.091  -5.537  1.00 29.81           C  
ANISOU 6521  C4'  DA B2011     3749   4675   2903    -24    773    -71       C  
ATOM   6522  O4'  DA B2011     -41.748 -28.530  -6.865  1.00 34.52           O  
ANISOU 6522  O4'  DA B2011     4372   5223   3522   -132    567    132       O  
ATOM   6523  C3'  DA B2011     -41.371 -27.910  -4.617  1.00 32.18           C  
ANISOU 6523  C3'  DA B2011     4195   4731   3303     17    700   -147       C  
ATOM   6524  O3'  DA B2011     -40.527 -28.321  -3.575  1.00 29.82           O  
ANISOU 6524  O3'  DA B2011     3950   4512   2869    -27    825   -254       O  
ATOM   6525  C2'  DA B2011     -40.619 -26.941  -5.534  1.00 33.59           C  
ANISOU 6525  C2'  DA B2011     4468   4823   3472   -169    478     60       C  
ATOM   6526  C1'  DA B2011     -41.270 -27.204  -6.874  1.00 33.80           C  
ANISOU 6526  C1'  DA B2011     4400   4926   3516   -187    397    209       C  
ATOM   6527  N9   DA B2011     -42.415 -26.330  -7.256  1.00 32.78           N  
ANISOU 6527  N9   DA B2011     4246   4587   3623    -68    238    266       N  
ATOM   6528  C8   DA B2011     -43.746 -26.689  -7.348  1.00 28.98           C  
ANISOU 6528  C8   DA B2011     3610   4102   3298     87    252    256       C  
ATOM   6529  N7   DA B2011     -44.519 -25.756  -7.894  1.00 32.40           N  
ANISOU 6529  N7   DA B2011     4010   4350   3951    150     73    404       N  
ATOM   6530  C5   DA B2011     -43.631 -24.727  -8.192  1.00 33.22           C  
ANISOU 6530  C5   DA B2011     4283   4321   4017     28    -59    486       C  
ATOM   6531  C6   DA B2011     -43.807 -23.477  -8.765  1.00 37.98           C  
ANISOU 6531  C6   DA B2011     4946   4703   4783     23   -257    649       C  
ATOM   6532  N6   DA B2011     -45.008 -23.022  -9.159  1.00 41.32           N  
ANISOU 6532  N6   DA B2011     5240   4997   5462    163   -357    784       N  
ATOM   6533  N1   DA B2011     -42.704 -22.691  -8.934  1.00 38.05           N  
ANISOU 6533  N1   DA B2011     5129   4623   4706   -135   -357    708       N  
ATOM   6534  C2   DA B2011     -41.510 -23.152  -8.544  1.00 36.24           C  
ANISOU 6534  C2   DA B2011     4977   4531   4261   -282   -269    638       C  
ATOM   6535  N3   DA B2011     -41.219 -24.328  -7.990  1.00 33.04           N  
ANISOU 6535  N3   DA B2011     4509   4345   3697   -283    -76    504       N  
ATOM   6536  C4   DA B2011     -42.323 -25.079  -7.849  1.00 33.45           C  
ANISOU 6536  C4   DA B2011     4421   4472   3818   -122     26    416       C  
ATOM   6537  P    DC B2012     -40.570 -27.655  -2.126  1.00 30.97           P  
ANISOU 6537  P    DC B2012     4288   4428   3049     64    850   -445       P  
ATOM   6538  OP1  DC B2012     -39.680 -28.537  -1.328  1.00 31.85           O  
ANISOU 6538  OP1  DC B2012     4382   4742   2977    -27    975   -498       O  
ATOM   6539  OP2  DC B2012     -41.933 -27.464  -1.623  1.00 29.95           O  
ANISOU 6539  OP2  DC B2012     4166   4117   3096    340    963   -592       O  
ATOM   6540  O5'  DC B2012     -39.876 -26.212  -2.330  1.00 31.73           O  
ANISOU 6540  O5'  DC B2012     4599   4281   3176   -103    593   -333       O  
ATOM   6541  C5'  DC B2012     -38.534 -26.096  -2.820  1.00 27.72           C  
ANISOU 6541  C5'  DC B2012     4083   3890   2558   -376    451   -128       C  
ATOM   6542  C4'  DC B2012     -38.201 -24.632  -3.075  1.00 30.27           C  
ANISOU 6542  C4'  DC B2012     4605   3933   2965   -501    196    -26       C  
ATOM   6543  O4'  DC B2012     -39.107 -24.113  -4.104  1.00 34.90           O  
ANISOU 6543  O4'  DC B2012     5141   4409   3712   -385    133     47       O  
ATOM   6544  C3'  DC B2012     -38.396 -23.737  -1.874  1.00 34.03           C  
ANISOU 6544  C3'  DC B2012     5397   4078   3455   -460    147   -215       C  
ATOM   6545  O3'  DC B2012     -37.378 -22.844  -1.799  1.00 38.48           O  
ANISOU 6545  O3'  DC B2012     6144   4502   3976   -722    -93    -92       O  
ATOM   6546  C2'  DC B2012     -39.736 -23.034  -2.135  1.00 35.29           C  
ANISOU 6546  C2'  DC B2012     5617   3973   3818   -201    187   -290       C  
ATOM   6547  C1'  DC B2012     -39.801 -22.960  -3.630  1.00 35.01           C  
ANISOU 6547  C1'  DC B2012     5370   4057   3874   -255     71    -56       C  
ATOM   6548  N1   DC B2012     -41.234 -22.965  -4.167  1.00 34.53           N  
ANISOU 6548  N1   DC B2012     5168   3937   4016      2    145    -54       N  
ATOM   6549  C2   DC B2012     -41.691 -21.887  -4.960  1.00 37.58           C  
ANISOU 6549  C2   DC B2012     5589   4104   4585     35    -13     96       C  
ATOM   6550  O2   DC B2012     -40.902 -20.963  -5.241  1.00 36.87           O  
ANISOU 6550  O2   DC B2012     5660   3874   4476   -146   -200    202       O  
ATOM   6551  N3   DC B2012     -42.984 -21.903  -5.429  1.00 36.30           N  
ANISOU 6551  N3   DC B2012     5257   3901   4635    252     28    157       N  
ATOM   6552  C4   DC B2012     -43.792 -22.923  -5.144  1.00 35.07           C  
ANISOU 6552  C4   DC B2012     4907   3906   4512    415    207     74       C  
ATOM   6553  N4   DC B2012     -45.049 -22.878  -5.614  1.00 36.30           N  
ANISOU 6553  N4   DC B2012     4866   4015   4910    599    208    193       N  
ATOM   6554  C5   DC B2012     -43.346 -24.041  -4.339  1.00 33.42           C  
ANISOU 6554  C5   DC B2012     4679   3914   4107    388    385   -105       C  
ATOM   6555  C6   DC B2012     -42.074 -24.010  -3.877  1.00 33.84           C  
ANISOU 6555  C6   DC B2012     4899   4007   3950    188    350   -162       C  
ATOM   6556  P    DC B2013     -37.203 -21.931  -0.492  1.00 45.65           P  
ANISOU 6556  P    DC B2013     6602   4074   6668    522  -2697   -146       P  
ATOM   6557  OP1  DC B2013     -35.769 -21.590  -0.389  1.00 47.51           O  
ANISOU 6557  OP1  DC B2013     6699   4220   7133    390  -3003   -233       O  
ATOM   6558  OP2  DC B2013     -37.935 -22.549   0.625  1.00 47.69           O  
ANISOU 6558  OP2  DC B2013     7049   4528   6542    600  -2712      6       O  
ATOM   6559  O5'  DC B2013     -38.036 -20.613  -0.834  1.00 47.88           O  
ANISOU 6559  O5'  DC B2013     7072   4295   6827    569  -2455   -343       O  
ATOM   6560  C5'  DC B2013     -37.567 -19.715  -1.813  1.00 49.15           C  
ANISOU 6560  C5'  DC B2013     7143   4262   7270    493  -2396   -466       C  
ATOM   6561  C4'  DC B2013     -38.453 -18.492  -1.876  1.00 50.28           C  
ANISOU 6561  C4'  DC B2013     7509   4315   7281    588  -2193   -603       C  
ATOM   6562  O4'  DC B2013     -39.700 -18.842  -2.496  1.00 50.65           O  
ANISOU 6562  O4'  DC B2013     7495   4471   7278    733  -1913   -449       O  
ATOM   6563  C3'  DC B2013     -38.812 -17.872  -0.525  1.00 53.74           C  
ANISOU 6563  C3'  DC B2013     8284   4786   7349    657  -2249   -795       C  
ATOM   6564  O3'  DC B2013     -38.541 -16.527  -0.583  1.00 56.76           O  
ANISOU 6564  O3'  DC B2013     8834   4907   7827    612  -2255  -1032       O  
ATOM   6565  C2'  DC B2013     -40.322 -18.116  -0.390  1.00 52.58           C  
ANISOU 6565  C2'  DC B2013     8204   4809   6966    879  -1936   -687       C  
ATOM   6566  C1'  DC B2013     -40.751 -18.165  -1.832  1.00 50.18           C  
ANISOU 6566  C1'  DC B2013     7656   4448   6961    908  -1748   -527       C  
ATOM   6567  N1   DC B2013     -42.009 -18.961  -2.089  1.00 46.82           N  
ANISOU 6567  N1   DC B2013     7098   4245   6447   1027  -1532   -310       N  
ATOM   6568  C2   DC B2013     -43.049 -18.391  -2.812  1.00 43.95           C  
ANISOU 6568  C2   DC B2013     6663   3884   6152   1172  -1302   -238       C  
ATOM   6569  O2   DC B2013     -42.937 -17.218  -3.192  1.00 45.69           O  
ANISOU 6569  O2   DC B2013     6971   3890   6499   1231  -1260   -339       O  
ATOM   6570  N3   DC B2013     -44.167 -19.130  -3.068  1.00 41.65           N  
ANISOU 6570  N3   DC B2013     6191   3820   5814   1234  -1151    -32       N  
ATOM   6571  C4   DC B2013     -44.243 -20.392  -2.635  1.00 40.95           C  
ANISOU 6571  C4   DC B2013     6029   3899   5632   1139  -1197     92       C  
ATOM   6572  N4   DC B2013     -45.362 -21.100  -2.917  1.00 36.82           N  
ANISOU 6572  N4   DC B2013     5308   3575   5107   1148  -1056    295       N  
ATOM   6573  C5   DC B2013     -43.177 -20.991  -1.886  1.00 43.79           C  
ANISOU 6573  C5   DC B2013     6493   4218   5928   1019  -1413     45       C  
ATOM   6574  C6   DC B2013     -42.092 -20.250  -1.641  1.00 45.46           C  
ANISOU 6574  C6   DC B2013     6846   4256   6170    975  -1588   -152       C  
HETATM 6575  P   A2M B2014     -38.282 -15.697   0.747  1.00 60.31           P  
ANISOU 6575  P   A2M B2014     9656   5285   7973    564  -2432  -1369       P  
HETATM 6576  OP1 A2M B2014     -37.034 -14.929   0.478  1.00 62.62           O  
ANISOU 6576  OP1 A2M B2014     9904   5306   8583    301  -2688  -1527       O  
HETATM 6577  O5' A2M B2014     -39.578 -14.663   0.805  1.00 63.37           O  
ANISOU 6577  O5' A2M B2014    10313   5522   8243    829  -2054  -1527       O  
HETATM 6578  C5' A2M B2014     -39.807 -13.867  -0.318  1.00 62.26           C  
ANISOU 6578  C5' A2M B2014    10083   5098   8477    884  -1869  -1470       C  
HETATM 6579  C4' A2M B2014     -41.323 -13.449  -0.254  1.00 62.21           C  
ANISOU 6579  C4' A2M B2014    10188   5104   8345   1238  -1481  -1456       C  
HETATM 6580  O4' A2M B2014     -42.019 -14.496  -0.540  1.00 59.23           O  
ANISOU 6580  O4' A2M B2014     9569   5052   7883   1332  -1363  -1171       O  
HETATM 6581  C3' A2M B2014     -41.695 -13.019   1.222  1.00 65.77           C  
ANISOU 6581  C3' A2M B2014    11040   5582   8366   1363  -1412  -1810       C  
HETATM 6582  O3' A2M B2014     -42.472 -11.971   1.064  1.00 69.11           O  
ANISOU 6582  O3' A2M B2014    11606   5733   8920   1616  -1121  -1932       O  
HETATM 6583  C2' A2M B2014     -42.524 -14.208   1.700  1.00 64.23           C  
ANISOU 6583  C2' A2M B2014    10724   5849   7830   1494  -1269  -1586       C  
HETATM 6584  O2' A2M B2014     -43.498 -13.751   2.752  1.00 68.51           O  
ANISOU 6584  O2' A2M B2014    11561   6476   7993   1762   -957  -1811       O  
HETATM 6585  C1' A2M B2014     -43.153 -14.681   0.608  1.00 60.98           C  
ANISOU 6585  C1' A2M B2014     9963   5523   7683   1580  -1115  -1245       C  
HETATM 6586  CM' A2M B2014     -43.295 -14.367   3.994  1.00 71.53           C  
ANISOU 6586  CM' A2M B2014    12156   7171   7851   1675  -1067  -1903       C  
HETATM 6587  N9  A2M B2014     -43.620 -16.064   0.675  1.00 57.64           N  
ANISOU 6587  N9  A2M B2014     9309   5484   7107   1564  -1085   -948       N  
HETATM 6588  C8  A2M B2014     -43.094 -17.068   1.397  1.00 56.46           C  
ANISOU 6588  C8  A2M B2014     9184   5555   6714   1406  -1288   -882       C  
HETATM 6589  N7  A2M B2014     -43.813 -18.197   1.190  1.00 53.96           N  
ANISOU 6589  N7  A2M B2014     8624   5498   6379   1428  -1167   -566       N  
HETATM 6590  C5  A2M B2014     -44.806 -17.879   0.353  1.00 52.57           C  
ANISOU 6590  C5  A2M B2014     8256   5309   6410   1586   -911   -456       C  
HETATM 6591  C6  A2M B2014     -45.858 -18.624  -0.215  1.00 50.73           C  
ANISOU 6591  C6  A2M B2014     7717   5288   6272   1634   -733   -162       C  
HETATM 6592  N6  A2M B2014     -46.287 -20.036  -0.074  1.00 47.71           N  
ANISOU 6592  N6  A2M B2014     7141   5164   5821   1515   -721    116       N  
HETATM 6593  N1  A2M B2014     -46.735 -18.073  -1.034  1.00 52.20           N  
ANISOU 6593  N1  A2M B2014     7716   5453   6666   1794   -548    -74       N  
HETATM 6594  C2  A2M B2014     -46.627 -16.753  -1.357  1.00 52.05           C  
ANISOU 6594  C2  A2M B2014     7821   5158   6796   1945   -500   -243       C  
HETATM 6595  N3  A2M B2014     -45.591 -16.022  -0.820  1.00 53.66           N  
ANISOU 6595  N3  A2M B2014     8351   5098   6939   1883   -644   -546       N  
HETATM 6596  C4  A2M B2014     -44.694 -16.575   0.032  1.00 54.10           C  
ANISOU 6596  C4  A2M B2014     8578   5216   6760   1693   -860   -665       C  
HETATM 6597  OP2 A2M B2014     -38.269 -16.535   2.074  1.00 62.35           O  
ANISOU 6597  OP2 A2M B2014    10056   5866   7766    565  -2619  -1356       O  
HETATM 6598  P   OMG B2015     -42.012 -10.481   1.483  1.00 73.10           P  
ANISOU 6598  P   OMG B2015    12522   5714   9538   1581  -1155  -2385       P  
HETATM 6599  OP1 OMG B2015     -41.039  -9.933   0.464  1.00 71.47           O  
ANISOU 6599  OP1 OMG B2015    12091   5257   9810   1275  -1311  -2227       O  
HETATM 6600  OP2 OMG B2015     -41.754 -10.448   2.973  1.00 76.60           O  
ANISOU 6600  OP2 OMG B2015    13365   6275   9465   1510  -1267  -2808       O  
HETATM 6601  O5' OMG B2015     -43.349  -9.647   1.345  1.00 75.23           O  
ANISOU 6601  O5' OMG B2015    12831   5820   9932   2002   -681  -2384       O  
HETATM 6602  C5' OMG B2015     -44.500 -10.029   2.075  1.00 74.85           C  
ANISOU 6602  C5' OMG B2015    12852   6060   9528   2349   -362  -2426       C  
HETATM 6603  C4' OMG B2015     -45.725  -9.952   1.213  1.00 72.03           C  
ANISOU 6603  C4' OMG B2015    12161   5738   9468   2705    -26  -2068       C  
HETATM 6604  O4' OMG B2015     -45.830 -11.149   0.408  1.00 65.84           O  
ANISOU 6604  O4' OMG B2015    10934   5354   8729   2569   -149  -1603       O  
HETATM 6605  C3' OMG B2015     -47.041  -9.889   1.959  1.00 75.39           C  
ANISOU 6605  C3' OMG B2015    12614   6365   9666   3122    429  -2143       C  
HETATM 6606  O3' OMG B2015     -47.345  -8.578   2.401  1.00 80.84           O  
ANISOU 6606  O3' OMG B2015    13538   6686  10492   3312    688  -2477       O  
HETATM 6607  C2' OMG B2015     -48.034 -10.448   0.949  1.00 72.64           C  
ANISOU 6607  C2' OMG B2015    11731   6289   9581   3298    571  -1611       C  
HETATM 6608  O2' OMG B2015     -48.408  -9.449   0.006  1.00 75.11           O  
ANISOU 6608  O2' OMG B2015    11912   6230  10397   3507    664  -1459       O  
HETATM 6609  CM2 OMG B2015     -48.494  -9.868  -1.335  1.00 71.25           C  
ANISOU 6609  CM2 OMG B2015    11031   5850  10191   3422    489   -984       C  
HETATM 6610  C1' OMG B2015     -47.185 -11.499   0.240  1.00 66.40           C  
ANISOU 6610  C1' OMG B2015    10713   5712   8802   2879    170  -1334       C  
HETATM 6611  N9  OMG B2015     -47.370 -12.862   0.761  1.00 64.38           N  
ANISOU 6611  N9  OMG B2015    10308   5966   8187   2744    143  -1183       N  
HETATM 6612  C8  OMG B2015     -46.424 -13.463   1.505  1.00 63.79           C  
ANISOU 6612  C8  OMG B2015    10440   6009   7790   2458   -113  -1336       C  
HETATM 6613  N7  OMG B2015     -46.851 -14.708   1.766  1.00 61.78           N  
ANISOU 6613  N7  OMG B2015     9976   6183   7313   2394    -79  -1075       N  
HETATM 6614  C5  OMG B2015     -48.031 -14.878   1.177  1.00 61.16           C  
ANISOU 6614  C5  OMG B2015     9551   6263   7422   2598    183   -791       C  
HETATM 6615  C6  OMG B2015     -48.979 -16.085   1.138  1.00 59.88           C  
ANISOU 6615  C6  OMG B2015     9023   6539   7190   2583    325   -421       C  
HETATM 6616  O6  OMG B2015     -48.697 -17.114   1.695  1.00 58.78           O  
ANISOU 6616  O6  OMG B2015     8909   6630   6795   2378    221   -327       O  
HETATM 6617  N1  OMG B2015     -50.201 -15.969   0.398  1.00 59.33           N  
ANISOU 6617  N1  OMG B2015     8556   6585   7402   2797    555   -155       N  
HETATM 6618  C2  OMG B2015     -50.526 -14.742  -0.281  1.00 61.53           C  
ANISOU 6618  C2  OMG B2015     8794   6571   8012   3070    651   -198       C  
HETATM 6619  N2  OMG B2015     -51.784 -14.656  -0.999  1.00 62.98           N  
ANISOU 6619  N2  OMG B2015     8525   6923   8483   3302    835    127       N  
HETATM 6620  N3  OMG B2015     -49.621 -13.599  -0.225  1.00 62.33           N  
ANISOU 6620  N3  OMG B2015     9286   6205   8190   3103    548   -532       N  
HETATM 6621  C4  OMG B2015     -48.353 -13.718   0.534  1.00 62.86           C  
ANISOU 6621  C4  OMG B2015     9752   6157   7973   2831    306   -847       C  
ATOM   6622  P    DA B2016     -48.508  -8.372   3.463  1.00 85.92           P  
ANISOU 6622  P    DA B2016    14289   7518  10839   3707   1192  -2703       P  
ATOM   6623  OP1  DA B2016     -48.557  -6.928   3.764  1.00 93.22           O  
ANISOU 6623  OP1  DA B2016    15385   7999  12037   3764   1356  -3058       O  
ATOM   6624  OP2  DA B2016     -48.316  -9.316   4.588  1.00 84.99           O  
ANISOU 6624  OP2  DA B2016    14470   7806  10017   3644   1183  -2905       O  
ATOM   6625  O5'  DA B2016     -49.815  -8.753   2.628  1.00 83.67           O  
ANISOU 6625  O5'  DA B2016    13460   7474  10857   4072   1473  -2187       O  
ATOM   6626  C5'  DA B2016     -51.073  -8.660   3.226  1.00 88.39           C  
ANISOU 6626  C5'  DA B2016    13914   8308  11363   4460   1964  -2200       C  
ATOM   6627  C4'  DA B2016     -52.082  -9.379   2.376  1.00 85.40           C  
ANISOU 6627  C4'  DA B2016    12942   8280  11227   4661   2078  -1630       C  
ATOM   6628  O4'  DA B2016     -51.431 -10.473   1.721  1.00 78.57           O  
ANISOU 6628  O4'  DA B2016    11924   7637  10293   4299   1672  -1327       O  
ATOM   6629  C3'  DA B2016     -53.267  -9.941   3.143  1.00 88.58           C  
ANISOU 6629  C3'  DA B2016    13124   9171  11363   4962   2564  -1546       C  
ATOM   6630  O3'  DA B2016     -54.410  -9.161   2.836  1.00 92.40           O  
ANISOU 6630  O3'  DA B2016    13219   9599  12289   5276   2844  -1400       O  
ATOM   6631  C2'  DA B2016     -53.421 -11.381   2.636  1.00 83.21           C  
ANISOU 6631  C2'  DA B2016    12009   9002  10606   4693   2358  -1052       C  
ATOM   6632  C1'  DA B2016     -52.072 -11.701   2.021  1.00 78.07           C  
ANISOU 6632  C1'  DA B2016    11535   8165   9965   4218   1778  -1046       C  
ATOM   6633  N9   DA B2016     -51.185 -12.543   2.862  1.00 76.91           N  
ANISOU 6633  N9   DA B2016    11690   8229   9302   3837   1560  -1211       N  
ATOM   6634  C8   DA B2016     -50.077 -12.141   3.569  1.00 77.14           C  
ANISOU 6634  C8   DA B2016    12250   8017   9042   3654   1356  -1645       C  
ATOM   6635  N7   DA B2016     -49.477 -13.114   4.216  1.00 75.35           N  
ANISOU 6635  N7   DA B2016    12147   8097   8385   3337   1139  -1628       N  
ATOM   6636  C5   DA B2016     -50.235 -14.241   3.910  1.00 73.60           C  
ANISOU 6636  C5   DA B2016    11471   8299   8194   3300   1233  -1162       C  
ATOM   6637  C6   DA B2016     -50.120 -15.621   4.280  1.00 70.93           C  
ANISOU 6637  C6   DA B2016    11019   8365   7568   3021   1104   -882       C  
ATOM   6638  N6   DA B2016     -49.159 -16.110   5.081  1.00 69.43           N  
ANISOU 6638  N6   DA B2016    11159   8258   6965   2756    831  -1002       N  
ATOM   6639  N1   DA B2016     -51.053 -16.471   3.801  1.00 69.72           N  
ANISOU 6639  N1   DA B2016    10387   8509   7594   3021   1249   -452       N  
ATOM   6640  C2   DA B2016     -52.018 -15.991   3.002  1.00 70.82           C  
ANISOU 6640  C2   DA B2016    10155   8611   8142   3278   1465   -298       C  
ATOM   6641  N3   DA B2016     -52.225 -14.736   2.585  1.00 72.94           N  
ANISOU 6641  N3   DA B2016    10463   8549   8703   3587   1588   -482       N  
ATOM   6642  C4   DA B2016     -51.290 -13.904   3.076  1.00 74.03           C  
ANISOU 6642  C4   DA B2016    11112   8334   8681   3583   1479   -921       C  
ATOM   6643  P    DA B2017     -55.497  -8.839   3.960  1.00100.48           P  
ANISOU 6643  P    DA B2017    14205  10838  13135   5619   3433  -1618       P  
ATOM   6644  OP1  DA B2017     -56.312  -7.710   3.469  1.00106.25           O  
ANISOU 6644  OP1  DA B2017    14643  11285  14443   5916   3557  -1558       O  
ATOM   6645  OP2  DA B2017     -54.794  -8.686   5.248  1.00104.01           O  
ANISOU 6645  OP2  DA B2017    15293  11226  12999   5507   3539  -2190       O  
ATOM   6646  O5'  DA B2017     -56.396 -10.162   4.013  1.00100.39           O  
ANISOU 6646  O5'  DA B2017    13693  11499  12954   5673   3665  -1157       O  
ATOM   6647  C5'  DA B2017     -57.172 -10.529   2.882  1.00 99.96           C  
ANISOU 6647  C5'  DA B2017    12965  11643  13373   5708   3539   -590       C  
ATOM   6648  C4'  DA B2017     -57.594 -11.985   2.945  1.00 99.09           C  
ANISOU 6648  C4'  DA B2017    12466  12137  13046   5583   3625   -193       C  
ATOM   6649  O4'  DA B2017     -56.435 -12.819   3.236  1.00 94.97           O  
ANISOU 6649  O4'  DA B2017    12346  11667  12071   5130   3282   -311       O  
ATOM   6650  C3'  DA B2017     -58.637 -12.325   4.015  1.00106.01           C  
ANISOU 6650  C3'  DA B2017    13138  13475  13666   5755   4200   -175       C  
ATOM   6651  O3'  DA B2017     -59.460 -13.407   3.548  1.00105.46           O  
ANISOU 6651  O3'  DA B2017    12387  13915  13768   5633   4214    386       O  
ATOM   6652  C2'  DA B2017     -57.763 -12.750   5.198  1.00106.19           C  
ANISOU 6652  C2'  DA B2017    13804  13586  12958   5618   4321   -551       C  
ATOM   6653  C1'  DA B2017     -56.619 -13.482   4.485  1.00 98.35           C  
ANISOU 6653  C1'  DA B2017    12934  12492  11943   5053   3603   -410       C  
ATOM   6654  N9   DA B2017     -55.341 -13.479   5.218  1.00 97.23           N  
ANISOU 6654  N9   DA B2017    13482  12173  11289   4774   3347   -823       N  
ATOM   6655  C8   DA B2017     -54.581 -12.389   5.559  1.00 98.97           C  
ANISOU 6655  C8   DA B2017    14272  11921  11410   4890   3298  -1356       C  
ATOM   6656  N7   DA B2017     -53.475 -12.687   6.204  1.00 97.40           N  
ANISOU 6656  N7   DA B2017    14571  11709  10728   4539   2987  -1616       N  
ATOM   6657  C5   DA B2017     -53.505 -14.077   6.292  1.00 94.17           C  
ANISOU 6657  C5   DA B2017    13912  11770  10100   4206   2839  -1202       C  
ATOM   6658  C6   DA B2017     -52.611 -15.024   6.863  1.00 90.75           C  
ANISOU 6658  C6   DA B2017    13739  11543   9199   3785   2494  -1158       C  
ATOM   6659  N6   DA B2017     -51.469 -14.692   7.476  1.00 90.08           N  
ANISOU 6659  N6   DA B2017    14211  11274   8742   3605   2192  -1553       N  
ATOM   6660  N1   DA B2017     -52.947 -16.325   6.777  1.00 88.60           N  
ANISOU 6660  N1   DA B2017    13112  11659   8892   3550   2450   -672       N  
ATOM   6661  C2   DA B2017     -54.090 -16.657   6.163  1.00 89.16           C  
ANISOU 6661  C2   DA B2017    12602  11927   9348   3678   2710   -288       C  
ATOM   6662  N3   DA B2017     -55.004 -15.868   5.590  1.00 91.31           N  
ANISOU 6662  N3   DA B2017    12540  12098  10054   4050   3007   -273       N  
ATOM   6663  C4   DA B2017     -54.648 -14.579   5.687  1.00 93.89           C  
ANISOU 6663  C4   DA B2017    13237  12013  10424   4325   3066   -732       C  
ATOM   6664  P    DT B2018     -60.888 -13.737   4.216  1.00112.93           P  
ANISOU 6664  P    DT B2018    12823  15365  14722   5761   4745    614       P  
ATOM   6665  OP1  DT B2018     -61.710 -14.261   3.103  1.00112.30           O  
ANISOU 6665  OP1  DT B2018    11984  15531  15153   5624   4490   1170       O  
ATOM   6666  OP2  DT B2018     -61.345 -12.581   5.030  1.00119.24           O  
ANISOU 6666  OP2  DT B2018    13854  15963  15490   6121   5169    203       O  
ATOM   6667  O5'  DT B2018     -60.574 -14.979   5.189  1.00111.71           O  
ANISOU 6667  O5'  DT B2018    12846  15662  13938   5505   4969    677       O  
ATOM   6668  C5'  DT B2018     -61.543 -16.025   5.381  1.00112.46           C  
ANISOU 6668  C5'  DT B2018    12354  16316  14058   5321   5208   1149       C  
ATOM   6669  C4'  DT B2018     -60.900 -17.282   5.962  1.00107.44           C  
ANISOU 6669  C4'  DT B2018    12004  15921  12899   4796   5039   1267       C  
ATOM   6670  O4'  DT B2018     -60.124 -17.953   4.935  1.00 99.93           O  
ANISOU 6670  O4'  DT B2018    11048  14768  12154   4327   4310   1434       O  
ATOM   6671  C3'  DT B2018     -59.943 -17.050   7.127  1.00107.41           C  
ANISOU 6671  C3'  DT B2018    12834  15805  12172   4778   5127    800       C  
ATOM   6672  O3'  DT B2018     -60.026 -18.132   8.025  1.00109.14           O  
ANISOU 6672  O3'  DT B2018    13116  16449  11901   4464   5304   1043       O  
ATOM   6673  C2'  DT B2018     -58.580 -17.009   6.436  1.00100.56           C  
ANISOU 6673  C2'  DT B2018    12382  14480  11348   4479   4392    610       C  
ATOM   6674  C1'  DT B2018     -58.769 -18.037   5.331  1.00 95.56           C  
ANISOU 6674  C1'  DT B2018    11204  13949  11157   4093   3969   1113       C  
ATOM   6675  N1   DT B2018     -57.876 -17.811   4.130  1.00 88.53           N  
ANISOU 6675  N1   DT B2018    10410  12632  10596   3928   3337   1031       N  
ATOM   6676  C2   DT B2018     -56.795 -18.647   3.948  1.00 82.57           C  
ANISOU 6676  C2   DT B2018     9930  11763   9679   3472   2839   1052       C  
ATOM   6677  O2   DT B2018     -56.544 -19.566   4.709  1.00 82.33           O  
ANISOU 6677  O2   DT B2018    10065  11935   9281   3206   2850   1164       O  
ATOM   6678  N3   DT B2018     -56.021 -18.376   2.831  1.00 77.79           N  
ANISOU 6678  N3   DT B2018     9384  10799   9374   3355   2345    970       N  
ATOM   6679  C4   DT B2018     -56.208 -17.354   1.903  1.00 78.00           C  
ANISOU 6679  C4   DT B2018     9260  10573   9805   3622   2278    907       C  
ATOM   6680  O4   DT B2018     -55.446 -17.184   0.935  1.00 74.38           O  
ANISOU 6680  O4   DT B2018     8887   9827   9547   3469   1851    867       O  
ATOM   6681  C5   DT B2018     -57.374 -16.495   2.159  1.00 83.79           C  
ANISOU 6681  C5   DT B2018     9712  11407  10717   4115   2779    922       C  
ATOM   6682  C7   DT B2018     -57.698 -15.351   1.235  1.00 83.77           C  
ANISOU 6682  C7   DT B2018     9518  11121  11191   4474   2744    927       C  
ATOM   6683  C6   DT B2018     -58.134 -16.765   3.252  1.00 88.23           C  
ANISOU 6683  C6   DT B2018    10188  12323  11014   4253   3292    960       C  
HETATM 6684  P   A2M B2019     -59.964 -17.884   9.610  1.00118.11           P  
ANISOU 6684  P   A2M B2019    14822  17836  12219   4634   5856    723       P  
HETATM 6685  OP1 A2M B2019     -60.317 -19.233  10.326  1.00119.56           O  
ANISOU 6685  OP1 A2M B2019    14857  18546  12026   4256   6049   1226       O  
HETATM 6686  O5' A2M B2019     -58.384 -17.449   9.911  1.00117.10           O  
ANISOU 6686  O5' A2M B2019    15568  17295  11629   4483   5327    195       O  
HETATM 6687  C5' A2M B2019     -57.355 -18.394   9.736  1.00113.57           C  
ANISOU 6687  C5' A2M B2019    15324  16782  11044   3973   4688    388       C  
HETATM 6688  C4' A2M B2019     -55.944 -17.766  10.122  1.00114.43           C  
ANISOU 6688  C4' A2M B2019    16202  16537  10739   3903   4259   -156       C  
HETATM 6689  O4' A2M B2019     -55.620 -16.799   9.323  1.00112.77           O  
ANISOU 6689  O4' A2M B2019    16018  15857  10973   4082   4047   -469       O  
HETATM 6690  C3' A2M B2019     -55.981 -17.159  11.601  1.00124.07           C  
ANISOU 6690  C3' A2M B2019    18026  17980  11134   4128   4741   -607       C  
HETATM 6691  O3' A2M B2019     -54.853 -17.445  12.247  1.00125.42           O  
ANISOU 6691  O3' A2M B2019    18763  18159  10732   3821   4312   -758       O  
HETATM 6692  C2' A2M B2019     -56.098 -15.654  11.390  1.00125.79           C  
ANISOU 6692  C2' A2M B2019    18421  17775  11599   4578   4959  -1193       C  
HETATM 6693  O2' A2M B2019     -55.509 -14.909  12.589  1.00129.40           O  
ANISOU 6693  O2' A2M B2019    19668  18190  11308   4640   5063  -1839       O  
HETATM 6694  C1' A2M B2019     -55.446 -15.438  10.226  1.00120.35           C  
ANISOU 6694  C1' A2M B2019    17599  16620  11510   4451   4385  -1179       C  
HETATM 6695  CM' A2M B2019     -55.825 -13.543  12.694  1.00133.44           C  
ANISOU 6695  CM' A2M B2019    20274  18317  12111   4917   5284  -2369       C  
HETATM 6696  N9  A2M B2019     -56.017 -14.308   9.552  1.00123.65           N  
ANISOU 6696  N9  A2M B2019    17803  16670  12508   4890   4631  -1386       N  
HETATM 6697  C8  A2M B2019     -57.280 -14.208   9.139  1.00126.60           C  
ANISOU 6697  C8  A2M B2019    17569  17195  13338   5229   5091  -1102       C  
HETATM 6698  N7  A2M B2019     -57.438 -12.999   8.572  1.00128.26           N  
ANISOU 6698  N7  A2M B2019    17737  16920  14074   5541   5102  -1365       N  
HETATM 6699  C5  A2M B2019     -56.270 -12.349   8.641  1.00126.66           C  
ANISOU 6699  C5  A2M B2019    18148  16259  13718   5425   4725  -1834       C  
HETATM 6700  C6  A2M B2019     -55.871 -11.064   8.212  1.00127.25           C  
ANISOU 6700  C6  A2M B2019    18425  15708  14217   5517   4516  -2205       C  
HETATM 6701  N6  A2M B2019     -56.612  -9.952   7.513  1.00129.84           N  
ANISOU 6701  N6  A2M B2019    18390  15660  15285   5822   4634  -2192       N  
HETATM 6702  N1  A2M B2019     -54.641 -10.665   8.405  1.00125.90           N  
ANISOU 6702  N1  A2M B2019    18835  15183  13820   5277   4115  -2614       N  
HETATM 6703  C2  A2M B2019     -53.750 -11.488   9.022  1.00123.89           C  
ANISOU 6703  C2  A2M B2019    18998  15177  12899   4963   3861  -2691       C  
HETATM 6704  N3  A2M B2019     -54.128 -12.742   9.441  1.00123.09           N  
ANISOU 6704  N3  A2M B2019    18672  15685  12411   4801   3975  -2279       N  
HETATM 6705  C4  A2M B2019     -55.389 -13.159   9.248  1.00124.28           C  
ANISOU 6705  C4  A2M B2019    18240  16184  12797   5038   4436  -1862       C  
HETATM 6706  OP2 A2M B2019     -60.903 -16.790  10.003  1.00126.28           O  
ANISOU 6706  OP2 A2M B2019    15731  18862  13389   5121   6427    430       O  
HETATM 6707  N1  OMC B2020     -49.396 -16.888  11.803  1.00123.34           N  
ANISOU 6707  N1  OMC B2020    19884  16712  10268   2748   1642  -1672       N  
HETATM 6708  C2  OMC B2020     -48.215 -16.065  12.140  1.00126.66           C  
ANISOU 6708  C2  OMC B2020    20808  16852  10467   2605   1193  -2211       C  
HETATM 6709  N3  OMC B2020     -48.272 -14.588  11.931  1.00129.45           N  
ANISOU 6709  N3  OMC B2020    21401  16743  11043   2842   1368  -2832       N  
HETATM 6710  C4  OMC B2020     -49.484 -13.954  11.397  1.00129.83           C  
ANISOU 6710  C4  OMC B2020    21173  16625  11531   3273   1980  -2873       C  
HETATM 6711  C5  OMC B2020     -50.657 -14.758  11.063  1.00127.70           C  
ANISOU 6711  C5  OMC B2020    20354  16695  11471   3436   2402  -2322       C  
HETATM 6712  C6  OMC B2020     -50.605 -16.239  11.268  1.00124.94           C  
ANISOU 6712  C6  OMC B2020    19778  16798  10895   3139   2227  -1735       C  
HETATM 6713  O2  OMC B2020     -47.241 -16.583  12.567  1.00127.13           O  
ANISOU 6713  O2  OMC B2020    21056  17034  10213   2297    687  -2130       O  
HETATM 6714  N4  OMC B2020     -49.525 -12.541  11.199  1.00132.63           N  
ANISOU 6714  N4  OMC B2020    21771  16462  12160   3528   2147  -3431       N  
HETATM 6715  C1' OMC B2020     -49.344 -18.344  12.015  1.00117.98           C  
ANISOU 6715  C1' OMC B2020    18999  16404   9425   2490   1477  -1057       C  
HETATM 6716  C2' OMC B2020     -49.493 -18.771  13.488  1.00122.14           C  
ANISOU 6716  C2' OMC B2020    19934  17457   9015   2438   1675   -990       C  
HETATM 6717  O2' OMC B2020     -48.259 -18.848  14.169  1.00123.80           O  
ANISOU 6717  O2' OMC B2020    20595  17717   8729   2172   1097  -1136       O  
HETATM 6718  CM2 OMC B2020     -48.321 -18.359  15.506  1.00131.61           C  
ANISOU 6718  CM2 OMC B2020    22184  19047   8775   2227   1309  -1508       C  
HETATM 6719  C3' OMC B2020     -50.249 -20.084  13.338  1.00117.40           C  
ANISOU 6719  C3' OMC B2020    18876  17160   8570   2348   1890   -270       C  
HETATM 6720  C4' OMC B2020     -51.235 -19.698  12.259  1.00116.79           C  
ANISOU 6720  C4' OMC B2020    18276  16867   9231   2593   2267   -257       C  
HETATM 6721  O4' OMC B2020     -50.438 -18.938  11.319  1.00113.84           O  
ANISOU 6721  O4' OMC B2020    17903  15976   9375   2593   1842   -606       O  
HETATM 6722  O3' OMC B2020     -49.358 -21.081  12.819  1.00106.21           O  
ANISOU 6722  O3' OMC B2020    17272  15597   7487   2030   1277    132       O  
HETATM 6723  C5' OMC B2020     -52.318 -18.776  12.746  1.00122.15           C  
ANISOU 6723  C5' OMC B2020    19027  17700   9687   2989   2988   -582       C  
HETATM 6724  O5' OMC B2020     -53.540 -19.435  13.029  1.00124.43           O  
ANISOU 6724  O5' OMC B2020    18952  18413   9914   3070   3565   -139       O  
HETATM 6725  P   OMC B2020     -54.812 -18.561  13.410  1.00130.23           P  
ANISOU 6725  P   OMC B2020    19593  19329  10560   3538   4407   -400       P  
HETATM 6726  OP1 OMC B2020     -56.005 -19.445  13.320  1.00132.01           O  
ANISOU 6726  OP1 OMC B2020    19212  19943  11003   3526   4867    212       O  
HETATM 6727  OP2 OMC B2020     -54.478 -17.841  14.735  1.00137.20           O  
ANISOU 6727  OP2 OMC B2020    21227  20383  10519   3667   4633   -959       O  
ATOM   6728  P    DT B2021     -49.396 -22.603  13.344  1.00103.14           P  
ANISOU 6728  P    DT B2021    16790  15539   6857   1777   1193    839       P  
ATOM   6729  OP1  DT B2021     -49.827 -22.636  14.766  1.00111.59           O  
ANISOU 6729  OP1  DT B2021    18268  17132   6998   1819   1564    888       O  
ATOM   6730  OP2  DT B2021     -48.115 -23.215  12.934  1.00 98.75           O  
ANISOU 6730  OP2  DT B2021    16209  14718   6593   1526    472   1008       O  
ATOM   6731  O5'  DT B2021     -50.573 -23.273  12.497  1.00 99.54           O  
ANISOU 6731  O5'  DT B2021    15714  15072   7035   1801   1590   1275       O  
ATOM   6732  C5'  DT B2021     -50.335 -23.814  11.188  1.00 88.97           C  
ANISOU 6732  C5'  DT B2021    13933  13355   6515   1663   1261   1471       C  
ATOM   6733  C4'  DT B2021     -51.658 -24.014  10.450  1.00 85.50           C  
ANISOU 6733  C4'  DT B2021    12949  12959   6577   1737   1713   1696       C  
ATOM   6734  O4'  DT B2021     -52.207 -22.721  10.101  1.00 82.98           O  
ANISOU 6734  O4'  DT B2021    12572  12567   6390   2065   2026   1243       O  
ATOM   6735  C3'  DT B2021     -51.572 -24.775   9.120  1.00 80.18           C  
ANISOU 6735  C3'  DT B2021    11821  11964   6679   1537   1404   1945       C  
ATOM   6736  O3'  DT B2021     -52.865 -25.352   8.798  1.00 82.72           O  
ANISOU 6736  O3'  DT B2021    11659  12464   7305   1485   1798   2317       O  
ATOM   6737  C2'  DT B2021     -51.202 -23.655   8.163  1.00 74.56           C  
ANISOU 6737  C2'  DT B2021    11077  10922   6329   1712   1233   1464       C  
ATOM   6738  C1'  DT B2021     -52.070 -22.513   8.702  1.00 77.64           C  
ANISOU 6738  C1'  DT B2021    11555  11515   6429   2057   1764   1164       C  
ATOM   6739  N1   DT B2021     -51.493 -21.163   8.488  1.00 77.42           N  
ANISOU 6739  N1   DT B2021    11802  11198   6416   2271   1643    601       N  
ATOM   6740  C2   DT B2021     -52.321 -20.164   8.064  1.00 77.74           C  
ANISOU 6740  C2   DT B2021    11661  11166   6712   2593   2006    382       C  
ATOM   6741  O2   DT B2021     -53.501 -20.346   7.842  1.00 79.11           O  
ANISOU 6741  O2   DT B2021    11412  11544   7102   2716   2403    633       O  
ATOM   6742  N3   DT B2021     -51.715 -18.940   7.899  1.00 77.54           N  
ANISOU 6742  N3   DT B2021    11935  10799   6726   2761   1876   -118       N  
ATOM   6743  C4   DT B2021     -50.381 -18.625   8.122  1.00 77.68           C  
ANISOU 6743  C4   DT B2021    12384  10578   6551   2601   1415   -426       C  
ATOM   6744  O4   DT B2021     -49.936 -17.493   7.950  1.00 75.04           O  
ANISOU 6744  O4   DT B2021    12289   9913   6311   2728   1333   -863       O  
ATOM   6745  C5   DT B2021     -49.553 -19.730   8.569  1.00 76.82           C  
ANISOU 6745  C5   DT B2021    12396  10618   6173   2267   1025   -166       C  
ATOM   6746  C7   DT B2021     -48.091 -19.519   8.855  1.00 75.92           C  
ANISOU 6746  C7   DT B2021    12660  10316   5872   2070    480   -425       C  
ATOM   6747  C6   DT B2021     -50.144 -20.932   8.734  1.00 76.98           C  
ANISOU 6747  C6   DT B2021    12156  10938   6156   2140   1163    337       C  
ATOM   6748  P    DT B2022     -53.114 -26.157   7.422  1.00 79.29           P  
ANISOU 6748  P    DT B2022    10720  11768   7639   1251   1571   2557       P  
ATOM   6749  OP1  DT B2022     -54.192 -27.124   7.748  1.00 83.59           O  
ANISOU 6749  OP1  DT B2022    10940  12582   8239   1063   1916   3067       O  
ATOM   6750  OP2  DT B2022     -51.842 -26.565   6.786  1.00 74.76           O  
ANISOU 6750  OP2  DT B2022    10287  10800   7320   1082    994   2471       O  
ATOM   6751  O5'  DT B2022     -53.716 -25.060   6.430  1.00 75.01           O  
ANISOU 6751  O5'  DT B2022     9878  11150   7474   1501   1703   2238       O  
ATOM   6752  C5'  DT B2022     -54.893 -24.372   6.789  1.00 77.37           C  
ANISOU 6752  C5'  DT B2022     9970  11754   7675   1775   2248   2215       C  
ATOM   6753  C4'  DT B2022     -55.284 -23.423   5.690  1.00 75.16           C  
ANISOU 6753  C4'  DT B2022     9393  11313   7850   2003   2237   1979       C  
ATOM   6754  O4'  DT B2022     -54.429 -22.254   5.734  1.00 70.73           O  
ANISOU 6754  O4'  DT B2022     9255  10493   7127   2245   2092   1492       O  
ATOM   6755  C3'  DT B2022     -55.160 -23.999   4.279  1.00 70.44           C  
ANISOU 6755  C3'  DT B2022     8457  10485   7823   1742   1819   2112       C  
ATOM   6756  O3'  DT B2022     -56.369 -23.707   3.533  1.00 72.88           O  
ANISOU 6756  O3'  DT B2022     8208  10951   8533   1853   2020   2248       O  
ATOM   6757  C2'  DT B2022     -53.919 -23.292   3.703  1.00 64.76           C  
ANISOU 6757  C2'  DT B2022     8079   9380   7149   1808   1409   1722       C  
ATOM   6758  C1'  DT B2022     -53.966 -21.959   4.436  1.00 67.14           C  
ANISOU 6758  C1'  DT B2022     8669   9705   7136   2201   1705   1372       C  
ATOM   6759  N1   DT B2022     -52.671 -21.260   4.577  1.00 65.27           N  
ANISOU 6759  N1   DT B2022     8925   9159   6715   2242   1402    975       N  
ATOM   6760  C2   DT B2022     -52.609 -19.923   4.288  1.00 65.88           C  
ANISOU 6760  C2   DT B2022     9120   9016   6896   2534   1466    625       C  
ATOM   6761  O2   DT B2022     -53.560 -19.292   3.872  1.00 68.52           O  
ANISOU 6761  O2   DT B2022     9162   9386   7488   2799   1747    646       O  
ATOM   6762  N3   DT B2022     -51.386 -19.341   4.486  1.00 64.27           N  
ANISOU 6762  N3   DT B2022     9362   8527   6532   2501   1172    271       N  
ATOM   6763  C4   DT B2022     -50.237 -19.949   4.942  1.00 63.86           C  
ANISOU 6763  C4   DT B2022     9603   8432   6228   2232    807    247       C  
ATOM   6764  O4   DT B2022     -49.194 -19.323   5.095  1.00 60.91           O  
ANISOU 6764  O4   DT B2022     9567   7819   5757   2202    540    -74       O  
ATOM   6765  C5   DT B2022     -50.364 -21.371   5.238  1.00 63.95           C  
ANISOU 6765  C5   DT B2022     9469   8685   6144   1984    756    656       C  
ATOM   6766  C7   DT B2022     -49.190 -22.160   5.733  1.00 60.40           C  
ANISOU 6766  C7   DT B2022     9273   8195   5479   1727    357    732       C  
ATOM   6767  C6   DT B2022     -51.567 -21.942   5.054  1.00 65.06           C  
ANISOU 6767  C6   DT B2022     9217   9065   6438   1991   1066    987       C  
ATOM   6768  P    DT B2023     -56.618 -24.356   2.082  1.00 70.62           P  
ANISOU 6768  P    DT B2023     7485  10561   8785   1553   1652   2429       P  
ATOM   6769  OP1  DT B2023     -58.060 -24.705   2.058  1.00 74.83           O  
ANISOU 6769  OP1  DT B2023     7422  11455   9553   1506   1962   2782       O  
ATOM   6770  OP2  DT B2023     -55.581 -25.371   1.794  1.00 68.50           O  
ANISOU 6770  OP2  DT B2023     7464  10022   8541   1185   1231   2440       O  
ATOM   6771  O5'  DT B2023     -56.272 -23.159   1.082  1.00 66.26           O  
ANISOU 6771  O5'  DT B2023     6968   9777   8429   1812   1441   2123       O  
ATOM   6772  C5'  DT B2023     -56.838 -21.877   1.308  1.00 69.12           C  
ANISOU 6772  C5'  DT B2023     7269  10207   8784   2270   1768   1984       C  
ATOM   6773  C4'  DT B2023     -56.117 -20.811   0.513  1.00 66.00           C  
ANISOU 6773  C4'  DT B2023     7093   9467   8517   2458   1508   1691       C  
ATOM   6774  O4'  DT B2023     -54.799 -20.584   1.059  1.00 63.23           O  
ANISOU 6774  O4'  DT B2023     7333   8838   7853   2427   1352   1369       O  
ATOM   6775  C3'  DT B2023     -55.908 -21.133  -0.970  1.00 62.51           C  
ANISOU 6775  C3'  DT B2023     6434   8909   8409   2208   1061   1791       C  
ATOM   6776  O3'  DT B2023     -56.707 -20.232  -1.761  1.00 65.57           O  
ANISOU 6776  O3'  DT B2023     6466   9349   9097   2486   1103   1885       O  
ATOM   6777  C2'  DT B2023     -54.379 -20.960  -1.202  1.00 55.70           C  
ANISOU 6777  C2'  DT B2023     6074   7670   7421   2095    727   1493       C  
ATOM   6778  C1'  DT B2023     -53.971 -20.134   0.010  1.00 58.31           C  
ANISOU 6778  C1'  DT B2023     6824   7895   7435   2375    978   1216       C  
ATOM   6779  N1   DT B2023     -52.549 -20.285   0.460  1.00 54.38           N  
ANISOU 6779  N1   DT B2023     6817   7158   6687   2210    730    970       N  
ATOM   6780  C2   DT B2023     -51.765 -19.152   0.579  1.00 53.97           C  
ANISOU 6780  C2   DT B2023     7124   6811   6573   2384    670    633       C  
ATOM   6781  O2   DT B2023     -52.157 -18.025   0.284  1.00 57.63           O  
ANISOU 6781  O2   DT B2023     7559   7140   7197   2679    819    525       O  
ATOM   6782  N3   DT B2023     -50.511 -19.382   1.055  1.00 52.36           N  
ANISOU 6782  N3   DT B2023     7292   6450   6152   2199    418    446       N  
ATOM   6783  C4   DT B2023     -49.963 -20.621   1.426  1.00 51.47           C  
ANISOU 6783  C4   DT B2023     7229   6434   5894   1908    226    590       C  
ATOM   6784  O4   DT B2023     -48.817 -20.733   1.832  1.00 50.84           O  
ANISOU 6784  O4   DT B2023     7441   6216   5661   1781    -29    444       O  
ATOM   6785  C5   DT B2023     -50.838 -21.761   1.290  1.00 51.45           C  
ANISOU 6785  C5   DT B2023     6885   6682   5980   1760    329    947       C  
ATOM   6786  C7   DT B2023     -50.351 -23.138   1.666  1.00 50.12           C  
ANISOU 6786  C7   DT B2023     6762   6552   5730   1463    150   1154       C  
ATOM   6787  C6   DT B2023     -52.083 -21.539   0.833  1.00 53.06           C  
ANISOU 6787  C6   DT B2023     6718   7061   6381   1894    573   1105       C  
ATOM   6788  P    DT B2024     -56.691 -20.324  -3.364  1.00 64.71           P  
ANISOU 6788  P    DT B2024     6110   9205   9271   2290    665   2016       P  
ATOM   6789  OP1  DT B2024     -57.975 -19.819  -3.875  1.00 68.63           O  
ANISOU 6789  OP1  DT B2024     6053   9957  10065   2524    762   2296       O  
ATOM   6790  OP2  DT B2024     -56.218 -21.668  -3.734  1.00 61.32           O  
ANISOU 6790  OP2  DT B2024     5717   8784   8797   1792    371   2050       O  
ATOM   6791  O5'  DT B2024     -55.593 -19.247  -3.756  1.00 63.46           O  
ANISOU 6791  O5'  DT B2024     6392   8644   9076   2465    510   1739       O  
ATOM   6792  C5'  DT B2024     -55.759 -17.897  -3.328  1.00 65.43           C  
ANISOU 6792  C5'  DT B2024     6766   8720   9373   2931    777   1613       C  
ATOM   6793  C4'  DT B2024     -54.567 -17.068  -3.744  1.00 62.96           C  
ANISOU 6793  C4'  DT B2024     6891   7980   9049   2960    572   1365       C  
ATOM   6794  O4'  DT B2024     -53.395 -17.507  -3.028  1.00 59.09           O  
ANISOU 6794  O4'  DT B2024     6847   7329   8274   2735    493   1084       O  
ATOM   6795  C3'  DT B2024     -54.218 -17.163  -5.225  1.00 61.14           C  
ANISOU 6795  C3'  DT B2024     6553   7708   8970   2737    181   1517       C  
ATOM   6796  O3'  DT B2024     -54.257 -15.876  -5.777  1.00 64.44           O  
ANISOU 6796  O3'  DT B2024     7007   7885   9592   3041    184   1562       O  
ATOM   6797  C2'  DT B2024     -52.811 -17.781  -5.260  1.00 54.28           C  
ANISOU 6797  C2'  DT B2024     6062   6651   7913   2380    -54   1286       C  
ATOM   6798  C1'  DT B2024     -52.281 -17.439  -3.879  1.00 54.88           C  
ANISOU 6798  C1'  DT B2024     6515   6547   7788   2517    158    993       C  
ATOM   6799  N1   DT B2024     -51.253 -18.393  -3.296  1.00 50.09           N  
ANISOU 6799  N1   DT B2024     6173   5909   6951   2207     15    832       N  
ATOM   6800  C2   DT B2024     -50.134 -17.868  -2.668  1.00 49.47           C  
ANISOU 6800  C2   DT B2024     6512   5552   6734   2214    -39    534       C  
ATOM   6801  O2   DT B2024     -49.885 -16.676  -2.617  1.00 52.22           O  
ANISOU 6801  O2   DT B2024     7060   5633   7148   2417     19    359       O  
ATOM   6802  N3   DT B2024     -49.319 -18.793  -2.097  1.00 45.85           N  
ANISOU 6802  N3   DT B2024     6217   5117   6087   1966   -186    462       N  
ATOM   6803  C4   DT B2024     -49.497 -20.169  -2.084  1.00 45.11           C  
ANISOU 6803  C4   DT B2024     5951   5232   5957   1729   -254    656       C  
ATOM   6804  O4   DT B2024     -48.690 -20.935  -1.560  1.00 43.01           O  
ANISOU 6804  O4   DT B2024     5847   4931   5565   1545   -399    618       O  
ATOM   6805  C5   DT B2024     -50.690 -20.651  -2.732  1.00 46.21           C  
ANISOU 6805  C5   DT B2024     5691   5614   6255   1702   -169    924       C  
ATOM   6806  C7   DT B2024     -50.966 -22.136  -2.771  1.00 46.21           C  
ANISOU 6806  C7   DT B2024     5502   5781   6277   1404   -240   1126       C  
ATOM   6807  C6   DT B2024     -51.505 -19.754  -3.295  1.00 47.15           C  
ANISOU 6807  C6   DT B2024     5608   5774   6531   1932    -55   1000       C  
ATOM   6808  P    DG B2025     -54.173 -15.667  -7.360  1.00 64.89           P  
ANISOU 6808  P    DG B2025     6912   7954   9789   2917   -160   1819       P  
ATOM   6809  OP1  DG B2025     -55.095 -14.577  -7.726  1.00 69.80           O  
ANISOU 6809  OP1  DG B2025     7302   8549  10671   3287    -72   2046       O  
ATOM   6810  OP2  DG B2025     -54.143 -16.990  -8.022  1.00 63.51           O  
ANISOU 6810  OP2  DG B2025     6561   8086   9482   2472   -427   1906       O  
ATOM   6811  O5'  DG B2025     -52.721 -15.062  -7.532  1.00 62.83           O  
ANISOU 6811  O5'  DG B2025     7146   7255   9470   2823   -266   1569       O  
ATOM   6812  C5'  DG B2025     -52.470 -13.720  -7.121  1.00 64.06           C  
ANISOU 6812  C5'  DG B2025     7569   6992   9780   3154    -92   1439       C  
ATOM   6813  C4'  DG B2025     -51.009 -13.360  -7.368  1.00 59.48           C  
ANISOU 6813  C4'  DG B2025     7399   6044   9158   2930   -248   1227       C  
ATOM   6814  O4'  DG B2025     -50.134 -14.245  -6.617  1.00 54.45           O  
ANISOU 6814  O4'  DG B2025     6971   5441   8275   2640   -295    927       O  
ATOM   6815  C3'  DG B2025     -50.557 -13.449  -8.812  1.00 56.62           C  
ANISOU 6815  C3'  DG B2025     6970   5729   8814   2685   -520   1464       C  
ATOM   6816  O3'  DG B2025     -49.721 -12.336  -9.056  1.00 58.00           O  
ANISOU 6816  O3'  DG B2025     7440   5459   9139   2722   -526   1409       O  
ATOM   6817  C2'  DG B2025     -49.807 -14.796  -8.859  1.00 50.54           C  
ANISOU 6817  C2'  DG B2025     6233   5167   7802   2264   -673   1302       C  
ATOM   6818  C1'  DG B2025     -49.189 -14.867  -7.469  1.00 50.01           C  
ANISOU 6818  C1'  DG B2025     6442   4910   7650   2274   -546    944       C  
ATOM   6819  N9   DG B2025     -48.947 -16.229  -6.932  1.00 45.36           N  
ANISOU 6819  N9   DG B2025     5824   4549   6861   2025   -600    825       N  
ATOM   6820  C8   DG B2025     -49.763 -17.324  -7.075  1.00 45.69           C  
ANISOU 6820  C8   DG B2025     5578   4947   6835   1915   -619    984       C  
ATOM   6821  N7   DG B2025     -49.325 -18.390  -6.432  1.00 44.79           N  
ANISOU 6821  N7   DG B2025     5534   4899   6586   1710   -652    859       N  
ATOM   6822  C5   DG B2025     -48.170 -17.966  -5.786  1.00 41.50           C  
ANISOU 6822  C5   DG B2025     5447   4202   6118   1702   -675    608       C  
ATOM   6823  C6   DG B2025     -47.293 -18.675  -4.935  1.00 39.92           C  
ANISOU 6823  C6   DG B2025     5427   3956   5786   1544   -751    439       C  
ATOM   6824  O6   DG B2025     -47.342 -19.869  -4.579  1.00 38.26           O  
ANISOU 6824  O6   DG B2025     5145   3902   5491   1390   -790    495       O  
ATOM   6825  N1   DG B2025     -46.239 -17.883  -4.501  1.00 41.39           N  
ANISOU 6825  N1   DG B2025     5892   3863   5970   1557   -816    211       N  
ATOM   6826  C2   DG B2025     -46.072 -16.564  -4.832  1.00 43.41           C  
ANISOU 6826  C2   DG B2025     6268   3862   6363   1690   -778    141       C  
ATOM   6827  N2   DG B2025     -45.000 -15.964  -4.304  1.00 45.32           N  
ANISOU 6827  N2   DG B2025     6773   3835   6610   1624   -874   -102       N  
ATOM   6828  N3   DG B2025     -46.888 -15.884  -5.620  1.00 43.25           N  
ANISOU 6828  N3   DG B2025     6110   3835   6489   1863   -679    321       N  
ATOM   6829  C4   DG B2025     -47.925 -16.638  -6.057  1.00 43.10           C  
ANISOU 6829  C4   DG B2025     5789   4140   6445   1872   -642    557       C  
ATOM   6830  P    DG B2026     -48.921 -12.147 -10.431  1.00 58.02           P  
ANISOU 6830  P    DG B2026     7503   5417   9126   2453   -730   1606       P  
ATOM   6831  OP1  DG B2026     -48.887 -10.677 -10.700  1.00 60.75           O  
ANISOU 6831  OP1  DG B2026     8033   5413   9636   2605   -674   1665       O  
ATOM   6832  OP2  DG B2026     -49.496 -13.097 -11.403  1.00 57.79           O  
ANISOU 6832  OP2  DG B2026     7162   5865   8931   2296   -903   1875       O  
ATOM   6833  O5'  DG B2026     -47.454 -12.679 -10.102  1.00 54.59           O  
ANISOU 6833  O5'  DG B2026     7309   4844   8587   2109   -788   1279       O  
ATOM   6834  C5'  DG B2026     -46.751 -12.205  -8.988  1.00 53.12           C  
ANISOU 6834  C5'  DG B2026     7405   4306   8474   2135   -704    936       C  
ATOM   6835  C4'  DG B2026     -45.357 -12.811  -8.949  1.00 49.44           C  
ANISOU 6835  C4'  DG B2026     7053   3811   7920   1768   -830    718       C  
ATOM   6836  O4'  DG B2026     -45.411 -14.084  -8.279  1.00 47.80           O  
ANISOU 6836  O4'  DG B2026     6763   3899   7502   1667   -867    560       O  
ATOM   6837  C3'  DG B2026     -44.722 -13.069 -10.313  1.00 48.64           C  
ANISOU 6837  C3'  DG B2026     6859   3820   7804   1507   -927    921       C  
ATOM   6838  O3'  DG B2026     -43.489 -12.358 -10.368  1.00 50.67           O  
ANISOU 6838  O3'  DG B2026     7294   3725   8231   1337   -940    823       O  
ATOM   6839  C2'  DG B2026     -44.520 -14.597 -10.369  1.00 44.37           C  
ANISOU 6839  C2'  DG B2026     6172   3635   7051   1292  -1006    816       C  
ATOM   6840  C1'  DG B2026     -44.546 -14.998  -8.894  1.00 42.92           C  
ANISOU 6840  C1'  DG B2026     6071   3419   6818   1364   -990    546       C  
ATOM   6841  N9   DG B2026     -45.080 -16.341  -8.629  1.00 39.33           N  
ANISOU 6841  N9   DG B2026     5456   3293   6195   1309  -1015    538       N  
ATOM   6842  C8   DG B2026     -46.325 -16.818  -8.955  1.00 38.22           C  
ANISOU 6842  C8   DG B2026     5098   3444   5978   1388   -987    730       C  
ATOM   6843  N7   DG B2026     -46.531 -18.057  -8.577  1.00 38.17           N  
ANISOU 6843  N7   DG B2026     4994   3642   5868   1266  -1017    681       N  
ATOM   6844  C5   DG B2026     -45.341 -18.420  -7.918  1.00 37.30           C  
ANISOU 6844  C5   DG B2026     5051   3366   5756   1141  -1071    461       C  
ATOM   6845  C6   DG B2026     -44.973 -19.632  -7.283  1.00 36.62           C  
ANISOU 6845  C6   DG B2026     4959   3343   5611   1006  -1131    371       C  
ATOM   6846  O6   DG B2026     -45.633 -20.667  -7.165  1.00 37.60           O  
ANISOU 6846  O6   DG B2026     4954   3653   5681    940  -1124    453       O  
ATOM   6847  N1   DG B2026     -43.684 -19.579  -6.749  1.00 35.42           N  
ANISOU 6847  N1   DG B2026     4956   2995   5507    931  -1223    198       N  
ATOM   6848  C2   DG B2026     -42.863 -18.493  -6.832  1.00 38.45           C  
ANISOU 6848  C2   DG B2026     5466   3150   5992    937  -1251     98       C  
ATOM   6849  N2   DG B2026     -41.656 -18.614  -6.268  1.00 35.94           N  
ANISOU 6849  N2   DG B2026     5221   2698   5737    826  -1384    -53       N  
ATOM   6850  N3   DG B2026     -43.212 -17.327  -7.419  1.00 39.63           N  
ANISOU 6850  N3   DG B2026     5653   3192   6212   1040  -1170    171       N  
ATOM   6851  C4   DG B2026     -44.446 -17.374  -7.943  1.00 38.58           C  
ANISOU 6851  C4   DG B2026     5384   3249   6024   1156  -1084    363       C  
ATOM   6852  P    DT B2027     -42.578 -12.313 -11.687  1.00 50.01           P  
ANISOU 6852  P    DT B2027     7162   3669   8169   1062   -956   1019       P  
ATOM   6853  OP1  DT B2027     -41.667 -11.158 -11.532  1.00 55.27           O  
ANISOU 6853  OP1  DT B2027     8008   3872   9119    969   -929    981       O  
ATOM   6854  OP2  DT B2027     -43.450 -12.470 -12.868  1.00 50.06           O  
ANISOU 6854  OP2  DT B2027     7027   3984   8011   1121   -960   1372       O  
ATOM   6855  O5'  DT B2027     -41.699 -13.646 -11.576  1.00 46.76           O  
ANISOU 6855  O5'  DT B2027     6644   3495   7628    809  -1011    787       O  
ATOM   6856  C5'  DT B2027     -40.548 -13.699 -10.745  1.00 45.70           C  
ANISOU 6856  C5'  DT B2027     6568   3163   7633    661  -1069    513       C  
ATOM   6857  C4'  DT B2027     -39.974 -15.131 -10.696  1.00 43.17           C  
ANISOU 6857  C4'  DT B2027     6091   3103   7210    512  -1119    365       C  
ATOM   6858  O4'  DT B2027     -40.973 -16.080 -10.239  1.00 39.89           O  
ANISOU 6858  O4'  DT B2027     5628   2930   6598    645  -1149    331       O  
ATOM   6859  C3'  DT B2027     -39.445 -15.696 -12.034  1.00 46.87           C  
ANISOU 6859  C3'  DT B2027     6414   3769   7623    331  -1022    475       C  
ATOM   6860  O3'  DT B2027     -38.122 -16.066 -11.889  1.00 50.86           O  
ANISOU 6860  O3'  DT B2027     6818   4207   8298    158  -1026    323       O  
ATOM   6861  C2'  DT B2027     -40.276 -16.952 -12.292  1.00 42.36           C  
ANISOU 6861  C2'  DT B2027     5755   3521   6817    373  -1035    459       C  
ATOM   6862  C1'  DT B2027     -40.706 -17.335 -10.880  1.00 40.38           C  
ANISOU 6862  C1'  DT B2027     5541   3227   6575    506  -1142    310       C  
ATOM   6863  N1   DT B2027     -41.974 -18.239 -10.843  1.00 38.08           N  
ANISOU 6863  N1   DT B2027     5178   3198   6094    589  -1158    364       N  
ATOM   6864  C2   DT B2027     -41.929 -19.450 -10.172  1.00 35.97           C  
ANISOU 6864  C2   DT B2027     4859   3001   5807    552  -1212    237       C  
ATOM   6865  O2   DT B2027     -40.970 -19.837  -9.590  1.00 36.04           O  
ANISOU 6865  O2   DT B2027     4875   2892   5926    496  -1266    102       O  
ATOM   6866  N3   DT B2027     -43.073 -20.172 -10.187  1.00 33.57           N  
ANISOU 6866  N3   DT B2027     4475   2903   5377    578  -1218    313       N  
ATOM   6867  C4   DT B2027     -44.266 -19.834 -10.804  1.00 37.63           C  
ANISOU 6867  C4   DT B2027     4911   3605   5782    642  -1204    497       C  
ATOM   6868  O4   DT B2027     -45.257 -20.583 -10.765  1.00 36.62           O  
ANISOU 6868  O4   DT B2027     4658   3677   5578    620  -1231    562       O  
ATOM   6869  C5   DT B2027     -44.258 -18.560 -11.525  1.00 38.13           C  
ANISOU 6869  C5   DT B2027     5021   3608   5858    717  -1171    647       C  
ATOM   6870  C7   DT B2027     -45.480 -18.083 -12.234  1.00 41.42           C  
ANISOU 6870  C7   DT B2027     5326   4227   6186    820  -1196    913       C  
ATOM   6871  C6   DT B2027     -43.128 -17.835 -11.510  1.00 37.93           C  
ANISOU 6871  C6   DT B2027     5116   3336   5959    683  -1136    578       C  
ATOM   6872  P    DC B2028     -37.016 -15.366 -12.796  1.00 56.66           P  
ANISOU 6872  P    DC B2028     7484   4835   9209    -49   -886    440       P  
ATOM   6873  OP1  DC B2028     -35.769 -16.100 -12.409  1.00 62.46           O  
ANISOU 6873  OP1  DC B2028     8019   5568  10143   -176   -913    245       O  
ATOM   6874  OP2  DC B2028     -37.191 -13.929 -12.680  1.00 56.72           O  
ANISOU 6874  OP2  DC B2028     7653   4544   9356    -34   -899    583       O  
ATOM   6875  O5'  DC B2028     -37.336 -15.860 -14.295  1.00 53.90           O  
ANISOU 6875  O5'  DC B2028     7089   4800   8591    -99   -699    605       O  
ATOM   6876  C5'  DC B2028     -36.827 -17.105 -14.720  1.00 49.07           C  
ANISOU 6876  C5'  DC B2028     6336   4401   7909   -173   -600    440       C  
ATOM   6877  C4'  DC B2028     -37.344 -17.489 -16.087  1.00 50.21           C  
ANISOU 6877  C4'  DC B2028     6522   4855   7700   -224   -451    544       C  
ATOM   6878  O4'  DC B2028     -38.800 -17.522 -16.098  1.00 47.83           O  
ANISOU 6878  O4'  DC B2028     6327   4694   7152    -99   -604    652       O  
ATOM   6879  C3'  DC B2028     -36.931 -16.562 -17.236  1.00 54.41           C  
ANISOU 6879  C3'  DC B2028     7094   5440   8140   -363   -254    815       C  
ATOM   6880  O3'  DC B2028     -36.635 -17.375 -18.373  1.00 57.82           O  
ANISOU 6880  O3'  DC B2028     7499   6180   8289   -477    -34    734       O  
ATOM   6881  C2'  DC B2028     -38.174 -15.676 -17.457  1.00 51.16           C  
ANISOU 6881  C2'  DC B2028     6842   5043   7551   -249   -390   1126       C  
ATOM   6882  C1'  DC B2028     -39.307 -16.648 -17.115  1.00 48.47           C  
ANISOU 6882  C1'  DC B2028     6501   4897   7018   -120   -564    977       C  
ATOM   6883  N1   DC B2028     -40.560 -16.019 -16.561  1.00 47.01           N  
ANISOU 6883  N1   DC B2028     6369   4645   6848     89   -752   1155       N  
ATOM   6884  C2   DC B2028     -41.816 -16.522 -16.938  1.00 46.23           C  
ANISOU 6884  C2   DC B2028     6241   4848   6478    152   -881   1239       C  
ATOM   6885  O2   DC B2028     -41.883 -17.440 -17.774  1.00 46.62           O  
ANISOU 6885  O2   DC B2028     6273   5201   6239     -1   -864   1145       O  
ATOM   6886  N3   DC B2028     -42.933 -15.975 -16.407  1.00 46.22           N  
ANISOU 6886  N3   DC B2028     6216   4802   6545    372  -1013   1410       N  
ATOM   6887  C4   DC B2028     -42.841 -15.009 -15.523  1.00 45.57           C  
ANISOU 6887  C4   DC B2028     6196   4366   6754    540   -997   1442       C  
ATOM   6888  N4   DC B2028     -43.982 -14.520 -15.028  1.00 45.45           N  
ANISOU 6888  N4   DC B2028     6145   4316   6809    796  -1072   1585       N  
ATOM   6889  C5   DC B2028     -41.569 -14.481 -15.102  1.00 45.97           C  
ANISOU 6889  C5   DC B2028     6334   4078   7056    445   -898   1314       C  
ATOM   6890  C6   DC B2028     -40.466 -15.021 -15.635  1.00 46.34           C  
ANISOU 6890  C6   DC B2028     6342   4201   7064    213   -793   1195       C  
ATOM   6891  P    DT B2029     -35.921 -16.750 -19.657  1.00 62.60           P  
ANISOU 6891  P    DT B2029     8119   6933   8732   -662    273    969       P  
ATOM   6892  OP1  DT B2029     -35.088 -17.819 -20.253  1.00 64.12           O  
ANISOU 6892  OP1  DT B2029     8203   7323   8839   -744    560    686       O  
ATOM   6893  OP2  DT B2029     -35.356 -15.436 -19.275  1.00 63.22           O  
ANISOU 6893  OP2  DT B2029     8165   6692   9163   -721    276   1223       O  
ATOM   6894  O5'  DT B2029     -37.143 -16.501 -20.645  1.00 63.38           O  
ANISOU 6894  O5'  DT B2029     8428   7339   8315   -656    187   1238       O  
ATOM   6895  C5'  DT B2029     -37.992 -17.601 -20.971  1.00 61.28           C  
ANISOU 6895  C5'  DT B2029     8226   7366   7692   -634     78   1026       C  
ATOM   6896  C4'  DT B2029     -39.283 -17.127 -21.593  1.00 60.17           C  
ANISOU 6896  C4'  DT B2029     8220   7471   7172   -606   -140   1354       C  
ATOM   6897  O4'  DT B2029     -40.082 -16.499 -20.589  1.00 55.85           O  
ANISOU 6897  O4'  DT B2029     7631   6673   6915   -402   -398   1510       O  
ATOM   6898  C3'  DT B2029     -39.127 -16.087 -22.717  1.00 64.61           C  
ANISOU 6898  C3'  DT B2029     8901   8192   7456   -712    -13   1807       C  
ATOM   6899  O3'  DT B2029     -39.512 -16.686 -23.949  1.00 70.81           O  
ANISOU 6899  O3'  DT B2029     9818   9466   7618   -859     11   1792       O  
ATOM   6900  C2'  DT B2029     -40.072 -14.930 -22.302  1.00 62.47           C  
ANISOU 6900  C2'  DT B2029     8650   7726   7360   -524   -279   2233       C  
ATOM   6901  C1'  DT B2029     -40.937 -15.589 -21.240  1.00 58.71           C  
ANISOU 6901  C1'  DT B2029     8073   7170   7063   -348   -531   1963       C  
ATOM   6902  N1   DT B2029     -41.527 -14.664 -20.198  1.00 57.96           N  
ANISOU 6902  N1   DT B2029     7940   6713   7368    -98   -693   2140       N  
ATOM   6903  C2   DT B2029     -42.883 -14.760 -19.902  1.00 57.32           C  
ANISOU 6903  C2   DT B2029     7787   6754   7239     88   -941   2236       C  
ATOM   6904  O2   DT B2029     -43.636 -15.515 -20.477  1.00 57.77           O  
ANISOU 6904  O2   DT B2029     7796   7203   6952     21  -1085   2218       O  
ATOM   6905  N3   DT B2029     -43.325 -13.911 -18.919  1.00 56.79           N  
ANISOU 6905  N3   DT B2029     7695   6332   7549    346  -1006   2343       N  
ATOM   6906  C4   DT B2029     -42.567 -13.004 -18.197  1.00 56.67           C  
ANISOU 6906  C4   DT B2029     7764   5838   7929    404   -887   2321       C  
ATOM   6907  O4   DT B2029     -43.057 -12.284 -17.339  1.00 56.84           O  
ANISOU 6907  O4   DT B2029     7804   5549   8245    643   -937   2361       O  
ATOM   6908  C5   DT B2029     -41.158 -12.955 -18.542  1.00 56.88           C  
ANISOU 6908  C5   DT B2029     7847   5760   8007    152   -688   2233       C  
ATOM   6909  C7   DT B2029     -40.250 -11.995 -17.838  1.00 56.67           C  
ANISOU 6909  C7   DT B2029     7884   5227   8420    127   -596   2202       C  
ATOM   6910  C6   DT B2029     -40.706 -13.788 -19.506  1.00 57.37           C  
ANISOU 6910  C6   DT B2029     7889   6189   7721    -67   -580   2159       C  
ATOM   6911  P    DC B2030     -39.384 -15.892 -25.334  1.00 78.38           P  
ANISOU 6911  P    DC B2030    10949  10749   8083  -1014    155   2254       P  
ATOM   6912  OP1  DC B2030     -38.900 -16.873 -26.315  1.00 82.34           O  
ANISOU 6912  OP1  DC B2030    11565  11647   8072  -1216    418   1923       O  
ATOM   6913  OP2  DC B2030     -38.648 -14.621 -25.115  1.00 80.35           O  
ANISOU 6913  OP2  DC B2030    11162  10644   8724  -1001    322   2639       O  
ATOM   6914  O5'  DC B2030     -40.887 -15.547 -25.731  1.00 79.08           O  
ANISOU 6914  O5'  DC B2030    11107  11108   7833   -935   -268   2631       O  
ATOM   6915  C5'  DC B2030     -41.869 -16.562 -25.747  1.00 77.68           C  
ANISOU 6915  C5'  DC B2030    10910  11208   7396   -949   -553   2349       C  
ATOM   6916  C4'  DC B2030     -43.237 -15.956 -25.516  1.00 78.16           C  
ANISOU 6916  C4'  DC B2030    10870  11310   7517   -764   -975   2759       C  
ATOM   6917  O4'  DC B2030     -43.257 -15.326 -24.220  1.00 73.38           O  
ANISOU 6917  O4'  DC B2030    10116  10181   7584   -502   -990   2812       O  
ATOM   6918  C3'  DC B2030     -43.622 -14.855 -26.499  1.00 84.80           C  
ANISOU 6918  C3'  DC B2030    11812  12383   8026   -758  -1092   3430       C  
ATOM   6919  O3'  DC B2030     -44.502 -15.367 -27.500  1.00 93.89           O  
ANISOU 6919  O3'  DC B2030    13024  14129   8521   -914  -1390   3511       O  
ATOM   6920  C2'  DC B2030     -44.317 -13.797 -25.643  1.00 81.14           C  
ANISOU 6920  C2'  DC B2030    11188  11526   8116   -427  -1289   3826       C  
ATOM   6921  C1'  DC B2030     -44.263 -14.357 -24.227  1.00 73.87           C  
ANISOU 6921  C1'  DC B2030    10111  10227   7730   -291  -1251   3330       C  
ATOM   6922  N1   DC B2030     -43.935 -13.331 -23.232  1.00 69.27           N  
ANISOU 6922  N1   DC B2030     9494   9062   7761    -60  -1142   3461       N  
ATOM   6923  C2   DC B2030     -44.903 -12.943 -22.317  1.00 66.79           C  
ANISOU 6923  C2   DC B2030     9029   8529   7819    245  -1334   3552       C  
ATOM   6924  O2   DC B2030     -46.008 -13.486 -22.367  1.00 67.49           O  
ANISOU 6924  O2   DC B2030     8960   8936   7745    307  -1590   3562       O  
ATOM   6925  N3   DC B2030     -44.600 -11.989 -21.394  1.00 64.46           N  
ANISOU 6925  N3   DC B2030     8759   7677   8057    451  -1220   3602       N  
ATOM   6926  C4   DC B2030     -43.387 -11.431 -21.396  1.00 65.56           C  
ANISOU 6926  C4   DC B2030     9040   7488   8380    318   -975   3594       C  
ATOM   6927  N4   DC B2030     -43.126 -10.494 -20.481  1.00 66.13           N  
ANISOU 6927  N4   DC B2030     9158   6995   8971    482   -904   3602       N  
ATOM   6928  C5   DC B2030     -42.383 -11.810 -22.337  1.00 67.34           C  
ANISOU 6928  C5   DC B2030     9360   7957   8270     -2   -775   3558       C  
ATOM   6929  C6   DC B2030     -42.701 -12.753 -23.231  1.00 68.92           C  
ANISOU 6929  C6   DC B2030     9563   8709   7916   -161   -844   3483       C  
ATOM   6930  P    DC B2031     -44.973 -14.440 -28.731  1.00105.74           P  
ANISOU 6930  P    DC B2031    14652  16035   9490   -956  -1587   4234       P  
ATOM   6931  OP1  DC B2031     -45.431 -15.347 -29.802  1.00110.73           O  
ANISOU 6931  OP1  DC B2031    15422  17335   9316  -1247  -1795   4052       O  
ATOM   6932  OP2  DC B2031     -43.915 -13.465 -29.090  1.00107.67           O  
ANISOU 6932  OP2  DC B2031    15059  16065   9787   -981  -1214   4595       O  
ATOM   6933  O5'  DC B2031     -46.242 -13.661 -28.147  1.00109.03           O  
ANISOU 6933  O5'  DC B2031    14803  16288  10335   -614  -1996   4709       O  
ATOM   6934  C5'  DC B2031     -47.401 -14.381 -27.777  1.00110.64           C  
ANISOU 6934  C5'  DC B2031    14763  16667  10609   -555  -2344   4465       C  
ATOM   6935  C4'  DC B2031     -48.395 -13.474 -27.083  1.00114.74           C  
ANISOU 6935  C4'  DC B2031    15000  16837  11758   -142  -2494   4743       C  
ATOM   6936  O4'  DC B2031     -47.876 -13.105 -25.794  1.00106.46           O  
ANISOU 6936  O4'  DC B2031    13903  15214  11331     74  -2272   4667       O  
ATOM   6937  C3'  DC B2031     -48.650 -12.140 -27.766  1.00128.49           C  
ANISOU 6937  C3'  DC B2031    16792  18472  13557     48  -2505   5272       C  
ATOM   6938  O3'  DC B2031     -49.639 -12.276 -28.788  1.00149.60           O  
ANISOU 6938  O3'  DC B2031    19391  21634  15816    -22  -2835   5431       O  
ATOM   6939  C2'  DC B2031     -49.174 -11.293 -26.613  1.00119.88           C  
ANISOU 6939  C2'  DC B2031    15490  16834  13226    462  -2469   5362       C  
ATOM   6940  C1'  DC B2031     -48.479 -11.892 -25.390  1.00106.40           C  
ANISOU 6940  C1'  DC B2031    13775  14816  11835    449  -2270   4956       C  
ATOM   6941  N1   DC B2031     -47.442 -11.000 -24.789  1.00 96.96           N  
ANISOU 6941  N1   DC B2031    12748  13021  11071    557  -1951   5029       N  
ATOM   6942  C2   DC B2031     -47.796 -10.161 -23.724  1.00 92.26           C  
ANISOU 6942  C2   DC B2031    12060  11888  11108    910  -1870   4997       C  
ATOM   6943  O2   DC B2031     -48.968 -10.171 -23.314  1.00 91.35           O  
ANISOU 6943  O2   DC B2031    11708  11836  11166   1145  -2028   4951       O  
ATOM   6944  N3   DC B2031     -46.844  -9.361 -23.169  1.00 89.56           N  
ANISOU 6944  N3   DC B2031    11893  10976  11160    957  -1604   4984       N  
ATOM   6945  C4   DC B2031     -45.596  -9.379 -23.646  1.00 88.81           C  
ANISOU 6945  C4   DC B2031    12000  10840  10904    668  -1411   5062       C  
ATOM   6946  N4   DC B2031     -44.697  -8.572 -23.072  1.00 87.19           N  
ANISOU 6946  N4   DC B2031    11928  10052  11150    679  -1170   5026       N  
ATOM   6947  C5   DC B2031     -45.219 -10.221 -24.739  1.00 90.74           C  
ANISOU 6947  C5   DC B2031    12322  11658  10497    327  -1437   5140       C  
ATOM   6948  C6   DC B2031     -46.164 -11.006 -25.273  1.00 93.66           C  
ANISOU 6948  C6   DC B2031    12575  12587  10425    285  -1716   5089       C  
HETATM 6949  P   A2M B2032     -49.877 -11.108 -29.878  1.00 73.25           P  
HETATM 6950  OP1 A2M B2032     -50.775 -11.727 -30.909  1.00 76.83           O  
HETATM 6951  O5' A2M B2032     -50.691  -9.890 -29.054  1.00 77.22           O  
HETATM 6952  C5' A2M B2032     -51.953 -10.155 -28.498  1.00 80.70           C  
HETATM 6953  C4' A2M B2032     -52.270  -9.106 -27.340  1.00 84.71           C  
HETATM 6954  O4' A2M B2032     -51.447  -9.234 -26.359  1.00 84.91           O  
HETATM 6955  C3' A2M B2032     -52.043  -7.588 -27.766  1.00 88.27           C  
HETATM 6956  O3' A2M B2032     -53.077  -7.111 -28.443  1.00 92.09           O  
HETATM 6957  C2' A2M B2032     -51.973  -6.918 -26.405  1.00 86.81           C  
HETATM 6958  O2' A2M B2032     -53.362  -6.908 -25.754  1.00 86.80           O  
HETATM 6959  C1' A2M B2032     -51.168  -7.738 -25.727  1.00 83.83           C  
HETATM 6960  CM' A2M B2032     -53.679  -5.829 -24.900  1.00 85.48           C  
HETATM 6961  N9  A2M B2032     -49.754  -7.436 -25.735  1.00 79.00           N  
HETATM 6962  C8  A2M B2032     -48.834  -7.908 -26.591  1.00 77.62           C  
HETATM 6963  N7  A2M B2032     -47.621  -7.429 -26.241  1.00 76.14           N  
HETATM 6964  C5  A2M B2032     -47.806  -6.672 -25.145  1.00 75.22           C  
HETATM 6965  C6  A2M B2032     -46.913  -5.937 -24.351  1.00 73.96           C  
HETATM 6966  N6  A2M B2032     -45.424  -5.749 -24.454  1.00 73.71           N  
HETATM 6967  N1  A2M B2032     -47.359  -5.263 -23.316  1.00 73.86           N  
HETATM 6968  C2  A2M B2032     -48.686  -5.254 -22.989  1.00 73.78           C  
HETATM 6969  N3  A2M B2032     -49.565  -5.972 -23.761  1.00 74.51           N  
HETATM 6970  C4  A2M B2032     -49.114  -6.675 -24.825  1.00 76.01           C  
HETATM 6971  OP2 A2M B2032     -48.525 -10.559 -30.484  1.00 73.85           O  
HETATM 6972  P   OMG B2033     -52.855  -6.153 -29.717  1.00 95.03           P  
HETATM 6973  OP1 OMG B2033     -53.836  -6.660 -30.756  1.00 97.06           O  
HETATM 6974  OP2 OMG B2033     -51.388  -6.023 -30.093  1.00 95.60           O  
HETATM 6975  O5' OMG B2033     -53.372  -4.740 -29.211  1.00 94.14           O  
HETATM 6976  C5' OMG B2033     -52.484  -3.651 -29.086  1.00 94.27           C  
HETATM 6977  C4' OMG B2033     -52.606  -3.028 -27.727  1.00 94.94           C  
HETATM 6978  O4' OMG B2033     -51.964  -3.889 -26.745  1.00 94.01           O  
HETATM 6979  C3' OMG B2033     -51.921  -1.675 -27.559  1.00 96.30           C  
HETATM 6980  O3' OMG B2033     -52.759  -0.596 -27.922  1.00 98.76           O  
HETATM 6981  C2' OMG B2033     -51.514  -1.689 -26.094  1.00 94.38           C  
HETATM 6982  O2' OMG B2033     -52.669  -1.536 -25.272  1.00 94.49           O  
HETATM 6983  CM2 OMG B2033     -52.869  -0.299 -24.653  1.00 93.98           C  
HETATM 6984  C1' OMG B2033     -51.063  -3.136 -25.969  1.00 91.44           C  
HETATM 6985  N9  OMG B2033     -49.692  -3.389 -26.483  1.00 85.26           N  
HETATM 6986  C8  OMG B2033     -49.401  -4.120 -27.593  1.00 83.40           C  
HETATM 6987  N7  OMG B2033     -48.060  -4.182 -27.757  1.00 81.22           N  
HETATM 6988  C5  OMG B2033     -47.522  -3.503 -26.751  1.00 80.38           C  
HETATM 6989  C6  OMG B2033     -46.049  -3.226 -26.400  1.00 78.27           C  
HETATM 6990  O6  OMG B2033     -45.165  -3.644 -27.098  1.00 77.09           O  
HETATM 6991  N1  OMG B2033     -45.789  -2.453 -25.218  1.00 77.02           N  
HETATM 6992  C2  OMG B2033     -46.872  -1.956 -24.400  1.00 77.71           C  
HETATM 6993  N2  OMG B2033     -46.611  -1.178 -23.216  1.00 78.17           N  
HETATM 6994  N3  OMG B2033     -48.261  -2.226 -24.734  1.00 78.70           N  
HETATM 6995  C4  OMG B2033     -48.539  -3.023 -25.952  1.00 81.19           C  
HETATM 6996  P   OMG B2034     -52.225   0.533 -28.931  1.00100.46           P  
HETATM 6997  OP1 OMG B2034     -53.472   1.303 -29.287  1.00101.17           O  
HETATM 6998  OP2 OMG B2034     -51.353  -0.081 -30.021  1.00 99.06           O  
HETATM 6999  O5' OMG B2034     -51.377   1.494 -27.982  1.00101.31           O  
HETATM 7000  C5' OMG B2034     -51.999   2.136 -26.867  1.00101.80           C  
HETATM 7001  C4' OMG B2034     -50.990   2.648 -25.867  1.00102.32           C  
HETATM 7002  O4' OMG B2034     -49.884   1.695 -25.759  1.00101.99           O  
HETATM 7003  C3' OMG B2034     -50.347   3.986 -26.239  1.00102.67           C  
HETATM 7004  O3' OMG B2034     -49.950   4.663 -25.045  1.00103.03           O  
HETATM 7005  C2' OMG B2034     -49.108   3.528 -26.996  1.00101.67           C  
HETATM 7006  O2' OMG B2034     -48.113   4.519 -27.211  1.00100.74           O  
HETATM 7007  CM2 OMG B2034     -48.368   5.315 -28.345  1.00 99.26           C  
HETATM 7008  C1' OMG B2034     -48.671   2.351 -26.111  1.00100.29           C  
HETATM 7009  N9  OMG B2034     -47.752   1.396 -26.752  1.00 96.04           N  
HETATM 7010  C8  OMG B2034     -48.020   0.598 -27.810  1.00 94.15           C  
HETATM 7011  N7  OMG B2034     -46.888  -0.087 -28.104  1.00 92.48           N  
HETATM 7012  C5  OMG B2034     -45.941   0.289 -27.244  1.00 91.57           C  
HETATM 7013  C6  OMG B2034     -44.474  -0.125 -27.063  1.00 89.63           C  
HETATM 7014  O6  OMG B2034     -43.985  -0.929 -27.792  1.00 88.32           O  
HETATM 7015  N1  OMG B2034     -43.706   0.484 -26.011  1.00 89.59           N  
HETATM 7016  C2  OMG B2034     -44.306   1.464 -25.128  1.00 89.70           C  
HETATM 7017  N2  OMG B2034     -43.565   2.097 -24.053  1.00 88.78           N  
HETATM 7018  N3  OMG B2034     -45.696   1.840 -25.312  1.00 91.13           N  
HETATM 7019  C4  OMG B2034     -46.487   1.216 -26.404  1.00 92.93           C  
TER    7020      OMG B2034                                                      
HETATM 7021  C1  NAG C   1     -36.027 -47.852  16.837  1.00 20.76           C  
HETATM 7022  C2  NAG C   1     -36.907 -49.071  17.097  1.00 22.76           C  
HETATM 7023  C3  NAG C   1     -38.034 -48.704  18.100  1.00 22.77           C  
HETATM 7024  C4  NAG C   1     -37.478 -48.057  19.364  1.00 24.21           C  
HETATM 7025  C5  NAG C   1     -36.501 -46.917  19.046  1.00 25.15           C  
HETATM 7026  C6  NAG C   1     -35.759 -46.424  20.283  1.00 24.62           C  
HETATM 7027  C7  NAG C   1     -37.225 -50.821  15.427  1.00 25.05           C  
HETATM 7028  C8  NAG C   1     -37.993 -51.268  14.197  1.00 23.61           C  
HETATM 7029  N2  NAG C   1     -37.492 -49.590  15.870  1.00 21.52           N  
HETATM 7030  O3  NAG C   1     -38.780 -49.859  18.468  1.00 20.68           O  
HETATM 7031  O4  NAG C   1     -38.608 -47.432  19.958  1.00 29.04           O  
HETATM 7032  O5  NAG C   1     -35.495 -47.358  18.112  1.00 22.93           O  
HETATM 7033  O6  NAG C   1     -35.135 -47.512  20.970  1.00 24.60           O  
HETATM 7034  O7  NAG C   1     -36.352 -51.515  15.948  1.00 26.40           O  
HETATM 7035  C1  NAG C   2     -38.739 -47.748  21.314  1.00 32.03           C  
HETATM 7036  C2  NAG C   2     -39.552 -46.621  21.937  1.00 34.15           C  
HETATM 7037  C3  NAG C   2     -39.961 -46.984  23.371  1.00 37.01           C  
HETATM 7038  C4  NAG C   2     -40.594 -48.366  23.432  1.00 39.35           C  
HETATM 7039  C5  NAG C   2     -39.696 -49.377  22.730  1.00 36.34           C  
HETATM 7040  C6  NAG C   2     -40.333 -50.742  22.629  1.00 35.14           C  
HETATM 7041  C7  NAG C   2     -38.977 -44.387  21.003  1.00 35.65           C  
HETATM 7042  C8  NAG C   2     -38.104 -43.165  21.170  1.00 35.36           C  
HETATM 7043  N2  NAG C   2     -38.816 -45.357  21.928  1.00 34.36           N  
HETATM 7044  O3  NAG C   2     -40.860 -45.979  23.818  1.00 37.61           O  
HETATM 7045  O4  NAG C   2     -40.643 -48.812  24.782  1.00 46.62           O  
HETATM 7046  O5  NAG C   2     -39.447 -48.938  21.385  1.00 35.11           O  
HETATM 7047  O6  NAG C   2     -41.685 -50.575  22.229  1.00 37.39           O  
HETATM 7048  O7  NAG C   2     -39.753 -44.504  20.034  1.00 34.71           O  
HETATM 7049  C1  BMA C   3     -41.860 -48.552  25.499  1.00 52.69           C  
HETATM 7050  C2  BMA C   3     -42.090 -49.692  26.519  1.00 55.65           C  
HETATM 7051  C3  BMA C   3     -43.317 -49.334  27.387  1.00 62.73           C  
HETATM 7052  C4  BMA C   3     -43.208 -47.944  28.013  1.00 62.09           C  
HETATM 7053  C5  BMA C   3     -42.902 -46.904  26.905  1.00 59.47           C  
HETATM 7054  C6  BMA C   3     -42.671 -45.463  27.429  1.00 59.58           C  
HETATM 7055  O2  BMA C   3     -40.956 -49.812  27.389  1.00 52.76           O  
HETATM 7056  O3  BMA C   3     -43.574 -50.279  28.395  1.00 70.22           O  
HETATM 7057  O4  BMA C   3     -44.446 -47.624  28.579  1.00 63.55           O  
HETATM 7058  O5  BMA C   3     -41.721 -47.353  26.166  1.00 55.30           O  
HETATM 7059  O6  BMA C   3     -42.605 -44.591  26.293  1.00 61.02           O  
HETATM 7060  C1  MAN C   4     -42.319 -43.231  26.690  1.00 62.01           C  
HETATM 7061  C2  MAN C   4     -42.510 -42.359  25.417  1.00 62.66           C  
HETATM 7062  C3  MAN C   4     -41.320 -42.499  24.448  1.00 63.83           C  
HETATM 7063  C4  MAN C   4     -39.986 -42.311  25.184  1.00 64.19           C  
HETATM 7064  C5  MAN C   4     -39.904 -43.333  26.352  1.00 64.60           C  
HETATM 7065  C6  MAN C   4     -38.581 -43.326  27.156  1.00 67.04           C  
HETATM 7066  O2  MAN C   4     -42.611 -40.955  25.721  1.00 63.00           O  
HETATM 7067  O3  MAN C   4     -41.394 -41.578  23.340  1.00 63.92           O  
HETATM 7068  O4  MAN C   4     -38.918 -42.518  24.272  1.00 64.07           O  
HETATM 7069  O5  MAN C   4     -41.011 -43.117  27.255  1.00 62.74           O  
HETATM 7070  O6  MAN C   4     -38.246 -41.985  27.512  1.00 69.93           O  
HETATM 7071  C1  MAN C   5     -42.566 -41.779  22.499  1.00 63.70           C  
HETATM 7072  C2  MAN C   5     -42.174 -41.529  20.986  1.00 61.27           C  
HETATM 7073  C3  MAN C   5     -41.962 -39.978  20.712  1.00 61.87           C  
HETATM 7074  C4  MAN C   5     -43.132 -39.141  21.303  1.00 64.11           C  
HETATM 7075  C5  MAN C   5     -43.358 -39.552  22.801  1.00 65.41           C  
HETATM 7076  C6  MAN C   5     -44.524 -38.869  23.438  1.00 67.65           C  
HETATM 7077  O2  MAN C   5     -43.204 -41.984  20.087  1.00 56.25           O  
HETATM 7078  O3  MAN C   5     -41.753 -39.634  19.325  1.00 59.53           O  
HETATM 7079  O4  MAN C   5     -42.879 -37.699  21.196  1.00 63.64           O  
HETATM 7080  O5  MAN C   5     -43.648 -40.946  22.866  1.00 64.21           O  
HETATM 7081  O6  MAN C   5     -45.672 -39.534  22.956  1.00 69.47           O  
HETATM 7082  C1  MAN C   6     -42.710 -43.165  19.456  1.00 52.48           C  
HETATM 7083  C2  MAN C   6     -43.534 -43.345  18.185  1.00 47.83           C  
HETATM 7084  C3  MAN C   6     -44.982 -43.629  18.630  1.00 51.05           C  
HETATM 7085  C4  MAN C   6     -45.022 -44.958  19.510  1.00 52.18           C  
HETATM 7086  C5  MAN C   6     -44.127 -44.784  20.754  1.00 52.68           C  
HETATM 7087  C6  MAN C   6     -43.998 -46.075  21.623  1.00 54.02           C  
HETATM 7088  O2  MAN C   6     -43.114 -44.527  17.497  1.00 41.84           O  
HETATM 7089  O3  MAN C   6     -45.828 -43.695  17.534  1.00 51.72           O  
HETATM 7090  O4  MAN C   6     -46.316 -45.294  19.959  1.00 52.34           O  
HETATM 7091  O5  MAN C   6     -42.785 -44.312  20.375  1.00 51.27           O  
HETATM 7092  O6  MAN C   6     -43.458 -45.653  22.914  1.00 54.18           O  
HETATM 7093  C1  MAN C   7     -44.148 -51.428  27.761  1.00 78.54           C  
HETATM 7094  C2  MAN C   7     -45.497 -51.816  28.502  1.00 83.46           C  
HETATM 7095  C3  MAN C   7     -45.179 -52.457  29.870  1.00 85.31           C  
HETATM 7096  C4  MAN C   7     -44.025 -53.490  29.728  1.00 84.88           C  
HETATM 7097  C5  MAN C   7     -42.802 -52.825  29.116  1.00 84.08           C  
HETATM 7098  C6  MAN C   7     -41.626 -53.747  29.014  1.00 84.92           C  
HETATM 7099  O2  MAN C   7     -46.323 -52.773  27.755  1.00 84.70           O  
HETATM 7100  O3  MAN C   7     -46.337 -53.050  30.493  1.00 87.20           O  
HETATM 7101  O4  MAN C   7     -43.674 -53.985  30.954  1.00 85.31           O  
HETATM 7102  O5  MAN C   7     -43.167 -52.440  27.787  1.00 81.67           O  
HETATM 7103  O6  MAN C   7     -40.541 -52.990  28.512  1.00 85.13           O  
HETATM 7104  C1  NAG D   1     -64.601 -44.709  -8.673  1.00 28.67           C  
HETATM 7105  C2  NAG D   1     -65.524 -43.640  -8.071  1.00 30.69           C  
HETATM 7106  C3  NAG D   1     -66.952 -43.734  -8.646  1.00 33.29           C  
HETATM 7107  C4  NAG D   1     -66.904 -43.771 -10.167  1.00 36.38           C  
HETATM 7108  C5  NAG D   1     -66.031 -44.951 -10.590  1.00 38.06           C  
HETATM 7109  C6  NAG D   1     -65.917 -45.128 -12.084  1.00 40.30           C  
HETATM 7110  C7  NAG D   1     -64.863 -42.868  -5.847  1.00 34.14           C  
HETATM 7111  C8  NAG D   1     -64.951 -43.084  -4.377  1.00 34.62           C  
HETATM 7112  N2  NAG D   1     -65.531 -43.738  -6.614  1.00 32.46           N  
HETATM 7113  O3  NAG D   1     -67.675 -42.582  -8.218  1.00 31.05           O  
HETATM 7114  O4  NAG D   1     -68.217 -43.940 -10.697  1.00 39.77           O  
HETATM 7115  O5  NAG D   1     -64.703 -44.693 -10.125  1.00 35.16           O  
HETATM 7116  O6  NAG D   1     -65.285 -43.964 -12.594  1.00 45.70           O  
HETATM 7117  O7  NAG D   1     -64.236 -41.926  -6.330  1.00 33.68           O  
HETATM 7118  C1  NAG D   2     -68.589 -42.906 -11.630  1.00 43.20           C  
HETATM 7119  C2  NAG D   2     -69.794 -43.432 -12.390  1.00 43.52           C  
HETATM 7120  C3  NAG D   2     -70.337 -42.377 -13.356  1.00 43.04           C  
HETATM 7121  C4  NAG D   2     -70.656 -41.096 -12.599  1.00 48.62           C  
HETATM 7122  C5  NAG D   2     -69.421 -40.599 -11.858  1.00 49.82           C  
HETATM 7123  C6  NAG D   2     -69.740 -39.423 -10.956  1.00 51.21           C  
HETATM 7124  C7  NAG D   2     -69.842 -45.859 -12.617  1.00 44.32           C  
HETATM 7125  C8  NAG D   2     -69.458 -47.038 -13.442  1.00 44.77           C  
HETATM 7126  N2  NAG D   2     -69.482 -44.664 -13.095  1.00 43.07           N  
HETATM 7127  O3  NAG D   2     -71.532 -42.886 -13.927  1.00 39.13           O  
HETATM 7128  O4  NAG D   2     -71.371 -40.066 -13.304  1.00 52.25           O  
HETATM 7129  O5  NAG D   2     -68.917 -41.641 -10.999  1.00 46.03           O  
HETATM 7130  O6  NAG D   2     -70.803 -39.746 -10.070  1.00 51.69           O  
HETATM 7131  O7  NAG D   2     -70.439 -45.979 -11.556  1.00 45.73           O  
HETATM 7132  C1  BMA D   3     -71.280 -39.498 -14.634  1.00 54.76           C  
HETATM 7133  C2  BMA D   3     -71.947 -40.494 -15.600  1.00 58.81           C  
HETATM 7134  C3  BMA D   3     -72.896 -39.952 -16.542  1.00 62.05           C  
HETATM 7135  C4  BMA D   3     -73.843 -39.055 -15.883  1.00 56.34           C  
HETATM 7136  C5  BMA D   3     -73.078 -37.829 -15.659  1.00 51.27           C  
HETATM 7137  C6  BMA D   3     -74.000 -36.635 -15.356  1.00 46.76           C  
HETATM 7138  O2  BMA D   3     -72.788 -41.254 -14.931  1.00 61.41           O  
HETATM 7139  O3  BMA D   3     -73.554 -41.086 -17.180  1.00 68.24           O  
HETATM 7140  O4  BMA D   3     -74.811 -38.779 -16.833  1.00 57.08           O  
HETATM 7141  O5  BMA D   3     -71.854 -38.130 -14.666  1.00 53.12           O  
HETATM 7142  O6  BMA D   3     -73.372 -35.626 -14.643  1.00 45.54           O  
HETATM 7143  C1  MAN D   4     -72.878 -41.123 -18.479  1.00 71.99           C  
HETATM 7144  C2  MAN D   4     -73.887 -41.390 -19.715  1.00 73.00           C  
HETATM 7145  C3  MAN D   4     -73.084 -41.170 -20.988  1.00 73.40           C  
HETATM 7146  C4  MAN D   4     -71.587 -40.832 -20.620  1.00 74.57           C  
HETATM 7147  C5  MAN D   4     -71.032 -42.034 -19.815  1.00 74.21           C  
HETATM 7148  C6  MAN D   4     -69.547 -41.935 -19.509  1.00 75.06           C  
HETATM 7149  O2  MAN D   4     -74.999 -40.447 -19.797  1.00 73.58           O  
HETATM 7150  O3  MAN D   4     -73.686 -40.189 -21.822  1.00 72.74           O  
HETATM 7151  O4  MAN D   4     -70.780 -40.577 -21.743  1.00 76.54           O  
HETATM 7152  O5  MAN D   4     -71.764 -42.093 -18.535  1.00 73.31           O  
HETATM 7153  O6  MAN D   4     -68.916 -41.217 -20.554  1.00 75.03           O  
HETATM 7154 ZN    ZN A 912     -33.442 -31.212   2.292  1.00 27.64          ZN  
HETATM 7155 ZN    ZN A 913     -35.873 -29.549  -1.648  1.00 25.22          ZN  
HETATM 7156 CA    CA A 914     -45.236 -56.003  16.385  1.00 22.16          CA  
HETATM 7157 NA    NA A 915     -52.688 -57.880  -9.268  1.00 30.64          NA  
HETATM 7158 CL    CL A 916     -43.933 -34.113   3.739  1.00 42.65          CL  
HETATM 7159  K     K A 917     -58.488 -73.982   3.008  1.00 23.43           K  
HETATM 7160  C1  GOL A 918     -44.467 -54.206  -8.638  1.00 63.06           C  
HETATM 7161  O1  GOL A 918     -45.386 -53.563  -9.499  1.00 61.80           O  
HETATM 7162  C2  GOL A 918     -45.216 -54.844  -7.467  1.00 62.14           C  
HETATM 7163  O2  GOL A 918     -45.350 -56.234  -7.653  1.00 57.88           O  
HETATM 7164  C3  GOL A 918     -44.564 -54.483  -6.122  1.00 63.28           C  
HETATM 7165  O3  GOL A 918     -44.067 -53.176  -6.238  1.00 65.05           O  
HETATM 7166  C1  GOL A 919     -19.201 -71.053   6.534  1.00 57.26           C  
HETATM 7167  O1  GOL A 919     -19.105 -69.968   5.631  1.00 57.35           O  
HETATM 7168  C2  GOL A 919     -18.694 -72.296   5.801  1.00 57.63           C  
HETATM 7169  O2  GOL A 919     -18.831 -72.139   4.399  1.00 53.08           O  
HETATM 7170  C3  GOL A 919     -19.376 -73.573   6.286  1.00 59.16           C  
HETATM 7171  O3  GOL A 919     -19.809 -73.353   7.611  1.00 60.95           O  
HETATM 7172  C1  GOL A 920     -44.367 -76.675  -1.952  1.00 61.34           C  
HETATM 7173  O1  GOL A 920     -45.519 -77.041  -2.651  1.00 64.16           O  
HETATM 7174  C2  GOL A 920     -44.355 -75.155  -1.994  1.00 59.13           C  
HETATM 7175  O2  GOL A 920     -45.233 -74.654  -3.004  1.00 62.10           O  
HETATM 7176  C3  GOL A 920     -44.923 -74.778  -0.658  1.00 49.86           C  
HETATM 7177  O3  GOL A 920     -43.888 -74.295   0.066  1.00 47.17           O  
HETATM 7178  C1  GOL A 921     -45.073 -47.028 -11.156  1.00 62.51           C  
HETATM 7179  O1  GOL A 921     -44.109 -47.714 -11.914  1.00 63.83           O  
HETATM 7180  C2  GOL A 921     -45.172 -47.821  -9.879  1.00 63.24           C  
HETATM 7181  O2  GOL A 921     -45.951 -48.971 -10.173  1.00 64.62           O  
HETATM 7182  C3  GOL A 921     -45.654 -46.945  -8.723  1.00 61.40           C  
HETATM 7183  O3  GOL A 921     -44.770 -46.969  -7.593  1.00 60.19           O  
HETATM 7184  C1  GOL A 922      -0.634 -47.348   6.616  1.00 70.18           C  
HETATM 7185  O1  GOL A 922      -0.873 -47.154   8.002  1.00 71.25           O  
HETATM 7186  C2  GOL A 922      -0.740 -46.038   5.837  1.00 69.76           C  
HETATM 7187  O2  GOL A 922      -0.740 -44.947   6.726  1.00 69.66           O  
HETATM 7188  C3  GOL A 922       0.436 -45.897   4.875  1.00 69.18           C  
HETATM 7189  O3  GOL A 922       0.531 -47.101   4.143  1.00 68.93           O  
HETATM 7190  C1  GOL A 923     -32.273 -59.183  17.320  1.00 66.76           C  
HETATM 7191  O1  GOL A 923     -33.008 -60.388  17.437  1.00 63.99           O  
HETATM 7192  C2  GOL A 923     -30.871 -59.129  17.936  1.00 66.69           C  
HETATM 7193  O2  GOL A 923     -29.935 -59.482  16.953  1.00 66.63           O  
HETATM 7194  C3  GOL A 923     -30.653 -57.717  18.492  1.00 67.49           C  
HETATM 7195  O3  GOL A 923     -29.422 -57.491  19.147  1.00 68.80           O  
HETATM 7196  C1  GOL A 924     -51.086 -33.867   6.717  1.00 61.01           C  
HETATM 7197  O1  GOL A 924     -52.331 -34.414   6.377  1.00 56.85           O  
HETATM 7198  C2  GOL A 924     -51.342 -32.451   7.252  1.00 64.99           C  
HETATM 7199  O2  GOL A 924     -52.517 -31.835   6.712  1.00 65.45           O  
HETATM 7200  C3  GOL A 924     -50.095 -31.634   7.002  1.00 64.66           C  
HETATM 7201  O3  GOL A 924     -49.905 -31.742   5.634  1.00 65.55           O  
HETATM 7202  C1  GOL A 925     -47.933 -79.099  -2.351  1.00 58.99           C  
HETATM 7203  O1  GOL A 925     -48.734 -79.775  -3.287  1.00 57.38           O  
HETATM 7204  C2  GOL A 925     -48.463 -77.674  -2.229  1.00 61.09           C  
HETATM 7205  O2  GOL A 925     -47.856 -77.037  -1.122  1.00 61.13           O  
HETATM 7206  C3  GOL A 925     -49.988 -77.648  -2.161  1.00 61.09           C  
HETATM 7207  O3  GOL A 925     -50.395 -77.273  -0.858  1.00 62.00           O  
HETATM 7208  C1  GOL A 926     -39.933 -46.409  -7.766  1.00 51.80           C  
HETATM 7209  O1  GOL A 926     -39.601 -45.204  -8.408  1.00 44.89           O  
HETATM 7210  C2  GOL A 926     -41.066 -46.291  -6.725  1.00 57.01           C  
HETATM 7211  O2  GOL A 926     -42.221 -46.909  -7.239  1.00 60.60           O  
HETATM 7212  C3  GOL A 926     -40.767 -47.045  -5.432  1.00 56.61           C  
HETATM 7213  O3  GOL A 926     -39.639 -47.874  -5.655  1.00 57.24           O  
HETATM 7214  C1  GOL A 927     -44.944 -53.632  21.516  1.00 58.48           C  
HETATM 7215  O1  GOL A 927     -46.262 -54.032  21.376  1.00 52.79           O  
HETATM 7216  C2  GOL A 927     -44.140 -54.901  21.469  1.00 60.32           C  
HETATM 7217  O2  GOL A 927     -43.046 -54.821  20.613  1.00 56.71           O  
HETATM 7218  C3  GOL A 927     -43.811 -55.392  22.867  1.00 65.97           C  
HETATM 7219  O3  GOL A 927     -44.602 -56.562  23.076  1.00 67.64           O  
HETATM 7220 CA    CA B2101     -53.802 -18.782  -9.393  1.00 49.82          CA  
HETATM 7221  O   HOH A1001     -33.107 -45.617  -9.492  1.00 35.87           O  
HETATM 7222  O   HOH A1002     -51.935 -58.889   5.224  1.00 67.70           O  
HETATM 7223  O   HOH A1003     -31.993 -70.383  21.359  1.00 37.13           O  
HETATM 7224  O   HOH A1004     -47.351 -53.198 -10.484  1.00 24.25           O  
HETATM 7225  O   HOH A1005     -12.671 -66.038   7.309  1.00 51.92           O  
HETATM 7226  O   HOH A1006     -35.304 -65.214 -12.711  1.00 49.68           O  
HETATM 7227  O   HOH A1007     -30.401 -61.381  25.231  1.00 50.29           O  
HETATM 7228  O   HOH A1008     -36.117 -28.721   2.125  1.00 51.17           O  
HETATM 7229  O   HOH A1009       0.858 -22.006   5.679  1.00 37.60           O  
HETATM 7230  O   HOH A1010     -43.256 -94.037  16.067  1.00 51.64           O  
HETATM 7231  O   HOH A1011     -46.573 -72.938  -1.949  1.00 40.16           O  
HETATM 7232  O   HOH A1012     -42.743 -69.038 -14.902  1.00 51.18           O  
HETATM 7233  O   HOH A1013     -49.426 -81.384   0.633  1.00 30.21           O  
HETATM 7234  O   HOH A1014     -22.917 -24.870  15.843  1.00 34.10           O  
HETATM 7235  O   HOH A1015      -2.286 -20.970  -0.772  1.00 35.33           O  
HETATM 7236  O   HOH A1016     -44.617 -57.280  -9.797  1.00 32.36           O  
HETATM 7237  O   HOH A1017     -29.323 -70.585 -13.579  1.00 41.30           O  
HETATM 7238  O   HOH A1018     -23.476 -74.260  11.969  1.00 38.81           O  
HETATM 7239  O   HOH A1019     -58.190 -59.508  -0.658  1.00 52.25           O  
HETATM 7240  O   HOH A1020     -43.348 -49.716  11.150  1.00 24.59           O  
HETATM 7241  O   HOH A1021     -40.536 -50.399  11.886  1.00 27.27           O  
HETATM 7242  O   HOH A1022     -31.397 -44.360   6.424  1.00 26.54           O  
HETATM 7243  O   HOH A1023     -46.659 -56.431 -11.563  1.00 42.26           O  
HETATM 7244  O   HOH A1024     -51.357 -52.740  -1.868  1.00 61.80           O  
HETATM 7245  O   HOH A1025     -47.987 -42.357  17.499  1.00 30.30           O  
HETATM 7246  O   HOH A1026     -45.571 -24.978  12.336  1.00 42.66           O  
HETATM 7247  O   HOH A1027     -12.559  -6.598   3.136  1.00 56.56           O  
HETATM 7248  O   HOH A1028     -32.940 -59.116  -1.553  1.00 33.59           O  
HETATM 7249  O   HOH A1029      -5.822 -30.858   8.080  1.00 24.21           O  
HETATM 7250  O   HOH A1030     -28.366 -57.682   5.605  1.00 16.49           O  
HETATM 7251  O   HOH A1031     -13.661 -66.772   0.903  1.00 40.59           O  
HETATM 7252  O   HOH A1032     -19.922 -44.618  22.406  1.00 38.09           O  
HETATM 7253  O   HOH A1033     -13.390 -23.259  -3.333  1.00 30.87           O  
HETATM 7254  O   HOH A1034     -27.957 -49.016  -4.233  1.00 40.98           O  
HETATM 7255  O   HOH A1035     -47.852 -82.463  -8.145  1.00 48.23           O  
HETATM 7256  O   HOH A1036     -26.610 -70.387  10.511  1.00 26.75           O  
HETATM 7257  O   HOH A1037     -40.155 -43.819   9.594  1.00 31.43           O  
HETATM 7258  O   HOH A1038     -59.259 -64.214   0.714  1.00 57.24           O  
HETATM 7259  O   HOH A1039     -39.319 -54.033  -8.023  1.00 27.25           O  
HETATM 7260  O   HOH A1040     -36.407 -83.394   1.915  1.00 28.94           O  
HETATM 7261  O   HOH A1041     -14.815 -36.859  -7.149  1.00 49.01           O  
HETATM 7262  O   HOH A1042     -37.536 -30.906   2.026  1.00 33.11           O  
HETATM 7263  O   HOH A1043     -14.904  -7.011   7.262  1.00 36.56           O  
HETATM 7264  O   HOH A1044     -41.768 -49.169  15.754  1.00 30.72           O  
HETATM 7265  O   HOH A1045     -49.557 -55.678  23.512  1.00 52.26           O  
HETATM 7266  O   HOH A1046     -28.576 -49.586   8.615  1.00 24.60           O  
HETATM 7267  O   HOH A1047     -52.038 -50.001 -13.763  1.00 46.95           O  
HETATM 7268  O   HOH A1048     -45.280 -76.448  10.921  1.00 37.55           O  
HETATM 7269  O   HOH A1049     -33.240 -49.506   8.141  1.00 28.01           O  
HETATM 7270  O   HOH A1050     -16.429 -10.888  13.419  1.00 53.20           O  
HETATM 7271  O   HOH A1051     -11.527 -41.328   1.030  1.00 27.05           O  
HETATM 7272  O   HOH A1052     -29.325 -50.631  12.163  1.00 21.81           O  
HETATM 7273  O   HOH A1053     -49.778 -36.030   8.877  1.00 37.05           O  
HETATM 7274  O   HOH A1054     -50.758 -88.543   6.787  1.00 37.42           O  
HETATM 7275  O   HOH A1055      -6.497 -35.197  -2.113  1.00 46.33           O  
HETATM 7276  O   HOH A1056     -42.504 -62.649  14.510  1.00 18.31           O  
HETATM 7277  O   HOH A1057       1.786 -25.870   1.792  1.00 52.50           O  
HETATM 7278  O   HOH A1058     -21.557 -66.125  -3.894  1.00 23.40           O  
HETATM 7279  O   HOH A1059     -23.706 -52.954   5.474  1.00 36.74           O  
HETATM 7280  O   HOH A1060     -42.830 -37.187  18.615  1.00 33.59           O  
HETATM 7281  O   HOH A1061     -40.307 -65.326  17.095  1.00 38.60           O  
HETATM 7282  O   HOH A1062     -60.503 -51.589  -1.435  1.00 46.41           O  
HETATM 7283  O   HOH A1063     -40.983 -46.129  18.358  1.00 26.43           O  
HETATM 7284  O   HOH A1064     -24.858 -48.951  22.207  1.00 46.21           O  
HETATM 7285  O   HOH A1065     -49.135 -55.423   9.989  1.00 35.04           O  
HETATM 7286  O   HOH A1066     -38.672 -43.952   7.451  1.00 28.78           O  
HETATM 7287  O   HOH A1067     -29.615 -30.316  -5.549  1.00 24.86           O  
HETATM 7288  O   HOH A1068     -45.424 -31.892 -11.676  1.00 42.87           O  
HETATM 7289  O   HOH A1069     -55.650 -65.781  -1.662  1.00 23.32           O  
HETATM 7290  O   HOH A1070     -25.326 -16.763   3.446  1.00 46.56           O  
HETATM 7291  O   HOH A1071     -15.907 -37.173  26.033  1.00 30.84           O  
HETATM 7292  O   HOH A1072     -28.687 -67.796   5.071  1.00 22.82           O  
HETATM 7293  O   HOH A1073     -28.004 -78.004  15.534  1.00 36.93           O  
HETATM 7294  O   HOH A1074     -39.632 -31.319  -1.954  1.00 28.83           O  
HETATM 7295  O   HOH A1075     -31.667 -30.074 -15.942  1.00 42.74           O  
HETATM 7296  O   HOH A1076     -53.567 -41.640  12.941  1.00 54.88           O  
HETATM 7297  O   HOH A1077     -34.779 -84.206   4.217  1.00 27.90           O  
HETATM 7298  O   HOH A1078     -13.526 -60.216   9.924  1.00 37.06           O  
HETATM 7299  O   HOH A1079     -39.681 -43.005 -13.921  1.00 39.38           O  
HETATM 7300  O   HOH A1080     -42.373 -80.420  25.310  1.00 52.93           O  
HETATM 7301  O   HOH A1081     -31.343 -88.160  -0.109  1.00 43.61           O  
HETATM 7302  O   HOH A1082     -41.170 -82.919  20.924  1.00 44.76           O  
HETATM 7303  O   HOH A1083     -20.015 -48.770   5.528  1.00 26.57           O  
HETATM 7304  O   HOH A1084     -31.645 -39.049 -12.026  1.00 47.71           O  
HETATM 7305  O   HOH A1085      -6.641 -40.340  10.811  1.00 31.65           O  
HETATM 7306  O   HOH A1086     -50.567 -84.790  22.835  1.00 42.83           O  
HETATM 7307  O   HOH A1087     -70.331 -41.988  -8.705  1.00 47.26           O  
HETATM 7308  O   HOH A1088       4.035 -31.030   2.969  1.00 37.66           O  
HETATM 7309  O   HOH A1089     -35.456 -73.431  -7.076  1.00 24.94           O  
HETATM 7310  O   HOH A1090     -39.190 -76.628   8.332  1.00 25.47           O  
HETATM 7311  O   HOH A1091     -32.520 -71.703  17.325  1.00 24.30           O  
HETATM 7312  O   HOH A1092     -31.520 -31.981 -14.674  1.00 32.13           O  
HETATM 7313  O   HOH A1093     -37.599 -71.537   1.719  1.00 24.41           O  
HETATM 7314  O   HOH A1094     -34.224 -87.253   7.227  1.00 35.35           O  
HETATM 7315  O   HOH A1095     -41.370 -55.772   2.969  1.00 19.92           O  
HETATM 7316  O   HOH A1096     -34.967 -82.155  -6.410  1.00 40.97           O  
HETATM 7317  O   HOH A1097     -48.287 -58.134  -2.605  1.00 27.89           O  
HETATM 7318  O   HOH A1098     -50.616 -88.126  -0.919  1.00 42.67           O  
HETATM 7319  O   HOH A1099     -19.441 -75.429  -7.530  1.00 41.63           O  
HETATM 7320  O   HOH A1100     -45.114 -46.560 -14.811  1.00 47.84           O  
HETATM 7321  O   HOH A1101     -10.918  -3.762  11.902  1.00 43.42           O  
HETATM 7322  O   HOH A1102     -34.207 -83.531  17.100  1.00 30.04           O  
HETATM 7323  O   HOH A1103      -4.294 -28.911  14.906  1.00 29.11           O  
HETATM 7324  O   HOH A1104     -42.828 -79.976  20.991  1.00 40.54           O  
HETATM 7325  O   HOH A1105     -27.173 -50.729   4.536  1.00 37.84           O  
HETATM 7326  O   HOH A1106     -45.768 -31.983  -0.807  1.00 49.25           O  
HETATM 7327  O   HOH A1107     -33.312 -49.323  20.151  1.00 44.61           O  
HETATM 7328  O   HOH A1108     -33.696 -49.581   4.358  1.00 45.61           O  
HETATM 7329  O   HOH A1109     -28.161 -41.090  12.715  1.00 19.65           O  
HETATM 7330  O   HOH A1110     -29.782 -47.214  -4.420  1.00 43.25           O  
HETATM 7331  O   HOH A1111     -43.167 -41.716  -2.723  1.00 23.16           O  
HETATM 7332  O   HOH A1112     -39.673 -78.426  10.299  1.00 22.67           O  
HETATM 7333  O   HOH A1113     -43.139 -50.078  20.006  1.00 48.87           O  
HETATM 7334  O   HOH A1114     -53.474 -63.466  19.977  1.00 34.19           O  
HETATM 7335  O   HOH A1115     -10.598 -25.991  -8.787  1.00 42.39           O  
HETATM 7336  O   HOH A1116     -59.477 -69.728  15.967  1.00 38.61           O  
HETATM 7337  O   HOH A1117     -61.030 -67.589   6.731  1.00 59.47           O  
HETATM 7338  O   HOH A1118     -29.881 -58.896   3.514  1.00 22.32           O  
HETATM 7339  O   HOH A1119     -60.569 -44.931 -10.718  1.00 34.96           O  
HETATM 7340  O   HOH A1120     -49.193 -74.492  21.725  1.00 40.55           O  
HETATM 7341  O   HOH A1121      -3.093  -3.467  13.211  1.00 54.02           O  
HETATM 7342  O   HOH A1122      -8.439 -32.523  11.786  1.00 25.68           O  
HETATM 7343  O   HOH A1123     -39.380 -47.722  14.743  1.00 24.84           O  
HETATM 7344  O   HOH A1124     -13.742 -56.889   8.070  1.00 44.05           O  
HETATM 7345  O   HOH A1125     -30.573 -63.131  -9.948  1.00 59.45           O  
HETATM 7346  O   HOH A1126     -15.332 -22.357  -5.061  1.00 34.55           O  
HETATM 7347  O   HOH A1127     -28.044 -48.669  18.454  1.00 29.66           O  
HETATM 7348  O   HOH A1128     -18.919 -61.111   5.954  1.00 28.54           O  
HETATM 7349  O   HOH A1129     -41.295 -48.823  18.501  1.00 29.74           O  
HETATM 7350  O   HOH A1130     -12.095 -14.922   4.418  1.00 35.20           O  
HETATM 7351  O   HOH A1131     -21.339 -69.253   3.007  1.00 31.06           O  
HETATM 7352  O   HOH A1132     -51.928 -56.286  17.247  1.00 28.55           O  
HETATM 7353  O   HOH A1133     -48.559 -58.987  -5.342  1.00 20.05           O  
HETATM 7354  O   HOH A1134     -51.101 -42.309 -16.008  1.00 48.36           O  
HETATM 7355  O   HOH A1135     -31.961 -40.457  20.021  1.00 24.66           O  
HETATM 7356  O   HOH A1136      -0.462 -29.300  -2.218  1.00 22.78           O  
HETATM 7357  O   HOH A1137     -32.766 -50.780  12.646  1.00 26.78           O  
HETATM 7358  O   HOH A1138     -61.386 -75.801  12.110  1.00 42.58           O  
HETATM 7359  O   HOH A1139      -3.665 -30.670   4.624  1.00 29.76           O  
HETATM 7360  O   HOH A1140     -24.274 -53.623  18.998  1.00 35.15           O  
HETATM 7361  O   HOH A1141     -14.017 -14.465   6.991  1.00 33.51           O  
HETATM 7362  O   HOH A1142     -20.723 -39.521  -3.353  1.00 32.78           O  
HETATM 7363  O   HOH A1143     -31.856 -80.464  -4.994  1.00 45.44           O  
HETATM 7364  O   HOH A1144     -22.282 -34.961 -11.208  1.00 45.25           O  
HETATM 7365  O   HOH A1145     -66.766 -46.071  -5.919  1.00 48.19           O  
HETATM 7366  O   HOH A1146     -38.437 -62.961 -15.079  1.00 32.86           O  
HETATM 7367  O   HOH A1147     -20.302 -39.507  -0.259  1.00 35.52           O  
HETATM 7368  O   HOH A1148     -41.570 -57.158  20.606  1.00 27.78           O  
HETATM 7369  O   HOH A1149     -55.846 -42.163   5.659  1.00 31.57           O  
HETATM 7370  O   HOH A1150     -39.855 -66.464  13.030  1.00 30.56           O  
HETATM 7371  O   HOH A1151     -55.683 -75.690  -0.430  1.00 33.87           O  
HETATM 7372  O   HOH A1152     -11.609 -49.700  12.726  1.00 35.25           O  
HETATM 7373  O   HOH A1153     -33.730 -50.771  16.231  1.00 29.92           O  
HETATM 7374  O   HOH A1154     -14.721 -35.531  17.761  1.00 26.88           O  
HETATM 7375  O   HOH A1155     -45.228 -56.044  18.817  1.00 26.22           O  
HETATM 7376  O   HOH A1156     -13.188 -30.253  22.695  1.00 31.51           O  
HETATM 7377  O   HOH A1157     -57.676 -66.610  -0.009  1.00 31.42           O  
HETATM 7378  O   HOH A1158     -46.183 -84.092  14.502  1.00 27.19           O  
HETATM 7379  O   HOH A1159     -64.389 -47.717  -5.491  1.00 52.00           O  
HETATM 7380  O   HOH A1160     -25.394 -30.752 -12.916  1.00 37.71           O  
HETATM 7381  O   HOH A1161     -12.124 -15.859  13.026  1.00 41.66           O  
HETATM 7382  O   HOH A1162     -36.705 -74.643 -11.744  1.00 32.85           O  
HETATM 7383  O   HOH A1163     -47.260 -78.807  13.042  1.00 26.92           O  
HETATM 7384  O   HOH A1164     -30.283 -77.466  24.774  1.00 33.22           O  
HETATM 7385  O   HOH A1165     -37.936 -63.984 -12.715  1.00 30.98           O  
HETATM 7386  O   HOH A1166     -27.002 -44.472  15.289  1.00 24.69           O  
HETATM 7387  O   HOH A1167     -26.079 -65.608  30.328  1.00 46.39           O  
HETATM 7388  O   HOH A1168     -49.717 -42.082   4.336  1.00 32.54           O  
HETATM 7389  O   HOH A1169     -35.003 -68.377  33.816  1.00 35.60           O  
HETATM 7390  O   HOH A1170     -16.459 -67.770   6.026  1.00 46.36           O  
HETATM 7391  O   HOH A1171     -37.346 -57.968  18.656  1.00 37.80           O  
HETATM 7392  O   HOH A1172     -47.455 -60.453  -1.382  1.00 26.34           O  
HETATM 7393  O   HOH A1173     -20.068 -62.071  -4.640  1.00 42.53           O  
HETATM 7394  O   HOH A1174     -37.386 -51.488  20.203  1.00 30.47           O  
HETATM 7395  O   HOH A1175      -7.193 -41.053  -1.539  1.00 43.63           O  
HETATM 7396  O   HOH A1176     -23.025 -10.674   9.968  1.00 43.62           O  
HETATM 7397  O   HOH A1177       0.313 -30.727   4.733  1.00 42.74           O  
HETATM 7398  O   HOH A1178     -34.315 -51.289   6.347  1.00 24.63           O  
HETATM 7399  O   HOH A1179     -35.278 -48.791   1.857  1.00 26.33           O  
HETATM 7400  O   HOH A1180     -33.618 -42.211  21.699  1.00 30.42           O  
HETATM 7401  O   HOH A1181     -31.113 -78.981   0.962  1.00 26.25           O  
HETATM 7402  O   HOH A1182      -8.699 -23.861   1.789  1.00 29.06           O  
HETATM 7403  O   HOH A1183     -24.054 -50.183   8.777  1.00 31.80           O  
HETATM 7404  O   HOH A1184     -39.136 -40.110  22.686  1.00 51.37           O  
HETATM 7405  O   HOH A1185     -27.697 -71.520   8.115  1.00 27.22           O  
HETATM 7406  O   HOH A1186     -29.178 -82.604   1.317  1.00 38.92           O  
HETATM 7407  O   HOH A1187     -31.246 -57.448   1.027  1.00 23.41           O  
HETATM 7408  O   HOH A1188     -19.267 -47.155  15.550  1.00 46.07           O  
HETATM 7409  O   HOH A1189      -8.748 -30.661  -4.233  1.00 29.67           O  
HETATM 7410  O   HOH A1190     -44.022 -51.474   9.030  1.00 32.51           O  
HETATM 7411  O   HOH A1191     -53.712 -62.153 -10.079  1.00 30.16           O  
HETATM 7412  O   HOH A1192     -51.332 -51.906  -7.096  1.00 22.23           O  
HETATM 7413  O   HOH A1193     -54.801 -59.056  -8.010  1.00 36.50           O  
HETATM 7414  O   HOH A1194      -5.523  -8.287  -1.536  1.00 48.57           O  
HETATM 7415  O   HOH A1195     -19.976 -64.804  14.079  1.00 33.71           O  
HETATM 7416  O   HOH A1196     -40.647 -62.846 -11.965  1.00 24.82           O  
HETATM 7417  O   HOH A1197     -65.916 -73.456   7.547  1.00 54.30           O  
HETATM 7418  O   HOH A1198     -28.016 -64.225  -7.924  1.00 36.70           O  
HETATM 7419  O   HOH A1199     -17.154 -29.645  25.950  1.00 43.92           O  
HETATM 7420  O   HOH A1200     -63.670 -69.994   5.869  1.00 33.05           O  
HETATM 7421  O   HOH A1201     -53.876 -78.460  15.863  1.00 47.34           O  
HETATM 7422  O   HOH A1202      -5.626 -38.950   8.672  1.00 28.63           O  
HETATM 7423  O   HOH A1203     -51.879 -49.732  -8.529  1.00 27.76           O  
HETATM 7424  O   HOH A1204     -51.691 -51.375  -4.396  1.00 28.26           O  
HETATM 7425  O   HOH A1205     -34.267 -71.494 -12.106  1.00 24.56           O  
HETATM 7426  O   HOH A1206     -10.364 -18.111   3.903  1.00 29.68           O  
HETATM 7427  O   HOH A1207     -29.750 -46.973  -1.431  1.00 30.02           O  
HETATM 7428  O   HOH A1208     -46.117 -70.088  -8.719  1.00 29.98           O  
HETATM 7429  O   HOH A1209     -13.660 -27.769  22.325  1.00 35.61           O  
HETATM 7430  O   HOH A1210     -31.203 -61.781  -4.575  1.00 52.30           O  
HETATM 7431  O   HOH A1211     -41.514 -43.327  -4.052  1.00 23.87           O  
HETATM 7432  O   HOH A1212      -0.499 -28.062   8.332  1.00 43.95           O  
HETATM 7433  O   HOH A1213     -14.621 -23.847  -7.366  1.00 35.66           O  
HETATM 7434  O   HOH A1214     -47.901 -55.120   0.388  1.00 27.62           O  
HETATM 7435  O   HOH A1215     -15.106 -64.538   0.602  1.00 33.71           O  
HETATM 7436  O   HOH A1216     -15.177 -54.025  11.001  1.00 37.79           O  
HETATM 7437  O   HOH A1217     -40.136 -81.057   9.591  1.00 22.39           O  
HETATM 7438  O   HOH A1218     -42.749 -49.638   6.255  1.00 22.79           O  
HETATM 7439  O   HOH A1219     -22.749 -31.198  30.925  1.00 47.44           O  
HETATM 7440  O   HOH A1220     -37.368 -52.492  -6.901  1.00 42.77           O  
HETATM 7441  O   HOH A1221     -64.721 -78.035   5.206  1.00 39.36           O  
HETATM 7442  O   HOH A1222     -12.157 -32.149 -11.343  1.00 45.23           O  
HETATM 7443  O   HOH A1223     -29.437 -63.676  -5.082  1.00 41.25           O  
HETATM 7444  O   HOH A1224     -41.160 -51.879   9.109  1.00 34.74           O  
HETATM 7445  O   HOH A1225     -46.921 -54.618   8.719  1.00 34.41           O  
HETATM 7446  O   HOH A1226      -5.579 -19.827   7.478  1.00 41.51           O  
HETATM 7447  O   HOH A1227     -20.655 -69.185  -2.615  1.00 28.07           O  
HETATM 7448  O   HOH A1228     -53.399 -38.466 -14.089  1.00 38.00           O  
HETATM 7449  O   HOH A1229     -25.218 -70.581  17.352  1.00 40.21           O  
HETATM 7450  O   HOH A1230     -37.125 -74.692  24.393  1.00 37.07           O  
HETATM 7451  O   HOH A1231     -42.969 -32.973  -3.339  1.00 29.49           O  
HETATM 7452  O   HOH A1232     -59.013 -34.303 -13.765  1.00 53.45           O  
HETATM 7453  O   HOH A1233     -45.337 -48.885  19.319  1.00 40.60           O  
HETATM 7454  O   HOH A1234     -45.745 -54.727   4.713  1.00 31.20           O  
HETATM 7455  O   HOH A1235     -48.865 -58.067   5.393  1.00 34.23           O  
HETATM 7456  O   HOH A1236      -4.153 -33.379   5.494  1.00 35.34           O  
HETATM 7457  O   HOH A1237     -12.830 -20.129   0.593  1.00 35.96           O  
HETATM 7458  O   HOH A1238     -24.123 -47.058  13.994  1.00 23.56           O  
HETATM 7459  O   HOH A1239     -26.985 -50.990  18.654  1.00 31.31           O  
HETATM 7460  O   HOH A1240     -51.981 -70.827  -5.499  1.00 35.20           O  
HETATM 7461  O   HOH A1241     -35.955 -48.276  23.579  1.00 45.01           O  
HETATM 7462  O   HOH A1242     -27.485 -79.232  -2.663  1.00 36.28           O  
HETATM 7463  O   HOH A1243     -42.987 -67.894  24.258  1.00 48.41           O  
HETATM 7464  O   HOH A1244     -26.377 -68.151  14.242  1.00 28.75           O  
HETATM 7465  O   HOH A1245     -25.666 -81.039   1.410  1.00 51.32           O  
HETATM 7466  O   HOH A1246      -2.897 -28.319   6.104  1.00 35.87           O  
HETATM 7467  O   HOH A1247     -45.224 -50.931   6.442  1.00 23.81           O  
HETATM 7468  O   HOH A1248     -17.544 -52.492  11.155  1.00 30.19           O  
HETATM 7469  O   HOH A1249     -52.059 -55.027  10.577  1.00 59.13           O  
HETATM 7470  O   HOH A1250     -35.824 -85.837  -5.206  1.00 50.80           O  
HETATM 7471  O   HOH A1251     -29.412 -38.133   5.096  1.00 27.17           O  
HETATM 7472  O   HOH A1252     -48.550 -64.823 -18.981  1.00 40.57           O  
HETATM 7473  O   HOH A1253      -5.838 -15.815  -1.577  1.00 48.98           O  
HETATM 7474  O   HOH A1254     -53.038 -43.177  11.070  1.00 50.04           O  
HETATM 7475  O   HOH A1255     -34.980 -47.272   5.694  1.00 30.41           O  
HETATM 7476  O   HOH A1256     -19.928 -13.952  15.023  1.00 46.09           O  
HETATM 7477  O   HOH A1257     -31.461 -80.624  -0.893  1.00 32.12           O  
HETATM 7478  O   HOH A1258      -5.756  -4.644  -1.252  1.00 51.90           O  
HETATM 7479  O   HOH A1259     -44.400 -39.199  17.577  1.00 34.25           O  
HETATM 7480  O   HOH A1260     -24.566 -62.402  15.748  1.00 52.32           O  
HETATM 7481  O   HOH A1261      -8.757 -39.437  17.912  1.00 31.60           O  
HETATM 7482  O   HOH A1262     -13.307 -55.847  11.840  1.00 49.00           O  
HETATM 7483  O   HOH A1263     -49.664 -62.325  -2.237  1.00 32.26           O  
HETATM 7484  O   HOH A1264     -34.734 -58.756  19.059  1.00 44.61           O  
HETATM 7485  O   HOH A1265      -5.894 -17.578   6.975  1.00 49.76           O  
HETATM 7486  O   HOH A1266     -38.853 -54.526   2.940  1.00 20.26           O  
HETATM 7487  O   HOH A1267     -24.597 -56.515  19.211  1.00 46.95           O  
HETATM 7488  O   HOH A1268     -10.657 -20.597   1.179  1.00 43.69           O  
HETATM 7489  O   HOH A1269     -35.758 -52.769  18.473  1.00 49.55           O  
HETATM 7490  O   HOH A1270     -49.510 -48.870  -9.588  1.00 24.68           O  
HETATM 7491  O   HOH A1271     -33.601 -56.628  17.720  1.00 51.36           O  
HETATM 7492  O   HOH A1272     -52.036 -37.161 -15.712  1.00 52.48           O  
HETATM 7493  O   HOH A1273     -21.636 -48.053  14.701  1.00 29.37           O  
HETATM 7494  O   HOH A1274     -54.203 -52.010  -3.655  1.00 49.69           O  
HETATM 7495  O   HOH A1275     -27.452 -67.818  11.350  1.00 38.23           O  
HETATM 7496  O   HOH A1276     -58.061 -77.084  15.130  1.00 39.32           O  
HETATM 7497  O   HOH A1277     -53.298 -58.570 -13.686  1.00 36.29           O  
HETATM 7498  O   HOH A1278     -57.574 -67.328   8.590  1.00 41.47           O  
HETATM 7499  O   HOH A1279     -37.939 -23.085  -8.891  1.00 44.99           O  
HETATM 7500  O   HOH A1280     -52.623 -37.269  10.028  1.00 43.17           O  
HETATM 7501  O   HOH A1281     -23.686 -51.348   1.439  1.00 38.77           O  
HETATM 7502  O   HOH A1282     -54.442 -85.739  17.306  1.00 40.19           O  
HETATM 7503  O   HOH A1283     -62.626 -46.399 -11.225  1.00 45.53           O  
HETATM 7504  O   HOH A1284     -50.978 -57.551  -2.878  1.00 23.39           O  
HETATM 7505  O   HOH A1285     -56.091 -79.871   4.616  1.00 31.06           O  
HETATM 7506  O   HOH A1286       1.204 -25.036  -0.730  1.00 39.41           O  
HETATM 7507  O   HOH A1287     -52.762 -51.788   0.923  1.00 29.68           O  
HETATM 7508  O   HOH A1288     -27.605 -39.575  27.355  1.00 33.46           O  
HETATM 7509  O   HOH A1289     -15.307 -56.781  16.397  1.00 26.59           O  
HETATM 7510  O   HOH A1290     -38.661 -63.378  27.376  1.00 43.68           O  
HETATM 7511  O   HOH A1291     -35.256 -25.430  -1.314  1.00 40.30           O  
HETATM 7512  O   HOH A1292     -51.486 -61.335   6.743  1.00 44.67           O  
HETATM 7513  O   HOH A1293     -37.961 -54.465  11.684  1.00 20.13           O  
HETATM 7514  O   HOH A1294     -53.519 -84.156   3.849  1.00 37.45           O  
HETATM 7515  O   HOH A1295     -55.045 -61.577  -6.725  1.00 33.57           O  
HETATM 7516  O   HOH A1296     -12.355 -49.751   6.475  1.00 42.60           O  
HETATM 7517  O   HOH A1297      -9.300 -38.481   8.316  1.00 25.94           O  
HETATM 7518  O   HOH A1298     -53.454 -55.744  -9.282  1.00 27.19           O  
HETATM 7519  O   HOH A1299     -26.059 -59.906  -2.291  1.00 38.70           O  
HETATM 7520  O   HOH A1300     -17.573 -67.944   8.513  1.00 42.71           O  
HETATM 7521  O   HOH A1301     -40.912 -88.855  -3.708  1.00 42.14           O  
HETATM 7522  O   HOH A1302     -67.145 -75.396   5.475  1.00 30.47           O  
HETATM 7523  O   HOH A1303     -27.510 -79.923  -0.235  1.00 56.87           O  
HETATM 7524  O   HOH A1304      -2.318 -27.336  17.781  1.00 45.38           O  
HETATM 7525  O   HOH A1305      -9.700 -18.288  12.439  1.00 41.67           O  
HETATM 7526  O   HOH A1306     -30.877 -51.534  15.833  1.00 35.22           O  
HETATM 7527  O   HOH A1307     -34.274 -84.705  14.717  1.00 27.90           O  
HETATM 7528  O   HOH A1308     -46.532 -25.183 -14.213  1.00 42.89           O  
HETATM 7529  O   HOH A1309     -22.055 -74.874  -4.688  1.00 30.83           O  
HETATM 7530  O   HOH A1310     -37.921 -45.071 -13.411  1.00 45.89           O  
HETATM 7531  O   HOH A1311     -22.284 -51.234   4.629  1.00 78.80           O  
HETATM 7532  O   HOH A1312     -40.821 -60.146 -12.121  1.00 27.10           O  
HETATM 7533  O   HOH A1313     -50.057 -52.866  20.061  1.00 46.17           O  
HETATM 7534  O   HOH A1314     -44.326 -24.553 -12.425  1.00 39.77           O  
HETATM 7535  O   HOH A1315     -43.746 -82.289  21.515  1.00 33.04           O  
HETATM 7536  O   HOH A1316     -18.978 -43.263  26.815  1.00 40.96           O  
HETATM 7537  O   HOH A1317     -11.146 -34.473  -8.943  1.00 38.77           O  
HETATM 7538  O   HOH A1318     -42.779 -88.892  11.518  1.00 29.75           O  
HETATM 7539  O   HOH A1319     -26.199 -49.154   7.103  1.00 24.08           O  
HETATM 7540  O   HOH A1320     -14.775 -59.910  16.982  1.00 37.65           O  
HETATM 7541  O   HOH A1321     -32.730 -82.083  24.385  1.00 40.51           O  
HETATM 7542  O   HOH A1322       0.842 -38.930   5.302  1.00 36.86           O  
HETATM 7543  O   HOH A1323     -30.451 -21.594   6.394  1.00 49.27           O  
HETATM 7544  O   HOH A1324     -27.084 -41.497  -9.802  1.00 30.59           O  
HETATM 7545  O   HOH A1325     -23.547 -16.156   1.751  1.00 66.56           O  
HETATM 7546  O   HOH A1326     -12.207 -29.026  25.158  1.00 32.14           O  
HETATM 7547  O   HOH A1327     -59.040 -84.130  13.224  1.00 62.27           O  
HETATM 7548  O   HOH A1328     -35.392 -72.654  27.269  1.00 46.21           O  
HETATM 7549  O   HOH A1329     -53.083 -31.007  -2.207  1.00 46.99           O  
HETATM 7550  O   HOH A1330      -7.222 -37.632   6.943  1.00 29.31           O  
HETATM 7551  O   HOH A1331     -42.544 -64.292  19.376  1.00 49.46           O  
HETATM 7552  O   HOH A1332     -33.035 -46.609   6.894  1.00 33.19           O  
HETATM 7553  O   HOH A1333     -32.023 -55.313  19.248  1.00 49.52           O  
HETATM 7554  O   HOH A1334     -36.682 -45.109  24.027  1.00 50.24           O  
HETATM 7555  O   HOH A1335     -36.627 -45.284   5.914  1.00 33.71           O  
HETATM 7556  O   HOH A1336     -25.084 -69.171  19.882  1.00 49.88           O  
HETATM 7557  O   HOH A1337     -27.109 -53.044  -3.212  1.00 34.34           O  
HETATM 7558  O   HOH A1338     -25.765 -66.568  25.020  1.00 35.14           O  
HETATM 7559  O   HOH A1339     -23.806 -58.699   1.054  1.00 30.08           O  
HETATM 7560  O   HOH A1340      -6.309 -45.023   8.532  1.00 27.50           O  
HETATM 7561  O   HOH A1341     -53.381 -87.593  11.163  1.00 33.58           O  
HETATM 7562  O   HOH A1342      -0.655 -30.673   7.393  1.00 40.25           O  
HETATM 7563  O   HOH A1343     -37.494 -59.857  20.765  1.00 54.77           O  
HETATM 7564  O   HOH A1344     -43.917 -62.808  16.874  1.00 34.76           O  
HETATM 7565  O   HOH A1345     -28.332 -76.843  23.143  1.00 47.20           O  
HETATM 7566  O   HOH A1346     -29.201 -48.233  20.697  1.00 34.50           O  
HETATM 7567  O   HOH A1347     -32.577 -42.762  -9.780  1.00 31.17           O  
HETATM 7568  O   HOH A1348     -55.018 -75.802  16.919  1.00 34.02           O  
HETATM 7569  O   HOH A1349      -7.812 -14.684  -0.107  1.00 52.66           O  
HETATM 7570  O   HOH A1350      -3.585 -45.851   7.332  1.00 55.64           O  
HETATM 7571  O   HOH A1351     -41.542 -36.410 -19.721  1.00 41.14           O  
HETATM 7572  O   HOH A1352     -36.882 -34.578 -17.595  1.00 51.44           O  
HETATM 7573  O   HOH A1353     -44.480 -49.937  -5.601  1.00 44.82           O  
HETATM 7574  O   HOH A1354       2.016 -28.562   2.002  1.00 45.95           O  
HETATM 7575  O   HOH A1355      -6.538 -40.906  16.496  1.00 50.45           O  
HETATM 7576  O   HOH A1356     -51.218 -45.697  13.732  1.00 29.29           O  
HETATM 7577  O   HOH A1357     -16.416 -10.530   0.895  1.00 42.31           O  
HETATM 7578  O   HOH A1358      -3.205 -31.736   7.763  1.00 41.84           O  
HETATM 7579  O   HOH A1359      -4.539 -36.938  -3.300  1.00 40.43           O  
HETATM 7580  O   HOH A1360     -21.240 -25.446 -15.859  1.00 59.56           O  
HETATM 7581  O   HOH A1361      -8.342 -35.692  -5.393  1.00 52.07           O  
HETATM 7582  O   HOH A1362     -27.730 -76.591  17.752  1.00 33.93           O  
HETATM 7583  O   HOH A1363     -24.815 -73.715  16.884  1.00 28.02           O  
HETATM 7584  O   HOH A1364     -24.946 -50.705   4.949  1.00 60.88           O  
HETATM 7585  O   HOH A1365     -26.896 -40.103  -6.996  1.00 30.27           O  
HETATM 7586  O   HOH A1366     -16.357 -16.394   6.904  1.00 46.88           O  
HETATM 7587  O   HOH A1367     -26.592 -51.422   1.902  1.00 28.36           O  
HETATM 7588  O   HOH A1368     -56.993 -75.692   2.239  1.00 30.02           O  
HETATM 7589  O   HOH A1369     -59.078 -65.404  13.288  1.00 36.12           O  
HETATM 7590  O   HOH A1370     -55.337 -31.061  -0.200  1.00 48.07           O  
HETATM 7591  O   HOH A1371     -13.449 -49.988   4.358  1.00 42.38           O  
HETATM 7592  O   HOH A1372     -22.777 -58.701  -1.487  1.00 58.40           O  
HETATM 7593  O   HOH A1373     -44.647 -80.019  -9.304  1.00 31.70           O  
HETATM 7594  O   HOH A1374     -62.873 -39.442 -12.352  1.00 48.30           O  
HETATM 7595  O   HOH A1375     -54.772 -28.936  -3.524  1.00 56.77           O  
HETATM 7596  O   HOH A1376     -16.667 -74.400  -7.050  1.00 48.47           O  
HETATM 7597  O   HOH A1377       2.575 -22.689   4.148  1.00 54.30           O  
HETATM 7598  O   HOH A1378     -53.587 -64.175  -7.443  1.00 17.95           O  
HETATM 7599  O   HOH A1379     -55.546 -41.672   8.462  1.00 39.78           O  
HETATM 7600  O   HOH A1380     -48.851 -49.275 -12.281  1.00 41.83           O  
HETATM 7601  O   HOH A1381     -39.011 -76.558  27.415  1.00 58.17           O  
HETATM 7602  O   HOH A1382      -9.808 -22.347  -0.683  1.00 42.29           O  
HETATM 7603  O   HOH A1383     -43.872 -71.536 -10.190  1.00 24.52           O  
HETATM 7604  O   HOH A1384     -22.625 -75.094  -1.658  1.00 31.77           O  
HETATM 7605  O   HOH A1385     -41.488 -34.860  23.160  1.00 56.12           O  
HETATM 7606  O   HOH A1386     -20.671 -69.446  -9.911  1.00 55.50           O  
HETATM 7607  O   HOH A1387     -63.005 -41.558 -12.674  1.00 59.32           O  
HETATM 7608  O   HOH A1388     -53.436 -55.065  15.621  1.00 36.65           O  
HETATM 7609  O   HOH A1389     -35.299 -55.587  18.679  1.00 42.16           O  
HETATM 7610  O   HOH A1390     -53.191 -72.768  -3.771  1.00 43.30           O  
HETATM 7611  O   HOH A1391     -53.558 -78.157  18.841  1.00 61.91           O  
HETATM 7612  O   HOH A1392     -54.347 -58.031 -11.271  1.00 40.35           O  
HETATM 7613  O   HOH A1393     -13.070 -38.476  22.518  1.00 53.00           O  
HETATM 7614  O   HOH A1394     -10.697 -41.690  -3.533  1.00 50.04           O  
HETATM 7615  O   HOH A1395     -27.597 -53.110  18.222  1.00 57.30           O  
HETATM 7616  O   HOH A1396     -38.067 -77.106  24.983  1.00 48.92           O  
HETATM 7617  O   HOH A1397     -30.745 -42.211 -11.465  1.00 52.82           O  
HETATM 7618  O   HOH A1398     -41.502 -65.121  14.752  1.00 32.16           O  
HETATM 7619  O   HOH A1399     -11.987 -23.840  -8.123  1.00 44.33           O  
HETATM 7620  O   HOH A1400     -49.388 -71.996  -6.226  1.00 47.79           O  
HETATM 7621  O   HOH A1401     -27.317 -47.608  22.412  1.00 52.03           O  
HETATM 7622  O   HOH A1402     -39.999 -53.741   9.739  1.00 40.49           O  
HETATM 7623  O   HOH A1403     -56.984 -78.184   2.780  1.00 37.44           O  
HETATM 7624  O   HOH A1404      -7.620 -33.501  -3.858  1.00 32.86           O  
HETATM 7625  O   HOH A1405     -66.407 -71.433   6.316  1.00 61.49           O  
HETATM 7626  O   HOH A1406     -35.455 -26.823   2.347  1.00 54.98           O  
HETATM 7627  O   HOH A1407     -76.541 -43.783 -20.059  1.00 65.20           O  
HETATM 7628  O   HOH A1408     -32.884 -63.870 -15.056  1.00 50.99           O  
HETATM 7629  O   HOH A1409     -54.693 -66.917  -6.461  1.00 44.32           O  
HETATM 7630  O   HOH A1410     -25.787 -61.407  -4.275  1.00 59.25           O  
HETATM 7631  O   HOH A1411      -9.920 -42.629  -0.963  1.00 45.27           O  
HETATM 7632  O   HOH A1412       3.642 -44.611  11.094  1.00 53.69           O  
HETATM 7633  O   HOH A1413     -13.718 -38.388  24.772  1.00 46.48           O  
HETATM 7634  O   HOH A1414     -59.652 -82.122   1.378  1.00 46.71           O  
HETATM 7635  O   HOH A1415     -49.659 -34.251 -17.670  1.00 68.60           O  
HETATM 7636  O   HOH A1416     -29.855 -80.713  -2.973  1.00 58.14           O  
HETATM 7637  O   HOH A1417     -22.031 -50.349   6.765  1.00 37.38           O  
HETATM 7638  O   HOH A1418     -35.121 -41.688  23.798  1.00 47.56           O  
HETATM 7639  O   HOH A1419     -16.347 -54.522   7.863  1.00 53.82           O  
HETATM 7640  O   HOH A1420     -21.901 -63.937  -5.198  1.00 36.61           O  
HETATM 7641  O   HOH A1421     -56.832 -66.414  -4.541  1.00 51.32           O  
HETATM 7642  O   HOH A1422     -50.032 -56.537   7.740  1.00 57.25           O  
HETATM 7643  O   HOH A1423     -46.408 -39.795  18.822  1.00 58.47           O  
HETATM 7644  O   HOH A1424     -17.887 -39.982  -3.549  1.00 42.77           O  
HETATM 7645  O   HOH A1425     -50.202 -39.791 -16.951  1.00 48.72           O  
HETATM 7646  O   HOH A1426     -67.304 -78.142   5.535  1.00 37.80           O  
HETATM 7647  O   HOH A1427     -48.300 -71.435  -8.444  1.00 42.29           O  
HETATM 7648  O   HOH A1428     -53.986 -69.787  -7.220  1.00 52.70           O  
HETATM 7649  O   HOH A1429     -13.178 -36.668  -8.867  1.00 54.81           O  
HETATM 7650  O   HOH A1430     -55.517 -52.546   0.966  1.00 42.58           O  
HETATM 7651  O   HOH A1431     -31.887 -85.103  17.799  1.00 42.60           O  
HETATM 7652  O   HOH A1432     -42.413 -70.629  27.647  1.00 58.34           O  
HETATM 7653  O   HOH A1433     -10.067 -44.800  -2.047  1.00 58.54           O  
HETATM 7654  O   HOH A1434     -39.977 -88.256  -6.216  1.00 44.55           O  
HETATM 7655  O   HOH A1435     -30.603 -61.194  -8.197  1.00 52.93           O  
HETATM 7656  O   HOH A1436     -25.692 -62.899  -7.844  1.00 46.08           O  
HETATM 7657  O   HOH A1437     -39.032 -56.829  20.482  1.00 45.25           O  
HETATM 7658  O   HOH A1438     -52.085 -54.780  19.578  1.00 40.07           O  
HETATM 7659  O   HOH A1439     -58.870 -58.550   2.001  1.00 52.78           O  
HETATM 7660  O   HOH A1440      -8.592 -24.054  -5.009  1.00 38.70           O  
HETATM 7661  O   HOH A1441     -21.658 -52.987   0.354  1.00 53.09           O  
HETATM 7662  O   HOH B2201     -52.794 -17.406 -13.345  1.00 48.58           O  
HETATM 7663  O   HOH B2202     -43.159 -29.736  -1.113  1.00 42.31           O  
HETATM 7664  O   HOH B2203     -33.881 -23.529  -0.123  1.00 51.58           O  
HETATM 7665  O   HOH B2204     -47.647 -24.281  -4.586  1.00 40.86           O  
HETATM 7666  O   HOH B2205     -38.673 -24.535  -7.012  1.00 30.66           O  
HETATM 7667  O   HOH B2206     -37.139 -28.859  -0.288  1.00 27.92           O  
HETATM 7668  O   HOH B2207     -52.118 -17.280 -10.346  1.00 45.30           O  
HETATM 7669  O   HOH B2208     -47.561 -28.686  -1.140  1.00 51.72           O  
HETATM 7670  O   HOH B2209     -53.837 -28.556 -16.049  1.00 53.45           O  
HETATM 7671  O   HOH B2210     -53.065 -24.309  -5.175  1.00 49.40           O  
HETATM 7672  O   HOH B2211     -50.209 -28.663 -15.048  1.00 59.16           O  
HETATM 7673  O   HOH B2212     -44.537 -26.439  -2.479  1.00 42.28           O  
HETATM 7674  O   HOH B2213     -53.891 -20.381 -11.004  1.00 44.19           O  
HETATM 7675  O   HOH B2214     -56.346 -18.795  -9.327  1.00 52.69           O  
HETATM 7676  O   HOH B2215     -54.923 -20.015  -7.530  1.00 43.28           O  
HETATM 7677  O   HOH B2216     -45.254 -23.983  -1.383  1.00 45.37           O  
HETATM 7678  O   HOH B2217     -50.814 -25.766  -4.494  1.00 49.84           O  
HETATM 7679  O   HOH B2218     -54.559 -17.424 -11.548  1.00 42.99           O  
CONECT   44  135                                                                
CONECT   70  272                                                                
CONECT  118  216                                                                
CONECT  135   44                                                                
CONECT  165  210                                                                
CONECT  210  165                                                                
CONECT  216  118                                                                
CONECT  272   70                                                                
CONECT  345  466                                                                
CONECT  382  600                                                                
CONECT  450  544                                                                
CONECT  466  345                                                                
CONECT  495  538                                                                
CONECT  538  495                                                                
CONECT  544  450                                                                
CONECT  600  382                                                                
CONECT  689 1047                                                                
CONECT  755 2320                                                                
CONECT  869 7154                                                                
CONECT 1047  689                                                                
CONECT 1166 7154                                                                
CONECT 2009 7155                                                                
CONECT 2010 7155                                                                
CONECT 2041 7155                                                                
CONECT 2320  755                                                                
CONECT 2380 7154                                                                
CONECT 2390 7154                                                                
CONECT 2439 3263                                                                
CONECT 2773 7104                                                                
CONECT 2794 5813                                                                
CONECT 3263 2439                                                                
CONECT 3316 7155                                                                
CONECT 3714 7021                                                                
CONECT 4041 4677                                                                
CONECT 4054 4562                                                                
CONECT 4562 4054                                                                
CONECT 4677 4041                                                                
CONECT 4694 7159                                                                
CONECT 4723 7159                                                                
CONECT 4749 7159                                                                
CONECT 5273 7156                                                                
CONECT 5293 7156                                                                
CONECT 5313 7156                                                                
CONECT 5322 7156                                                                
CONECT 5549 5627                                                                
CONECT 5627 5549                                                                
CONECT 5780 7157                                                                
CONECT 5805 7157                                                                
CONECT 5813 2794                                                                
CONECT 5827 7157                                                                
CONECT 6415 6446                                                                
CONECT 6428 6429 6433 6436                                                      
CONECT 6429 6428 6430 6434                                                      
CONECT 6430 6429 6431                                                           
CONECT 6431 6430 6432 6435                                                      
CONECT 6432 6431 6433                                                           
CONECT 6433 6428 6432                                                           
CONECT 6434 6429                                                                
CONECT 6435 6431                                                                
CONECT 6436 6428 6437 6442                                                      
CONECT 6437 6436 6438 6440                                                      
CONECT 6438 6437 6439                                                           
CONECT 6439 6438                                                                
CONECT 6440 6437 6441 6443                                                      
CONECT 6441 6440 6442 6444                                                      
CONECT 6442 6436 6441                                                           
CONECT 6443 6440 6449                                                           
CONECT 6444 6441 6445                                                           
CONECT 6445 6444 6446                                                           
CONECT 6446 6415 6445 6447 6448                                                 
CONECT 6447 6446                                                                
CONECT 6448 6446                                                                
CONECT 6449 6443                                                                
CONECT 6457 6471                                                                
CONECT 6471 6457 6472 6473 6474                                                 
CONECT 6472 6471                                                                
CONECT 6473 6471                                                                
CONECT 6474 6471 6475                                                           
CONECT 6475 6474 6476                                                           
CONECT 6476 6475 6477 6478                                                      
CONECT 6477 6476 6483                                                           
CONECT 6478 6476 6479 6480                                                      
CONECT 6479 6478 6495                                                           
CONECT 6480 6478 6481 6483                                                      
CONECT 6481 6480 6482                                                           
CONECT 6482 6481                                                                
CONECT 6483 6477 6480 6484                                                      
CONECT 6484 6483 6485 6494                                                      
CONECT 6485 6484 6486                                                           
CONECT 6486 6485 6487                                                           
CONECT 6487 6486 6488 6494                                                      
CONECT 6488 6487 6489 6490                                                      
CONECT 6489 6488 7220                                                           
CONECT 6490 6488 6491                                                           
CONECT 6491 6490 6492 6493                                                      
CONECT 6492 6491                                                                
CONECT 6493 6491 6494                                                           
CONECT 6494 6484 6487 6493                                                      
CONECT 6495 6479                                                                
CONECT 6564 6575                                                                
CONECT 6575 6564 6576 6577 6597                                                 
CONECT 6576 6575                                                                
CONECT 6577 6575 6578                                                           
CONECT 6578 6577 6579                                                           
CONECT 6579 6578 6580 6581                                                      
CONECT 6580 6579 6585                                                           
CONECT 6581 6579 6582 6583                                                      
CONECT 6582 6581 6598                                                           
CONECT 6583 6581 6584 6585                                                      
CONECT 6584 6583 6586                                                           
CONECT 6585 6580 6583 6587                                                      
CONECT 6586 6584                                                                
CONECT 6587 6585 6588 6596                                                      
CONECT 6588 6587 6589                                                           
CONECT 6589 6588 6590                                                           
CONECT 6590 6589 6591 6596                                                      
CONECT 6591 6590 6592 6593                                                      
CONECT 6592 6591                                                                
CONECT 6593 6591 6594                                                           
CONECT 6594 6593 6595                                                           
CONECT 6595 6594 6596                                                           
CONECT 6596 6587 6590 6595                                                      
CONECT 6597 6575                                                                
CONECT 6598 6582 6599 6600 6601                                                 
CONECT 6599 6598                                                                
CONECT 6600 6598                                                                
CONECT 6601 6598 6602                                                           
CONECT 6602 6601 6603                                                           
CONECT 6603 6602 6604 6605                                                      
CONECT 6604 6603 6610                                                           
CONECT 6605 6603 6606 6607                                                      
CONECT 6606 6605 6622                                                           
CONECT 6607 6605 6608 6610                                                      
CONECT 6608 6607 6609                                                           
CONECT 6609 6608                                                                
CONECT 6610 6604 6607 6611                                                      
CONECT 6611 6610 6612 6621                                                      
CONECT 6612 6611 6613                                                           
CONECT 6613 6612 6614                                                           
CONECT 6614 6613 6615 6621                                                      
CONECT 6615 6614 6616 6617                                                      
CONECT 6616 6615                                                                
CONECT 6617 6615 6618                                                           
CONECT 6618 6617 6619 6620                                                      
CONECT 6619 6618                                                                
CONECT 6620 6618 6621                                                           
CONECT 6621 6611 6614 6620                                                      
CONECT 6622 6606                                                                
CONECT 6672 6684                                                                
CONECT 6684 6672 6685 6686 6706                                                 
CONECT 6685 6684                                                                
CONECT 6686 6684 6687                                                           
CONECT 6687 6686 6688                                                           
CONECT 6688 6687 6689 6690                                                      
CONECT 6689 6688 6694                                                           
CONECT 6690 6688 6691 6692                                                      
CONECT 6691 6690 6725                                                           
CONECT 6692 6690 6693 6694                                                      
CONECT 6693 6692 6695                                                           
CONECT 6694 6689 6692 6696                                                      
CONECT 6695 6693                                                                
CONECT 6696 6694 6697 6705                                                      
CONECT 6697 6696 6698                                                           
CONECT 6698 6697 6699                                                           
CONECT 6699 6698 6700 6705                                                      
CONECT 6700 6699 6701 6702                                                      
CONECT 6701 6700                                                                
CONECT 6702 6700 6703                                                           
CONECT 6703 6702 6704                                                           
CONECT 6704 6703 6705                                                           
CONECT 6705 6696 6699 6704                                                      
CONECT 6706 6684                                                                
CONECT 6707 6708 6712 6715                                                      
CONECT 6708 6707 6709 6713                                                      
CONECT 6709 6708 6710                                                           
CONECT 6710 6709 6711 6714                                                      
CONECT 6711 6710 6712                                                           
CONECT 6712 6707 6711                                                           
CONECT 6713 6708                                                                
CONECT 6714 6710                                                                
CONECT 6715 6707 6716 6721                                                      
CONECT 6716 6715 6717 6719                                                      
CONECT 6717 6716 6718                                                           
CONECT 6718 6717                                                                
CONECT 6719 6716 6720 6722                                                      
CONECT 6720 6719 6721 6723                                                      
CONECT 6721 6715 6720                                                           
CONECT 6722 6719 6728                                                           
CONECT 6723 6720 6724                                                           
CONECT 6724 6723 6725                                                           
CONECT 6725 6691 6724 6726 6727                                                 
CONECT 6726 6725                                                                
CONECT 6727 6725                                                                
CONECT 6728 6722                                                                
CONECT 6810 7220                                                                
CONECT 6938 6949                                                                
CONECT 6949 6938 6950 6951 6971                                                 
CONECT 6950 6949                                                                
CONECT 6951 6949 6952                                                           
CONECT 6952 6951 6953                                                           
CONECT 6953 6952 6954 6955                                                      
CONECT 6954 6953 6959                                                           
CONECT 6955 6953 6956 6957                                                      
CONECT 6956 6955 6972                                                           
CONECT 6957 6955 6958 6959                                                      
CONECT 6958 6957 6960                                                           
CONECT 6959 6954 6957 6961                                                      
CONECT 6960 6958                                                                
CONECT 6961 6959 6962 6970                                                      
CONECT 6962 6961 6963                                                           
CONECT 6963 6962 6964                                                           
CONECT 6964 6963 6965 6970                                                      
CONECT 6965 6964 6966 6967                                                      
CONECT 6966 6965                                                                
CONECT 6967 6965 6968                                                           
CONECT 6968 6967 6969                                                           
CONECT 6969 6968 6970                                                           
CONECT 6970 6961 6964 6969                                                      
CONECT 6971 6949                                                                
CONECT 6972 6956 6973 6974 6975                                                 
CONECT 6973 6972                                                                
CONECT 6974 6972                                                                
CONECT 6975 6972 6976                                                           
CONECT 6976 6975 6977                                                           
CONECT 6977 6976 6978 6979                                                      
CONECT 6978 6977 6984                                                           
CONECT 6979 6977 6980 6981                                                      
CONECT 6980 6979 6996                                                           
CONECT 6981 6979 6982 6984                                                      
CONECT 6982 6981 6983                                                           
CONECT 6983 6982                                                                
CONECT 6984 6978 6981 6985                                                      
CONECT 6985 6984 6986 6995                                                      
CONECT 6986 6985 6987                                                           
CONECT 6987 6986 6988                                                           
CONECT 6988 6987 6989 6995                                                      
CONECT 6989 6988 6990 6991                                                      
CONECT 6990 6989                                                                
CONECT 6991 6989 6992                                                           
CONECT 6992 6991 6993 6994                                                      
CONECT 6993 6992                                                                
CONECT 6994 6992 6995                                                           
CONECT 6995 6985 6988 6994                                                      
CONECT 6996 6980 6997 6998 6999                                                 
CONECT 6997 6996                                                                
CONECT 6998 6996                                                                
CONECT 6999 6996 7000                                                           
CONECT 7000 6999 7001                                                           
CONECT 7001 7000 7002 7003                                                      
CONECT 7002 7001 7008                                                           
CONECT 7003 7001 7004 7005                                                      
CONECT 7004 7003                                                                
CONECT 7005 7003 7006 7008                                                      
CONECT 7006 7005 7007                                                           
CONECT 7007 7006                                                                
CONECT 7008 7002 7005 7009                                                      
CONECT 7009 7008 7010 7019                                                      
CONECT 7010 7009 7011                                                           
CONECT 7011 7010 7012                                                           
CONECT 7012 7011 7013 7019                                                      
CONECT 7013 7012 7014 7015                                                      
CONECT 7014 7013                                                                
CONECT 7015 7013 7016                                                           
CONECT 7016 7015 7017 7018                                                      
CONECT 7017 7016                                                                
CONECT 7018 7016 7019                                                           
CONECT 7019 7009 7012 7018                                                      
CONECT 7021 3714 7022 7032                                                      
CONECT 7022 7021 7023 7029                                                      
CONECT 7023 7022 7024 7030                                                      
CONECT 7024 7023 7025 7031                                                      
CONECT 7025 7024 7026 7032                                                      
CONECT 7026 7025 7033                                                           
CONECT 7027 7028 7029 7034                                                      
CONECT 7028 7027                                                                
CONECT 7029 7022 7027                                                           
CONECT 7030 7023                                                                
CONECT 7031 7024 7035                                                           
CONECT 7032 7021 7025                                                           
CONECT 7033 7026                                                                
CONECT 7034 7027                                                                
CONECT 7035 7031 7036 7046                                                      
CONECT 7036 7035 7037 7043                                                      
CONECT 7037 7036 7038 7044                                                      
CONECT 7038 7037 7039 7045                                                      
CONECT 7039 7038 7040 7046                                                      
CONECT 7040 7039 7047                                                           
CONECT 7041 7042 7043 7048                                                      
CONECT 7042 7041                                                                
CONECT 7043 7036 7041                                                           
CONECT 7044 7037                                                                
CONECT 7045 7038 7049                                                           
CONECT 7046 7035 7039                                                           
CONECT 7047 7040                                                                
CONECT 7048 7041                                                                
CONECT 7049 7045 7050 7058                                                      
CONECT 7050 7049 7051 7055                                                      
CONECT 7051 7050 7052 7056                                                      
CONECT 7052 7051 7053 7057                                                      
CONECT 7053 7052 7054 7058                                                      
CONECT 7054 7053 7059                                                           
CONECT 7055 7050                                                                
CONECT 7056 7051 7093                                                           
CONECT 7057 7052                                                                
CONECT 7058 7049 7053                                                           
CONECT 7059 7054 7060                                                           
CONECT 7060 7059 7061 7069                                                      
CONECT 7061 7060 7062 7066                                                      
CONECT 7062 7061 7063 7067                                                      
CONECT 7063 7062 7064 7068                                                      
CONECT 7064 7063 7065 7069                                                      
CONECT 7065 7064 7070                                                           
CONECT 7066 7061                                                                
CONECT 7067 7062 7071                                                           
CONECT 7068 7063                                                                
CONECT 7069 7060 7064                                                           
CONECT 7070 7065                                                                
CONECT 7071 7067 7072 7080                                                      
CONECT 7072 7071 7073 7077                                                      
CONECT 7073 7072 7074 7078                                                      
CONECT 7074 7073 7075 7079                                                      
CONECT 7075 7074 7076 7080                                                      
CONECT 7076 7075 7081                                                           
CONECT 7077 7072 7082                                                           
CONECT 7078 7073                                                                
CONECT 7079 7074                                                                
CONECT 7080 7071 7075                                                           
CONECT 7081 7076                                                                
CONECT 7082 7077 7083 7091                                                      
CONECT 7083 7082 7084 7088                                                      
CONECT 7084 7083 7085 7089                                                      
CONECT 7085 7084 7086 7090                                                      
CONECT 7086 7085 7087 7091                                                      
CONECT 7087 7086 7092                                                           
CONECT 7088 7083                                                                
CONECT 7089 7084                                                                
CONECT 7090 7085                                                                
CONECT 7091 7082 7086                                                           
CONECT 7092 7087                                                                
CONECT 7093 7056 7094 7102                                                      
CONECT 7094 7093 7095 7099                                                      
CONECT 7095 7094 7096 7100                                                      
CONECT 7096 7095 7097 7101                                                      
CONECT 7097 7096 7098 7102                                                      
CONECT 7098 7097 7103                                                           
CONECT 7099 7094                                                                
CONECT 7100 7095                                                                
CONECT 7101 7096                                                                
CONECT 7102 7093 7097                                                           
CONECT 7103 7098                                                                
CONECT 7104 2773 7105 7115                                                      
CONECT 7105 7104 7106 7112                                                      
CONECT 7106 7105 7107 7113                                                      
CONECT 7107 7106 7108 7114                                                      
CONECT 7108 7107 7109 7115                                                      
CONECT 7109 7108 7116                                                           
CONECT 7110 7111 7112 7117                                                      
CONECT 7111 7110                                                                
CONECT 7112 7105 7110                                                           
CONECT 7113 7106                                                                
CONECT 7114 7107 7118                                                           
CONECT 7115 7104 7108                                                           
CONECT 7116 7109                                                                
CONECT 7117 7110                                                                
CONECT 7118 7114 7119 7129                                                      
CONECT 7119 7118 7120 7126                                                      
CONECT 7120 7119 7121 7127                                                      
CONECT 7121 7120 7122 7128                                                      
CONECT 7122 7121 7123 7129                                                      
CONECT 7123 7122 7130                                                           
CONECT 7124 7125 7126 7131                                                      
CONECT 7125 7124                                                                
CONECT 7126 7119 7124                                                           
CONECT 7127 7120                                                                
CONECT 7128 7121 7132                                                           
CONECT 7129 7118 7122                                                           
CONECT 7130 7123                                                                
CONECT 7131 7124                                                                
CONECT 7132 7128 7133 7141                                                      
CONECT 7133 7132 7134 7138                                                      
CONECT 7134 7133 7135 7139                                                      
CONECT 7135 7134 7136 7140                                                      
CONECT 7136 7135 7137 7141                                                      
CONECT 7137 7136 7142                                                           
CONECT 7138 7133                                                                
CONECT 7139 7134 7143                                                           
CONECT 7140 7135                                                                
CONECT 7141 7132 7136                                                           
CONECT 7142 7137                                                                
CONECT 7143 7139 7144 7152                                                      
CONECT 7144 7143 7145 7149                                                      
CONECT 7145 7144 7146 7150                                                      
CONECT 7146 7145 7147 7151                                                      
CONECT 7147 7146 7148 7152                                                      
CONECT 7148 7147 7153                                                           
CONECT 7149 7144                                                                
CONECT 7150 7145                                                                
CONECT 7151 7146                                                                
CONECT 7152 7143 7147                                                           
CONECT 7153 7148                                                                
CONECT 7154  869 1166 2380 2390                                                 
CONECT 7155 2009 2010 2041 3316                                                 
CONECT 7155 7667                                                                
CONECT 7156 5273 5293 5313 5322                                                 
CONECT 7156 7375                                                                
CONECT 7157 5780 5805 5827 7413                                                 
CONECT 7157 7518 7612                                                           
CONECT 7159 4694 4723 4749 7588                                                 
CONECT 7160 7161 7162                                                           
CONECT 7161 7160                                                                
CONECT 7162 7160 7163 7164                                                      
CONECT 7163 7162                                                                
CONECT 7164 7162 7165                                                           
CONECT 7165 7164                                                                
CONECT 7166 7167 7168                                                           
CONECT 7167 7166                                                                
CONECT 7168 7166 7169 7170                                                      
CONECT 7169 7168                                                                
CONECT 7170 7168 7171                                                           
CONECT 7171 7170                                                                
CONECT 7172 7173 7174                                                           
CONECT 7173 7172                                                                
CONECT 7174 7172 7175 7176                                                      
CONECT 7175 7174                                                                
CONECT 7176 7174 7177                                                           
CONECT 7177 7176                                                                
CONECT 7178 7179 7180                                                           
CONECT 7179 7178                                                                
CONECT 7180 7178 7181 7182                                                      
CONECT 7181 7180                                                                
CONECT 7182 7180 7183                                                           
CONECT 7183 7182                                                                
CONECT 7184 7185 7186                                                           
CONECT 7185 7184                                                                
CONECT 7186 7184 7187 7188                                                      
CONECT 7187 7186                                                                
CONECT 7188 7186 7189                                                           
CONECT 7189 7188                                                                
CONECT 7190 7191 7192                                                           
CONECT 7191 7190                                                                
CONECT 7192 7190 7193 7194                                                      
CONECT 7193 7192                                                                
CONECT 7194 7192 7195                                                           
CONECT 7195 7194                                                                
CONECT 7196 7197 7198                                                           
CONECT 7197 7196                                                                
CONECT 7198 7196 7199 7200                                                      
CONECT 7199 7198                                                                
CONECT 7200 7198 7201                                                           
CONECT 7201 7200                                                                
CONECT 7202 7203 7204                                                           
CONECT 7203 7202                                                                
CONECT 7204 7202 7205 7206                                                      
CONECT 7205 7204                                                                
CONECT 7206 7204 7207                                                           
CONECT 7207 7206                                                                
CONECT 7208 7209 7210                                                           
CONECT 7209 7208                                                                
CONECT 7210 7208 7211 7212                                                      
CONECT 7211 7210                                                                
CONECT 7212 7210 7213                                                           
CONECT 7213 7212                                                                
CONECT 7214 7215 7216                                                           
CONECT 7215 7214                                                                
CONECT 7216 7214 7217 7218                                                      
CONECT 7217 7216                                                                
CONECT 7218 7216 7219                                                           
CONECT 7219 7218                                                                
CONECT 7220 6489 6810 7668 7674                                                 
CONECT 7220 7675 7676 7679                                                      
CONECT 7375 7156                                                                
CONECT 7413 7157                                                                
CONECT 7518 7157                                                                
CONECT 7588 7159                                                                
CONECT 7612 7157                                                                
CONECT 7667 7155                                                                
CONECT 7668 7220                                                                
CONECT 7674 7220                                                                
CONECT 7675 7220                                                                
CONECT 7676 7220                                                                
CONECT 7679 7220                                                                
MASTER      581    0   37   40   33    0    0    6 7626    2  481   67          
END

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Related entries of code: 5hrt

Entries with 90% protein sequence similarity cutoff in PDBbind
PDB Code	Check Database	Protein Sequence Similarity
No similar entries are found!
Complexes with the same small molecule ligand
PDB Code	Check Database	Ligand Name
No complexes with the same small molecule ligand are found!

Entry Information

PDB ID	5hrt
Complex Type	Protein-Nucleic Acid
PDBbind Subset	general set
Protein Name	mouse autotaxin (ATX)
Ligand Name	anti-ATX aptamer RB011
EC.Number	E.C.3.1.4.39
Resolution	2(Å)
Affinity (Kd/Ki/IC50)	Kd=1.3nM
Release Year	2016
Protein/NA Sequence	Check fasta file
Primary Reference	(2016) Nat.Struct.Mol.Biol. Vol. 23: pp. 395-401

Links to External Databases

RCSB PDB	The mother database
PDBsum	Enhanced annotations on PDB entries
Pubchem	Comprehensive collection of chemical and biological data
UniProtKB AC	UniProt accession number (AC): Q9R1E6
Entrez Gene ID	NCBI Entrez Gene ID: 18606
ASD	Information of known allosteric effects of PDB entries

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