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***  Cas9_for_virtual_labs  ***

elNémo ID: 20111815163253854

Job options:

ID        	=	 20111815163253854
JOBID     	=	 Cas9_for_virtual_labs
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER Cas9_for_virtual_labs

HEADER    HYDROLASE                               16-JAN-14   4CMP              
TITLE     CRYSTAL STRUCTURE OF S. PYOGENES CAS9                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CRISPR-ASSOCIATED ENDONUCLEASE CAS9/CSN1;                  
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: CAS9;                                                       
COMPND   5 EC: 3.1.-.-;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: STREPTOCOCCUS PYOGENES;                         
SOURCE   3 ORGANISM_TAXID: 301447;                                              
SOURCE   4 STRAIN: SEROTYPE M1;                                                 
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VARIANT: ROSETTA2;                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PEC-K-MBP                                 
KEYWDS    HYDROLASE, DNASE, RNA-GUIDED, IMMUNITY, CRRNA, GENOME EDITING         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.JINEK,F.JIANG,D.W.TAYLOR,S.H.STERNBERG,E.KAYA,E.MA,C.ANDERS,        
AUTHOR   2 M.HAUER,K.ZHOU,S.LIN,M.KAPLAN,A.T.IAVARONE,E.CHARPENTIER,E.NOGALES,  
AUTHOR   3 J.A.DOUDNA                                                           
REVDAT   3   26-MAR-14 4CMP    1       JRNL                                     
REVDAT   2   19-FEB-14 4CMP    1       JRNL   ATOM                              
REVDAT   1   12-FEB-14 4CMP    0                                                
JRNL        AUTH   M.JINEK,F.JIANG,D.W.TAYLOR,S.H.STERNBERG,E.KAYA,E.MA,        
JRNL        AUTH 2 C.ANDERS,M.HAUER,K.ZHOU,S.LIN,M.KAPLAN,A.T.IAVARONE,         
JRNL        AUTH 3 E.CHARPENTIER,E.NOGALES,J.A.DOUDNA                           
JRNL        TITL   STRUCTURES OF CAS9 ENDONUCLEASES REVEAL RNA-MEDIATED         
JRNL        TITL 2 CONFORMATIONAL ACTIVATION.                                   
JRNL        REF    SCIENCE                       V. 343 47997 2014              
JRNL        REFN                   ISSN 0036-8075                               
JRNL        PMID   24505130                                                     
JRNL        DOI    10.1126/SCIENCE.1247997                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.62 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT 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) : 2.620                          
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.481                         
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.36                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.61                          
REMARK   3   NUMBER OF REFLECTIONS             : 92408                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.2532                          
REMARK   3   R VALUE            (WORKING SET) : 0.2523                          
REMARK   3   FREE R VALUE                     : 0.2858                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.6                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 2424                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 47.4890 -  6.7305    0.98     5508   194  0.2350 0.2259        
REMARK   3     2  6.7305 -  5.3445    0.99     5402    99  0.2683 0.2739        
REMARK   3     3  5.3445 -  4.6696    0.99     5395   105  0.2228 0.2598        
REMARK   3     4  4.6696 -  4.2430    0.99     5270   193  0.2129 0.2878        
REMARK   3     5  4.2430 -  3.9390    0.99     5321    98  0.2280 0.2726        
REMARK   3     6  3.9390 -  3.7069    0.99     5237   198  0.2419 0.2672        
REMARK   3     7  3.7069 -  3.5213    1.00     5298   100  0.2508 0.2999        
REMARK   3     8  3.5213 -  3.3680    1.00     5245   195  0.2636 0.2986        
REMARK   3     9  3.3680 -  3.2384    1.00     5315   105  0.2777 0.2915        
REMARK   3    10  3.2384 -  3.1267    1.00     5276   137  0.2891 0.3531        
REMARK   3    11  3.1267 -  3.0289    1.00     5238   163  0.3044 0.3904        
REMARK   3    12  3.0289 -  2.9424    1.00     5306   103  0.3173 0.3392        
REMARK   3    13  2.9424 -  2.8649    1.00     5172   197  0.3195 0.4338        
REMARK   3    14  2.8649 -  2.7950    1.00     5312   114  0.3003 0.3180        
REMARK   3    15  2.7950 -  2.7315    1.00     5261   142  0.2921 0.3314        
REMARK   3    16  2.7315 -  2.6734    1.00     5212   140  0.2967 0.3480        
REMARK   3    17  2.6734 -  2.6199    1.00     5216   141  0.3124 0.3463        
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)     : 0.41             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.27            
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 64.77                          
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      :  0.005          19183                                  
REMARK   3   ANGLE     :  0.948          25770                                  
REMARK   3   CHIRALITY :  0.053           2899                                  
REMARK   3   PLANARITY :  0.003           3268                                  
REMARK   3   DIHEDRAL  : 16.958           7339                                  
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 4  THROUGH  65) OR (RESID 718      
REMARK   3               THROUGH 764) OR (RESID 908 THROUGH 1363))              
REMARK   3    ORIGIN FOR THE GROUP (A): -36.4050 -29.7107 -24.0474              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3044 T22:   0.2146                                     
REMARK   3      T33:   0.0788 T12:   0.1514                                     
REMARK   3      T13:  -0.0432 T23:   0.0004                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9611 L22:   1.3429                                     
REMARK   3      L33:   3.1131 L12:  -0.3317                                     
REMARK   3      L13:  -0.5577 L23:  -0.2998                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0860 S12:   0.1160 S13:   0.0292                       
REMARK   3      S21:   0.0029 S22:   0.0488 S23:   0.0601                       
REMARK   3      S31:  -0.5508 S32:  -0.3253 S33:  -0.0354                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN A AND (RESID  66  THROUGH  447 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -18.4746 -58.9459   3.9740              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2600 T22:   0.1559                                     
REMARK   3      T33:   0.2398 T12:  -0.0311                                     
REMARK   3      T13:   0.0013 T23:   0.0290                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8415 L22:   1.0919                                     
REMARK   3      L33:   1.2968 L12:  -0.0559                                     
REMARK   3      L13:   0.4635 L23:  -0.5167                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1031 S12:   0.0134 S13:   0.0044                       
REMARK   3      S21:  -0.0153 S22:   0.0531 S23:  -0.1155                       
REMARK   3      S31:  -0.2501 S32:   0.1419 S33:   0.0105                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN A AND (RESID  775  THROUGH 902 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.4501 -16.0601 -13.8044              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1180 T22:   0.3889                                     
REMARK   3      T33:   0.4699 T12:  -1.0348                                     
REMARK   3      T13:  -0.1854 T23:   0.5934                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0752 L22:   0.3391                                     
REMARK   3      L33:   0.4171 L12:  -0.0494                                     
REMARK   3      L13:  -0.0088 L23:   0.3176                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0434 S12:  -0.1717 S13:   0.1136                       
REMARK   3      S21:   0.2927 S22:  -0.1880 S23:  -0.1308                       
REMARK   3      S31:  -1.0157 S32:   0.9933 S33:  -0.3390                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN B AND ((RESID  4  THROUGH  65) OR (RESID 718     
REMARK   3               THROUGH 764) OR (RESID 908 THROUGH 1363))              
REMARK   3    ORIGIN FOR THE GROUP (A): -39.0221-125.3115  69.1741              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2543 T22:   0.2600                                     
REMARK   3      T33:   0.1256 T12:  -0.1163                                     
REMARK   3      T13:   0.1277 T23:  -0.0347                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3551 L22:   1.3934                                     
REMARK   3      L33:   2.1217 L12:   0.5395                                     
REMARK   3      L13:   0.4431 L23:  -0.0122                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1625 S12:  -0.2388 S13:   0.1222                       
REMARK   3      S21:   0.3479 S22:  -0.1566 S23:   0.1335                       
REMARK   3      S31:   0.2210 S32:  -0.0673 S33:   0.0222                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN B AND (RESID  66  THROUGH  447 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -19.4030 -96.9345  40.4661              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0959 T22:   0.2241                                     
REMARK   3      T33:   0.3003 T12:   0.0033                                     
REMARK   3      T13:  -0.0149 T23:   0.0700                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4942 L22:   2.1738                                     
REMARK   3      L33:   0.7753 L12:  -0.1358                                     
REMARK   3      L13:  -0.1607 L23:  -0.4719                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0953 S12:   0.0437 S13:  -0.0552                       
REMARK   3      S21:  -0.0424 S22:   0.0421 S23:  -0.0456                       
REMARK   3      S31:   0.0409 S32:   0.0790 S33:   0.0319                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN B AND (RESID  773  THROUGH 901 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.6030-140.1196  58.6578              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4324 T22:   0.7022                                     
REMARK   3      T33:   0.7410 T12:  -0.0616                                     
REMARK   3      T13:  -0.0984 T23:   0.1768                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8212 L22:   0.7623                                     
REMARK   3      L33:   0.9868 L12:  -0.0362                                     
REMARK   3      L13:  -0.1933 L23:   0.1648                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0013 S12:  -0.7989 S13:  -0.8501                       
REMARK   3      S21:  -0.1659 S22:   0.1853 S23:   0.1471                       
REMARK   3      S31:   0.4582 S32:  -0.1772 S33:  -0.0236                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN A AND (RESID 503 THROUGH 714)                    
REMARK   3    ORIGIN FOR THE GROUP (A): -56.0746 -83.9324  -2.4003              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3571 T22:   0.7350                                     
REMARK   3      T33:   0.6340 T12:   0.1635                                     
REMARK   3      T13:   0.0291 T23:   0.4250                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8727 L22:   0.4085                                     
REMARK   3      L33:   1.8746 L12:  -0.0201                                     
REMARK   3      L13:   0.3388 L23:  -0.0385                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2565 S12:  -0.2140 S13:  -0.1835                       
REMARK   3      S21:   0.0395 S22:   0.3375 S23:   0.3252                       
REMARK   3      S31:  -0.3051 S32:  -1.3947 S33:  -0.1969                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN B AND (RESID 502 THROUGH 713)                    
REMARK   3    ORIGIN FOR THE GROUP (A): -58.0188 -71.4269  46.3373              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1736 T22:   0.4626                                     
REMARK   3      T33:   0.9453 T12:   0.1290                                     
REMARK   3      T13:  -0.0588 T23:   0.5871                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9802 L22:   1.1606                                     
REMARK   3      L33:   3.1914 L12:   0.1150                                     
REMARK   3      L13:   0.1082 L23:   0.6695                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2400 S12:   0.1218 S13:   0.4269                       
REMARK   3      S21:  -0.0017 S22:   0.0255 S23:   0.8302                       
REMARK   3      S31:  -0.0196 S32:  -1.2544 S33:  -1.3053                       
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 4CMP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-JAN-14.                  
REMARK 100 THE PDBE ID CODE IS EBI-59472.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 31-AUG-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X06SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00000                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL (PILATUS 6M)                 
REMARK 200  DETECTOR MANUFACTURER          : PILATUS                            
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 92408                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.62                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 47.52                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.94                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.2                               
REMARK 200  DATA REDUNDANCY                : 2.3                                
REMARK 200  R MERGE                    (I) : 0.05                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 13.02                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.62                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.69                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.3                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.64                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 1.94                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIRAS                        
REMARK 200 SOFTWARE USED: AUTOSHARP                                             
REMARK 200 STARTING MODEL: NONE                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS PH 8.5, 0.3 M                 
REMARK 280  LITHIUM SULFATE, 15% PEG 3350                                       
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       79.89000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000      104.81000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       79.89000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000      104.81000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A    -3                                                      
REMARK 465     ALA A    -2                                                      
REMARK 465     ALA A    -1                                                      
REMARK 465     SER A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     ASP A     2                                                      
REMARK 465     LYS A     3                                                      
REMARK 465     GLU A   103                                                      
REMARK 465     SER A   104                                                      
REMARK 465     PHE A   105                                                      
REMARK 465     LEU A   106                                                      
REMARK 465     VAL A   107                                                      
REMARK 465     GLU A   108                                                      
REMARK 465     GLU A   109                                                      
REMARK 465     ASP A   110                                                      
REMARK 465     LYS A   111                                                      
REMARK 465     LYS A   112                                                      
REMARK 465     HIS A   113                                                      
REMARK 465     GLU A   114                                                      
REMARK 465     VAL A   308                                                      
REMARK 465     ASN A   309                                                      
REMARK 465     THR A   310                                                      
REMARK 465     GLU A   311                                                      
REMARK 465     ILE A   312                                                      
REMARK 465     THR A   313                                                      
REMARK 465     ILE A   448                                                      
REMARK 465     PRO A   449                                                      
REMARK 465     TYR A   450                                                      
REMARK 465     TYR A   451                                                      
REMARK 465     VAL A   452                                                      
REMARK 465     GLY A   453                                                      
REMARK 465     PRO A   454                                                      
REMARK 465     LEU A   455                                                      
REMARK 465     ALA A   456                                                      
REMARK 465     ARG A   457                                                      
REMARK 465     GLY A   458                                                      
REMARK 465     ASN A   459                                                      
REMARK 465     SER A   460                                                      
REMARK 465     ARG A   461                                                      
REMARK 465     PHE A   462                                                      
REMARK 465     ALA A   463                                                      
REMARK 465     TRP A   464                                                      
REMARK 465     MET A   465                                                      
REMARK 465     THR A   466                                                      
REMARK 465     ARG A   467                                                      
REMARK 465     LYS A   468                                                      
REMARK 465     SER A   469                                                      
REMARK 465     GLU A   470                                                      
REMARK 465     GLU A   471                                                      
REMARK 465     THR A   472                                                      
REMARK 465     ILE A   473                                                      
REMARK 465     THR A   474                                                      
REMARK 465     PRO A   475                                                      
REMARK 465     TRP A   476                                                      
REMARK 465     ASN A   477                                                      
REMARK 465     PHE A   478                                                      
REMARK 465     GLU A   479                                                      
REMARK 465     GLU A   480                                                      
REMARK 465     VAL A   481                                                      
REMARK 465     VAL A   482                                                      
REMARK 465     ASP A   483                                                      
REMARK 465     LYS A   484                                                      
REMARK 465     GLY A   485                                                      
REMARK 465     ALA A   486                                                      
REMARK 465     SER A   487                                                      
REMARK 465     ALA A   488                                                      
REMARK 465     GLN A   489                                                      
REMARK 465     SER A   490                                                      
REMARK 465     PHE A   491                                                      
REMARK 465     ILE A   492                                                      
REMARK 465     GLU A   493                                                      
REMARK 465     ARG A   494                                                      
REMARK 465     MET A   495                                                      
REMARK 465     THR A   496                                                      
REMARK 465     ASN A   497                                                      
REMARK 465     PHE A   498                                                      
REMARK 465     ASP A   499                                                      
REMARK 465     LYS A   500                                                      
REMARK 465     ASN A   501                                                      
REMARK 465     LEU A   502                                                      
REMARK 465     LYS A   528                                                      
REMARK 465     TYR A   529                                                      
REMARK 465     VAL A   530                                                      
REMARK 465     THR A   531                                                      
REMARK 465     GLU A   532                                                      
REMARK 465     GLY A   533                                                      
REMARK 465     MET A   534                                                      
REMARK 465     ARG A   535                                                      
REMARK 465     LYS A   536                                                      
REMARK 465     PRO A   537                                                      
REMARK 465     ALA A   538                                                      
REMARK 465     PHE A   539                                                      
REMARK 465     TYR A   568                                                      
REMARK 465     PHE A   569                                                      
REMARK 465     LYS A   570                                                      
REMARK 465     LYS A   571                                                      
REMARK 465     ILE A   572                                                      
REMARK 465     GLU A   573                                                      
REMARK 465     CYS A   574                                                      
REMARK 465     PHE A   575                                                      
REMARK 465     ASP A   576                                                      
REMARK 465     SER A   577                                                      
REMARK 465     VAL A   578                                                      
REMARK 465     GLU A   579                                                      
REMARK 465     ILE A   580                                                      
REMARK 465     SER A   581                                                      
REMARK 465     GLY A   582                                                      
REMARK 465     VAL A   583                                                      
REMARK 465     GLU A   584                                                      
REMARK 465     ASP A   585                                                      
REMARK 465     ARG A   586                                                      
REMARK 465     LYS A   673                                                      
REMARK 465     GLN A   674                                                      
REMARK 465     SER A   675                                                      
REMARK 465     GLY A   676                                                      
REMARK 465     SER A   685                                                      
REMARK 465     ASP A   686                                                      
REMARK 465     GLY A   687                                                      
REMARK 465     PHE A   688                                                      
REMARK 465     ALA A   689                                                      
REMARK 465     ASN A   690                                                      
REMARK 465     GLY A   715                                                      
REMARK 465     GLN A   716                                                      
REMARK 465     GLY A   717                                                      
REMARK 465     ARG A   765                                                      
REMARK 465     GLU A   766                                                      
REMARK 465     ASN A   767                                                      
REMARK 465     GLN A   768                                                      
REMARK 465     THR A   769                                                      
REMARK 465     THR A   770                                                      
REMARK 465     GLN A   771                                                      
REMARK 465     LYS A   772                                                      
REMARK 465     GLY A   773                                                      
REMARK 465     GLN A   774                                                      
REMARK 465     GLY A   792                                                      
REMARK 465     SER A   793                                                      
REMARK 465     GLN A   794                                                      
REMARK 465     ILE A   795                                                      
REMARK 465     LEU A   796                                                      
REMARK 465     LYS A   797                                                      
REMARK 465     GLU A   798                                                      
REMARK 465     SER A   860                                                      
REMARK 465     ASP A   861                                                      
REMARK 465     ALA A   903                                                      
REMARK 465     GLU A   904                                                      
REMARK 465     ARG A   905                                                      
REMARK 465     GLY A   906                                                      
REMARK 465     GLY A   907                                                      
REMARK 465     GLU A  1028                                                      
REMARK 465     ILE A  1029                                                      
REMARK 465     GLY A  1030                                                      
REMARK 465     LYS A  1031                                                      
REMARK 465     ALA A  1032                                                      
REMARK 465     THR A  1033                                                      
REMARK 465     ALA A  1034                                                      
REMARK 465     LYS A  1035                                                      
REMARK 465     GLY A  1103                                                      
REMARK 465     GLY A  1104                                                      
REMARK 465     PHE A  1105                                                      
REMARK 465     SER A  1106                                                      
REMARK 465     LYS A  1107                                                      
REMARK 465     GLU A  1108                                                      
REMARK 465     SER A  1109                                                      
REMARK 465     ILE A  1110                                                      
REMARK 465     LEU A  1111                                                      
REMARK 465     PRO A  1112                                                      
REMARK 465     LYS A  1113                                                      
REMARK 465     ARG A  1114                                                      
REMARK 465     ASN A  1115                                                      
REMARK 465     SER A  1116                                                      
REMARK 465     ASP A  1117                                                      
REMARK 465     LYS A  1118                                                      
REMARK 465     LEU A  1119                                                      
REMARK 465     ILE A  1120                                                      
REMARK 465     ALA A  1121                                                      
REMARK 465     ARG A  1122                                                      
REMARK 465     LYS A  1123                                                      
REMARK 465     LYS A  1124                                                      
REMARK 465     ASP A  1125                                                      
REMARK 465     TRP A  1126                                                      
REMARK 465     ASP A  1127                                                      
REMARK 465     PRO A  1128                                                      
REMARK 465     LYS A  1129                                                      
REMARK 465     LYS A  1130                                                      
REMARK 465     TYR A  1131                                                      
REMARK 465     GLY A  1132                                                      
REMARK 465     GLY A  1133                                                      
REMARK 465     PHE A  1134                                                      
REMARK 465     ASP A  1135                                                      
REMARK 465     SER A  1136                                                      
REMARK 465     ALA A  1147                                                      
REMARK 465     LYS A  1148                                                      
REMARK 465     VAL A  1149                                                      
REMARK 465     GLU A  1150                                                      
REMARK 465     LYS A  1151                                                      
REMARK 465     GLY A  1152                                                      
REMARK 465     LYS A  1153                                                      
REMARK 465     SER A  1154                                                      
REMARK 465     LYS A  1155                                                      
REMARK 465     LYS A  1156                                                      
REMARK 465     LEU A  1157                                                      
REMARK 465     LYS A  1158                                                      
REMARK 465     TYR A  1187                                                      
REMARK 465     LYS A  1188                                                      
REMARK 465     GLU A  1189                                                      
REMARK 465     VAL A  1190                                                      
REMARK 465     LYS A  1191                                                      
REMARK 465     GLU A  1243                                                      
REMARK 465     LYS A  1244                                                      
REMARK 465     LEU A  1245                                                      
REMARK 465     LYS A  1246                                                      
REMARK 465     GLY A  1247                                                      
REMARK 465     SER A  1248                                                      
REMARK 465     PRO A  1249                                                      
REMARK 465     GLU A  1250                                                      
REMARK 465     ASP A  1251                                                      
REMARK 465     ASN A  1252                                                      
REMARK 465     GLU A  1253                                                      
REMARK 465     GLN A  1254                                                      
REMARK 465     LYS A  1255                                                      
REMARK 465     GLN A  1256                                                      
REMARK 465     LEU A  1257                                                      
REMARK 465     PHE A  1258                                                      
REMARK 465     GLN A  1364                                                      
REMARK 465     LEU A  1365                                                      
REMARK 465     GLY A  1366                                                      
REMARK 465     GLY A  1367                                                      
REMARK 465     ASP A  1368                                                      
REMARK 465     GLY B    -3                                                      
REMARK 465     ALA B    -2                                                      
REMARK 465     ALA B    -1                                                      
REMARK 465     SER B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ASP B     2                                                      
REMARK 465     LYS B     3                                                      
REMARK 465     SER B   104                                                      
REMARK 465     PHE B   105                                                      
REMARK 465     LEU B   106                                                      
REMARK 465     VAL B   107                                                      
REMARK 465     GLU B   108                                                      
REMARK 465     GLU B   109                                                      
REMARK 465     ASP B   110                                                      
REMARK 465     LYS B   111                                                      
REMARK 465     LYS B   112                                                      
REMARK 465     HIS B   113                                                      
REMARK 465     GLU B   114                                                      
REMARK 465     ARG B   115                                                      
REMARK 465     ASN B   309                                                      
REMARK 465     ILE B   448                                                      
REMARK 465     PRO B   449                                                      
REMARK 465     TYR B   450                                                      
REMARK 465     TYR B   451                                                      
REMARK 465     VAL B   452                                                      
REMARK 465     GLY B   453                                                      
REMARK 465     PRO B   454                                                      
REMARK 465     LEU B   455                                                      
REMARK 465     ALA B   456                                                      
REMARK 465     ARG B   457                                                      
REMARK 465     GLY B   458                                                      
REMARK 465     ASN B   459                                                      
REMARK 465     SER B   460                                                      
REMARK 465     ARG B   461                                                      
REMARK 465     PHE B   462                                                      
REMARK 465     ALA B   463                                                      
REMARK 465     TRP B   464                                                      
REMARK 465     MET B   465                                                      
REMARK 465     THR B   466                                                      
REMARK 465     ARG B   467                                                      
REMARK 465     LYS B   468                                                      
REMARK 465     SER B   469                                                      
REMARK 465     GLU B   470                                                      
REMARK 465     GLU B   471                                                      
REMARK 465     THR B   472                                                      
REMARK 465     ILE B   473                                                      
REMARK 465     THR B   474                                                      
REMARK 465     PRO B   475                                                      
REMARK 465     TRP B   476                                                      
REMARK 465     ASN B   477                                                      
REMARK 465     PHE B   478                                                      
REMARK 465     GLU B   479                                                      
REMARK 465     GLU B   480                                                      
REMARK 465     VAL B   481                                                      
REMARK 465     VAL B   482                                                      
REMARK 465     ASP B   483                                                      
REMARK 465     LYS B   484                                                      
REMARK 465     GLY B   485                                                      
REMARK 465     ALA B   486                                                      
REMARK 465     SER B   487                                                      
REMARK 465     ALA B   488                                                      
REMARK 465     GLN B   489                                                      
REMARK 465     SER B   490                                                      
REMARK 465     PHE B   491                                                      
REMARK 465     ILE B   492                                                      
REMARK 465     GLU B   493                                                      
REMARK 465     ARG B   494                                                      
REMARK 465     MET B   495                                                      
REMARK 465     THR B   496                                                      
REMARK 465     ASN B   497                                                      
REMARK 465     PHE B   498                                                      
REMARK 465     ASP B   499                                                      
REMARK 465     LYS B   500                                                      
REMARK 465     ASN B   501                                                      
REMARK 465     LYS B   528                                                      
REMARK 465     TYR B   529                                                      
REMARK 465     VAL B   530                                                      
REMARK 465     THR B   531                                                      
REMARK 465     GLU B   532                                                      
REMARK 465     GLY B   533                                                      
REMARK 465     MET B   534                                                      
REMARK 465     ARG B   535                                                      
REMARK 465     LYS B   536                                                      
REMARK 465     PRO B   537                                                      
REMARK 465     ALA B   538                                                      
REMARK 465     LYS B   571                                                      
REMARK 465     ILE B   572                                                      
REMARK 465     GLU B   573                                                      
REMARK 465     CYS B   574                                                      
REMARK 465     PHE B   575                                                      
REMARK 465     ASP B   576                                                      
REMARK 465     SER B   577                                                      
REMARK 465     VAL B   578                                                      
REMARK 465     GLU B   579                                                      
REMARK 465     ILE B   580                                                      
REMARK 465     SER B   581                                                      
REMARK 465     GLY B   582                                                      
REMARK 465     VAL B   583                                                      
REMARK 465     GLU B   584                                                      
REMARK 465     ASP B   585                                                      
REMARK 465     ARG B   586                                                      
REMARK 465     GLN B   674                                                      
REMARK 465     SER B   675                                                      
REMARK 465     SER B   714                                                      
REMARK 465     GLY B   715                                                      
REMARK 465     GLN B   716                                                      
REMARK 465     GLY B   717                                                      
REMARK 465     ARG B   765                                                      
REMARK 465     GLU B   766                                                      
REMARK 465     ASN B   767                                                      
REMARK 465     GLN B   768                                                      
REMARK 465     THR B   769                                                      
REMARK 465     THR B   770                                                      
REMARK 465     GLN B   771                                                      
REMARK 465     LYS B   772                                                      
REMARK 465     GLY B   792                                                      
REMARK 465     SER B   793                                                      
REMARK 465     GLN B   794                                                      
REMARK 465     ILE B   795                                                      
REMARK 465     LEU B   796                                                      
REMARK 465     LYS B   797                                                      
REMARK 465     GLU B   798                                                      
REMARK 465     HIS B   799                                                      
REMARK 465     SER B   860                                                      
REMARK 465     ASP B   861                                                      
REMARK 465     ALA B   903                                                      
REMARK 465     GLU B   904                                                      
REMARK 465     ARG B   905                                                      
REMARK 465     GLY B   906                                                      
REMARK 465     GLY B   907                                                      
REMARK 465     GLU B  1026                                                      
REMARK 465     GLN B  1027                                                      
REMARK 465     GLU B  1028                                                      
REMARK 465     ILE B  1029                                                      
REMARK 465     GLY B  1030                                                      
REMARK 465     LYS B  1031                                                      
REMARK 465     ALA B  1032                                                      
REMARK 465     THR B  1033                                                      
REMARK 465     ALA B  1034                                                      
REMARK 465     LYS B  1035                                                      
REMARK 465     GLY B  1103                                                      
REMARK 465     GLY B  1104                                                      
REMARK 465     PHE B  1105                                                      
REMARK 465     SER B  1106                                                      
REMARK 465     LYS B  1107                                                      
REMARK 465     GLU B  1108                                                      
REMARK 465     SER B  1109                                                      
REMARK 465     ILE B  1110                                                      
REMARK 465     LEU B  1111                                                      
REMARK 465     PRO B  1112                                                      
REMARK 465     LYS B  1113                                                      
REMARK 465     ARG B  1114                                                      
REMARK 465     ASN B  1115                                                      
REMARK 465     SER B  1116                                                      
REMARK 465     ASP B  1117                                                      
REMARK 465     LYS B  1118                                                      
REMARK 465     LEU B  1119                                                      
REMARK 465     ILE B  1120                                                      
REMARK 465     ALA B  1121                                                      
REMARK 465     ARG B  1122                                                      
REMARK 465     LYS B  1123                                                      
REMARK 465     LYS B  1124                                                      
REMARK 465     ASP B  1125                                                      
REMARK 465     TRP B  1126                                                      
REMARK 465     ASP B  1127                                                      
REMARK 465     PRO B  1128                                                      
REMARK 465     LYS B  1129                                                      
REMARK 465     LYS B  1130                                                      
REMARK 465     TYR B  1131                                                      
REMARK 465     GLY B  1132                                                      
REMARK 465     GLY B  1133                                                      
REMARK 465     PHE B  1134                                                      
REMARK 465     ASP B  1135                                                      
REMARK 465     SER B  1136                                                      
REMARK 465     VAL B  1149                                                      
REMARK 465     GLU B  1150                                                      
REMARK 465     LYS B  1151                                                      
REMARK 465     GLY B  1152                                                      
REMARK 465     LYS B  1153                                                      
REMARK 465     SER B  1154                                                      
REMARK 465     LYS B  1155                                                      
REMARK 465     LYS B  1156                                                      
REMARK 465     LEU B  1157                                                      
REMARK 465     LYS B  1158                                                      
REMARK 465     SER B  1159                                                      
REMARK 465     GLY B  1186                                                      
REMARK 465     TYR B  1187                                                      
REMARK 465     TYR B  1242                                                      
REMARK 465     GLU B  1243                                                      
REMARK 465     LYS B  1244                                                      
REMARK 465     LEU B  1245                                                      
REMARK 465     LYS B  1246                                                      
REMARK 465     GLY B  1247                                                      
REMARK 465     SER B  1248                                                      
REMARK 465     PRO B  1249                                                      
REMARK 465     GLU B  1250                                                      
REMARK 465     ASP B  1251                                                      
REMARK 465     ASN B  1252                                                      
REMARK 465     GLU B  1253                                                      
REMARK 465     GLN B  1254                                                      
REMARK 465     LYS B  1255                                                      
REMARK 465     GLN B  1364                                                      
REMARK 465     LEU B  1365                                                      
REMARK 465     GLY B  1366                                                      
REMARK 465     GLY B  1367                                                      
REMARK 465     ASP B  1368                                                      
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 684    CG   CD   CE   NZ                                   
REMARK 470     LYS A 775    CG   CD   CE   NZ                                   
REMARK 470     ASN A 776    CG   OD1  ND2                                       
REMARK 470     ARG A 778    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 782    CG   CD   CE   NZ                                   
REMARK 470     GLU A 785    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 786    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 789    CG   CD   CE   NZ                                   
REMARK 470     HIS A 799    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ARG A 832    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     TYR A 836    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ASP A 837    CG   OD1  OD2                                       
REMARK 470     ARG A 859    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 862    CG   CD   CE   NZ                                   
REMARK 470     ARG A 864    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 873    CG   CD   OE1  OE2                                  
REMARK 470     LYS A1192    CG   CD   CE   NZ                                   
REMARK 470     ARG B 832    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     TYR B 836    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ARG B 859    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 862    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500  HD12  ILE B  1179     HD2  LYS B  1192              0.98            
REMARK 500   O    ILE B  1179     HG3  GLU B  1183              1.17            
REMARK 500   HZ2  LYS B  1003     OE1  GLU B  1068              1.47            
REMARK 500   HZ3  LYS B   877     O    THR B   901              1.52            
REMARK 500   O    LYS B   209     HG   SER B   213              1.52            
REMARK 500   HZ3  LYS B  1325     O    PHE B  1327              1.58            
REMARK 500   O    ILE A  1270     HG   SER A  1274              1.58            
REMARK 500   OD2  ASP B    54     HH   TYR B  1201              1.58            
REMARK 500   O    ASP B   681     H    SER B   685              1.58            
REMARK 500  HH22  ARG B   165     O    PHE B   446              1.58            
REMARK 500  HH11  ARG B   324     O    LYS B   401              1.60            
REMARK 500   OG   SER B   297     OD1  ASN B   407              1.94            
REMARK 500   O    PHE B  1080     O    HOH B  2087              1.95            
REMARK 500   O    MET A  1169     O    HOH A  2082              2.00            
REMARK 500   NH1  ARG B    78     O    ILE B   162              2.03            
REMARK 500   NH2  ARG B   400     O    HOH B  2052              2.05            
REMARK 500   OE1  GLU B  1205     NH2  ARG B  1359              2.05            
REMARK 500   O    ASN A  1208     NH1  ARG A  1279              2.06            
REMARK 500   O    ILE B  1179     CG   GLU B  1183              2.07            
REMARK 500   OG   SER B   254     O    HOH B  2040              2.07            
REMARK 500   O    HIS A   799     OH   TYR A   815              2.10            
REMARK 500   NH2  ARG B   557     OD1  ASP B   596              2.11            
REMARK 500   NH2  ARG A   165     O    PHE A   446              2.12            
REMARK 500   O    LYS A   848     NZ   LYS A   961              2.12            
REMARK 500   O    LEU A   398     O    HOH A  2040              2.13            
REMARK 500   O    ALA B  1147     N    LYS B  1188              2.14            
REMARK 500   O    ARG A   919     NZ   LYS A   959              2.15            
REMARK 500   NH1  ARG A   100     O    LEU A   625              2.16            
REMARK 500   NZ   LYS B  1334     O    HOH B  2103              2.17            
REMARK 500   O    LEU A   551     OG1  THR A   555              2.18            
REMARK 500   NH2  ARG A   557     OD1  ASP A   596              2.19            
REMARK 500   O    ILE A  1270     OG   SER A  1274              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    PRO A  28      154.57    -49.90                                   
REMARK 500    ASP A  39       45.76    -83.31                                   
REMARK 500    ASP A  94       96.79   -166.57                                   
REMARK 500    PHE A 164       72.94   -113.45                                   
REMARK 500    SER A 204     -118.21     42.73                                   
REMARK 500    GLN A 354      -19.91     81.46                                   
REMARK 500    LEU A 591       59.61    -93.30                                   
REMARK 500    ASN A 668       -8.00   -140.10                                   
REMARK 500    ARG A 671     -169.47   -105.33                                   
REMARK 500    ASN A 692      144.70   -175.22                                   
REMARK 500    ARG A 753       -1.15     66.78                                   
REMARK 500    LEU A 806       -3.54    -58.87                                   
REMARK 500    SER A 867     -115.15     56.41                                   
REMARK 500    PHE A1008       11.66   -142.28                                   
REMARK 500    PRO A1199      153.32    -46.07                                   
REMARK 500    GLU A1207     -146.58     60.05                                   
REMARK 500    ASN A1208       63.04    -68.25                                   
REMARK 500    VAL A1280      -37.90   -131.56                                   
REMARK 500    ALA A1283       75.27   -117.77                                   
REMARK 500    PHE A1327     -127.47     51.82                                   
REMARK 500    ASP A1361       94.13   -162.20                                   
REMARK 500    HIS B  41      -43.62     62.76                                   
REMARK 500    PHE B 164       78.83   -111.39                                   
REMARK 500    SER B 204     -139.86     50.77                                   
REMARK 500    THR B 249       76.99   -117.65                                   
REMARK 500    PRO B 503     -173.60    -62.81                                   
REMARK 500    LEU B 591       56.80   -115.14                                   
REMARK 500    LEU B 666      -70.03    -59.67                                   
REMARK 500    SER B 685       64.35   -156.88                                   
REMARK 500    MET B 751       31.04    -95.75                                   
REMARK 500    ARG B 753       -1.97     67.11                                   
REMARK 500    MET B 763       66.64   -156.03                                   
REMARK 500    VAL B 824       33.12   -145.54                                   
REMARK 500    SER B 867     -117.59     55.88                                   
REMARK 500    PRO B 871      157.99    -44.69                                   
REMARK 500    SER B 872      138.74    -36.10                                   
REMARK 500    MET B 879       60.86   -101.66                                   
REMARK 500    ASP B 944     -160.00    -84.16                                   
REMARK 500    PHE B 972       72.72   -104.93                                   
REMARK 500    PHE B1008       11.33   -141.96                                   
REMARK 500    GLU B1207     -137.41     60.29                                   
REMARK 500    PHE B1327     -122.47     57.68                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH B2109        DISTANCE =  5.66 ANGSTROMS                       
REMARK 525    HOH B2110        DISTANCE =  7.72 ANGSTROMS                       
REMARK 525    HOH B2111        DISTANCE =  5.09 ANGSTROMS                       
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                              MG B2367  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B2004   O                                                      
REMARK 620 2 ASP B 986   OD2  66.2                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B2364                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A2364                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B2365                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A2365                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B2366                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG B2367                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4CMQ   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MN-BOUND S.PYOGENES CAS9                       
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 M-TERMINAL GAAS IS DERIVED FROM THE EXPRESSION VECTOR                
DBREF  4CMP A    1  1368  UNP    Q99ZW2   CAS9_STRP1       1   1368             
DBREF  4CMP B    1  1368  UNP    Q99ZW2   CAS9_STRP1       1   1368             
SEQADV 4CMP GLY A   -3  UNP  Q99ZW2              EXPRESSION TAG                 
SEQADV 4CMP ALA A   -2  UNP  Q99ZW2              EXPRESSION TAG                 
SEQADV 4CMP ALA A   -1  UNP  Q99ZW2              EXPRESSION TAG                 
SEQADV 4CMP SER A    0  UNP  Q99ZW2              EXPRESSION TAG                 
SEQADV 4CMP GLY B   -3  UNP  Q99ZW2              EXPRESSION TAG                 
SEQADV 4CMP ALA B   -2  UNP  Q99ZW2              EXPRESSION TAG                 
SEQADV 4CMP ALA B   -1  UNP  Q99ZW2              EXPRESSION TAG                 
SEQADV 4CMP SER B    0  UNP  Q99ZW2              EXPRESSION TAG                 
SEQRES   1 A 1372  GLY ALA ALA SER MET ASP LYS LYS TYR SER ILE GLY LEU          
SEQRES   2 A 1372  ASP ILE GLY THR ASN SER VAL GLY TRP ALA VAL ILE THR          
SEQRES   3 A 1372  ASP GLU TYR LYS VAL PRO SER LYS LYS PHE LYS VAL LEU          
SEQRES   4 A 1372  GLY ASN THR ASP ARG HIS SER ILE LYS LYS ASN LEU ILE          
SEQRES   5 A 1372  GLY ALA LEU LEU PHE ASP SER GLY GLU THR ALA GLU ALA          
SEQRES   6 A 1372  THR ARG LEU LYS ARG THR ALA ARG ARG ARG TYR THR ARG          
SEQRES   7 A 1372  ARG LYS ASN ARG ILE CYS TYR LEU GLN GLU ILE PHE SER          
SEQRES   8 A 1372  ASN GLU MET ALA LYS VAL ASP ASP SER PHE PHE HIS ARG          
SEQRES   9 A 1372  LEU GLU GLU SER PHE LEU VAL GLU GLU ASP LYS LYS HIS          
SEQRES  10 A 1372  GLU ARG HIS PRO ILE PHE GLY ASN ILE VAL ASP GLU VAL          
SEQRES  11 A 1372  ALA TYR HIS GLU LYS TYR PRO THR ILE TYR HIS LEU ARG          
SEQRES  12 A 1372  LYS LYS LEU VAL ASP SER THR ASP LYS ALA ASP LEU ARG          
SEQRES  13 A 1372  LEU ILE TYR LEU ALA LEU ALA HIS MET ILE LYS PHE ARG          
SEQRES  14 A 1372  GLY HIS PHE LEU ILE GLU GLY ASP LEU ASN PRO ASP ASN          
SEQRES  15 A 1372  SER ASP VAL ASP LYS LEU PHE ILE GLN LEU VAL GLN THR          
SEQRES  16 A 1372  TYR ASN GLN LEU PHE GLU GLU ASN PRO ILE ASN ALA SER          
SEQRES  17 A 1372  GLY VAL ASP ALA LYS ALA ILE LEU SER ALA ARG LEU SER          
SEQRES  18 A 1372  LYS SER ARG ARG LEU GLU ASN LEU ILE ALA GLN LEU PRO          
SEQRES  19 A 1372  GLY GLU LYS LYS ASN GLY LEU PHE GLY ASN LEU ILE ALA          
SEQRES  20 A 1372  LEU SER LEU GLY LEU THR PRO ASN PHE LYS SER ASN PHE          
SEQRES  21 A 1372  ASP LEU ALA GLU ASP ALA LYS LEU GLN LEU SER LYS ASP          
SEQRES  22 A 1372  THR TYR ASP ASP ASP LEU ASP ASN LEU LEU ALA GLN ILE          
SEQRES  23 A 1372  GLY ASP GLN TYR ALA ASP LEU PHE LEU ALA ALA LYS ASN          
SEQRES  24 A 1372  LEU SER ASP ALA ILE LEU LEU SER ASP ILE LEU ARG VAL          
SEQRES  25 A 1372  ASN THR GLU ILE THR LYS ALA PRO LEU SER ALA SER MET          
SEQRES  26 A 1372  ILE LYS ARG TYR ASP GLU HIS HIS GLN ASP LEU THR LEU          
SEQRES  27 A 1372  LEU LYS ALA LEU VAL ARG GLN GLN LEU PRO GLU LYS TYR          
SEQRES  28 A 1372  LYS GLU ILE PHE PHE ASP GLN SER LYS ASN GLY TYR ALA          
SEQRES  29 A 1372  GLY TYR ILE ASP GLY GLY ALA SER GLN GLU GLU PHE TYR          
SEQRES  30 A 1372  LYS PHE ILE LYS PRO ILE LEU GLU LYS MET ASP GLY THR          
SEQRES  31 A 1372  GLU GLU LEU LEU VAL LYS LEU ASN ARG GLU ASP LEU LEU          
SEQRES  32 A 1372  ARG LYS GLN ARG THR PHE ASP ASN GLY SER ILE PRO HIS          
SEQRES  33 A 1372  GLN ILE HIS LEU GLY GLU LEU HIS ALA ILE LEU ARG ARG          
SEQRES  34 A 1372  GLN GLU ASP PHE TYR PRO PHE LEU LYS ASP ASN ARG GLU          
SEQRES  35 A 1372  LYS ILE GLU LYS ILE LEU THR PHE ARG ILE PRO TYR TYR          
SEQRES  36 A 1372  VAL GLY PRO LEU ALA ARG GLY ASN SER ARG PHE ALA TRP          
SEQRES  37 A 1372  MET THR ARG LYS SER GLU GLU THR ILE THR PRO TRP ASN          
SEQRES  38 A 1372  PHE GLU GLU VAL VAL ASP LYS GLY ALA SER ALA GLN SER          
SEQRES  39 A 1372  PHE ILE GLU ARG MET THR ASN PHE ASP LYS ASN LEU PRO          
SEQRES  40 A 1372  ASN GLU LYS VAL LEU PRO LYS HIS SER LEU LEU TYR GLU          
SEQRES  41 A 1372  TYR PHE THR VAL TYR ASN GLU LEU THR LYS VAL LYS TYR          
SEQRES  42 A 1372  VAL THR GLU GLY MET ARG LYS PRO ALA PHE LEU SER GLY          
SEQRES  43 A 1372  GLU GLN LYS LYS ALA ILE VAL ASP LEU LEU PHE LYS THR          
SEQRES  44 A 1372  ASN ARG LYS VAL THR VAL LYS GLN LEU LYS GLU ASP TYR          
SEQRES  45 A 1372  PHE LYS LYS ILE GLU CYS PHE ASP SER VAL GLU ILE SER          
SEQRES  46 A 1372  GLY VAL GLU ASP ARG PHE ASN ALA SER LEU GLY THR TYR          
SEQRES  47 A 1372  HIS ASP LEU LEU LYS ILE ILE LYS ASP LYS ASP PHE LEU          
SEQRES  48 A 1372  ASP ASN GLU GLU ASN GLU ASP ILE LEU GLU ASP ILE VAL          
SEQRES  49 A 1372  LEU THR LEU THR LEU PHE GLU ASP ARG GLU MET ILE GLU          
SEQRES  50 A 1372  GLU ARG LEU LYS THR TYR ALA HIS LEU PHE ASP ASP LYS          
SEQRES  51 A 1372  VAL MET LYS GLN LEU LYS ARG ARG ARG TYR THR GLY TRP          
SEQRES  52 A 1372  GLY ARG LEU SER ARG LYS LEU ILE ASN GLY ILE ARG ASP          
SEQRES  53 A 1372  LYS GLN SER GLY LYS THR ILE LEU ASP PHE LEU LYS SER          
SEQRES  54 A 1372  ASP GLY PHE ALA ASN ARG ASN PHE MET GLN LEU ILE HIS          
SEQRES  55 A 1372  ASP ASP SER LEU THR PHE LYS GLU ASP ILE GLN LYS ALA          
SEQRES  56 A 1372  GLN VAL SER GLY GLN GLY ASP SER LEU HIS GLU HIS ILE          
SEQRES  57 A 1372  ALA ASN LEU ALA GLY SER PRO ALA ILE LYS LYS GLY ILE          
SEQRES  58 A 1372  LEU GLN THR VAL LYS VAL VAL ASP GLU LEU VAL LYS VAL          
SEQRES  59 A 1372  MET GLY ARG HIS LYS PRO GLU ASN ILE VAL ILE GLU MET          
SEQRES  60 A 1372  ALA ARG GLU ASN GLN THR THR GLN LYS GLY GLN LYS ASN          
SEQRES  61 A 1372  SER ARG GLU ARG MET LYS ARG ILE GLU GLU GLY ILE LYS          
SEQRES  62 A 1372  GLU LEU GLY SER GLN ILE LEU LYS GLU HIS PRO VAL GLU          
SEQRES  63 A 1372  ASN THR GLN LEU GLN ASN GLU LYS LEU TYR LEU TYR TYR          
SEQRES  64 A 1372  LEU GLN ASN GLY ARG ASP MET TYR VAL ASP GLN GLU LEU          
SEQRES  65 A 1372  ASP ILE ASN ARG LEU SER ASP TYR ASP VAL ASP HIS ILE          
SEQRES  66 A 1372  VAL PRO GLN SER PHE LEU LYS ASP ASP SER ILE ASP ASN          
SEQRES  67 A 1372  LYS VAL LEU THR ARG SER ASP LYS ASN ARG GLY LYS SER          
SEQRES  68 A 1372  ASP ASN VAL PRO SER GLU GLU VAL VAL LYS LYS MET LYS          
SEQRES  69 A 1372  ASN TYR TRP ARG GLN LEU LEU ASN ALA LYS LEU ILE THR          
SEQRES  70 A 1372  GLN ARG LYS PHE ASP ASN LEU THR LYS ALA GLU ARG GLY          
SEQRES  71 A 1372  GLY LEU SER GLU LEU ASP LYS ALA GLY PHE ILE LYS ARG          
SEQRES  72 A 1372  GLN LEU VAL GLU THR ARG GLN ILE THR LYS HIS VAL ALA          
SEQRES  73 A 1372  GLN ILE LEU ASP SER ARG MET ASN THR LYS TYR ASP GLU          
SEQRES  74 A 1372  ASN ASP LYS LEU ILE ARG GLU VAL LYS VAL ILE THR LEU          
SEQRES  75 A 1372  LYS SER LYS LEU VAL SER ASP PHE ARG LYS ASP PHE GLN          
SEQRES  76 A 1372  PHE TYR LYS VAL ARG GLU ILE ASN ASN TYR HIS HIS ALA          
SEQRES  77 A 1372  HIS ASP ALA TYR LEU ASN ALA VAL VAL GLY THR ALA LEU          
SEQRES  78 A 1372  ILE LYS LYS TYR PRO LYS LEU GLU SER GLU PHE VAL TYR          
SEQRES  79 A 1372  GLY ASP TYR LYS VAL TYR ASP VAL ARG LYS MET ILE ALA          
SEQRES  80 A 1372  LYS SER GLU GLN GLU ILE GLY LYS ALA THR ALA LYS TYR          
SEQRES  81 A 1372  PHE PHE TYR SER ASN ILE MET ASN PHE PHE LYS THR GLU          
SEQRES  82 A 1372  ILE THR LEU ALA ASN GLY GLU ILE ARG LYS ARG PRO LEU          
SEQRES  83 A 1372  ILE GLU THR ASN GLY GLU THR GLY GLU ILE VAL TRP ASP          
SEQRES  84 A 1372  LYS GLY ARG ASP PHE ALA THR VAL ARG LYS VAL LEU SER          
SEQRES  85 A 1372  MET PRO GLN VAL ASN ILE VAL LYS LYS THR GLU VAL GLN          
SEQRES  86 A 1372  THR GLY GLY PHE SER LYS GLU SER ILE LEU PRO LYS ARG          
SEQRES  87 A 1372  ASN SER ASP LYS LEU ILE ALA ARG LYS LYS ASP TRP ASP          
SEQRES  88 A 1372  PRO LYS LYS TYR GLY GLY PHE ASP SER PRO THR VAL ALA          
SEQRES  89 A 1372  TYR SER VAL LEU VAL VAL ALA LYS VAL GLU LYS GLY LYS          
SEQRES  90 A 1372  SER LYS LYS LEU LYS SER VAL LYS GLU LEU LEU GLY ILE          
SEQRES  91 A 1372  THR ILE MET GLU ARG SER SER PHE GLU LYS ASN PRO ILE          
SEQRES  92 A 1372  ASP PHE LEU GLU ALA LYS GLY TYR LYS GLU VAL LYS LYS          
SEQRES  93 A 1372  ASP LEU ILE ILE LYS LEU PRO LYS TYR SER LEU PHE GLU          
SEQRES  94 A 1372  LEU GLU ASN GLY ARG LYS ARG MET LEU ALA SER ALA GLY          
SEQRES  95 A 1372  GLU LEU GLN LYS GLY ASN GLU LEU ALA LEU PRO SER LYS          
SEQRES  96 A 1372  TYR VAL ASN PHE LEU TYR LEU ALA SER HIS TYR GLU LYS          
SEQRES  97 A 1372  LEU LYS GLY SER PRO GLU ASP ASN GLU GLN LYS GLN LEU          
SEQRES  98 A 1372  PHE VAL GLU GLN HIS LYS HIS TYR LEU ASP GLU ILE ILE          
SEQRES  99 A 1372  GLU GLN ILE SER GLU PHE SER LYS ARG VAL ILE LEU ALA          
SEQRES 100 A 1372  ASP ALA ASN LEU ASP LYS VAL LEU SER ALA TYR ASN LYS          
SEQRES 101 A 1372  HIS ARG ASP LYS PRO ILE ARG GLU GLN ALA GLU ASN ILE          
SEQRES 102 A 1372  ILE HIS LEU PHE THR LEU THR ASN LEU GLY ALA PRO ALA          
SEQRES 103 A 1372  ALA PHE LYS TYR PHE ASP THR THR ILE ASP ARG LYS ARG          
SEQRES 104 A 1372  TYR THR SER THR LYS GLU VAL LEU ASP ALA THR LEU ILE          
SEQRES 105 A 1372  HIS GLN SER ILE THR GLY LEU TYR GLU THR ARG ILE ASP          
SEQRES 106 A 1372  LEU SER GLN LEU GLY GLY ASP                                  
SEQRES   1 B 1372  GLY ALA ALA SER MET ASP LYS LYS TYR SER ILE GLY LEU          
SEQRES   2 B 1372  ASP ILE GLY THR ASN SER VAL GLY TRP ALA VAL ILE THR          
SEQRES   3 B 1372  ASP GLU TYR LYS VAL PRO SER LYS LYS PHE LYS VAL LEU          
SEQRES   4 B 1372  GLY ASN THR ASP ARG HIS SER ILE LYS LYS ASN LEU ILE          
SEQRES   5 B 1372  GLY ALA LEU LEU PHE ASP SER GLY GLU THR ALA GLU ALA          
SEQRES   6 B 1372  THR ARG LEU LYS ARG THR ALA ARG ARG ARG TYR THR ARG          
SEQRES   7 B 1372  ARG LYS ASN ARG ILE CYS TYR LEU GLN GLU ILE PHE SER          
SEQRES   8 B 1372  ASN GLU MET ALA LYS VAL ASP ASP SER PHE PHE HIS ARG          
SEQRES   9 B 1372  LEU GLU GLU SER PHE LEU VAL GLU GLU ASP LYS LYS HIS          
SEQRES  10 B 1372  GLU ARG HIS PRO ILE PHE GLY ASN ILE VAL ASP GLU VAL          
SEQRES  11 B 1372  ALA TYR HIS GLU LYS TYR PRO THR ILE TYR HIS LEU ARG          
SEQRES  12 B 1372  LYS LYS LEU VAL ASP SER THR ASP LYS ALA ASP LEU ARG          
SEQRES  13 B 1372  LEU ILE TYR LEU ALA LEU ALA HIS MET ILE LYS PHE ARG          
SEQRES  14 B 1372  GLY HIS PHE LEU ILE GLU GLY ASP LEU ASN PRO ASP ASN          
SEQRES  15 B 1372  SER ASP VAL ASP LYS LEU PHE ILE GLN LEU VAL GLN THR          
SEQRES  16 B 1372  TYR ASN GLN LEU PHE GLU GLU ASN PRO ILE ASN ALA SER          
SEQRES  17 B 1372  GLY VAL ASP ALA LYS ALA ILE LEU SER ALA ARG LEU SER          
SEQRES  18 B 1372  LYS SER ARG ARG LEU GLU ASN LEU ILE ALA GLN LEU PRO          
SEQRES  19 B 1372  GLY GLU LYS LYS ASN GLY LEU PHE GLY ASN LEU ILE ALA          
SEQRES  20 B 1372  LEU SER LEU GLY LEU THR PRO ASN PHE LYS SER ASN PHE          
SEQRES  21 B 1372  ASP LEU ALA GLU ASP ALA LYS LEU GLN LEU SER LYS ASP          
SEQRES  22 B 1372  THR TYR ASP ASP ASP LEU ASP ASN LEU LEU ALA GLN ILE          
SEQRES  23 B 1372  GLY ASP GLN TYR ALA ASP LEU PHE LEU ALA ALA LYS ASN          
SEQRES  24 B 1372  LEU SER ASP ALA ILE LEU LEU SER ASP ILE LEU ARG VAL          
SEQRES  25 B 1372  ASN THR GLU ILE THR LYS ALA PRO LEU SER ALA SER MET          
SEQRES  26 B 1372  ILE LYS ARG TYR ASP GLU HIS HIS GLN ASP LEU THR LEU          
SEQRES  27 B 1372  LEU LYS ALA LEU VAL ARG GLN GLN LEU PRO GLU LYS TYR          
SEQRES  28 B 1372  LYS GLU ILE PHE PHE ASP GLN SER LYS ASN GLY TYR ALA          
SEQRES  29 B 1372  GLY TYR ILE ASP GLY GLY ALA SER GLN GLU GLU PHE TYR          
SEQRES  30 B 1372  LYS PHE ILE LYS PRO ILE LEU GLU LYS MET ASP GLY THR          
SEQRES  31 B 1372  GLU GLU LEU LEU VAL LYS LEU ASN ARG GLU ASP LEU LEU          
SEQRES  32 B 1372  ARG LYS GLN ARG THR PHE ASP ASN GLY SER ILE PRO HIS          
SEQRES  33 B 1372  GLN ILE HIS LEU GLY GLU LEU HIS ALA ILE LEU ARG ARG          
SEQRES  34 B 1372  GLN GLU ASP PHE TYR PRO PHE LEU LYS ASP ASN ARG GLU          
SEQRES  35 B 1372  LYS ILE GLU LYS ILE LEU THR PHE ARG ILE PRO TYR TYR          
SEQRES  36 B 1372  VAL GLY PRO LEU ALA ARG GLY ASN SER ARG PHE ALA TRP          
SEQRES  37 B 1372  MET THR ARG LYS SER GLU GLU THR ILE THR PRO TRP ASN          
SEQRES  38 B 1372  PHE GLU GLU VAL VAL ASP LYS GLY ALA SER ALA GLN SER          
SEQRES  39 B 1372  PHE ILE GLU ARG MET THR ASN PHE ASP LYS ASN LEU PRO          
SEQRES  40 B 1372  ASN GLU LYS VAL LEU PRO LYS HIS SER LEU LEU TYR GLU          
SEQRES  41 B 1372  TYR PHE THR VAL TYR ASN GLU LEU THR LYS VAL LYS TYR          
SEQRES  42 B 1372  VAL THR GLU GLY MET ARG LYS PRO ALA PHE LEU SER GLY          
SEQRES  43 B 1372  GLU GLN LYS LYS ALA ILE VAL ASP LEU LEU PHE LYS THR          
SEQRES  44 B 1372  ASN ARG LYS VAL THR VAL LYS GLN LEU LYS GLU ASP TYR          
SEQRES  45 B 1372  PHE LYS LYS ILE GLU CYS PHE ASP SER VAL GLU ILE SER          
SEQRES  46 B 1372  GLY VAL GLU ASP ARG PHE ASN ALA SER LEU GLY THR TYR          
SEQRES  47 B 1372  HIS ASP LEU LEU LYS ILE ILE LYS ASP LYS ASP PHE LEU          
SEQRES  48 B 1372  ASP ASN GLU GLU ASN GLU ASP ILE LEU GLU ASP ILE VAL          
SEQRES  49 B 1372  LEU THR LEU THR LEU PHE GLU ASP ARG GLU MET ILE GLU          
SEQRES  50 B 1372  GLU ARG LEU LYS THR TYR ALA HIS LEU PHE ASP ASP LYS          
SEQRES  51 B 1372  VAL MET LYS GLN LEU LYS ARG ARG ARG TYR THR GLY TRP          
SEQRES  52 B 1372  GLY ARG LEU SER ARG LYS LEU ILE ASN GLY ILE ARG ASP          
SEQRES  53 B 1372  LYS GLN SER GLY LYS THR ILE LEU ASP PHE LEU LYS SER          
SEQRES  54 B 1372  ASP GLY PHE ALA ASN ARG ASN PHE MET GLN LEU ILE HIS          
SEQRES  55 B 1372  ASP ASP SER LEU THR PHE LYS GLU ASP ILE GLN LYS ALA          
SEQRES  56 B 1372  GLN VAL SER GLY GLN GLY ASP SER LEU HIS GLU HIS ILE          
SEQRES  57 B 1372  ALA ASN LEU ALA GLY SER PRO ALA ILE LYS LYS GLY ILE          
SEQRES  58 B 1372  LEU GLN THR VAL LYS VAL VAL ASP GLU LEU VAL LYS VAL          
SEQRES  59 B 1372  MET GLY ARG HIS LYS PRO GLU ASN ILE VAL ILE GLU MET          
SEQRES  60 B 1372  ALA ARG GLU ASN GLN THR THR GLN LYS GLY GLN LYS ASN          
SEQRES  61 B 1372  SER ARG GLU ARG MET LYS ARG ILE GLU GLU GLY ILE LYS          
SEQRES  62 B 1372  GLU LEU GLY SER GLN ILE LEU LYS GLU HIS PRO VAL GLU          
SEQRES  63 B 1372  ASN THR GLN LEU GLN ASN GLU LYS LEU TYR LEU TYR TYR          
SEQRES  64 B 1372  LEU GLN ASN GLY ARG ASP MET TYR VAL ASP GLN GLU LEU          
SEQRES  65 B 1372  ASP ILE ASN ARG LEU SER ASP TYR ASP VAL ASP HIS ILE          
SEQRES  66 B 1372  VAL PRO GLN SER PHE LEU LYS ASP ASP SER ILE ASP ASN          
SEQRES  67 B 1372  LYS VAL LEU THR ARG SER ASP LYS ASN ARG GLY LYS SER          
SEQRES  68 B 1372  ASP ASN VAL PRO SER GLU GLU VAL VAL LYS LYS MET LYS          
SEQRES  69 B 1372  ASN TYR TRP ARG GLN LEU LEU ASN ALA LYS LEU ILE THR          
SEQRES  70 B 1372  GLN ARG LYS PHE ASP ASN LEU THR LYS ALA GLU ARG GLY          
SEQRES  71 B 1372  GLY LEU SER GLU LEU ASP LYS ALA GLY PHE ILE LYS ARG          
SEQRES  72 B 1372  GLN LEU VAL GLU THR ARG GLN ILE THR LYS HIS VAL ALA          
SEQRES  73 B 1372  GLN ILE LEU ASP SER ARG MET ASN THR LYS TYR ASP GLU          
SEQRES  74 B 1372  ASN ASP LYS LEU ILE ARG GLU VAL LYS VAL ILE THR LEU          
SEQRES  75 B 1372  LYS SER LYS LEU VAL SER ASP PHE ARG LYS ASP PHE GLN          
SEQRES  76 B 1372  PHE TYR LYS VAL ARG GLU ILE ASN ASN TYR HIS HIS ALA          
SEQRES  77 B 1372  HIS ASP ALA TYR LEU ASN ALA VAL VAL GLY THR ALA LEU          
SEQRES  78 B 1372  ILE LYS LYS TYR PRO LYS LEU GLU SER GLU PHE VAL TYR          
SEQRES  79 B 1372  GLY ASP TYR LYS VAL TYR ASP VAL ARG LYS MET ILE ALA          
SEQRES  80 B 1372  LYS SER GLU GLN GLU ILE GLY LYS ALA THR ALA LYS TYR          
SEQRES  81 B 1372  PHE PHE TYR SER ASN ILE MET ASN PHE PHE LYS THR GLU          
SEQRES  82 B 1372  ILE THR LEU ALA ASN GLY GLU ILE ARG LYS ARG PRO LEU          
SEQRES  83 B 1372  ILE GLU THR ASN GLY GLU THR GLY GLU ILE VAL TRP ASP          
SEQRES  84 B 1372  LYS GLY ARG ASP PHE ALA THR VAL ARG LYS VAL LEU SER          
SEQRES  85 B 1372  MET PRO GLN VAL ASN ILE VAL LYS LYS THR GLU VAL GLN          
SEQRES  86 B 1372  THR GLY GLY PHE SER LYS GLU SER ILE LEU PRO LYS ARG          
SEQRES  87 B 1372  ASN SER ASP LYS LEU ILE ALA ARG LYS LYS ASP TRP ASP          
SEQRES  88 B 1372  PRO LYS LYS TYR GLY GLY PHE ASP SER PRO THR VAL ALA          
SEQRES  89 B 1372  TYR SER VAL LEU VAL VAL ALA LYS VAL GLU LYS GLY LYS          
SEQRES  90 B 1372  SER LYS LYS LEU LYS SER VAL LYS GLU LEU LEU GLY ILE          
SEQRES  91 B 1372  THR ILE MET GLU ARG SER SER PHE GLU LYS ASN PRO ILE          
SEQRES  92 B 1372  ASP PHE LEU GLU ALA LYS GLY TYR LYS GLU VAL LYS LYS          
SEQRES  93 B 1372  ASP LEU ILE ILE LYS LEU PRO LYS TYR SER LEU PHE GLU          
SEQRES  94 B 1372  LEU GLU ASN GLY ARG LYS ARG MET LEU ALA SER ALA GLY          
SEQRES  95 B 1372  GLU LEU GLN LYS GLY ASN GLU LEU ALA LEU PRO SER LYS          
SEQRES  96 B 1372  TYR VAL ASN PHE LEU TYR LEU ALA SER HIS TYR GLU LYS          
SEQRES  97 B 1372  LEU LYS GLY SER PRO GLU ASP ASN GLU GLN LYS GLN LEU          
SEQRES  98 B 1372  PHE VAL GLU GLN HIS LYS HIS TYR LEU ASP GLU ILE ILE          
SEQRES  99 B 1372  GLU GLN ILE SER GLU PHE SER LYS ARG VAL ILE LEU ALA          
SEQRES 100 B 1372  ASP ALA ASN LEU ASP LYS VAL LEU SER ALA TYR ASN LYS          
SEQRES 101 B 1372  HIS ARG ASP LYS PRO ILE ARG GLU GLN ALA GLU ASN ILE          
SEQRES 102 B 1372  ILE HIS LEU PHE THR LEU THR ASN LEU GLY ALA PRO ALA          
SEQRES 103 B 1372  ALA PHE LYS TYR PHE ASP THR THR ILE ASP ARG LYS ARG          
SEQRES 104 B 1372  TYR THR SER THR LYS GLU VAL LEU ASP ALA THR LEU ILE          
SEQRES 105 B 1372  HIS GLN SER ILE THR GLY LEU TYR GLU THR ARG ILE ASP          
SEQRES 106 B 1372  LEU SER GLN LEU GLY GLY ASP                                  
HET    SO4  B2364       5                                                       
HET    SO4  A2364       5                                                       
HET    SO4  B2365       5                                                       
HET    SO4  A2365       5                                                       
HET    SO4  B2366       5                                                       
HET     MG  B2367       1                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM      MG MAGNESIUM ION                                                    
FORMUL   3  SO4    5(O4 S 2-)                                                   
FORMUL   4   MG    MG 2+                                                        
FORMUL   5  HOH   *203(H2 O)                                                    
HELIX    1   1 THR A   58  LEU A   64  1                                   7    
HELIX    2   2 THR A   67  ASP A   94  1                                  28    
HELIX    3   3 SER A   96  LEU A  101  1                                   6    
HELIX    4   4 ASN A  121  TYR A  132  1                                  12    
HELIX    5   5 THR A  134  SER A  145  1                                  12    
HELIX    6   6 ASP A  150  PHE A  164  1                                  15    
HELIX    7   7 ASN A  175  SER A  179  5                                   5    
HELIX    8   8 ASP A  180  PHE A  196  1                                  17    
HELIX    9   9 ASP A  207  ALA A  214  1                                   8    
HELIX   10  10 SER A  217  ALA A  227  1                                  11    
HELIX   11  11 GLY A  236  GLY A  247  1                                  12    
HELIX   12  12 PHE A  252  ASP A  257  1                                   6    
HELIX   13  13 THR A  270  GLY A  283  1                                  14    
HELIX   14  14 TYR A  286  ARG A  307  1                                  22    
HELIX   15  15 ALA A  315  LEU A  343  1                                  29    
HELIX   16  16 PRO A  344  ASP A  353  1                                  10    
HELIX   17  17 GLY A  358  ASP A  364  1                                   7    
HELIX   18  18 SER A  368  ASP A  384  1                                  17    
HELIX   19  19 GLU A  387  ARG A  395  1                                   9    
HELIX   20  20 PRO A  411  GLU A  427  1                                  17    
HELIX   21  21 TYR A  430  PHE A  446  1                                  17    
HELIX   22  22 SER A  512  THR A  525  1                                  14    
HELIX   23  23 SER A  541  LEU A  552  1                                  12    
HELIX   24  24 THR A  560  ASP A  567  1                                   8    
HELIX   25  25 LEU A  591  LYS A  602  1                                  12    
HELIX   26  26 ASP A  603  ASN A  609  1                                   7    
HELIX   27  27 ASN A  612  PHE A  626  1                                  15    
HELIX   28  28 ASP A  628  LYS A  637  1                                  10    
HELIX   29  29 THR A  638  ALA A  640  5                                   3    
HELIX   30  30 ASP A  644  ARG A  654  1                                  11    
HELIX   31  31 SER A  663  GLY A  669  1                                   7    
HELIX   32  32 THR A  678  LYS A  684  1                                   7    
HELIX   33  33 ASN A  692  HIS A  698  1                                   7    
HELIX   34  34 THR A  703  SER A  714  1                                  12    
HELIX   35  35 ASP A  718  ASN A  726  1                                   9    
HELIX   36  36 SER A  730  MET A  751  1                                  22    
HELIX   37  37 LYS A  775  LYS A  789  1                                  15    
HELIX   38  38 GLU A  802  GLN A  807  5                                   6    
HELIX   39  39 ASN A  808  GLN A  817  1                                  10    
HELIX   40  40 ASP A  829  ASP A  837  1                                   9    
HELIX   41  41 SER A  851  ASP A  853  5                                   3    
HELIX   42  42 VAL A  875  LYS A  878  5                                   4    
HELIX   43  43 MET A  879  ALA A  889  1                                  11    
HELIX   44  44 THR A  893  LYS A  902  1                                  10    
HELIX   45  45 SER A  909  VAL A  922  1                                  14    
HELIX   46  46 ARG A  925  ASN A  940  1                                  16    
HELIX   47  47 LYS A  959  PHE A  970  1                                  12    
HELIX   48  48 ASN A  980  TYR A 1001  1                                  22    
HELIX   49  49 LEU A 1004  VAL A 1009  1                                   6    
HELIX   50  50 ASP A 1017  ILE A 1022  1                                   6    
HELIX   51  51 ASN A 1041  LYS A 1047  5                                   7    
HELIX   52  52 GLY A 1077  MET A 1089  1                                  13    
HELIX   53  53 ILE A 1168  ASN A 1177  1                                  10    
HELIX   54  54 ASN A 1177  GLY A 1186  1                                  10    
HELIX   55  55 PRO A 1229  HIS A 1241  1                                  13    
HELIX   56  56 LYS A 1263  ILE A 1281  1                                  19    
HELIX   57  57 ALA A 1283  HIS A 1297  1                                  15    
HELIX   58  58 PRO A 1301  LEU A 1312  1                                  12    
HELIX   59  59 LEU A 1312  ASN A 1317  1                                   6    
HELIX   60  60 GLU A 1341  ALA A 1345  5                                   5    
HELIX   61  61 THR B   58  LEU B   64  1                                   7    
HELIX   62  62 THR B   67  ASP B   94  1                                  28    
HELIX   63  63 SER B   96  LEU B  101  1                                   6    
HELIX   64  64 ASN B  121  TYR B  132  1                                  12    
HELIX   65  65 THR B  134  SER B  145  1                                  12    
HELIX   66  66 ASP B  150  PHE B  164  1                                  15    
HELIX   67  67 ASN B  175  SER B  179  5                                   5    
HELIX   68  68 ASP B  180  PHE B  196  1                                  17    
HELIX   69  69 ASP B  207  SER B  213  1                                   7    
HELIX   70  70 SER B  217  GLN B  228  1                                  12    
HELIX   71  71 GLY B  236  GLY B  247  1                                  12    
HELIX   72  72 THR B  270  GLY B  283  1                                  14    
HELIX   73  73 TYR B  286  ARG B  307  1                                  22    
HELIX   74  74 ALA B  315  LEU B  343  1                                  29    
HELIX   75  75 LEU B  343  ASP B  353  1                                  11    
HELIX   76  76 GLN B  354  ASN B  357  5                                   4    
HELIX   77  77 GLY B  358  GLY B  365  1                                   8    
HELIX   78  78 SER B  368  ASP B  384  1                                  17    
HELIX   79  79 GLU B  387  GLU B  396  1                                  10    
HELIX   80  80 PRO B  411  GLU B  427  1                                  17    
HELIX   81  81 TYR B  430  ASN B  436  1                                   7    
HELIX   82  82 ASN B  436  PHE B  446  1                                  11    
HELIX   83  83 SER B  512  LEU B  524  1                                  13    
HELIX   84  84 THR B  525  VAL B  527  5                                   3    
HELIX   85  85 GLU B  543  LEU B  552  1                                  10    
HELIX   86  86 THR B  560  LYS B  570  1                                  11    
HELIX   87  87 LEU B  591  ILE B  601  1                                  11    
HELIX   88  88 ASP B  603  ASP B  608  1                                   6    
HELIX   89  89 ASN B  609  PHE B  626  1                                  18    
HELIX   90  90 ASP B  628  LEU B  636  1                                   9    
HELIX   91  91 ASP B  644  ARG B  654  1                                  11    
HELIX   92  92 SER B  663  ILE B  670  1                                   8    
HELIX   93  93 THR B  678  ASP B  686  1                                   9    
HELIX   94  94 ASN B  692  HIS B  698  1                                   7    
HELIX   95  95 LEU B  702  VAL B  713  1                                  12    
HELIX   96  96 ASP B  718  ASN B  726  1                                   9    
HELIX   97  97 SER B  730  MET B  751  1                                  22    
HELIX   98  98 GLY B  773  LYS B  789  1                                  17    
HELIX   99  99 GLU B  802  GLN B  807  5                                   6    
HELIX  100 100 ASN B  808  GLN B  817  1                                  10    
HELIX  101 101 ASP B  829  SER B  834  1                                   6    
HELIX  102 102 SER B  851  ASP B  853  5                                   3    
HELIX  103 103 LYS B  862  SER B  867  1                                   6    
HELIX  104 104 MET B  879  ALA B  889  1                                  11    
HELIX  105 105 THR B  893  LYS B  902  1                                  10    
HELIX  106 106 SER B  909  VAL B  922  1                                  14    
HELIX  107 107 ARG B  925  ASN B  940  1                                  16    
HELIX  108 108 LYS B  959  GLN B  971  1                                  13    
HELIX  109 109 TYR B  981  TYR B 1001  1                                  21    
HELIX  110 110 LEU B 1004  VAL B 1009  1                                   6    
HELIX  111 111 ASP B 1017  ILE B 1022  1                                   6    
HELIX  112 112 ASN B 1041  LYS B 1047  5                                   7    
HELIX  113 113 LYS B 1076  MET B 1089  1                                  14    
HELIX  114 114 ILE B 1168  LYS B 1176  1                                   9    
HELIX  115 115 ASN B 1177  LYS B 1185  1                                   9    
HELIX  116 116 PRO B 1229  HIS B 1241  1                                  13    
HELIX  117 117 LEU B 1257  HIS B 1262  1                                   6    
HELIX  118 118 HIS B 1264  ILE B 1281  1                                  18    
HELIX  119 119 ALA B 1283  HIS B 1297  1                                  15    
HELIX  120 120 PRO B 1301  LEU B 1312  1                                  12    
HELIX  121 121 LEU B 1312  ASN B 1317  1                                   6    
HELIX  122 122 LYS B 1340  ASP B 1344  5                                   5    
SHEET    1  AA 6 LYS A 954  THR A 957  0                                        
SHEET    2  AA 6 ASN A 758  MET A 763  1  O  ILE A 759   N  ILE A 956           
SHEET    3  AA 6 SER A   6  ILE A  11  1  O  ILE A   7   N  VAL A 760           
SHEET    4  AA 6 SER A  15  ILE A  21 -1  O  GLY A  17   N  ASP A  10           
SHEET    5  AA 6 ILE A  48  LEU A  52 -1  O  GLY A  49   N  TRP A  18           
SHEET    6  AA 6 ASN A1093  LYS A1096  1  O  ASN A1093   N  ALA A  50           
SHEET    1  AB 2 SER A  29  LYS A  33  0                                        
SHEET    2  AB 2 SER A  42  ASN A  46 -1  O  ILE A  43   N  PHE A  32           
SHEET    1  AC 2 VAL A 838  HIS A 840  0                                        
SHEET    2  AC 2 LYS A 855  LEU A 857 -1  O  VAL A 856   N  ASP A 839           
SHEET    1  AD 2 GLU A1049  THR A1051  0                                        
SHEET    2  AD 2 ILE A1057  LYS A1059 -1  O  ARG A1058   N  ILE A1050           
SHEET    1  AE 2 ILE A1063  THR A1065  0                                        
SHEET    2  AE 2 ILE A1072  ASP A1075 -1  N  VAL A1073   O  GLU A1064           
SHEET    1  AF 3 GLU A1162  THR A1167  0                                        
SHEET    2  AF 3 VAL A1139  VAL A1145 -1  N  ALA A1140   O  ILE A1166           
SHEET    3  AF 3 LYS A1197  LEU A1198 -1  O  LEU A1198   N  SER A1142           
SHEET    1  AG 5 GLU A1219  LYS A1222  0                                        
SHEET    2  AG 5 ARG A1210  SER A1216 -1  O  MET A1213   N  GLN A1221           
SHEET    3  AG 5 SER A1202  LEU A1206 -1  O  SER A1202   N  LEU A1214           
SHEET    4  AG 5 THR A1346  GLN A1350 -1  O  THR A1346   N  GLU A1205           
SHEET    5  AG 5 GLU A1357  ILE A1360 -1  O  THR A1358   N  HIS A1349           
SHEET    1  AH 2 PHE A1324  TYR A1326  0                                        
SHEET    2  AH 2 THR A1329  ILE A1331 -1  O  THR A1329   N  TYR A1326           
SHEET    1  BA 6 LYS B 954  THR B 957  0                                        
SHEET    2  BA 6 ASN B 758  GLU B 762  1  O  ILE B 759   N  ILE B 956           
SHEET    3  BA 6 SER B   6  ILE B  11  1  O  ILE B   7   N  VAL B 760           
SHEET    4  BA 6 SER B  15  ILE B  21 -1  O  GLY B  17   N  ASP B  10           
SHEET    5  BA 6 ILE B  48  LEU B  52 -1  O  GLY B  49   N  TRP B  18           
SHEET    6  BA 6 ASN B1093  LYS B1096  1  O  ASN B1093   N  ALA B  50           
SHEET    1  BB 7 SER B  42  ASN B  46  0                                        
SHEET    2  BB 7 SER B  29  GLY B  36 -1  O  LYS B  30   N  LYS B  45           
SHEET    3  BB 7 GLU B1357  ASP B1361  1  O  GLU B1357   N  LEU B  35           
SHEET    4  BB 7 THR B1346  GLN B1350 -1  O  LEU B1347   N  ILE B1360           
SHEET    5  BB 7 SER B1202  LEU B1206 -1  O  LEU B1203   N  ILE B1348           
SHEET    6  BB 7 ARG B1210  LEU B1214 -1  O  ARG B1210   N  LEU B1206           
SHEET    7  BB 7 LEU B1220  LYS B1222 -1  O  GLN B1221   N  MET B1213           
SHEET    1  BC 2 ASP B 839  HIS B 840  0                                        
SHEET    2  BC 2 LYS B 855  VAL B 856 -1  O  VAL B 856   N  ASP B 839           
SHEET    1  BD 2 GLU B1049  THR B1051  0                                        
SHEET    2  BD 2 ILE B1057  LYS B1059 -1  O  ARG B1058   N  ILE B1050           
SHEET    1  BE 2 ILE B1063  THR B1065  0                                        
SHEET    2  BE 2 ILE B1072  ASP B1075 -1  N  VAL B1073   O  GLU B1064           
SHEET    1  BF 3 LYS B1161  THR B1167  0                                        
SHEET    2  BF 3 VAL B1139  VAL B1146 -1  N  ALA B1140   O  ILE B1166           
SHEET    3  BF 3 ILE B1196  LEU B1198 -1  O  ILE B1196   N  LEU B1144           
SHEET    1  BG 2 PHE B1324  TYR B1326  0                                        
SHEET    2  BG 2 THR B1329  ILE B1331 -1  O  THR B1329   N  TYR B1326           
LINK        MG    MG B2367                 O   HOH B2004     1555   1555  2.16  
LINK        MG    MG B2367                 OD2 ASP B 986     1555   1555  2.20  
SITE     1 AC1  5 ARG B  71  ARG B  74  ARG B  75  ARG B  78                    
SITE     2 AC1  5 ARG B 165                                                     
SITE     1 AC2  5 ARG A  74  ARG A  75  ARG A  78  ARG A 165                    
SITE     2 AC2  5 HOH A2013                                                     
SITE     1 AC3  5 TYR B 325  HIS B 328  HIS B 329  ARG B 403                    
SITE     2 AC3  5 HOH B2059                                                     
SITE     1 AC4  6 TYR A 325  HIS A 328  HIS A 329  ARG A 403                    
SITE     2 AC4  6 HOH A2041  HOH A2046                                          
SITE     1 AC5  4 GLY B1209  LYS B1211  ASN B1224  GLU B1225                    
SITE     1 AC6  4 ASP B  10  GLU B 762  ASP B 986  HOH B2004                    
CRYST1  159.780  209.620   91.260  90.00  90.00  90.00 P 21 21 2     8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.006259  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.004771  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010958        0.00000                         
MTRIX1   1  0.999750 -0.021970  0.004300       -1.20034    1                    
MTRIX2   1 -0.022100 -0.999270  0.031090     -157.83882    1                    
MTRIX3   1  0.003610 -0.031170 -0.999510       41.34232    1                    
ATOM      1  N   LYS A   4     -33.167 -43.253 -41.239  1.00 91.52           N  
ANISOU    1  N   LYS A   4    12075  12375  10325    762   -650  -1254       N  
ATOM      2  CA  LYS A   4     -33.384 -41.977 -41.910  1.00 75.18           C  
ANISOU    2  CA  LYS A   4     9988  10432   8145    815   -647  -1145       C  
ATOM      3  C   LYS A   4     -33.366 -40.821 -40.916  1.00 69.25           C  
ANISOU    3  C   LYS A   4     9212   9659   7440    867   -630   -993       C  
ATOM      4  O   LYS A   4     -33.247 -39.661 -41.312  1.00 78.60           O  
ANISOU    4  O   LYS A   4    10409  10901   8555    923   -600   -887       O  
ATOM      5  CB  LYS A   4     -34.715 -41.996 -42.668  1.00 74.80           C  
ANISOU    5  CB  LYS A   4     9898  10514   8007    771   -731  -1180       C  
ATOM      6  CG  LYS A   4     -34.998 -40.726 -43.468  1.00 89.38           C  
ANISOU    6  CG  LYS A   4    11735  12491   9733    844   -727  -1067       C  
ATOM      7  CD  LYS A   4     -36.291 -40.820 -44.262  1.00 88.36           C  
ANISOU    7  CD  LYS A   4    11555  12511   9506    810   -816  -1106       C  
ATOM      8  CE  LYS A   4     -36.597 -39.499 -44.957  1.00 86.58           C  
ANISOU    8  CE  LYS A   4    11322  12406   9168    906   -807   -978       C  
ATOM      9  NZ  LYS A   4     -37.866 -39.538 -45.732  1.00 92.24           N  
ANISOU    9  NZ  LYS A   4    11975  13291   9782    889   -899  -1005       N  
ATOM     10  HA  LYS A   4     -32.672 -41.833 -42.554  1.00 90.22           H  
ATOM     11  HB2 LYS A   4     -34.710 -42.741 -43.290  1.00 89.76           H  
ATOM     12  HB3 LYS A   4     -35.436 -42.109 -42.029  1.00 89.76           H  
ATOM     13  HG2 LYS A   4     -35.073 -39.976 -42.857  1.00107.25           H  
ATOM     14  HG3 LYS A   4     -34.271 -40.576 -44.092  1.00107.25           H  
ATOM     15  HD2 LYS A   4     -36.205 -41.509 -44.939  1.00106.03           H  
ATOM     16  HD3 LYS A   4     -37.024 -41.026 -43.661  1.00106.03           H  
ATOM     17  HE2 LYS A   4     -36.675 -38.801 -44.288  1.00103.90           H  
ATOM     18  HE3 LYS A   4     -35.876 -39.291 -45.571  1.00103.90           H  
ATOM     19  HZ1 LYS A   4     -38.548 -39.720 -45.190  1.00110.69           H  
ATOM     20  HZ2 LYS A   4     -38.009 -38.751 -46.122  1.00110.69           H  
ATOM     21  HZ3 LYS A   4     -37.820 -40.167 -46.360  1.00110.69           H  
ATOM     22  N   TYR A   5     -33.467 -41.138 -39.626  1.00 37.41           N  
ANISOU   22  N   TYR A   5     5158   5534   3522    847   -646   -984       N  
ATOM     23  CA  TYR A   5     -33.554 -40.107 -38.598  1.00 32.45           C  
ANISOU   23  CA  TYR A   5     4515   4879   2936    888   -634   -853       C  
ATOM     24  C   TYR A   5     -32.785 -40.482 -37.334  1.00 33.98           C  
ANISOU   24  C   TYR A   5     4723   4949   3241    888   -610   -849       C  
ATOM     25  O   TYR A   5     -32.406 -41.637 -37.131  1.00 30.69           O  
ANISOU   25  O   TYR A   5     4317   4460   2884    860   -612   -947       O  
ATOM     26  CB  TYR A   5     -35.020 -39.821 -38.249  1.00 28.08           C  
ANISOU   26  CB  TYR A   5     3897   4392   2379    876   -700   -817       C  
ATOM     27  CG  TYR A   5     -35.656 -40.866 -37.359  1.00 36.21           C  
ANISOU   27  CG  TYR A   5     4883   5381   3495    808   -758   -888       C  
ATOM     28  CD1 TYR A   5     -36.186 -42.035 -37.892  1.00 33.17           C  
ANISOU   28  CD1 TYR A   5     4477   5021   3105    721   -814  -1024       C  
ATOM     29  CD2 TYR A   5     -35.728 -40.682 -35.983  1.00 35.95           C  
ANISOU   29  CD2 TYR A   5     4836   5278   3544    821   -756   -825       C  
ATOM     30  CE1 TYR A   5     -36.769 -42.992 -37.079  1.00 37.85           C  
ANISOU   30  CE1 TYR A   5     5036   5564   3783    642   -867  -1094       C  
ATOM     31  CE2 TYR A   5     -36.311 -41.630 -35.163  1.00 37.50           C  
ANISOU   31  CE2 TYR A   5     4993   5440   3814    759   -811   -885       C  
ATOM     32  CZ  TYR A   5     -36.826 -42.784 -35.715  1.00 40.60           C  
ANISOU   32  CZ  TYR A   5     5366   5851   4211    665   -866  -1021       C  
ATOM     33  OH  TYR A   5     -37.404 -43.729 -34.897  1.00 40.56           O  
ANISOU   33  OH  TYR A   5     5326   5796   4290    584   -922  -1088       O  
ATOM     34  H   TYR A   5     -33.486 -41.942 -39.322  1.00 44.89           H  
ATOM     35  HA  TYR A   5     -33.169 -39.287 -38.946  1.00 38.94           H  
ATOM     36  HB2 TYR A   5     -35.071 -38.969 -37.787  1.00 33.69           H  
ATOM     37  HB3 TYR A   5     -35.534 -39.780 -39.070  1.00 33.69           H  
ATOM     38  HD1 TYR A   5     -36.147 -42.178 -38.810  1.00 39.80           H  
ATOM     39  HD2 TYR A   5     -35.380 -39.905 -35.607  1.00 43.14           H  
ATOM     40  HE1 TYR A   5     -37.119 -43.771 -37.448  1.00 45.42           H  
ATOM     41  HE2 TYR A   5     -36.349 -41.493 -34.244  1.00 45.00           H  
ATOM     42  HH  TYR A   5     -37.679 -44.377 -35.356  1.00 48.67           H  
ATOM     43  N   SER A   6     -32.550 -39.475 -36.498  1.00 26.37           N  
ANISOU   43  N   SER A   6     3767   3953   2298    923   -583   -735       N  
ATOM     44  CA  SER A   6     -31.941 -39.664 -35.188  1.00 21.85           C  
ANISOU   44  CA  SER A   6     3203   3285   1816    926   -572   -714       C  
ATOM     45  C   SER A   6     -32.693 -38.872 -34.122  1.00 21.95           C  
ANISOU   45  C   SER A   6     3200   3284   1856    937   -590   -619       C  
ATOM     46  O   SER A   6     -33.380 -37.891 -34.429  1.00 18.78           O  
ANISOU   46  O   SER A   6     2799   2934   1404    961   -584   -551       O  
ATOM     47  CB  SER A   6     -30.487 -39.208 -35.203  1.00 22.82           C  
ANISOU   47  CB  SER A   6     3363   3382   1927    951   -504   -680       C  
ATOM     48  OG  SER A   6     -29.703 -39.997 -36.078  1.00 28.08           O  
ANISOU   48  OG  SER A   6     4037   4060   2572    958   -471   -767       O  
ATOM     49  H   SER A   6     -32.740 -38.655 -36.673  1.00 31.64           H  
ATOM     50  HA  SER A   6     -31.967 -40.605 -34.950  1.00 26.23           H  
ATOM     51  HB2 SER A   6     -30.452 -38.284 -35.497  1.00 27.39           H  
ATOM     52  HB3 SER A   6     -30.126 -39.282 -34.305  1.00 27.39           H  
ATOM     53  HG  SER A   6     -28.907 -39.728 -36.071  1.00 33.70           H  
ATOM     54  N   ILE A   7     -32.529 -39.299 -32.871  1.00 21.81           N  
ANISOU   54  N   ILE A   7     3178   3195   1914    930   -605   -615       N  
ATOM     55  CA  ILE A   7     -33.177 -38.672 -31.726  1.00 23.24           C  
ANISOU   55  CA  ILE A   7     3348   3358   2124    941   -612   -531       C  
ATOM     56  C   ILE A   7     -32.140 -37.990 -30.834  1.00 26.06           C  
ANISOU   56  C   ILE A   7     3750   3649   2503    952   -570   -466       C  
ATOM     57  O   ILE A   7     -31.053 -38.528 -30.594  1.00 25.30           O  
ANISOU   57  O   ILE A   7     3665   3518   2430    949   -564   -500       O  
ATOM     58  CB  ILE A   7     -33.947 -39.709 -30.870  1.00 27.26           C  
ANISOU   58  CB  ILE A   7     3814   3853   2691    917   -674   -569       C  
ATOM     59  CG1 ILE A   7     -34.978 -40.460 -31.724  1.00 30.78           C  
ANISOU   59  CG1 ILE A   7     4209   4373   3115    874   -730   -654       C  
ATOM     60  CG2 ILE A   7     -34.619 -39.026 -29.674  1.00 21.88           C  
ANISOU   60  CG2 ILE A   7     3115   3166   2032    935   -665   -470       C  
ATOM     61  CD1 ILE A   7     -35.784 -41.522 -30.963  1.00 30.94           C  
ANISOU   61  CD1 ILE A   7     4173   4368   3214    812   -781   -690       C  
ATOM     62  H   ILE A   7     -32.034 -39.969 -32.657  1.00 26.17           H  
ATOM     63  HA  ILE A   7     -33.805 -38.001 -32.037  1.00 27.89           H  
ATOM     64  HB  ILE A   7     -33.308 -40.355 -30.529  1.00 32.71           H  
ATOM     65 HG12 ILE A   7     -35.607 -39.817 -32.086  1.00 36.94           H  
ATOM     66 HG13 ILE A   7     -34.513 -40.907 -32.449  1.00 36.94           H  
ATOM     67 HG21 ILE A   7     -35.242 -38.358 -30.002  1.00 26.25           H  
ATOM     68 HG22 ILE A   7     -35.094 -39.695 -29.155  1.00 26.25           H  
ATOM     69 HG23 ILE A   7     -33.938 -38.605 -29.128  1.00 26.25           H  
ATOM     70 HD11 ILE A   7     -36.269 -41.093 -30.241  1.00 37.13           H  
ATOM     71 HD12 ILE A   7     -36.407 -41.944 -31.576  1.00 37.13           H  
ATOM     72 HD13 ILE A   7     -35.173 -42.185 -30.604  1.00 37.13           H  
ATOM     73  N   GLY A   8     -32.494 -36.806 -30.339  1.00 20.48           N  
ANISOU   73  N   GLY A   8     3069   2928   1783    965   -540   -384       N  
ATOM     74  CA  GLY A   8     -31.685 -36.089 -29.371  1.00 15.03           C  
ANISOU   74  CA  GLY A   8     2427   2176   1108    954   -509   -333       C  
ATOM     75  C   GLY A   8     -32.426 -35.987 -28.055  1.00 14.96           C  
ANISOU   75  C   GLY A   8     2406   2138   1141    959   -515   -295       C  
ATOM     76  O   GLY A   8     -33.636 -35.718 -28.049  1.00 19.55           O  
ANISOU   76  O   GLY A   8     2966   2750   1711    986   -514   -275       O  
ATOM     77  H   GLY A   8     -33.216 -36.393 -30.556  1.00 24.57           H  
ATOM     78  HA2 GLY A   8     -30.848 -36.557 -29.226  1.00 18.04           H  
ATOM     79  HA3 GLY A   8     -31.494 -35.195 -29.696  1.00 18.04           H  
ATOM     80  N   LEU A   9     -31.702 -36.202 -26.955  1.00 16.30           N  
ANISOU   80  N   LEU A   9     2580   2265   1348    937   -518   -283       N  
ATOM     81  CA  LEU A   9     -32.284 -36.215 -25.614  1.00 21.65           C  
ANISOU   81  CA  LEU A   9     3246   2922   2059    937   -516   -246       C  
ATOM     82  C   LEU A   9     -31.501 -35.403 -24.580  1.00 19.08           C  
ANISOU   82  C   LEU A   9     2972   2553   1722    914   -496   -215       C  
ATOM     83  O   LEU A   9     -30.303 -35.629 -24.365  1.00 18.39           O  
ANISOU   83  O   LEU A   9     2882   2463   1641    884   -512   -224       O  
ATOM     84  CB  LEU A   9     -32.396 -37.653 -25.110  1.00 23.04           C  
ANISOU   84  CB  LEU A   9     3360   3101   2294    933   -558   -259       C  
ATOM     85  CG  LEU A   9     -33.359 -38.569 -25.862  1.00 22.80           C  
ANISOU   85  CG  LEU A   9     3279   3111   2271    945   -604   -299       C  
ATOM     86  CD1 LEU A   9     -33.206 -39.996 -25.365  1.00 19.23           C  
ANISOU   86  CD1 LEU A   9     2785   2613   1908    926   -630   -311       C  
ATOM     87  CD2 LEU A   9     -34.798 -38.099 -25.704  1.00 19.35           C  
ANISOU   87  CD2 LEU A   9     2811   2728   1815    955   -592   -265       C  
ATOM     88  H   LEU A   9     -30.854 -36.345 -26.962  1.00 19.56           H  
ATOM     89  HA  LEU A   9     -33.181 -35.847 -25.660  1.00 25.98           H  
ATOM     90  HB2 LEU A   9     -31.516 -38.060 -25.159  1.00 27.65           H  
ATOM     91  HB3 LEU A   9     -32.686 -37.629 -24.185  1.00 27.65           H  
ATOM     92  HG  LEU A   9     -33.139 -38.554 -26.806  1.00 27.35           H  
ATOM     93 HD11 LEU A   9     -33.407 -40.023 -24.416  1.00 23.07           H  
ATOM     94 HD12 LEU A   9     -33.823 -40.566 -25.850  1.00 23.07           H  
ATOM     95 HD13 LEU A   9     -32.294 -40.287 -25.520  1.00 23.07           H  
ATOM     96 HD21 LEU A   9     -34.877 -37.200 -26.060  1.00 23.23           H  
ATOM     97 HD22 LEU A   9     -35.382 -38.701 -26.192  1.00 23.23           H  
ATOM     98 HD23 LEU A   9     -35.030 -38.104 -24.762  1.00 23.23           H  
ATOM     99  N   ASP A  10     -32.210 -34.482 -23.926  1.00 30.52           N  
ANISOU   99  N   ASP A  10     4466   3982   3147    934   -467   -186       N  
ATOM    100  CA  ASP A  10     -31.674 -33.711 -22.805  1.00 27.32           C  
ANISOU  100  CA  ASP A  10     4124   3536   2719    915   -458   -170       C  
ATOM    101  C   ASP A  10     -32.415 -34.118 -21.534  1.00 26.48           C  
ANISOU  101  C   ASP A  10     3983   3446   2632    933   -452   -148       C  
ATOM    102  O   ASP A  10     -33.624 -33.934 -21.435  1.00 35.85           O  
ANISOU  102  O   ASP A  10     5161   4652   3807    982   -426   -133       O  
ATOM    103  CB  ASP A  10     -31.861 -32.215 -23.052  1.00 26.06           C  
ANISOU  103  CB  ASP A  10     4082   3324   2498    941   -426   -159       C  
ATOM    104  CG  ASP A  10     -30.785 -31.377 -22.392  1.00 39.27           C  
ANISOU  104  CG  ASP A  10     5851   4945   4125    882   -434   -164       C  
ATOM    105  OD1 ASP A  10     -29.594 -31.622 -22.673  1.00 39.08           O  
ANISOU  105  OD1 ASP A  10     5809   4943   4096    810   -459   -180       O  
ATOM    106  OD2 ASP A  10     -31.128 -30.478 -21.593  1.00 35.69           O  
ANISOU  106  OD2 ASP A  10     5493   4438   3631    906   -416   -159       O  
ATOM    107  H   ASP A  10     -33.023 -34.281 -24.119  1.00 36.62           H  
ATOM    108  HA  ASP A  10     -30.729 -33.897 -22.694  1.00 32.78           H  
ATOM    109  HB2 ASP A  10     -31.831 -32.046 -24.006  1.00 31.28           H  
ATOM    110  HB3 ASP A  10     -32.719 -31.940 -22.692  1.00 31.28           H  
ATOM    111  N   ILE A  11     -31.681 -34.649 -20.562  1.00 23.27           N  
ANISOU  111  N   ILE A  11     3552   3046   2243    899   -474   -139       N  
ATOM    112  CA  ILE A  11     -32.279 -35.308 -19.405  1.00 20.77           C  
ANISOU  112  CA  ILE A  11     3191   2757   1945    913   -468   -104       C  
ATOM    113  C   ILE A  11     -31.967 -34.596 -18.089  1.00 26.98           C  
ANISOU  113  C   ILE A  11     4034   3537   2679    911   -464    -95       C  
ATOM    114  O   ILE A  11     -30.806 -34.469 -17.708  1.00 27.01           O  
ANISOU  114  O   ILE A  11     4052   3545   2667    866   -496   -104       O  
ATOM    115  CB  ILE A  11     -31.786 -36.766 -19.342  1.00 27.94           C  
ANISOU  115  CB  ILE A  11     4019   3682   2916    893   -498    -86       C  
ATOM    116  CG1 ILE A  11     -32.138 -37.474 -20.656  1.00 23.62           C  
ANISOU  116  CG1 ILE A  11     3435   3133   2408    901   -513   -112       C  
ATOM    117  CG2 ILE A  11     -32.369 -37.494 -18.124  1.00 16.54           C  
ANISOU  117  CG2 ILE A  11     2536   2259   1489    905   -487    -28       C  
ATOM    118  CD1 ILE A  11     -31.555 -38.867 -20.795  1.00 26.44           C  
ANISOU  118  CD1 ILE A  11     3739   3476   2830    905   -545   -108       C  
ATOM    119  H   ILE A  11     -30.821 -34.640 -20.549  1.00 27.92           H  
ATOM    120  HA  ILE A  11     -33.242 -35.323 -19.516  1.00 24.93           H  
ATOM    121  HB  ILE A  11     -30.820 -36.755 -19.254  1.00 33.53           H  
ATOM    122 HG12 ILE A  11     -33.102 -37.551 -20.719  1.00 28.35           H  
ATOM    123 HG13 ILE A  11     -31.804 -36.940 -21.395  1.00 28.35           H  
ATOM    124 HG21 ILE A  11     -33.337 -37.492 -18.189  1.00 19.85           H  
ATOM    125 HG22 ILE A  11     -32.040 -38.406 -18.115  1.00 19.85           H  
ATOM    126 HG23 ILE A  11     -32.090 -37.032 -17.318  1.00 19.85           H  
ATOM    127 HD11 ILE A  11     -31.889 -39.422 -20.073  1.00 31.73           H  
ATOM    128 HD12 ILE A  11     -31.825 -39.238 -21.650  1.00 31.73           H  
ATOM    129 HD13 ILE A  11     -30.588 -38.810 -20.750  1.00 31.73           H  
ATOM    130  N   GLY A  12     -33.016 -34.151 -17.396  1.00 21.56           N  
ANISOU  130  N   GLY A  12     3377   2858   1958    964   -428    -79       N  
ATOM    131  CA  GLY A  12     -32.876 -33.465 -16.121  1.00 16.80           C  
ANISOU  131  CA  GLY A  12     2841   2250   1291    978   -422    -79       C  
ATOM    132  C   GLY A  12     -33.806 -34.006 -15.047  1.00 25.83           C  
ANISOU  132  C   GLY A  12     3941   3449   2422   1025   -392    -33       C  
ATOM    133  O   GLY A  12     -34.528 -34.980 -15.267  1.00 23.14           O  
ANISOU  133  O   GLY A  12     3513   3148   2130   1032   -380      9       O  
ATOM    134  H   GLY A  12     -33.833 -34.238 -17.653  1.00 25.88           H  
ATOM    135  HA2 GLY A  12     -31.963 -33.555 -15.807  1.00 20.16           H  
ATOM    136  HA3 GLY A  12     -33.066 -32.521 -16.241  1.00 20.16           H  
ATOM    137  N   THR A  13     -33.787 -33.361 -13.883  1.00 24.03           N  
ANISOU  137  N   THR A  13     3783   3226   2122   1054   -382    -37       N  
ATOM    138  CA  THR A  13     -34.545 -33.816 -12.720  1.00 28.87           C  
ANISOU  138  CA  THR A  13     4363   3903   2703   1103   -350     12       C  
ATOM    139  C   THR A  13     -36.013 -33.393 -12.748  1.00 27.25           C  
ANISOU  139  C   THR A  13     4164   3721   2468   1205   -286     28       C  
ATOM    140  O   THR A  13     -36.826 -33.936 -12.000  1.00 31.04           O  
ANISOU  140  O   THR A  13     4589   4275   2930   1248   -250     85       O  
ATOM    141  CB  THR A  13     -33.925 -33.280 -11.416  1.00 37.39           C  
ANISOU  141  CB  THR A  13     5515   4995   3698   1098   -366     -5       C  
ATOM    142  OG1 THR A  13     -33.656 -31.880 -11.553  1.00 43.20           O  
ANISOU  142  OG1 THR A  13     6383   5655   4375   1103   -371    -73       O  
ATOM    143  CG2 THR A  13     -32.631 -34.009 -11.099  1.00 32.26           C  
ANISOU  143  CG2 THR A  13     4812   4379   3066   1011   -427      9       C  
ATOM    144  H   THR A  13     -33.335 -32.644 -13.739  1.00 28.84           H  
ATOM    145  HA  THR A  13     -34.516 -34.785 -12.687  1.00 34.64           H  
ATOM    146  HB  THR A  13     -34.544 -33.419 -10.682  1.00 44.87           H  
ATOM    147  HG1 THR A  13     -33.317 -31.581 -10.845  1.00 51.84           H  
ATOM    148 HG21 THR A  13     -31.994 -33.883 -11.819  1.00 38.71           H  
ATOM    149 HG22 THR A  13     -32.249 -33.664 -10.276  1.00 38.71           H  
ATOM    150 HG23 THR A  13     -32.803 -34.958 -10.993  1.00 38.71           H  
ATOM    151  N   ASN A  14     -36.347 -32.415 -13.586  1.00 35.78           N  
ANISOU  151  N   ASN A  14     5309   4750   3534   1252   -269    -13       N  
ATOM    152  CA  ASN A  14     -37.738 -31.986 -13.743  1.00 39.15           C  
ANISOU  152  CA  ASN A  14     5728   5219   3927   1367   -207      6       C  
ATOM    153  C   ASN A  14     -38.152 -31.771 -15.200  1.00 42.67           C  
ANISOU  153  C   ASN A  14     6149   5659   4407   1375   -205     -7       C  
ATOM    154  O   ASN A  14     -39.265 -31.314 -15.470  1.00 47.06           O  
ANISOU  154  O   ASN A  14     6693   6265   4925   1474   -157      9       O  
ATOM    155  CB  ASN A  14     -38.017 -30.724 -12.915  1.00 37.33           C  
ANISOU  155  CB  ASN A  14     5637   4945   3602   1485   -166    -19       C  
ATOM    156  CG  ASN A  14     -37.208 -29.521 -13.373  1.00 49.45           C  
ANISOU  156  CG  ASN A  14     7331   6341   5117   1476   -193    -73       C  
ATOM    157  OD1 ASN A  14     -36.425 -29.602 -14.320  1.00 58.05           O  
ANISOU  157  OD1 ASN A  14     8417   7384   6256   1385   -235    -92       O  
ATOM    158  ND2 ASN A  14     -37.403 -28.390 -12.702  1.00 52.03           N  
ANISOU  158  ND2 ASN A  14     7808   6597   5364   1565   -167    -87       N  
ATOM    159  H   ASN A  14     -35.788 -31.983 -14.077  1.00 42.93           H  
ATOM    160  HA  ASN A  14     -38.307 -32.688 -13.389  1.00 46.97           H  
ATOM    161  HB2 ASN A  14     -38.958 -30.498 -12.991  1.00 44.80           H  
ATOM    162  HB3 ASN A  14     -37.793 -30.899 -11.987  1.00 44.80           H  
ATOM    163 HD21 ASN A  14     -37.963 -28.369 -12.049  1.00 62.44           H  
ATOM    164 HD22 ASN A  14     -36.970 -27.680 -12.921  1.00 62.44           H  
ATOM    165  N   SER A  15     -37.260 -32.096 -16.132  1.00 26.24           N  
ANISOU  165  N   SER A  15     4053   3530   2385   1279   -255    -30       N  
ATOM    166  CA  SER A  15     -37.587 -32.025 -17.553  1.00 23.87           C  
ANISOU  166  CA  SER A  15     3721   3238   2112   1277   -260    -39       C  
ATOM    167  C   SER A  15     -36.851 -33.068 -18.396  1.00 26.43           C  
ANISOU  167  C   SER A  15     3969   3560   2513   1170   -314    -46       C  
ATOM    168  O   SER A  15     -35.802 -33.580 -18.004  1.00 29.33           O  
ANISOU  168  O   SER A  15     4337   3897   2910   1101   -347    -53       O  
ATOM    169  CB  SER A  15     -37.261 -30.639 -18.107  1.00 21.48           C  
ANISOU  169  CB  SER A  15     3560   2841   1761   1331   -243    -75       C  
ATOM    170  OG  SER A  15     -35.874 -30.375 -18.000  1.00 20.61           O  
ANISOU  170  OG  SER A  15     3533   2638   1659   1254   -284   -102       O  
ATOM    171  H   SER A  15     -36.458 -32.360 -15.968  1.00 31.48           H  
ATOM    172  HA  SER A  15     -38.539 -32.173 -17.663  1.00 28.65           H  
ATOM    173  HB2 SER A  15     -37.519 -30.603 -19.041  1.00 25.78           H  
ATOM    174  HB3 SER A  15     -37.750 -29.973 -17.600  1.00 25.78           H  
ATOM    175  HG  SER A  15     -35.438 -30.947 -18.434  1.00 24.73           H  
ATOM    176  N   VAL A  16     -37.422 -33.363 -19.561  1.00 18.51           N  
ANISOU  176  N   VAL A  16     2901   2599   1532   1170   -325    -44       N  
ATOM    177  CA  VAL A  16     -36.766 -34.174 -20.579  1.00 20.27           C  
ANISOU  177  CA  VAL A  16     3079   2813   1809   1097   -372    -66       C  
ATOM    178  C   VAL A  16     -37.002 -33.500 -21.922  1.00 25.44           C  
ANISOU  178  C   VAL A  16     3757   3472   2437   1130   -368    -86       C  
ATOM    179  O   VAL A  16     -38.131 -33.448 -22.409  1.00 23.60           O  
ANISOU  179  O   VAL A  16     3468   3316   2184   1178   -362    -68       O  
ATOM    180  CB  VAL A  16     -37.317 -35.618 -20.633  1.00 20.76           C  
ANISOU  180  CB  VAL A  16     3024   2938   1926   1062   -409    -40       C  
ATOM    181  CG1 VAL A  16     -36.775 -36.362 -21.853  1.00 17.95           C  
ANISOU  181  CG1 VAL A  16     2640   2571   1608   1017   -460    -81       C  
ATOM    182  CG2 VAL A  16     -36.961 -36.374 -19.374  1.00 14.67           C  
ANISOU  182  CG2 VAL A  16     2237   2153   1185   1035   -412     -3       C  
ATOM    183  H   VAL A  16     -38.208 -33.098 -19.788  1.00 22.21           H  
ATOM    184  HA  VAL A  16     -35.812 -34.209 -20.408  1.00 24.32           H  
ATOM    185  HB  VAL A  16     -38.284 -35.587 -20.704  1.00 24.91           H  
ATOM    186 HG11 VAL A  16     -35.807 -36.395 -21.797  1.00 21.54           H  
ATOM    187 HG12 VAL A  16     -37.137 -37.262 -21.860  1.00 21.54           H  
ATOM    188 HG13 VAL A  16     -37.045 -35.890 -22.656  1.00 21.54           H  
ATOM    189 HG21 VAL A  16     -37.346 -35.915 -18.611  1.00 17.61           H  
ATOM    190 HG22 VAL A  16     -37.318 -37.274 -19.435  1.00 17.61           H  
ATOM    191 HG23 VAL A  16     -35.995 -36.405 -19.288  1.00 17.61           H  
ATOM    192  N   GLY A  17     -35.939 -32.963 -22.507  1.00 21.12           N  
ANISOU  192  N   GLY A  17     3287   2855   1882   1107   -374   -113       N  
ATOM    193  CA  GLY A  17     -36.023 -32.353 -23.817  1.00 16.63           C  
ANISOU  193  CA  GLY A  17     2749   2287   1283   1138   -368   -119       C  
ATOM    194  C   GLY A  17     -35.771 -33.398 -24.882  1.00 31.01           C  
ANISOU  194  C   GLY A  17     4492   4153   3137   1089   -412   -144       C  
ATOM    195  O   GLY A  17     -34.946 -34.295 -24.685  1.00 32.71           O  
ANISOU  195  O   GLY A  17     4681   4351   3397   1029   -443   -165       O  
ATOM    196  H   GLY A  17     -35.153 -32.942 -22.160  1.00 25.34           H  
ATOM    197  HA2 GLY A  17     -36.905 -31.971 -23.950  1.00 19.96           H  
ATOM    198  HA3 GLY A  17     -35.359 -31.651 -23.900  1.00 19.96           H  
ATOM    199  N   TRP A  18     -36.487 -33.295 -26.000  1.00 23.35           N  
ANISOU  199  N   TRP A  18     3488   3247   2136   1126   -418   -144       N  
ATOM    200  CA  TRP A  18     -36.313 -34.234 -27.103  1.00 20.77           C  
ANISOU  200  CA  TRP A  18     3101   2970   1821   1089   -465   -182       C  
ATOM    201  C   TRP A  18     -36.385 -33.566 -28.470  1.00 24.65           C  
ANISOU  201  C   TRP A  18     3621   3493   2253   1128   -457   -179       C  
ATOM    202  O   TRP A  18     -37.113 -32.578 -28.658  1.00 26.12           O  
ANISOU  202  O   TRP A  18     3834   3700   2389   1201   -425   -140       O  
ATOM    203  CB  TRP A  18     -37.361 -35.346 -27.036  1.00 15.86           C  
ANISOU  203  CB  TRP A  18     2364   2439   1221   1073   -513   -194       C  
ATOM    204  CG  TRP A  18     -38.785 -34.855 -27.030  1.00 22.79           C  
ANISOU  204  CG  TRP A  18     3187   3411   2059   1134   -502   -154       C  
ATOM    205  CD1 TRP A  18     -39.533 -34.522 -25.935  1.00 18.17           C  
ANISOU  205  CD1 TRP A  18     2585   2845   1474   1173   -469   -108       C  
ATOM    206  CD2 TRP A  18     -39.632 -34.653 -28.169  1.00 24.53           C  
ANISOU  206  CD2 TRP A  18     3355   3741   2226   1171   -523   -155       C  
ATOM    207  NE1 TRP A  18     -40.789 -34.124 -26.322  1.00 21.46           N  
ANISOU  207  NE1 TRP A  18     2936   3376   1842   1239   -465    -78       N  
ATOM    208  CE2 TRP A  18     -40.877 -34.194 -27.690  1.00 26.88           C  
ANISOU  208  CE2 TRP A  18     3596   4121   2495   1237   -502   -105       C  
ATOM    209  CE3 TRP A  18     -39.460 -34.812 -29.549  1.00 22.28           C  
ANISOU  209  CE3 TRP A  18     3061   3502   1904   1161   -556   -193       C  
ATOM    210  CZ2 TRP A  18     -41.942 -33.894 -28.538  1.00 26.51           C  
ANISOU  210  CZ2 TRP A  18     3477   4207   2389   1294   -518    -87       C  
ATOM    211  CZ3 TRP A  18     -40.520 -34.511 -30.391  1.00 25.28           C  
ANISOU  211  CZ3 TRP A  18     3376   4010   2220   1210   -575   -177       C  
ATOM    212  CH2 TRP A  18     -41.744 -34.059 -29.882  1.00 27.01           C  
ANISOU  212  CH2 TRP A  18     3532   4315   2416   1276   -559   -123       C  
ATOM    213  H   TRP A  18     -37.080 -32.689 -26.144  1.00 28.02           H  
ATOM    214  HA  TRP A  18     -35.439 -34.648 -27.023  1.00 24.92           H  
ATOM    215  HB2 TRP A  18     -37.252 -35.924 -27.807  1.00 19.03           H  
ATOM    216  HB3 TRP A  18     -37.222 -35.856 -26.222  1.00 19.03           H  
ATOM    217  HD1 TRP A  18     -39.235 -34.561 -25.055  1.00 21.80           H  
ATOM    218  HE1 TRP A  18     -41.418 -33.871 -25.793  1.00 25.75           H  
ATOM    219  HE3 TRP A  18     -38.651 -35.113 -29.894  1.00 26.74           H  
ATOM    220  HZ2 TRP A  18     -42.756 -33.592 -28.203  1.00 31.81           H  
ATOM    221  HZ3 TRP A  18     -40.417 -34.615 -31.310  1.00 30.34           H  
ATOM    222  HH2 TRP A  18     -42.438 -33.865 -30.471  1.00 32.41           H  
ATOM    223  N   ALA A  19     -35.622 -34.109 -29.419  1.00 23.34           N  
ANISOU  223  N   ALA A  19     3450   3335   2082   1090   -481   -219       N  
ATOM    224  CA  ALA A  19     -35.725 -33.675 -30.816  1.00 18.26           C  
ANISOU  224  CA  ALA A  19     2820   2745   1372   1122   -478   -216       C  
ATOM    225  C   ALA A  19     -35.518 -34.814 -31.817  1.00 16.82           C  
ANISOU  225  C   ALA A  19     2580   2627   1182   1079   -526   -286       C  
ATOM    226  O   ALA A  19     -34.744 -35.736 -31.568  1.00 22.95           O  
ANISOU  226  O   ALA A  19     3348   3369   2004   1028   -545   -337       O  
ATOM    227  CB  ALA A  19     -34.731 -32.561 -31.092  1.00 17.02           C  
ANISOU  227  CB  ALA A  19     2777   2511   1177   1134   -429   -177       C  
ATOM    228  H   ALA A  19     -35.040 -34.728 -29.283  1.00 28.00           H  
ATOM    229  HA  ALA A  19     -36.614 -33.316 -30.962  1.00 21.91           H  
ATOM    230  HB1 ALA A  19     -33.834 -32.890 -30.923  1.00 20.42           H  
ATOM    231  HB2 ALA A  19     -34.813 -32.287 -32.019  1.00 20.42           H  
ATOM    232  HB3 ALA A  19     -34.925 -31.812 -30.507  1.00 20.42           H  
ATOM    233  N   VAL A  20     -36.209 -34.734 -32.953  1.00 25.08           N  
ANISOU  233  N   VAL A  20     3593   3771   2164   1106   -545   -293       N  
ATOM    234  CA  VAL A  20     -36.027 -35.681 -34.050  1.00 23.97           C  
ANISOU  234  CA  VAL A  20     3416   3698   1994   1066   -586   -372       C  
ATOM    235  C   VAL A  20     -35.288 -34.967 -35.170  1.00 30.27           C  
ANISOU  235  C   VAL A  20     4282   4503   2718   1093   -546   -348       C  
ATOM    236  O   VAL A  20     -35.574 -33.804 -35.466  1.00 27.47           O  
ANISOU  236  O   VAL A  20     3972   4157   2310   1157   -513   -272       O  
ATOM    237  CB  VAL A  20     -37.370 -36.215 -34.584  1.00 23.44           C  
ANISOU  237  CB  VAL A  20     3253   3761   1890   1059   -650   -408       C  
ATOM    238  CG1 VAL A  20     -37.150 -37.128 -35.789  1.00 22.06           C  
ANISOU  238  CG1 VAL A  20     3061   3649   1671   1008   -690   -506       C  
ATOM    239  CG2 VAL A  20     -38.110 -36.956 -33.493  1.00 20.23           C  
ANISOU  239  CG2 VAL A  20     2775   3362   1551   1020   -691   -425       C  
ATOM    240  H   VAL A  20     -36.800 -34.130 -33.114  1.00 30.09           H  
ATOM    241  HA  VAL A  20     -35.490 -36.431 -33.750  1.00 28.77           H  
ATOM    242  HB  VAL A  20     -37.919 -35.468 -34.868  1.00 28.12           H  
ATOM    243 HG11 VAL A  20     -36.596 -37.878 -35.519  1.00 26.47           H  
ATOM    244 HG12 VAL A  20     -38.011 -37.449 -36.103  1.00 26.47           H  
ATOM    245 HG13 VAL A  20     -36.708 -36.625 -36.490  1.00 26.47           H  
ATOM    246 HG21 VAL A  20     -38.277 -36.347 -32.756  1.00 24.28           H  
ATOM    247 HG22 VAL A  20     -38.951 -37.284 -33.849  1.00 24.28           H  
ATOM    248 HG23 VAL A  20     -37.566 -37.700 -33.191  1.00 24.28           H  
ATOM    249  N   ILE A  21     -34.347 -35.665 -35.798  1.00 41.97           N  
ANISOU  249  N   ILE A  21     5775   5982   4190   1052   -544   -413       N  
ATOM    250  CA  ILE A  21     -33.471 -35.036 -36.783  1.00 40.43           C  
ANISOU  250  CA  ILE A  21     5645   5797   3919   1070   -495   -386       C  
ATOM    251  C   ILE A  21     -33.221 -35.913 -38.007  1.00 44.81           C  
ANISOU  251  C   ILE A  21     6178   6430   4418   1047   -510   -473       C  
ATOM    252  O   ILE A  21     -33.082 -37.127 -37.888  1.00 48.85           O  
ANISOU  252  O   ILE A  21     6654   6932   4975   1002   -540   -571       O  
ATOM    253  CB  ILE A  21     -32.130 -34.651 -36.122  1.00 37.80           C  
ANISOU  253  CB  ILE A  21     5375   5369   3620   1046   -440   -355       C  
ATOM    254  CG1 ILE A  21     -32.271 -33.294 -35.437  1.00 41.76           C  
ANISOU  254  CG1 ILE A  21     5946   5802   4119   1077   -405   -256       C  
ATOM    255  CG2 ILE A  21     -30.992 -34.615 -37.135  1.00 44.14           C  
ANISOU  255  CG2 ILE A  21     6215   6203   4352   1035   -391   -369       C  
ATOM    256  CD1 ILE A  21     -31.130 -32.972 -34.533  1.00 60.48           C  
ANISOU  256  CD1 ILE A  21     8370   8084   6524   1032   -370   -236       C  
ATOM    257  H   ILE A  21     -34.195 -36.502 -35.673  1.00 50.37           H  
ATOM    258  HA  ILE A  21     -33.891 -34.218 -37.091  1.00 48.51           H  
ATOM    259  HB  ILE A  21     -31.919 -35.315 -35.448  1.00 45.37           H  
ATOM    260 HG12 ILE A  21     -32.320 -32.602 -36.115  1.00 50.11           H  
ATOM    261 HG13 ILE A  21     -33.083 -33.293 -34.905  1.00 50.11           H  
ATOM    262 HG21 ILE A  21     -31.199 -33.959 -37.819  1.00 52.96           H  
ATOM    263 HG22 ILE A  21     -30.172 -34.370 -36.678  1.00 52.96           H  
ATOM    264 HG23 ILE A  21     -30.898 -35.494 -37.535  1.00 52.96           H  
ATOM    265 HD11 ILE A  21     -30.311 -32.959 -35.052  1.00 72.57           H  
ATOM    266 HD12 ILE A  21     -31.281 -32.102 -34.132  1.00 72.57           H  
ATOM    267 HD13 ILE A  21     -31.074 -33.650 -33.842  1.00 72.57           H  
ATOM    268  N   THR A  22     -33.159 -35.281 -39.178  1.00 37.81           N  
ANISOU  268  N   THR A  22     5326   5612   3427   1083   -486   -440       N  
ATOM    269  CA  THR A  22     -32.874 -35.982 -40.428  1.00 39.98           C  
ANISOU  269  CA  THR A  22     5596   5969   3628   1068   -490   -520       C  
ATOM    270  C   THR A  22     -31.390 -35.885 -40.777  1.00 45.79           C  
ANISOU  270  C   THR A  22     6387   6675   4337   1061   -413   -518       C  
ATOM    271  O   THR A  22     -30.583 -35.420 -39.972  1.00 38.74           O  
ANISOU  271  O   THR A  22     5525   5704   3491   1052   -367   -468       O  
ATOM    272  CB  THR A  22     -33.712 -35.426 -41.601  1.00 34.71           C  
ANISOU  272  CB  THR A  22     4926   5422   2840   1116   -512   -486       C  
ATOM    273  OG1 THR A  22     -33.364 -34.056 -41.845  1.00 41.92           O  
ANISOU  273  OG1 THR A  22     5913   6320   3696   1176   -450   -363       O  
ATOM    274  CG2 THR A  22     -35.202 -35.530 -41.294  1.00 30.89           C  
ANISOU  274  CG2 THR A  22     4367   4999   2371   1126   -587   -488       C  
ATOM    275  H   THR A  22     -33.281 -34.435 -39.276  1.00 45.37           H  
ATOM    276  HA  THR A  22     -33.095 -36.920 -40.320  1.00 47.98           H  
ATOM    277  HB  THR A  22     -33.531 -35.948 -42.398  1.00 41.65           H  
ATOM    278  HG1 THR A  22     -33.819 -33.753 -42.483  1.00 50.31           H  
ATOM    279 HG21 THR A  22     -35.411 -35.021 -40.495  1.00 37.07           H  
ATOM    280 HG22 THR A  22     -35.718 -35.178 -42.036  1.00 37.07           H  
ATOM    281 HG23 THR A  22     -35.446 -36.457 -41.151  1.00 37.07           H  
ATOM    282  N   ASP A  23     -31.038 -36.327 -41.981  1.00 83.07           N  
ANISOU  282  N   ASP A  23    11117  11473   8972   1063   -396   -578       N  
ATOM    283  CA  ASP A  23     -29.644 -36.393 -42.407  1.00 88.14           C  
ANISOU  283  CA  ASP A  23    11795  12115   9580   1062   -314   -590       C  
ATOM    284  C   ASP A  23     -28.986 -35.016 -42.466  1.00 81.24           C  
ANISOU  284  C   ASP A  23    10986  11234   8649   1081   -238   -460       C  
ATOM    285  O   ASP A  23     -27.809 -34.876 -42.132  1.00 90.49           O  
ANISOU  285  O   ASP A  23    12174  12376   9833   1062   -169   -444       O  
ATOM    286  CB  ASP A  23     -29.548 -37.078 -43.771  1.00 98.18           C  
ANISOU  286  CB  ASP A  23    13071  13481  10753   1070   -307   -678       C  
ATOM    287  CG  ASP A  23     -28.121 -37.418 -44.154  1.00100.57           C  
ANISOU  287  CG  ASP A  23    13393  13790  11030   1077   -215   -714       C  
ATOM    288  OD1 ASP A  23     -27.413 -36.526 -44.669  1.00 95.78           O  
ANISOU  288  OD1 ASP A  23    12825  13228  10339   1097   -138   -629       O  
ATOM    289  OD2 ASP A  23     -27.709 -38.578 -43.943  1.00100.98           O  
ANISOU  289  OD2 ASP A  23    13423  13802  11145   1066   -213   -824       O  
ATOM    290  H   ASP A  23     -31.596 -36.597 -42.577  1.00 99.68           H  
ATOM    291  HA  ASP A  23     -29.149 -36.931 -41.770  1.00105.77           H  
ATOM    292  HB2 ASP A  23     -30.058 -37.903 -43.748  1.00117.82           H  
ATOM    293  HB3 ASP A  23     -29.908 -36.484 -44.449  1.00117.82           H  
ATOM    294  N   GLU A  24     -29.745 -34.006 -42.883  1.00 53.12           N  
ANISOU  294  N   GLU A  24     7460   7702   5020   1120   -248   -369       N  
ATOM    295  CA  GLU A  24     -29.230 -32.640 -42.972  1.00 55.64           C  
ANISOU  295  CA  GLU A  24     7866   7993   5281   1135   -172   -238       C  
ATOM    296  C   GLU A  24     -29.622 -31.805 -41.753  1.00 52.90           C  
ANISOU  296  C   GLU A  24     7553   7534   5010   1136   -183   -161       C  
ATOM    297  O   GLU A  24     -29.702 -30.578 -41.824  1.00 46.64           O  
ANISOU  297  O   GLU A  24     6849   6702   4171   1166   -140    -49       O  
ATOM    298  CB  GLU A  24     -29.720 -31.969 -44.258  1.00 58.81           C  
ANISOU  298  CB  GLU A  24     8309   8485   5549   1195   -160   -174       C  
ATOM    299  CG  GLU A  24     -28.746 -32.056 -45.412  1.00 63.59           C  
ANISOU  299  CG  GLU A  24     8943   9173   6043   1190    -84   -179       C  
ATOM    300  CD  GLU A  24     -28.441 -30.701 -46.027  1.00 71.87           C  
ANISOU  300  CD  GLU A  24    10093  10227   6987   1219     -2    -31       C  
ATOM    301  OE1 GLU A  24     -29.396 -29.959 -46.342  1.00 73.11           O  
ANISOU  301  OE1 GLU A  24    10285  10394   7100   1286    -32     46       O  
ATOM    302  OE2 GLU A  24     -27.246 -30.380 -46.194  1.00 71.79           O  
ANISOU  302  OE2 GLU A  24    10127  10213   6937   1177    101     12       O  
ATOM    303  H   GLU A  24     -30.567 -34.086 -43.123  1.00 63.74           H  
ATOM    304  HA  GLU A  24     -28.262 -32.675 -43.007  1.00 66.77           H  
ATOM    305  HB2 GLU A  24     -30.546 -32.394 -44.536  1.00 70.57           H  
ATOM    306  HB3 GLU A  24     -29.880 -31.029 -44.077  1.00 70.57           H  
ATOM    307  HG2 GLU A  24     -27.912 -32.436 -45.094  1.00 76.30           H  
ATOM    308  HG3 GLU A  24     -29.125 -32.621 -46.104  1.00 76.30           H  
ATOM    309  N   TYR A  25     -29.865 -32.483 -40.635  1.00 36.33           N  
ANISOU  309  N   TYR A  25     5397   5378   3027   1107   -235   -221       N  
ATOM    310  CA  TYR A  25     -30.102 -31.816 -39.359  1.00 34.44           C  
ANISOU  310  CA  TYR A  25     5191   5031   2863   1102   -240   -165       C  
ATOM    311  C   TYR A  25     -31.402 -31.017 -39.332  1.00 28.90           C  
ANISOU  311  C   TYR A  25     4509   4323   2148   1175   -267    -99       C  
ATOM    312  O   TYR A  25     -31.570 -30.130 -38.497  1.00 33.10           O  
ANISOU  312  O   TYR A  25     5106   4760   2711   1192   -247    -34       O  
ATOM    313  CB  TYR A  25     -28.916 -30.917 -39.011  1.00 34.50           C  
ANISOU  313  CB  TYR A  25     5295   4970   2844   1059   -159    -96       C  
ATOM    314  CG  TYR A  25     -27.591 -31.621 -39.172  1.00 37.04           C  
ANISOU  314  CG  TYR A  25     5584   5335   3156   1003   -115   -155       C  
ATOM    315  CD1 TYR A  25     -27.186 -32.583 -38.258  1.00 32.98           C  
ANISOU  315  CD1 TYR A  25     4997   4801   2733    971   -148   -236       C  
ATOM    316  CD2 TYR A  25     -26.752 -31.338 -40.245  1.00 33.14           C  
ANISOU  316  CD2 TYR A  25     5124   4912   2555    996    -34   -125       C  
ATOM    317  CE1 TYR A  25     -25.980 -33.240 -38.399  1.00 27.05           C  
ANISOU  317  CE1 TYR A  25     4204   4102   1971    948   -102   -292       C  
ATOM    318  CE2 TYR A  25     -25.542 -31.989 -40.394  1.00 28.63           C  
ANISOU  318  CE2 TYR A  25     4507   4402   1971    963     20   -180       C  
ATOM    319  CZ  TYR A  25     -25.163 -32.939 -39.470  1.00 26.90           C  
ANISOU  319  CZ  TYR A  25     4210   4165   1846    946    -14   -267       C  
ATOM    320  OH  TYR A  25     -23.962 -33.587 -39.620  1.00 27.95           O  
ANISOU  320  OH  TYR A  25     4281   4372   1965    941     48   -321       O  
ATOM    321  H   TYR A  25     -29.897 -33.341 -40.589  1.00 43.59           H  
ATOM    322  HA  TYR A  25     -30.165 -32.494 -38.668  1.00 41.32           H  
ATOM    323  HB2 TYR A  25     -28.920 -30.145 -39.598  1.00 41.40           H  
ATOM    324  HB3 TYR A  25     -28.995 -30.633 -38.087  1.00 41.40           H  
ATOM    325  HD1 TYR A  25     -27.735 -32.788 -37.536  1.00 39.57           H  
ATOM    326  HD2 TYR A  25     -27.008 -30.698 -40.869  1.00 39.77           H  
ATOM    327  HE1 TYR A  25     -25.720 -33.881 -37.777  1.00 32.46           H  
ATOM    328  HE2 TYR A  25     -24.989 -31.789 -41.115  1.00 34.36           H  
ATOM    329  HH  TYR A  25     -23.569 -33.308 -40.309  1.00 33.54           H  
ATOM    330  N   LYS A  26     -32.320 -31.336 -40.240  1.00 35.20           N  
ANISOU  330  N   LYS A  26     5253   5229   2894   1223   -311   -121       N  
ATOM    331  CA  LYS A  26     -33.643 -30.716 -40.235  1.00 32.08           C  
ANISOU  331  CA  LYS A  26     4846   4862   2481   1306   -340    -68       C  
ATOM    332  C   LYS A  26     -34.551 -31.441 -39.255  1.00 26.63           C  
ANISOU  332  C   LYS A  26     4061   4172   1884   1292   -404   -126       C  
ATOM    333  O   LYS A  26     -34.431 -32.650 -39.070  1.00 29.48           O  
ANISOU  333  O   LYS A  26     4350   4556   2296   1225   -446   -221       O  
ATOM    334  CB  LYS A  26     -34.274 -30.761 -41.628  1.00 25.19           C  
ANISOU  334  CB  LYS A  26     3944   4132   1496   1361   -367    -67       C  
ATOM    335  CG  LYS A  26     -33.605 -29.861 -42.645  1.00 32.90           C  
ANISOU  335  CG  LYS A  26     5022   5119   2362   1398   -297     18       C  
ATOM    336  CD  LYS A  26     -34.244 -30.006 -44.018  1.00 46.28           C  
ANISOU  336  CD  LYS A  26     6680   6971   3936   1454   -333     12       C  
ATOM    337  CE  LYS A  26     -33.530 -29.152 -45.051  1.00 51.42           C  
ANISOU  337  CE  LYS A  26     7434   7636   4469   1489   -256    104       C  
ATOM    338  NZ  LYS A  26     -34.093 -29.326 -46.418  1.00 53.24           N  
ANISOU  338  NZ  LYS A  26     7631   8030   4567   1546   -293     97       N  
ATOM    339  H   LYS A  26     -32.203 -31.908 -40.871  1.00 42.24           H  
ATOM    340  HA  LYS A  26     -33.567 -29.789 -39.960  1.00 38.50           H  
ATOM    341  HB2 LYS A  26     -34.225 -31.671 -41.962  1.00 30.23           H  
ATOM    342  HB3 LYS A  26     -35.202 -30.488 -41.558  1.00 30.23           H  
ATOM    343  HG2 LYS A  26     -33.695 -28.937 -42.364  1.00 39.48           H  
ATOM    344  HG3 LYS A  26     -32.668 -30.101 -42.719  1.00 39.48           H  
ATOM    345  HD2 LYS A  26     -34.191 -30.933 -44.299  1.00 55.54           H  
ATOM    346  HD3 LYS A  26     -35.169 -29.720 -43.973  1.00 55.54           H  
ATOM    347  HE2 LYS A  26     -33.619 -28.218 -44.805  1.00 61.71           H  
ATOM    348  HE3 LYS A  26     -32.593 -29.403 -45.076  1.00 61.71           H  
ATOM    349  HZ1 LYS A  26     -34.952 -29.097 -46.425  1.00 63.89           H  
ATOM    350  HZ2 LYS A  26     -33.652 -28.812 -46.996  1.00 63.89           H  
ATOM    351  HZ3 LYS A  26     -34.018 -30.176 -46.672  1.00 63.89           H  
ATOM    352  N   VAL A  27     -35.452 -30.695 -38.627  1.00 23.01           N  
ANISOU  352  N   VAL A  27     3610   3689   1445   1359   -401    -67       N  
ATOM    353  CA  VAL A  27     -36.456 -31.274 -37.744  1.00 29.01           C  
ANISOU  353  CA  VAL A  27     4275   4474   2275   1355   -451   -106       C  
ATOM    354  C   VAL A  27     -37.769 -31.423 -38.515  1.00 33.04           C  
ANISOU  354  C   VAL A  27     4694   5142   2716   1411   -504   -109       C  
ATOM    355  O   VAL A  27     -38.403 -30.423 -38.846  1.00 34.46           O  
ANISOU  355  O   VAL A  27     4902   5358   2835   1515   -480    -31       O  
ATOM    356  CB  VAL A  27     -36.679 -30.388 -36.504  1.00 27.30           C  
ANISOU  356  CB  VAL A  27     4115   4148   2111   1399   -409    -47       C  
ATOM    357  CG1 VAL A  27     -37.804 -30.942 -35.632  1.00 23.53           C  
ANISOU  357  CG1 VAL A  27     3533   3721   1688   1402   -449    -75       C  
ATOM    358  CG2 VAL A  27     -35.386 -30.273 -35.702  1.00 23.96           C  
ANISOU  358  CG2 VAL A  27     3775   3584   1744   1329   -370    -50       C  
ATOM    359  H   VAL A  27     -35.504 -29.839 -38.697  1.00 27.62           H  
ATOM    360  HA  VAL A  27     -36.165 -32.152 -37.451  1.00 34.82           H  
ATOM    361  HB  VAL A  27     -36.933 -29.498 -36.793  1.00 32.76           H  
ATOM    362 HG11 VAL A  27     -37.567 -31.836 -35.342  1.00 28.24           H  
ATOM    363 HG12 VAL A  27     -37.919 -30.364 -34.862  1.00 28.24           H  
ATOM    364 HG13 VAL A  27     -38.622 -30.968 -36.153  1.00 28.24           H  
ATOM    365 HG21 VAL A  27     -34.701 -29.875 -36.263  1.00 28.75           H  
ATOM    366 HG22 VAL A  27     -35.545 -29.712 -34.926  1.00 28.75           H  
ATOM    367 HG23 VAL A  27     -35.110 -31.158 -35.419  1.00 28.75           H  
ATOM    368  N   PRO A  28     -38.177 -32.672 -38.814  1.00 33.83           N  
ANISOU  368  N   PRO A  28     4691   5342   2823   1342   -576   -202       N  
ATOM    369  CA  PRO A  28     -39.408 -32.913 -39.579  1.00 30.00           C  
ANISOU  369  CA  PRO A  28     4108   5029   2262   1371   -641   -217       C  
ATOM    370  C   PRO A  28     -40.640 -32.174 -39.063  1.00 38.24           C  
ANISOU  370  C   PRO A  28     5103   6129   3298   1466   -638   -143       C  
ATOM    371  O   PRO A  28     -40.719 -31.815 -37.888  1.00 40.49           O  
ANISOU  371  O   PRO A  28     5407   6321   3656   1484   -600   -108       O  
ATOM    372  CB  PRO A  28     -39.634 -34.422 -39.429  1.00 28.90           C  
ANISOU  372  CB  PRO A  28     3877   4936   2167   1253   -715   -338       C  
ATOM    373  CG  PRO A  28     -38.305 -35.007 -39.094  1.00 24.53           C  
ANISOU  373  CG  PRO A  28     3389   4250   1681   1180   -684   -392       C  
ATOM    374  CD  PRO A  28     -37.388 -33.905 -38.638  1.00 28.35           C  
ANISOU  374  CD  PRO A  28     3979   4605   2186   1233   -599   -302       C  
ATOM    375  HA  PRO A  28     -39.272 -32.699 -40.515  1.00 36.00           H  
ATOM    376  HB2 PRO A  28     -40.268 -34.585 -38.714  1.00 34.68           H  
ATOM    377  HB3 PRO A  28     -39.963 -34.784 -40.266  1.00 34.68           H  
ATOM    378  HG2 PRO A  28     -38.418 -35.659 -38.384  1.00 29.44           H  
ATOM    379  HG3 PRO A  28     -37.941 -35.436 -39.883  1.00 29.44           H  
ATOM    380  HD2 PRO A  28     -37.158 -34.026 -37.703  1.00 34.02           H  
ATOM    381  HD3 PRO A  28     -36.595 -33.878 -39.195  1.00 34.02           H  
ATOM    382  N   SER A  29     -41.581 -31.940 -39.972  1.00 58.62           N  
ANISOU  382  N   SER A  29     7621   8871   5780   1532   -676   -120       N  
ATOM    383  CA  SER A  29     -42.925 -31.503 -39.628  1.00 56.37           C  
ANISOU  383  CA  SER A  29     7248   8696   5475   1619   -690    -67       C  
ATOM    384  C   SER A  29     -43.838 -32.685 -39.899  1.00 51.12           C  
ANISOU  384  C   SER A  29     6427   8203   4794   1530   -793   -151       C  
ATOM    385  O   SER A  29     -43.606 -33.436 -40.847  1.00 51.72           O  
ANISOU  385  O   SER A  29     6483   8347   4820   1453   -852   -230       O  
ATOM    386  CB  SER A  29     -43.341 -30.326 -40.505  1.00 48.16           C  
ANISOU  386  CB  SER A  29     6246   7731   4321   1773   -659     29       C  
ATOM    387  OG  SER A  29     -44.550 -29.745 -40.047  1.00 59.55           O  
ANISOU  387  OG  SER A  29     7619   9262   5744   1884   -649     92       O  
ATOM    388  H   SER A  29     -41.459 -32.030 -40.819  1.00 70.34           H  
ATOM    389  HA  SER A  29     -42.978 -31.253 -38.692  1.00 67.65           H  
ATOM    390  HB2 SER A  29     -42.642 -29.655 -40.483  1.00 57.79           H  
ATOM    391  HB3 SER A  29     -43.468 -30.641 -41.414  1.00 57.79           H  
ATOM    392  HG  SER A  29     -44.764 -29.100 -40.541  1.00 71.46           H  
ATOM    393  N   LYS A  30     -44.868 -32.862 -39.080  1.00 51.19           N  
ANISOU  393  N   LYS A  30     6326   8284   4839   1533   -815   -138       N  
ATOM    394  CA  LYS A  30     -45.786 -33.977 -39.287  1.00 43.04           C  
ANISOU  394  CA  LYS A  30     5137   7421   3796   1429   -919   -216       C  
ATOM    395  C   LYS A  30     -47.219 -33.620 -38.914  1.00 41.11           C  
ANISOU  395  C   LYS A  30     4754   7344   3524   1506   -934   -153       C  
ATOM    396  O   LYS A  30     -47.466 -32.826 -38.000  1.00 47.32           O  
ANISOU  396  O   LYS A  30     5564   8074   4343   1607   -860    -69       O  
ATOM    397  CB  LYS A  30     -45.309 -35.200 -38.494  1.00 42.18           C  
ANISOU  397  CB  LYS A  30     5017   7213   3796   1270   -948   -309       C  
ATOM    398  CG  LYS A  30     -45.364 -36.518 -39.256  1.00 38.62           C  
ANISOU  398  CG  LYS A  30     4506   6844   3325   1117  -1048   -443       C  
ATOM    399  CD  LYS A  30     -44.407 -37.548 -38.657  1.00 40.09           C  
ANISOU  399  CD  LYS A  30     4752   6867   3611    990  -1047   -535       C  
ATOM    400  CE  LYS A  30     -44.136 -38.708 -39.606  1.00 48.39           C  
ANISOU  400  CE  LYS A  30     5808   7948   4631    857  -1118   -682       C  
ATOM    401  NZ  LYS A  30     -42.821 -38.556 -40.292  1.00 50.81           N  
ANISOU  401  NZ  LYS A  30     6256   8143   4907    886  -1062   -706       N  
ATOM    402  H   LYS A  30     -45.057 -32.361 -38.407  1.00 61.42           H  
ATOM    403  HA  LYS A  30     -45.777 -34.215 -40.227  1.00 51.65           H  
ATOM    404  HB2 LYS A  30     -44.388 -35.055 -38.226  1.00 50.61           H  
ATOM    405  HB3 LYS A  30     -45.866 -35.294 -37.706  1.00 50.61           H  
ATOM    406  HG2 LYS A  30     -46.264 -36.876 -39.212  1.00 46.35           H  
ATOM    407  HG3 LYS A  30     -45.108 -36.365 -40.179  1.00 46.35           H  
ATOM    408  HD2 LYS A  30     -43.561 -37.118 -38.458  1.00 48.10           H  
ATOM    409  HD3 LYS A  30     -44.797 -37.909 -37.845  1.00 48.10           H  
ATOM    410  HE2 LYS A  30     -44.123 -39.538 -39.104  1.00 58.07           H  
ATOM    411  HE3 LYS A  30     -44.831 -38.737 -40.283  1.00 58.07           H  
ATOM    412  HZ1 LYS A  30     -42.166 -38.531 -39.691  1.00 60.98           H  
ATOM    413  HZ2 LYS A  30     -42.684 -39.243 -40.841  1.00 60.98           H  
ATOM    414  HZ3 LYS A  30     -42.810 -37.802 -40.764  1.00 60.98           H  
ATOM    415  N   LYS A  31     -48.157 -34.204 -39.654  1.00 46.39           N  
ANISOU  415  N   LYS A  31     5279   8225   4123   1457  -1030   -198       N  
ATOM    416  CA  LYS A  31     -49.579 -34.039 -39.388  1.00 54.95           C  
ANISOU  416  CA  LYS A  31     6196   9511   5173   1510  -1059   -148       C  
ATOM    417  C   LYS A  31     -50.052 -35.137 -38.450  1.00 57.29           C  
ANISOU  417  C   LYS A  31     6368   9833   5565   1357  -1109   -206       C  
ATOM    418  O   LYS A  31     -49.839 -36.322 -38.716  1.00 62.37           O  
ANISOU  418  O   LYS A  31     6980  10478   6241   1179  -1190   -322       O  
ATOM    419  CB  LYS A  31     -50.388 -34.102 -40.686  1.00 52.09           C  
ANISOU  419  CB  LYS A  31     5724   9390   4679   1528  -1145   -166       C  
ATOM    420  CG  LYS A  31     -50.103 -32.975 -41.662  1.00 64.64           C  
ANISOU  420  CG  LYS A  31     7414  10991   6157   1698  -1099    -90       C  
ATOM    421  CD  LYS A  31     -50.919 -33.132 -42.937  1.00 71.20           C  
ANISOU  421  CD  LYS A  31     8126  12081   6847   1710  -1196   -111       C  
ATOM    422  CE  LYS A  31     -50.662 -31.980 -43.890  1.00 75.73           C  
ANISOU  422  CE  LYS A  31     8799  12672   7303   1894  -1147    -20       C  
ATOM    423  NZ  LYS A  31     -51.381 -32.114 -45.188  1.00 80.07           N  
ANISOU  423  NZ  LYS A  31     9241  13481   7699   1916  -1243    -39       N  
ATOM    424  H   LYS A  31     -47.990 -34.710 -40.329  1.00 55.67           H  
ATOM    425  HA  LYS A  31     -49.736 -33.180 -38.965  1.00 65.94           H  
ATOM    426  HB2 LYS A  31     -50.187 -34.938 -41.135  1.00 62.51           H  
ATOM    427  HB3 LYS A  31     -51.331 -34.068 -40.465  1.00 62.51           H  
ATOM    428  HG2 LYS A  31     -50.337 -32.128 -41.252  1.00 77.57           H  
ATOM    429  HG3 LYS A  31     -49.162 -32.986 -41.899  1.00 77.57           H  
ATOM    430  HD2 LYS A  31     -50.668 -33.957 -43.380  1.00 85.44           H  
ATOM    431  HD3 LYS A  31     -51.863 -33.141 -42.715  1.00 85.44           H  
ATOM    432  HE2 LYS A  31     -50.955 -31.155 -43.472  1.00 90.88           H  
ATOM    433  HE3 LYS A  31     -49.712 -31.934 -44.079  1.00 90.88           H  
ATOM    434  HZ1 LYS A  31     -52.259 -32.148 -45.047  1.00 96.08           H  
ATOM    435  HZ2 LYS A  31     -51.198 -31.416 -45.710  1.00 96.08           H  
ATOM    436  HZ3 LYS A  31     -51.125 -32.859 -45.601  1.00 96.08           H  
ATOM    437  N   PHE A  32     -50.688 -34.736 -37.354  1.00 50.17           N  
ANISOU  437  N   PHE A  32     5405   8950   4706   1426  -1055   -127       N  
ATOM    438  CA  PHE A  32     -51.255 -35.687 -36.404  1.00 43.53           C  
ANISOU  438  CA  PHE A  32     4429   8158   3951   1293  -1094   -159       C  
ATOM    439  C   PHE A  32     -52.756 -35.483 -36.288  1.00 50.12           C  
ANISOU  439  C   PHE A  32     5062   9248   4734   1348  -1114    -97       C  
ATOM    440  O   PHE A  32     -53.245 -34.350 -36.310  1.00 49.67           O  
ANISOU  440  O   PHE A  32     5010   9259   4604   1541  -1047      4       O  
ATOM    441  CB  PHE A  32     -50.600 -35.542 -35.031  1.00 43.31           C  
ANISOU  441  CB  PHE A  32     4501   7926   4029   1310  -1006   -120       C  
ATOM    442  CG  PHE A  32     -49.119 -35.766 -35.043  1.00 37.09           C  
ANISOU  442  CG  PHE A  32     3895   6902   3295   1255   -984   -176       C  
ATOM    443  CD1 PHE A  32     -48.256 -34.721 -35.318  1.00 40.24           C  
ANISOU  443  CD1 PHE A  32     4465   7160   3664   1377   -904   -131       C  
ATOM    444  CD2 PHE A  32     -48.589 -37.019 -34.787  1.00 31.34           C  
ANISOU  444  CD2 PHE A  32     3162   6099   2648   1080  -1040   -274       C  
ATOM    445  CE1 PHE A  32     -46.893 -34.918 -35.332  1.00 43.88           C  
ANISOU  445  CE1 PHE A  32     5075   7424   4172   1324   -880   -177       C  
ATOM    446  CE2 PHE A  32     -47.223 -37.223 -34.800  1.00 36.41           C  
ANISOU  446  CE2 PHE A  32     3963   6539   3331   1045  -1014   -323       C  
ATOM    447  CZ  PHE A  32     -46.374 -36.171 -35.075  1.00 38.92           C  
ANISOU  447  CZ  PHE A  32     4436   6734   3617   1166   -934   -272       C  
ATOM    448  H   PHE A  32     -50.805 -33.913 -37.135  1.00 60.20           H  
ATOM    449  HA  PHE A  32     -51.095 -36.590 -36.722  1.00 52.23           H  
ATOM    450  HB2 PHE A  32     -50.762 -34.644 -34.700  1.00 51.97           H  
ATOM    451  HB3 PHE A  32     -50.994 -36.190 -34.426  1.00 51.97           H  
ATOM    452  HD1 PHE A  32     -48.600 -33.875 -35.492  1.00 48.29           H  
ATOM    453  HD2 PHE A  32     -49.159 -37.731 -34.601  1.00 37.61           H  
ATOM    454  HE1 PHE A  32     -46.323 -34.207 -35.518  1.00 52.65           H  
ATOM    455  HE2 PHE A  32     -46.877 -38.069 -34.626  1.00 43.69           H  
ATOM    456  HZ  PHE A  32     -45.453 -36.305 -35.084  1.00 46.70           H  
ATOM    457  N   LYS A  33     -53.477 -36.595 -36.172  1.00 65.68           N  
ANISOU  457  N   LYS A  33     6855  11360   6741   1174  -1203   -162       N  
ATOM    458  CA  LYS A  33     -54.922 -36.574 -35.994  1.00 69.32           C  
ANISOU  458  CA  LYS A  33     7092  12083   7164   1190  -1228   -110       C  
ATOM    459  C   LYS A  33     -55.285 -36.065 -34.603  1.00 64.54           C  
ANISOU  459  C   LYS A  33     6461  11452   6609   1294  -1123     -2       C  
ATOM    460  O   LYS A  33     -54.587 -36.351 -33.630  1.00 67.40           O  
ANISOU  460  O   LYS A  33     6913  11626   7072   1246  -1076     -6       O  
ATOM    461  CB  LYS A  33     -55.496 -37.980 -36.197  1.00 65.37           C  
ANISOU  461  CB  LYS A  33     6413  11716   6707    935  -1350   -221       C  
ATOM    462  CG  LYS A  33     -55.375 -38.511 -37.622  1.00 73.69           C  
ANISOU  462  CG  LYS A  33     7472  12839   7688    827  -1461   -340       C  
ATOM    463  CD  LYS A  33     -55.953 -39.915 -37.751  1.00 80.93           C  
ANISOU  463  CD  LYS A  33     8228  13862   8659    551  -1577   -466       C  
ATOM    464  CE  LYS A  33     -55.875 -40.419 -39.186  1.00 88.74           C  
ANISOU  464  CE  LYS A  33     9235  14922   9560    446  -1687   -595       C  
ATOM    465  NZ  LYS A  33     -56.424 -41.796 -39.340  1.00 92.59           N  
ANISOU  465  NZ  LYS A  33     9589  15487  10104    156  -1798   -737       N  
ATOM    466  H   LYS A  33     -53.144 -37.387 -36.194  1.00 78.82           H  
ATOM    467  HA  LYS A  33     -55.320 -35.982 -36.651  1.00 83.19           H  
ATOM    468  HB2 LYS A  33     -55.026 -38.595 -35.613  1.00 78.44           H  
ATOM    469  HB3 LYS A  33     -56.439 -37.967 -35.967  1.00 78.44           H  
ATOM    470  HG2 LYS A  33     -55.861 -37.926 -38.224  1.00 88.43           H  
ATOM    471  HG3 LYS A  33     -54.438 -38.544 -37.872  1.00 88.43           H  
ATOM    472  HD2 LYS A  33     -55.448 -40.522 -37.188  1.00 97.11           H  
ATOM    473  HD3 LYS A  33     -56.885 -39.904 -37.483  1.00 97.11           H  
ATOM    474  HE2 LYS A  33     -56.388 -39.825 -39.758  1.00106.49           H  
ATOM    475  HE3 LYS A  33     -54.947 -40.431 -39.467  1.00106.49           H  
ATOM    476  HZ1 LYS A  33     -57.279 -41.812 -39.095  1.00111.11           H  
ATOM    477  HZ2 LYS A  33     -56.361 -42.055 -40.190  1.00111.11           H  
ATOM    478  HZ3 LYS A  33     -55.966 -42.364 -38.831  1.00111.11           H  
ATOM    479  N   VAL A  34     -56.377 -35.310 -34.523  1.00 42.09           N  
ANISOU  479  N   VAL A  34     3499   8809   3685   1446  -1085     95       N  
ATOM    480  CA  VAL A  34     -56.880 -34.791 -33.257  1.00 41.97           C  
ANISOU  480  CA  VAL A  34     3449   8807   3692   1560   -981    198       C  
ATOM    481  C   VAL A  34     -58.213 -35.473 -32.965  1.00 55.77           C  
ANISOU  481  C   VAL A  34     4917  10831   5443   1460  -1031    214       C  
ATOM    482  O   VAL A  34     -59.174 -35.324 -33.721  1.00 69.57           O  
ANISOU  482  O   VAL A  34     6509  12830   7096   1495  -1082    231       O  
ATOM    483  CB  VAL A  34     -57.058 -33.263 -33.321  1.00 44.29           C  
ANISOU  483  CB  VAL A  34     3846   9101   3881   1839   -874    304       C  
ATOM    484  CG1 VAL A  34     -57.600 -32.726 -32.007  1.00 48.15           C  
ANISOU  484  CG1 VAL A  34     4311   9605   4377   1963   -761    401       C  
ATOM    485  CG2 VAL A  34     -55.731 -32.594 -33.658  1.00 40.26           C  
ANISOU  485  CG2 VAL A  34     3603   8319   3375   1911   -825    285       C  
ATOM    486  H   VAL A  34     -56.852 -35.080 -35.202  1.00 50.51           H  
ATOM    487  HA  VAL A  34     -56.258 -35.003 -32.544  1.00 50.37           H  
ATOM    488  HB  VAL A  34     -57.693 -33.046 -34.021  1.00 53.15           H  
ATOM    489 HG11 VAL A  34     -56.977 -32.943 -31.296  1.00 57.77           H  
ATOM    490 HG12 VAL A  34     -57.701 -31.764 -32.077  1.00 57.77           H  
ATOM    491 HG13 VAL A  34     -58.461 -33.138 -31.829  1.00 57.77           H  
ATOM    492 HG21 VAL A  34     -55.424 -32.918 -34.519  1.00 48.31           H  
ATOM    493 HG22 VAL A  34     -55.863 -31.633 -33.694  1.00 48.31           H  
ATOM    494 HG23 VAL A  34     -55.083 -32.814 -32.971  1.00 48.31           H  
ATOM    495  N   LEU A  35     -58.266 -36.225 -31.870  1.00 69.81           N  
ANISOU  495  N   LEU A  35     6625  12571   7330   1330  -1014    214       N  
ATOM    496  CA  LEU A  35     -59.396 -37.112 -31.604  1.00 72.57           C  
ANISOU  496  CA  LEU A  35     6702  13159   7711   1167  -1069    212       C  
ATOM    497  C   LEU A  35     -60.529 -36.454 -30.821  1.00 78.86           C  
ANISOU  497  C   LEU A  35     7356  14154   8452   1324   -979    344       C  
ATOM    498  O   LEU A  35     -61.448 -37.132 -30.360  1.00 90.62           O  
ANISOU  498  O   LEU A  35     8619  15833   9979   1195   -998    364       O  
ATOM    499  CB  LEU A  35     -58.920 -38.357 -30.853  1.00 66.35           C  
ANISOU  499  CB  LEU A  35     5893  12241   7075    924  -1094    147       C  
ATOM    500  CG  LEU A  35     -57.910 -39.272 -31.555  1.00 63.16           C  
ANISOU  500  CG  LEU A  35     5599  11664   6735    728  -1191      1       C  
ATOM    501  CD1 LEU A  35     -58.183 -40.717 -31.166  1.00 61.76           C  
ANISOU  501  CD1 LEU A  35     5268  11516   6683    428  -1253    -74       C  
ATOM    502  CD2 LEU A  35     -57.916 -39.117 -33.075  1.00 66.21           C  
ANISOU  502  CD2 LEU A  35     6011  12126   7018    736  -1283    -75       C  
ATOM    503  H   LEU A  35     -57.657 -36.241 -31.262  1.00 83.78           H  
ATOM    504  HA  LEU A  35     -59.762 -37.406 -32.453  1.00 87.08           H  
ATOM    505  HB2 LEU A  35     -58.509 -38.066 -30.024  1.00 79.61           H  
ATOM    506  HB3 LEU A  35     -59.698 -38.898 -30.648  1.00 79.61           H  
ATOM    507  HG  LEU A  35     -57.020 -39.047 -31.241  1.00 75.79           H  
ATOM    508 HD11 LEU A  35     -59.083 -40.953 -31.439  1.00 74.12           H  
ATOM    509 HD12 LEU A  35     -57.541 -41.290 -31.614  1.00 74.12           H  
ATOM    510 HD13 LEU A  35     -58.094 -40.808 -30.205  1.00 74.12           H  
ATOM    511 HD21 LEU A  35     -57.693 -38.200 -33.299  1.00 79.45           H  
ATOM    512 HD22 LEU A  35     -57.259 -39.721 -33.455  1.00 79.45           H  
ATOM    513 HD23 LEU A  35     -58.799 -39.335 -33.411  1.00 79.45           H  
ATOM    514  N   GLY A  36     -60.466 -35.137 -30.677  1.00 72.09           N  
ANISOU  514  N   GLY A  36     6635  13252   7505   1595   -876    432       N  
ATOM    515  CA  GLY A  36     -61.480 -34.407 -29.944  1.00 78.43           C  
ANISOU  515  CA  GLY A  36     7335  14229   8236   1776   -779    556       C  
ATOM    516  C   GLY A  36     -62.793 -34.284 -30.692  1.00 84.43           C  
ANISOU  516  C   GLY A  36     7858  15333   8887   1819   -834    594       C  
ATOM    517  O   GLY A  36     -62.844 -34.461 -31.908  1.00 92.72           O  
ANISOU  517  O   GLY A  36     8869  16473   9889   1763   -937    531       O  
ATOM    518  H   GLY A  36     -59.840 -34.643 -30.999  1.00 86.51           H  
ATOM    519  HA2 GLY A  36     -61.651 -34.856 -29.102  1.00 94.12           H  
ATOM    520  HA3 GLY A  36     -61.155 -33.513 -29.753  1.00 94.12           H  
ATOM    521  N   ASN A  37     -63.861 -33.984 -29.958  1.00 71.86           N  
ANISOU  521  N   ASN A  37     6107  13949   7248   1921   -764    699       N  
ATOM    522  CA  ASN A  37     -65.163 -33.723 -30.568  1.00 75.92           C  
ANISOU  522  CA  ASN A  37     6389  14815   7643   2001   -801    756       C  
ATOM    523  C   ASN A  37     -65.205 -32.377 -31.283  1.00 75.31           C  
ANISOU  523  C   ASN A  37     6437  14760   7416   2295   -755    816       C  
ATOM    524  O   ASN A  37     -66.130 -32.107 -32.049  1.00 84.82           O  
ANISOU  524  O   ASN A  37     7474  16246   8507   2377   -801    855       O  
ATOM    525  CB  ASN A  37     -66.287 -33.791 -29.525  1.00 75.61           C  
ANISOU  525  CB  ASN A  37     6137  14998   7593   2033   -731    861       C  
ATOM    526  CG  ASN A  37     -65.948 -33.050 -28.242  1.00 81.09           C  
ANISOU  526  CG  ASN A  37     7005  15515   8289   2219   -573    945       C  
ATOM    527  OD1 ASN A  37     -66.051 -31.825 -28.171  1.00 72.19           O  
ANISOU  527  OD1 ASN A  37     6005  14374   7049   2500   -478   1022       O  
ATOM    528  ND2 ASN A  37     -65.551 -33.794 -27.216  1.00 86.85           N  
ANISOU  528  ND2 ASN A  37     7745  16110   9144   2062   -542    930       N  
ATOM    529  H   ASN A  37     -63.858 -33.924 -29.100  1.00 86.23           H  
ATOM    530  HA  ASN A  37     -65.336 -34.411 -31.229  1.00 91.10           H  
ATOM    531  HB2 ASN A  37     -67.088 -33.392 -29.898  1.00 90.73           H  
ATOM    532  HB3 ASN A  37     -66.453 -34.719 -29.299  1.00 90.73           H  
ATOM    533 HD21 ASN A  37     -65.498 -34.648 -27.300  1.00104.22           H  
ATOM    534 HD22 ASN A  37     -65.348 -33.422 -26.468  1.00104.22           H  
ATOM    535  N   THR A  38     -64.205 -31.535 -31.037  1.00 56.44           N  
ANISOU  535  N   THR A  38     4338  12078   5029   2447   -663    825       N  
ATOM    536  CA  THR A  38     -64.148 -30.222 -31.666  1.00 63.82           C  
ANISOU  536  CA  THR A  38     5420  12992   5835   2719   -603    884       C  
ATOM    537  C   THR A  38     -63.900 -30.393 -33.160  1.00 66.44           C  
ANISOU  537  C   THR A  38     5745  13374   6126   2659   -721    815       C  
ATOM    538  O   THR A  38     -63.428 -31.441 -33.599  1.00 62.70           O  
ANISOU  538  O   THR A  38     5238  12851   5736   2411   -833    705       O  
ATOM    539  CB  THR A  38     -63.022 -29.351 -31.076  1.00 58.60           C  
ANISOU  539  CB  THR A  38     5085  11978   5203   2851   -483    890       C  
ATOM    540  OG1 THR A  38     -61.751 -29.849 -31.511  1.00 51.55           O  
ANISOU  540  OG1 THR A  38     4351  10829   4408   2682   -544    780       O  
ATOM    541  CG2 THR A  38     -63.071 -29.346 -29.551  1.00 63.49           C  
ANISOU  541  CG2 THR A  38     5736  12513   5874   2871   -379    933       C  
ATOM    542  H   THR A  38     -63.547 -31.702 -30.509  1.00 67.73           H  
ATOM    543  HA  THR A  38     -64.994 -29.763 -31.542  1.00 76.58           H  
ATOM    544  HB  THR A  38     -63.129 -28.438 -31.385  1.00 70.32           H  
ATOM    545  HG1 THR A  38     -61.133 -29.378 -31.192  1.00 61.87           H  
ATOM    546 HG21 THR A  38     -62.968 -30.249 -29.213  1.00 76.19           H  
ATOM    547 HG22 THR A  38     -62.356 -28.793 -29.198  1.00 76.19           H  
ATOM    548 HG23 THR A  38     -63.922 -28.991 -29.248  1.00 76.19           H  
ATOM    549  N   ASP A  39     -64.208 -29.359 -33.936  1.00107.25           N  
ANISOU  549  N   ASP A  39    10954  18639  11158   2892   -694    882       N  
ATOM    550  CA  ASP A  39     -64.024 -29.406 -35.385  1.00106.84           C  
ANISOU  550  CA  ASP A  39    10898  18657  11042   2868   -797    834       C  
ATOM    551  C   ASP A  39     -62.578 -29.074 -35.781  1.00107.46           C  
ANISOU  551  C   ASP A  39    11272  18391  11168   2865   -775    776       C  
ATOM    552  O   ASP A  39     -62.319 -28.292 -36.699  1.00114.24           O  
ANISOU  552  O   ASP A  39    12241  19229  11936   3016   -765    805       O  
ATOM    553  CB  ASP A  39     -65.037 -28.484 -36.079  1.00111.36           C  
ANISOU  553  CB  ASP A  39    11362  19512  11439   3123   -782    943       C  
ATOM    554  CG  ASP A  39     -66.044 -29.248 -36.930  1.00120.76           C  
ANISOU  554  CG  ASP A  39    12249  21072  12561   3002   -928    915       C  
ATOM    555  OD1 ASP A  39     -65.683 -30.295 -37.512  1.00122.04           O  
ANISOU  555  OD1 ASP A  39    12360  21226  12784   2744  -1056    793       O  
ATOM    556  OD2 ASP A  39     -67.203 -28.794 -37.022  1.00123.08           O  
ANISOU  556  OD2 ASP A  39    12357  21673  12734   3166   -914   1014       O  
ATOM    557  H   ASP A  39     -64.527 -28.614 -33.648  1.00128.70           H  
ATOM    558  HA  ASP A  39     -64.204 -30.311 -35.685  1.00128.21           H  
ATOM    559  HB2 ASP A  39     -65.529 -27.990 -35.404  1.00133.64           H  
ATOM    560  HB3 ASP A  39     -64.560 -27.870 -36.658  1.00133.64           H  
ATOM    561  N   ARG A  40     -61.643 -29.688 -35.062  1.00117.54           N  
ANISOU  561  N   ARG A  40    12666  19407  12586   2692   -765    701       N  
ATOM    562  CA  ARG A  40     -60.238 -29.702 -35.435  1.00104.96           C  
ANISOU  562  CA  ARG A  40    11311  17512  11058   2621   -770    626       C  
ATOM    563  C   ARG A  40     -59.840 -31.168 -35.525  1.00102.78           C  
ANISOU  563  C   ARG A  40    10955  17205  10891   2317   -889    501       C  
ATOM    564  O   ARG A  40     -59.936 -31.903 -34.541  1.00103.96           O  
ANISOU  564  O   ARG A  40    11032  17328  11141   2181   -886    479       O  
ATOM    565  CB  ARG A  40     -59.386 -28.978 -34.393  1.00100.82           C  
ANISOU  565  CB  ARG A  40    11029  16682  10596   2715   -635    654       C  
ATOM    566  CG  ARG A  40     -57.906 -28.915 -34.748  1.00101.60           C  
ANISOU  566  CG  ARG A  40    11369  16475  10760   2646   -632    585       C  
ATOM    567  CD  ARG A  40     -57.099 -28.156 -33.704  1.00104.77           C  
ANISOU  567  CD  ARG A  40    12002  16592  11215   2731   -503    609       C  
ATOM    568  NE  ARG A  40     -56.722 -26.818 -34.164  1.00108.58           N  
ANISOU  568  NE  ARG A  40    12680  16956  11618   2938   -417    666       N  
ATOM    569  CZ  ARG A  40     -57.087 -25.672 -33.589  1.00107.43           C  
ANISOU  569  CZ  ARG A  40    12630  16780  11407   3156   -297    751       C  
ATOM    570  NH1 ARG A  40     -57.851 -25.659 -32.502  1.00101.68           N  
ANISOU  570  NH1 ARG A  40    11820  16141  10673   3210   -241    793       N  
ATOM    571  NH2 ARG A  40     -56.678 -24.521 -34.105  1.00106.80           N  
ANISOU  571  NH2 ARG A  40    12739  16578  11261   3324   -227    797       N  
ATOM    572  H   ARG A  40     -61.807 -30.115 -34.334  1.00141.05           H  
ATOM    573  HA  ARG A  40     -60.114 -29.282 -36.300  1.00125.96           H  
ATOM    574  HB2 ARG A  40     -59.709 -28.068 -34.303  1.00120.98           H  
ATOM    575  HB3 ARG A  40     -59.469 -29.442 -33.545  1.00120.98           H  
ATOM    576  HG2 ARG A  40     -57.553 -29.816 -34.805  1.00121.92           H  
ATOM    577  HG3 ARG A  40     -57.802 -28.460 -35.599  1.00121.92           H  
ATOM    578  HD2 ARG A  40     -57.631 -28.060 -32.899  1.00125.73           H  
ATOM    579  HD3 ARG A  40     -56.287 -28.649 -33.510  1.00125.73           H  
ATOM    580  HE  ARG A  40     -56.223 -26.767 -34.863  1.00130.29           H  
ATOM    581 HH11 ARG A  40     -58.123 -26.399 -32.158  1.00122.02           H  
ATOM    582 HH12 ARG A  40     -58.077 -24.910 -32.143  1.00122.02           H  
ATOM    583 HH21 ARG A  40     -56.182 -24.517 -34.807  1.00128.15           H  
ATOM    584 HH22 ARG A  40     -56.909 -23.779 -33.737  1.00128.15           H  
ATOM    585  N   HIS A  41     -59.397 -31.589 -36.706  1.00 76.62           N  
ANISOU  585  N   HIS A  41     7661  13897   7554   2217   -990    421       N  
ATOM    586  CA  HIS A  41     -59.244 -33.009 -37.013  1.00 78.01           C  
ANISOU  586  CA  HIS A  41     7737  14101   7803   1934  -1119    293       C  
ATOM    587  C   HIS A  41     -57.797 -33.388 -37.281  1.00 69.22           C  
ANISOU  587  C   HIS A  41     6836  12699   6764   1820  -1134    200       C  
ATOM    588  O   HIS A  41     -57.440 -34.567 -37.253  1.00 72.39           O  
ANISOU  588  O   HIS A  41     7209  13045   7251   1589  -1214     91       O  
ATOM    589  CB  HIS A  41     -60.095 -33.366 -38.229  1.00 80.90           C  
ANISOU  589  CB  HIS A  41     7913  14767   8058   1884  -1244    258       C  
ATOM    590  CG  HIS A  41     -61.431 -32.693 -38.240  1.00 92.44           C  
ANISOU  590  CG  HIS A  41     9188  16528   9405   2061  -1222    369       C  
ATOM    591  ND1 HIS A  41     -61.577 -31.331 -38.379  1.00100.56           N  
ANISOU  591  ND1 HIS A  41    10307  17570  10330   2352  -1122    489       N  
ATOM    592  CD2 HIS A  41     -62.682 -33.195 -38.115  1.00 93.38           C  
ANISOU  592  CD2 HIS A  41     9033  16950   9496   1988  -1283    381       C  
ATOM    593  CE1 HIS A  41     -62.860 -31.021 -38.345  1.00 95.12           C  
ANISOU  593  CE1 HIS A  41     9410  17185   9547   2467  -1121    573       C  
ATOM    594  NE2 HIS A  41     -63.552 -32.135 -38.187  1.00 94.78           N  
ANISOU  594  NE2 HIS A  41     9135  17329   9546   2247  -1219    510       N  
ATOM    595  H   HIS A  41     -59.177 -31.067 -37.353  1.00 91.94           H  
ATOM    596  HA  HIS A  41     -59.559 -33.533 -36.259  1.00 93.61           H  
ATOM    597  HB2 HIS A  41     -59.621 -33.099 -39.032  1.00 97.08           H  
ATOM    598  HB3 HIS A  41     -60.244 -34.324 -38.237  1.00 97.08           H  
ATOM    599  HD1 HIS A  41     -60.932 -30.769 -38.474  1.00120.67           H  
ATOM    600  HD2 HIS A  41     -62.910 -34.090 -38.005  1.00112.05           H  
ATOM    601  HE1 HIS A  41     -63.217 -30.165 -38.422  1.00114.14           H  
ATOM    602  HE2 HIS A  41     -64.409 -32.188 -38.137  1.00113.73           H  
ATOM    603  N   SER A  42     -56.970 -32.391 -37.570  1.00 61.08           N  
ANISOU  603  N   SER A  42     6020  11489   5700   1981  -1055    243       N  
ATOM    604  CA  SER A  42     -55.543 -32.624 -37.749  1.00 62.14           C  
ANISOU  604  CA  SER A  42     6361  11348   5902   1894  -1050    171       C  
ATOM    605  C   SER A  42     -54.738 -31.411 -37.314  1.00 60.44           C  
ANISOU  605  C   SER A  42     6370  10899   5695   2071   -916    247       C  
ATOM    606  O   SER A  42     -55.256 -30.293 -37.285  1.00 68.64           O  
ANISOU  606  O   SER A  42     7427  11998   6655   2282   -839    348       O  
ATOM    607  CB  SER A  42     -55.227 -32.937 -39.208  1.00 66.24           C  
ANISOU  607  CB  SER A  42     6895  11930   6342   1834  -1145     99       C  
ATOM    608  OG  SER A  42     -55.293 -31.766 -40.005  1.00 65.84           O  
ANISOU  608  OG  SER A  42     6915  11929   6171   2046  -1100    184       O  
ATOM    609  H   SER A  42     -57.209 -31.571 -37.667  1.00 73.30           H  
ATOM    610  HA  SER A  42     -55.270 -33.381 -37.208  1.00 74.57           H  
ATOM    611  HB2 SER A  42     -54.331 -33.306 -39.265  1.00 79.49           H  
ATOM    612  HB3 SER A  42     -55.872 -33.581 -39.540  1.00 79.49           H  
ATOM    613  HG  SER A  42     -55.117 -31.952 -40.805  1.00 79.01           H  
ATOM    614  N   ILE A  43     -53.473 -31.639 -36.976  1.00 53.99           N  
ANISOU  614  N   ILE A  43     5723   9818   4970   1983   -888    195       N  
ATOM    615  CA  ILE A  43     -52.577 -30.544 -36.625  1.00 52.62           C  
ANISOU  615  CA  ILE A  43     5772   9411   4812   2115   -771    249       C  
ATOM    616  C   ILE A  43     -51.143 -30.808 -37.078  1.00 54.96           C  
ANISOU  616  C   ILE A  43     6233   9494   5154   2014   -781    182       C  
ATOM    617  O   ILE A  43     -50.639 -31.930 -36.978  1.00 56.12           O  
ANISOU  617  O   ILE A  43     6360   9589   5376   1831   -844     90       O  
ATOM    618  CB  ILE A  43     -52.614 -30.281 -35.108  1.00 55.87           C  
ANISOU  618  CB  ILE A  43     6222   9706   5299   2149   -680    287       C  
ATOM    619  CG1 ILE A  43     -51.588 -29.217 -34.709  1.00 57.42           C  
ANISOU  619  CG1 ILE A  43     6660   9642   5515   2250   -568    320       C  
ATOM    620  CG2 ILE A  43     -52.371 -31.572 -34.347  1.00 49.17           C  
ANISOU  620  CG2 ILE A  43     5305   8813   4565   1944   -734    212       C  
ATOM    621  CD1 ILE A  43     -52.070 -28.291 -33.608  1.00 65.27           C  
ANISOU  621  CD1 ILE A  43     7703  10601   6495   2405   -457    394       C  
ATOM    622  H   ILE A  43     -53.109 -32.418 -36.942  1.00 64.78           H  
ATOM    623  HA  ILE A  43     -52.883 -29.739 -37.071  1.00 63.15           H  
ATOM    624  HB  ILE A  43     -53.498 -29.953 -34.877  1.00 67.04           H  
ATOM    625 HG12 ILE A  43     -50.784 -29.659 -34.395  1.00 68.91           H  
ATOM    626 HG13 ILE A  43     -51.382 -28.673 -35.486  1.00 68.91           H  
ATOM    627 HG21 ILE A  43     -51.501 -31.923 -34.591  1.00 59.01           H  
ATOM    628 HG22 ILE A  43     -52.398 -31.387 -33.395  1.00 59.01           H  
ATOM    629 HG23 ILE A  43     -53.063 -32.211 -34.580  1.00 59.01           H  
ATOM    630 HD11 ILE A  43     -52.270 -28.818 -32.819  1.00 78.32           H  
ATOM    631 HD12 ILE A  43     -51.372 -27.647 -33.410  1.00 78.32           H  
ATOM    632 HD13 ILE A  43     -52.869 -27.831 -33.911  1.00 78.32           H  
ATOM    633  N   LYS A  44     -50.499 -29.757 -37.579  1.00 43.97           N  
ANISOU  633  N   LYS A  44     5004   7987   3715   2140   -713    231       N  
ATOM    634  CA  LYS A  44     -49.119 -29.833 -38.038  1.00 47.62           C  
ANISOU  634  CA  LYS A  44     5624   8260   4210   2066   -706    186       C  
ATOM    635  C   LYS A  44     -48.189 -29.455 -36.911  1.00 50.67           C  
ANISOU  635  C   LYS A  44     6164   8395   4694   2056   -616    193       C  
ATOM    636  O   LYS A  44     -48.291 -28.359 -36.355  1.00 41.38           O  
ANISOU  636  O   LYS A  44     5081   7139   3504   2195   -523    264       O  
ATOM    637  CB  LYS A  44     -48.883 -28.886 -39.209  1.00 56.32           C  
ANISOU  637  CB  LYS A  44     6819   9376   5205   2197   -680    244       C  
ATOM    638  CG  LYS A  44     -49.078 -29.523 -40.563  1.00 67.50           C  
ANISOU  638  CG  LYS A  44     8146  10968   6533   2140   -783    196       C  
ATOM    639  CD  LYS A  44     -49.071 -28.470 -41.651  1.00 72.54           C  
ANISOU  639  CD  LYS A  44     8858  11654   7048   2305   -751    280       C  
ATOM    640  CE  LYS A  44     -50.074 -28.791 -42.739  1.00 77.34           C  
ANISOU  640  CE  LYS A  44     9307  12548   7530   2332   -849    274       C  
ATOM    641  NZ  LYS A  44     -50.547 -27.568 -43.435  1.00 78.40           N  
ANISOU  641  NZ  LYS A  44     9476  12775   7540   2554   -802    395       N  
ATOM    642  H   LYS A  44     -50.849 -28.976 -37.665  1.00 52.76           H  
ATOM    643  HA  LYS A  44     -48.917 -30.738 -38.321  1.00 57.14           H  
ATOM    644  HB2 LYS A  44     -49.503 -28.143 -39.139  1.00 67.59           H  
ATOM    645  HB3 LYS A  44     -47.971 -28.558 -39.165  1.00 67.59           H  
ATOM    646  HG2 LYS A  44     -48.355 -30.147 -40.734  1.00 81.00           H  
ATOM    647  HG3 LYS A  44     -49.933 -29.981 -40.584  1.00 81.00           H  
ATOM    648  HD2 LYS A  44     -49.304 -27.611 -41.267  1.00 87.04           H  
ATOM    649  HD3 LYS A  44     -48.189 -28.431 -42.053  1.00 87.04           H  
ATOM    650  HE2 LYS A  44     -49.657 -29.371 -43.396  1.00 92.81           H  
ATOM    651  HE3 LYS A  44     -50.843 -29.232 -42.344  1.00 92.81           H  
ATOM    652  HZ1 LYS A  44     -49.859 -27.146 -43.811  1.00 94.08           H  
ATOM    653  HZ2 LYS A  44     -51.134 -27.785 -44.067  1.00 94.08           H  
ATOM    654  HZ3 LYS A  44     -50.939 -27.020 -42.853  1.00 94.08           H  
ATOM    655  N   LYS A  45     -47.282 -30.364 -36.575  1.00 60.39           N  
ANISOU  655  N   LYS A  45     7427   9505   6015   1894   -645    113       N  
ATOM    656  CA  LYS A  45     -46.345 -30.110 -35.497  1.00 54.44           C  
ANISOU  656  CA  LYS A  45     6805   8527   5351   1868   -573    112       C  
ATOM    657  C   LYS A  45     -44.938 -30.557 -35.859  1.00 45.00           C  
ANISOU  657  C   LYS A  45     5713   7186   4200   1756   -584     52       C  
ATOM    658  O   LYS A  45     -44.741 -31.528 -36.597  1.00 49.47           O  
ANISOU  658  O   LYS A  45     6220   7818   4758   1650   -659    -17       O  
ATOM    659  CB  LYS A  45     -46.836 -30.785 -34.214  1.00 57.31           C  
ANISOU  659  CB  LYS A  45     7079   8904   5792   1803   -580     94       C  
ATOM    660  CG  LYS A  45     -48.335 -30.593 -34.004  1.00 61.73           C  
ANISOU  660  CG  LYS A  45     7491   9665   6298   1896   -585    147       C  
ATOM    661  CD  LYS A  45     -48.769 -30.749 -32.562  1.00 57.92           C  
ANISOU  661  CD  LYS A  45     6966   9166   5874   1891   -545    167       C  
ATOM    662  CE  LYS A  45     -48.965 -32.191 -32.168  1.00 63.46           C  
ANISOU  662  CE  LYS A  45     7529   9934   6650   1721   -627    109       C  
ATOM    663  NZ  LYS A  45     -50.371 -32.497 -31.777  1.00 68.41           N  
ANISOU  663  NZ  LYS A  45     7960  10778   7255   1739   -650    146       N  
ATOM    664  H   LYS A  45     -47.191 -31.130 -36.954  1.00 72.47           H  
ATOM    665  HA  LYS A  45     -46.315 -29.154 -35.332  1.00 65.32           H  
ATOM    666  HB2 LYS A  45     -46.658 -31.737 -34.266  1.00 68.77           H  
ATOM    667  HB3 LYS A  45     -46.373 -30.400 -33.453  1.00 68.77           H  
ATOM    668  HG2 LYS A  45     -48.581 -29.700 -34.294  1.00 74.07           H  
ATOM    669  HG3 LYS A  45     -48.813 -31.253 -34.531  1.00 74.07           H  
ATOM    670  HD2 LYS A  45     -48.089 -30.369 -31.984  1.00 69.50           H  
ATOM    671  HD3 LYS A  45     -49.612 -30.285 -32.433  1.00 69.50           H  
ATOM    672  HE2 LYS A  45     -48.732 -32.758 -32.919  1.00 76.15           H  
ATOM    673  HE3 LYS A  45     -48.393 -32.392 -31.411  1.00 76.15           H  
ATOM    674  HZ1 LYS A  45     -50.919 -32.328 -32.458  1.00 82.09           H  
ATOM    675  HZ2 LYS A  45     -50.444 -33.355 -31.552  1.00 82.09           H  
ATOM    676  HZ3 LYS A  45     -50.610 -31.995 -31.082  1.00 82.09           H  
ATOM    677  N   ASN A  46     -43.967 -29.803 -35.357  1.00 38.75           N  
ANISOU  677  N   ASN A  46     5078   6203   3443   1782   -505     78       N  
ATOM    678  CA  ASN A  46     -42.564 -30.150 -35.486  1.00 42.11           C  
ANISOU  678  CA  ASN A  46     5598   6486   3916   1681   -502     32       C  
ATOM    679  C   ASN A  46     -42.202 -31.171 -34.424  1.00 45.14           C  
ANISOU  679  C   ASN A  46     5944   6805   4401   1559   -525    -30       C  
ATOM    680  O   ASN A  46     -42.742 -31.142 -33.318  1.00 42.61           O  
ANISOU  680  O   ASN A  46     5593   6476   4122   1574   -506    -13       O  
ATOM    681  CB  ASN A  46     -41.690 -28.909 -35.319  1.00 43.67           C  
ANISOU  681  CB  ASN A  46     5972   6514   4106   1748   -415     87       C  
ATOM    682  CG  ASN A  46     -42.297 -27.682 -35.958  1.00 43.32           C  
ANISOU  682  CG  ASN A  46     5981   6511   3966   1906   -370    171       C  
ATOM    683  OD1 ASN A  46     -43.514 -27.519 -35.985  1.00 54.38           O  
ANISOU  683  OD1 ASN A  46     7292   8049   5322   1998   -379    202       O  
ATOM    684  ND2 ASN A  46     -41.449 -26.814 -36.485  1.00 45.63           N  
ANISOU  684  ND2 ASN A  46     6421   6693   4222   1942   -317    216       N  
ATOM    685  H   ASN A  46     -44.102 -29.070 -34.929  1.00 46.50           H  
ATOM    686  HA  ASN A  46     -42.398 -30.535 -36.361  1.00 50.53           H  
ATOM    687  HB2 ASN A  46     -41.574 -28.729 -34.373  1.00 52.40           H  
ATOM    688  HB3 ASN A  46     -40.829 -29.070 -35.735  1.00 52.40           H  
ATOM    689 HD21 ASN A  46     -40.603 -26.965 -36.451  1.00 54.75           H  
ATOM    690 HD22 ASN A  46     -41.744 -26.099 -36.860  1.00 54.75           H  
ATOM    691  N   LEU A  47     -41.287 -32.072 -34.762  1.00 44.10           N  
ANISOU  691  N   LEU A  47     5821   6633   4304   1448   -562    -98       N  
ATOM    692  CA  LEU A  47     -40.864 -33.114 -33.841  1.00 42.89           C  
ANISOU  692  CA  LEU A  47     5639   6416   4241   1340   -586   -155       C  
ATOM    693  C   LEU A  47     -39.732 -32.604 -32.958  1.00 33.96           C  
ANISOU  693  C   LEU A  47     4630   5108   3166   1333   -521   -136       C  
ATOM    694  O   LEU A  47     -38.609 -33.107 -33.001  1.00 34.12           O  
ANISOU  694  O   LEU A  47     4692   5050   3222   1262   -525   -178       O  
ATOM    695  CB  LEU A  47     -40.429 -34.348 -34.621  1.00 45.21           C  
ANISOU  695  CB  LEU A  47     5891   6750   4537   1237   -652   -247       C  
ATOM    696  CG  LEU A  47     -41.440 -34.811 -35.672  1.00 39.55           C  
ANISOU  696  CG  LEU A  47     5068   6214   3747   1227   -725   -282       C  
ATOM    697  CD1 LEU A  47     -40.947 -36.079 -36.336  1.00 47.03           C  
ANISOU  697  CD1 LEU A  47     5997   7176   4697   1114   -785   -397       C  
ATOM    698  CD2 LEU A  47     -42.829 -35.018 -35.075  1.00 38.24           C  
ANISOU  698  CD2 LEU A  47     4773   6169   3588   1233   -763   -261       C  
ATOM    699  H   LEU A  47     -40.894 -32.099 -35.527  1.00 52.93           H  
ATOM    700  HA  LEU A  47     -41.609 -33.360 -33.271  1.00 51.47           H  
ATOM    701  HB2 LEU A  47     -39.597 -34.151 -35.078  1.00 54.25           H  
ATOM    702  HB3 LEU A  47     -40.296 -35.080 -33.997  1.00 54.25           H  
ATOM    703  HG  LEU A  47     -41.512 -34.127 -36.357  1.00 47.46           H  
ATOM    704 HD11 LEU A  47     -40.842 -36.768 -35.661  1.00 56.44           H  
ATOM    705 HD12 LEU A  47     -41.596 -36.361 -36.999  1.00 56.44           H  
ATOM    706 HD13 LEU A  47     -40.094 -35.901 -36.762  1.00 56.44           H  
ATOM    707 HD21 LEU A  47     -43.139 -34.179 -34.698  1.00 45.89           H  
ATOM    708 HD22 LEU A  47     -43.433 -35.309 -35.776  1.00 45.89           H  
ATOM    709 HD23 LEU A  47     -42.777 -35.693 -34.381  1.00 45.89           H  
ATOM    710  N   ILE A  48     -40.049 -31.581 -32.174  1.00 23.44           N  
ANISOU  710  N   ILE A  48     3353   3723   1831   1412   -463    -77       N  
ATOM    711  CA  ILE A  48     -39.138 -31.028 -31.184  1.00 21.96           C  
ANISOU  711  CA  ILE A  48     3280   3379   1686   1401   -410    -65       C  
ATOM    712  C   ILE A  48     -39.973 -30.666 -29.968  1.00 23.17           C  
ANISOU  712  C   ILE A  48     3420   3531   1851   1454   -377    -37       C  
ATOM    713  O   ILE A  48     -41.082 -30.146 -30.105  1.00 20.65           O  
ANISOU  713  O   ILE A  48     3065   3301   1480   1550   -361      1       O  
ATOM    714  CB  ILE A  48     -38.405 -29.777 -31.717  1.00 21.27           C  
ANISOU  714  CB  ILE A  48     3337   3198   1548   1455   -355    -23       C  
ATOM    715  CG1 ILE A  48     -37.387 -29.266 -30.696  1.00 18.26           C  
ANISOU  715  CG1 ILE A  48     3077   2660   1203   1420   -315    -21       C  
ATOM    716  CG2 ILE A  48     -39.399 -28.670 -32.062  1.00 20.41           C  
ANISOU  716  CG2 ILE A  48     3259   3132   1363   1592   -315     39       C  
ATOM    717  CD1 ILE A  48     -36.110 -28.745 -31.333  1.00 21.63           C  
ANISOU  717  CD1 ILE A  48     3618   2998   1603   1384   -294     -5       C  
ATOM    718  H   ILE A  48     -40.810 -31.180 -32.198  1.00 28.13           H  
ATOM    719  HA  ILE A  48     -38.480 -31.694 -30.929  1.00 26.35           H  
ATOM    720  HB  ILE A  48     -37.929 -30.024 -32.526  1.00 25.53           H  
ATOM    721 HG12 ILE A  48     -37.785 -28.541 -30.190  1.00 21.92           H  
ATOM    722 HG13 ILE A  48     -37.147 -29.993 -30.100  1.00 21.92           H  
ATOM    723 HG21 ILE A  48     -39.894 -28.430 -31.262  1.00 24.49           H  
ATOM    724 HG22 ILE A  48     -38.912 -27.900 -32.393  1.00 24.49           H  
ATOM    725 HG23 ILE A  48     -40.009 -28.995 -32.743  1.00 24.49           H  
ATOM    726 HD11 ILE A  48     -36.331 -28.010 -31.926  1.00 25.96           H  
ATOM    727 HD12 ILE A  48     -35.511 -28.438 -30.634  1.00 25.96           H  
ATOM    728 HD13 ILE A  48     -35.693 -29.462 -31.836  1.00 25.96           H  
ATOM    729  N   GLY A  49     -39.465 -30.953 -28.777  1.00 27.17           N  
ANISOU  729  N   GLY A  49     3953   3954   2416   1400   -367    -55       N  
ATOM    730  CA  GLY A  49     -40.266 -30.717 -27.591  1.00 32.29           C  
ANISOU  730  CA  GLY A  49     4585   4617   3066   1449   -335    -31       C  
ATOM    731  C   GLY A  49     -39.579 -30.882 -26.253  1.00 24.52           C  
ANISOU  731  C   GLY A  49     3652   3535   2130   1397   -320    -46       C  
ATOM    732  O   GLY A  49     -38.383 -31.176 -26.168  1.00 22.41           O  
ANISOU  732  O   GLY A  49     3432   3180   1901   1318   -336    -75       O  
ATOM    733  H   GLY A  49     -38.681 -31.275 -28.632  1.00 32.61           H  
ATOM    734  HA2 GLY A  49     -40.614 -29.813 -27.630  1.00 38.74           H  
ATOM    735  HA3 GLY A  49     -41.023 -31.324 -27.606  1.00 38.74           H  
ATOM    736  N   ALA A  50     -40.371 -30.686 -25.202  1.00 18.93           N  
ANISOU  736  N   ALA A  50     2928   2857   1408   1450   -287    -23       N  
ATOM    737  CA  ALA A  50     -39.920 -30.856 -23.826  1.00 18.96           C  
ANISOU  737  CA  ALA A  50     2969   2795   1441   1416   -272    -31       C  
ATOM    738  C   ALA A  50     -41.054 -31.371 -22.943  1.00 21.39           C  
ANISOU  738  C   ALA A  50     3172   3209   1748   1446   -263      2       C  
ATOM    739  O   ALA A  50     -42.204 -30.914 -23.036  1.00 25.18           O  
ANISOU  739  O   ALA A  50     3608   3784   2175   1544   -232     38       O  
ATOM    740  CB  ALA A  50     -39.389 -29.545 -23.276  1.00 25.22           C  
ANISOU  740  CB  ALA A  50     3934   3467   2183   1478   -219    -38       C  
ATOM    741  H   ALA A  50     -41.195 -30.449 -25.263  1.00 22.72           H  
ATOM    742  HA  ALA A  50     -39.200 -31.506 -23.805  1.00 22.75           H  
ATOM    743  HB1 ALA A  50     -40.098 -28.884 -23.301  1.00 30.27           H  
ATOM    744  HB2 ALA A  50     -39.096 -29.683 -22.362  1.00 30.27           H  
ATOM    745  HB3 ALA A  50     -38.644 -29.253 -23.823  1.00 30.27           H  
ATOM    746  N   LEU A  51     -40.711 -32.331 -22.090  1.00 20.69           N  
ANISOU  746  N   LEU A  51     3038   3110   1714   1367   -287      1       N  
ATOM    747  CA  LEU A  51     -41.629 -32.860 -21.095  1.00 17.46           C  
ANISOU  747  CA  LEU A  51     2540   2790   1305   1390   -273     46       C  
ATOM    748  C   LEU A  51     -41.191 -32.396 -19.716  1.00 27.42           C  
ANISOU  748  C   LEU A  51     3897   3981   2541   1419   -226     47       C  
ATOM    749  O   LEU A  51     -40.080 -32.693 -19.283  1.00 31.28           O  
ANISOU  749  O   LEU A  51     4440   4381   3064   1346   -247     22       O  
ATOM    750  CB  LEU A  51     -41.645 -34.387 -21.150  1.00 17.17           C  
ANISOU  750  CB  LEU A  51     2382   2800   1342   1291   -338     58       C  
ATOM    751  CG  LEU A  51     -42.491 -35.071 -20.075  1.00 24.71           C  
ANISOU  751  CG  LEU A  51     3237   3845   2306   1304   -326    122       C  
ATOM    752  CD1 LEU A  51     -43.975 -34.798 -20.309  1.00 25.01           C  
ANISOU  752  CD1 LEU A  51     3161   4044   2297   1386   -307    166       C  
ATOM    753  CD2 LEU A  51     -42.197 -36.560 -20.035  1.00 26.36           C  
ANISOU  753  CD2 LEU A  51     3366   4056   2593   1208   -394    133       C  
ATOM    754  H   LEU A  51     -39.934 -32.699 -22.070  1.00 24.83           H  
ATOM    755  HA  LEU A  51     -42.525 -32.531 -21.266  1.00 20.96           H  
ATOM    756  HB2 LEU A  51     -41.994 -34.660 -22.013  1.00 20.60           H  
ATOM    757  HB3 LEU A  51     -40.735 -34.708 -21.052  1.00 20.60           H  
ATOM    758  HG  LEU A  51     -42.256 -34.700 -19.210  1.00 29.65           H  
ATOM    759 HD11 LEU A  51     -44.225 -35.144 -21.180  1.00 30.01           H  
ATOM    760 HD12 LEU A  51     -44.490 -35.241 -19.617  1.00 30.01           H  
ATOM    761 HD13 LEU A  51     -44.128 -33.841 -20.276  1.00 30.01           H  
ATOM    762 HD21 LEU A  51     -41.257 -36.690 -19.833  1.00 31.63           H  
ATOM    763 HD22 LEU A  51     -42.744 -36.971 -19.348  1.00 31.63           H  
ATOM    764 HD23 LEU A  51     -42.406 -36.946 -20.900  1.00 31.63           H  
ATOM    765  N   LEU A  52     -42.082 -31.682 -19.036  1.00 24.48           N  
ANISOU  765  N   LEU A  52     3542   3663   2098   1537   -163     75       N  
ATOM    766  CA  LEU A  52     -41.829 -31.141 -17.711  1.00 26.68           C  
ANISOU  766  CA  LEU A  52     3922   3889   2325   1595   -114     69       C  
ATOM    767  C   LEU A  52     -42.617 -31.962 -16.702  1.00 25.67           C  
ANISOU  767  C   LEU A  52     3681   3876   2197   1609    -94    132       C  
ATOM    768  O   LEU A  52     -43.799 -32.243 -16.905  1.00 27.17           O  
ANISOU  768  O   LEU A  52     3746   4203   2375   1656    -78    186       O  
ATOM    769  CB  LEU A  52     -42.259 -29.673 -17.644  1.00 21.65           C  
ANISOU  769  CB  LEU A  52     3417   3225   1585   1747    -45     55       C  
ATOM    770  CG  LEU A  52     -41.841 -28.802 -18.830  1.00 27.27           C  
ANISOU  770  CG  LEU A  52     4228   3853   2282   1760    -52     23       C  
ATOM    771  CD1 LEU A  52     -42.360 -27.385 -18.635  1.00 24.81           C  
ANISOU  771  CD1 LEU A  52     4069   3512   1847   1924     26     24       C  
ATOM    772  CD2 LEU A  52     -40.324 -28.804 -19.029  1.00 21.92           C  
ANISOU  772  CD2 LEU A  52     3644   3029   1656   1650   -102    -27       C  
ATOM    773  H   LEU A  52     -42.865 -31.492 -19.336  1.00 29.38           H  
ATOM    774  HA  LEU A  52     -40.885 -31.204 -17.501  1.00 32.01           H  
ATOM    775  HB2 LEU A  52     -43.226 -29.640 -17.587  1.00 25.98           H  
ATOM    776  HB3 LEU A  52     -41.875 -29.279 -16.845  1.00 25.98           H  
ATOM    777  HG  LEU A  52     -42.246 -29.157 -19.636  1.00 32.73           H  
ATOM    778 HD11 LEU A  52     -41.986 -27.022 -17.817  1.00 29.78           H  
ATOM    779 HD12 LEU A  52     -42.088 -26.843 -19.393  1.00 29.78           H  
ATOM    780 HD13 LEU A  52     -43.328 -27.410 -18.575  1.00 29.78           H  
ATOM    781 HD21 LEU A  52     -40.029 -29.713 -19.195  1.00 26.31           H  
ATOM    782 HD22 LEU A  52     -40.106 -28.241 -19.789  1.00 26.31           H  
ATOM    783 HD23 LEU A  52     -39.900 -28.459 -18.228  1.00 26.31           H  
ATOM    784  N   PHE A  53     -41.952 -32.361 -15.625  1.00 24.33           N  
ANISOU  784  N   PHE A  53     3547   3661   2037   1569    -97    133       N  
ATOM    785  CA  PHE A  53     -42.582 -33.187 -14.603  1.00 26.48           C  
ANISOU  785  CA  PHE A  53     3722   4036   2305   1581    -72    207       C  
ATOM    786  C   PHE A  53     -42.213 -32.746 -13.193  1.00 25.30           C  
ANISOU  786  C   PHE A  53     3675   3853   2087   1643    -29    200       C  
ATOM    787  O   PHE A  53     -41.143 -32.182 -12.960  1.00 26.65           O  
ANISOU  787  O   PHE A  53     3975   3904   2247   1620    -52    136       O  
ATOM    788  CB  PHE A  53     -42.197 -34.653 -14.800  1.00 30.41           C  
ANISOU  788  CB  PHE A  53     4120   4536   2900   1446   -138    244       C  
ATOM    789  CG  PHE A  53     -40.720 -34.885 -14.907  1.00 26.31           C  
ANISOU  789  CG  PHE A  53     3680   3887   2428   1345   -191    191       C  
ATOM    790  CD1 PHE A  53     -40.087 -34.840 -16.136  1.00 19.50           C  
ANISOU  790  CD1 PHE A  53     2837   2959   1615   1282   -241    135       C  
ATOM    791  CD2 PHE A  53     -39.968 -35.168 -13.781  1.00 23.63           C  
ANISOU  791  CD2 PHE A  53     3388   3513   2077   1319   -190    204       C  
ATOM    792  CE1 PHE A  53     -38.729 -35.062 -16.237  1.00 17.26           C  
ANISOU  792  CE1 PHE A  53     2609   2582   1369   1201   -282     96       C  
ATOM    793  CE2 PHE A  53     -38.612 -35.392 -13.876  1.00 19.29           C  
ANISOU  793  CE2 PHE A  53     2889   2874   1566   1234   -240    164       C  
ATOM    794  CZ  PHE A  53     -37.990 -35.337 -15.106  1.00 16.14           C  
ANISOU  794  CZ  PHE A  53     2499   2414   1218   1177   -284    111       C  
ATOM    795  H   PHE A  53     -41.130 -32.167 -15.462  1.00 29.20           H  
ATOM    796  HA  PHE A  53     -43.545 -33.117 -14.694  1.00 31.78           H  
ATOM    797  HB2 PHE A  53     -42.524 -35.166 -14.044  1.00 36.50           H  
ATOM    798  HB3 PHE A  53     -42.607 -34.976 -15.618  1.00 36.50           H  
ATOM    799  HD1 PHE A  53     -40.581 -34.654 -16.901  1.00 23.40           H  
ATOM    800  HD2 PHE A  53     -40.383 -35.205 -12.949  1.00 28.35           H  
ATOM    801  HE1 PHE A  53     -38.312 -35.026 -17.068  1.00 20.72           H  
ATOM    802  HE2 PHE A  53     -38.116 -35.576 -13.111  1.00 23.15           H  
ATOM    803  HZ  PHE A  53     -37.075 -35.487 -15.172  1.00 19.37           H  
ATOM    804  N   ASP A  54     -43.117 -33.017 -12.258  1.00 46.52           N  
ANISOU  804  N   ASP A  54     6294   6659   4724   1722     31    273       N  
ATOM    805  CA  ASP A  54     -42.885 -32.734 -10.849  1.00 53.28           C  
ANISOU  805  CA  ASP A  54     7230   7507   5506   1789     74    276       C  
ATOM    806  C   ASP A  54     -42.351 -33.967 -10.141  1.00 52.91           C  
ANISOU  806  C   ASP A  54     7126   7475   5503   1677     42    335       C  
ATOM    807  O   ASP A  54     -42.402 -35.077 -10.671  1.00 42.69           O  
ANISOU  807  O   ASP A  54     5723   6206   4292   1578      3    389       O  
ATOM    808  CB  ASP A  54     -44.181 -32.285 -10.168  1.00 56.49           C  
ANISOU  808  CB  ASP A  54     7598   8050   5816   1967    175    332       C  
ATOM    809  CG  ASP A  54     -44.331 -30.774 -10.122  1.00 70.18           C  
ANISOU  809  CG  ASP A  54     9484   9715   7468   2137    222    261       C  
ATOM    810  OD1 ASP A  54     -43.308 -30.053 -10.123  1.00 67.24           O  
ANISOU  810  OD1 ASP A  54     9273   9171   7105   2116    173    181       O  
ATOM    811  OD2 ASP A  54     -45.483 -30.304 -10.073  1.00 79.16           O  
ANISOU  811  OD2 ASP A  54    10579  10958   8540   2264    290    308       O  
ATOM    812  H   ASP A  54     -43.884 -33.371 -12.418  1.00 55.83           H  
ATOM    813  HA  ASP A  54     -42.231 -32.023 -10.765  1.00 63.93           H  
ATOM    814  HB2 ASP A  54     -44.937 -32.646 -10.658  1.00 67.79           H  
ATOM    815  HB3 ASP A  54     -44.189 -32.615  -9.256  1.00 67.79           H  
ATOM    816  N   SER A  55     -41.838 -33.753  -8.935  1.00 65.65           N  
ANISOU  816  N   SER A  55     8823   9068   7055   1701     56    325       N  
ATOM    817  CA  SER A  55     -41.371 -34.837  -8.087  1.00 67.18           C  
ANISOU  817  CA  SER A  55     8974   9288   7262   1620     40    393       C  
ATOM    818  C   SER A  55     -42.307 -34.965  -6.896  1.00 62.96           C  
ANISOU  818  C   SER A  55     8398   8882   6641   1725    129    480       C  
ATOM    819  O   SER A  55     -42.043 -34.417  -5.825  1.00 73.87           O  
ANISOU  819  O   SER A  55     9869  10261   7937   1782    149    452       O  
ATOM    820  CB  SER A  55     -39.949 -34.557  -7.608  1.00 71.43           C  
ANISOU  820  CB  SER A  55     9623   9729   7787   1551    -23    321       C  
ATOM    821  OG  SER A  55     -39.912 -33.410  -6.776  1.00 73.79           O  
ANISOU  821  OG  SER A  55    10042  10011   7982   1642      2    262       O  
ATOM    822  H   SER A  55     -41.749 -32.975  -8.582  1.00 78.79           H  
ATOM    823  HA  SER A  55     -41.378 -35.670  -8.583  1.00 80.61           H  
ATOM    824  HB2 SER A  55     -39.629 -35.323  -7.105  1.00 85.71           H  
ATOM    825  HB3 SER A  55     -39.380 -34.406  -8.379  1.00 85.71           H  
ATOM    826  HG  SER A  55     -40.401 -33.528  -6.103  1.00 88.54           H  
ATOM    827  N   GLY A  56     -43.406 -35.685  -7.097  1.00 61.34           N  
ANISOU  827  N   GLY A  56     8050   8799   6456   1746    178    591       N  
ATOM    828  CA  GLY A  56     -44.409 -35.868  -6.064  1.00 70.10           C  
ANISOU  828  CA  GLY A  56     9090  10061   7486   1846    278    699       C  
ATOM    829  C   GLY A  56     -44.663 -37.332  -5.766  1.00 68.77           C  
ANISOU  829  C   GLY A  56     8799   9966   7365   1759    294    855       C  
ATOM    830  O   GLY A  56     -44.026 -38.214  -6.343  1.00 72.95           O  
ANISOU  830  O   GLY A  56     9311  10410   7995   1633    222    874       O  
ATOM    831  H   GLY A  56     -43.593 -36.083  -7.836  1.00 73.61           H  
ATOM    832  HA2 GLY A  56     -44.117 -35.434  -5.247  1.00 84.12           H  
ATOM    833  HA3 GLY A  56     -45.244 -35.462  -6.347  1.00 84.12           H  
ATOM    834  N   GLU A  57     -45.602 -37.586  -4.861  1.00 61.23           N  
ANISOU  834  N   GLU A  57     7762   9164   6340   1834    397    977       N  
ATOM    835  CA  GLU A  57     -45.962 -38.946  -4.481  1.00 58.78           C  
ANISOU  835  CA  GLU A  57     7337   8929   6066   1753    439   1159       C  
ATOM    836  C   GLU A  57     -46.929 -39.521  -5.509  1.00 54.80           C  
ANISOU  836  C   GLU A  57     6657   8525   5640   1704    441   1258       C  
ATOM    837  O   GLU A  57     -48.093 -39.129  -5.566  1.00 61.90           O  
ANISOU  837  O   GLU A  57     7429   9583   6505   1778    515   1290       O  
ATOM    838  CB  GLU A  57     -46.609 -38.960  -3.094  1.00 67.84           C  
ANISOU  838  CB  GLU A  57     8456  10211   7110   1837    559   1255       C  
ATOM    839  CG  GLU A  57     -45.840 -38.181  -2.021  1.00 65.27           C  
ANISOU  839  CG  GLU A  57     8290   9817   6693   1906    546   1142       C  
ATOM    840  CD  GLU A  57     -45.075 -39.062  -1.041  1.00 75.70           C  
ANISOU  840  CD  GLU A  57     9655  11099   8007   1830    538   1210       C  
ATOM    841  OE1 GLU A  57     -44.994 -40.293  -1.246  1.00 71.30           O  
ANISOU  841  OE1 GLU A  57     9032  10522   7536   1723    539   1339       O  
ATOM    842  OE2 GLU A  57     -44.544 -38.509  -0.053  1.00 83.05           O  
ANISOU  842  OE2 GLU A  57    10693  12017   8845   1883    529   1140       O  
ATOM    843  H   GLU A  57     -46.051 -36.980  -4.447  1.00 73.48           H  
ATOM    844  HA  GLU A  57     -45.166 -39.500  -4.458  1.00 70.53           H  
ATOM    845  HB2 GLU A  57     -47.495 -38.570  -3.162  1.00 81.41           H  
ATOM    846  HB3 GLU A  57     -46.680 -39.880  -2.795  1.00 81.41           H  
ATOM    847  HG2 GLU A  57     -45.198 -37.600  -2.459  1.00 78.32           H  
ATOM    848  HG3 GLU A  57     -46.470 -37.649  -1.511  1.00 78.32           H  
ATOM    849  N   THR A  58     -46.432 -40.443  -6.327  1.00 53.88           N  
ANISOU  849  N   THR A  58     6509   8274   5687   1536    362   1243       N  
ATOM    850  CA  THR A  58     -47.229 -41.055  -7.383  1.00 59.06           C  
ANISOU  850  CA  THR A  58     6990   8957   6495   1405    347   1246       C  
ATOM    851  C   THR A  58     -46.882 -42.535  -7.469  1.00 60.03           C  
ANISOU  851  C   THR A  58     7084   8951   6774   1209    336   1313       C  
ATOM    852  O   THR A  58     -45.939 -42.988  -6.825  1.00 65.55           O  
ANISOU  852  O   THR A  58     7906   9537   7463   1203    329   1353       O  
ATOM    853  CB  THR A  58     -46.944 -40.399  -8.746  1.00 53.19           C  
ANISOU  853  CB  THR A  58     6270   8150   5788   1415    239   1098       C  
ATOM    854  OG1 THR A  58     -45.719 -40.916  -9.281  1.00 60.21           O  
ANISOU  854  OG1 THR A  58     7265   8844   6766   1315    144   1030       O  
ATOM    855  CG2 THR A  58     -46.840 -38.878  -8.614  1.00 59.72           C  
ANISOU  855  CG2 THR A  58     7214   9018   6459   1618    240   1019       C  
ATOM    856  H   THR A  58     -45.624 -40.734  -6.290  1.00 64.65           H  
ATOM    857  HA  THR A  58     -48.173 -40.963  -7.180  1.00 70.88           H  
ATOM    858  HB  THR A  58     -47.670 -40.603  -9.356  1.00 63.82           H  
ATOM    859  HG1 THR A  58     -45.559 -40.561 -10.026  1.00 72.25           H  
ATOM    860 HG21 THR A  58     -46.120 -38.647  -8.007  1.00 71.66           H  
ATOM    861 HG22 THR A  58     -46.661 -38.482  -9.481  1.00 71.66           H  
ATOM    862 HG23 THR A  58     -47.672 -38.518  -8.269  1.00 71.66           H  
ATOM    863  N   ALA A  59     -47.635 -43.284  -8.269  1.00 48.33           N  
ANISOU  863  N   ALA A  59     5446   7485   5432   1053    332   1324       N  
ATOM    864  CA  ALA A  59     -47.401 -44.718  -8.420  1.00 49.31           C  
ANISOU  864  CA  ALA A  59     5558   7460   5717    855    331   1378       C  
ATOM    865  C   ALA A  59     -46.014 -44.970  -9.003  1.00 50.16           C  
ANISOU  865  C   ALA A  59     5825   7349   5884    834    228   1279       C  
ATOM    866  O   ALA A  59     -45.256 -45.818  -8.509  1.00 53.47           O  
ANISOU  866  O   ALA A  59     6339   7625   6353    793    241   1346       O  
ATOM    867  CB  ALA A  59     -48.478 -45.339  -9.305  1.00 47.43           C  
ANISOU  867  CB  ALA A  59     5128   7285   5608    676    330   1368       C  
ATOM    868  H   ALA A  59     -48.291 -42.985  -8.738  1.00 57.99           H  
ATOM    869  HA  ALA A  59     -47.444 -45.141  -7.548  1.00 59.17           H  
ATOM    870  HB1 ALA A  59     -48.452 -44.916 -10.177  1.00 56.92           H  
ATOM    871  HB2 ALA A  59     -48.305 -46.289  -9.392  1.00 56.92           H  
ATOM    872  HB3 ALA A  59     -49.345 -45.197  -8.894  1.00 56.92           H  
ATOM    873  N   GLU A  60     -45.685 -44.218 -10.051  1.00 47.49           N  
ANISOU  873  N   GLU A  60     5514   6997   5535    877    132   1131       N  
ATOM    874  CA  GLU A  60     -44.377 -44.311 -10.686  1.00 49.86           C  
ANISOU  874  CA  GLU A  60     5948   7119   5878    870     39   1029       C  
ATOM    875  C   GLU A  60     -43.276 -44.119  -9.651  1.00 46.70           C  
ANISOU  875  C   GLU A  60     5695   6661   5388    977     44   1073       C  
ATOM    876  O   GLU A  60     -42.351 -44.924  -9.564  1.00 51.02           O  
ANISOU  876  O   GLU A  60     6318   7064   6002    935     23   1095       O  
ATOM    877  CB  GLU A  60     -44.243 -43.262 -11.792  1.00 40.66           C  
ANISOU  877  CB  GLU A  60     4795   5985   4670    933    -46    883       C  
ATOM    878  CG  GLU A  60     -44.676 -43.751 -13.166  1.00 47.45           C  
ANISOU  878  CG  GLU A  60     5561   6825   5641    802   -103    798       C  
ATOM    879  CD  GLU A  60     -44.672 -42.649 -14.209  1.00 55.06           C  
ANISOU  879  CD  GLU A  60     6531   7850   6540    885   -175    680       C  
ATOM    880  OE1 GLU A  60     -44.145 -41.553 -13.922  1.00 60.06           O  
ANISOU  880  OE1 GLU A  60     7269   8491   7060   1030   -182    655       O  
ATOM    881  OE2 GLU A  60     -45.201 -42.878 -15.317  1.00 51.63           O  
ANISOU  881  OE2 GLU A  60     6003   7455   6160    800   -224    613       O  
ATOM    882  H   GLU A  60     -46.208 -43.641 -10.415  1.00 56.99           H  
ATOM    883  HA  GLU A  60     -44.273 -45.190 -11.083  1.00 59.83           H  
ATOM    884  HB2 GLU A  60     -44.793 -42.497 -11.564  1.00 48.79           H  
ATOM    885  HB3 GLU A  60     -43.313 -42.991 -11.855  1.00 48.79           H  
ATOM    886  HG2 GLU A  60     -44.066 -44.445 -13.461  1.00 56.93           H  
ATOM    887  HG3 GLU A  60     -45.577 -44.105 -13.106  1.00 56.93           H  
ATOM    888  N   ALA A  61     -43.401 -43.061  -8.854  1.00 32.25           N  
ANISOU  888  N   ALA A  61     3902   4952   3398   1120     74   1086       N  
ATOM    889  CA  ALA A  61     -42.400 -42.726  -7.845  1.00 37.44           C  
ANISOU  889  CA  ALA A  61     4695   5591   3940   1219     67   1109       C  
ATOM    890  C   ALA A  61     -42.139 -43.902  -6.905  1.00 43.73           C  
ANISOU  890  C   ALA A  61     5504   6340   4770   1177    120   1258       C  
ATOM    891  O   ALA A  61     -40.988 -44.206  -6.592  1.00 45.80           O  
ANISOU  891  O   ALA A  61     5862   6518   5023   1199     75   1267       O  
ATOM    892  CB  ALA A  61     -42.830 -41.490  -7.051  1.00 28.73           C  
ANISOU  892  CB  ALA A  61     3627   4628   2661   1359    114   1092       C  
ATOM    893  H   ALA A  61     -44.064 -42.514  -8.879  1.00 38.70           H  
ATOM    894  HA  ALA A  61     -41.566 -42.515  -8.292  1.00 44.93           H  
ATOM    895  HB1 ALA A  61     -43.675 -41.675  -6.613  1.00 34.48           H  
ATOM    896  HB2 ALA A  61     -42.151 -41.289  -6.389  1.00 34.48           H  
ATOM    897  HB3 ALA A  61     -42.929 -40.743  -7.661  1.00 34.48           H  
ATOM    898  N   THR A  62     -43.203 -44.568  -6.463  1.00 46.64           N  
ANISOU  898  N   THR A  62     5772   6771   5177   1118    220   1384       N  
ATOM    899  CA  THR A  62     -43.047 -45.739  -5.605  1.00 56.34           C  
ANISOU  899  CA  THR A  62     7020   7939   6446   1071    287   1548       C  
ATOM    900  C   THR A  62     -42.381 -46.866  -6.376  1.00 53.30           C  
ANISOU  900  C   THR A  62     6668   7344   6240    955    240   1535       C  
ATOM    901  O   THR A  62     -41.486 -47.532  -5.854  1.00 49.36           O  
ANISOU  901  O   THR A  62     6259   6744   5749    984    238   1614       O  
ATOM    902  CB  THR A  62     -44.392 -46.256  -5.040  1.00 49.42           C  
ANISOU  902  CB  THR A  62     6020   7169   5589   1004    418   1694       C  
ATOM    903  OG1 THR A  62     -45.179 -46.824  -6.095  1.00 60.56           O  
ANISOU  903  OG1 THR A  62     7307   8537   7167    837    417   1657       O  
ATOM    904  CG2 THR A  62     -45.170 -45.139  -4.350  1.00 49.65           C  
ANISOU  904  CG2 THR A  62     6004   7420   5442   1137    479   1703       C  
ATOM    905  H   THR A  62     -44.019 -44.364  -6.643  1.00 55.96           H  
ATOM    906  HA  THR A  62     -42.476 -45.508  -4.856  1.00 67.60           H  
ATOM    907  HB  THR A  62     -44.211 -46.944  -4.380  1.00 59.30           H  
ATOM    908  HG1 THR A  62     -45.335 -46.243  -6.682  1.00 72.68           H  
ATOM    909 HG21 THR A  62     -45.359 -44.428  -4.982  1.00 59.58           H  
ATOM    910 HG22 THR A  62     -46.008 -45.484  -4.004  1.00 59.58           H  
ATOM    911 HG23 THR A  62     -44.650 -44.779  -3.615  1.00 59.58           H  
ATOM    912  N   ARG A  63     -42.816 -47.086  -7.615  1.00 48.36           N  
ANISOU  912  N   ARG A  63     5970   6657   5746    835    205   1435       N  
ATOM    913  CA  ARG A  63     -42.194 -48.112  -8.448  1.00 50.23           C  
ANISOU  913  CA  ARG A  63     6254   6686   6147    731    163   1393       C  
ATOM    914  C   ARG A  63     -40.693 -47.882  -8.652  1.00 53.65           C  
ANISOU  914  C   ARG A  63     6808   7028   6551    831     74   1318       C  
ATOM    915  O   ARG A  63     -39.960 -48.824  -8.947  1.00 56.34           O  
ANISOU  915  O   ARG A  63     7213   7197   6998    798     62   1329       O  
ATOM    916  CB  ARG A  63     -42.890 -48.206  -9.808  1.00 54.42           C  
ANISOU  916  CB  ARG A  63     6690   7197   6789    595    124   1266       C  
ATOM    917  CG  ARG A  63     -44.165 -49.035  -9.805  1.00 60.93           C  
ANISOU  917  CG  ARG A  63     7394   8040   7717    422    205   1345       C  
ATOM    918  CD  ARG A  63     -44.712 -49.172 -11.214  1.00 61.85           C  
ANISOU  918  CD  ARG A  63     7422   8143   7933    280    142   1199       C  
ATOM    919  NE  ARG A  63     -46.089 -48.695 -11.324  1.00 75.67           N  
ANISOU  919  NE  ARG A  63     8989  10112   9650    228    168   1206       N  
ATOM    920  CZ  ARG A  63     -46.611 -48.129 -12.410  1.00 84.87           C  
ANISOU  920  CZ  ARG A  63    10054  11387  10807    201     93   1075       C  
ATOM    921  NH1 ARG A  63     -45.879 -47.948 -13.503  1.00 84.31           N  
ANISOU  921  NH1 ARG A  63    10056  11221  10755    213     -9    923       N  
ATOM    922  NH2 ARG A  63     -47.877 -47.733 -12.401  1.00 84.26           N  
ANISOU  922  NH2 ARG A  63     9792  11531  10692    174    124   1106       N  
ATOM    923  H   ARG A  63     -43.461 -46.660  -7.992  1.00 58.03           H  
ATOM    924  HA  ARG A  63     -42.300 -48.970  -8.008  1.00 60.28           H  
ATOM    925  HB2 ARG A  63     -43.121 -47.310 -10.100  1.00 65.30           H  
ATOM    926  HB3 ARG A  63     -42.277 -48.609 -10.443  1.00 65.30           H  
ATOM    927  HG2 ARG A  63     -43.973 -49.922  -9.463  1.00 73.12           H  
ATOM    928  HG3 ARG A  63     -44.834 -48.597  -9.256  1.00 73.12           H  
ATOM    929  HD2 ARG A  63     -44.163 -48.650 -11.819  1.00 74.22           H  
ATOM    930  HD3 ARG A  63     -44.695 -50.107 -11.471  1.00 74.22           H  
ATOM    931  HE  ARG A  63     -46.599 -48.787 -10.637  1.00 90.80           H  
ATOM    932 HH11 ARG A  63     -45.057 -48.202 -13.517  1.00101.17           H  
ATOM    933 HH12 ARG A  63     -46.227 -47.580 -14.198  1.00101.17           H  
ATOM    934 HH21 ARG A  63     -48.357 -47.845 -11.696  1.00101.11           H  
ATOM    935 HH22 ARG A  63     -48.218 -47.365 -13.099  1.00101.11           H  
ATOM    936  N   LEU A  64     -40.238 -46.642  -8.485  1.00 42.45           N  
ANISOU  936  N   LEU A  64     5420   5722   4987    952     19   1242       N  
ATOM    937  CA  LEU A  64     -38.830 -46.306  -8.709  1.00 33.10           C  
ANISOU  937  CA  LEU A  64     4326   4483   3768   1028    -68   1163       C  
ATOM    938  C   LEU A  64     -37.986 -46.410  -7.436  1.00 33.21           C  
ANISOU  938  C   LEU A  64     4410   4529   3678   1129    -62   1267       C  
ATOM    939  O   LEU A  64     -36.787 -46.128  -7.454  1.00 29.58           O  
ANISOU  939  O   LEU A  64     3994   4044   3201   1136   -130   1159       O  
ATOM    940  CB  LEU A  64     -38.698 -44.900  -9.303  1.00 28.99           C  
ANISOU  940  CB  LEU A  64     3811   4047   3156   1077   -136   1013       C  
ATOM    941  CG  LEU A  64     -39.273 -44.671 -10.704  1.00 30.07           C  
ANISOU  941  CG  LEU A  64     3888   4163   3374   1001   -167    891       C  
ATOM    942  CD1 LEU A  64     -38.945 -43.268 -11.172  1.00 29.49           C  
ANISOU  942  CD1 LEU A  64     3853   4153   3198   1073   -227    769       C  
ATOM    943  CD2 LEU A  64     -38.761 -45.694 -11.704  1.00 25.57           C  
ANISOU  943  CD2 LEU A  64     3325   3434   2956    912   -199    842       C  
ATOM    944  H   LEU A  64     -40.723 -45.974  -8.243  1.00 50.94           H  
ATOM    945  HA  LEU A  64     -38.463 -46.932  -9.354  1.00 39.72           H  
ATOM    946  HB2 LEU A  64     -39.146 -44.279  -8.707  1.00 34.78           H  
ATOM    947  HB3 LEU A  64     -37.755 -44.678  -9.343  1.00 34.78           H  
ATOM    948  HG  LEU A  64     -40.239 -44.753 -10.664  1.00 36.08           H  
ATOM    949 HD11 LEU A  64     -37.981 -43.162 -11.196  1.00 35.38           H  
ATOM    950 HD12 LEU A  64     -39.314 -43.137 -12.060  1.00 35.38           H  
ATOM    951 HD13 LEU A  64     -39.333 -42.630 -10.554  1.00 35.38           H  
ATOM    952 HD21 LEU A  64     -39.018 -46.581 -11.408  1.00 30.69           H  
ATOM    953 HD22 LEU A  64     -39.152 -45.508 -12.573  1.00 30.69           H  
ATOM    954 HD23 LEU A  64     -37.795 -45.628 -11.755  1.00 30.69           H  
ATOM    955  N   LYS A  65     -38.611 -46.817  -6.336  1.00 30.12           N  
ANISOU  955  N   LYS A  65     4008   4196   3242   1140     25   1415       N  
ATOM    956  CA  LYS A  65     -37.896 -47.008  -5.080  1.00 32.43           C  
ANISOU  956  CA  LYS A  65     4347   4517   3458   1175     37   1449       C  
ATOM    957  C   LYS A  65     -37.548 -48.475  -4.878  1.00 35.94           C  
ANISOU  957  C   LYS A  65     4824   4820   4010   1161     77   1597       C  
ATOM    958  O   LYS A  65     -38.298 -49.360  -5.287  1.00 45.38           O  
ANISOU  958  O   LYS A  65     6005   5911   5325   1108    148   1729       O  
ATOM    959  CB  LYS A  65     -38.732 -46.512  -3.897  1.00 37.89           C  
ANISOU  959  CB  LYS A  65     5018   5364   4016   1212    114   1510       C  
ATOM    960  CG  LYS A  65     -38.368 -45.110  -3.434  1.00 37.54           C  
ANISOU  960  CG  LYS A  65     5000   5432   3831   1258     68   1350       C  
ATOM    961  CD  LYS A  65     -39.099 -44.730  -2.156  1.00 53.39           C  
ANISOU  961  CD  LYS A  65     7001   7581   5705   1316    151   1412       C  
ATOM    962  CE  LYS A  65     -40.453 -44.109  -2.449  1.00 50.23           C  
ANISOU  962  CE  LYS A  65     6540   7274   5273   1339    219   1416       C  
ATOM    963  NZ  LYS A  65     -41.262 -43.937  -1.211  1.00 57.66           N  
ANISOU  963  NZ  LYS A  65     7459   8355   6096   1403    322   1503       N  
ATOM    964  H   LYS A  65     -39.453 -46.991  -6.291  1.00 36.15           H  
ATOM    965  HA  LYS A  65     -37.070 -46.500  -5.102  1.00 38.92           H  
ATOM    966  HB2 LYS A  65     -39.667 -46.506  -4.156  1.00 45.47           H  
ATOM    967  HB3 LYS A  65     -38.602 -47.115  -3.148  1.00 45.47           H  
ATOM    968  HG2 LYS A  65     -37.414 -45.069  -3.262  1.00 45.05           H  
ATOM    969  HG3 LYS A  65     -38.612 -44.473  -4.124  1.00 45.05           H  
ATOM    970  HD2 LYS A  65     -39.239 -45.526  -1.620  1.00 64.07           H  
ATOM    971  HD3 LYS A  65     -38.568 -44.084  -1.665  1.00 64.07           H  
ATOM    972  HE2 LYS A  65     -40.323 -43.236  -2.850  1.00 60.28           H  
ATOM    973  HE3 LYS A  65     -40.944 -44.686  -3.055  1.00 60.28           H  
ATOM    974  HZ1 LYS A  65     -40.834 -43.406  -0.639  1.00 69.20           H  
ATOM    975  HZ2 LYS A  65     -42.049 -43.572  -1.410  1.00 69.20           H  
ATOM    976  HZ3 LYS A  65     -41.400 -44.727  -0.825  1.00 69.20           H  
ATOM    977  N   ARG A  66     -36.403 -48.727  -4.255  1.00 39.53           N  
ANISOU  977  N   ARG A  66     6045   3872   5102    378   -478    768       N  
ATOM    978  CA  ARG A  66     -36.037 -50.081  -3.878  1.00 28.65           C  
ANISOU  978  CA  ARG A  66     4574   2574   3739    332   -425    747       C  
ATOM    979  C   ARG A  66     -37.020 -50.606  -2.845  1.00 31.80           C  
ANISOU  979  C   ARG A  66     4862   3040   4180    445   -388    772       C  
ATOM    980  O   ARG A  66     -37.481 -49.865  -1.975  1.00 28.91           O  
ANISOU  980  O   ARG A  66     4513   2658   3815    565   -372    771       O  
ATOM    981  CB  ARG A  66     -34.632 -50.119  -3.288  1.00 23.50           C  
ANISOU  981  CB  ARG A  66     3968   1905   3057    275   -385    679       C  
ATOM    982  CG  ARG A  66     -33.516 -50.104  -4.310  1.00 21.57           C  
ANISOU  982  CG  ARG A  66     3786   1634   2776    138   -400    660       C  
ATOM    983  CD  ARG A  66     -32.169 -49.900  -3.637  1.00 20.77           C  
ANISOU  983  CD  ARG A  66     3729   1511   2651     93   -368    604       C  
ATOM    984  NE  ARG A  66     -31.600 -48.593  -3.971  1.00 40.59           N  
ANISOU  984  NE  ARG A  66     6361   3934   5126     56   -409    600       N  
ATOM    985  CZ  ARG A  66     -30.510 -48.395  -4.711  1.00 41.20           C  
ANISOU  985  CZ  ARG A  66     6488   3993   5172    -63   -416    594       C  
ATOM    986  NH1 ARG A  66     -29.816 -49.415  -5.205  1.00 49.41           N  
ANISOU  986  NH1 ARG A  66     7471   5097   6206   -149   -377    582       N  
ATOM    987  NH2 ARG A  66     -30.098 -47.157  -4.947  1.00 27.49           N  
ANISOU  987  NH2 ARG A  66     4862   2172   3409    -96   -461    602       N  
ATOM    988  H   ARG A  66     -35.822 -48.130  -4.040  1.00 47.43           H  
ATOM    989  HA  ARG A  66     -36.065 -50.658  -4.658  1.00 34.38           H  
ATOM    990  HB2 ARG A  66     -34.516 -49.345  -2.716  1.00 28.20           H  
ATOM    991  HB3 ARG A  66     -34.539 -50.930  -2.764  1.00 28.20           H  
ATOM    992  HG2 ARG A  66     -33.498 -50.953  -4.780  1.00 25.88           H  
ATOM    993  HG3 ARG A  66     -33.660 -49.376  -4.934  1.00 25.88           H  
ATOM    994  HD2 ARG A  66     -32.281 -49.946  -2.675  1.00 24.92           H  
ATOM    995  HD3 ARG A  66     -31.553 -50.586  -3.938  1.00 24.92           H  
ATOM    996  HE  ARG A  66     -32.002 -47.898  -3.664  1.00 48.70           H  
ATOM    997 HH11 ARG A  66     -30.075 -50.222  -5.058  1.00 59.29           H  
ATOM    998 HH12 ARG A  66     -29.113 -49.268  -5.677  1.00 59.29           H  
ATOM    999 HH21 ARG A  66     -30.537 -46.490  -4.628  1.00 32.98           H  
ATOM   1000 HH22 ARG A  66     -29.392 -47.022  -5.418  1.00 32.98           H  
ATOM   1001  N   THR A  67     -37.325 -51.893  -2.940  1.00 41.77           N  
ANISOU 1001  N   THR A  67     6017   4378   5475    408   -373    797       N  
ATOM   1002  CA  THR A  67     -38.197 -52.550  -1.973  1.00 42.62           C  
ANISOU 1002  CA  THR A  67     6006   4562   5625    495   -334    832       C  
ATOM   1003  C   THR A  67     -37.629 -53.925  -1.657  1.00 42.55           C  
ANISOU 1003  C   THR A  67     5930   4608   5631    423   -297    813       C  
ATOM   1004  O   THR A  67     -37.065 -54.584  -2.531  1.00 41.38           O  
ANISOU 1004  O   THR A  67     5794   4452   5478    312   -319    797       O  
ATOM   1005  CB  THR A  67     -39.640 -52.716  -2.498  1.00 40.73           C  
ANISOU 1005  CB  THR A  67     5678   4365   5433    537   -376    920       C  
ATOM   1006  OG1 THR A  67     -39.733 -53.906  -3.288  1.00 41.55           O  
ANISOU 1006  OG1 THR A  67     5720   4505   5562    431   -407    947       O  
ATOM   1007  CG2 THR A  67     -40.068 -51.512  -3.331  1.00 55.40           C  
ANISOU 1007  CG2 THR A  67     7613   6157   7277    566   -437    945       C  
ATOM   1008  H   THR A  67     -37.038 -52.414  -3.562  1.00 50.12           H  
ATOM   1009  HA  THR A  67     -38.223 -52.031  -1.154  1.00 51.14           H  
ATOM   1010  HB  THR A  67     -40.245 -52.789  -1.744  1.00 48.88           H  
ATOM   1011  HG1 THR A  67     -40.517 -53.999  -3.575  1.00 49.86           H  
ATOM   1012 HG21 THR A  67     -39.477 -51.410  -4.094  1.00 66.48           H  
ATOM   1013 HG22 THR A  67     -40.976 -51.636  -3.651  1.00 66.48           H  
ATOM   1014 HG23 THR A  67     -40.031 -50.706  -2.793  1.00 66.48           H  
ATOM   1015  N   ALA A  68     -37.780 -54.354  -0.408  1.00 42.03           N  
ANISOU 1015  N   ALA A  68     5797   4594   5579    490   -241    813       N  
ATOM   1016  CA  ALA A  68     -37.267 -55.646   0.029  1.00 27.66           C  
ANISOU 1016  CA  ALA A  68     3912   2821   3776    432   -208    800       C  
ATOM   1017  C   ALA A  68     -37.932 -56.783  -0.745  1.00 34.09           C  
ANISOU 1017  C   ALA A  68     4639   3675   4638    367   -246    856       C  
ATOM   1018  O   ALA A  68     -37.301 -57.800  -1.051  1.00 34.59           O  
ANISOU 1018  O   ALA A  68     4692   3742   4710    278   -248    833       O  
ATOM   1019  CB  ALA A  68     -37.492 -55.819   1.523  1.00 30.10           C  
ANISOU 1019  CB  ALA A  68     4164   3185   4088    526   -146    807       C  
ATOM   1020  H   ALA A  68     -38.179 -53.909   0.211  1.00 50.44           H  
ATOM   1021  HA  ALA A  68     -36.312 -55.684  -0.139  1.00 33.19           H  
ATOM   1022  HB1 ALA A  68     -38.444 -55.770   1.706  1.00 36.12           H  
ATOM   1023  HB2 ALA A  68     -37.146 -56.683   1.796  1.00 36.12           H  
ATOM   1024  HB3 ALA A  68     -37.028 -55.111   1.996  1.00 36.12           H  
ATOM   1025  N   ARG A  69     -39.208 -56.599  -1.069  1.00 35.01           N  
ANISOU 1025  N   ARG A  69     4696   3818   4788    413   -281    931       N  
ATOM   1026  CA  ARG A  69     -39.987 -57.635  -1.738  1.00 39.74           C  
ANISOU 1026  CA  ARG A  69     5206   4455   5437    353   -330    996       C  
ATOM   1027  C   ARG A  69     -39.499 -57.893  -3.169  1.00 42.87           C  
ANISOU 1027  C   ARG A  69     5676   4799   5813    235   -393    968       C  
ATOM   1028  O   ARG A  69     -39.388 -59.046  -3.597  1.00 41.18           O  
ANISOU 1028  O   ARG A  69     5434   4595   5619    151   -418    970       O  
ATOM   1029  CB  ARG A  69     -41.477 -57.268  -1.725  1.00 50.22           C  
ANISOU 1029  CB  ARG A  69     6445   5828   6806    434   -356   1092       C  
ATOM   1030  CG  ARG A  69     -42.307 -58.117  -0.764  1.00 58.54           C  
ANISOU 1030  CG  ARG A  69     7354   6974   7914    478   -322   1166       C  
ATOM   1031  CD  ARG A  69     -43.453 -57.344  -0.126  1.00 66.81           C  
ANISOU 1031  CD  ARG A  69     8326   8078   8981    618   -294   1236       C  
ATOM   1032  NE  ARG A  69     -43.005 -56.531   1.004  1.00 74.92           N  
ANISOU 1032  NE  ARG A  69     9406   9102   9959    729   -214   1181       N  
ATOM   1033  CZ  ARG A  69     -43.802 -56.083   1.972  1.00 76.93           C  
ANISOU 1033  CZ  ARG A  69     9594   9420  10217    868   -156   1226       C  
ATOM   1034  NH1 ARG A  69     -45.098 -56.367   1.963  1.00 71.33           N  
ANISOU 1034  NH1 ARG A  69     8743   8793   9564    913   -165   1335       N  
ATOM   1035  NH2 ARG A  69     -43.300 -55.351   2.958  1.00 79.74           N  
ANISOU 1035  NH2 ARG A  69    10023   9761  10516    964    -90   1162       N  
ATOM   1036  H   ARG A  69     -39.648 -55.878  -0.911  1.00 42.01           H  
ATOM   1037  HA  ARG A  69     -39.887 -58.463  -1.242  1.00 47.68           H  
ATOM   1038  HB2 ARG A  69     -41.569 -56.340  -1.457  1.00 60.26           H  
ATOM   1039  HB3 ARG A  69     -41.837 -57.390  -2.617  1.00 60.26           H  
ATOM   1040  HG2 ARG A  69     -42.685 -58.866  -1.252  1.00 70.25           H  
ATOM   1041  HG3 ARG A  69     -41.732 -58.442  -0.054  1.00 70.25           H  
ATOM   1042  HD2 ARG A  69     -43.845 -56.753  -0.787  1.00 80.17           H  
ATOM   1043  HD3 ARG A  69     -44.118 -57.971   0.198  1.00 80.17           H  
ATOM   1044  HE  ARG A  69     -42.171 -56.328   1.046  1.00 89.91           H  
ATOM   1045 HH11 ARG A  69     -45.430 -56.842   1.327  1.00 85.59           H  
ATOM   1046 HH12 ARG A  69     -45.607 -56.075   2.592  1.00 85.59           H  
ATOM   1047 HH21 ARG A  69     -42.460 -55.164   2.970  1.00 95.69           H  
ATOM   1048 HH22 ARG A  69     -43.814 -55.062   3.584  1.00 95.69           H  
ATOM   1049  N   ARG A  70     -39.203 -56.823  -3.904  1.00 34.59           N  
ANISOU 1049  N   ARG A  70     4729   3694   4721    230   -418    942       N  
ATOM   1050  CA  ARG A  70     -38.708 -56.948  -5.275  1.00 28.79           C  
ANISOU 1050  CA  ARG A  70     4073   2916   3951    124   -470    916       C  
ATOM   1051  C   ARG A  70     -37.377 -57.701  -5.275  1.00 34.86           C  
ANISOU 1051  C   ARG A  70     4882   3673   4692     47   -429    839       C  
ATOM   1052  O   ARG A  70     -37.151 -58.592  -6.099  1.00 33.02           O  
ANISOU 1052  O   ARG A  70     4659   3436   4452    -37   -458    826       O  
ATOM   1053  CB  ARG A  70     -38.551 -55.563  -5.921  1.00 34.28           C  
ANISOU 1053  CB  ARG A  70     4873   3552   4600    137   -496    907       C  
ATOM   1054  CG  ARG A  70     -39.154 -55.441  -7.321  1.00 35.35           C  
ANISOU 1054  CG  ARG A  70     5040   3669   4724     81   -582    951       C  
ATOM   1055  CD  ARG A  70     -39.866 -54.109  -7.537  1.00 38.04           C  
ANISOU 1055  CD  ARG A  70     5414   3977   5062    154   -621    997       C  
ATOM   1056  NE  ARG A  70     -38.974 -52.960  -7.395  1.00 34.52           N  
ANISOU 1056  NE  ARG A  70     5080   3470   4568    169   -594    947       N  
ATOM   1057  CZ  ARG A  70     -39.179 -51.775  -7.965  1.00 34.57           C  
ANISOU 1057  CZ  ARG A  70     5167   3419   4551    190   -640    970       C  
ATOM   1058  NH1 ARG A  70     -40.242 -51.571  -8.732  1.00 32.35           N  
ANISOU 1058  NH1 ARG A  70     4864   3141   4288    204   -714   1041       N  
ATOM   1059  NH2 ARG A  70     -38.314 -50.790  -7.774  1.00 39.20           N  
ANISOU 1059  NH2 ARG A  70     5855   3942   5096    193   -619    926       N  
ATOM   1060  H   ARG A  70     -39.280 -56.011  -3.631  1.00 41.51           H  
ATOM   1061  HA  ARG A  70     -39.346 -57.458  -5.800  1.00 34.55           H  
ATOM   1062  HB2 ARG A  70     -38.986 -54.906  -5.356  1.00 41.14           H  
ATOM   1063  HB3 ARG A  70     -37.605 -55.359  -5.990  1.00 41.14           H  
ATOM   1064  HG2 ARG A  70     -38.445 -55.514  -7.978  1.00 42.42           H  
ATOM   1065  HG3 ARG A  70     -39.801 -56.152  -7.449  1.00 42.42           H  
ATOM   1066  HD2 ARG A  70     -40.237 -54.092  -8.433  1.00 45.65           H  
ATOM   1067  HD3 ARG A  70     -40.575 -54.020  -6.882  1.00 45.65           H  
ATOM   1068  HE  ARG A  70     -38.270 -53.056  -6.912  1.00 41.43           H  
ATOM   1069 HH11 ARG A  70     -40.808 -52.205  -8.860  1.00 38.83           H  
ATOM   1070 HH12 ARG A  70     -40.367 -50.803  -9.098  1.00 38.83           H  
ATOM   1071 HH21 ARG A  70     -37.622 -50.916  -7.280  1.00 47.04           H  
ATOM   1072 HH22 ARG A  70     -38.445 -50.025  -8.145  1.00 47.04           H  
ATOM   1073  N   ARG A  71     -36.512 -57.346  -4.328  1.00 24.01           N  
ANISOU 1073  N   ARG A  71     3530   2292   3301     81   -365    790       N  
ATOM   1074  CA  ARG A  71     -35.218 -58.000  -4.146  1.00 28.54           C  
ANISOU 1074  CA  ARG A  71     4126   2861   3855     24   -321    723       C  
ATOM   1075  C   ARG A  71     -35.409 -59.490  -3.843  1.00 36.97           C  
ANISOU 1075  C   ARG A  71     5108   3969   4969      0   -316    735       C  
ATOM   1076  O   ARG A  71     -34.796 -60.366  -4.478  1.00 38.15           O  
ANISOU 1076  O   ARG A  71     5277   4109   5110    -74   -323    700       O  
ATOM   1077  CB  ARG A  71     -34.462 -57.298  -3.009  1.00 22.36           C  
ANISOU 1077  CB  ARG A  71     3369   2070   3056     76   -265    684       C  
ATOM   1078  CG  ARG A  71     -33.065 -57.835  -2.727  1.00 26.15           C  
ANISOU 1078  CG  ARG A  71     3866   2550   3520     23   -221    621       C  
ATOM   1079  CD  ARG A  71     -32.203 -56.836  -1.957  1.00 25.45           C  
ANISOU 1079  CD  ARG A  71     3835   2436   3401     49   -190    581       C  
ATOM   1080  NE  ARG A  71     -32.906 -56.217  -0.830  1.00 37.16           N  
ANISOU 1080  NE  ARG A  71     5301   3925   4891    152   -179    602       N  
ATOM   1081  CZ  ARG A  71     -33.255 -54.933  -0.753  1.00 40.47           C  
ANISOU 1081  CZ  ARG A  71     5786   4304   5288    207   -197    608       C  
ATOM   1082  NH1 ARG A  71     -32.973 -54.083  -1.736  1.00 36.63           N  
ANISOU 1082  NH1 ARG A  71     5384   3762   4771    160   -234    602       N  
ATOM   1083  NH2 ARG A  71     -33.890 -54.491   0.325  1.00 35.71           N  
ANISOU 1083  NH2 ARG A  71     5166   3713   4688    314   -178    621       N  
ATOM   1084  H   ARG A  71     -36.656 -56.712  -3.765  1.00 28.81           H  
ATOM   1085  HA  ARG A  71     -34.696 -57.917  -4.959  1.00 34.24           H  
ATOM   1086  HB2 ARG A  71     -34.373 -56.358  -3.233  1.00 26.83           H  
ATOM   1087  HB3 ARG A  71     -34.980 -57.389  -2.193  1.00 26.83           H  
ATOM   1088  HG2 ARG A  71     -33.137 -58.643  -2.195  1.00 31.38           H  
ATOM   1089  HG3 ARG A  71     -32.624 -58.028  -3.568  1.00 31.38           H  
ATOM   1090  HD2 ARG A  71     -31.424 -57.297  -1.606  1.00 30.55           H  
ATOM   1091  HD3 ARG A  71     -31.925 -56.129  -2.560  1.00 30.55           H  
ATOM   1092  HE  ARG A  71     -33.110 -56.723  -0.165  1.00 44.59           H  
ATOM   1093 HH11 ARG A  71     -32.560 -54.360  -2.438  1.00 43.95           H  
ATOM   1094 HH12 ARG A  71     -33.204 -53.258  -1.670  1.00 43.95           H  
ATOM   1095 HH21 ARG A  71     -34.077 -55.033   0.966  1.00 42.85           H  
ATOM   1096 HH22 ARG A  71     -34.118 -53.664   0.381  1.00 42.85           H  
ATOM   1097  N   TYR A  72     -36.278 -59.761  -2.873  1.00 39.56           N  
ANISOU 1097  N   TYR A  72     5346   4342   5345     66   -305    788       N  
ATOM   1098  CA  TYR A  72     -36.656 -61.125  -2.521  1.00 38.35           C  
ANISOU 1098  CA  TYR A  72     5104   4225   5243     44   -311    820       C  
ATOM   1099  C   TYR A  72     -37.091 -61.915  -3.756  1.00 37.08           C  
ANISOU 1099  C   TYR A  72     4946   4047   5095    -38   -384    839       C  
ATOM   1100  O   TYR A  72     -36.603 -63.023  -4.003  1.00 39.58           O  
ANISOU 1100  O   TYR A  72     5266   4351   5421    -99   -392    810       O  
ATOM   1101  CB  TYR A  72     -37.785 -61.092  -1.486  1.00 31.77           C  
ANISOU 1101  CB  TYR A  72     4167   3451   4454    128   -296    897       C  
ATOM   1102  CG  TYR A  72     -38.432 -62.430  -1.203  1.00 38.30           C  
ANISOU 1102  CG  TYR A  72     4891   4319   5342     98   -316    958       C  
ATOM   1103  CD1 TYR A  72     -39.513 -62.877  -1.956  1.00 33.98           C  
ANISOU 1103  CD1 TYR A  72     4292   3783   4836     59   -390   1029       C  
ATOM   1104  CD2 TYR A  72     -37.976 -63.239  -0.171  1.00 42.96           C  
ANISOU 1104  CD2 TYR A  72     5437   4934   5950    103   -271    951       C  
ATOM   1105  CE1 TYR A  72     -40.110 -64.094  -1.698  1.00 36.02           C  
ANISOU 1105  CE1 TYR A  72     4458   4073   5154     20   -419   1092       C  
ATOM   1106  CE2 TYR A  72     -38.568 -64.461   0.095  1.00 39.22           C  
ANISOU 1106  CE2 TYR A  72     4874   4493   5536     69   -296   1015       C  
ATOM   1107  CZ  TYR A  72     -39.634 -64.882  -0.671  1.00 47.17           C  
ANISOU 1107  CZ  TYR A  72     5832   5507   6586     24   -371   1086       C  
ATOM   1108  OH  TYR A  72     -40.226 -66.097  -0.409  1.00 57.48           O  
ANISOU 1108  OH  TYR A  72     7049   6837   7953    -21   -405   1156       O  
ATOM   1109  H   TYR A  72     -36.668 -59.161  -2.397  1.00 47.48           H  
ATOM   1110  HA  TYR A  72     -35.894 -61.576  -2.125  1.00 46.02           H  
ATOM   1111  HB2 TYR A  72     -37.427 -60.758  -0.648  1.00 38.13           H  
ATOM   1112  HB3 TYR A  72     -38.479 -60.493  -1.804  1.00 38.13           H  
ATOM   1113  HD1 TYR A  72     -39.836 -62.348  -2.650  1.00 40.78           H  
ATOM   1114  HD2 TYR A  72     -37.256 -62.958   0.346  1.00 51.55           H  
ATOM   1115  HE1 TYR A  72     -40.829 -64.381  -2.213  1.00 43.22           H  
ATOM   1116  HE2 TYR A  72     -38.249 -64.994   0.787  1.00 47.07           H  
ATOM   1117  HH  TYR A  72     -39.841 -66.471   0.236  1.00 68.97           H  
ATOM   1118  N   THR A  73     -37.997 -61.335  -4.537  1.00 27.41           N  
ANISOU 1118  N   THR A  73     3727   2817   3869    -37   -442    887       N  
ATOM   1119  CA  THR A  73     -38.516 -62.001  -5.730  1.00 31.97           C  
ANISOU 1119  CA  THR A  73     4315   3377   4453   -115   -525    911       C  
ATOM   1120  C   THR A  73     -37.408 -62.239  -6.765  1.00 34.76           C  
ANISOU 1120  C   THR A  73     4781   3683   4745   -193   -529    828       C  
ATOM   1121  O   THR A  73     -37.336 -63.306  -7.385  1.00 32.72           O  
ANISOU 1121  O   THR A  73     4538   3406   4488   -260   -569    812       O  
ATOM   1122  CB  THR A  73     -39.660 -61.182  -6.364  1.00 28.17           C  
ANISOU 1122  CB  THR A  73     3823   2902   3977    -94   -590    981       C  
ATOM   1123  OG1 THR A  73     -40.658 -60.913  -5.373  1.00 34.28           O  
ANISOU 1123  OG1 THR A  73     4486   3731   4807     -7   -572   1059       O  
ATOM   1124  CG2 THR A  73     -40.295 -61.931  -7.539  1.00 28.08           C  
ANISOU 1124  CG2 THR A  73     3818   2876   3976   -180   -690   1014       C  
ATOM   1125  H   THR A  73     -38.330 -60.554  -4.398  1.00 32.89           H  
ATOM   1126  HA  THR A  73     -38.875 -62.865  -5.475  1.00 38.36           H  
ATOM   1127  HB  THR A  73     -39.305 -60.342  -6.696  1.00 33.80           H  
ATOM   1128  HG1 THR A  73     -40.323 -60.477  -4.738  1.00 41.13           H  
ATOM   1129 HG21 THR A  73     -40.659 -62.777  -7.235  1.00 33.70           H  
ATOM   1130 HG22 THR A  73     -41.010 -61.400  -7.923  1.00 33.70           H  
ATOM   1131 HG23 THR A  73     -39.628 -62.102  -8.223  1.00 33.70           H  
ATOM   1132  N   ARG A  74     -36.550 -61.238  -6.941  1.00 34.14           N  
ANISOU 1132  N   ARG A  74     4782   3582   4608   -182   -487    778       N  
ATOM   1133  CA  ARG A  74     -35.389 -61.335  -7.827  1.00 24.77           C  
ANISOU 1133  CA  ARG A  74     3692   2363   3356   -246   -471    704       C  
ATOM   1134  C   ARG A  74     -34.557 -62.582  -7.479  1.00 30.53           C  
ANISOU 1134  C   ARG A  74     4405   3095   4100   -271   -433    651       C  
ATOM   1135  O   ARG A  74     -34.352 -63.497  -8.310  1.00 29.61           O  
ANISOU 1135  O   ARG A  74     4326   2960   3965   -328   -462    620       O  
ATOM   1136  CB  ARG A  74     -34.543 -60.060  -7.672  1.00 24.99           C  
ANISOU 1136  CB  ARG A  74     3782   2377   3337   -224   -420    672       C  
ATOM   1137  CG  ARG A  74     -33.860 -59.549  -8.932  1.00 27.72           C  
ANISOU 1137  CG  ARG A  74     4232   2695   3604   -286   -429    639       C  
ATOM   1138  CD  ARG A  74     -33.095 -58.260  -8.642  1.00 26.60           C  
ANISOU 1138  CD  ARG A  74     4142   2536   3429   -270   -387    623       C  
ATOM   1139  NE  ARG A  74     -33.948 -57.217  -8.069  1.00 34.04           N  
ANISOU 1139  NE  ARG A  74     5069   3466   4397   -199   -410    673       N  
ATOM   1140  CZ  ARG A  74     -33.584 -56.385  -7.094  1.00 30.98           C  
ANISOU 1140  CZ  ARG A  74     4687   3067   4017   -146   -373    662       C  
ATOM   1141  NH1 ARG A  74     -32.375 -56.457  -6.555  1.00 27.91           N  
ANISOU 1141  NH1 ARG A  74     4310   2679   3614   -165   -315    609       N  
ATOM   1142  NH2 ARG A  74     -34.436 -55.473  -6.649  1.00 34.78           N  
ANISOU 1142  NH2 ARG A  74     5164   3532   4517    -71   -396    704       N  
ATOM   1143  H   ARG A  74     -36.620 -60.474  -6.551  1.00 40.97           H  
ATOM   1144  HA  ARG A  74     -35.683 -61.404  -8.748  1.00 29.72           H  
ATOM   1145  HB2 ARG A  74     -35.119 -59.350  -7.348  1.00 29.99           H  
ATOM   1146  HB3 ARG A  74     -33.848 -60.233  -7.018  1.00 29.99           H  
ATOM   1147  HG2 ARG A  74     -33.231 -60.215  -9.251  1.00 33.26           H  
ATOM   1148  HG3 ARG A  74     -34.529 -59.363  -9.610  1.00 33.26           H  
ATOM   1149  HD2 ARG A  74     -32.385 -58.449  -8.008  1.00 31.92           H  
ATOM   1150  HD3 ARG A  74     -32.720 -57.921  -9.470  1.00 31.92           H  
ATOM   1151  HE  ARG A  74     -34.743 -57.135  -8.386  1.00 40.84           H  
ATOM   1152 HH11 ARG A  74     -31.813 -57.044  -6.836  1.00 33.49           H  
ATOM   1153 HH12 ARG A  74     -32.151 -55.914  -5.926  1.00 33.49           H  
ATOM   1154 HH21 ARG A  74     -35.224 -55.417  -6.990  1.00 41.73           H  
ATOM   1155 HH22 ARG A  74     -34.202 -54.937  -6.019  1.00 41.73           H  
ATOM   1156  N   ARG A  75     -34.109 -62.624  -6.227  1.00 28.49           N  
ANISOU 1156  N   ARG A  75     4094   2857   3872   -223   -371    640       N  
ATOM   1157  CA  ARG A  75     -33.309 -63.740  -5.742  1.00 23.12           C  
ANISOU 1157  CA  ARG A  75     3391   2180   3214   -236   -335    597       C  
ATOM   1158  C   ARG A  75     -34.044 -65.075  -5.904  1.00 28.17           C  
ANISOU 1158  C   ARG A  75     3987   2814   3902   -266   -391    627       C  
ATOM   1159  O   ARG A  75     -33.482 -66.057  -6.422  1.00 27.69           O  
ANISOU 1159  O   ARG A  75     3962   2725   3832   -308   -399    579       O  
ATOM   1160  CB  ARG A  75     -32.917 -63.488  -4.284  1.00 18.54           C  
ANISOU 1160  CB  ARG A  75     2757   1628   2661   -176   -273    598       C  
ATOM   1161  CG  ARG A  75     -31.729 -62.537  -4.156  1.00 22.64           C  
ANISOU 1161  CG  ARG A  75     3332   2139   3131   -171   -219    546       C  
ATOM   1162  CD  ARG A  75     -31.719 -61.755  -2.853  1.00 26.74           C  
ANISOU 1162  CD  ARG A  75     3823   2677   3661   -104   -184    560       C  
ATOM   1163  NE  ARG A  75     -30.611 -60.803  -2.819  1.00 32.45           N  
ANISOU 1163  NE  ARG A  75     4607   3383   4338   -114   -150    515       N  
ATOM   1164  CZ  ARG A  75     -30.126 -60.247  -1.713  1.00 33.86           C  
ANISOU 1164  CZ  ARG A  75     4782   3568   4515    -74   -117    503       C  
ATOM   1165  NH1 ARG A  75     -30.640 -60.546  -0.527  1.00 27.74           N  
ANISOU 1165  NH1 ARG A  75     3946   2821   3773    -13   -104    529       N  
ATOM   1166  NH2 ARG A  75     -29.114 -59.391  -1.794  1.00 23.53           N  
ANISOU 1166  NH2 ARG A  75     3532   2239   3168    -99   -100    467       N  
ATOM   1167  H   ARG A  75     -34.255 -62.015  -5.638  1.00 34.18           H  
ATOM   1168  HA  ARG A  75     -32.492 -63.788  -6.264  1.00 27.75           H  
ATOM   1169  HB2 ARG A  75     -33.670 -63.093  -3.818  1.00 22.25           H  
ATOM   1170  HB3 ARG A  75     -32.674 -64.331  -3.871  1.00 22.25           H  
ATOM   1171  HG2 ARG A  75     -30.908 -63.052  -4.200  1.00 27.17           H  
ATOM   1172  HG3 ARG A  75     -31.758 -61.898  -4.885  1.00 27.17           H  
ATOM   1173  HD2 ARG A  75     -32.549 -61.261  -2.768  1.00 32.09           H  
ATOM   1174  HD3 ARG A  75     -31.616 -62.371  -2.110  1.00 32.09           H  
ATOM   1175  HE  ARG A  75     -30.246 -60.588  -3.568  1.00 38.93           H  
ATOM   1176 HH11 ARG A  75     -31.296 -61.100  -0.470  1.00 33.29           H  
ATOM   1177 HH12 ARG A  75     -30.321 -60.184   0.184  1.00 33.29           H  
ATOM   1178 HH21 ARG A  75     -28.777 -59.195  -2.560  1.00 28.23           H  
ATOM   1179 HH22 ARG A  75     -28.797 -59.031  -1.080  1.00 28.23           H  
ATOM   1180  N   LYS A  76     -35.306 -65.097  -5.485  1.00 22.68           N  
ANISOU 1180  N   LYS A  76     3217   2142   3258   -244   -433    708       N  
ATOM   1181  CA  LYS A  76     -36.136 -66.287  -5.624  1.00 26.83           C  
ANISOU 1181  CA  LYS A  76     3695   2662   3838   -284   -501    755       C  
ATOM   1182  C   LYS A  76     -36.121 -66.810  -7.053  1.00 29.54           C  
ANISOU 1182  C   LYS A  76     4123   2958   4145   -358   -570    720       C  
ATOM   1183  O   LYS A  76     -35.909 -68.001  -7.280  1.00 37.72           O  
ANISOU 1183  O   LYS A  76     5176   3960   5197   -400   -599    694       O  
ATOM   1184  CB  LYS A  76     -37.575 -65.991  -5.204  1.00 35.00           C  
ANISOU 1184  CB  LYS A  76     4634   3739   4924   -255   -541    860       C  
ATOM   1185  CG  LYS A  76     -38.533 -67.139  -5.483  1.00 34.44           C  
ANISOU 1185  CG  LYS A  76     4511   3662   4913   -314   -629    924       C  
ATOM   1186  CD  LYS A  76     -39.799 -67.054  -4.638  1.00 37.25           C  
ANISOU 1186  CD  LYS A  76     4735   4081   5336   -275   -642   1039       C  
ATOM   1187  CE  LYS A  76     -40.187 -68.408  -4.049  1.00 46.49           C  
ANISOU 1187  CE  LYS A  76     5826   5259   6579   -315   -673   1094       C  
ATOM   1188  NZ  LYS A  76     -40.592 -68.285  -2.621  1.00 50.89           N  
ANISOU 1188  NZ  LYS A  76     6268   5891   7178   -245   -608   1164       N  
ATOM   1189  H   LYS A  76     -35.707 -64.432  -5.116  1.00 27.22           H  
ATOM   1190  HA  LYS A  76     -35.790 -66.984  -5.044  1.00 32.20           H  
ATOM   1191  HB2 LYS A  76     -37.594 -65.812  -4.251  1.00 42.00           H  
ATOM   1192  HB3 LYS A  76     -37.891 -65.214  -5.692  1.00 42.00           H  
ATOM   1193  HG2 LYS A  76     -38.793 -67.116  -6.418  1.00 41.33           H  
ATOM   1194  HG3 LYS A  76     -38.091 -67.978  -5.281  1.00 41.33           H  
ATOM   1195  HD2 LYS A  76     -39.651 -66.437  -3.905  1.00 44.70           H  
ATOM   1196  HD3 LYS A  76     -40.532 -66.745  -5.193  1.00 44.70           H  
ATOM   1197  HE2 LYS A  76     -40.936 -68.771  -4.547  1.00 55.79           H  
ATOM   1198  HE3 LYS A  76     -39.427 -69.009  -4.099  1.00 55.79           H  
ATOM   1199  HZ1 LYS A  76     -41.292 -67.739  -2.550  1.00 61.07           H  
ATOM   1200  HZ2 LYS A  76     -40.814 -69.083  -2.298  1.00 61.07           H  
ATOM   1201  HZ3 LYS A  76     -39.918 -67.955  -2.142  1.00 61.07           H  
ATOM   1202  N   ASN A  77     -36.339 -65.918  -8.015  1.00 25.92           N  
ANISOU 1202  N   ASN A  77     3725   2491   3632   -372   -598    720       N  
ATOM   1203  CA  ASN A  77     -36.330 -66.316  -9.421  1.00 25.26           C  
ANISOU 1203  CA  ASN A  77     3736   2367   3497   -441   -664    687       C  
ATOM   1204  C   ASN A  77     -34.989 -66.897  -9.858  1.00 25.79           C  
ANISOU 1204  C   ASN A  77     3886   2403   3508   -461   -614    585       C  
ATOM   1205  O   ASN A  77     -34.948 -67.965 -10.492  1.00 29.14           O  
ANISOU 1205  O   ASN A  77     4360   2788   3924   -505   -662    551       O  
ATOM   1206  CB  ASN A  77     -36.732 -65.151 -10.327  1.00 27.92           C  
ANISOU 1206  CB  ASN A  77     4126   2705   3778   -449   -698    709       C  
ATOM   1207  CG  ASN A  77     -38.197 -64.777 -10.174  1.00 41.52           C  
ANISOU 1207  CG  ASN A  77     5769   4452   5556   -435   -770    814       C  
ATOM   1208  OD1 ASN A  77     -39.003 -65.571  -9.687  1.00 48.94           O  
ANISOU 1208  OD1 ASN A  77     6621   5405   6568   -443   -814    872       O  
ATOM   1209  ND2 ASN A  77     -38.550 -63.571 -10.595  1.00 46.05           N  
ANISOU 1209  ND2 ASN A  77     6367   5033   6099   -413   -784    844       N  
ATOM   1210  H   ASN A  77     -36.494 -65.083  -7.883  1.00 31.10           H  
ATOM   1211  HA  ASN A  77     -36.994 -67.013  -9.540  1.00 30.32           H  
ATOM   1212  HB2 ASN A  77     -36.197 -64.374 -10.101  1.00 33.51           H  
ATOM   1213  HB3 ASN A  77     -36.580 -65.402 -11.252  1.00 33.51           H  
ATOM   1214 HD21 ASN A  77     -37.961 -63.044 -10.934  1.00 55.27           H  
ATOM   1215 HD22 ASN A  77     -39.368 -63.315 -10.528  1.00 55.27           H  
ATOM   1216  N   ARG A  78     -33.893 -66.217  -9.521  1.00 19.91           N  
ANISOU 1216  N   ARG A  78     3161   1677   2729   -427   -522    537       N  
ATOM   1217  CA  ARG A  78     -32.576 -66.788  -9.829  1.00 19.82           C  
ANISOU 1217  CA  ARG A  78     3206   1649   2674   -436   -464    449       C  
ATOM   1218  C   ARG A  78     -32.453 -68.214  -9.295  1.00 24.51           C  
ANISOU 1218  C   ARG A  78     3766   2221   3327   -433   -472    430       C  
ATOM   1219  O   ARG A  78     -32.059 -69.130 -10.029  1.00 29.13           O  
ANISOU 1219  O   ARG A  78     4417   2767   3882   -459   -490    372       O  
ATOM   1220  CB  ARG A  78     -31.439 -65.922  -9.285  1.00 23.78           C  
ANISOU 1220  CB  ARG A  78     3703   2181   3152   -401   -367    417       C  
ATOM   1221  CG  ARG A  78     -31.255 -64.611 -10.024  1.00 19.39           C  
ANISOU 1221  CG  ARG A  78     3208   1634   2524   -417   -356    420       C  
ATOM   1222  CD  ARG A  78     -29.820 -64.127  -9.922  1.00 26.52           C  
ANISOU 1222  CD  ARG A  78     4133   2557   3386   -412   -266    369       C  
ATOM   1223  NE  ARG A  78     -29.444 -63.803  -8.548  1.00 21.98           N  
ANISOU 1223  NE  ARG A  78     3486   2001   2864   -368   -219    380       N  
ATOM   1224  CZ  ARG A  78     -29.776 -62.675  -7.927  1.00 21.65           C  
ANISOU 1224  CZ  ARG A  78     3427   1965   2834   -341   -219    421       C  
ATOM   1225  NH1 ARG A  78     -30.501 -61.755  -8.552  1.00 25.29           N  
ANISOU 1225  NH1 ARG A  78     3929   2413   3265   -352   -263    459       N  
ATOM   1226  NH2 ARG A  78     -29.391 -62.467  -6.675  1.00 17.87           N  
ANISOU 1226  NH2 ARG A  78     2893   1501   2394   -300   -179    422       N  
ATOM   1227  H   ARG A  78     -33.880 -65.453  -9.128  1.00 23.90           H  
ATOM   1228  HA  ARG A  78     -32.477 -66.828 -10.794  1.00 23.78           H  
ATOM   1229  HB2 ARG A  78     -31.623 -65.714  -8.355  1.00 28.54           H  
ATOM   1230  HB3 ARG A  78     -30.609 -66.419  -9.352  1.00 28.54           H  
ATOM   1231  HG2 ARG A  78     -31.469 -64.737 -10.962  1.00 23.26           H  
ATOM   1232  HG3 ARG A  78     -31.834 -63.937  -9.634  1.00 23.26           H  
ATOM   1233  HD2 ARG A  78     -29.226 -64.824 -10.241  1.00 31.82           H  
ATOM   1234  HD3 ARG A  78     -29.715 -63.327 -10.460  1.00 31.82           H  
ATOM   1235  HE  ARG A  78     -28.977 -64.379  -8.113  1.00 26.37           H  
ATOM   1236 HH11 ARG A  78     -30.755 -61.885  -9.363  1.00 30.34           H  
ATOM   1237 HH12 ARG A  78     -30.715 -61.027  -8.146  1.00 30.34           H  
ATOM   1238 HH21 ARG A  78     -28.922 -63.060  -6.266  1.00 21.44           H  
ATOM   1239 HH22 ARG A  78     -29.607 -61.737  -6.274  1.00 21.44           H  
ATOM   1240  N   ILE A  79     -32.811 -68.413  -8.028  1.00 23.19           N  
ANISOU 1240  N   ILE A  79     3501   2073   3238   -400   -462    480       N  
ATOM   1241  CA  ILE A  79     -32.755 -69.756  -7.450  1.00 19.53           C  
ANISOU 1241  CA  ILE A  79     3001   1584   2836   -402   -478    476       C  
ATOM   1242  C   ILE A  79     -33.683 -70.740  -8.176  1.00 28.81           C  
ANISOU 1242  C   ILE A  79     4204   2710   4031   -459   -585    499       C  
ATOM   1243  O   ILE A  79     -33.318 -71.900  -8.408  1.00 24.63           O  
ANISOU 1243  O   ILE A  79     3717   2130   3512   -476   -609    453       O  
ATOM   1244  CB  ILE A  79     -33.062 -69.739  -5.937  1.00 19.09           C  
ANISOU 1244  CB  ILE A  79     2834   1567   2853   -359   -449    539       C  
ATOM   1245  CG1 ILE A  79     -31.919 -69.052  -5.181  1.00 18.44           C  
ANISOU 1245  CG1 ILE A  79     2740   1517   2750   -309   -352    499       C  
ATOM   1246  CG2 ILE A  79     -33.268 -71.153  -5.397  1.00 19.34           C  
ANISOU 1246  CG2 ILE A  79     2825   1568   2954   -374   -487    559       C  
ATOM   1247  CD1 ILE A  79     -30.523 -69.680  -5.395  1.00 18.37           C  
ANISOU 1247  CD1 ILE A  79     2776   1485   2718   -307   -302    413       C  
ATOM   1248  H   ILE A  79     -33.086 -67.801  -7.490  1.00 27.83           H  
ATOM   1249  HA  ILE A  79     -31.850 -70.090  -7.553  1.00 23.44           H  
ATOM   1250  HB  ILE A  79     -33.876 -69.232  -5.793  1.00 22.91           H  
ATOM   1251 HG12 ILE A  79     -31.871 -68.127  -5.470  1.00 22.13           H  
ATOM   1252 HG13 ILE A  79     -32.113 -69.087  -4.231  1.00 22.13           H  
ATOM   1253 HG21 ILE A  79     -32.460 -71.668  -5.547  1.00 23.20           H  
ATOM   1254 HG22 ILE A  79     -33.457 -71.104  -4.448  1.00 23.20           H  
ATOM   1255 HG23 ILE A  79     -34.013 -71.563  -5.863  1.00 23.20           H  
ATOM   1256 HD11 ILE A  79     -30.301 -69.641  -6.339  1.00 22.04           H  
ATOM   1257 HD12 ILE A  79     -29.871 -69.181  -4.880  1.00 22.04           H  
ATOM   1258 HD13 ILE A  79     -30.544 -70.603  -5.098  1.00 22.04           H  
ATOM   1259  N   CYS A  80     -34.876 -70.280  -8.537  1.00 31.57           N  
ANISOU 1259  N   CYS A  80     4533   3071   4388   -486   -657    570       N  
ATOM   1260  CA  CYS A  80     -35.812 -71.115  -9.283  1.00 26.55           C  
ANISOU 1260  CA  CYS A  80     3926   2391   3772   -552   -774    600       C  
ATOM   1261  C   CYS A  80     -35.158 -71.598 -10.570  1.00 32.13           C  
ANISOU 1261  C   CYS A  80     4771   3040   4396   -586   -797    504       C  
ATOM   1262  O   CYS A  80     -35.311 -72.759 -10.957  1.00 38.77           O  
ANISOU 1262  O   CYS A  80     5661   3819   5252   -627   -869    481       O  
ATOM   1263  CB  CYS A  80     -37.090 -70.346  -9.608  1.00 21.86           C  
ANISOU 1263  CB  CYS A  80     3291   1828   3188   -573   -843    689       C  
ATOM   1264  SG  CYS A  80     -38.284 -71.299 -10.577  1.00 72.99           S  
ANISOU 1264  SG  CYS A  80     9797   8250   9685   -668  -1007    737       S  
ATOM   1265  H   CYS A  80     -35.168 -69.490  -8.362  1.00 37.88           H  
ATOM   1266  HA  CYS A  80     -36.048 -71.890  -8.749  1.00 31.87           H  
ATOM   1267  HB2 CYS A  80     -37.521 -70.089  -8.778  1.00 26.24           H  
ATOM   1268  HB3 CYS A  80     -36.858 -69.555 -10.118  1.00 26.24           H  
ATOM   1269  HG  CYS A  80     -39.251 -70.619 -10.784  1.00 87.59           H  
ATOM   1270  N   TYR A  81     -34.421 -70.708 -11.230  1.00 41.43           N  
ANISOU 1270  N   TYR A  81     6017   4237   5486   -569   -736    448       N  
ATOM   1271  CA  TYR A  81     -33.658 -71.114 -12.410  1.00 36.52           C  
ANISOU 1271  CA  TYR A  81     5526   3576   4772   -588   -733    353       C  
ATOM   1272  C   TYR A  81     -32.523 -72.074 -12.071  1.00 37.81           C  
ANISOU 1272  C   TYR A  81     5711   3712   4943   -552   -670    272       C  
ATOM   1273  O   TYR A  81     -32.285 -73.023 -12.814  1.00 37.67           O  
ANISOU 1273  O   TYR A  81     5787   3636   4890   -569   -707    207       O  
ATOM   1274  CB  TYR A  81     -33.126 -69.904 -13.179  1.00 33.47           C  
ANISOU 1274  CB  TYR A  81     5201   3228   4288   -582   -678    326       C  
ATOM   1275  CG  TYR A  81     -33.952 -69.597 -14.407  1.00 49.17           C  
ANISOU 1275  CG  TYR A  81     7269   5200   6214   -638   -773    347       C  
ATOM   1276  CD1 TYR A  81     -35.318 -69.378 -14.303  1.00 58.30           C  
ANISOU 1276  CD1 TYR A  81     8368   6358   7425   -669   -872    442       C  
ATOM   1277  CD2 TYR A  81     -33.373 -69.546 -15.670  1.00 60.14           C  
ANISOU 1277  CD2 TYR A  81     8788   6578   7486   -659   -764    277       C  
ATOM   1278  CE1 TYR A  81     -36.087 -69.109 -15.417  1.00 65.87           C  
ANISOU 1278  CE1 TYR A  81     9396   7303   8330   -722   -969    469       C  
ATOM   1279  CE2 TYR A  81     -34.137 -69.275 -16.795  1.00 66.98           C  
ANISOU 1279  CE2 TYR A  81     9733   7429   8288   -713   -858    300       C  
ATOM   1280  CZ  TYR A  81     -35.493 -69.058 -16.661  1.00 72.24           C  
ANISOU 1280  CZ  TYR A  81    10340   8092   9016   -746   -965    396       C  
ATOM   1281  OH  TYR A  81     -36.258 -68.788 -17.773  1.00 76.14           O  
ANISOU 1281  OH  TYR A  81    10909   8572   9449   -802  -1068    424       O  
ATOM   1282  H   TYR A  81     -34.346 -69.877 -11.022  1.00 49.71           H  
ATOM   1283  HA  TYR A  81     -34.260 -71.587 -13.006  1.00 43.82           H  
ATOM   1284  HB2 TYR A  81     -33.146 -69.126 -12.600  1.00 40.16           H  
ATOM   1285  HB3 TYR A  81     -32.217 -70.083 -13.465  1.00 40.16           H  
ATOM   1286  HD1 TYR A  81     -35.723 -69.412 -13.467  1.00 69.96           H  
ATOM   1287  HD2 TYR A  81     -32.460 -69.694 -15.762  1.00 72.17           H  
ATOM   1288  HE1 TYR A  81     -37.001 -68.961 -15.330  1.00 79.05           H  
ATOM   1289  HE2 TYR A  81     -33.738 -69.241 -17.634  1.00 80.38           H  
ATOM   1290  HH  TYR A  81     -35.776 -68.786 -18.460  1.00 91.37           H  
ATOM   1291  N   LEU A  82     -31.824 -71.840 -10.963  1.00 30.32           N  
ANISOU 1291  N   LEU A  82     4680   2802   4039   -500   -579    275       N  
ATOM   1292  CA  LEU A  82     -30.788 -72.784 -10.538  1.00 30.13           C  
ANISOU 1292  CA  LEU A  82     4660   2752   4035   -462   -525    210       C  
ATOM   1293  C   LEU A  82     -31.341 -74.196 -10.328  1.00 30.86           C  
ANISOU 1293  C   LEU A  82     4757   2774   4196   -484   -612    220       C  
ATOM   1294  O   LEU A  82     -30.738 -75.178 -10.758  1.00 28.21           O  
ANISOU 1294  O   LEU A  82     4497   2380   3842   -472   -616    144       O  
ATOM   1295  CB  LEU A  82     -30.110 -72.315  -9.247  1.00 20.55           C  
ANISOU 1295  CB  LEU A  82     3347   1593   2870   -410   -433    229       C  
ATOM   1296  CG  LEU A  82     -28.996 -73.227  -8.715  1.00 29.98           C  
ANISOU 1296  CG  LEU A  82     4531   2768   4092   -365   -377    171       C  
ATOM   1297  CD1 LEU A  82     -27.849 -73.332  -9.714  1.00 20.97           C  
ANISOU 1297  CD1 LEU A  82     3478   1624   2867   -344   -317     74       C  
ATOM   1298  CD2 LEU A  82     -28.492 -72.739  -7.362  1.00 19.81           C  
ANISOU 1298  CD2 LEU A  82     3140   1533   2854   -323   -307    205       C  
ATOM   1299  H   LEU A  82     -31.925 -71.159 -10.448  1.00 36.39           H  
ATOM   1300  HA  LEU A  82     -30.108 -72.832 -11.228  1.00 36.15           H  
ATOM   1301  HB2 LEU A  82     -29.720 -71.441  -9.406  1.00 24.66           H  
ATOM   1302  HB3 LEU A  82     -30.785 -72.246  -8.554  1.00 24.66           H  
ATOM   1303  HG  LEU A  82     -29.359 -74.118  -8.590  1.00 35.98           H  
ATOM   1304 HD11 LEU A  82     -27.483 -72.447  -9.869  1.00 25.16           H  
ATOM   1305 HD12 LEU A  82     -27.164 -73.914  -9.347  1.00 25.16           H  
ATOM   1306 HD13 LEU A  82     -28.187 -73.701 -10.545  1.00 25.16           H  
ATOM   1307 HD21 LEU A  82     -29.229 -72.741  -6.732  1.00 23.77           H  
ATOM   1308 HD22 LEU A  82     -27.791 -73.334  -7.054  1.00 23.77           H  
ATOM   1309 HD23 LEU A  82     -28.143 -71.839  -7.461  1.00 23.77           H  
ATOM   1310  N   GLN A  83     -32.485 -74.294  -9.660  1.00 23.13           N  
ANISOU 1310  N   GLN A  83     3696   1797   3295   -514   -682    316       N  
ATOM   1311  CA  GLN A  83     -33.043 -75.596  -9.298  1.00 25.69           C  
ANISOU 1311  CA  GLN A  83     4007   2056   3697   -545   -767    346       C  
ATOM   1312  C   GLN A  83     -33.522 -76.423 -10.498  1.00 33.86           C  
ANISOU 1312  C   GLN A  83     5159   3006   4699   -605   -881    311       C  
ATOM   1313  O   GLN A  83     -33.469 -77.655 -10.466  1.00 32.97           O  
ANISOU 1313  O   GLN A  83     5089   2813   4623   -619   -938    286       O  
ATOM   1314  CB  GLN A  83     -34.171 -75.422  -8.275  1.00 22.19           C  
ANISOU 1314  CB  GLN A  83     3433   1654   3343   -566   -806    472       C  
ATOM   1315  CG  GLN A  83     -33.665 -75.010  -6.896  1.00 26.68           C  
ANISOU 1315  CG  GLN A  83     3898   2286   3953   -504   -707    501       C  
ATOM   1316  CD  GLN A  83     -34.772 -74.812  -5.874  1.00 33.48           C  
ANISOU 1316  CD  GLN A  83     4632   3198   4889   -512   -731    625       C  
ATOM   1317  OE1 GLN A  83     -35.950 -75.007  -6.168  1.00 33.22           O  
ANISOU 1317  OE1 GLN A  83     4573   3158   4889   -567   -823    699       O  
ATOM   1318  NE2 GLN A  83     -34.390 -74.420  -4.663  1.00 78.46           N  
ANISOU 1318  NE2 GLN A  83    10248   8953  10611   -457   -648    650       N  
ATOM   1319  H   GLN A  83     -32.958 -73.623  -9.403  1.00 27.76           H  
ATOM   1320  HA  GLN A  83     -32.343 -76.109  -8.863  1.00 30.82           H  
ATOM   1321  HB2 GLN A  83     -34.778 -74.733  -8.589  1.00 26.62           H  
ATOM   1322  HB3 GLN A  83     -34.645 -76.263  -8.181  1.00 26.62           H  
ATOM   1323  HG2 GLN A  83     -33.072 -75.701  -6.561  1.00 32.01           H  
ATOM   1324  HG3 GLN A  83     -33.183 -74.173  -6.977  1.00 32.01           H  
ATOM   1325 HE21 GLN A  83     -33.557 -74.293  -4.494  1.00 94.16           H  
ATOM   1326 HE22 GLN A  83     -34.977 -74.293  -4.047  1.00 94.16           H  
ATOM   1327  N   GLU A  84     -33.975 -75.753 -11.554  1.00 39.97           N  
ANISOU 1327  N   GLU A  84     5996   3792   5400   -640   -920    307       N  
ATOM   1328  CA  GLU A  84     -34.418 -76.438 -12.769  1.00 41.01           C  
ANISOU 1328  CA  GLU A  84     6254   3845   5481   -699  -1033    268       C  
ATOM   1329  C   GLU A  84     -33.270 -77.203 -13.420  1.00 41.00           C  
ANISOU 1329  C   GLU A  84     6384   3784   5410   -660   -994    137       C  
ATOM   1330  O   GLU A  84     -33.455 -78.308 -13.929  1.00 58.92           O  
ANISOU 1330  O   GLU A  84     8750   5958   7677   -690  -1086     95       O  
ATOM   1331  CB  GLU A  84     -34.997 -75.437 -13.771  1.00 42.65           C  
ANISOU 1331  CB  GLU A  84     6505   4088   5611   -737  -1071    288       C  
ATOM   1332  CG  GLU A  84     -36.463 -75.094 -13.543  1.00 56.63           C  
ANISOU 1332  CG  GLU A  84     8184   5884   7450   -796  -1172    416       C  
ATOM   1333  CD  GLU A  84     -37.018 -74.167 -14.609  1.00 66.55           C  
ANISOU 1333  CD  GLU A  84     9492   7165   8628   -831  -1221    435       C  
ATOM   1334  OE1 GLU A  84     -36.759 -74.415 -15.806  1.00 71.25           O  
ANISOU 1334  OE1 GLU A  84    10231   7715   9125   -857  -1262    359       O  
ATOM   1335  OE2 GLU A  84     -37.710 -73.189 -14.252  1.00 67.26           O  
ANISOU 1335  OE2 GLU A  84     9484   7321   8751   -827  -1218    525       O  
ATOM   1336  H   GLU A  84     -34.036 -74.896 -11.594  1.00 47.97           H  
ATOM   1337  HA  GLU A  84     -35.114 -77.074 -12.540  1.00 49.21           H  
ATOM   1338  HB2 GLU A  84     -34.489 -74.612 -13.714  1.00 51.18           H  
ATOM   1339  HB3 GLU A  84     -34.917 -75.809 -14.663  1.00 51.18           H  
ATOM   1340  HG2 GLU A  84     -36.985 -75.911 -13.554  1.00 67.96           H  
ATOM   1341  HG3 GLU A  84     -36.555 -74.653 -12.684  1.00 67.96           H  
ATOM   1342  N   ILE A  85     -32.086 -76.602 -13.403  1.00 31.68           N  
ANISOU 1342  N   ILE A  85     5207   2658   4173   -591   -859     74       N  
ATOM   1343  CA  ILE A  85     -30.894 -77.231 -13.962  1.00 28.66           C  
ANISOU 1343  CA  ILE A  85     4929   2239   3723   -535   -796    -47       C  
ATOM   1344  C   ILE A  85     -30.507 -78.451 -13.130  1.00 35.02           C  
ANISOU 1344  C   ILE A  85     5711   2980   4616   -500   -801    -67       C  
ATOM   1345  O   ILE A  85     -29.902 -79.394 -13.638  1.00 51.43           O  
ANISOU 1345  O   ILE A  85     7894   4986   6660   -465   -805   -160       O  
ATOM   1346  CB  ILE A  85     -29.719 -76.224 -14.019  1.00 28.21           C  
ANISOU 1346  CB  ILE A  85     4850   2272   3598   -475   -646    -88       C  
ATOM   1347  CG1 ILE A  85     -30.074 -75.070 -14.959  1.00 28.74           C  
ANISOU 1347  CG1 ILE A  85     4960   2390   3570   -514   -649    -71       C  
ATOM   1348  CG2 ILE A  85     -28.431 -76.899 -14.489  1.00 29.40           C  
ANISOU 1348  CG2 ILE A  85     5083   2400   3687   -405   -566   -205       C  
ATOM   1349  CD1 ILE A  85     -29.140 -73.881 -14.870  1.00 30.09           C  
ANISOU 1349  CD1 ILE A  85     5088   2654   3692   -477   -519    -76       C  
ATOM   1350  H   ILE A  85     -31.945 -75.822 -13.071  1.00 38.02           H  
ATOM   1351  HA  ILE A  85     -31.083 -77.528 -14.865  1.00 34.40           H  
ATOM   1352  HB  ILE A  85     -29.574 -75.865 -13.130  1.00 33.86           H  
ATOM   1353 HG12 ILE A  85     -30.051 -75.395 -15.873  1.00 34.49           H  
ATOM   1354 HG13 ILE A  85     -30.967 -74.759 -14.745  1.00 34.49           H  
ATOM   1355 HG21 ILE A  85     -28.572 -77.265 -15.376  1.00 35.28           H  
ATOM   1356 HG22 ILE A  85     -27.719 -76.240 -14.513  1.00 35.28           H  
ATOM   1357 HG23 ILE A  85     -28.203 -77.610 -13.870  1.00 35.28           H  
ATOM   1358 HD11 ILE A  85     -28.241 -74.169 -15.095  1.00 36.11           H  
ATOM   1359 HD12 ILE A  85     -29.435 -73.201 -15.495  1.00 36.11           H  
ATOM   1360 HD13 ILE A  85     -29.159 -73.532 -13.966  1.00 36.11           H  
ATOM   1361  N   PHE A  86     -30.881 -78.432 -11.855  1.00 28.04           N  
ANISOU 1361  N   PHE A  86     4694   2120   3842   -505   -803     23       N  
ATOM   1362  CA  PHE A  86     -30.519 -79.490 -10.918  1.00 25.97           C  
ANISOU 1362  CA  PHE A  86     4392   1806   3668   -473   -804     23       C  
ATOM   1363  C   PHE A  86     -31.646 -80.502 -10.707  1.00 29.34           C  
ANISOU 1363  C   PHE A  86     4824   2146   4178   -545   -950     88       C  
ATOM   1364  O   PHE A  86     -31.405 -81.612 -10.239  1.00 34.02           O  
ANISOU 1364  O   PHE A  86     5431   2663   4833   -531   -982     75       O  
ATOM   1365  CB  PHE A  86     -30.165 -78.863  -9.570  1.00 23.72           C  
ANISOU 1365  CB  PHE A  86     3960   1606   3447   -434   -712     86       C  
ATOM   1366  CG  PHE A  86     -28.720 -78.479  -9.433  1.00 23.95           C  
ANISOU 1366  CG  PHE A  86     3980   1686   3435   -352   -577     13       C  
ATOM   1367  CD1 PHE A  86     -28.218 -77.350 -10.062  1.00 24.05           C  
ANISOU 1367  CD1 PHE A  86     4009   1771   3357   -338   -498    -20       C  
ATOM   1368  CD2 PHE A  86     -27.866 -79.240  -8.655  1.00 23.26           C  
ANISOU 1368  CD2 PHE A  86     3860   1575   3402   -294   -535    -12       C  
ATOM   1369  CE1 PHE A  86     -26.888 -77.000  -9.925  1.00 22.70           C  
ANISOU 1369  CE1 PHE A  86     3818   1652   3154   -273   -378    -74       C  
ATOM   1370  CE2 PHE A  86     -26.539 -78.895  -8.517  1.00 22.96           C  
ANISOU 1370  CE2 PHE A  86     3800   1590   3333   -221   -416    -69       C  
ATOM   1371  CZ  PHE A  86     -26.048 -77.776  -9.152  1.00 22.69           C  
ANISOU 1371  CZ  PHE A  86     3778   1633   3212   -214   -337    -99       C  
ATOM   1372  H   PHE A  86     -31.353 -77.805 -11.502  1.00 33.65           H  
ATOM   1373  HA  PHE A  86     -29.741 -79.963 -11.251  1.00 31.16           H  
ATOM   1374  HB2 PHE A  86     -30.697 -78.061  -9.451  1.00 28.46           H  
ATOM   1375  HB3 PHE A  86     -30.370 -79.500  -8.868  1.00 28.46           H  
ATOM   1376  HD1 PHE A  86     -28.780 -76.827 -10.586  1.00 28.86           H  
ATOM   1377  HD2 PHE A  86     -28.190 -79.998  -8.226  1.00 27.91           H  
ATOM   1378  HE1 PHE A  86     -26.559 -76.244 -10.355  1.00 27.23           H  
ATOM   1379  HE2 PHE A  86     -25.974 -79.418  -7.994  1.00 27.55           H  
ATOM   1380  HZ  PHE A  86     -25.153 -77.542  -9.058  1.00 27.23           H  
ATOM   1381  N   SER A  87     -32.868 -80.099 -11.047  1.00 31.37           N  
ANISOU 1381  N   SER A  87     5066   2417   4439   -625  -1042    165       N  
ATOM   1382  CA  SER A  87     -34.083 -80.870 -10.766  1.00 31.63           C  
ANISOU 1382  CA  SER A  87     5068   2390   4559   -710  -1183    258       C  
ATOM   1383  C   SER A  87     -34.010 -82.386 -11.020  1.00 42.87           C  
ANISOU 1383  C   SER A  87     6601   3674   6013   -732  -1283    209       C  
ATOM   1384  O   SER A  87     -34.058 -83.184 -10.075  1.00 50.36           O  
ANISOU 1384  O   SER A  87     7492   4584   7059   -736  -1308    258       O  
ATOM   1385  CB  SER A  87     -35.252 -80.276 -11.559  1.00 26.77           C  
ANISOU 1385  CB  SER A  87     4463   1795   3913   -789  -1278    316       C  
ATOM   1386  OG  SER A  87     -36.449 -80.326 -10.802  1.00 46.43           O  
ANISOU 1386  OG  SER A  87     6826   4311   6505   -853  -1353    457       O  
ATOM   1387  H   SER A  87     -33.025 -79.358 -11.454  1.00 37.65           H  
ATOM   1388  HA  SER A  87     -34.294 -80.756  -9.826  1.00 37.95           H  
ATOM   1389  HB2 SER A  87     -35.052 -79.351 -11.772  1.00 32.12           H  
ATOM   1390  HB3 SER A  87     -35.372 -80.786 -12.375  1.00 32.12           H  
ATOM   1391  HG  SER A  87     -37.083 -79.998 -11.245  1.00 55.72           H  
ATOM   1392  N   ASN A  88     -33.908 -82.785 -12.285  1.00 42.54           N  
ANISOU 1392  N   ASN A  88     6722   3553   5886   -747  -1346    113       N  
ATOM   1393  CA  ASN A  88     -34.007 -84.197 -12.633  1.00 45.95           C  
ANISOU 1393  CA  ASN A  88     7280   3838   6342   -777  -1466     67       C  
ATOM   1394  C   ASN A  88     -32.910 -85.025 -11.974  1.00 39.12           C  
ANISOU 1394  C   ASN A  88     6427   2920   5517   -689  -1397      3       C  
ATOM   1395  O   ASN A  88     -33.102 -86.204 -11.676  1.00 41.56           O  
ANISOU 1395  O   ASN A  88     6741   3171   5880   -697  -1463     16       O  
ATOM   1396  CB  ASN A  88     -33.955 -84.392 -14.148  1.00 47.10           C  
ANISOU 1396  CB  ASN A  88     7608   3926   6362   -785  -1522    -42       C  
ATOM   1397  CG  ASN A  88     -32.542 -84.353 -14.689  1.00 63.22           C  
ANISOU 1397  CG  ASN A  88     9759   5959   8303   -673  -1397   -191       C  
ATOM   1398  OD1 ASN A  88     -31.753 -83.479 -14.333  1.00 69.61           O  
ANISOU 1398  OD1 ASN A  88    10484   6878   9087   -602  -1245   -201       O  
ATOM   1399  ND2 ASN A  88     -32.209 -85.315 -15.542  1.00 65.60           N  
ANISOU 1399  ND2 ASN A  88    10231   6155   8540   -648  -1449   -303       N  
ATOM   1400  H   ASN A  88     -33.782 -82.261 -12.955  1.00 51.04           H  
ATOM   1401  HA  ASN A  88     -34.861 -84.535 -12.321  1.00 55.14           H  
ATOM   1402  HB2 ASN A  88     -34.339 -85.255 -14.370  1.00 56.52           H  
ATOM   1403  HB3 ASN A  88     -34.460 -83.683 -14.576  1.00 56.52           H  
ATOM   1404 HD21 ASN A  88     -32.785 -85.916 -15.759  1.00 78.72           H  
ATOM   1405 HD22 ASN A  88     -31.418 -85.337 -15.878  1.00 78.72           H  
ATOM   1406  N   GLU A  89     -31.761 -84.399 -11.748  1.00 36.31           N  
ANISOU 1406  N   GLU A  89     6034   2646   5117   -587  -1235    -56       N  
ATOM   1407  CA  GLU A  89     -30.634 -85.069 -11.114  1.00 37.35           C  
ANISOU 1407  CA  GLU A  89     6161   2745   5284   -493  -1158   -113       C  
ATOM   1408  C   GLU A  89     -30.803 -85.106  -9.600  1.00 42.62           C  
ANISOU 1408  C   GLU A  89     6666   3455   6074   -500  -1138      2       C  
ATOM   1409  O   GLU A  89     -30.367 -86.049  -8.941  1.00 44.51           O  
ANISOU 1409  O   GLU A  89     6904   3625   6383   -465  -1149     -3       O  
ATOM   1410  CB  GLU A  89     -29.330 -84.366 -11.492  1.00 44.45           C  
ANISOU 1410  CB  GLU A  89     7076   3725   6090   -388   -997   -213       C  
ATOM   1411  CG  GLU A  89     -28.886 -84.642 -12.922  1.00 57.86           C  
ANISOU 1411  CG  GLU A  89     8953   5367   7664   -353  -1000   -346       C  
ATOM   1412  CD  GLU A  89     -28.650 -86.113 -13.188  1.00 69.64           C  
ANISOU 1412  CD  GLU A  89    10580   6704   9174   -321  -1080   -426       C  
ATOM   1413  OE1 GLU A  89     -28.212 -86.812 -12.257  1.00 67.57           O  
ANISOU 1413  OE1 GLU A  89    10267   6402   9006   -276  -1067   -411       O  
ATOM   1414  OE2 GLU A  89     -28.911 -86.572 -14.320  1.00 74.22           O  
ANISOU 1414  OE2 GLU A  89    11327   7199   9674   -339  -1160   -504       O  
ATOM   1415  H   GLU A  89     -31.608 -83.578 -11.954  1.00 43.57           H  
ATOM   1416  HA  GLU A  89     -30.588 -85.983 -11.434  1.00 44.82           H  
ATOM   1417  HB2 GLU A  89     -29.451 -83.409 -11.397  1.00 53.34           H  
ATOM   1418  HB3 GLU A  89     -28.627 -84.670 -10.898  1.00 53.34           H  
ATOM   1419  HG2 GLU A  89     -29.574 -84.333 -13.532  1.00 69.43           H  
ATOM   1420  HG3 GLU A  89     -28.055 -84.170 -13.092  1.00 69.43           H  
ATOM   1421  N   MET A  90     -31.445 -84.080  -9.054  1.00 41.26           N  
ANISOU 1421  N   MET A  90     6361   3395   5921   -540  -1110    105       N  
ATOM   1422  CA  MET A  90     -31.714 -84.028  -7.627  1.00 43.45           C  
ANISOU 1422  CA  MET A  90     6485   3726   6299   -548  -1090    220       C  
ATOM   1423  C   MET A  90     -32.812 -85.028  -7.288  1.00 35.79           C  
ANISOU 1423  C   MET A  90     5505   2672   5423   -642  -1237    317       C  
ATOM   1424  O   MET A  90     -32.853 -85.566  -6.183  1.00 33.66           O  
ANISOU 1424  O   MET A  90     5147   2409   5234   -639  -1236    389       O  
ATOM   1425  CB  MET A  90     -32.127 -82.615  -7.216  1.00 37.97           C  
ANISOU 1425  CB  MET A  90     5667   3171   5588   -556  -1018    295       C  
ATOM   1426  CG  MET A  90     -32.252 -82.416  -5.715  1.00 34.06           C  
ANISOU 1426  CG  MET A  90     5020   2748   5173   -543   -971    400       C  
ATOM   1427  SD  MET A  90     -30.695 -82.687  -4.843  1.00 35.16           S  
ANISOU 1427  SD  MET A  90     5136   2897   5326   -437   -854    338       S  
ATOM   1428  CE  MET A  90     -29.738 -81.265  -5.368  1.00 23.23           C  
ANISOU 1428  CE  MET A  90     3630   1487   3709   -371   -717    253       C  
ATOM   1429  H   MET A  90     -31.736 -83.399  -9.492  1.00 49.51           H  
ATOM   1430  HA  MET A  90     -30.907 -84.262  -7.141  1.00 52.14           H  
ATOM   1431  HB2 MET A  90     -31.462 -81.989  -7.543  1.00 45.56           H  
ATOM   1432  HB3 MET A  90     -32.989 -82.415  -7.614  1.00 45.56           H  
ATOM   1433  HG2 MET A  90     -32.540 -81.507  -5.540  1.00 40.87           H  
ATOM   1434  HG3 MET A  90     -32.904 -83.044  -5.366  1.00 40.87           H  
ATOM   1435  HE1 MET A  90     -30.199 -80.456  -5.094  1.00 27.88           H  
ATOM   1436  HE2 MET A  90     -28.862 -81.304  -4.953  1.00 27.88           H  
ATOM   1437  HE3 MET A  90     -29.648 -81.284  -6.333  1.00 27.88           H  
ATOM   1438  N   ALA A  91     -33.698 -85.278  -8.247  1.00 28.10           N  
ANISOU 1438  N   ALA A  91     4601   1661   4416   -715  -1348    317       N  
ATOM   1439  CA  ALA A  91     -34.758 -86.269  -8.066  1.00 29.12           C  
ANISOU 1439  CA  ALA A  91     4697   1770   4599   -791  -1470    399       C  
ATOM   1440  C   ALA A  91     -34.203 -87.662  -7.755  1.00 32.18           C  
ANISOU 1440  C   ALA A  91     5139   2065   5021   -757  -1497    355       C  
ATOM   1441  O   ALA A  91     -34.868 -88.474  -7.109  1.00 32.55           O  
ANISOU 1441  O   ALA A  91     5123   2108   5137   -806  -1570    444       O  
ATOM   1442  CB  ALA A  91     -35.649 -86.317  -9.298  1.00 30.10           C  
ANISOU 1442  CB  ALA A  91     4906   1866   4666   -865  -1585    388       C  
ATOM   1443  H   ALA A  91     -33.708 -84.888  -9.014  1.00 33.72           H  
ATOM   1444  HA  ALA A  91     -35.309 -85.998  -7.315  1.00 34.95           H  
ATOM   1445  HB1 ALA A  91     -35.110 -86.561 -10.067  1.00 36.12           H  
ATOM   1446  HB2 ALA A  91     -36.344 -86.979  -9.158  1.00 36.12           H  
ATOM   1447  HB3 ALA A  91     -36.046 -85.443  -9.434  1.00 36.12           H  
ATOM   1448  N   LYS A  92     -32.985 -87.933  -8.212  1.00 30.10           N  
ANISOU 1448  N   LYS A  92     4994   1730   4711   -669  -1439    221       N  
ATOM   1449  CA  LYS A  92     -32.342 -89.224  -7.976  1.00 30.97           C  
ANISOU 1449  CA  LYS A  92     5166   1748   4852   -620  -1458    168       C  
ATOM   1450  C   LYS A  92     -31.677 -89.268  -6.602  1.00 35.80           C  
ANISOU 1450  C   LYS A  92     5667   2394   5541   -565  -1373    217       C  
ATOM   1451  O   LYS A  92     -31.561 -90.332  -5.990  1.00 43.24           O  
ANISOU 1451  O   LYS A  92     6601   3287   6541   -556  -1410    240       O  
ATOM   1452  CB  LYS A  92     -31.298 -89.501  -9.058  1.00 31.67           C  
ANISOU 1452  CB  LYS A  92     5425   1752   4854   -534  -1424      1       C  
ATOM   1453  CG  LYS A  92     -31.885 -89.659 -10.443  1.00 33.64           C  
ANISOU 1453  CG  LYS A  92     5809   1957   5016   -582  -1515    -57       C  
ATOM   1454  CD  LYS A  92     -30.845 -89.453 -11.529  1.00 35.98           C  
ANISOU 1454  CD  LYS A  92     6256   2215   5201   -491  -1444   -217       C  
ATOM   1455  CE  LYS A  92     -31.507 -89.318 -12.887  1.00 39.11           C  
ANISOU 1455  CE  LYS A  92     6773   2592   5495   -547  -1526   -261       C  
ATOM   1456  NZ  LYS A  92     -30.729 -89.984 -13.964  1.00 49.56           N  
ANISOU 1456  NZ  LYS A  92     8280   3833   6719   -465  -1516   -415       N  
ATOM   1457  H   LYS A  92     -32.505 -87.382  -8.665  1.00 36.11           H  
ATOM   1458  HA  LYS A  92     -33.011 -89.925  -8.012  1.00 37.16           H  
ATOM   1459  HB2 LYS A  92     -30.670 -88.762  -9.084  1.00 38.00           H  
ATOM   1460  HB3 LYS A  92     -30.830 -90.322  -8.838  1.00 38.00           H  
ATOM   1461  HG2 LYS A  92     -32.245 -90.555 -10.536  1.00 40.37           H  
ATOM   1462  HG3 LYS A  92     -32.587 -89.002 -10.568  1.00 40.37           H  
ATOM   1463  HD2 LYS A  92     -30.347 -88.641 -11.348  1.00 43.18           H  
ATOM   1464  HD3 LYS A  92     -30.248 -90.217 -11.553  1.00 43.18           H  
ATOM   1465  HE2 LYS A  92     -32.386 -89.726 -12.854  1.00 46.93           H  
ATOM   1466  HE3 LYS A  92     -31.585 -88.377 -13.110  1.00 46.93           H  
ATOM   1467  HZ1 LYS A  92     -30.648 -90.852 -13.788  1.00 59.48           H  
ATOM   1468  HZ2 LYS A  92     -31.145 -89.885 -14.745  1.00 59.48           H  
ATOM   1469  HZ3 LYS A  92     -29.918 -89.622 -14.021  1.00 59.48           H  
ATOM   1470  N   VAL A  93     -31.242 -88.107  -6.123  1.00 42.18           N  
ANISOU 1470  N   VAL A  93     6393   3287   6348   -529  -1266    235       N  
ATOM   1471  CA  VAL A  93     -30.545 -88.007  -4.844  1.00 27.96           C  
ANISOU 1471  CA  VAL A  93     4488   1526   4609   -472  -1182    279       C  
ATOM   1472  C   VAL A  93     -31.531 -87.828  -3.702  1.00 33.60           C  
ANISOU 1472  C   VAL A  93     5046   2331   5388   -540  -1201    436       C  
ATOM   1473  O   VAL A  93     -31.426 -88.485  -2.668  1.00 33.33           O  
ANISOU 1473  O   VAL A  93     4948   2301   5416   -531  -1203    496       O  
ATOM   1474  CB  VAL A  93     -29.558 -86.809  -4.828  1.00 35.42           C  
ANISOU 1474  CB  VAL A  93     5403   2552   5505   -391  -1043    222       C  
ATOM   1475  CG1 VAL A  93     -28.882 -86.661  -3.463  1.00 36.45           C  
ANISOU 1475  CG1 VAL A  93     5411   2753   5687   -334   -955    273       C  
ATOM   1476  CG2 VAL A  93     -28.508 -86.977  -5.895  1.00 33.14           C  
ANISOU 1476  CG2 VAL A  93     5243   2215   5134   -308   -994     67       C  
ATOM   1477  H   VAL A  93     -31.340 -87.352  -6.525  1.00 50.62           H  
ATOM   1478  HA  VAL A  93     -30.042 -88.822  -4.688  1.00 33.55           H  
ATOM   1479  HB  VAL A  93     -30.047 -85.992  -5.012  1.00 42.51           H  
ATOM   1480 HG11 VAL A  93     -28.390 -87.473  -3.265  1.00 43.74           H  
ATOM   1481 HG12 VAL A  93     -28.275 -85.905  -3.492  1.00 43.74           H  
ATOM   1482 HG13 VAL A  93     -29.562 -86.513  -2.788  1.00 43.74           H  
ATOM   1483 HG21 VAL A  93     -28.943 -87.021  -6.761  1.00 39.77           H  
ATOM   1484 HG22 VAL A  93     -27.905 -86.218  -5.865  1.00 39.77           H  
ATOM   1485 HG23 VAL A  93     -28.017 -87.797  -5.729  1.00 39.77           H  
ATOM   1486  N   ASP A  94     -32.495 -86.938  -3.901  1.00 29.74           N  
ANISOU 1486  N   ASP A  94     4499   1919   4880   -603  -1215    503       N  
ATOM   1487  CA  ASP A  94     -33.332 -86.479  -2.808  1.00 26.58           C  
ANISOU 1487  CA  ASP A  94     3942   1629   4530   -645  -1202    646       C  
ATOM   1488  C   ASP A  94     -34.538 -85.738  -3.376  1.00 26.61           C  
ANISOU 1488  C   ASP A  94     3909   1692   4510   -718  -1249    706       C  
ATOM   1489  O   ASP A  94     -34.459 -84.553  -3.697  1.00 32.72           O  
ANISOU 1489  O   ASP A  94     4674   2515   5242   -701  -1190    691       O  
ATOM   1490  CB  ASP A  94     -32.511 -85.571  -1.893  1.00 25.34           C  
ANISOU 1490  CB  ASP A  94     3707   1542   4379   -573  -1076    657       C  
ATOM   1491  CG  ASP A  94     -33.160 -85.357  -0.547  1.00 26.95           C  
ANISOU 1491  CG  ASP A  94     3758   1851   4631   -593  -1052    795       C  
ATOM   1492  OD1 ASP A  94     -34.395 -85.509  -0.444  1.00 25.48           O  
ANISOU 1492  OD1 ASP A  94     3507   1707   4466   -666  -1117    891       O  
ATOM   1493  OD2 ASP A  94     -32.432 -85.034   0.415  1.00 29.77           O  
ANISOU 1493  OD2 ASP A  94     4059   2250   5003   -534   -967    810       O  
ATOM   1494  H   ASP A  94     -32.684 -86.586  -4.662  1.00 35.68           H  
ATOM   1495  HA  ASP A  94     -33.646 -87.239  -2.293  1.00 31.90           H  
ATOM   1496  HB2 ASP A  94     -31.641 -85.974  -1.746  1.00 30.41           H  
ATOM   1497  HB3 ASP A  94     -32.408 -84.705  -2.318  1.00 30.41           H  
ATOM   1498  N   ASP A  95     -35.654 -86.449  -3.500  1.00 32.75           N  
ANISOU 1498  N   ASP A  95     4665   2462   5317   -799  -1361    778       N  
ATOM   1499  CA  ASP A  95     -36.815 -85.943  -4.226  1.00 33.77           C  
ANISOU 1499  CA  ASP A  95     4775   2628   5427   -872  -1432    829       C  
ATOM   1500  C   ASP A  95     -37.499 -84.742  -3.557  1.00 33.61           C  
ANISOU 1500  C   ASP A  95     4606   2739   5424   -877  -1372    940       C  
ATOM   1501  O   ASP A  95     -38.178 -83.966  -4.230  1.00 28.51           O  
ANISOU 1501  O   ASP A  95     3952   2130   4751   -911  -1398    962       O  
ATOM   1502  CB  ASP A  95     -37.831 -87.074  -4.441  1.00 39.65           C  
ANISOU 1502  CB  ASP A  95     5524   3333   6209   -959  -1576    890       C  
ATOM   1503  CG  ASP A  95     -38.671 -86.877  -5.693  1.00 54.34           C  
ANISOU 1503  CG  ASP A  95     7445   5174   8027  -1027  -1679    882       C  
ATOM   1504  OD1 ASP A  95     -38.660 -85.763  -6.257  1.00 57.86           O  
ANISOU 1504  OD1 ASP A  95     7902   5659   8424  -1013  -1636    856       O  
ATOM   1505  OD2 ASP A  95     -39.346 -87.840  -6.114  1.00 59.10           O  
ANISOU 1505  OD2 ASP A  95     8088   5721   8646  -1095  -1808    906       O  
ATOM   1506  H   ASP A  95     -35.765 -87.235  -3.169  1.00 39.30           H  
ATOM   1507  HA  ASP A  95     -36.519 -85.652  -5.103  1.00 40.52           H  
ATOM   1508  HB2 ASP A  95     -37.355 -87.914  -4.528  1.00 47.58           H  
ATOM   1509  HB3 ASP A  95     -38.430 -87.109  -3.679  1.00 47.58           H  
ATOM   1510  N   SER A  96     -37.311 -84.582  -2.248  1.00 29.96           N  
ANISOU 1510  N   SER A  96     4032   2348   5003   -839  -1291   1009       N  
ATOM   1511  CA  SER A  96     -37.988 -83.526  -1.490  1.00 30.59           C  
ANISOU 1511  CA  SER A  96     3969   2556   5099   -833  -1229   1119       C  
ATOM   1512  C   SER A  96     -37.037 -82.405  -1.076  1.00 24.86           C  
ANISOU 1512  C   SER A  96     3237   1871   4337   -746  -1095   1076       C  
ATOM   1513  O   SER A  96     -37.412 -81.515  -0.313  1.00 30.10           O  
ANISOU 1513  O   SER A  96     3793   2638   5007   -719  -1027   1157       O  
ATOM   1514  CB  SER A  96     -38.636 -84.121  -0.239  1.00 30.43           C  
ANISOU 1514  CB  SER A  96     3817   2603   5143   -856  -1237   1247       C  
ATOM   1515  OG  SER A  96     -39.522 -85.171  -0.582  1.00 38.56           O  
ANISOU 1515  OG  SER A  96     4847   3595   6210   -941  -1367   1297       O  
ATOM   1516  H   SER A  96     -36.793 -85.075  -1.771  1.00 35.95           H  
ATOM   1517  HA  SER A  96     -38.689 -83.140  -2.039  1.00 36.71           H  
ATOM   1518  HB2 SER A  96     -37.941 -84.470   0.341  1.00 36.52           H  
ATOM   1519  HB3 SER A  96     -39.132 -83.425   0.220  1.00 36.52           H  
ATOM   1520  HG  SER A  96     -39.872 -85.490   0.112  1.00 46.27           H  
ATOM   1521  N   PHE A  97     -35.812 -82.446  -1.592  1.00 25.35           N  
ANISOU 1521  N   PHE A  97     3414   1861   4357   -696  -1058    945       N  
ATOM   1522  CA  PHE A  97     -34.755 -81.529  -1.163  1.00 27.53           C  
ANISOU 1522  CA  PHE A  97     3677   2209   4575   -597   -920    875       C  
ATOM   1523  C   PHE A  97     -35.106 -80.048  -1.369  1.00 28.22           C  
ANISOU 1523  C   PHE A  97     3720   2400   4601   -571   -856    880       C  
ATOM   1524  O   PHE A  97     -35.043 -79.259  -0.425  1.00 27.22           O  
ANISOU 1524  O   PHE A  97     3508   2369   4466   -520   -770    921       O  
ATOM   1525  CB  PHE A  97     -33.443 -81.883  -1.871  1.00 23.11           C  
ANISOU 1525  CB  PHE A  97     3242   1570   3970   -548   -893    728       C  
ATOM   1526  CG  PHE A  97     -32.299 -80.973  -1.531  1.00 24.04           C  
ANISOU 1526  CG  PHE A  97     3346   1758   4030   -459   -763    657       C  
ATOM   1527  CD1 PHE A  97     -31.727 -80.997  -0.269  1.00 21.67           C  
ANISOU 1527  CD1 PHE A  97     2972   1503   3760   -410   -697    688       C  
ATOM   1528  CD2 PHE A  97     -31.781 -80.104  -2.481  1.00 21.79           C  
ANISOU 1528  CD2 PHE A  97     3124   1493   3661   -430   -711    564       C  
ATOM   1529  CE1 PHE A  97     -30.667 -80.161   0.043  1.00 22.91           C  
ANISOU 1529  CE1 PHE A  97     3117   1721   3867   -338   -590    627       C  
ATOM   1530  CE2 PHE A  97     -30.723 -79.270  -2.176  1.00 21.01           C  
ANISOU 1530  CE2 PHE A  97     3009   1458   3515   -360   -600    508       C  
ATOM   1531  CZ  PHE A  97     -30.165 -79.298  -0.912  1.00 20.56           C  
ANISOU 1531  CZ  PHE A  97     2877   1442   3493   -315   -542    539       C  
ATOM   1532  H   PHE A  97     -35.564 -83.002  -2.199  1.00 30.42           H  
ATOM   1533  HA  PHE A  97     -34.612 -81.658  -0.212  1.00 33.04           H  
ATOM   1534  HB2 PHE A  97     -33.188 -82.785  -1.622  1.00 27.74           H  
ATOM   1535  HB3 PHE A  97     -33.584 -81.835  -2.830  1.00 27.74           H  
ATOM   1536  HD1 PHE A  97     -32.062 -81.576   0.377  1.00 26.01           H  
ATOM   1537  HD2 PHE A  97     -32.154 -80.081  -3.333  1.00 26.15           H  
ATOM   1538  HE1 PHE A  97     -30.292 -80.183   0.894  1.00 27.49           H  
ATOM   1539  HE2 PHE A  97     -30.388 -78.689  -2.820  1.00 25.21           H  
ATOM   1540  HZ  PHE A  97     -29.453 -78.737  -0.704  1.00 24.67           H  
ATOM   1541  N   PHE A  98     -35.476 -79.668  -2.589  1.00 33.05           N  
ANISOU 1541  N   PHE A  98     4399   2990   5168   -603   -902    841       N  
ATOM   1542  CA  PHE A  98     -35.814 -78.273  -2.868  1.00 25.58           C  
ANISOU 1542  CA  PHE A  98     3423   2131   4167   -578   -851    847       C  
ATOM   1543  C   PHE A  98     -37.106 -77.835  -2.172  1.00 31.43           C  
ANISOU 1543  C   PHE A  98     4032   2957   4954   -598   -867    987       C  
ATOM   1544  O   PHE A  98     -37.304 -76.645  -1.929  1.00 32.04           O  
ANISOU 1544  O   PHE A  98     4057   3119   4996   -550   -800   1005       O  
ATOM   1545  CB  PHE A  98     -35.930 -78.023  -4.376  1.00 22.58           C  
ANISOU 1545  CB  PHE A  98     3150   1704   3724   -613   -906    778       C  
ATOM   1546  CG  PHE A  98     -34.642 -78.224  -5.136  1.00 22.47           C  
ANISOU 1546  CG  PHE A  98     3262   1630   3644   -577   -867    637       C  
ATOM   1547  CD1 PHE A  98     -33.433 -77.791  -4.616  1.00 21.69           C  
ANISOU 1547  CD1 PHE A  98     3158   1568   3516   -500   -750    574       C  
ATOM   1548  CD2 PHE A  98     -34.646 -78.837  -6.378  1.00 23.26           C  
ANISOU 1548  CD2 PHE A  98     3486   1641   3709   -620   -947    570       C  
ATOM   1549  CE1 PHE A  98     -32.253 -77.973  -5.319  1.00 22.08           C  
ANISOU 1549  CE1 PHE A  98     3308   1575   3507   -465   -708    454       C  
ATOM   1550  CE2 PHE A  98     -33.470 -79.023  -7.082  1.00 23.29           C  
ANISOU 1550  CE2 PHE A  98     3604   1601   3646   -577   -900    442       C  
ATOM   1551  CZ  PHE A  98     -32.274 -78.590  -6.552  1.00 27.73           C  
ANISOU 1551  CZ  PHE A  98     4143   2209   4185   -498   -777    387       C  
ATOM   1552  H   PHE A  98     -35.540 -80.192  -3.267  1.00 39.66           H  
ATOM   1553  HA  PHE A  98     -35.098 -77.710  -2.534  1.00 30.70           H  
ATOM   1554  HB2 PHE A  98     -36.588 -78.635  -4.743  1.00 27.09           H  
ATOM   1555  HB3 PHE A  98     -36.219 -77.108  -4.520  1.00 27.09           H  
ATOM   1556  HD1 PHE A  98     -33.412 -77.375  -3.785  1.00 26.03           H  
ATOM   1557  HD2 PHE A  98     -35.450 -79.133  -6.741  1.00 27.91           H  
ATOM   1558  HE1 PHE A  98     -31.447 -77.680  -4.958  1.00 26.50           H  
ATOM   1559  HE2 PHE A  98     -33.487 -79.438  -7.914  1.00 27.95           H  
ATOM   1560  HZ  PHE A  98     -31.482 -78.713  -7.025  1.00 33.28           H  
ATOM   1561  N   HIS A  99     -37.983 -78.786  -1.855  1.00 27.57           N  
ANISOU 1561  N   HIS A  99     3487   2445   4544   -666   -954   1088       N  
ATOM   1562  CA  HIS A  99     -39.215 -78.471  -1.133  1.00 27.81           C  
ANISOU 1562  CA  HIS A  99     3375   2569   4624   -683   -963   1235       C  
ATOM   1563  C   HIS A  99     -38.938 -78.258   0.354  1.00 30.95           C  
ANISOU 1563  C   HIS A  99     3678   3049   5035   -615   -860   1284       C  
ATOM   1564  O   HIS A  99     -39.690 -77.569   1.044  1.00 34.26           O  
ANISOU 1564  O   HIS A  99     3985   3571   5460   -584   -815   1376       O  
ATOM   1565  CB  HIS A  99     -40.247 -79.588  -1.300  1.00 27.76           C  
ANISOU 1565  CB  HIS A  99     3334   2514   4700   -791  -1097   1340       C  
ATOM   1566  CG  HIS A  99     -40.763 -79.737  -2.698  1.00 33.28           C  
ANISOU 1566  CG  HIS A  99     4114   3144   5387   -867  -1215   1314       C  
ATOM   1567  ND1 HIS A  99     -40.144 -80.527  -3.643  1.00 43.91           N  
ANISOU 1567  ND1 HIS A  99     5609   4368   6707   -901  -1283   1203       N  
ATOM   1568  CD2 HIS A  99     -41.846 -79.200  -3.309  1.00 29.46           C  
ANISOU 1568  CD2 HIS A  99     3585   2702   4907   -908  -1277   1382       C  
ATOM   1569  CE1 HIS A  99     -40.822 -80.469  -4.775  1.00 39.12           C  
ANISOU 1569  CE1 HIS A  99     5053   3732   6080   -963  -1384   1200       C  
ATOM   1570  NE2 HIS A  99     -41.859 -79.670  -4.599  1.00 41.82           N  
ANISOU 1570  NE2 HIS A  99     5277   4165   6448   -977  -1389   1315       N  
ATOM   1571  H   HIS A  99     -37.889 -79.619  -2.045  1.00 33.09           H  
ATOM   1572  HA  HIS A  99     -39.593 -77.653  -1.491  1.00 33.38           H  
ATOM   1573  HB2 HIS A  99     -39.840 -80.430  -1.044  1.00 33.31           H  
ATOM   1574  HB3 HIS A  99     -41.005 -79.401  -0.724  1.00 33.31           H  
ATOM   1575  HD1 HIS A  99     -39.429 -80.987  -3.515  1.00 52.69           H  
ATOM   1576  HD2 HIS A  99     -42.464 -78.620  -2.926  1.00 35.36           H  
ATOM   1577  HE1 HIS A  99     -40.606 -80.914  -5.563  1.00 46.95           H  
ATOM   1578  HE2 HIS A  99     -42.447 -79.475  -5.196  1.00 50.18           H  
ATOM   1579  N   ARG A 100     -37.858 -78.860   0.845  1.00 32.54           N  
ANISOU 1579  N   ARG A 100     3926   3204   5236   -588   -824   1223       N  
ATOM   1580  CA  ARG A 100     -37.501 -78.764   2.257  1.00 36.68           C  
ANISOU 1580  CA  ARG A 100     4374   3797   5766   -529   -736   1265       C  
ATOM   1581  C   ARG A 100     -36.928 -77.395   2.603  1.00 30.44           C  
ANISOU 1581  C   ARG A 100     3581   3084   4901   -435   -621   1205       C  
ATOM   1582  O   ARG A 100     -37.064 -76.925   3.732  1.00 40.65           O  
ANISOU 1582  O   ARG A 100     4795   4464   6185   -382   -550   1262       O  
ATOM   1583  CB  ARG A 100     -36.477 -79.841   2.630  1.00 33.75           C  
ANISOU 1583  CB  ARG A 100     4057   3345   5421   -529   -744   1217       C  
ATOM   1584  CG  ARG A 100     -37.013 -80.919   3.558  1.00 31.40           C  
ANISOU 1584  CG  ARG A 100     3685   3044   5201   -578   -791   1340       C  
ATOM   1585  CD  ARG A 100     -35.890 -81.732   4.186  1.00 34.87           C  
ANISOU 1585  CD  ARG A 100     4166   3425   5657   -550   -774   1297       C  
ATOM   1586  NE  ARG A 100     -35.076 -82.411   3.182  1.00 36.52           N  
ANISOU 1586  NE  ARG A 100     4504   3506   5866   -560   -826   1179       N  
ATOM   1587  CZ  ARG A 100     -35.481 -83.464   2.482  1.00 37.05           C  
ANISOU 1587  CZ  ARG A 100     4623   3493   5961   -625   -932   1167       C  
ATOM   1588  NH1 ARG A 100     -36.694 -83.963   2.667  1.00 36.76           N  
ANISOU 1588  NH1 ARG A 100     4513   3493   5961   -694  -1002   1269       N  
ATOM   1589  NH2 ARG A 100     -34.673 -84.014   1.591  1.00 44.99           N  
ANISOU 1589  NH2 ARG A 100     5755   4385   6955   -617   -966   1050       N  
ATOM   1590  H   ARG A 100     -37.313 -79.333   0.378  1.00 39.05           H  
ATOM   1591  HA  ARG A 100     -38.296 -78.903   2.796  1.00 44.02           H  
ATOM   1592  HB2 ARG A 100     -36.172 -80.276   1.818  1.00 40.50           H  
ATOM   1593  HB3 ARG A 100     -35.726 -79.416   3.075  1.00 40.50           H  
ATOM   1594  HG2 ARG A 100     -37.521 -80.503   4.272  1.00 37.68           H  
ATOM   1595  HG3 ARG A 100     -37.579 -81.524   3.053  1.00 37.68           H  
ATOM   1596  HD2 ARG A 100     -35.313 -81.140   4.693  1.00 41.84           H  
ATOM   1597  HD3 ARG A 100     -36.272 -82.406   4.771  1.00 41.84           H  
ATOM   1598  HE  ARG A 100     -34.275 -82.126   3.055  1.00 43.82           H  
ATOM   1599 HH11 ARG A 100     -37.222 -83.607   3.245  1.00 44.11           H  
ATOM   1600 HH12 ARG A 100     -36.952 -84.644   2.210  1.00 44.11           H  
ATOM   1601 HH21 ARG A 100     -33.885 -83.692   1.468  1.00 53.99           H  
ATOM   1602 HH22 ARG A 100     -34.935 -84.695   1.136  1.00 53.99           H  
ATOM   1603  N   LEU A 101     -36.291 -76.756   1.628  1.00 40.42           N  
ANISOU 1603  N   LEU A 101     4937   4314   6106   -416   -605   1093       N  
ATOM   1604  CA  LEU A 101     -35.526 -75.540   1.886  1.00 40.04           C  
ANISOU 1604  CA  LEU A 101     4908   4318   5989   -337   -506   1024       C  
ATOM   1605  C   LEU A 101     -36.398 -74.327   2.201  1.00 47.96           C  
ANISOU 1605  C   LEU A 101     5844   5413   6967   -296   -467   1085       C  
ATOM   1606  O   LEU A 101     -37.496 -74.169   1.663  1.00 50.67           O  
ANISOU 1606  O   LEU A 101     6152   5772   7329   -329   -520   1147       O  
ATOM   1607  CB  LEU A 101     -34.604 -75.235   0.704  1.00 34.94           C  
ANISOU 1607  CB  LEU A 101     4376   3611   5288   -337   -502    898       C  
ATOM   1608  CG  LEU A 101     -33.480 -76.249   0.468  1.00 37.04           C  
ANISOU 1608  CG  LEU A 101     4714   3796   5563   -344   -511    817       C  
ATOM   1609  CD1 LEU A 101     -32.708 -75.896  -0.794  1.00 32.24           C  
ANISOU 1609  CD1 LEU A 101     4212   3145   4892   -342   -501    703       C  
ATOM   1610  CD2 LEU A 101     -32.538 -76.330   1.664  1.00 33.58           C  
ANISOU 1610  CD2 LEU A 101     4243   3387   5131   -289   -440    807       C  
ATOM   1611  H   LEU A 101     -36.286 -77.006   0.805  1.00 48.50           H  
ATOM   1612  HA  LEU A 101     -34.962 -75.696   2.660  1.00 48.05           H  
ATOM   1613  HB2 LEU A 101     -35.141 -75.203  -0.103  1.00 41.93           H  
ATOM   1614  HB3 LEU A 101     -34.190 -74.371   0.852  1.00 41.93           H  
ATOM   1615  HG  LEU A 101     -33.872 -77.127   0.339  1.00 44.44           H  
ATOM   1616 HD11 LEU A 101     -32.326 -75.010  -0.691  1.00 38.68           H  
ATOM   1617 HD12 LEU A 101     -32.003 -76.548  -0.925  1.00 38.68           H  
ATOM   1618 HD13 LEU A 101     -33.316 -75.909  -1.549  1.00 38.68           H  
ATOM   1619 HD21 LEU A 101     -33.043 -76.603   2.445  1.00 40.30           H  
ATOM   1620 HD22 LEU A 101     -31.843 -76.980   1.474  1.00 40.30           H  
ATOM   1621 HD23 LEU A 101     -32.142 -75.457   1.814  1.00 40.30           H  
ATOM   1622  N   GLU A 102     -35.877 -73.480   3.085  1.00106.10           N  
ANISOU 1622  N   GLU A 102    13192  12835  14288   -221   -377   1064       N  
ATOM   1623  CA  GLU A 102     -36.542 -72.252   3.508  1.00109.31           C  
ANISOU 1623  CA  GLU A 102    13550  13322  14661   -160   -328   1105       C  
ATOM   1624  C   GLU A 102     -36.960 -71.400   2.313  1.00109.60           C  
ANISOU 1624  C   GLU A 102    13631  13343  14668   -169   -357   1077       C  
ATOM   1625  O   GLU A 102     -37.391 -70.258   2.471  1.00109.98           O  
ANISOU 1625  O   GLU A 102    13661  13442  14683   -112   -320   1092       O  
ATOM   1626  CB  GLU A 102     -35.606 -71.448   4.419  1.00105.49           C  
ANISOU 1626  CB  GLU A 102    13089  12872  14120    -84   -239   1050       C  
ATOM   1627  CG  GLU A 102     -35.962 -71.500   5.899  1.00110.50           C  
ANISOU 1627  CG  GLU A 102    13641  13585  14758    -32   -189   1128       C  
ATOM   1628  CD  GLU A 102     -34.874 -70.912   6.780  1.00116.61           C  
ANISOU 1628  CD  GLU A 102    14455  14375  15476     29   -120   1063       C  
ATOM   1629  OE1 GLU A 102     -33.977 -70.229   6.243  1.00120.56           O  
ANISOU 1629  OE1 GLU A 102    15037  14837  15936     36   -107    967       O  
ATOM   1630  OE2 GLU A 102     -34.914 -71.137   8.009  1.00114.87           O  
ANISOU 1630  OE2 GLU A 102    14186  14208  15251     64    -83   1113       O  
ATOM   1631  H   GLU A 102     -35.115 -73.600   3.465  1.00127.33           H  
ATOM   1632  HA  GLU A 102     -37.339 -72.478   4.014  1.00131.17           H  
ATOM   1633  HB2 GLU A 102     -34.705 -71.794   4.321  1.00126.59           H  
ATOM   1634  HB3 GLU A 102     -35.630 -70.518   4.144  1.00126.59           H  
ATOM   1635  HG2 GLU A 102     -36.776 -70.994   6.047  1.00132.59           H  
ATOM   1636  HG3 GLU A 102     -36.094 -72.425   6.161  1.00132.59           H  
ATOM   1637  N   ARG A 115     -33.631 -73.336  14.040  1.00162.19           N  
ANISOU 1637  N   ARG A 115    20036  20407  21182    172     50   1324       N  
ATOM   1638  CA  ARG A 115     -33.018 -73.943  12.864  1.00165.38           C  
ANISOU 1638  CA  ARG A 115    20481  20706  21649    104    -13   1261       C  
ATOM   1639  C   ARG A 115     -34.024 -74.814  12.115  1.00167.49           C  
ANISOU 1639  C   ARG A 115    20695  20949  21996     36    -70   1337       C  
ATOM   1640  O   ARG A 115     -34.867 -75.470  12.730  1.00171.46           O  
ANISOU 1640  O   ARG A 115    21119  21500  22528     17    -76   1454       O  
ATOM   1641  CB  ARG A 115     -31.803 -74.780  13.271  1.00166.70           C  
ANISOU 1641  CB  ARG A 115    20678  20824  21838     84    -36   1229       C  
ATOM   1642  CG  ARG A 115     -30.646 -73.957  13.818  1.00163.07           C  
ANISOU 1642  CG  ARG A 115    20277  20374  21310    135      1   1144       C  
ATOM   1643  CD  ARG A 115     -29.516 -74.840  14.320  1.00162.50           C  
ANISOU 1643  CD  ARG A 115    20215  20264  21264    119    -26   1132       C  
ATOM   1644  NE  ARG A 115     -29.916 -75.651  15.468  1.00165.47           N  
ANISOU 1644  NE  ARG A 115    20538  20686  21648    119    -28   1239       N  
ATOM   1645  CZ  ARG A 115     -29.119 -76.518  16.085  1.00164.10           C  
ANISOU 1645  CZ  ARG A 115    20363  20487  21499    107    -56   1255       C  
ATOM   1646  NH1 ARG A 115     -27.871 -76.697  15.666  1.00157.10           N  
ANISOU 1646  NH1 ARG A 115    19520  19535  20637    102    -80   1170       N  
ATOM   1647  NH2 ARG A 115     -29.569 -77.212  17.122  1.00161.38           N  
ANISOU 1647  NH2 ARG A 115    19971  20188  21156    103    -58   1364       N  
ATOM   1648  HA  ARG A 115     -32.717 -73.244  12.264  1.00198.45           H  
ATOM   1649  HB2 ARG A 115     -32.072 -75.408  13.960  1.00200.05           H  
ATOM   1650  HB3 ARG A 115     -31.481 -75.263  12.494  1.00200.05           H  
ATOM   1651  HG2 ARG A 115     -30.297 -73.388  13.114  1.00195.69           H  
ATOM   1652  HG3 ARG A 115     -30.961 -73.416  14.560  1.00195.69           H  
ATOM   1653  HD2 ARG A 115     -29.241 -75.439  13.609  1.00195.00           H  
ATOM   1654  HD3 ARG A 115     -28.771 -74.280  14.591  1.00195.00           H  
ATOM   1655  HE  ARG A 115     -30.718 -75.561  15.764  1.00198.56           H  
ATOM   1656 HH11 ARG A 115     -27.574 -76.249  14.994  1.00188.52           H  
ATOM   1657 HH12 ARG A 115     -27.358 -77.259  16.068  1.00188.52           H  
ATOM   1658 HH21 ARG A 115     -30.377 -77.100  17.397  1.00193.65           H  
ATOM   1659 HH22 ARG A 115     -29.054 -77.774  17.521  1.00193.65           H  
ATOM   1660  N   HIS A 116     -33.929 -74.807  10.787  1.00 90.74           N  
ANISOU 1660  N   HIS A 116    11019  11153  12306     -5   -114   1273       N  
ATOM   1661  CA  HIS A 116     -34.771 -75.643   9.933  1.00 84.69           C  
ANISOU 1661  CA  HIS A 116    10222  10344  11612    -80   -187   1329       C  
ATOM   1662  C   HIS A 116     -33.902 -76.627   9.157  1.00 88.09           C  
ANISOU 1662  C   HIS A 116    10719  10660  12090   -135   -250   1261       C  
ATOM   1663  O   HIS A 116     -32.839 -76.256   8.656  1.00 85.16           O  
ANISOU 1663  O   HIS A 116    10423  10245  11690   -115   -234   1149       O  
ATOM   1664  CB  HIS A 116     -35.587 -74.779   8.971  1.00 80.69           C  
ANISOU 1664  CB  HIS A 116     9715   9850  11093    -79   -193   1319       C  
ATOM   1665  CG  HIS A 116     -36.772 -74.126   9.605  1.00 98.13           C  
ANISOU 1665  CG  HIS A 116    11836  12166  13281    -33   -149   1416       C  
ATOM   1666  ND1 HIS A 116     -37.436 -74.671  10.687  1.00102.52           N  
ANISOU 1666  ND1 HIS A 116    12300  12798  13856    -30   -130   1538       N  
ATOM   1667  CD2 HIS A 116     -37.421 -72.970   9.320  1.00101.48           C  
ANISOU 1667  CD2 HIS A 116    12250  12639  13668     18   -117   1413       C  
ATOM   1668  CE1 HIS A 116     -38.435 -73.886  11.035  1.00100.50           C  
ANISOU 1668  CE1 HIS A 116    11975  12638  13571     26    -81   1603       C  
ATOM   1669  NE2 HIS A 116     -38.447 -72.842  10.218  1.00101.95           N  
ANISOU 1669  NE2 HIS A 116    12208  12804  13723     59    -75   1527       N  
ATOM   1670  H   HIS A 116     -33.374 -74.317  10.348  1.00108.89           H  
ATOM   1671  HA  HIS A 116     -35.387 -76.149  10.486  1.00101.63           H  
ATOM   1672  HB2 HIS A 116     -35.016 -74.079   8.618  1.00 96.83           H  
ATOM   1673  HB3 HIS A 116     -35.909 -75.337   8.246  1.00 96.83           H  
ATOM   1674  HD1 HIS A 116     -37.230 -75.411  11.074  1.00123.03           H  
ATOM   1675  HD2 HIS A 116     -37.208 -72.374   8.639  1.00121.77           H  
ATOM   1676  HE1 HIS A 116     -39.029 -74.037  11.735  1.00120.60           H  
ATOM   1677  HE2 HIS A 116     -39.008 -72.191  10.246  1.00122.34           H  
ATOM   1678  N   PRO A 117     -34.353 -77.887   9.045  1.00 60.35           N  
ANISOU 1678  N   PRO A 117     7181   7099   8651   -203   -321   1332       N  
ATOM   1679  CA  PRO A 117     -33.459 -78.910   8.500  1.00 57.58           C  
ANISOU 1679  CA  PRO A 117     6899   6635   8342   -238   -378   1267       C  
ATOM   1680  C   PRO A 117     -33.333 -78.864   6.984  1.00 52.90           C  
ANISOU 1680  C   PRO A 117     6385   5962   7753   -269   -422   1176       C  
ATOM   1681  O   PRO A 117     -34.326 -78.726   6.270  1.00 51.12           O  
ANISOU 1681  O   PRO A 117     6147   5738   7540   -311   -464   1211       O  
ATOM   1682  CB  PRO A 117     -34.130 -80.212   8.928  1.00 54.80           C  
ANISOU 1682  CB  PRO A 117     6498   6255   8067   -304   -447   1384       C  
ATOM   1683  CG  PRO A 117     -35.582 -79.885   8.930  1.00 62.16           C  
ANISOU 1683  CG  PRO A 117     7347   7262   9010   -335   -456   1493       C  
ATOM   1684  CD  PRO A 117     -35.690 -78.435   9.347  1.00 61.32           C  
ANISOU 1684  CD  PRO A 117     7213   7263   8824   -253   -360   1474       C  
ATOM   1685  HA  PRO A 117     -32.579 -78.848   8.904  1.00 69.09           H  
ATOM   1686  HB2 PRO A 117     -33.934 -80.912   8.286  1.00 65.76           H  
ATOM   1687  HB3 PRO A 117     -33.830 -80.462   9.816  1.00 65.76           H  
ATOM   1688  HG2 PRO A 117     -35.943 -80.010   8.039  1.00 74.59           H  
ATOM   1689  HG3 PRO A 117     -36.041 -80.456   9.566  1.00 74.59           H  
ATOM   1690  HD2 PRO A 117     -36.367 -77.982   8.821  1.00 73.59           H  
ATOM   1691  HD3 PRO A 117     -35.875 -78.369  10.297  1.00 73.59           H  
ATOM   1692  N   ILE A 118     -32.100 -78.985   6.508  1.00 34.46           N  
ANISOU 1692  N   ILE A 118     4129   3564   5402   -246   -412   1062       N  
ATOM   1693  CA  ILE A 118     -31.821 -79.053   5.085  1.00 36.12           C  
ANISOU 1693  CA  ILE A 118     4424   3696   5604   -268   -448    968       C  
ATOM   1694  C   ILE A 118     -32.119 -80.459   4.579  1.00 39.38           C  
ANISOU 1694  C   ILE A 118     4871   4004   6085   -331   -547    989       C  
ATOM   1695  O   ILE A 118     -32.640 -80.635   3.477  1.00 48.90           O  
ANISOU 1695  O   ILE A 118     6126   5157   7296   -379   -608    968       O  
ATOM   1696  CB  ILE A 118     -30.348 -78.700   4.816  1.00 41.90           C  
ANISOU 1696  CB  ILE A 118     5218   4409   6293   -215   -392    847       C  
ATOM   1697  CG1 ILE A 118     -30.103 -77.226   5.145  1.00 35.19           C  
ANISOU 1697  CG1 ILE A 118     4348   3647   5374   -167   -311    823       C  
ATOM   1698  CG2 ILE A 118     -29.960 -78.981   3.363  1.00 44.93           C  
ANISOU 1698  CG2 ILE A 118     5695   4711   6666   -233   -424    750       C  
ATOM   1699  CD1 ILE A 118     -28.738 -76.956   5.725  1.00 35.35           C  
ANISOU 1699  CD1 ILE A 118     4378   3684   5369   -115   -252    763       C  
ATOM   1700  H   ILE A 118     -31.397 -79.031   7.001  1.00 41.36           H  
ATOM   1701  HA  ILE A 118     -32.385 -78.424   4.609  1.00 43.34           H  
ATOM   1702  HB  ILE A 118     -29.790 -79.242   5.395  1.00 50.28           H  
ATOM   1703 HG12 ILE A 118     -30.189 -76.705   4.332  1.00 42.22           H  
ATOM   1704 HG13 ILE A 118     -30.764 -76.936   5.794  1.00 42.22           H  
ATOM   1705 HG21 ILE A 118     -30.520 -78.447   2.778  1.00 53.92           H  
ATOM   1706 HG22 ILE A 118     -29.027 -78.746   3.235  1.00 53.92           H  
ATOM   1707 HG23 ILE A 118     -30.092 -79.924   3.179  1.00 53.92           H  
ATOM   1708 HD11 ILE A 118     -28.064 -77.230   5.084  1.00 42.42           H  
ATOM   1709 HD12 ILE A 118     -28.655 -76.007   5.908  1.00 42.42           H  
ATOM   1710 HD13 ILE A 118     -28.639 -77.462   6.547  1.00 42.42           H  
ATOM   1711  N   PHE A 119     -31.799 -81.453   5.405  1.00 33.76           N  
ANISOU 1711  N   PHE A 119     4141   3260   5425   -333   -569   1032       N  
ATOM   1712  CA  PHE A 119     -31.913 -82.856   5.020  1.00 32.65           C  
ANISOU 1712  CA  PHE A 119     4049   3003   5354   -386   -667   1045       C  
ATOM   1713  C   PHE A 119     -33.132 -83.521   5.647  1.00 31.35           C  
ANISOU 1713  C   PHE A 119     3810   2851   5253   -459   -734   1194       C  
ATOM   1714  O   PHE A 119     -33.703 -83.011   6.610  1.00 34.94           O  
ANISOU 1714  O   PHE A 119     4167   3412   5697   -451   -687   1290       O  
ATOM   1715  CB  PHE A 119     -30.643 -83.605   5.421  1.00 26.37           C  
ANISOU 1715  CB  PHE A 119     3292   2146   4579   -338   -656    989       C  
ATOM   1716  CG  PHE A 119     -29.405 -83.062   4.779  1.00 34.84           C  
ANISOU 1716  CG  PHE A 119     4428   3212   5598   -270   -592    850       C  
ATOM   1717  CD1 PHE A 119     -29.066 -83.425   3.489  1.00 30.33           C  
ANISOU 1717  CD1 PHE A 119     3956   2551   5016   -271   -625    750       C  
ATOM   1718  CD2 PHE A 119     -28.587 -82.178   5.459  1.00 40.82           C  
ANISOU 1718  CD2 PHE A 119     5146   4054   6310   -207   -499    824       C  
ATOM   1719  CE1 PHE A 119     -27.932 -82.923   2.889  1.00 35.51           C  
ANISOU 1719  CE1 PHE A 119     4660   3214   5619   -209   -557    632       C  
ATOM   1720  CE2 PHE A 119     -27.449 -81.671   4.864  1.00 37.20           C  
ANISOU 1720  CE2 PHE A 119     4733   3596   5806   -154   -442    709       C  
ATOM   1721  CZ  PHE A 119     -27.121 -82.044   3.578  1.00 33.81           C  
ANISOU 1721  CZ  PHE A 119     4391   3087   5367   -154   -466    617       C  
ATOM   1722  H   PHE A 119     -31.510 -81.337   6.206  1.00 40.51           H  
ATOM   1723  HA  PHE A 119     -32.003 -82.913   4.056  1.00 39.18           H  
ATOM   1724  HB2 PHE A 119     -30.532 -83.542   6.382  1.00 31.64           H  
ATOM   1725  HB3 PHE A 119     -30.731 -84.534   5.159  1.00 31.64           H  
ATOM   1726  HD1 PHE A 119     -29.610 -84.017   3.021  1.00 36.39           H  
ATOM   1727  HD2 PHE A 119     -28.805 -81.923   6.326  1.00 48.99           H  
ATOM   1728  HE1 PHE A 119     -27.713 -83.177   2.022  1.00 42.62           H  
ATOM   1729  HE2 PHE A 119     -26.905 -81.079   5.331  1.00 44.64           H  
ATOM   1730  HZ  PHE A 119     -26.354 -81.705   3.176  1.00 40.57           H  
ATOM   1731  N   GLY A 120     -33.515 -84.672   5.100  1.00 30.18           N  
ANISOU 1731  N   GLY A 120     3705   2625   5139   -517   -831   1187       N  
ATOM   1732  CA  GLY A 120     -34.719 -85.363   5.521  1.00 35.10           C  
ANISOU 1732  CA  GLY A 120     4252   3286   5797   -588   -897   1299       C  
ATOM   1733  C   GLY A 120     -34.513 -86.366   6.638  1.00 38.37           C  
ANISOU 1733  C   GLY A 120     4629   3702   6248   -591   -911   1358       C  
ATOM   1734  O   GLY A 120     -35.482 -86.950   7.126  1.00 51.38           O  
ANISOU 1734  O   GLY A 120     6205   5391   7929   -651   -962   1463       O  
ATOM   1735  H   GLY A 120     -33.084 -85.075   4.474  1.00 36.22           H  
ATOM   1736  HA2 GLY A 120     -35.369 -84.708   5.822  1.00 42.12           H  
ATOM   1737  HA3 GLY A 120     -35.096 -85.833   4.761  1.00 42.12           H  
ATOM   1738  N   ASN A 121     -33.260 -86.573   7.040  1.00 33.66           N  
ANISOU 1738  N   ASN A 121     4078   3061   5649   -528   -871   1297       N  
ATOM   1739  CA  ASN A 121     -32.941 -87.427   8.184  1.00 47.61           C  
ANISOU 1739  CA  ASN A 121     5811   4833   7446   -521   -878   1354       C  
ATOM   1740  C   ASN A 121     -31.935 -86.741   9.101  1.00 52.61           C  
ANISOU 1740  C   ASN A 121     6419   5519   8051   -440   -781   1343       C  
ATOM   1741  O   ASN A 121     -31.122 -85.932   8.651  1.00 59.52           O  
ANISOU 1741  O   ASN A 121     7338   6381   8898   -383   -726   1258       O  
ATOM   1742  CB  ASN A 121     -32.430 -88.795   7.729  1.00 43.15           C  
ANISOU 1742  CB  ASN A 121     5339   4133   6923   -534   -963   1295       C  
ATOM   1743  CG  ASN A 121     -31.073 -88.725   7.062  1.00 45.56           C  
ANISOU 1743  CG  ASN A 121     5747   4348   7217   -457   -935   1159       C  
ATOM   1744  OD1 ASN A 121     -30.056 -88.489   7.715  1.00 53.11           O  
ANISOU 1744  OD1 ASN A 121     6693   5318   8169   -388   -873   1139       O  
ATOM   1745  ND2 ASN A 121     -31.047 -88.948   5.753  1.00 45.26           N  
ANISOU 1745  ND2 ASN A 121     5807   4217   7173   -468   -982   1067       N  
ATOM   1746  H   ASN A 121     -32.570 -86.227   6.662  1.00 40.39           H  
ATOM   1747  HA  ASN A 121     -33.752 -87.573   8.696  1.00 57.14           H  
ATOM   1748  HB2 ASN A 121     -32.354 -89.377   8.502  1.00 51.78           H  
ATOM   1749  HB3 ASN A 121     -33.058 -89.171   7.092  1.00 51.78           H  
ATOM   1750 HD21 ASN A 121     -31.776 -89.122   5.332  1.00 54.31           H  
ATOM   1751 HD22 ASN A 121     -30.300 -88.920   5.327  1.00 54.31           H  
ATOM   1752  N   ILE A 122     -32.019 -87.046  10.393  1.00 56.23           N  
ANISOU 1752  N   ILE A 122     6807   6043   8514   -438   -763   1434       N  
ATOM   1753  CA  ILE A 122     -31.278 -86.299  11.404  1.00 52.25           C  
ANISOU 1753  CA  ILE A 122     6268   5613   7972   -369   -675   1447       C  
ATOM   1754  C   ILE A 122     -29.776 -86.553  11.294  1.00 45.25           C  
ANISOU 1754  C   ILE A 122     5452   4643   7098   -305   -668   1351       C  
ATOM   1755  O   ILE A 122     -28.975 -85.637  11.467  1.00 52.26           O  
ANISOU 1755  O   ILE A 122     6343   5562   7953   -242   -600   1309       O  
ATOM   1756  CB  ILE A 122     -31.801 -86.611  12.836  1.00 46.10           C  
ANISOU 1756  CB  ILE A 122     5400   4930   7187   -387   -662   1574       C  
ATOM   1757  CG1 ILE A 122     -33.196 -85.986  13.020  1.00 52.90           C  
ANISOU 1757  CG1 ILE A 122     6172   5904   8024   -423   -636   1669       C  
ATOM   1758  CG2 ILE A 122     -30.812 -86.112  13.897  1.00 49.68           C  
ANISOU 1758  CG2 ILE A 122     5842   5434   7600   -314   -591   1574       C  
ATOM   1759  CD1 ILE A 122     -33.714 -85.895  14.462  1.00 59.82           C  
ANISOU 1759  CD1 ILE A 122     6953   6907   8870   -418   -587   1792       C  
ATOM   1760  H   ILE A 122     -32.500 -87.684  10.711  1.00 67.47           H  
ATOM   1761  HA  ILE A 122     -31.421 -85.352  11.246  1.00 62.70           H  
ATOM   1762  HB  ILE A 122     -31.884 -87.573  12.927  1.00 55.32           H  
ATOM   1763 HG12 ILE A 122     -33.175 -85.084  12.664  1.00 63.48           H  
ATOM   1764 HG13 ILE A 122     -33.835 -86.515  12.517  1.00 63.48           H  
ATOM   1765 HG21 ILE A 122     -30.704 -85.153  13.801  1.00 59.62           H  
ATOM   1766 HG22 ILE A 122     -31.163 -86.320  14.777  1.00 59.62           H  
ATOM   1767 HG23 ILE A 122     -29.960 -86.556  13.767  1.00 59.62           H  
ATOM   1768 HD11 ILE A 122     -33.102 -85.352  14.984  1.00 71.79           H  
ATOM   1769 HD12 ILE A 122     -34.595 -85.487  14.456  1.00 71.79           H  
ATOM   1770 HD13 ILE A 122     -33.765 -86.788  14.836  1.00 71.79           H  
ATOM   1771  N   VAL A 123     -29.405 -87.793  10.994  1.00 43.09           N  
ANISOU 1771  N   VAL A 123     5236   4263   6875   -318   -740   1318       N  
ATOM   1772  CA  VAL A 123     -27.999 -88.177  10.883  1.00 42.08           C  
ANISOU 1772  CA  VAL A 123     5168   4053   6768   -249   -737   1232       C  
ATOM   1773  C   VAL A 123     -27.270 -87.249   9.902  1.00 52.52           C  
ANISOU 1773  C   VAL A 123     6538   5348   8068   -195   -687   1121       C  
ATOM   1774  O   VAL A 123     -26.279 -86.596  10.257  1.00 61.61           O  
ANISOU 1774  O   VAL A 123     7674   6540   9194   -128   -622   1079       O  
ATOM   1775  CB  VAL A 123     -27.872 -89.665  10.450  1.00 46.14           C  
ANISOU 1775  CB  VAL A 123     5752   4442   7337   -269   -829   1203       C  
ATOM   1776  CG1 VAL A 123     -26.417 -90.061  10.157  1.00 54.05           C  
ANISOU 1776  CG1 VAL A 123     6820   5353   8364   -183   -823   1102       C  
ATOM   1777  CG2 VAL A 123     -28.473 -90.579  11.518  1.00 40.71           C  
ANISOU 1777  CG2 VAL A 123     5013   3781   6675   -322   -878   1318       C  
ATOM   1778  H   VAL A 123     -29.954 -88.439  10.848  1.00 51.71           H  
ATOM   1779  HA  VAL A 123     -27.578 -88.082  11.752  1.00 50.50           H  
ATOM   1780  HB  VAL A 123     -28.381 -89.793   9.634  1.00 55.37           H  
ATOM   1781 HG11 VAL A 123     -25.887 -89.929  10.958  1.00 64.86           H  
ATOM   1782 HG12 VAL A 123     -26.392 -90.993   9.891  1.00 64.86           H  
ATOM   1783 HG13 VAL A 123     -26.077 -89.503   9.439  1.00 64.86           H  
ATOM   1784 HG21 VAL A 123     -29.410 -90.357  11.633  1.00 48.86           H  
ATOM   1785 HG22 VAL A 123     -28.384 -91.501  11.229  1.00 48.86           H  
ATOM   1786 HG23 VAL A 123     -27.996 -90.446  12.352  1.00 48.86           H  
ATOM   1787  N   ASP A 124     -27.788 -87.174   8.679  1.00 46.83           N  
ANISOU 1787  N   ASP A 124     5871   4578   7343   -228   -716   1067       N  
ATOM   1788  CA  ASP A 124     -27.208 -86.320   7.645  1.00 39.03           C  
ANISOU 1788  CA  ASP A 124     4930   3587   6311   -186   -663    949       C  
ATOM   1789  C   ASP A 124     -27.160 -84.846   8.055  1.00 38.20           C  
ANISOU 1789  C   ASP A 124     4762   3623   6128   -159   -566    944       C  
ATOM   1790  O   ASP A 124     -26.145 -84.178   7.866  1.00 31.96           O  
ANISOU 1790  O   ASP A 124     3983   2867   5294    -99   -499    855       O  
ATOM   1791  CB  ASP A 124     -27.995 -86.452   6.338  1.00 38.74           C  
ANISOU 1791  CB  ASP A 124     4961   3484   6274   -240   -720    912       C  
ATOM   1792  CG  ASP A 124     -27.650 -87.712   5.570  1.00 45.28           C  
ANISOU 1792  CG  ASP A 124     5891   4170   7145   -237   -797    846       C  
ATOM   1793  OD1 ASP A 124     -26.454 -88.069   5.507  1.00 46.19           O  
ANISOU 1793  OD1 ASP A 124     6047   4228   7277   -161   -776    770       O  
ATOM   1794  OD2 ASP A 124     -28.577 -88.342   5.019  1.00 47.41           O  
ANISOU 1794  OD2 ASP A 124     6196   4400   7420   -305   -875    860       O  
ATOM   1795  H   ASP A 124     -28.481 -87.611   8.421  1.00 56.19           H  
ATOM   1796  HA  ASP A 124     -26.298 -86.610   7.475  1.00 46.83           H  
ATOM   1797  HB2 ASP A 124     -28.943 -86.475   6.541  1.00 46.49           H  
ATOM   1798  HB3 ASP A 124     -27.795 -85.691   5.771  1.00 46.49           H  
ATOM   1799  N   GLU A 125     -28.269 -84.344   8.591  1.00 31.62           N  
ANISOU 1799  N   GLU A 125     3864   2870   5278   -202   -560   1043       N  
ATOM   1800  CA  GLU A 125     -28.363 -82.960   9.056  1.00 32.33           C  
ANISOU 1800  CA  GLU A 125     3903   3086   5294   -173   -474   1046       C  
ATOM   1801  C   GLU A 125     -27.263 -82.632  10.070  1.00 40.18           C  
ANISOU 1801  C   GLU A 125     4871   4134   6260   -110   -418   1029       C  
ATOM   1802  O   GLU A 125     -26.458 -81.697   9.881  1.00 35.97           O  
ANISOU 1802  O   GLU A 125     4352   3642   5674    -65   -357    946       O  
ATOM   1803  CB  GLU A 125     -29.743 -82.734   9.686  1.00 30.65           C  
ANISOU 1803  CB  GLU A 125     3617   2950   5080   -218   -480   1174       C  
ATOM   1804  CG  GLU A 125     -30.008 -81.318  10.195  1.00 39.64           C  
ANISOU 1804  CG  GLU A 125     4709   4214   6140   -180   -396   1182       C  
ATOM   1805  CD  GLU A 125     -30.286 -80.325   9.081  1.00 41.89           C  
ANISOU 1805  CD  GLU A 125     5026   4509   6382   -179   -374   1109       C  
ATOM   1806  OE1 GLU A 125     -30.781 -80.742   8.014  1.00 47.42           O  
ANISOU 1806  OE1 GLU A 125     5761   5143   7114   -227   -432   1094       O  
ATOM   1807  OE2 GLU A 125     -30.015 -79.121   9.277  1.00 39.30           O  
ANISOU 1807  OE2 GLU A 125     4693   4252   5986   -133   -305   1068       O  
ATOM   1808  H   GLU A 125     -28.995 -84.793   8.698  1.00 37.94           H  
ATOM   1809  HA  GLU A 125     -28.270 -82.359   8.300  1.00 38.79           H  
ATOM   1810  HB2 GLU A 125     -30.421 -82.936   9.021  1.00 36.78           H  
ATOM   1811  HB3 GLU A 125     -29.839 -83.337  10.440  1.00 36.78           H  
ATOM   1812  HG2 GLU A 125     -30.782 -81.334  10.780  1.00 47.57           H  
ATOM   1813  HG3 GLU A 125     -29.230 -81.009  10.684  1.00 47.57           H  
ATOM   1814  N   VAL A 126     -27.234 -83.410  11.148  1.00 38.50           N  
ANISOU 1814  N   VAL A 126     4623   3919   6085   -114   -445   1116       N  
ATOM   1815  CA  VAL A 126     -26.262 -83.211  12.213  1.00 28.86           C  
ANISOU 1815  CA  VAL A 126     3377   2747   4840    -62   -407   1117       C  
ATOM   1816  C   VAL A 126     -24.842 -83.296  11.649  1.00 28.73           C  
ANISOU 1816  C   VAL A 126     3405   2679   4834    -10   -395   1001       C  
ATOM   1817  O   VAL A 126     -24.001 -82.429  11.927  1.00 32.55           O  
ANISOU 1817  O   VAL A 126     3877   3224   5268     32   -340    950       O  
ATOM   1818  CB  VAL A 126     -26.474 -84.226  13.368  1.00 37.92           C  
ANISOU 1818  CB  VAL A 126     4489   3886   6033    -81   -453   1236       C  
ATOM   1819  CG1 VAL A 126     -25.391 -84.084  14.431  1.00 26.69           C  
ANISOU 1819  CG1 VAL A 126     3049   2508   4586    -27   -425   1234       C  
ATOM   1820  CG2 VAL A 126     -27.850 -84.028  13.999  1.00 36.52           C  
ANISOU 1820  CG2 VAL A 126     4253   3786   5835   -126   -447   1360       C  
ATOM   1821  H   VAL A 126     -27.773 -84.066  11.286  1.00 46.20           H  
ATOM   1822  HA  VAL A 126     -26.381 -82.320  12.579  1.00 34.63           H  
ATOM   1823  HB  VAL A 126     -26.432 -85.127  13.012  1.00 45.51           H  
ATOM   1824 HG11 VAL A 126     -25.421 -83.185  14.794  1.00 32.03           H  
ATOM   1825 HG12 VAL A 126     -25.553 -84.731  15.135  1.00 32.03           H  
ATOM   1826 HG13 VAL A 126     -24.526 -84.248  14.024  1.00 32.03           H  
ATOM   1827 HG21 VAL A 126     -28.530 -84.165  13.321  1.00 43.82           H  
ATOM   1828 HG22 VAL A 126     -27.963 -84.670  14.717  1.00 43.82           H  
ATOM   1829 HG23 VAL A 126     -27.909 -83.125  14.349  1.00 43.82           H  
ATOM   1830  N   ALA A 127     -24.581 -84.315  10.832  1.00 28.64           N  
ANISOU 1830  N   ALA A 127     3444   2555   4884    -13   -447    959       N  
ATOM   1831  CA  ALA A 127     -23.262 -84.457  10.217  1.00 33.49           C  
ANISOU 1831  CA  ALA A 127     4094   3123   5508     46   -429    850       C  
ATOM   1832  C   ALA A 127     -22.895 -83.222   9.392  1.00 29.97           C  
ANISOU 1832  C   ALA A 127     3661   2733   4993     64   -358    755       C  
ATOM   1833  O   ALA A 127     -21.785 -82.694   9.511  1.00 30.57           O  
ANISOU 1833  O   ALA A 127     3721   2851   5045    110   -310    700       O  
ATOM   1834  CB  ALA A 127     -23.209 -85.702   9.352  1.00 29.10           C  
ANISOU 1834  CB  ALA A 127     3605   2432   5018     46   -494    813       C  
ATOM   1835  H   ALA A 127     -25.142 -84.930  10.620  1.00 34.37           H  
ATOM   1836  HA  ALA A 127     -22.599 -84.554  10.918  1.00 40.19           H  
ATOM   1837  HB1 ALA A 127     -23.880 -85.631   8.655  1.00 34.91           H  
ATOM   1838  HB2 ALA A 127     -22.327 -85.774   8.956  1.00 34.91           H  
ATOM   1839  HB3 ALA A 127     -23.388 -86.478   9.906  1.00 34.91           H  
ATOM   1840  N   TYR A 128     -23.829 -82.764   8.561  1.00 22.57           N  
ANISOU 1840  N   TYR A 128     2752   1798   4028     22   -359    743       N  
ATOM   1841  CA  TYR A 128     -23.591 -81.595   7.723  1.00 20.63           C  
ANISOU 1841  CA  TYR A 128     2525   1598   3715     30   -300    663       C  
ATOM   1842  C   TYR A 128     -23.191 -80.403   8.573  1.00 26.80           C  
ANISOU 1842  C   TYR A 128     3257   2484   4441     50   -239    673       C  
ATOM   1843  O   TYR A 128     -22.188 -79.740   8.294  1.00 23.05           O  
ANISOU 1843  O   TYR A 128     2786   2039   3934     80   -192    604       O  
ATOM   1844  CB  TYR A 128     -24.828 -81.221   6.906  1.00 19.60           C  
ANISOU 1844  CB  TYR A 128     2422   1464   3562    -23   -318    673       C  
ATOM   1845  CG  TYR A 128     -24.710 -79.855   6.256  1.00 29.21           C  
ANISOU 1845  CG  TYR A 128     3652   2742   4705    -18   -258    613       C  
ATOM   1846  CD1 TYR A 128     -24.076 -79.701   5.032  1.00 26.42           C  
ANISOU 1846  CD1 TYR A 128     3356   2357   4326     -5   -236    515       C  
ATOM   1847  CD2 TYR A 128     -25.225 -78.719   6.874  1.00 28.84           C  
ANISOU 1847  CD2 TYR A 128     3566   2783   4611    -24   -222    656       C  
ATOM   1848  CE1 TYR A 128     -23.957 -78.457   4.437  1.00 25.35           C  
ANISOU 1848  CE1 TYR A 128     3234   2276   4124     -7   -186    469       C  
ATOM   1849  CE2 TYR A 128     -25.109 -77.471   6.288  1.00 23.88           C  
ANISOU 1849  CE2 TYR A 128     2957   2199   3918    -21   -176    604       C  
ATOM   1850  CZ  TYR A 128     -24.476 -77.346   5.071  1.00 25.62           C  
ANISOU 1850  CZ  TYR A 128     3230   2385   4118    -18   -160    515       C  
ATOM   1851  OH  TYR A 128     -24.361 -76.106   4.485  1.00 34.27           O  
ANISOU 1851  OH  TYR A 128     4348   3523   5151    -22   -118    473       O  
ATOM   1852  H   TYR A 128     -24.609 -83.113   8.465  1.00 27.09           H  
ATOM   1853  HA  TYR A 128     -22.866 -81.786   7.107  1.00 24.75           H  
ATOM   1854  HB2 TYR A 128     -24.953 -81.878   6.203  1.00 23.52           H  
ATOM   1855  HB3 TYR A 128     -25.601 -81.210   7.491  1.00 23.52           H  
ATOM   1856  HD1 TYR A 128     -23.723 -80.447   4.603  1.00 31.71           H  
ATOM   1857  HD2 TYR A 128     -25.651 -78.800   7.697  1.00 34.61           H  
ATOM   1858  HE1 TYR A 128     -23.529 -78.370   3.616  1.00 30.43           H  
ATOM   1859  HE2 TYR A 128     -25.459 -76.721   6.712  1.00 28.66           H  
ATOM   1860  HH  TYR A 128     -24.718 -75.523   4.974  1.00 41.13           H  
ATOM   1861  N   HIS A 129     -23.977 -80.126   9.608  1.00 34.72           N  
ANISOU 1861  N   HIS A 129     4219   3545   5430     32   -243    763       N  
ATOM   1862  CA  HIS A 129     -23.686 -78.967  10.448  1.00 33.95           C  
ANISOU 1862  CA  HIS A 129     4091   3539   5270     54   -192    769       C  
ATOM   1863  C   HIS A 129     -22.372 -79.118  11.209  1.00 30.14           C  
ANISOU 1863  C   HIS A 129     3587   3070   4795     92   -184    753       C  
ATOM   1864  O   HIS A 129     -21.655 -78.138  11.407  1.00 24.48           O  
ANISOU 1864  O   HIS A 129     2865   2406   4030    110   -146    713       O  
ATOM   1865  CB  HIS A 129     -24.845 -78.675  11.398  1.00 22.00           C  
ANISOU 1865  CB  HIS A 129     2541   2087   3730     38   -192    866       C  
ATOM   1866  CG  HIS A 129     -26.061 -78.147  10.704  1.00 23.39           C  
ANISOU 1866  CG  HIS A 129     2724   2276   3886      9   -188    880       C  
ATOM   1867  ND1 HIS A 129     -26.046 -76.979   9.973  1.00 23.29           N  
ANISOU 1867  ND1 HIS A 129     2742   2287   3821     15   -151    815       N  
ATOM   1868  CD2 HIS A 129     -27.324 -78.627  10.618  1.00 25.66           C  
ANISOU 1868  CD2 HIS A 129     2991   2557   4203    -29   -222    958       C  
ATOM   1869  CE1 HIS A 129     -27.247 -76.760   9.469  1.00 30.10           C  
ANISOU 1869  CE1 HIS A 129     3601   3156   4679    -12   -162    850       C  
ATOM   1870  NE2 HIS A 129     -28.041 -77.746   9.846  1.00 27.85           N  
ANISOU 1870  NE2 HIS A 129     3281   2856   4446    -40   -205    937       N  
ATOM   1871  H   HIS A 129     -24.668 -80.580   9.843  1.00 41.67           H  
ATOM   1872  HA  HIS A 129     -23.592 -78.194   9.869  1.00 40.74           H  
ATOM   1873  HB2 HIS A 129     -25.093 -79.496  11.851  1.00 26.40           H  
ATOM   1874  HB3 HIS A 129     -24.560 -78.012  12.046  1.00 26.40           H  
ATOM   1875  HD1 HIS A 129     -25.360 -76.471   9.862  1.00 27.95           H  
ATOM   1876  HD2 HIS A 129     -27.645 -79.407  11.010  1.00 30.80           H  
ATOM   1877  HE1 HIS A 129     -27.492 -76.035   8.941  1.00 36.12           H  
ATOM   1878  HE2 HIS A 129     -28.873 -77.822   9.642  1.00 33.42           H  
ATOM   1879  N   GLU A 130     -22.043 -80.337  11.630  1.00 27.90           N  
ANISOU 1879  N   GLU A 130     3290   2735   4574    103   -227    788       N  
ATOM   1880  CA  GLU A 130     -20.745 -80.556  12.273  1.00 26.29           C  
ANISOU 1880  CA  GLU A 130     3061   2540   4387    144   -226    775       C  
ATOM   1881  C   GLU A 130     -19.584 -80.317  11.302  1.00 27.91           C  
ANISOU 1881  C   GLU A 130     3278   2728   4597    173   -195    673       C  
ATOM   1882  O   GLU A 130     -18.593 -79.681  11.662  1.00 33.91           O  
ANISOU 1882  O   GLU A 130     4011   3541   5334    194   -169    648       O  
ATOM   1883  CB  GLU A 130     -20.628 -81.964  12.870  1.00 30.09           C  
ANISOU 1883  CB  GLU A 130     3529   2961   4941    154   -285    836       C  
ATOM   1884  CG  GLU A 130     -19.420 -82.124  13.805  1.00 33.35           C  
ANISOU 1884  CG  GLU A 130     3905   3398   5367    195   -292    847       C  
ATOM   1885  CD  GLU A 130     -18.724 -83.469  13.676  1.00 52.78           C  
ANISOU 1885  CD  GLU A 130     6368   5771   7916    231   -338    844       C  
ATOM   1886  OE1 GLU A 130     -18.327 -83.833  12.549  1.00 59.98           O  
ANISOU 1886  OE1 GLU A 130     7310   6620   8862    256   -331    767       O  
ATOM   1887  OE2 GLU A 130     -18.563 -84.156  14.708  1.00 52.50           O  
ANISOU 1887  OE2 GLU A 130     6309   5728   7911    240   -382    920       O  
ATOM   1888  H   GLU A 130     -22.537 -81.037  11.559  1.00 33.47           H  
ATOM   1889  HA  GLU A 130     -20.652 -79.922  13.000  1.00 31.55           H  
ATOM   1890  HB2 GLU A 130     -21.430 -82.156  13.382  1.00 36.10           H  
ATOM   1891  HB3 GLU A 130     -20.535 -82.605  12.149  1.00 36.10           H  
ATOM   1892  HG2 GLU A 130     -18.772 -81.433  13.599  1.00 40.01           H  
ATOM   1893  HG3 GLU A 130     -19.720 -82.031  14.723  1.00 40.01           H  
ATOM   1894  N   LYS A 131     -19.697 -80.828  10.078  1.00 27.78           N  
ANISOU 1894  N   LYS A 131     3303   2643   4608    174   -199    619       N  
ATOM   1895  CA  LYS A 131     -18.609 -80.684   9.106  1.00 31.18           C  
ANISOU 1895  CA  LYS A 131     3744   3064   5038    209   -160    526       C  
ATOM   1896  C   LYS A 131     -18.504 -79.274   8.522  1.00 32.32           C  
ANISOU 1896  C   LYS A 131     3896   3274   5110    188   -104    477       C  
ATOM   1897  O   LYS A 131     -17.404 -78.780   8.280  1.00 26.14           O  
ANISOU 1897  O   LYS A 131     3090   2529   4314    210    -64    430       O  
ATOM   1898  CB  LYS A 131     -18.754 -81.700   7.968  1.00 34.04           C  
ANISOU 1898  CB  LYS A 131     4163   3330   5440    224   -182    476       C  
ATOM   1899  CG  LYS A 131     -17.482 -81.879   7.138  1.00 26.00           C  
ANISOU 1899  CG  LYS A 131     3148   2299   4432    284   -140    388       C  
ATOM   1900  CD  LYS A 131     -17.608 -83.022   6.142  1.00 35.46           C  
ANISOU 1900  CD  LYS A 131     4417   3391   5667    313   -168    337       C  
ATOM   1901  CE  LYS A 131     -16.277 -83.320   5.463  1.00 40.08           C  
ANISOU 1901  CE  LYS A 131     4997   3969   6263    393   -119    255       C  
ATOM   1902  NZ  LYS A 131     -16.358 -84.498   4.553  1.00 49.68           N  
ANISOU 1902  NZ  LYS A 131     6295   5071   7510    436   -148    197       N  
ATOM   1903  H   LYS A 131     -20.383 -81.256   9.786  1.00 33.33           H  
ATOM   1904  HA  LYS A 131     -17.771 -80.872   9.557  1.00 37.41           H  
ATOM   1905  HB2 LYS A 131     -18.986 -82.562   8.346  1.00 40.85           H  
ATOM   1906  HB3 LYS A 131     -19.458 -81.402   7.371  1.00 40.85           H  
ATOM   1907  HG2 LYS A 131     -17.307 -81.063   6.643  1.00 31.20           H  
ATOM   1908  HG3 LYS A 131     -16.740 -82.075   7.732  1.00 31.20           H  
ATOM   1909  HD2 LYS A 131     -17.898 -83.822   6.607  1.00 42.56           H  
ATOM   1910  HD3 LYS A 131     -18.251 -82.780   5.457  1.00 42.56           H  
ATOM   1911  HE2 LYS A 131     -16.008 -82.551   4.938  1.00 48.10           H  
ATOM   1912  HE3 LYS A 131     -15.610 -83.510   6.142  1.00 48.10           H  
ATOM   1913  HZ1 LYS A 131     -16.961 -84.348   3.915  1.00 59.62           H  
ATOM   1914  HZ2 LYS A 131     -15.566 -84.644   4.174  1.00 59.62           H  
ATOM   1915  HZ3 LYS A 131     -16.598 -85.221   5.012  1.00 59.62           H  
ATOM   1916  N   TYR A 132     -19.647 -78.637   8.287  1.00 20.94           N  
ANISOU 1916  N   TYR A 132     2482   1847   3626    145   -103    495       N  
ATOM   1917  CA  TYR A 132     -19.670 -77.300   7.696  1.00 18.09           C  
ANISOU 1917  CA  TYR A 132     2139   1536   3197    123    -59    454       C  
ATOM   1918  C   TYR A 132     -20.372 -76.289   8.597  1.00 18.02           C  
ANISOU 1918  C   TYR A 132     2119   1588   3141    101    -56    506       C  
ATOM   1919  O   TYR A 132     -21.538 -75.963   8.380  1.00 19.15           O  
ANISOU 1919  O   TYR A 132     2283   1732   3260     77    -63    531       O  
ATOM   1920  CB  TYR A 132     -20.337 -77.353   6.326  1.00 18.11           C  
ANISOU 1920  CB  TYR A 132     2200   1496   3186    101    -58    412       C  
ATOM   1921  CG  TYR A 132     -19.731 -78.414   5.442  1.00 20.56           C  
ANISOU 1921  CG  TYR A 132     2539   1739   3535    132    -62    355       C  
ATOM   1922  CD1 TYR A 132     -18.493 -78.219   4.845  1.00 21.28           C  
ANISOU 1922  CD1 TYR A 132     2622   1849   3613    166    -12    288       C  
ATOM   1923  CD2 TYR A 132     -20.385 -79.618   5.219  1.00 21.53           C  
ANISOU 1923  CD2 TYR A 132     2696   1779   3706    130   -118    370       C  
ATOM   1924  CE1 TYR A 132     -17.927 -79.189   4.046  1.00 19.66           C  
ANISOU 1924  CE1 TYR A 132     2446   1586   3437    210     -7    231       C  
ATOM   1925  CE2 TYR A 132     -19.827 -80.594   4.419  1.00 19.88           C  
ANISOU 1925  CE2 TYR A 132     2529   1499   3527    168   -125    309       C  
ATOM   1926  CZ  TYR A 132     -18.597 -80.375   3.836  1.00 23.06           C  
ANISOU 1926  CZ  TYR A 132     2926   1926   3911    215    -65    236       C  
ATOM   1927  OH  TYR A 132     -18.033 -81.341   3.036  1.00 29.61           O  
ANISOU 1927  OH  TYR A 132     3799   2689   4764    268    -63    171       O  
ATOM   1928  H   TYR A 132     -20.426 -78.957   8.460  1.00 25.12           H  
ATOM   1929  HA  TYR A 132     -18.756 -77.000   7.570  1.00 21.70           H  
ATOM   1930  HB2 TYR A 132     -21.279 -77.555   6.439  1.00 21.74           H  
ATOM   1931  HB3 TYR A 132     -20.230 -76.495   5.886  1.00 21.74           H  
ATOM   1932  HD1 TYR A 132     -18.038 -77.420   4.987  1.00 25.53           H  
ATOM   1933  HD2 TYR A 132     -21.213 -79.768   5.613  1.00 25.84           H  
ATOM   1934  HE1 TYR A 132     -17.098 -79.043   3.650  1.00 23.59           H  
ATOM   1935  HE2 TYR A 132     -20.277 -81.395   4.276  1.00 23.86           H  
ATOM   1936  HH  TYR A 132     -18.540 -82.009   2.992  1.00 35.54           H  
ATOM   1937  N   PRO A 133     -19.655 -75.793   9.621  1.00 25.40           N  
ANISOU 1937  N   PRO A 133     3020   2573   4057    114    -48    522       N  
ATOM   1938  CA  PRO A 133     -20.196 -74.799  10.558  1.00 21.82           C  
ANISOU 1938  CA  PRO A 133     2568   2177   3547    106    -43    562       C  
ATOM   1939  C   PRO A 133     -20.622 -73.492   9.887  1.00 16.86           C  
ANISOU 1939  C   PRO A 133     1979   1568   2857     85    -14    527       C  
ATOM   1940  O   PRO A 133     -21.524 -72.826  10.392  1.00 22.88           O  
ANISOU 1940  O   PRO A 133     2755   2359   3577     85    -12    560       O  
ATOM   1941  CB  PRO A 133     -19.043 -74.566  11.549  1.00 26.00           C  
ANISOU 1941  CB  PRO A 133     3066   2744   4069    121    -48    565       C  
ATOM   1942  CG  PRO A 133     -17.839 -75.199  10.937  1.00 24.09           C  
ANISOU 1942  CG  PRO A 133     2797   2476   3879    136    -44    522       C  
ATOM   1943  CD  PRO A 133     -18.321 -76.269  10.028  1.00 18.64           C  
ANISOU 1943  CD  PRO A 133     2124   1721   3238    143    -51    510       C  
ATOM   1944  HA  PRO A 133     -20.954 -75.170  11.036  1.00 26.19           H  
ATOM   1945  HB2 PRO A 133     -18.903 -73.614  11.666  1.00 31.20           H  
ATOM   1946  HB3 PRO A 133     -19.254 -74.987  12.397  1.00 31.20           H  
ATOM   1947  HG2 PRO A 133     -17.344 -74.531  10.438  1.00 28.90           H  
ATOM   1948  HG3 PRO A 133     -17.284 -75.577  11.637  1.00 28.90           H  
ATOM   1949  HD2 PRO A 133     -17.739 -76.345   9.256  1.00 22.37           H  
ATOM   1950  HD3 PRO A 133     -18.393 -77.111  10.505  1.00 22.37           H  
ATOM   1951  N   THR A 134     -19.984 -73.138   8.775  1.00 16.81           N  
ANISOU 1951  N   THR A 134     1993   1550   2846     71      9    464       N  
ATOM   1952  CA  THR A 134     -20.415 -71.999   7.971  1.00 17.14           C  
ANISOU 1952  CA  THR A 134     2078   1599   2835     47     30    434       C  
ATOM   1953  C   THR A 134     -20.410 -72.402   6.503  1.00 19.17           C  
ANISOU 1953  C   THR A 134     2362   1817   3106     33     42    389       C  
ATOM   1954  O   THR A 134     -19.795 -73.401   6.127  1.00 19.83           O  
ANISOU 1954  O   THR A 134     2430   1871   3232     49     42    365       O  
ATOM   1955  CB  THR A 134     -19.503 -70.766   8.157  1.00 21.47           C  
ANISOU 1955  CB  THR A 134     2635   2184   3339     32     48    406       C  
ATOM   1956  OG1 THR A 134     -18.273 -70.954   7.447  1.00 22.98           O  
ANISOU 1956  OG1 THR A 134     2805   2376   3551     24     69    363       O  
ATOM   1957  CG2 THR A 134     -19.205 -70.526   9.629  1.00 16.53           C  
ANISOU 1957  CG2 THR A 134     1988   1592   2699     48     29    440       C  
ATOM   1958  H   THR A 134     -19.294 -73.545   8.463  1.00 20.18           H  
ATOM   1959  HA  THR A 134     -21.320 -71.752   8.219  1.00 20.57           H  
ATOM   1960  HB  THR A 134     -19.954 -69.981   7.809  1.00 25.77           H  
ATOM   1961  HG1 THR A 134     -17.778 -70.283   7.548  1.00 27.58           H  
ATOM   1962 HG21 THR A 134     -18.757 -71.299  10.006  1.00 19.83           H  
ATOM   1963 HG22 THR A 134     -18.633 -69.750   9.729  1.00 19.83           H  
ATOM   1964 HG23 THR A 134     -20.032 -70.373  10.113  1.00 19.83           H  
ATOM   1965  N   ILE A 135     -21.095 -71.621   5.675  1.00 22.45           N  
ANISOU 1965  N   ILE A 135     2821   2229   3480      9     50    374       N  
ATOM   1966  CA  ILE A 135     -21.238 -71.942   4.259  1.00 16.61           C  
ANISOU 1966  CA  ILE A 135     2119   1453   2737     -7     55    333       C  
ATOM   1967  C   ILE A 135     -19.901 -71.779   3.536  1.00 16.88           C  
ANISOU 1967  C   ILE A 135     2154   1500   2759     -8     96    276       C  
ATOM   1968  O   ILE A 135     -19.650 -72.409   2.501  1.00 21.83           O  
ANISOU 1968  O   ILE A 135     2804   2100   3391     -4    109    234       O  
ATOM   1969  CB  ILE A 135     -22.340 -71.065   3.605  1.00 20.81           C  
ANISOU 1969  CB  ILE A 135     2698   1984   3225    -33     47    342       C  
ATOM   1970  CG1 ILE A 135     -22.766 -71.631   2.246  1.00 21.16           C  
ANISOU 1970  CG1 ILE A 135     2787   1984   3268    -52     34    313       C  
ATOM   1971  CG2 ILE A 135     -21.896 -69.609   3.504  1.00 23.98           C  
ANISOU 1971  CG2 ILE A 135     3121   2418   3571    -50     74    324       C  
ATOM   1972  CD1 ILE A 135     -23.702 -72.825   2.361  1.00 18.48           C  
ANISOU 1972  CD1 ILE A 135     2440   1601   2979    -51    -16    348       C  
ATOM   1973  H   ILE A 135     -21.489 -70.894   5.910  1.00 26.94           H  
ATOM   1974  HA  ILE A 135     -21.509 -72.870   4.175  1.00 19.93           H  
ATOM   1975  HB  ILE A 135     -23.116 -71.092   4.187  1.00 24.97           H  
ATOM   1976 HG12 ILE A 135     -23.227 -70.938   1.747  1.00 25.39           H  
ATOM   1977 HG13 ILE A 135     -21.976 -71.917   1.762  1.00 25.39           H  
ATOM   1978 HG21 ILE A 135     -21.093 -69.562   2.962  1.00 28.77           H  
ATOM   1979 HG22 ILE A 135     -22.605 -69.091   3.093  1.00 28.77           H  
ATOM   1980 HG23 ILE A 135     -21.714 -69.273   4.395  1.00 28.77           H  
ATOM   1981 HD11 ILE A 135     -24.504 -72.553   2.835  1.00 22.17           H  
ATOM   1982 HD12 ILE A 135     -23.932 -73.133   1.470  1.00 22.17           H  
ATOM   1983 HD13 ILE A 135     -23.252 -73.532   2.850  1.00 22.17           H  
ATOM   1984  N   TYR A 136     -19.032 -70.948   4.099  1.00 16.78           N  
ANISOU 1984  N   TYR A 136     2115   1532   2730    -15    116    276       N  
ATOM   1985  CA  TYR A 136     -17.729 -70.703   3.498  1.00 18.65           C  
ANISOU 1985  CA  TYR A 136     2334   1795   2957    -23    158    237       C  
ATOM   1986  C   TYR A 136     -16.793 -71.901   3.663  1.00 17.58           C  
ANISOU 1986  C   TYR A 136     2146   1656   2878     20    168    223       C  
ATOM   1987  O   TYR A 136     -15.940 -72.141   2.807  1.00 23.96           O  
ANISOU 1987  O   TYR A 136     2944   2476   3686     32    210    183       O  
ATOM   1988  CB  TYR A 136     -17.107 -69.430   4.073  1.00 17.02           C  
ANISOU 1988  CB  TYR A 136     2115   1633   2720    -54    162    250       C  
ATOM   1989  CG  TYR A 136     -17.950 -68.201   3.811  1.00 23.88           C  
ANISOU 1989  CG  TYR A 136     3045   2496   3533    -88    152    258       C  
ATOM   1990  CD1 TYR A 136     -18.040 -67.651   2.535  1.00 16.80           C  
ANISOU 1990  CD1 TYR A 136     2193   1595   2596   -120    175    234       C  
ATOM   1991  CD2 TYR A 136     -18.667 -67.597   4.835  1.00 16.40           C  
ANISOU 1991  CD2 TYR A 136     2114   1547   2570    -82    120    291       C  
ATOM   1992  CE1 TYR A 136     -18.818 -66.529   2.291  1.00 16.58           C  
ANISOU 1992  CE1 TYR A 136     2223   1556   2521   -147    159    245       C  
ATOM   1993  CE2 TYR A 136     -19.445 -66.480   4.601  1.00 16.22           C  
ANISOU 1993  CE2 TYR A 136     2149   1514   2498   -100    110    297       C  
ATOM   1994  CZ  TYR A 136     -19.517 -65.949   3.326  1.00 16.30           C  
ANISOU 1994  CZ  TYR A 136     2201   1513   2477   -133    127    275       C  
ATOM   1995  OH  TYR A 136     -20.288 -64.835   3.078  1.00 16.18           O  
ANISOU 1995  OH  TYR A 136     2246   1483   2419   -148    111    285       O  
ATOM   1996  H   TYR A 136     -19.173 -70.515   4.828  1.00 20.14           H  
ATOM   1997  HA  TYR A 136     -17.853 -70.562   2.547  1.00 22.38           H  
ATOM   1998  HB2 TYR A 136     -17.012 -69.529   5.034  1.00 20.43           H  
ATOM   1999  HB3 TYR A 136     -16.238 -69.290   3.666  1.00 20.43           H  
ATOM   2000  HD1 TYR A 136     -17.569 -68.041   1.834  1.00 20.16           H  
ATOM   2001  HD2 TYR A 136     -18.622 -67.951   5.694  1.00 19.68           H  
ATOM   2002  HE1 TYR A 136     -18.867 -66.172   1.434  1.00 19.90           H  
ATOM   2003  HE2 TYR A 136     -19.918 -66.086   5.299  1.00 19.46           H  
ATOM   2004  HH  TYR A 136     -20.660 -64.580   3.787  1.00 19.42           H  
ATOM   2005  N   HIS A 137     -16.956 -72.651   4.752  1.00 22.41           N  
ANISOU 2005  N   HIS A 137     2726   2254   3537     48    133    258       N  
ATOM   2006  CA  HIS A 137     -16.238 -73.909   4.920  1.00 27.66           C  
ANISOU 2006  CA  HIS A 137     3349   2899   4263     96    132    250       C  
ATOM   2007  C   HIS A 137     -16.559 -74.814   3.738  1.00 22.79           C  
ANISOU 2007  C   HIS A 137     2778   2226   3654    118    140    206       C  
ATOM   2008  O   HIS A 137     -15.663 -75.355   3.079  1.00 29.60           O  
ANISOU 2008  O   HIS A 137     3628   3086   4531    155    175    161       O  
ATOM   2009  CB  HIS A 137     -16.643 -74.597   6.227  1.00 22.56           C  
ANISOU 2009  CB  HIS A 137     2677   2235   3659    116     82    305       C  
ATOM   2010  CG  HIS A 137     -16.093 -73.940   7.456  1.00 23.83           C  
ANISOU 2010  CG  HIS A 137     2794   2448   3812    107     70    342       C  
ATOM   2011  ND1 HIS A 137     -16.763 -72.945   8.135  1.00 28.72           N  
ANISOU 2011  ND1 HIS A 137     3436   3092   4382     78     55    372       N  
ATOM   2012  CD2 HIS A 137     -14.935 -74.140   8.128  1.00 22.40           C  
ANISOU 2012  CD2 HIS A 137     2552   2297   3663    127     65    353       C  
ATOM   2013  CE1 HIS A 137     -16.040 -72.559   9.171  1.00 22.85           C  
ANISOU 2013  CE1 HIS A 137     2659   2389   3636     77     39    395       C  
ATOM   2014  NE2 HIS A 137     -14.926 -73.269   9.189  1.00 27.15           N  
ANISOU 2014  NE2 HIS A 137     3147   2937   4230    101     41    387       N  
ATOM   2015  H   HIS A 137     -17.478 -72.453   5.406  1.00 26.90           H  
ATOM   2016  HA  HIS A 137     -15.282 -73.743   4.937  1.00 33.20           H  
ATOM   2017  HB2 HIS A 137     -17.610 -74.591   6.296  1.00 27.07           H  
ATOM   2018  HB3 HIS A 137     -16.321 -75.512   6.212  1.00 27.07           H  
ATOM   2019  HD1 HIS A 137     -17.531 -72.624   7.917  1.00 34.46           H  
ATOM   2020  HD2 HIS A 137     -14.270 -74.752   7.911  1.00 26.88           H  
ATOM   2021  HE1 HIS A 137     -16.276 -71.900   9.784  1.00 27.42           H  
ATOM   2022  HE2 HIS A 137     -14.298 -73.197   9.772  1.00 32.58           H  
ATOM   2023  N   LEU A 138     -17.854 -74.954   3.472  1.00 18.14           N  
ANISOU 2023  N   LEU A 138     2243   1595   3053     95    106    219       N  
ATOM   2024  CA  LEU A 138     -18.348 -75.778   2.380  1.00 18.51           C  
ANISOU 2024  CA  LEU A 138     2351   1579   3103    104     95    180       C  
ATOM   2025  C   LEU A 138     -17.805 -75.306   1.038  1.00 19.12           C  
ANISOU 2025  C   LEU A 138     2464   1675   3124    100    149    116       C  
ATOM   2026  O   LEU A 138     -17.274 -76.106   0.256  1.00 22.54           O  
ANISOU 2026  O   LEU A 138     2922   2080   3563    141    170     63       O  
ATOM   2027  CB  LEU A 138     -19.875 -75.735   2.361  1.00 18.18           C  
ANISOU 2027  CB  LEU A 138     2350   1505   3053     64     43    219       C  
ATOM   2028  CG  LEU A 138     -20.552 -76.517   1.238  1.00 22.37           C  
ANISOU 2028  CG  LEU A 138     2952   1965   3581     56     12    186       C  
ATOM   2029  CD1 LEU A 138     -20.179 -77.981   1.330  1.00 19.26           C  
ANISOU 2029  CD1 LEU A 138     2565   1503   3249     99    -16    169       C  
ATOM   2030  CD2 LEU A 138     -22.062 -76.338   1.276  1.00 18.33           C  
ANISOU 2030  CD2 LEU A 138     2462   1436   3066      8    -43    240       C  
ATOM   2031  H   LEU A 138     -18.478 -74.572   3.923  1.00 21.76           H  
ATOM   2032  HA  LEU A 138     -18.069 -76.697   2.518  1.00 22.21           H  
ATOM   2033  HB2 LEU A 138     -20.201 -76.095   3.201  1.00 21.82           H  
ATOM   2034  HB3 LEU A 138     -20.153 -74.810   2.278  1.00 21.82           H  
ATOM   2035  HG  LEU A 138     -20.234 -76.181   0.385  1.00 26.84           H  
ATOM   2036 HD11 LEU A 138     -20.471 -78.327   2.187  1.00 23.11           H  
ATOM   2037 HD12 LEU A 138     -20.616 -78.463   0.611  1.00 23.11           H  
ATOM   2038 HD13 LEU A 138     -19.216 -78.066   1.249  1.00 23.11           H  
ATOM   2039 HD21 LEU A 138     -22.271 -75.397   1.173  1.00 21.99           H  
ATOM   2040 HD22 LEU A 138     -22.458 -76.847   0.551  1.00 21.99           H  
ATOM   2041 HD23 LEU A 138     -22.396 -76.660   2.128  1.00 21.99           H  
ATOM   2042  N   ARG A 139     -17.953 -74.010   0.771  1.00 24.16           N  
ANISOU 2042  N   ARG A 139     3113   2361   3705     55    171    123       N  
ATOM   2043  CA  ARG A 139     -17.395 -73.413  -0.439  1.00 18.71           C  
ANISOU 2043  CA  ARG A 139     2453   1701   2954     42    225     76       C  
ATOM   2044  C   ARG A 139     -15.939 -73.789  -0.605  1.00 19.35           C  
ANISOU 2044  C   ARG A 139     2482   1818   3051     87    284     42       C  
ATOM   2045  O   ARG A 139     -15.543 -74.330  -1.636  1.00 28.90           O  
ANISOU 2045  O   ARG A 139     3725   3018   4239    120    322    -12       O  
ATOM   2046  CB  ARG A 139     -17.474 -71.895  -0.373  1.00 18.25           C  
ANISOU 2046  CB  ARG A 139     2395   1693   2847    -12    238    102       C  
ATOM   2047  CG  ARG A 139     -18.824 -71.313  -0.697  1.00 17.84           C  
ANISOU 2047  CG  ARG A 139     2403   1615   2759    -51    199    123       C  
ATOM   2048  CD  ARG A 139     -19.065 -70.059   0.125  1.00 22.06           C  
ANISOU 2048  CD  ARG A 139     2923   2181   3278    -82    186    167       C  
ATOM   2049  NE  ARG A 139     -19.902 -69.078  -0.563  1.00 28.99           N  
ANISOU 2049  NE  ARG A 139     3859   3053   4101   -121    174    175       N  
ATOM   2050  CZ  ARG A 139     -19.439 -68.150  -1.396  1.00 24.62           C  
ANISOU 2050  CZ  ARG A 139     3337   2525   3494   -156    205    160       C  
ATOM   2051  NH1 ARG A 139     -18.145 -68.077  -1.672  1.00 25.90           N  
ANISOU 2051  NH1 ARG A 139     3467   2726   3647   -160    256    137       N  
ATOM   2052  NH2 ARG A 139     -20.272 -67.295  -1.969  1.00 19.79           N  
ANISOU 2052  NH2 ARG A 139     2781   1900   2837   -188    185    173       N  
ATOM   2053  H   ARG A 139     -18.374 -73.455   1.275  1.00 28.99           H  
ATOM   2054  HA  ARG A 139     -17.889 -73.720  -1.215  1.00 22.45           H  
ATOM   2055  HB2 ARG A 139     -17.242 -71.612   0.526  1.00 21.90           H  
ATOM   2056  HB3 ARG A 139     -16.837 -71.525  -1.004  1.00 21.90           H  
ATOM   2057  HG2 ARG A 139     -18.857 -71.076  -1.637  1.00 21.40           H  
ATOM   2058  HG3 ARG A 139     -19.515 -71.959  -0.485  1.00 21.40           H  
ATOM   2059  HD2 ARG A 139     -19.511 -70.305   0.951  1.00 26.47           H  
ATOM   2060  HD3 ARG A 139     -18.212 -69.641   0.321  1.00 26.47           H  
ATOM   2061  HE  ARG A 139     -20.749 -69.102  -0.420  1.00 34.78           H  
ATOM   2062 HH11 ARG A 139     -17.595 -68.627  -1.304  1.00 31.08           H  
ATOM   2063 HH12 ARG A 139     -17.854 -67.476  -2.214  1.00 31.08           H  
ATOM   2064 HH21 ARG A 139     -21.114 -67.336  -1.800  1.00 23.74           H  
ATOM   2065 HH22 ARG A 139     -19.970 -66.700  -2.512  1.00 23.74           H  
ATOM   2066  N   LYS A 140     -15.143 -73.487   0.414  1.00 19.24           N  
ANISOU 2066  N   LYS A 140     2389   1850   3072     92    291     76       N  
ATOM   2067  CA  LYS A 140     -13.709 -73.715   0.351  1.00 22.11           C  
ANISOU 2067  CA  LYS A 140     2682   2262   3457    131    345     58       C  
ATOM   2068  C   LYS A 140     -13.414 -75.174   0.040  1.00 29.66           C  
ANISOU 2068  C   LYS A 140     3643   3171   4456    211    352     17       C  
ATOM   2069  O   LYS A 140     -12.634 -75.474  -0.869  1.00 30.98           O  
ANISOU 2069  O   LYS A 140     3807   3361   4604    254    415    -31       O  
ATOM   2070  CB  LYS A 140     -13.050 -73.311   1.669  1.00 25.98           C  
ANISOU 2070  CB  LYS A 140     3088   2797   3988    120    325    109       C  
ATOM   2071  CG  LYS A 140     -11.668 -72.714   1.511  1.00 29.61           C  
ANISOU 2071  CG  LYS A 140     3470   3337   4443    111    379    113       C  
ATOM   2072  CD  LYS A 140     -10.618 -73.589   2.166  1.00 32.60           C  
ANISOU 2072  CD  LYS A 140     3758   3734   4894    174    383    122       C  
ATOM   2073  CE  LYS A 140      -9.240 -72.962   2.085  1.00 40.30           C  
ANISOU 2073  CE  LYS A 140     4638   4801   5873    158    430    140       C  
ATOM   2074  NZ  LYS A 140      -8.213 -73.821   2.733  1.00 47.79           N  
ANISOU 2074  NZ  LYS A 140     5488   5772   6898    225    430    156       N  
ATOM   2075  H   LYS A 140     -15.412 -73.147   1.157  1.00 23.09           H  
ATOM   2076  HA  LYS A 140     -13.330 -73.171  -0.357  1.00 26.53           H  
ATOM   2077  HB2 LYS A 140     -13.609 -72.651   2.108  1.00 31.18           H  
ATOM   2078  HB3 LYS A 140     -12.970 -74.098   2.231  1.00 31.18           H  
ATOM   2079  HG2 LYS A 140     -11.456 -72.639   0.567  1.00 35.53           H  
ATOM   2080  HG3 LYS A 140     -11.644 -71.841   1.933  1.00 35.53           H  
ATOM   2081  HD2 LYS A 140     -10.842 -73.710   3.103  1.00 39.12           H  
ATOM   2082  HD3 LYS A 140     -10.588 -74.446   1.715  1.00 39.12           H  
ATOM   2083  HE2 LYS A 140      -8.996 -72.846   1.154  1.00 48.36           H  
ATOM   2084  HE3 LYS A 140      -9.251 -72.105   2.539  1.00 48.36           H  
ATOM   2085  HZ1 LYS A 140      -8.181 -74.614   2.331  1.00 57.35           H  
ATOM   2086  HZ2 LYS A 140      -7.413 -73.435   2.674  1.00 57.35           H  
ATOM   2087  HZ3 LYS A 140      -8.414 -73.939   3.592  1.00 57.35           H  
ATOM   2088  N   LYS A 141     -14.050 -76.079   0.780  1.00 20.44           N  
ANISOU 2088  N   LYS A 141     2487   1936   3342    233    290     36       N  
ATOM   2089  CA  LYS A 141     -13.848 -77.502   0.549  1.00 21.16           C  
ANISOU 2089  CA  LYS A 141     2597   1963   3481    309    281     -1       C  
ATOM   2090  C   LYS A 141     -14.221 -77.899  -0.880  1.00 29.66           C  
ANISOU 2090  C   LYS A 141     3769   2994   4506    325    301    -70       C  
ATOM   2091  O   LYS A 141     -13.518 -78.690  -1.506  1.00 37.86           O  
ANISOU 2091  O   LYS A 141     4820   4015   5550    399    340   -127       O  
ATOM   2092  CB  LYS A 141     -14.645 -78.329   1.558  1.00 20.89           C  
ANISOU 2092  CB  LYS A 141     2571   1859   3509    311    199     44       C  
ATOM   2093  CG  LYS A 141     -14.579 -79.829   1.319  1.00 26.07           C  
ANISOU 2093  CG  LYS A 141     3264   2424   4216    381    172     10       C  
ATOM   2094  CD  LYS A 141     -15.880 -80.351   0.735  1.00 28.29           C  
ANISOU 2094  CD  LYS A 141     3649   2617   4485    350    114     -3       C  
ATOM   2095  CE  LYS A 141     -15.826 -81.850   0.499  1.00 33.19           C  
ANISOU 2095  CE  LYS A 141     4322   3131   5157    414     74    -39       C  
ATOM   2096  NZ  LYS A 141     -17.191 -82.426   0.358  1.00 38.07           N  
ANISOU 2096  NZ  LYS A 141     5022   3656   5786    364    -13    -20       N  
ATOM   2097  H   LYS A 141     -14.599 -75.895   1.416  1.00 24.52           H  
ATOM   2098  HA  LYS A 141     -12.909 -77.707   0.677  1.00 25.40           H  
ATOM   2099  HB2 LYS A 141     -14.298 -78.155   2.447  1.00 25.07           H  
ATOM   2100  HB3 LYS A 141     -15.577 -78.063   1.513  1.00 25.07           H  
ATOM   2101  HG2 LYS A 141     -13.864 -80.023   0.693  1.00 31.28           H  
ATOM   2102  HG3 LYS A 141     -14.420 -80.282   2.163  1.00 31.28           H  
ATOM   2103  HD2 LYS A 141     -16.605 -80.167   1.353  1.00 33.95           H  
ATOM   2104  HD3 LYS A 141     -16.046 -79.916  -0.116  1.00 33.95           H  
ATOM   2105  HE2 LYS A 141     -15.334 -82.028  -0.318  1.00 39.83           H  
ATOM   2106  HE3 LYS A 141     -15.392 -82.278   1.253  1.00 39.83           H  
ATOM   2107  HZ1 LYS A 141     -17.610 -82.051  -0.332  1.00 45.68           H  
ATOM   2108  HZ2 LYS A 141     -17.138 -83.304   0.220  1.00 45.68           H  
ATOM   2109  HZ3 LYS A 141     -17.662 -82.278   1.098  1.00 45.68           H  
ATOM   2110  N   LEU A 142     -15.315 -77.346  -1.398  1.00 24.76           N  
ANISOU 2110  N   LEU A 142     3221   2356   3833    261    275    -67       N  
ATOM   2111  CA  LEU A 142     -15.725 -77.644  -2.771  1.00 23.77           C  
ANISOU 2111  CA  LEU A 142     3195   2188   3647    266    283   -131       C  
ATOM   2112  C   LEU A 142     -14.785 -77.015  -3.799  1.00 24.22           C  
ANISOU 2112  C   LEU A 142     3250   2321   3632    280    378   -176       C  
ATOM   2113  O   LEU A 142     -14.601 -77.565  -4.883  1.00 32.39           O  
ANISOU 2113  O   LEU A 142     4354   3332   4622    324    410   -244       O  
ATOM   2114  CB  LEU A 142     -17.171 -77.202  -3.024  1.00 22.18           C  
ANISOU 2114  CB  LEU A 142     3063   1952   3412    190    221   -105       C  
ATOM   2115  CG  LEU A 142     -18.248 -78.026  -2.307  1.00 21.77           C  
ANISOU 2115  CG  LEU A 142     3029   1819   3424    175    127    -63       C  
ATOM   2116  CD1 LEU A 142     -19.630 -77.414  -2.504  1.00 22.13           C  
ANISOU 2116  CD1 LEU A 142     3116   1854   3439    100     74    -23       C  
ATOM   2117  CD2 LEU A 142     -18.251 -79.485  -2.764  1.00 21.77           C  
ANISOU 2117  CD2 LEU A 142     3096   1722   3455    228     91   -114       C  
ATOM   2118  H   LEU A 142     -15.833 -76.800  -0.982  1.00 29.72           H  
ATOM   2119  HA  LEU A 142     -15.690 -78.605  -2.898  1.00 28.52           H  
ATOM   2120  HB2 LEU A 142     -17.267 -76.282  -2.732  1.00 26.62           H  
ATOM   2121  HB3 LEU A 142     -17.347 -77.260  -3.976  1.00 26.62           H  
ATOM   2122  HG  LEU A 142     -18.059 -78.019  -1.355  1.00 26.13           H  
ATOM   2123 HD11 LEU A 142     -19.831 -77.390  -3.452  1.00 26.56           H  
ATOM   2124 HD12 LEU A 142     -20.285 -77.958  -2.039  1.00 26.56           H  
ATOM   2125 HD13 LEU A 142     -19.630 -76.514  -2.143  1.00 26.56           H  
ATOM   2126 HD21 LEU A 142     -17.385 -79.877  -2.572  1.00 26.13           H  
ATOM   2127 HD22 LEU A 142     -18.945 -79.964  -2.286  1.00 26.13           H  
ATOM   2128 HD23 LEU A 142     -18.424 -79.516  -3.718  1.00 26.13           H  
ATOM   2129  N   VAL A 143     -14.183 -75.877  -3.467  1.00 27.88           N  
ANISOU 2129  N   VAL A 143     3639   2875   4081    242    421   -137       N  
ATOM   2130  CA  VAL A 143     -13.219 -75.259  -4.372  1.00 31.14           C  
ANISOU 2130  CA  VAL A 143     4032   3370   4430    247    513   -164       C  
ATOM   2131  C   VAL A 143     -11.888 -76.016  -4.366  1.00 38.11           C  
ANISOU 2131  C   VAL A 143     4843   4288   5349    340    579   -193       C  
ATOM   2132  O   VAL A 143     -11.268 -76.177  -5.417  1.00 35.94           O  
ANISOU 2132  O   VAL A 143     4587   4048   5020    385    656   -244       O  
ATOM   2133  CB  VAL A 143     -12.996 -73.758  -4.043  1.00 25.17           C  
ANISOU 2133  CB  VAL A 143     3221   2693   3649    166    529   -106       C  
ATOM   2134  CG1 VAL A 143     -11.829 -73.184  -4.847  1.00 22.65           C  
ANISOU 2134  CG1 VAL A 143     2859   2468   3278    167    625   -116       C  
ATOM   2135  CG2 VAL A 143     -14.264 -72.958  -4.325  1.00 23.65           C  
ANISOU 2135  CG2 VAL A 143     3110   2470   3407     90    478    -86       C  
ATOM   2136  H   VAL A 143     -14.313 -75.447  -2.734  1.00 33.46           H  
ATOM   2137  HA  VAL A 143     -13.574 -75.306  -5.273  1.00 37.37           H  
ATOM   2138  HB  VAL A 143     -12.786 -73.668  -3.100  1.00 30.20           H  
ATOM   2139 HG11 VAL A 143     -12.025 -73.272  -5.793  1.00 27.18           H  
ATOM   2140 HG12 VAL A 143     -11.718 -72.248  -4.618  1.00 27.18           H  
ATOM   2141 HG13 VAL A 143     -11.023 -73.677  -4.629  1.00 27.18           H  
ATOM   2142 HG21 VAL A 143     -14.984 -73.303  -3.774  1.00 28.38           H  
ATOM   2143 HG22 VAL A 143     -14.102 -72.025  -4.113  1.00 28.38           H  
ATOM   2144 HG23 VAL A 143     -14.492 -73.049  -5.264  1.00 28.38           H  
ATOM   2145  N   ASP A 144     -11.458 -76.502  -3.201  1.00 39.97           N  
ANISOU 2145  N   ASP A 144     4997   4515   5673    374    550   -160       N  
ATOM   2146  CA  ASP A 144     -10.130 -77.118  -3.089  1.00 36.72           C  
ANISOU 2146  CA  ASP A 144     4498   4148   5306    463    610   -175       C  
ATOM   2147  C   ASP A 144     -10.066 -78.649  -3.211  1.00 41.50           C  
ANISOU 2147  C   ASP A 144     5144   4666   5956    572    596   -230       C  
ATOM   2148  O   ASP A 144      -9.007 -79.195  -3.523  1.00 42.63           O  
ANISOU 2148  O   ASP A 144     5239   4844   6115    665    664   -263       O  
ATOM   2149  CB  ASP A 144      -9.453 -76.682  -1.785  1.00 44.93           C  
ANISOU 2149  CB  ASP A 144     5414   5243   6414    441    590   -103       C  
ATOM   2150  CG  ASP A 144      -9.063 -75.213  -1.794  1.00 51.40           C  
ANISOU 2150  CG  ASP A 144     6180   6159   7192    352    621    -57       C  
ATOM   2151  OD1 ASP A 144      -9.094 -74.591  -2.878  1.00 46.92           O  
ANISOU 2151  OD1 ASP A 144     5653   5627   6545    320    675    -79       O  
ATOM   2152  OD2 ASP A 144      -8.717 -74.681  -0.719  1.00 49.78           O  
ANISOU 2152  OD2 ASP A 144     5897   5988   7029    311    586      3       O  
ATOM   2153  H   ASP A 144     -11.908 -76.488  -2.468  1.00 47.96           H  
ATOM   2154  HA  ASP A 144      -9.587 -76.765  -3.812  1.00 44.06           H  
ATOM   2155  HB2 ASP A 144     -10.065 -76.826  -1.047  1.00 53.92           H  
ATOM   2156  HB3 ASP A 144      -8.647 -77.207  -1.656  1.00 53.92           H  
ATOM   2157  N   SER A 145     -11.178 -79.340  -2.978  1.00 41.74           N  
ANISOU 2157  N   SER A 145     5263   4587   6010    562    509   -237       N  
ATOM   2158  CA  SER A 145     -11.165 -80.805  -2.966  1.00 40.67           C  
ANISOU 2158  CA  SER A 145     5173   4351   5927    655    476   -281       C  
ATOM   2159  C   SER A 145     -11.326 -81.393  -4.365  1.00 45.99           C  
ANISOU 2159  C   SER A 145     5969   4974   6533    709    508   -376       C  
ATOM   2160  O   SER A 145     -12.135 -80.916  -5.156  1.00 42.88           O  
ANISOU 2160  O   SER A 145     5663   4569   6061    646    497   -395       O  
ATOM   2161  CB  SER A 145     -12.272 -81.350  -2.060  1.00 30.61           C  
ANISOU 2161  CB  SER A 145     3938   2978   4714    613    361   -237       C  
ATOM   2162  OG  SER A 145     -12.161 -82.757  -1.921  1.00 39.62           O  
ANISOU 2162  OG  SER A 145     5117   4019   5919    699    321   -267       O  
ATOM   2163  H   SER A 145     -11.948 -78.990  -2.825  1.00 50.09           H  
ATOM   2164  HA  SER A 145     -10.314 -81.108  -2.612  1.00 48.80           H  
ATOM   2165  HB2 SER A 145     -12.195 -80.939  -1.185  1.00 36.73           H  
ATOM   2166  HB3 SER A 145     -13.134 -81.138  -2.452  1.00 36.73           H  
ATOM   2167  HG  SER A 145     -12.773 -83.045  -1.423  1.00 47.55           H  
ATOM   2168  N   THR A 146     -10.554 -82.437  -4.658  1.00 43.93           N  
ANISOU 2168  N   THR A 146     5717   4679   6297    831    543   -435       N  
ATOM   2169  CA  THR A 146     -10.687 -83.169  -5.918  1.00 45.71           C  
ANISOU 2169  CA  THR A 146     6074   4837   6455    900    565   -535       C  
ATOM   2170  C   THR A 146     -11.699 -84.311  -5.796  1.00 46.56           C  
ANISOU 2170  C   THR A 146     6305   4782   6604    904    446   -560       C  
ATOM   2171  O   THR A 146     -12.121 -84.885  -6.801  1.00 46.07           O  
ANISOU 2171  O   THR A 146     6383   4640   6483    933    430   -640       O  
ATOM   2172  CB  THR A 146      -9.339 -83.765  -6.383  1.00 42.40           C  
ANISOU 2172  CB  THR A 146     5615   4459   6035   1048    668   -596       C  
ATOM   2173  OG1 THR A 146      -8.720 -84.472  -5.302  1.00 44.67           O  
ANISOU 2173  OG1 THR A 146     5811   4722   6439   1117    641   -561       O  
ATOM   2174  CG2 THR A 146      -8.407 -82.674  -6.869  1.00 41.29           C  
ANISOU 2174  CG2 THR A 146     5375   4482   5831   1040    793   -581       C  
ATOM   2175  H   THR A 146      -9.940 -82.744  -4.140  1.00 52.72           H  
ATOM   2176  HA  THR A 146     -11.000 -82.561  -6.606  1.00 54.85           H  
ATOM   2177  HB  THR A 146      -9.498 -84.379  -7.118  1.00 50.88           H  
ATOM   2178  HG1 THR A 146      -7.987 -84.797  -5.553  1.00 53.60           H  
ATOM   2179 HG21 THR A 146      -8.234 -82.043  -6.153  1.00 49.55           H  
ATOM   2180 HG22 THR A 146      -7.566 -83.062  -7.158  1.00 49.55           H  
ATOM   2181 HG23 THR A 146      -8.809 -82.202  -7.615  1.00 49.55           H  
ATOM   2182  N   ASP A 147     -12.077 -84.641  -4.563  1.00 43.57           N  
ANISOU 2182  N   ASP A 147     5878   4354   6324    870    360   -488       N  
ATOM   2183  CA  ASP A 147     -13.032 -85.717  -4.312  1.00 33.97           C  
ANISOU 2183  CA  ASP A 147     4762   2985   5160    860    240   -489       C  
ATOM   2184  C   ASP A 147     -14.430 -85.358  -4.808  1.00 41.67           C  
ANISOU 2184  C   ASP A 147     5836   3916   6080    745    169   -481       C  
ATOM   2185  O   ASP A 147     -14.796 -84.183  -4.868  1.00 40.83           O  
ANISOU 2185  O   ASP A 147     5692   3898   5924    658    193   -440       O  
ATOM   2186  CB  ASP A 147     -13.110 -86.034  -2.815  1.00 41.23           C  
ANISOU 2186  CB  ASP A 147     5593   3882   6191    839    171   -396       C  
ATOM   2187  CG  ASP A 147     -11.796 -86.536  -2.247  1.00 53.53           C  
ANISOU 2187  CG  ASP A 147     7055   5466   7816    953    218   -396       C  
ATOM   2188  OD1 ASP A 147     -10.936 -87.000  -3.027  1.00 55.71           O  
ANISOU 2188  OD1 ASP A 147     7356   5741   8071   1068    288   -478       O  
ATOM   2189  OD2 ASP A 147     -11.631 -86.477  -1.011  1.00 53.69           O  
ANISOU 2189  OD2 ASP A 147     6976   5511   7911    932    184   -312       O  
ATOM   2190  H   ASP A 147     -11.793 -84.253  -3.850  1.00 52.29           H  
ATOM   2191  HA  ASP A 147     -12.741 -86.517  -4.777  1.00 40.76           H  
ATOM   2192  HB2 ASP A 147     -13.355 -85.229  -2.334  1.00 49.48           H  
ATOM   2193  HB3 ASP A 147     -13.779 -86.722  -2.673  1.00 49.48           H  
ATOM   2194  N   LYS A 148     -15.209 -86.380  -5.153  1.00 41.80           N  
ANISOU 2194  N   LYS A 148     5980   3792   6110    745     74   -515       N  
ATOM   2195  CA  LYS A 148     -16.599 -86.190  -5.553  1.00 38.32           C  
ANISOU 2195  CA  LYS A 148     5627   3298   5633    634    -14   -496       C  
ATOM   2196  C   LYS A 148     -17.431 -85.757  -4.356  1.00 37.88           C  
ANISOU 2196  C   LYS A 148     5485   3264   5644    531    -80   -376       C  
ATOM   2197  O   LYS A 148     -17.233 -86.244  -3.243  1.00 37.08           O  
ANISOU 2197  O   LYS A 148     5315   3142   5633    549   -111   -318       O  
ATOM   2198  CB  LYS A 148     -17.173 -87.476  -6.158  1.00 32.39           C  
ANISOU 2198  CB  LYS A 148     5034   2382   4890    655   -113   -558       C  
ATOM   2199  CG  LYS A 148     -18.690 -87.443  -6.366  1.00 38.31           C  
ANISOU 2199  CG  LYS A 148     5859   3066   5630    528   -231   -515       C  
ATOM   2200  CD  LYS A 148     -19.139 -88.312  -7.538  1.00 40.75           C  
ANISOU 2200  CD  LYS A 148     6352   3243   5888    542   -303   -609       C  
ATOM   2201  CE  LYS A 148     -19.859 -89.575  -7.102  1.00 41.45           C  
ANISOU 2201  CE  LYS A 148     6513   3167   6067    514   -449   -582       C  
ATOM   2202  NZ  LYS A 148     -21.329 -89.421  -7.279  1.00 49.59           N  
ANISOU 2202  NZ  LYS A 148     7590   4158   7095    373   -567   -520       N  
ATOM   2203  H   LYS A 148     -14.953 -87.201  -5.162  1.00 50.16           H  
ATOM   2204  HA  LYS A 148     -16.645 -85.491  -6.225  1.00 45.98           H  
ATOM   2205  HB2 LYS A 148     -16.760 -87.627  -7.022  1.00 38.87           H  
ATOM   2206  HB3 LYS A 148     -16.972 -88.217  -5.564  1.00 38.87           H  
ATOM   2207  HG2 LYS A 148     -19.126 -87.770  -5.564  1.00 45.97           H  
ATOM   2208  HG3 LYS A 148     -18.964 -86.530  -6.546  1.00 45.97           H  
ATOM   2209  HD2 LYS A 148     -19.745 -87.800  -8.095  1.00 48.90           H  
ATOM   2210  HD3 LYS A 148     -18.360 -88.575  -8.052  1.00 48.90           H  
ATOM   2211  HE2 LYS A 148     -19.561 -90.322  -7.645  1.00 49.74           H  
ATOM   2212  HE3 LYS A 148     -19.678 -89.744  -6.164  1.00 49.74           H  
ATOM   2213  HZ1 LYS A 148     -21.518 -89.265  -8.134  1.00 59.51           H  
ATOM   2214  HZ2 LYS A 148     -21.745 -90.165  -7.022  1.00 59.51           H  
ATOM   2215  HZ3 LYS A 148     -21.624 -88.740  -6.788  1.00 59.51           H  
ATOM   2216  N   ALA A 149     -18.356 -84.833  -4.593  1.00 35.98           N  
ANISOU 2216  N   ALA A 149     5249   3070   5354    430    -98   -337       N  
ATOM   2217  CA  ALA A 149     -19.207 -84.303  -3.537  1.00 32.47           C  
ANISOU 2217  CA  ALA A 149     4723   2659   4956    340   -148   -225       C  
ATOM   2218  C   ALA A 149     -20.671 -84.586  -3.834  1.00 29.12           C  
ANISOU 2218  C   ALA A 149     4375   2156   4533    250   -258   -192       C  
ATOM   2219  O   ALA A 149     -21.075 -84.672  -4.993  1.00 30.72           O  
ANISOU 2219  O   ALA A 149     4686   2315   4671    233   -282   -252       O  
ATOM   2220  CB  ALA A 149     -18.982 -82.814  -3.390  1.00 26.89           C  
ANISOU 2220  CB  ALA A 149     3930   2088   4197    305    -68   -194       C  
ATOM   2221  H   ALA A 149     -18.512 -84.493  -5.367  1.00 43.18           H  
ATOM   2222  HA  ALA A 149     -18.978 -84.730  -2.696  1.00 38.96           H  
ATOM   2223  HB1 ALA A 149     -19.199 -82.378  -4.229  1.00 32.26           H  
ATOM   2224  HB2 ALA A 149     -19.555 -82.476  -2.684  1.00 32.26           H  
ATOM   2225  HB3 ALA A 149     -18.051 -82.656  -3.166  1.00 32.26           H  
ATOM   2226  N   ASP A 150     -21.458 -84.740  -2.776  1.00 27.97           N  
ANISOU 2226  N   ASP A 150     4171   1997   4459    192   -327    -91       N  
ATOM   2227  CA  ASP A 150     -22.897 -84.899  -2.907  1.00 24.83           C  
ANISOU 2227  CA  ASP A 150     3814   1547   4073     96   -430    -33       C  
ATOM   2228  C   ASP A 150     -23.463 -83.700  -3.662  1.00 27.17           C  
ANISOU 2228  C   ASP A 150     4120   1919   4285     40   -403    -37       C  
ATOM   2229  O   ASP A 150     -22.971 -82.582  -3.529  1.00 31.46           O  
ANISOU 2229  O   ASP A 150     4598   2570   4785     53   -315    -35       O  
ATOM   2230  CB  ASP A 150     -23.531 -85.031  -1.518  1.00 23.83           C  
ANISOU 2230  CB  ASP A 150     3591   1434   4028     48   -478     90       C  
ATOM   2231  CG  ASP A 150     -25.029 -85.288  -1.568  1.00 33.96           C  
ANISOU 2231  CG  ASP A 150     4896   2670   5337    -52   -586    167       C  
ATOM   2232  OD1 ASP A 150     -25.654 -85.118  -2.635  1.00 43.20           O  
ANISOU 2232  OD1 ASP A 150     6143   3813   6457    -95   -624    133       O  
ATOM   2233  OD2 ASP A 150     -25.585 -85.662  -0.517  1.00 47.15           O  
ANISOU 2233  OD2 ASP A 150     6501   4335   7079    -90   -635    270       O  
ATOM   2234  H   ASP A 150     -21.178 -84.756  -1.963  1.00 33.57           H  
ATOM   2235  HA  ASP A 150     -23.091 -85.703  -3.413  1.00 29.80           H  
ATOM   2236  HB2 ASP A 150     -23.116 -85.774  -1.052  1.00 28.59           H  
ATOM   2237  HB3 ASP A 150     -23.385 -84.209  -1.026  1.00 28.59           H  
ATOM   2238  N   LEU A 151     -24.489 -83.952  -4.467  1.00 24.23           N  
ANISOU 2238  N   LEU A 151     3833   1482   3891    -23   -489    -39       N  
ATOM   2239  CA  LEU A 151     -25.083 -82.917  -5.306  1.00 23.88           C  
ANISOU 2239  CA  LEU A 151     3813   1495   3767    -76   -480    -44       C  
ATOM   2240  C   LEU A 151     -25.688 -81.790  -4.471  1.00 26.87           C  
ANISOU 2240  C   LEU A 151     4076   1977   4158   -123   -457     57       C  
ATOM   2241  O   LEU A 151     -25.655 -80.620  -4.861  1.00 31.30           O  
ANISOU 2241  O   LEU A 151     4621   2617   4652   -133   -401     49       O  
ATOM   2242  CB  LEU A 151     -26.161 -83.529  -6.203  1.00 24.72           C  
ANISOU 2242  CB  LEU A 151     4027   1504   3860   -143   -599    -50       C  
ATOM   2243  CG  LEU A 151     -26.567 -82.722  -7.437  1.00 28.85           C  
ANISOU 2243  CG  LEU A 151     4620   2058   4282   -181   -598    -89       C  
ATOM   2244  CD1 LEU A 151     -25.382 -82.535  -8.368  1.00 25.18           C  
ANISOU 2244  CD1 LEU A 151     4229   1614   3725   -103   -502   -207       C  
ATOM   2245  CD2 LEU A 151     -27.709 -83.414  -8.163  1.00 30.01           C  
ANISOU 2245  CD2 LEU A 151     4866   2104   4431   -258   -737    -80       C  
ATOM   2246  H   LEU A 151     -24.863 -84.722  -4.547  1.00 29.08           H  
ATOM   2247  HA  LEU A 151     -24.396 -82.536  -5.875  1.00 28.66           H  
ATOM   2248  HB2 LEU A 151     -25.842 -84.390  -6.516  1.00 29.66           H  
ATOM   2249  HB3 LEU A 151     -26.961 -83.659  -5.670  1.00 29.66           H  
ATOM   2250  HG  LEU A 151     -26.874 -81.845  -7.157  1.00 34.61           H  
ATOM   2251 HD11 LEU A 151     -25.062 -83.407  -8.649  1.00 30.22           H  
ATOM   2252 HD12 LEU A 151     -25.666 -82.022  -9.140  1.00 30.22           H  
ATOM   2253 HD13 LEU A 151     -24.681 -82.062  -7.894  1.00 30.22           H  
ATOM   2254 HD21 LEU A 151     -28.467 -83.487  -7.563  1.00 36.01           H  
ATOM   2255 HD22 LEU A 151     -27.952 -82.889  -8.942  1.00 36.01           H  
ATOM   2256 HD23 LEU A 151     -27.418 -84.298  -8.438  1.00 36.01           H  
ATOM   2257  N   ARG A 152     -26.245 -82.152  -3.321  1.00 27.67           N  
ANISOU 2257  N   ARG A 152     4100   2073   4342   -150   -502    152       N  
ATOM   2258  CA  ARG A 152     -26.901 -81.186  -2.450  1.00 24.92           C  
ANISOU 2258  CA  ARG A 152     3646   1818   4005   -185   -483    248       C  
ATOM   2259  C   ARG A 152     -25.910 -80.141  -1.926  1.00 24.28           C  
ANISOU 2259  C   ARG A 152     3500   1837   3890   -132   -371    231       C  
ATOM   2260  O   ARG A 152     -26.212 -78.946  -1.910  1.00 21.57           O  
ANISOU 2260  O   ARG A 152     3121   1570   3503   -150   -334    255       O  
ATOM   2261  CB  ARG A 152     -27.610 -81.914  -1.304  1.00 27.94           C  
ANISOU 2261  CB  ARG A 152     3962   2177   4477   -216   -547    354       C  
ATOM   2262  CG  ARG A 152     -28.842 -82.691  -1.765  1.00 23.37           C  
ANISOU 2262  CG  ARG A 152     3427   1517   3934   -295   -669    402       C  
ATOM   2263  CD  ARG A 152     -29.277 -83.761  -0.771  1.00 31.49           C  
ANISOU 2263  CD  ARG A 152     4412   2495   5058   -324   -739    493       C  
ATOM   2264  NE  ARG A 152     -28.313 -84.854  -0.678  1.00 36.94           N  
ANISOU 2264  NE  ARG A 152     5159   3095   5784   -272   -749    434       N  
ATOM   2265  CZ  ARG A 152     -28.450 -85.909   0.120  1.00 38.43           C  
ANISOU 2265  CZ  ARG A 152     5328   3219   6054   -287   -811    499       C  
ATOM   2266  NH1 ARG A 152     -29.509 -86.022   0.909  1.00 34.96           N  
ANISOU 2266  NH1 ARG A 152     4810   2806   5667   -357   -863    630       N  
ATOM   2267  NH2 ARG A 152     -27.520 -86.854   0.134  1.00 30.55           N  
ANISOU 2267  NH2 ARG A 152     4388   2133   5086   -228   -819    437       N  
ATOM   2268  H   ARG A 152     -26.256 -82.957  -3.021  1.00 33.21           H  
ATOM   2269  HA  ARG A 152     -27.578 -80.716  -2.963  1.00 29.91           H  
ATOM   2270  HB2 ARG A 152     -26.992 -82.544  -0.901  1.00 33.53           H  
ATOM   2271  HB3 ARG A 152     -27.896 -81.263  -0.645  1.00 33.53           H  
ATOM   2272  HG2 ARG A 152     -29.580 -82.073  -1.881  1.00 28.04           H  
ATOM   2273  HG3 ARG A 152     -28.642 -83.129  -2.607  1.00 28.04           H  
ATOM   2274  HD2 ARG A 152     -29.365 -83.361   0.108  1.00 37.79           H  
ATOM   2275  HD3 ARG A 152     -30.127 -84.132  -1.055  1.00 37.79           H  
ATOM   2276  HE  ARG A 152     -27.611 -84.813  -1.172  1.00 44.33           H  
ATOM   2277 HH11 ARG A 152     -30.116 -85.412   0.904  1.00 41.95           H  
ATOM   2278 HH12 ARG A 152     -29.592 -86.706   1.424  1.00 41.95           H  
ATOM   2279 HH21 ARG A 152     -26.829 -86.786  -0.375  1.00 36.66           H  
ATOM   2280 HH22 ARG A 152     -27.606 -87.535   0.651  1.00 36.66           H  
ATOM   2281  N   LEU A 153     -24.721 -80.591  -1.531  1.00 20.96           N  
ANISOU 2281  N   LEU A 153     3066   1410   3490    -68   -323    188       N  
ATOM   2282  CA  LEU A 153     -23.667 -79.690  -1.064  1.00 20.36           C  
ANISOU 2282  CA  LEU A 153     2929   1423   3386    -23   -227    170       C  
ATOM   2283  C   LEU A 153     -23.279 -78.701  -2.169  1.00 23.28           C  
ANISOU 2283  C   LEU A 153     3341   1838   3668    -23   -167    105       C  
ATOM   2284  O   LEU A 153     -23.219 -77.473  -1.949  1.00 20.15           O  
ANISOU 2284  O   LEU A 153     2903   1522   3234    -37   -120    127       O  
ATOM   2285  CB  LEU A 153     -22.443 -80.498  -0.617  1.00 20.75           C  
ANISOU 2285  CB  LEU A 153     2959   1448   3477     47   -197    134       C  
ATOM   2286  CG  LEU A 153     -22.661 -81.514   0.512  1.00 21.36           C  
ANISOU 2286  CG  LEU A 153     2997   1478   3642     52   -255    200       C  
ATOM   2287  CD1 LEU A 153     -21.334 -82.094   0.971  1.00 21.30           C  
ANISOU 2287  CD1 LEU A 153     2960   1462   3670    130   -217    166       C  
ATOM   2288  CD2 LEU A 153     -23.396 -80.900   1.695  1.00 20.25           C  
ANISOU 2288  CD2 LEU A 153     2774   1403   3519     12   -264    304       C  
ATOM   2289  H   LEU A 153     -24.498 -81.422  -1.523  1.00 25.16           H  
ATOM   2290  HA  LEU A 153     -23.992 -79.184  -0.303  1.00 24.44           H  
ATOM   2291  HB2 LEU A 153     -22.108 -80.990  -1.384  1.00 24.90           H  
ATOM   2292  HB3 LEU A 153     -21.763 -79.876  -0.315  1.00 24.90           H  
ATOM   2293  HG  LEU A 153     -23.202 -82.244   0.174  1.00 25.64           H  
ATOM   2294 HD11 LEU A 153     -20.771 -81.374   1.295  1.00 25.56           H  
ATOM   2295 HD12 LEU A 153     -21.499 -82.731   1.684  1.00 25.56           H  
ATOM   2296 HD13 LEU A 153     -20.907 -82.537   0.222  1.00 25.56           H  
ATOM   2297 HD21 LEU A 153     -24.262 -80.581   1.397  1.00 24.30           H  
ATOM   2298 HD22 LEU A 153     -23.510 -81.577   2.381  1.00 24.30           H  
ATOM   2299 HD23 LEU A 153     -22.872 -80.162   2.043  1.00 24.30           H  
ATOM   2300  N   ILE A 154     -23.027 -79.248  -3.357  1.00 20.99           N  
ANISOU 2300  N   ILE A 154     3142   1493   3340     -8   -173     27       N  
ATOM   2301  CA  ILE A 154     -22.699 -78.442  -4.524  1.00 21.08           C  
ANISOU 2301  CA  ILE A 154     3206   1543   3259    -11   -120    -33       C  
ATOM   2302  C   ILE A 154     -23.788 -77.388  -4.684  1.00 25.09           C  
ANISOU 2302  C   ILE A 154     3711   2089   3734    -80   -149     22       C  
ATOM   2303  O   ILE A 154     -23.505 -76.180  -4.741  1.00 23.86           O  
ANISOU 2303  O   ILE A 154     3528   2008   3531    -89    -91     29       O  
ATOM   2304  CB  ILE A 154     -22.568 -79.313  -5.808  1.00 22.13           C  
ANISOU 2304  CB  ILE A 154     3458   1600   3349     10   -141   -121       C  
ATOM   2305  CG1 ILE A 154     -21.437 -80.337  -5.631  1.00 22.80           C  
ANISOU 2305  CG1 ILE A 154     3545   1648   3469     97   -105   -179       C  
ATOM   2306  CG2 ILE A 154     -22.326 -78.436  -7.042  1.00 22.29           C  
ANISOU 2306  CG2 ILE A 154     3537   1669   3261      0    -87   -173       C  
ATOM   2307  CD1 ILE A 154     -21.128 -81.195  -6.857  1.00 25.39           C  
ANISOU 2307  CD1 ILE A 154     3997   1903   3747    142   -110   -280       C  
ATOM   2308  H   ILE A 154     -23.041 -80.094  -3.512  1.00 25.19           H  
ATOM   2309  HA  ILE A 154     -21.855 -77.989  -4.376  1.00 25.29           H  
ATOM   2310  HB  ILE A 154     -23.400 -79.796  -5.935  1.00 26.55           H  
ATOM   2311 HG12 ILE A 154     -20.625 -79.860  -5.398  1.00 27.36           H  
ATOM   2312 HG13 ILE A 154     -21.678 -80.939  -4.909  1.00 27.36           H  
ATOM   2313 HG21 ILE A 154     -21.505 -77.934  -6.916  1.00 26.74           H  
ATOM   2314 HG22 ILE A 154     -22.249 -79.006  -7.823  1.00 26.74           H  
ATOM   2315 HG23 ILE A 154     -23.074 -77.828  -7.148  1.00 26.74           H  
ATOM   2316 HD11 ILE A 154     -20.866 -80.616  -7.590  1.00 30.46           H  
ATOM   2317 HD12 ILE A 154     -20.404 -81.804  -6.642  1.00 30.46           H  
ATOM   2318 HD13 ILE A 154     -21.922 -81.697  -7.099  1.00 30.46           H  
ATOM   2319  N   TYR A 155     -25.038 -77.845  -4.705  1.00 20.68           N  
ANISOU 2319  N   TYR A 155     3174   1477   3205   -129   -242     69       N  
ATOM   2320  CA  TYR A 155     -26.162 -76.930  -4.836  1.00 21.19           C  
ANISOU 2320  CA  TYR A 155     3227   1576   3249   -186   -276    130       C  
ATOM   2321  C   TYR A 155     -26.124 -75.835  -3.782  1.00 27.56           C  
ANISOU 2321  C   TYR A 155     3938   2466   4066   -179   -226    189       C  
ATOM   2322  O   TYR A 155     -26.316 -74.668  -4.101  1.00 22.13           O  
ANISOU 2322  O   TYR A 155     3252   1829   3327   -196   -200    198       O  
ATOM   2323  CB  TYR A 155     -27.509 -77.645  -4.736  1.00 21.04           C  
ANISOU 2323  CB  TYR A 155     3213   1500   3283   -240   -385    194       C  
ATOM   2324  CG  TYR A 155     -28.643 -76.654  -4.651  1.00 21.85           C  
ANISOU 2324  CG  TYR A 155     3273   1653   3376   -285   -411    271       C  
ATOM   2325  CD1 TYR A 155     -29.179 -76.089  -5.800  1.00 21.05           C  
ANISOU 2325  CD1 TYR A 155     3236   1551   3211   -323   -441    255       C  
ATOM   2326  CD2 TYR A 155     -29.152 -76.252  -3.419  1.00 21.57           C  
ANISOU 2326  CD2 TYR A 155     3135   1671   3389   -282   -402    360       C  
ATOM   2327  CE1 TYR A 155     -30.204 -75.165  -5.728  1.00 27.91           C  
ANISOU 2327  CE1 TYR A 155     4063   2466   4076   -355   -466    328       C  
ATOM   2328  CE2 TYR A 155     -30.174 -75.328  -3.337  1.00 19.43           C  
ANISOU 2328  CE2 TYR A 155     2823   1450   3109   -308   -419    428       C  
ATOM   2329  CZ  TYR A 155     -30.694 -74.786  -4.494  1.00 21.36           C  
ANISOU 2329  CZ  TYR A 155     3127   1688   3300   -342   -452    413       C  
ATOM   2330  OH  TYR A 155     -31.713 -73.867  -4.419  1.00 23.36           O  
ANISOU 2330  OH  TYR A 155     3338   1989   3550   -359   -471    484       O  
ATOM   2331  H   TYR A 155     -25.258 -78.674  -4.645  1.00 24.81           H  
ATOM   2332  HA  TYR A 155     -26.116 -76.505  -5.706  1.00 25.43           H  
ATOM   2333  HB2 TYR A 155     -27.641 -78.194  -5.525  1.00 25.25           H  
ATOM   2334  HB3 TYR A 155     -27.523 -78.195  -3.937  1.00 25.25           H  
ATOM   2335  HD1 TYR A 155     -28.847 -76.340  -6.632  1.00 25.26           H  
ATOM   2336  HD2 TYR A 155     -28.799 -76.613  -2.638  1.00 25.88           H  
ATOM   2337  HE1 TYR A 155     -30.558 -74.797  -6.506  1.00 33.50           H  
ATOM   2338  HE2 TYR A 155     -30.508 -75.072  -2.507  1.00 23.32           H  
ATOM   2339  HH  TYR A 155     -31.914 -73.727  -3.616  1.00 28.04           H  
ATOM   2340  N   LEU A 156     -25.901 -76.215  -2.527  1.00 19.14           N  
ANISOU 2340  N   LEU A 156     2799   1411   3063   -154   -217    231       N  
ATOM   2341  CA  LEU A 156     -25.898 -75.247  -1.435  1.00 18.44           C  
ANISOU 2341  CA  LEU A 156     2630   1396   2979   -143   -177    285       C  
ATOM   2342  C   LEU A 156     -24.858 -74.155  -1.662  1.00 18.49           C  
ANISOU 2342  C   LEU A 156     2640   1458   2927   -123    -98    238       C  
ATOM   2343  O   LEU A 156     -25.176 -72.960  -1.577  1.00 17.70           O  
ANISOU 2343  O   LEU A 156     2529   1404   2791   -137    -81    263       O  
ATOM   2344  CB  LEU A 156     -25.671 -75.948  -0.092  1.00 18.35           C  
ANISOU 2344  CB  LEU A 156     2551   1386   3037   -116   -180    329       C  
ATOM   2345  CG  LEU A 156     -26.839 -76.811   0.413  1.00 18.64           C  
ANISOU 2345  CG  LEU A 156     2562   1386   3135   -146   -256    409       C  
ATOM   2346  CD1 LEU A 156     -26.457 -77.609   1.660  1.00 18.69           C  
ANISOU 2346  CD1 LEU A 156     2512   1387   3203   -119   -258    449       C  
ATOM   2347  CD2 LEU A 156     -28.081 -75.970   0.678  1.00 18.37           C  
ANISOU 2347  CD2 LEU A 156     2489   1401   3090   -175   -273    485       C  
ATOM   2348  H   LEU A 156     -25.750 -77.025  -2.281  1.00 22.97           H  
ATOM   2349  HA  LEU A 156     -26.768 -74.820  -1.399  1.00 22.12           H  
ATOM   2350  HB2 LEU A 156     -24.897 -76.527  -0.175  1.00 22.02           H  
ATOM   2351  HB3 LEU A 156     -25.497 -75.272   0.582  1.00 22.02           H  
ATOM   2352  HG  LEU A 156     -27.067 -77.451  -0.280  1.00 22.37           H  
ATOM   2353 HD11 LEU A 156     -26.202 -76.992   2.363  1.00 22.43           H  
ATOM   2354 HD12 LEU A 156     -27.219 -78.137   1.943  1.00 22.43           H  
ATOM   2355 HD13 LEU A 156     -25.712 -78.192   1.445  1.00 22.43           H  
ATOM   2356 HD21 LEU A 156     -28.349 -75.535  -0.147  1.00 22.04           H  
ATOM   2357 HD22 LEU A 156     -28.793 -76.549   0.994  1.00 22.04           H  
ATOM   2358 HD23 LEU A 156     -27.873 -75.304   1.352  1.00 22.04           H  
ATOM   2359  N   ALA A 157     -23.627 -74.553  -1.974  1.00 18.39           N  
ANISOU 2359  N   ALA A 157     2641   1440   2906    -91    -52    173       N  
ATOM   2360  CA  ALA A 157     -22.592 -73.561  -2.254  1.00 19.71           C  
ANISOU 2360  CA  ALA A 157     2803   1664   3020    -82     21    137       C  
ATOM   2361  C   ALA A 157     -23.014 -72.643  -3.406  1.00 22.05           C  
ANISOU 2361  C   ALA A 157     3162   1973   3243   -121     24    122       C  
ATOM   2362  O   ALA A 157     -23.018 -71.403  -3.268  1.00 18.49           O  
ANISOU 2362  O   ALA A 157     2699   1568   2758   -141     47    145       O  
ATOM   2363  CB  ALA A 157     -21.259 -74.244  -2.557  1.00 18.74           C  
ANISOU 2363  CB  ALA A 157     2680   1540   2902    -38     71     74       C  
ATOM   2364  H   ALA A 157     -23.369 -75.372  -2.029  1.00 22.07           H  
ATOM   2365  HA  ALA A 157     -22.468 -73.009  -1.466  1.00 23.65           H  
ATOM   2366  HB1 ALA A 157     -21.368 -74.817  -3.332  1.00 22.49           H  
ATOM   2367  HB2 ALA A 157     -20.591 -73.565  -2.739  1.00 22.49           H  
ATOM   2368  HB3 ALA A 157     -20.994 -74.773  -1.789  1.00 22.49           H  
ATOM   2369  N   LEU A 158     -23.409 -73.248  -4.526  1.00 18.82           N  
ANISOU 2369  N   LEU A 158     2827   1517   2806   -134     -7     85       N  
ATOM   2370  CA  LEU A 158     -23.804 -72.470  -5.699  1.00 19.75           C  
ANISOU 2370  CA  LEU A 158     3013   1644   2847   -173    -10     71       C  
ATOM   2371  C   LEU A 158     -24.965 -71.521  -5.391  1.00 22.39           C  
ANISOU 2371  C   LEU A 158     3332   1993   3183   -209    -54    141       C  
ATOM   2372  O   LEU A 158     -24.984 -70.366  -5.831  1.00 24.99           O  
ANISOU 2372  O   LEU A 158     3682   2356   3458   -231    -34    148       O  
ATOM   2373  CB  LEU A 158     -24.199 -73.398  -6.851  1.00 23.75           C  
ANISOU 2373  CB  LEU A 158     3611   2088   3325   -182    -56     25       C  
ATOM   2374  CG  LEU A 158     -23.141 -74.376  -7.363  1.00 34.98           C  
ANISOU 2374  CG  LEU A 158     5072   3487   4734   -133    -14    -56       C  
ATOM   2375  CD1 LEU A 158     -23.572 -74.993  -8.676  1.00 27.39           C  
ANISOU 2375  CD1 LEU A 158     4226   2468   3714   -147    -58   -110       C  
ATOM   2376  CD2 LEU A 158     -21.828 -73.672  -7.531  1.00 24.92           C  
ANISOU 2376  CD2 LEU A 158     3769   2285   3414   -108     88    -87       C  
ATOM   2377  H   LEU A 158     -23.456 -74.101  -4.631  1.00 22.58           H  
ATOM   2378  HA  LEU A 158     -23.050 -71.935  -5.991  1.00 23.70           H  
ATOM   2379  HB2 LEU A 158     -24.959 -73.927  -6.563  1.00 28.50           H  
ATOM   2380  HB3 LEU A 158     -24.463 -72.846  -7.604  1.00 28.50           H  
ATOM   2381  HG  LEU A 158     -23.023 -75.089  -6.716  1.00 41.98           H  
ATOM   2382 HD11 LEU A 158     -23.695 -74.288  -9.330  1.00 32.87           H  
ATOM   2383 HD12 LEU A 158     -22.884 -75.608  -8.976  1.00 32.87           H  
ATOM   2384 HD13 LEU A 158     -24.406 -75.470  -8.541  1.00 32.87           H  
ATOM   2385 HD21 LEU A 158     -21.549 -73.315  -6.673  1.00 29.90           H  
ATOM   2386 HD22 LEU A 158     -21.169 -74.305  -7.855  1.00 29.90           H  
ATOM   2387 HD23 LEU A 158     -21.937 -72.950  -8.170  1.00 29.90           H  
ATOM   2388  N   ALA A 159     -25.929 -72.016  -4.623  1.00 23.81           N  
ANISOU 2388  N   ALA A 159     3471   2150   3425   -211   -111    196       N  
ATOM   2389  CA  ALA A 159     -27.114 -71.240  -4.293  1.00 20.21           C  
ANISOU 2389  CA  ALA A 159     2990   1713   2978   -232   -150    267       C  
ATOM   2390  C   ALA A 159     -26.727 -70.056  -3.425  1.00 24.56           C  
ANISOU 2390  C   ALA A 159     3495   2318   3519   -211    -99    290       C  
ATOM   2391  O   ALA A 159     -27.190 -68.947  -3.657  1.00 23.61           O  
ANISOU 2391  O   ALA A 159     3389   2217   3363   -223   -102    313       O  
ATOM   2392  CB  ALA A 159     -28.159 -72.099  -3.588  1.00 18.13           C  
ANISOU 2392  CB  ALA A 159     2678   1425   2786   -237   -214    330       C  
ATOM   2393  H   ALA A 159     -25.920 -72.804  -4.279  1.00 28.57           H  
ATOM   2394  HA  ALA A 159     -27.508 -70.898  -5.111  1.00 24.26           H  
ATOM   2395  HB1 ALA A 159     -27.777 -72.452  -2.769  1.00 21.76           H  
ATOM   2396  HB2 ALA A 159     -28.932 -71.551  -3.383  1.00 21.76           H  
ATOM   2397  HB3 ALA A 159     -28.415 -72.828  -4.175  1.00 21.76           H  
ATOM   2398  N   HIS A 160     -25.869 -70.279  -2.434  1.00 19.93           N  
ANISOU 2398  N   HIS A 160     2858   1751   2963   -179    -58    283       N  
ATOM   2399  CA  HIS A 160     -25.403 -69.167  -1.615  1.00 18.88           C  
ANISOU 2399  CA  HIS A 160     2695   1664   2816   -163    -17    297       C  
ATOM   2400  C   HIS A 160     -24.693 -68.123  -2.467  1.00 25.44           C  
ANISOU 2400  C   HIS A 160     3574   2511   3581   -186     19    260       C  
ATOM   2401  O   HIS A 160     -24.910 -66.923  -2.286  1.00 16.69           O  
ANISOU 2401  O   HIS A 160     2476   1419   2445   -193     22    283       O  
ATOM   2402  CB  HIS A 160     -24.489 -69.651  -0.490  1.00 16.67           C  
ANISOU 2402  CB  HIS A 160     2358   1400   2575   -131     12    293       C  
ATOM   2403  CG  HIS A 160     -23.898 -68.541   0.324  1.00 17.59           C  
ANISOU 2403  CG  HIS A 160     2456   1557   2672   -121     45    300       C  
ATOM   2404  ND1 HIS A 160     -22.654 -68.010   0.066  1.00 19.32           N  
ANISOU 2404  ND1 HIS A 160     2682   1797   2863   -134     87    262       N  
ATOM   2405  CD2 HIS A 160     -24.385 -67.856   1.386  1.00 16.10           C  
ANISOU 2405  CD2 HIS A 160     2244   1390   2484   -102     38    342       C  
ATOM   2406  CE1 HIS A 160     -22.395 -67.050   0.936  1.00 16.22           C  
ANISOU 2406  CE1 HIS A 160     2276   1429   2458   -130     94    280       C  
ATOM   2407  NE2 HIS A 160     -23.432 -66.936   1.747  1.00 18.34           N  
ANISOU 2407  NE2 HIS A 160     2533   1696   2739   -106     66    323       N  
ATOM   2408  H   HIS A 160     -25.549 -71.048  -2.219  1.00 23.91           H  
ATOM   2409  HA  HIS A 160     -26.172 -68.740  -1.206  1.00 22.66           H  
ATOM   2410  HB2 HIS A 160     -25.001 -70.217   0.108  1.00 20.00           H  
ATOM   2411  HB3 HIS A 160     -23.757 -70.157  -0.877  1.00 20.00           H  
ATOM   2412  HD1 HIS A 160     -22.126 -68.266  -0.562  1.00 23.19           H  
ATOM   2413  HD2 HIS A 160     -25.210 -67.986   1.795  1.00 19.32           H  
ATOM   2414  HE1 HIS A 160     -21.618 -66.540   0.969  1.00 19.46           H  
ATOM   2415  HE2 HIS A 160     -23.498 -66.377   2.397  1.00 22.00           H  
ATOM   2416  N   MET A 161     -23.851 -68.570  -3.397  1.00 23.13           N  
ANISOU 2416  N   MET A 161     3313   2212   3262   -197     48    206       N  
ATOM   2417  CA  MET A 161     -23.198 -67.622  -4.305  1.00 21.79           C  
ANISOU 2417  CA  MET A 161     3188   2067   3025   -226     86    181       C  
ATOM   2418  C   MET A 161     -24.199 -66.828  -5.149  1.00 23.96           C  
ANISOU 2418  C   MET A 161     3523   2328   3253   -260     47    204       C  
ATOM   2419  O   MET A 161     -24.070 -65.614  -5.291  1.00 18.49           O  
ANISOU 2419  O   MET A 161     2852   1652   2523   -282     58    220       O  
ATOM   2420  CB  MET A 161     -22.220 -68.339  -5.236  1.00 26.02           C  
ANISOU 2420  CB  MET A 161     3747   2607   3533   -223    130    121       C  
ATOM   2421  CG  MET A 161     -20.993 -68.900  -4.543  1.00 19.99           C  
ANISOU 2421  CG  MET A 161     2919   1867   2808   -188    179     99       C  
ATOM   2422  SD  MET A 161     -20.055 -70.023  -5.575  1.00 32.21           S  
ANISOU 2422  SD  MET A 161     4492   3413   4333   -156    228     27       S  
ATOM   2423  CE  MET A 161     -18.943 -70.669  -4.343  1.00 41.75           C  
ANISOU 2423  CE  MET A 161     5603   4644   5618   -106    260     27       C  
ATOM   2424  H   MET A 161     -23.644 -69.395  -3.523  1.00 27.75           H  
ATOM   2425  HA  MET A 161     -22.684 -66.995  -3.772  1.00 26.15           H  
ATOM   2426  HB2 MET A 161     -22.682 -69.078  -5.661  1.00 31.23           H  
ATOM   2427  HB3 MET A 161     -21.917 -67.711  -5.910  1.00 31.23           H  
ATOM   2428  HG2 MET A 161     -20.410 -68.166  -4.293  1.00 23.98           H  
ATOM   2429  HG3 MET A 161     -21.273 -69.385  -3.751  1.00 23.98           H  
ATOM   2430  HE1 MET A 161     -19.462 -71.100  -3.645  1.00 50.10           H  
ATOM   2431  HE2 MET A 161     -18.350 -71.314  -4.760  1.00 50.10           H  
ATOM   2432  HE3 MET A 161     -18.427 -69.938  -3.969  1.00 50.10           H  
ATOM   2433  N   ILE A 162     -25.188 -67.515  -5.715  1.00 17.75           N  
ANISOU 2433  N   ILE A 162     2767   1506   2472   -267     -5    210       N  
ATOM   2434  CA  ILE A 162     -26.178 -66.855  -6.570  1.00 17.94           C  
ANISOU 2434  CA  ILE A 162     2845   1517   2454   -298    -52    236       C  
ATOM   2435  C   ILE A 162     -27.134 -65.948  -5.786  1.00 17.57           C  
ANISOU 2435  C   ILE A 162     2766   1477   2434   -286    -84    300       C  
ATOM   2436  O   ILE A 162     -27.540 -64.896  -6.280  1.00 24.71           O  
ANISOU 2436  O   ILE A 162     3709   2382   3298   -303   -100    322       O  
ATOM   2437  CB  ILE A 162     -26.963 -67.896  -7.413  1.00 23.36           C  
ANISOU 2437  CB  ILE A 162     3574   2162   3139   -316   -113    226       C  
ATOM   2438  CG1 ILE A 162     -26.025 -68.493  -8.461  1.00 26.26           C  
ANISOU 2438  CG1 ILE A 162     4004   2523   3450   -323    -76    153       C  
ATOM   2439  CG2 ILE A 162     -28.180 -67.270  -8.106  1.00 18.62           C  
ANISOU 2439  CG2 ILE A 162     3013   1550   2512   -348   -179    270       C  
ATOM   2440  CD1 ILE A 162     -26.576 -69.692  -9.193  1.00 25.10           C  
ANISOU 2440  CD1 ILE A 162     3913   2324   3301   -333   -135    125       C  
ATOM   2441  H   ILE A 162     -25.310 -68.361  -5.621  1.00 21.30           H  
ATOM   2442  HA  ILE A 162     -25.701 -66.287  -7.195  1.00 21.52           H  
ATOM   2443  HB  ILE A 162     -27.269 -68.606  -6.827  1.00 28.03           H  
ATOM   2444 HG12 ILE A 162     -25.826 -67.812  -9.122  1.00 31.51           H  
ATOM   2445 HG13 ILE A 162     -25.206 -68.769  -8.022  1.00 31.51           H  
ATOM   2446 HG21 ILE A 162     -27.878 -66.561  -8.696  1.00 22.34           H  
ATOM   2447 HG22 ILE A 162     -28.638 -67.954  -8.619  1.00 22.34           H  
ATOM   2448 HG23 ILE A 162     -28.776 -66.908  -7.432  1.00 22.34           H  
ATOM   2449 HD11 ILE A 162     -27.390 -69.433  -9.654  1.00 30.12           H  
ATOM   2450 HD12 ILE A 162     -25.917 -70.001  -9.834  1.00 30.12           H  
ATOM   2451 HD13 ILE A 162     -26.768 -70.393  -8.550  1.00 30.12           H  
ATOM   2452  N   LYS A 163     -27.474 -66.345  -4.565  1.00 22.86           N  
ANISOU 2452  N   LYS A 163     3367   2153   3166   -250    -90    331       N  
ATOM   2453  CA  LYS A 163     -28.387 -65.574  -3.725  1.00 19.13           C  
ANISOU 2453  CA  LYS A 163     2859   1694   2715   -222   -109    390       C  
ATOM   2454  C   LYS A 163     -27.789 -64.208  -3.409  1.00 28.97           C  
ANISOU 2454  C   LYS A 163     4128   2955   3926   -213    -74    383       C  
ATOM   2455  O   LYS A 163     -28.429 -63.174  -3.601  1.00 29.10           O  
ANISOU 2455  O   LYS A 163     4172   2965   3918   -209    -96    412       O  
ATOM   2456  CB  LYS A 163     -28.653 -66.325  -2.419  1.00 26.42           C  
ANISOU 2456  CB  LYS A 163     3705   2631   3702   -184   -108    420       C  
ATOM   2457  CG  LYS A 163     -30.109 -66.378  -1.986  1.00 25.60           C  
ANISOU 2457  CG  LYS A 163     3555   2537   3635   -164   -152    493       C  
ATOM   2458  CD  LYS A 163     -30.264 -67.086  -0.642  1.00 32.37           C  
ANISOU 2458  CD  LYS A 163     4336   3418   4547   -129   -140    530       C  
ATOM   2459  CE  LYS A 163     -29.847 -68.556  -0.691  1.00 28.91           C  
ANISOU 2459  CE  LYS A 163     3883   2954   4148   -152   -153    511       C  
ATOM   2460  NZ  LYS A 163     -30.843 -69.425  -1.376  1.00 31.94           N  
ANISOU 2460  NZ  LYS A 163     4265   3308   4564   -190   -221    545       N  
ATOM   2461  H   LYS A 163     -27.186 -67.065  -4.194  1.00 27.43           H  
ATOM   2462  HA  LYS A 163     -29.229 -65.445  -4.189  1.00 22.95           H  
ATOM   2463  HB2 LYS A 163     -28.346 -67.239  -2.522  1.00 31.70           H  
ATOM   2464  HB3 LYS A 163     -28.154 -65.892  -1.709  1.00 31.70           H  
ATOM   2465  HG2 LYS A 163     -30.451 -65.475  -1.896  1.00 30.72           H  
ATOM   2466  HG3 LYS A 163     -30.623 -66.867  -2.649  1.00 30.72           H  
ATOM   2467  HD2 LYS A 163     -29.709 -66.638   0.015  1.00 38.85           H  
ATOM   2468  HD3 LYS A 163     -31.195 -67.048  -0.371  1.00 38.85           H  
ATOM   2469  HE2 LYS A 163     -29.007 -68.629  -1.170  1.00 34.69           H  
ATOM   2470  HE3 LYS A 163     -29.739 -68.883   0.216  1.00 34.69           H  
ATOM   2471  HZ1 LYS A 163     -30.956 -69.153  -2.216  1.00 38.33           H  
ATOM   2472  HZ2 LYS A 163     -30.559 -70.268  -1.380  1.00 38.33           H  
ATOM   2473  HZ3 LYS A 163     -31.624 -69.385  -0.951  1.00 38.33           H  
ATOM   2474  N   PHE A 164     -26.550 -64.221  -2.925  1.00 25.36           N  
ANISOU 2474  N   PHE A 164     3658   2512   3466   -213    -27    348       N  
ATOM   2475  CA  PHE A 164     -25.850 -63.006  -2.528  1.00 16.60           C  
ANISOU 2475  CA  PHE A 164     2569   1412   2328   -215     -2    342       C  
ATOM   2476  C   PHE A 164     -24.677 -62.788  -3.474  1.00 17.14           C  
ANISOU 2476  C   PHE A 164     2674   1487   2353   -265     32    303       C  
ATOM   2477  O   PHE A 164     -23.518 -62.987  -3.108  1.00 20.81           O  
ANISOU 2477  O   PHE A 164     3109   1973   2824   -272     71    278       O  
ATOM   2478  CB  PHE A 164     -25.387 -63.136  -1.076  1.00 16.33           C  
ANISOU 2478  CB  PHE A 164     2482   1395   2327   -179     18    344       C  
ATOM   2479  CG  PHE A 164     -26.476 -63.590  -0.144  1.00 16.19           C  
ANISOU 2479  CG  PHE A 164     2418   1385   2349   -128     -3    385       C  
ATOM   2480  CD1 PHE A 164     -27.487 -62.722   0.234  1.00 16.25           C  
ANISOU 2480  CD1 PHE A 164     2437   1391   2347    -91    -23    423       C  
ATOM   2481  CD2 PHE A 164     -26.499 -64.888   0.344  1.00 26.34           C  
ANISOU 2481  CD2 PHE A 164     3647   2680   3682   -114     -2    392       C  
ATOM   2482  CE1 PHE A 164     -28.498 -63.137   1.087  1.00 16.26           C  
ANISOU 2482  CE1 PHE A 164     2384   1412   2381    -42    -33    470       C  
ATOM   2483  CE2 PHE A 164     -27.508 -65.309   1.196  1.00 16.09           C  
ANISOU 2483  CE2 PHE A 164     2300   1395   2419    -75    -19    442       C  
ATOM   2484  CZ  PHE A 164     -28.509 -64.431   1.565  1.00 16.18           C  
ANISOU 2484  CZ  PHE A 164     2313   1417   2416    -39    -31    483       C  
ATOM   2485  H   PHE A 164     -26.086 -64.936  -2.816  1.00 30.43           H  
ATOM   2486  HA  PHE A 164     -26.449 -62.246  -2.596  1.00 19.92           H  
ATOM   2487  HB2 PHE A 164     -24.667 -63.784  -1.032  1.00 19.59           H  
ATOM   2488  HB3 PHE A 164     -25.073 -62.271  -0.768  1.00 19.59           H  
ATOM   2489  HD1 PHE A 164     -27.486 -61.849  -0.087  1.00 19.50           H  
ATOM   2490  HD2 PHE A 164     -25.829 -65.483   0.096  1.00 31.61           H  
ATOM   2491  HE1 PHE A 164     -29.170 -62.543   1.334  1.00 19.51           H  
ATOM   2492  HE2 PHE A 164     -27.512 -66.182   1.518  1.00 19.31           H  
ATOM   2493  HZ  PHE A 164     -29.186 -64.710   2.139  1.00 19.41           H  
ATOM   2494  N   ARG A 165     -25.003 -62.383  -4.699  1.00 23.97           N  
ANISOU 2494  N   ARG A 165     3598   2338   3170   -301     17    305       N  
ATOM   2495  CA  ARG A 165     -24.039 -62.334  -5.790  1.00 23.24           C  
ANISOU 2495  CA  ARG A 165     3542   2261   3026   -348     53    274       C  
ATOM   2496  C   ARG A 165     -23.083 -61.147  -5.708  1.00 23.38           C  
ANISOU 2496  C   ARG A 165     3577   2293   3015   -384     80    281       C  
ATOM   2497  O   ARG A 165     -22.055 -61.145  -6.369  1.00 30.00           O  
ANISOU 2497  O   ARG A 165     4420   3161   3819   -422    124    262       O  
ATOM   2498  CB  ARG A 165     -24.782 -62.321  -7.133  1.00 21.21           C  
ANISOU 2498  CB  ARG A 165     3351   1987   2720   -376     21    279       C  
ATOM   2499  CG  ARG A 165     -25.209 -60.940  -7.605  1.00 22.39           C  
ANISOU 2499  CG  ARG A 165     3560   2120   2827   -404     -8    316       C  
ATOM   2500  CD  ARG A 165     -26.685 -60.838  -7.889  1.00 32.93           C  
ANISOU 2500  CD  ARG A 165     4917   3426   4169   -388    -77    353       C  
ATOM   2501  NE  ARG A 165     -27.006 -61.179  -9.271  1.00 35.08           N  
ANISOU 2501  NE  ARG A 165     5249   3693   4389   -426   -101    346       N  
ATOM   2502  CZ  ARG A 165     -27.841 -60.489 -10.044  1.00 25.65           C  
ANISOU 2502  CZ  ARG A 165     4109   2478   3159   -446   -155    383       C  
ATOM   2503  NH1 ARG A 165     -28.460 -59.412  -9.585  1.00 18.96           N  
ANISOU 2503  NH1 ARG A 165     3264   1610   2328   -425   -187    429       N  
ATOM   2504  NH2 ARG A 165     -28.066 -60.884 -11.283  1.00 27.16           N  
ANISOU 2504  NH2 ARG A 165     4358   2666   3294   -483   -180    373       N  
ATOM   2505  H   ARG A 165     -25.792 -62.127  -4.925  1.00 28.76           H  
ATOM   2506  HA  ARG A 165     -23.503 -63.142  -5.762  1.00 27.88           H  
ATOM   2507  HB2 ARG A 165     -24.201 -62.697  -7.812  1.00 25.45           H  
ATOM   2508  HB3 ARG A 165     -25.581 -62.863  -7.050  1.00 25.45           H  
ATOM   2509  HG2 ARG A 165     -24.993 -60.291  -6.917  1.00 26.87           H  
ATOM   2510  HG3 ARG A 165     -24.733 -60.726  -8.422  1.00 26.87           H  
ATOM   2511  HD2 ARG A 165     -27.164 -61.450  -7.308  1.00 39.52           H  
ATOM   2512  HD3 ARG A 165     -26.978 -59.927  -7.727  1.00 39.52           H  
ATOM   2513  HE  ARG A 165     -26.630 -61.874  -9.610  1.00 42.10           H  
ATOM   2514 HH11 ARG A 165     -28.321 -59.147  -8.778  1.00 22.75           H  
ATOM   2515 HH12 ARG A 165     -28.998 -58.975 -10.094  1.00 22.75           H  
ATOM   2516 HH21 ARG A 165     -27.670 -61.582 -11.591  1.00 32.59           H  
ATOM   2517 HH22 ARG A 165     -28.606 -60.440 -11.784  1.00 32.59           H  
ATOM   2518  N   GLY A 166     -23.432 -60.133  -4.922  1.00 23.62           N  
ANISOU 2518  N   GLY A 166     3617   2302   3055   -372     51    309       N  
ATOM   2519  CA  GLY A 166     -22.609 -58.939  -4.814  1.00 19.89           C  
ANISOU 2519  CA  GLY A 166     3173   1827   2558   -415     58    320       C  
ATOM   2520  C   GLY A 166     -22.959 -57.860  -5.825  1.00 18.78           C  
ANISOU 2520  C   GLY A 166     3113   1659   2362   -458     31    347       C  
ATOM   2521  O   GLY A 166     -24.042 -57.884  -6.411  1.00 18.22           O  
ANISOU 2521  O   GLY A 166     3076   1567   2279   -443     -4    363       O  
ATOM   2522  H   GLY A 166     -24.145 -60.114  -4.441  1.00 28.34           H  
ATOM   2523  HA2 GLY A 166     -22.707 -58.564  -3.925  1.00 23.87           H  
ATOM   2524  HA3 GLY A 166     -21.678 -59.182  -4.939  1.00 23.87           H  
ATOM   2525  N   HIS A 167     -22.041 -56.912  -6.023  1.00 25.62           N  
ANISOU 2525  N   HIS A 167     4008   2527   3201   -518     41    360       N  
ATOM   2526  CA  HIS A 167     -22.282 -55.767  -6.904  1.00 28.31           C  
ANISOU 2526  CA  HIS A 167     4431   2835   3490   -566     10    395       C  
ATOM   2527  C   HIS A 167     -21.637 -55.930  -8.280  1.00 30.09           C  
ANISOU 2527  C   HIS A 167     4676   3102   3657   -632     50    399       C  
ATOM   2528  O   HIS A 167     -20.831 -56.833  -8.494  1.00 36.01           O  
ANISOU 2528  O   HIS A 167     5371   3906   4403   -638    110    370       O  
ATOM   2529  CB  HIS A 167     -21.810 -54.464  -6.240  1.00 21.39           C  
ANISOU 2529  CB  HIS A 167     3590   1919   2616   -597    -20    418       C  
ATOM   2530  CG  HIS A 167     -20.323 -54.347  -6.086  1.00 21.85           C  
ANISOU 2530  CG  HIS A 167     3611   2016   2675   -663     17    419       C  
ATOM   2531  ND1 HIS A 167     -19.453 -54.392  -7.155  1.00 30.33           N  
ANISOU 2531  ND1 HIS A 167     4677   3139   3707   -735     63    433       N  
ATOM   2532  CD2 HIS A 167     -19.554 -54.151  -4.988  1.00 32.02           C  
ANISOU 2532  CD2 HIS A 167     4863   3305   3997   -669     13    412       C  
ATOM   2533  CE1 HIS A 167     -18.214 -54.249  -6.721  1.00 29.22           C  
ANISOU 2533  CE1 HIS A 167     4486   3033   3583   -783     88    440       C  
ATOM   2534  NE2 HIS A 167     -18.247 -54.100  -5.409  1.00 33.96           N  
ANISOU 2534  NE2 HIS A 167     5071   3601   4231   -747     53    427       N  
ATOM   2535  H   HIS A 167     -21.264 -56.910  -5.655  1.00 30.75           H  
ATOM   2536  HA  HIS A 167     -23.239 -55.689  -7.043  1.00 33.97           H  
ATOM   2537  HB2 HIS A 167     -22.110 -53.715  -6.779  1.00 25.66           H  
ATOM   2538  HB3 HIS A 167     -22.203 -54.407  -5.355  1.00 25.66           H  
ATOM   2539  HD1 HIS A 167     -19.681 -54.506  -7.976  1.00 36.39           H  
ATOM   2540  HD2 HIS A 167     -19.854 -54.075  -4.111  1.00 38.42           H  
ATOM   2541  HE1 HIS A 167     -17.448 -54.251  -7.250  1.00 35.06           H  
ATOM   2542  HE2 HIS A 167     -17.562 -53.989  -4.901  1.00 40.75           H  
ATOM   2543  N   PHE A 168     -21.990 -55.034  -9.200  1.00 35.16           N  
ANISOU 2543  N   PHE A 168     5395   3717   4246   -676     19    436       N  
ATOM   2544  CA  PHE A 168     -21.509 -55.089 -10.580  1.00 35.77           C  
ANISOU 2544  CA  PHE A 168     5505   3836   4251   -738     55    446       C  
ATOM   2545  C   PHE A 168     -20.825 -53.782 -10.987  1.00 37.54           C  
ANISOU 2545  C   PHE A 168     5778   4050   4435   -823     48    499       C  
ATOM   2546  O   PHE A 168     -20.809 -53.414 -12.161  1.00 41.34           O  
ANISOU 2546  O   PHE A 168     6317   4544   4847   -876     51    530       O  
ATOM   2547  CB  PHE A 168     -22.674 -55.393 -11.528  1.00 28.31           C  
ANISOU 2547  CB  PHE A 168     4617   2873   3268   -719     18    450       C  
ATOM   2548  CG  PHE A 168     -23.244 -56.773 -11.362  1.00 40.62           C  
ANISOU 2548  CG  PHE A 168     6132   4445   4857   -656     23    404       C  
ATOM   2549  CD1 PHE A 168     -22.710 -57.843 -12.061  1.00 37.62           C  
ANISOU 2549  CD1 PHE A 168     5738   4114   4442   -661     78    363       C  
ATOM   2550  CD2 PHE A 168     -24.309 -57.002 -10.507  1.00 46.55           C  
ANISOU 2550  CD2 PHE A 168     6858   5158   5672   -592    -26    404       C  
ATOM   2551  CE1 PHE A 168     -23.225 -59.115 -11.911  1.00 37.22           C  
ANISOU 2551  CE1 PHE A 168     5659   4062   4423   -608     72    322       C  
ATOM   2552  CE2 PHE A 168     -24.831 -58.274 -10.354  1.00 39.17           C  
ANISOU 2552  CE2 PHE A 168     5881   4232   4769   -546    -28    373       C  
ATOM   2553  CZ  PHE A 168     -24.287 -59.332 -11.056  1.00 31.76           C  
ANISOU 2553  CZ  PHE A 168     4939   3330   3799   -557     15    331       C  
ATOM   2554  H   PHE A 168     -22.517 -54.371  -9.046  1.00 42.19           H  
ATOM   2555  HA  PHE A 168     -20.861 -55.806 -10.661  1.00 42.93           H  
ATOM   2556  HB2 PHE A 168     -23.387 -54.756 -11.362  1.00 33.98           H  
ATOM   2557  HB3 PHE A 168     -22.364 -55.308 -12.443  1.00 33.98           H  
ATOM   2558  HD1 PHE A 168     -21.993 -57.703 -12.637  1.00 45.15           H  
ATOM   2559  HD2 PHE A 168     -24.678 -56.293 -10.031  1.00 55.87           H  
ATOM   2560  HE1 PHE A 168     -22.858 -59.825 -12.386  1.00 44.67           H  
ATOM   2561  HE2 PHE A 168     -25.547 -58.418  -9.777  1.00 47.00           H  
ATOM   2562  HZ  PHE A 168     -24.637 -60.187 -10.955  1.00 38.12           H  
ATOM   2563  N   LEU A 169     -20.253 -53.093 -10.005  1.00 32.28           N  
ANISOU 2563  N   LEU A 169     5093   3360   3810   -840     33    511       N  
ATOM   2564  CA  LEU A 169     -19.580 -51.815 -10.228  1.00 28.30           C  
ANISOU 2564  CA  LEU A 169     4638   2834   3283   -929     11    566       C  
ATOM   2565  C   LEU A 169     -18.344 -51.927 -11.121  1.00 36.46           C  
ANISOU 2565  C   LEU A 169     5637   3951   4266  -1014     84    592       C  
ATOM   2566  O   LEU A 169     -18.021 -50.989 -11.851  1.00 51.04           O  
ANISOU 2566  O   LEU A 169     7538   5790   6065  -1098     71    650       O  
ATOM   2567  CB  LEU A 169     -19.177 -51.200  -8.888  1.00 21.95           C  
ANISOU 2567  CB  LEU A 169     3818   1985   2535   -928    -26    566       C  
ATOM   2568  CG  LEU A 169     -20.323 -50.824  -7.947  1.00 23.84           C  
ANISOU 2568  CG  LEU A 169     4104   2141   2814   -845    -95    548       C  
ATOM   2569  CD1 LEU A 169     -19.777 -50.412  -6.591  1.00 21.37           C  
ANISOU 2569  CD1 LEU A 169     3776   1798   2547   -840   -121    535       C  
ATOM   2570  CD2 LEU A 169     -21.191 -49.717  -8.534  1.00 26.02           C  
ANISOU 2570  CD2 LEU A 169     4488   2339   3059   -853   -163    589       C  
ATOM   2571  H   LEU A 169     -20.242 -53.348  -9.184  1.00 38.73           H  
ATOM   2572  HA  LEU A 169     -20.202 -51.207 -10.659  1.00 33.97           H  
ATOM   2573  HB2 LEU A 169     -18.615 -51.836  -8.418  1.00 26.33           H  
ATOM   2574  HB3 LEU A 169     -18.671 -50.391  -9.064  1.00 26.33           H  
ATOM   2575  HG  LEU A 169     -20.887 -51.603  -7.815  1.00 28.61           H  
ATOM   2576 HD11 LEU A 169     -19.191 -49.647  -6.706  1.00 25.65           H  
ATOM   2577 HD12 LEU A 169     -20.517 -50.178  -6.010  1.00 25.65           H  
ATOM   2578 HD13 LEU A 169     -19.280 -51.155  -6.212  1.00 25.65           H  
ATOM   2579 HD21 LEU A 169     -21.567 -50.023  -9.375  1.00 31.22           H  
ATOM   2580 HD22 LEU A 169     -21.903 -49.509  -7.909  1.00 31.22           H  
ATOM   2581 HD23 LEU A 169     -20.642 -48.931  -8.684  1.00 31.22           H  
ATOM   2582  N   ILE A 170     -17.643 -53.055 -11.046  1.00 28.83           N  
ANISOU 2582  N   ILE A 170     4581   3064   3311   -989    160    552       N  
ATOM   2583  CA  ILE A 170     -16.458 -53.272 -11.873  1.00 33.01           C  
ANISOU 2583  CA  ILE A 170     5064   3687   3792  -1051    244    573       C  
ATOM   2584  C   ILE A 170     -16.863 -53.958 -13.175  1.00 44.93           C  
ANISOU 2584  C   ILE A 170     6610   5237   5222  -1032    288    554       C  
ATOM   2585  O   ILE A 170     -17.646 -54.907 -13.164  1.00 40.86           O  
ANISOU 2585  O   ILE A 170     6100   4709   4716   -953    283    498       O  
ATOM   2586  CB  ILE A 170     -15.393 -54.102 -11.128  1.00 34.86           C  
ANISOU 2586  CB  ILE A 170     5177   3988   4079  -1028    307    543       C  
ATOM   2587  CG1 ILE A 170     -15.082 -53.444  -9.776  1.00 27.15           C  
ANISOU 2587  CG1 ILE A 170     4175   2964   3177  -1045    248    558       C  
ATOM   2588  CG2 ILE A 170     -14.133 -54.238 -11.981  1.00 29.25           C  
ANISOU 2588  CG2 ILE A 170     4408   3385   3321  -1087    400    574       C  
ATOM   2589  CD1 ILE A 170     -13.937 -54.086  -8.990  1.00 31.93           C  
ANISOU 2589  CD1 ILE A 170     4660   3635   3838  -1038    295    544       C  
ATOM   2590  H   ILE A 170     -17.832 -53.711 -10.523  1.00 34.60           H  
ATOM   2591  HA  ILE A 170     -16.066 -52.413 -12.096  1.00 39.61           H  
ATOM   2592  HB  ILE A 170     -15.752 -54.988 -10.965  1.00 41.83           H  
ATOM   2593 HG12 ILE A 170     -14.845 -52.517  -9.932  1.00 32.58           H  
ATOM   2594 HG13 ILE A 170     -15.877 -53.488  -9.222  1.00 32.58           H  
ATOM   2595 HG21 ILE A 170     -13.779 -53.354 -12.164  1.00 35.10           H  
ATOM   2596 HG22 ILE A 170     -13.478 -54.763 -11.494  1.00 35.10           H  
ATOM   2597 HG23 ILE A 170     -14.361 -54.683 -12.813  1.00 35.10           H  
ATOM   2598 HD11 ILE A 170     -13.126 -54.039  -9.520  1.00 38.32           H  
ATOM   2599 HD12 ILE A 170     -13.817 -53.604  -8.157  1.00 38.32           H  
ATOM   2600 HD13 ILE A 170     -14.160 -55.012  -8.808  1.00 38.32           H  
ATOM   2601  N   GLU A 171     -16.326 -53.476 -14.293  1.00 99.80           N  
ANISOU 2601  N   GLU A 171    13591  12238  12092  -1107    328    603       N  
ATOM   2602  CA  GLU A 171     -16.829 -53.869 -15.608  1.00 97.23           C  
ANISOU 2602  CA  GLU A 171    13333  11938  11671  -1100    351    593       C  
ATOM   2603  C   GLU A 171     -16.297 -55.202 -16.136  1.00 97.36           C  
ANISOU 2603  C   GLU A 171    13300  12043  11649  -1048    450    533       C  
ATOM   2604  O   GLU A 171     -17.059 -55.991 -16.697  1.00100.05           O  
ANISOU 2604  O   GLU A 171    13692  12372  11951   -994    443    483       O  
ATOM   2605  CB  GLU A 171     -16.556 -52.764 -16.638  1.00102.40           C  
ANISOU 2605  CB  GLU A 171    14056  12608  12242  -1202    349    676       C  
ATOM   2606  CG  GLU A 171     -17.593 -51.640 -16.663  1.00107.82           C  
ANISOU 2606  CG  GLU A 171    14846  13190  12931  -1230    237    723       C  
ATOM   2607  CD  GLU A 171     -19.018 -52.154 -16.783  1.00111.41           C  
ANISOU 2607  CD  GLU A 171    15357  13585  13387  -1151    176    677       C  
ATOM   2608  OE1 GLU A 171     -19.224 -53.189 -17.454  1.00109.35           O  
ANISOU 2608  OE1 GLU A 171    15101  13370  13076  -1110    217    629       O  
ATOM   2609  OE2 GLU A 171     -19.931 -51.526 -16.205  1.00116.18           O  
ANISOU 2609  OE2 GLU A 171    16003  14097  14042  -1127     85    691       O  
ATOM   2610  H   GLU A 171     -15.670 -52.921 -14.318  1.00119.76           H  
ATOM   2611  HA  GLU A 171     -17.793 -53.960 -15.541  1.00116.67           H  
ATOM   2612  HB2 GLU A 171     -15.695 -52.363 -16.441  1.00122.88           H  
ATOM   2613  HB3 GLU A 171     -16.534 -53.163 -17.522  1.00122.88           H  
ATOM   2614  HG2 GLU A 171     -17.527 -51.131 -15.840  1.00129.39           H  
ATOM   2615  HG3 GLU A 171     -17.417 -51.065 -17.424  1.00129.39           H  
ATOM   2616  N   GLY A 172     -15.005 -55.454 -15.955  1.00 74.05           N  
ANISOU 2616  N   GLY A 172    10251   9175   8709  -1062    536    538       N  
ATOM   2617  CA  GLY A 172     -14.360 -56.589 -16.592  1.00 77.68           C  
ANISOU 2617  CA  GLY A 172    10669   9726   9119  -1012    642    488       C  
ATOM   2618  C   GLY A 172     -13.906 -57.664 -15.628  1.00 76.52           C  
ANISOU 2618  C   GLY A 172    10421   9596   9059   -929    677    427       C  
ATOM   2619  O   GLY A 172     -14.092 -57.554 -14.414  1.00 81.11           O  
ANISOU 2619  O   GLY A 172    10961  10122   9737   -914    618    424       O  
ATOM   2620  H   GLY A 172     -14.480 -54.980 -15.466  1.00 88.86           H  
ATOM   2621  HA2 GLY A 172     -14.976 -56.991 -17.223  1.00 93.21           H  
ATOM   2622  HA3 GLY A 172     -13.583 -56.278 -17.083  1.00 93.21           H  
ATOM   2623  N   ASP A 173     -13.320 -58.717 -16.187  1.00 53.43           N  
ANISOU 2623  N   ASP A 173     7462   6746   6092   -870    772    377       N  
ATOM   2624  CA  ASP A 173     -12.668 -59.746 -15.395  1.00 56.84           C  
ANISOU 2624  CA  ASP A 173     7790   7207   6601   -792    818    326       C  
ATOM   2625  C   ASP A 173     -11.621 -59.068 -14.524  1.00 64.63           C  
ANISOU 2625  C   ASP A 173     8663   8235   7660   -847    830    389       C  
ATOM   2626  O   ASP A 173     -10.826 -58.262 -15.007  1.00 76.81           O  
ANISOU 2626  O   ASP A 173    10176   9847   9161   -929    874    460       O  
ATOM   2627  CB  ASP A 173     -12.007 -60.780 -16.309  1.00 62.21           C  
ANISOU 2627  CB  ASP A 173     8455   7973   7208   -725    932    274       C  
ATOM   2628  CG  ASP A 173     -12.175 -62.209 -15.811  1.00 73.94           C  
ANISOU 2628  CG  ASP A 173     9919   9426   8750   -610    937    184       C  
ATOM   2629  OD1 ASP A 173     -13.162 -62.503 -15.102  1.00 74.51           O  
ANISOU 2629  OD1 ASP A 173    10024   9401   8886   -583    844    155       O  
ATOM   2630  OD2 ASP A 173     -11.313 -63.049 -16.146  1.00 74.67           O  
ANISOU 2630  OD2 ASP A 173     9958   9591   8820   -542   1035    144       O  
ATOM   2631  H   ASP A 173     -13.287 -58.858 -17.035  1.00 64.11           H  
ATOM   2632  HA  ASP A 173     -13.315 -60.192 -14.827  1.00 68.21           H  
ATOM   2633  HB2 ASP A 173     -12.406 -60.722 -17.191  1.00 74.65           H  
ATOM   2634  HB3 ASP A 173     -11.056 -60.592 -16.362  1.00 74.65           H  
ATOM   2635  N   LEU A 174     -11.637 -59.395 -13.237  1.00 58.43           N  
ANISOU 2635  N   LEU A 174     7814   7406   6980   -809    785    368       N  
ATOM   2636  CA  LEU A 174     -10.814 -58.710 -12.245  1.00 48.25           C  
ANISOU 2636  CA  LEU A 174     6433   6134   5766   -866    765    425       C  
ATOM   2637  C   LEU A 174      -9.327 -58.697 -12.611  1.00 52.73           C  
ANISOU 2637  C   LEU A 174     6887   6828   6321   -898    867    470       C  
ATOM   2638  O   LEU A 174      -8.764 -59.719 -13.001  1.00 56.92           O  
ANISOU 2638  O   LEU A 174     7360   7430   6836   -822    959    429       O  
ATOM   2639  CB  LEU A 174     -11.013 -59.358 -10.873  1.00 48.75           C  
ANISOU 2639  CB  LEU A 174     6445   6144   5932   -799    715    383       C  
ATOM   2640  CG  LEU A 174     -11.422 -58.400  -9.756  1.00 43.29           C  
ANISOU 2640  CG  LEU A 174     5774   5374   5300   -848    611    418       C  
ATOM   2641  CD1 LEU A 174     -11.927 -59.163  -8.541  1.00 41.71           C  
ANISOU 2641  CD1 LEU A 174     5551   5118   5178   -768    563    368       C  
ATOM   2642  CD2 LEU A 174     -10.244 -57.525  -9.391  1.00 56.32           C  
ANISOU 2642  CD2 LEU A 174     7348   7076   6977   -940    614    490       C  
ATOM   2643  H   LEU A 174     -12.126 -60.022 -12.907  1.00 70.11           H  
ATOM   2644  HA  LEU A 174     -11.109 -57.788 -12.181  1.00 57.90           H  
ATOM   2645  HB2 LEU A 174     -11.706 -60.032 -10.948  1.00 58.50           H  
ATOM   2646  HB3 LEU A 174     -10.180 -59.778 -10.607  1.00 58.50           H  
ATOM   2647  HG  LEU A 174     -12.138 -57.828 -10.073  1.00 51.95           H  
ATOM   2648 HD11 LEU A 174     -11.221 -59.742  -8.216  1.00 50.05           H  
ATOM   2649 HD12 LEU A 174     -12.178 -58.528  -7.852  1.00 50.05           H  
ATOM   2650 HD13 LEU A 174     -12.698 -59.693  -8.800  1.00 50.05           H  
ATOM   2651 HD21 LEU A 174      -9.973 -57.020 -10.174  1.00 67.59           H  
ATOM   2652 HD22 LEU A 174     -10.509 -56.919  -8.682  1.00 67.59           H  
ATOM   2653 HD23 LEU A 174      -9.514 -58.088  -9.090  1.00 67.59           H  
ATOM   2654  N   ASN A 175      -8.711 -57.523 -12.489  1.00 81.40           N  
ANISOU 2654  N   ASN A 175    10487  10483   9960  -1010    847    558       N  
ATOM   2655  CA  ASN A 175      -7.291 -57.333 -12.783  1.00 82.26           C  
ANISOU 2655  CA  ASN A 175    10473  10717  10064  -1063    933    624       C  
ATOM   2656  C   ASN A 175      -6.609 -56.613 -11.611  1.00 83.13           C  
ANISOU 2656  C   ASN A 175    10499  10817  10269  -1140    867    687       C  
ATOM   2657  O   ASN A 175      -7.295 -56.089 -10.735  1.00 88.81           O  
ANISOU 2657  O   ASN A 175    11281  11428  11034  -1161    755    680       O  
ATOM   2658  CB  ASN A 175      -7.152 -56.539 -14.081  1.00 81.74           C  
ANISOU 2658  CB  ASN A 175    10460  10707   9892  -1149    979    690       C  
ATOM   2659  CG  ASN A 175      -7.825 -55.187 -14.010  1.00 84.23           C  
ANISOU 2659  CG  ASN A 175    10880  10925  10197  -1257    869    748       C  
ATOM   2660  OD1 ASN A 175      -7.384 -54.299 -13.285  1.00 72.26           O  
ANISOU 2660  OD1 ASN A 175     9328   9386   8742  -1346    805    813       O  
ATOM   2661  ND2 ASN A 175      -8.902 -55.023 -14.766  1.00 90.69           N  
ANISOU 2661  ND2 ASN A 175    11834  11683  10941  -1247    840    725       N  
ATOM   2662  H   ASN A 175      -9.104 -56.803 -12.232  1.00 97.69           H  
ATOM   2663  HA  ASN A 175      -6.867 -58.197 -12.903  1.00 98.71           H  
ATOM   2664  HB2 ASN A 175      -6.210 -56.397 -14.266  1.00 98.09           H  
ATOM   2665  HB3 ASN A 175      -7.560 -57.041 -14.804  1.00 98.09           H  
ATOM   2666 HD21 ASN A 175      -9.181 -55.667 -15.262  1.00108.83           H  
ATOM   2667 HD22 ASN A 175      -9.321 -54.271 -14.761  1.00108.83           H  
ATOM   2668  N   PRO A 176      -5.263 -56.585 -11.580  1.00 80.36           N  
ANISOU 2668  N   PRO A 176    10006  10582   9946  -1181    932    749       N  
ATOM   2669  CA  PRO A 176      -4.619 -56.047 -10.372  1.00 84.81           C  
ANISOU 2669  CA  PRO A 176    10488  11131  10607  -1248    855    800       C  
ATOM   2670  C   PRO A 176      -4.886 -54.563 -10.093  1.00 87.89           C  
ANISOU 2670  C   PRO A 176    10959  11436  10998  -1384    741    869       C  
ATOM   2671  O   PRO A 176      -4.749 -54.140  -8.945  1.00 96.56           O  
ANISOU 2671  O   PRO A 176    12043  12475  12171  -1422    646    883       O  
ATOM   2672  CB  PRO A 176      -3.127 -56.286 -10.634  1.00 93.91           C  
ANISOU 2672  CB  PRO A 176    11466  12438  11777  -1272    956    866       C  
ATOM   2673  CG  PRO A 176      -3.013 -56.368 -12.109  1.00 98.70           C  
ANISOU 2673  CG  PRO A 176    12092  13134  12276  -1269   1072    881       C  
ATOM   2674  CD  PRO A 176      -4.262 -57.062 -12.551  1.00 87.63           C  
ANISOU 2674  CD  PRO A 176    10828  11652  10815  -1162   1073    775       C  
ATOM   2675  HA  PRO A 176      -4.889 -56.565  -9.597  1.00101.78           H  
ATOM   2676  HB2 PRO A 176      -2.610 -55.540 -10.290  1.00112.69           H  
ATOM   2677  HB3 PRO A 176      -2.849 -57.118 -10.220  1.00112.69           H  
ATOM   2678  HG2 PRO A 176      -2.965 -55.475 -12.485  1.00118.44           H  
ATOM   2679  HG3 PRO A 176      -2.229 -56.886 -12.349  1.00118.44           H  
ATOM   2680  HD2 PRO A 176      -4.503 -56.788 -13.450  1.00105.16           H  
ATOM   2681  HD3 PRO A 176      -4.158 -58.024 -12.486  1.00105.16           H  
ATOM   2682  N   ASP A 177      -5.255 -53.790 -11.110  1.00 51.42           N  
ANISOU 2682  N   ASP A 177     6433   6806   6297  -1454    746    911       N  
ATOM   2683  CA  ASP A 177      -5.587 -52.380 -10.901  1.00 54.77           C  
ANISOU 2683  CA  ASP A 177     6954   7134   6722  -1575    632    974       C  
ATOM   2684  C   ASP A 177      -6.806 -52.236 -10.003  1.00 53.06           C  
ANISOU 2684  C   ASP A 177     6857   6765   6538  -1520    518    904       C  
ATOM   2685  O   ASP A 177      -6.901 -51.294  -9.216  1.00 47.99           O  
ANISOU 2685  O   ASP A 177     6265   6034   5936  -1588    408    933       O  
ATOM   2686  CB  ASP A 177      -5.841 -51.672 -12.234  1.00 65.61           C  
ANISOU 2686  CB  ASP A 177     8412   8522   7996  -1647    661   1031       C  
ATOM   2687  CG  ASP A 177      -4.561 -51.211 -12.903  1.00 72.65           C  
ANISOU 2687  CG  ASP A 177     9197   9544   8864  -1762    733   1145       C  
ATOM   2688  OD1 ASP A 177      -3.494 -51.784 -12.603  1.00 74.92           O  
ANISOU 2688  OD1 ASP A 177     9326   9940   9198  -1748    801   1163       O  
ATOM   2689  OD2 ASP A 177      -4.623 -50.274 -13.728  1.00 74.47           O  
ANISOU 2689  OD2 ASP A 177     9496   9769   9030  -1865    722   1224       O  
ATOM   2690  H   ASP A 177      -5.322 -54.053 -11.926  1.00 61.70           H  
ATOM   2691  HA  ASP A 177      -4.840 -51.942 -10.466  1.00 65.72           H  
ATOM   2692  HB2 ASP A 177      -6.292 -52.284 -12.837  1.00 78.73           H  
ATOM   2693  HB3 ASP A 177      -6.395 -50.891 -12.077  1.00 78.73           H  
ATOM   2694  N   ASN A 178      -7.733 -53.179 -10.118  1.00 46.09           N  
ANISOU 2694  N   ASN A 178     6020   5855   5636  -1395    544    812       N  
ATOM   2695  CA  ASN A 178      -8.967 -53.128  -9.351  1.00 39.24           C  
ANISOU 2695  CA  ASN A 178     5257   4860   4794  -1332    451    750       C  
ATOM   2696  C   ASN A 178      -8.749 -53.220  -7.844  1.00 49.05           C  
ANISOU 2696  C   ASN A 178     6451   6059   6124  -1311    384    728       C  
ATOM   2697  O   ASN A 178      -9.552 -52.699  -7.069  1.00 54.39           O  
ANISOU 2697  O   ASN A 178     7217   6628   6821  -1298    289    706       O  
ATOM   2698  CB  ASN A 178      -9.904 -54.247  -9.794  1.00 37.77           C  
ANISOU 2698  CB  ASN A 178     5108   4667   4576  -1210    497    666       C  
ATOM   2699  CG  ASN A 178     -10.401 -54.067 -11.216  1.00 49.14           C  
ANISOU 2699  CG  ASN A 178     6631   6121   5918  -1227    535    678       C  
ATOM   2700  OD1 ASN A 178     -10.280 -54.969 -12.047  1.00 47.75           O  
ANISOU 2700  OD1 ASN A 178     6432   6017   5693  -1173    625    645       O  
ATOM   2701  ND2 ASN A 178     -10.963 -52.898 -11.506  1.00 48.30           N  
ANISOU 2701  ND2 ASN A 178     6630   5941   5780  -1299    463    725       N  
ATOM   2702  H   ASN A 178      -7.670 -53.862 -10.637  1.00 55.31           H  
ATOM   2703  HA  ASN A 178      -9.409 -52.284  -9.532  1.00 47.09           H  
ATOM   2704  HB2 ASN A 178      -9.431 -55.093  -9.747  1.00 45.32           H  
ATOM   2705  HB3 ASN A 178     -10.675 -54.265  -9.206  1.00 45.32           H  
ATOM   2706 HD21 ASN A 178     -11.030 -52.291 -10.901  1.00 57.96           H  
ATOM   2707 HD22 ASN A 178     -11.261 -52.749 -12.299  1.00 57.96           H  
ATOM   2708  N   SER A 179      -7.669 -53.879  -7.429  1.00 62.11           N  
ANISOU 2708  N   SER A 179     7968   7802   7827  -1301    434    735       N  
ATOM   2709  CA  SER A 179      -7.391 -54.060  -6.008  1.00 58.82           C  
ANISOU 2709  CA  SER A 179     7501   7356   7490  -1280    371    717       C  
ATOM   2710  C   SER A 179      -6.239 -53.170  -5.557  1.00 76.46           C  
ANISOU 2710  C   SER A 179     9670   9617   9762  -1406    322    801       C  
ATOM   2711  O   SER A 179      -5.712 -53.329  -4.455  1.00 84.23           O  
ANISOU 2711  O   SER A 179    10590  10602  10811  -1406    275    800       O  
ATOM   2712  CB  SER A 179      -7.073 -55.524  -5.703  1.00 68.86           C  
ANISOU 2712  CB  SER A 179     8667   8697   8802  -1169    442    663       C  
ATOM   2713  OG  SER A 179      -5.688 -55.789  -5.840  1.00 81.72           O  
ANISOU 2713  OG  SER A 179    10148  10443  10460  -1205    506    713       O  
ATOM   2714  H   SER A 179      -7.083 -54.230  -7.951  1.00 74.53           H  
ATOM   2715  HA  SER A 179      -8.179 -53.812  -5.498  1.00 70.58           H  
ATOM   2716  HB2 SER A 179      -7.342 -55.721  -4.792  1.00 82.64           H  
ATOM   2717  HB3 SER A 179      -7.563 -56.088  -6.322  1.00 82.64           H  
ATOM   2718  HG  SER A 179      -5.531 -56.596  -5.670  1.00 98.07           H  
ATOM   2719  N   ASP A 180      -5.858 -52.226  -6.411  1.00 62.59           N  
ANISOU 2719  N   ASP A 180     7934   7882   7966  -1520    327    879       N  
ATOM   2720  CA  ASP A 180      -4.787 -51.296  -6.092  1.00 66.53           C  
ANISOU 2720  CA  ASP A 180     8376   8401   8499  -1661    272    972       C  
ATOM   2721  C   ASP A 180      -5.362 -50.102  -5.335  1.00 65.31           C  
ANISOU 2721  C   ASP A 180     8361   8100   8354  -1724    126    977       C  
ATOM   2722  O   ASP A 180      -6.112 -49.301  -5.892  1.00 69.86           O  
ANISOU 2722  O   ASP A 180     9067   8596   8880  -1756     90    987       O  
ATOM   2723  CB  ASP A 180      -4.083 -50.841  -7.373  1.00 75.25           C  
ANISOU 2723  CB  ASP A 180     9434   9602   9556  -1761    346   1065       C  
ATOM   2724  CG  ASP A 180      -2.784 -50.099  -7.099  1.00 80.84           C  
ANISOU 2724  CG  ASP A 180    10039  10364  10311  -1909    307   1175       C  
ATOM   2725  OD1 ASP A 180      -2.659 -49.473  -6.026  1.00 84.14           O  
ANISOU 2725  OD1 ASP A 180    10488  10698  10782  -1969    183   1187       O  
ATOM   2726  OD2 ASP A 180      -1.883 -50.145  -7.963  1.00 84.49           O  
ANISOU 2726  OD2 ASP A 180    10391  10958  10754  -1968    400   1254       O  
ATOM   2727  H   ASP A 180      -6.209 -52.105  -7.188  1.00 75.11           H  
ATOM   2728  HA  ASP A 180      -4.136 -51.736  -5.524  1.00 79.83           H  
ATOM   2729  HB2 ASP A 180      -3.875 -51.619  -7.913  1.00 90.30           H  
ATOM   2730  HB3 ASP A 180      -4.671 -50.245  -7.863  1.00 90.30           H  
ATOM   2731  N   VAL A 181      -5.011 -50.002  -4.057  1.00 36.65           N  
ANISOU 2731  N   VAL A 181     4709   4431   4785  -1735     41    968       N  
ATOM   2732  CA  VAL A 181      -5.491 -48.924  -3.195  1.00 39.28           C  
ANISOU 2732  CA  VAL A 181     5179   4620   5124  -1782   -100    961       C  
ATOM   2733  C   VAL A 181      -4.999 -47.562  -3.694  1.00 40.99           C  
ANISOU 2733  C   VAL A 181     5447   4802   5327  -1947   -167   1059       C  
ATOM   2734  O   VAL A 181      -5.747 -46.581  -3.690  1.00 42.53           O  
ANISOU 2734  O   VAL A 181     5797   4869   5491  -1969   -251   1052       O  
ATOM   2735  CB  VAL A 181      -5.057 -49.168  -1.722  1.00 37.06           C  
ANISOU 2735  CB  VAL A 181     4855   4321   4904  -1766   -175    935       C  
ATOM   2736  CG1 VAL A 181      -5.315 -47.947  -0.846  1.00 37.74           C  
ANISOU 2736  CG1 VAL A 181     5084   4265   4991  -1832   -327    936       C  
ATOM   2737  CG2 VAL A 181      -5.783 -50.383  -1.162  1.00 43.01           C  
ANISOU 2737  CG2 VAL A 181     5595   5080   5665  -1602   -129    838       C  
ATOM   2738  H   VAL A 181      -4.487 -50.555  -3.658  1.00 43.98           H  
ATOM   2739  HA  VAL A 181      -6.461 -48.914  -3.220  1.00 47.13           H  
ATOM   2740  HB  VAL A 181      -4.105 -49.354  -1.702  1.00 44.47           H  
ATOM   2741 HG11 VAL A 181      -6.264 -47.745  -0.858  1.00 45.29           H  
ATOM   2742 HG12 VAL A 181      -5.030 -48.144   0.061  1.00 45.29           H  
ATOM   2743 HG13 VAL A 181      -4.812 -47.195  -1.195  1.00 45.29           H  
ATOM   2744 HG21 VAL A 181      -5.559 -51.160  -1.698  1.00 51.61           H  
ATOM   2745 HG22 VAL A 181      -5.502 -50.523  -0.244  1.00 51.61           H  
ATOM   2746 HG23 VAL A 181      -6.739 -50.222  -1.195  1.00 51.61           H  
ATOM   2747  N   ASP A 182      -3.746 -47.519  -4.139  1.00 50.74           N  
ANISOU 2747  N   ASP A 182     6545   6151   6584  -2051   -125   1150       N  
ATOM   2748  CA  ASP A 182      -3.126 -46.286  -4.623  1.00 62.19           C  
ANISOU 2748  CA  ASP A 182     8014   7594   8023  -2150   -179   1220       C  
ATOM   2749  C   ASP A 182      -3.935 -45.657  -5.756  1.00 57.84           C  
ANISOU 2749  C   ASP A 182     7583   6995   7400  -2147   -161   1225       C  
ATOM   2750  O   ASP A 182      -4.366 -44.501  -5.672  1.00 56.39           O  
ANISOU 2750  O   ASP A 182     7533   6695   7199  -2173   -266   1223       O  
ATOM   2751  CB  ASP A 182      -1.707 -46.581  -5.122  1.00 65.69           C  
ANISOU 2751  CB  ASP A 182     8266   8200   8494  -2216    -99   1304       C  
ATOM   2752  CG  ASP A 182      -0.668 -45.656  -4.517  1.00 74.24           C  
ANISOU 2752  CG  ASP A 182     9312   9273   9623  -2318   -210   1364       C  
ATOM   2753  OD1 ASP A 182      -0.654 -44.456  -4.870  1.00 77.82           O  
ANISOU 2753  OD1 ASP A 182     9855   9662  10051  -2390   -284   1403       O  
ATOM   2754  OD2 ASP A 182       0.147 -46.132  -3.697  1.00 70.43           O  
ANISOU 2754  OD2 ASP A 182     8710   8847   9202  -2328   -226   1376       O  
ATOM   2755  H   ASP A 182      -3.225 -48.202  -4.172  1.00 60.89           H  
ATOM   2756  HA  ASP A 182      -3.069 -45.647  -3.896  1.00 74.63           H  
ATOM   2757  HB2 ASP A 182      -1.472 -47.492  -4.885  1.00 78.83           H  
ATOM   2758  HB3 ASP A 182      -1.682 -46.471  -6.086  1.00 78.83           H  
ATOM   2759  N   LYS A 183      -4.133 -46.434  -6.815  1.00 52.13           N  
ANISOU 2759  N   LYS A 183     6812   6363   6631  -2110    -29   1231       N  
ATOM   2760  CA  LYS A 183      -4.816 -45.958  -8.010  1.00 51.87           C  
ANISOU 2760  CA  LYS A 183     6878   6307   6523  -2110     -1   1244       C  
ATOM   2761  C   LYS A 183      -6.243 -45.503  -7.725  1.00 47.85           C  
ANISOU 2761  C   LYS A 183     6550   5640   5990  -2043    -86   1175       C  
ATOM   2762  O   LYS A 183      -6.688 -44.475  -8.236  1.00 54.14           O  
ANISOU 2762  O   LYS A 183     7456   6363   6752  -2067   -145   1194       O  
ATOM   2763  CB  LYS A 183      -4.817 -47.048  -9.086  1.00 41.90           C  
ANISOU 2763  CB  LYS A 183     5539   5174   5208  -2069    157   1248       C  
ATOM   2764  CG  LYS A 183      -3.424 -47.410  -9.571  1.00 54.00           C  
ANISOU 2764  CG  LYS A 183     6891   6874   6751  -2120    258   1321       C  
ATOM   2765  CD  LYS A 183      -3.438 -48.007 -10.969  1.00 60.65           C  
ANISOU 2765  CD  LYS A 183     7701   7835   7509  -2094    405   1339       C  
ATOM   2766  CE  LYS A 183      -2.023 -48.228 -11.491  1.00 58.16           C  
ANISOU 2766  CE  LYS A 183     7208   7688   7201  -2135    507   1416       C  
ATOM   2767  NZ  LYS A 183      -2.005 -48.710 -12.900  1.00 57.64           N  
ANISOU 2767  NZ  LYS A 183     7123   7739   7037  -2106    653   1433       N  
ATOM   2768  H   LYS A 183      -3.878 -47.254  -6.866  1.00 62.55           H  
ATOM   2769  HA  LYS A 183      -4.330 -45.196  -8.363  1.00 62.24           H  
ATOM   2770  HB2 LYS A 183      -5.224 -47.849  -8.721  1.00 50.28           H  
ATOM   2771  HB3 LYS A 183      -5.328 -46.736  -9.849  1.00 50.28           H  
ATOM   2772  HG2 LYS A 183      -2.876 -46.609  -9.591  1.00 64.80           H  
ATOM   2773  HG3 LYS A 183      -3.037 -48.063  -8.967  1.00 64.80           H  
ATOM   2774  HD2 LYS A 183      -3.892 -48.864 -10.948  1.00 72.78           H  
ATOM   2775  HD3 LYS A 183      -3.894 -47.400 -11.573  1.00 72.78           H  
ATOM   2776  HE2 LYS A 183      -1.537 -47.389 -11.453  1.00 69.79           H  
ATOM   2777  HE3 LYS A 183      -1.582 -48.893 -10.939  1.00 69.79           H  
ATOM   2778  HZ1 LYS A 183      -2.399 -48.114 -13.431  1.00 69.17           H  
ATOM   2779  HZ2 LYS A 183      -1.166 -48.828 -13.171  1.00 69.17           H  
ATOM   2780  HZ3 LYS A 183      -2.440 -49.484 -12.962  1.00 69.17           H  
ATOM   2781  N   LEU A 184      -6.959 -46.257  -6.900  1.00 32.52           N  
ANISOU 2781  N   LEU A 184     4638   3650   4070  -1956    -92   1099       N  
ATOM   2782  CA  LEU A 184      -8.347 -45.926  -6.617  1.00 29.38           C  
ANISOU 2782  CA  LEU A 184     4399   3115   3651  -1876   -160   1034       C  
ATOM   2783  C   LEU A 184      -8.441 -44.720  -5.693  1.00 32.30           C  
ANISOU 2783  C   LEU A 184     4867   3359   4047  -1892   -302   1021       C  
ATOM   2784  O   LEU A 184      -9.353 -43.899  -5.826  1.00 34.21           O  
ANISOU 2784  O   LEU A 184     5243   3496   4260  -1856   -368    999       O  
ATOM   2785  CB  LEU A 184      -9.078 -47.138  -6.048  1.00 27.96           C  
ANISOU 2785  CB  LEU A 184     4196   2943   3484  -1727   -114    936       C  
ATOM   2786  CG  LEU A 184      -9.529 -48.080  -7.167  1.00 27.51           C  
ANISOU 2786  CG  LEU A 184     4106   2969   3377  -1651      3    910       C  
ATOM   2787  CD1 LEU A 184      -9.788 -49.461  -6.642  1.00 31.68           C  
ANISOU 2787  CD1 LEU A 184     4557   3546   3932  -1518     64    825       C  
ATOM   2788  CD2 LEU A 184     -10.773 -47.541  -7.844  1.00 27.22           C  
ANISOU 2788  CD2 LEU A 184     4213   2845   3287  -1622    -29    900       C  
ATOM   2789  H   LEU A 184      -6.668 -46.958  -6.497  1.00 39.03           H  
ATOM   2790  HA  LEU A 184      -8.783 -45.689  -7.451  1.00 35.26           H  
ATOM   2791  HB2 LEU A 184      -8.482 -47.627  -5.459  1.00 33.55           H  
ATOM   2792  HB3 LEU A 184      -9.864 -46.842  -5.563  1.00 33.55           H  
ATOM   2793  HG  LEU A 184      -8.827 -48.139  -7.833  1.00 33.01           H  
ATOM   2794 HD11 LEU A 184     -10.486 -49.417  -5.970  1.00 38.01           H  
ATOM   2795 HD12 LEU A 184     -10.071 -50.029  -7.376  1.00 38.01           H  
ATOM   2796 HD13 LEU A 184      -8.972 -49.808  -6.251  1.00 38.01           H  
ATOM   2797 HD21 LEU A 184     -10.575 -46.670  -8.221  1.00 32.67           H  
ATOM   2798 HD22 LEU A 184     -11.040 -48.153  -8.548  1.00 32.67           H  
ATOM   2799 HD23 LEU A 184     -11.482 -47.464  -7.187  1.00 32.67           H  
ATOM   2800  N   PHE A 185      -7.492 -44.599  -4.771  1.00 30.60           N  
ANISOU 2800  N   PHE A 185     4586   3158   3882  -1945   -352   1035       N  
ATOM   2801  CA  PHE A 185      -7.369 -43.373  -3.996  1.00 39.92           C  
ANISOU 2801  CA  PHE A 185     5859   4232   5077  -1982   -489   1033       C  
ATOM   2802  C   PHE A 185      -7.198 -42.193  -4.957  1.00 47.75           C  
ANISOU 2802  C   PHE A 185     6903   5205   6036  -2058   -524   1096       C  
ATOM   2803  O   PHE A 185      -7.949 -41.211  -4.898  1.00 40.91           O  
ANISOU 2803  O   PHE A 185     6179   4220   5144  -2033   -610   1073       O  
ATOM   2804  CB  PHE A 185      -6.190 -43.467  -3.023  1.00 36.25           C  
ANISOU 2804  CB  PHE A 185     5298   3808   4668  -2047   -534   1055       C  
ATOM   2805  CG  PHE A 185      -5.775 -42.146  -2.445  1.00 40.35           C  
ANISOU 2805  CG  PHE A 185     5898   4240   5194  -2117   -673   1074       C  
ATOM   2806  CD1 PHE A 185      -6.519 -41.549  -1.443  1.00 35.26           C  
ANISOU 2806  CD1 PHE A 185     5402   3457   4538  -2058   -780   1005       C  
ATOM   2807  CD2 PHE A 185      -4.639 -41.501  -2.903  1.00 44.93           C  
ANISOU 2807  CD2 PHE A 185     6407   4878   5787  -2239   -694   1163       C  
ATOM   2808  CE1 PHE A 185      -6.140 -40.333  -0.912  1.00 45.87           C  
ANISOU 2808  CE1 PHE A 185     6831   4716   5880  -2120   -911   1020       C  
ATOM   2809  CE2 PHE A 185      -4.255 -40.285  -2.375  1.00 35.75           C  
ANISOU 2809  CE2 PHE A 185     5325   3630   4628  -2309   -830   1184       C  
ATOM   2810  CZ  PHE A 185      -5.007 -39.701  -1.378  1.00 37.96           C  
ANISOU 2810  CZ  PHE A 185     5762   3767   4893  -2250   -940   1110       C  
ATOM   2811  H   PHE A 185      -6.915 -45.205  -4.576  1.00 36.72           H  
ATOM   2812  HA  PHE A 185      -8.179 -43.233  -3.482  1.00 47.91           H  
ATOM   2813  HB2 PHE A 185      -6.439 -44.047  -2.286  1.00 43.50           H  
ATOM   2814  HB3 PHE A 185      -5.427 -43.838  -3.491  1.00 43.50           H  
ATOM   2815  HD1 PHE A 185      -7.285 -41.971  -1.126  1.00 42.31           H  
ATOM   2816  HD2 PHE A 185      -4.129 -41.891  -3.576  1.00 53.92           H  
ATOM   2817  HE1 PHE A 185      -6.648 -39.941  -0.238  1.00 55.04           H  
ATOM   2818  HE2 PHE A 185      -3.491 -39.861  -2.691  1.00 42.90           H  
ATOM   2819  HZ  PHE A 185      -4.749 -38.882  -1.020  1.00 45.55           H  
ATOM   2820  N   ILE A 186      -6.228 -42.312  -5.861  1.00 43.57           N  
ANISOU 2820  N   ILE A 186     6255   4795   5503  -2144   -452   1177       N  
ATOM   2821  CA  ILE A 186      -5.997 -41.290  -6.883  1.00 38.15           C  
ANISOU 2821  CA  ILE A 186     5605   4109   4783  -2223   -472   1248       C  
ATOM   2822  C   ILE A 186      -7.276 -40.973  -7.663  1.00 37.92           C  
ANISOU 2822  C   ILE A 186     5705   4006   4695  -2158   -469   1220       C  
ATOM   2823  O   ILE A 186      -7.589 -39.802  -7.904  1.00 38.75           O  
ANISOU 2823  O   ILE A 186     5919   4023   4781  -2186   -556   1240       O  
ATOM   2824  CB  ILE A 186      -4.852 -41.707  -7.848  1.00 42.23           C  
ANISOU 2824  CB  ILE A 186     5962   4788   5294  -2304   -363   1337       C  
ATOM   2825  CG1 ILE A 186      -3.508 -41.599  -7.117  1.00 48.75           C  
ANISOU 2825  CG1 ILE A 186     6670   5671   6182  -2390   -401   1385       C  
ATOM   2826  CG2 ILE A 186      -4.852 -40.850  -9.121  1.00 36.46           C  
ANISOU 2826  CG2 ILE A 186     5276   4067   4512  -2368   -356   1407       C  
ATOM   2827  CD1 ILE A 186      -2.260 -41.835  -7.978  1.00 42.13           C  
ANISOU 2827  CD1 ILE A 186     5666   4995   5347  -2472   -304   1483       C  
ATOM   2828  H   ILE A 186      -5.686 -42.979  -5.905  1.00 52.28           H  
ATOM   2829  HA  ILE A 186      -5.718 -40.473  -6.440  1.00 45.79           H  
ATOM   2830  HB  ILE A 186      -4.989 -42.633  -8.103  1.00 50.67           H  
ATOM   2831 HG12 ILE A 186      -3.436 -40.709  -6.740  1.00 58.50           H  
ATOM   2832 HG13 ILE A 186      -3.495 -42.255  -6.403  1.00 58.50           H  
ATOM   2833 HG21 ILE A 186      -4.728 -39.920  -8.875  1.00 43.76           H  
ATOM   2834 HG22 ILE A 186      -4.126 -41.140  -9.696  1.00 43.76           H  
ATOM   2835 HG23 ILE A 186      -5.700 -40.962  -9.577  1.00 43.76           H  
ATOM   2836 HD11 ILE A 186      -2.240 -41.177  -8.691  1.00 50.56           H  
ATOM   2837 HD12 ILE A 186      -1.471 -41.743  -7.421  1.00 50.56           H  
ATOM   2838 HD13 ILE A 186      -2.300 -42.728  -8.352  1.00 50.56           H  
ATOM   2839  N   GLN A 187      -8.012 -42.012  -8.050  1.00 42.03           N  
ANISOU 2839  N   GLN A 187     6214   4565   5191  -2071   -375   1178       N  
ATOM   2840  CA  GLN A 187      -9.301 -41.828  -8.715  1.00 42.61           C  
ANISOU 2840  CA  GLN A 187     6406   4572   5214  -1999   -377   1147       C  
ATOM   2841  C   GLN A 187     -10.225 -40.971  -7.855  1.00 47.35           C  
ANISOU 2841  C   GLN A 187     7149   5016   5826  -1935   -500   1090       C  
ATOM   2842  O   GLN A 187     -10.802 -39.985  -8.336  1.00 47.41           O  
ANISOU 2842  O   GLN A 187     7262   4947   5806  -1935   -562   1103       O  
ATOM   2843  CB  GLN A 187      -9.957 -43.181  -9.005  1.00 37.12           C  
ANISOU 2843  CB  GLN A 187     5676   3931   4496  -1911   -271   1100       C  
ATOM   2844  CG  GLN A 187      -9.254 -43.994 -10.086  1.00 52.45           C  
ANISOU 2844  CG  GLN A 187     7503   6023   6401  -1955   -139   1151       C  
ATOM   2845  CD  GLN A 187      -9.799 -43.719 -11.472  1.00 65.86           C  
ANISOU 2845  CD  GLN A 187     9265   7737   8023  -1959   -106   1182       C  
ATOM   2846  OE1 GLN A 187     -10.014 -42.566 -11.848  1.00 67.95           O  
ANISOU 2846  OE1 GLN A 187     9613   7935   8272  -1996   -183   1216       O  
ATOM   2847  NE2 GLN A 187     -10.033 -44.781 -12.239  1.00 64.85           N  
ANISOU 2847  NE2 GLN A 187     9102   7694   7843  -1922      5   1170       N  
ATOM   2848  H   GLN A 187      -7.788 -42.835  -7.939  1.00 50.44           H  
ATOM   2849  HA  GLN A 187      -9.163 -41.371  -9.559  1.00 51.14           H  
ATOM   2850  HB2 GLN A 187      -9.956 -43.709  -8.191  1.00 44.54           H  
ATOM   2851  HB3 GLN A 187     -10.870 -43.029  -9.296  1.00 44.54           H  
ATOM   2852  HG2 GLN A 187      -8.310 -43.771 -10.085  1.00 62.93           H  
ATOM   2853  HG3 GLN A 187      -9.373 -44.938  -9.899  1.00 62.93           H  
ATOM   2854 HE21 GLN A 187      -9.874 -45.571 -11.939  1.00 77.82           H  
ATOM   2855 HE22 GLN A 187     -10.342 -44.677 -13.035  1.00 77.82           H  
ATOM   2856  N   LEU A 188     -10.353 -41.343  -6.583  1.00 36.31           N  
ANISOU 2856  N   LEU A 188     5753   3573   4468  -1879   -533   1027       N  
ATOM   2857  CA  LEU A 188     -11.190 -40.600  -5.652  1.00 30.92           C  
ANISOU 2857  CA  LEU A 188     5204   2753   3792  -1806   -640    966       C  
ATOM   2858  C   LEU A 188     -10.798 -39.126  -5.625  1.00 32.36           C  
ANISOU 2858  C   LEU A 188     5465   2859   3970  -1882   -751   1005       C  
ATOM   2859  O   LEU A 188     -11.650 -38.255  -5.821  1.00 34.00           O  
ANISOU 2859  O   LEU A 188     5795   2970   4153  -1838   -814    990       O  
ATOM   2860  CB  LEU A 188     -11.101 -41.208  -4.249  1.00 30.21           C  
ANISOU 2860  CB  LEU A 188     5093   2643   3740  -1755   -658    905       C  
ATOM   2861  CG  LEU A 188     -11.883 -40.505  -3.137  1.00 30.13           C  
ANISOU 2861  CG  LEU A 188     5219   2499   3730  -1671   -761    836       C  
ATOM   2862  CD1 LEU A 188     -13.379 -40.527  -3.425  1.00 29.36           C  
ANISOU 2862  CD1 LEU A 188     5211   2340   3604  -1545   -746    789       C  
ATOM   2863  CD2 LEU A 188     -11.574 -41.151  -1.793  1.00 29.61           C  
ANISOU 2863  CD2 LEU A 188     5121   2434   3697  -1642   -775    787       C  
ATOM   2864  H   LEU A 188      -9.962 -42.026  -6.236  1.00 43.57           H  
ATOM   2865  HA  LEU A 188     -12.113 -40.658  -5.944  1.00 37.11           H  
ATOM   2866  HB2 LEU A 188     -11.428 -42.121  -4.295  1.00 36.25           H  
ATOM   2867  HB3 LEU A 188     -10.169 -41.216  -3.982  1.00 36.25           H  
ATOM   2868  HG  LEU A 188     -11.602 -39.578  -3.094  1.00 36.16           H  
ATOM   2869 HD11 LEU A 188     -13.676 -41.449  -3.485  1.00 35.23           H  
ATOM   2870 HD12 LEU A 188     -13.846 -40.076  -2.705  1.00 35.23           H  
ATOM   2871 HD13 LEU A 188     -13.546 -40.071  -4.265  1.00 35.23           H  
ATOM   2872 HD21 LEU A 188     -10.623 -41.074  -1.618  1.00 35.53           H  
ATOM   2873 HD22 LEU A 188     -12.077 -40.694  -1.101  1.00 35.53           H  
ATOM   2874 HD23 LEU A 188     -11.830 -42.086  -1.826  1.00 35.53           H  
ATOM   2875  N   VAL A 189      -9.514 -38.842  -5.409  1.00 41.04           N  
ANISOU 2875  N   VAL A 189     6494   4005   5096  -1996   -779   1059       N  
ATOM   2876  CA  VAL A 189      -9.075 -37.446  -5.359  1.00 45.87           C  
ANISOU 2876  CA  VAL A 189     7181   4543   5705  -2080   -894   1102       C  
ATOM   2877  C   VAL A 189      -9.390 -36.740  -6.673  1.00 50.69           C  
ANISOU 2877  C   VAL A 189     7838   5146   6275  -2115   -889   1158       C  
ATOM   2878  O   VAL A 189      -9.791 -35.578  -6.679  1.00 43.26           O  
ANISOU 2878  O   VAL A 189     7020   4098   5320  -2119   -988   1161       O  
ATOM   2879  CB  VAL A 189      -7.561 -37.275  -5.099  1.00 48.07           C  
ANISOU 2879  CB  VAL A 189     7357   4889   6019  -2213   -920   1171       C  
ATOM   2880  CG1 VAL A 189      -7.274 -35.839  -4.692  1.00 50.47           C  
ANISOU 2880  CG1 VAL A 189     7769   5085   6322  -2281  -1066   1194       C  
ATOM   2881  CG2 VAL A 189      -7.070 -38.209  -4.018  1.00 48.79           C  
ANISOU 2881  CG2 VAL A 189     7361   5026   6151  -2193   -901   1132       C  
ATOM   2882  H   VAL A 189      -8.890 -39.422  -5.292  1.00 49.25           H  
ATOM   2883  HA  VAL A 189      -9.554 -36.990  -4.650  1.00 55.05           H  
ATOM   2884  HB  VAL A 189      -7.071 -37.466  -5.914  1.00 57.68           H  
ATOM   2885 HG11 VAL A 189      -7.769 -35.635  -3.883  1.00 60.57           H  
ATOM   2886 HG12 VAL A 189      -6.322 -35.741  -4.531  1.00 60.57           H  
ATOM   2887 HG13 VAL A 189      -7.551 -35.247  -5.409  1.00 60.57           H  
ATOM   2888 HG21 VAL A 189      -7.235 -39.124  -4.293  1.00 58.55           H  
ATOM   2889 HG22 VAL A 189      -6.119 -38.068  -3.888  1.00 58.55           H  
ATOM   2890 HG23 VAL A 189      -7.548 -38.019  -3.196  1.00 58.55           H  
ATOM   2891  N   GLN A 190      -9.197 -37.447  -7.783  1.00 41.51           N  
ANISOU 2891  N   GLN A 190     6580   4099   5092  -2140   -774   1204       N  
ATOM   2892  CA  GLN A 190      -9.484 -36.899  -9.106  1.00 42.87           C  
ANISOU 2892  CA  GLN A 190     6792   4280   5219  -2174   -759   1261       C  
ATOM   2893  C   GLN A 190     -10.950 -36.462  -9.226  1.00 55.86           C  
ANISOU 2893  C   GLN A 190     8578   5811   6836  -2067   -806   1207       C  
ATOM   2894  O   GLN A 190     -11.246 -35.291  -9.540  1.00 66.33           O  
ANISOU 2894  O   GLN A 190    10007   7051   8146  -2091   -893   1233       O  
ATOM   2895  CB  GLN A 190      -9.122 -37.939 -10.174  1.00 55.99           C  
ANISOU 2895  CB  GLN A 190     8331   6090   6852  -2196   -616   1303       C  
ATOM   2896  CG  GLN A 190      -9.164 -37.429 -11.611  1.00 64.95           C  
ANISOU 2896  CG  GLN A 190     9487   7259   7931  -2252   -590   1377       C  
ATOM   2897  CD  GLN A 190      -8.022 -37.956 -12.473  1.00 71.32           C  
ANISOU 2897  CD  GLN A 190    10152   8227   8720  -2342   -478   1457       C  
ATOM   2898  OE1 GLN A 190      -7.263 -38.835 -12.060  1.00 64.47           O  
ANISOU 2898  OE1 GLN A 190     9161   7452   7881  -2349   -407   1454       O  
ATOM   2899  NE2 GLN A 190      -7.899 -37.415 -13.682  1.00 72.50           N  
ANISOU 2899  NE2 GLN A 190    10317   8411   8818  -2405   -460   1533       N  
ATOM   2900  H   GLN A 190      -8.897 -38.253  -7.797  1.00 49.81           H  
ATOM   2901  HA  GLN A 190      -8.927 -36.117  -9.250  1.00 51.45           H  
ATOM   2902  HB2 GLN A 190      -8.221 -38.256 -10.002  1.00 67.19           H  
ATOM   2903  HB3 GLN A 190      -9.745 -38.679 -10.108  1.00 67.19           H  
ATOM   2904  HG2 GLN A 190      -9.998 -37.708 -12.019  1.00 77.94           H  
ATOM   2905  HG3 GLN A 190      -9.108 -36.461 -11.603  1.00 77.94           H  
ATOM   2906 HE21 GLN A 190      -8.447 -36.803 -13.937  1.00 87.00           H  
ATOM   2907 HE22 GLN A 190      -7.271 -37.676 -14.209  1.00 87.00           H  
ATOM   2908  N   THR A 191     -11.869 -37.388  -8.955  1.00 54.55           N  
ANISOU 2908  N   THR A 191     8415   5643   6667  -1948   -752   1135       N  
ATOM   2909  CA  THR A 191     -13.290 -37.058  -9.026  1.00 46.82           C  
ANISOU 2909  CA  THR A 191     7553   4568   5668  -1835   -791   1085       C  
ATOM   2910  C   THR A 191     -13.656 -35.982  -8.009  1.00 35.84           C  
ANISOU 2910  C   THR A 191     6281   3039   4296  -1796   -916   1043       C  
ATOM   2911  O   THR A 191     -14.556 -35.181  -8.254  1.00 45.82           O  
ANISOU 2911  O   THR A 191     7654   4213   5543  -1743   -976   1033       O  
ATOM   2912  CB  THR A 191     -14.202 -38.286  -8.815  1.00 34.15           C  
ANISOU 2912  CB  THR A 191     5923   2989   4063  -1714   -716   1018       C  
ATOM   2913  OG1 THR A 191     -13.948 -38.871  -7.532  1.00 49.39           O  
ANISOU 2913  OG1 THR A 191     7817   4915   6034  -1675   -715    963       O  
ATOM   2914  CG2 THR A 191     -13.981 -39.319  -9.914  1.00 35.48           C  
ANISOU 2914  CG2 THR A 191     5997   3284   4199  -1743   -597   1054       C  
ATOM   2915  H   THR A 191     -11.699 -38.200  -8.730  1.00 65.46           H  
ATOM   2916  HA  THR A 191     -13.479 -36.703  -9.909  1.00 56.18           H  
ATOM   2917  HB  THR A 191     -15.128 -38.001  -8.854  1.00 40.98           H  
ATOM   2918  HG1 THR A 191     -13.146 -39.116  -7.482  1.00 59.27           H  
ATOM   2919 HG21 THR A 191     -13.057 -39.615  -9.909  1.00 42.57           H  
ATOM   2920 HG22 THR A 191     -14.558 -40.085  -9.770  1.00 42.57           H  
ATOM   2921 HG23 THR A 191     -14.182 -38.930 -10.779  1.00 42.57           H  
ATOM   2922  N   TYR A 192     -12.963 -35.957  -6.873  1.00 34.18           N  
ANISOU 2922  N   TYR A 192     6055   2812   4119  -1819   -957   1019       N  
ATOM   2923  CA  TYR A 192     -13.164 -34.869  -5.915  1.00 35.62           C  
ANISOU 2923  CA  TYR A 192     6360   2864   4309  -1794  -1081    982       C  
ATOM   2924  C   TYR A 192     -12.726 -33.529  -6.507  1.00 41.54           C  
ANISOU 2924  C   TYR A 192     7176   3562   5046  -1897  -1169   1051       C  
ATOM   2925  O   TYR A 192     -13.425 -32.525  -6.385  1.00 47.61           O  
ANISOU 2925  O   TYR A 192     8074   4215   5801  -1850  -1257   1031       O  
ATOM   2926  CB  TYR A 192     -12.412 -35.121  -4.603  1.00 34.88           C  
ANISOU 2926  CB  TYR A 192     6238   2769   4247  -1812  -1113    948       C  
ATOM   2927  CG  TYR A 192     -12.406 -33.919  -3.675  1.00 35.99           C  
ANISOU 2927  CG  TYR A 192     6509   2780   4385  -1809  -1250    919       C  
ATOM   2928  CD1 TYR A 192     -13.431 -33.717  -2.759  1.00 35.59           C  
ANISOU 2928  CD1 TYR A 192     6571   2629   4322  -1672  -1292    831       C  
ATOM   2929  CD2 TYR A 192     -11.381 -32.981  -3.722  1.00 45.91           C  
ANISOU 2929  CD2 TYR A 192     7780   4016   5647  -1942  -1336    983       C  
ATOM   2930  CE1 TYR A 192     -13.431 -32.617  -1.917  1.00 44.09           C  
ANISOU 2930  CE1 TYR A 192     7778   3586   5386  -1663  -1414    801       C  
ATOM   2931  CE2 TYR A 192     -11.379 -31.878  -2.883  1.00 39.10           C  
ANISOU 2931  CE2 TYR A 192     7050   3030   4777  -1941  -1468    956       C  
ATOM   2932  CZ  TYR A 192     -12.404 -31.705  -1.983  1.00 45.78           C  
ANISOU 2932  CZ  TYR A 192     8013   3775   5605  -1799  -1505    862       C  
ATOM   2933  OH  TYR A 192     -12.407 -30.614  -1.145  1.00 43.79           O  
ANISOU 2933  OH  TYR A 192     7902   3399   5336  -1790  -1634    830       O  
ATOM   2934  H   TYR A 192     -12.382 -36.544  -6.635  1.00 41.01           H  
ATOM   2935  HA  TYR A 192     -14.110 -34.807  -5.707  1.00 42.74           H  
ATOM   2936  HB2 TYR A 192     -12.835 -35.858  -4.134  1.00 41.86           H  
ATOM   2937  HB3 TYR A 192     -11.490 -35.345  -4.807  1.00 41.86           H  
ATOM   2938  HD1 TYR A 192     -14.128 -34.330  -2.710  1.00 42.70           H  
ATOM   2939  HD2 TYR A 192     -10.686 -33.094  -4.330  1.00 55.09           H  
ATOM   2940  HE1 TYR A 192     -14.123 -32.497  -1.308  1.00 52.90           H  
ATOM   2941  HE2 TYR A 192     -10.684 -31.261  -2.925  1.00 46.92           H  
ATOM   2942  HH  TYR A 192     -11.728 -30.141  -1.288  1.00 52.55           H  
ATOM   2943  N   ASN A 193     -11.563 -33.522  -7.148  1.00 41.47           N  
ANISOU 2943  N   ASN A 193     7074   3641   5042  -2035  -1145   1137       N  
ATOM   2944  CA  ASN A 193     -11.005 -32.298  -7.705  1.00 43.75           C  
ANISOU 2944  CA  ASN A 193     7411   3891   5321  -2150  -1228   1215       C  
ATOM   2945  C   ASN A 193     -11.865 -31.733  -8.827  1.00 52.70           C  
ANISOU 2945  C   ASN A 193     8620   4987   6418  -2126  -1233   1242       C  
ATOM   2946  O   ASN A 193     -12.031 -30.515  -8.939  1.00 45.34           O  
ANISOU 2946  O   ASN A 193     7797   3953   5476  -2154  -1337   1265       O  
ATOM   2947  CB  ASN A 193      -9.584 -32.545  -8.213  1.00 40.96           C  
ANISOU 2947  CB  ASN A 193     6921   3662   4981  -2297  -1182   1308       C  
ATOM   2948  CG  ASN A 193      -8.563 -32.592  -7.091  1.00 42.55           C  
ANISOU 2948  CG  ASN A 193     7073   3872   5223  -2356  -1230   1304       C  
ATOM   2949  OD1 ASN A 193      -8.894 -32.382  -5.924  1.00 40.12           O  
ANISOU 2949  OD1 ASN A 193     6847   3471   4927  -2292  -1306   1232       O  
ATOM   2950  ND2 ASN A 193      -7.314 -32.876  -7.439  1.00 45.76           N  
ANISOU 2950  ND2 ASN A 193     7345   4395   5648  -2475  -1187   1385       N  
ATOM   2951  H   ASN A 193     -11.075 -34.218  -7.275  1.00 49.77           H  
ATOM   2952  HA  ASN A 193     -10.958 -31.629  -7.004  1.00 52.50           H  
ATOM   2953  HB2 ASN A 193      -9.558 -33.395  -8.679  1.00 49.16           H  
ATOM   2954  HB3 ASN A 193      -9.334 -31.827  -8.815  1.00 49.16           H  
ATOM   2955 HD21 ASN A 193      -7.120 -33.021  -8.264  1.00 54.92           H  
ATOM   2956 HD22 ASN A 193      -6.699 -32.915  -6.839  1.00 54.92           H  
ATOM   2957  N   GLN A 194     -12.410 -32.612  -9.663  1.00 57.90           N  
ANISOU 2957  N   GLN A 194     9222   5724   7054  -2076  -1125   1242       N  
ATOM   2958  CA  GLN A 194     -13.307 -32.156 -10.726  1.00 52.83           C  
ANISOU 2958  CA  GLN A 194     8650   5049   6374  -2046  -1131   1266       C  
ATOM   2959  C   GLN A 194     -14.553 -31.441 -10.198  1.00 53.31           C  
ANISOU 2959  C   GLN A 194     8853   4967   6437  -1925  -1218   1199       C  
ATOM   2960  O   GLN A 194     -15.125 -30.601 -10.889  1.00 62.19           O  
ANISOU 2960  O   GLN A 194    10061   6028   7540  -1922  -1271   1229       O  
ATOM   2961  CB  GLN A 194     -13.710 -33.319 -11.633  1.00 47.82           C  
ANISOU 2961  CB  GLN A 194     7936   4524   5710  -2007  -1005   1269       C  
ATOM   2962  CG  GLN A 194     -12.693 -33.595 -12.733  1.00 63.93           C  
ANISOU 2962  CG  GLN A 194     9875   6693   7722  -2132   -928   1361       C  
ATOM   2963  CD  GLN A 194     -13.038 -34.802 -13.582  1.00 74.37           C  
ANISOU 2963  CD  GLN A 194    11127   8125   9006  -2090   -802   1358       C  
ATOM   2964  OE1 GLN A 194     -14.169 -35.290 -13.565  1.00 77.21           O  
ANISOU 2964  OE1 GLN A 194    11526   8455   9355  -1976   -785   1298       O  
ATOM   2965  NE2 GLN A 194     -12.057 -35.289 -14.335  1.00 76.68           N  
ANISOU 2965  NE2 GLN A 194    11313   8547   9273  -2182   -712   1424       N  
ATOM   2966  H   GLN A 194     -12.281 -33.462  -9.639  1.00 69.48           H  
ATOM   2967  HA  GLN A 194     -12.823 -31.519 -11.275  1.00 63.39           H  
ATOM   2968  HB2 GLN A 194     -13.796 -34.123 -11.096  1.00 57.39           H  
ATOM   2969  HB3 GLN A 194     -14.558 -33.111 -12.055  1.00 57.39           H  
ATOM   2970  HG2 GLN A 194     -12.646 -32.823 -13.318  1.00 76.71           H  
ATOM   2971  HG3 GLN A 194     -11.827 -33.754 -12.327  1.00 76.71           H  
ATOM   2972 HE21 GLN A 194     -11.280 -34.920 -14.321  1.00 92.01           H  
ATOM   2973 HE22 GLN A 194     -12.199 -35.974 -14.836  1.00 92.01           H  
ATOM   2974  N   LEU A 195     -14.964 -31.766  -8.975  1.00 47.02           N  
ANISOU 2974  N   LEU A 195     8079   4121   5664  -1823  -1231   1112       N  
ATOM   2975  CA  LEU A 195     -16.154 -31.158  -8.378  1.00 45.10           C  
ANISOU 2975  CA  LEU A 195     7962   3752   5421  -1691  -1301   1044       C  
ATOM   2976  C   LEU A 195     -15.829 -29.886  -7.593  1.00 55.08           C  
ANISOU 2976  C   LEU A 195     9340   4895   6694  -1721  -1432   1035       C  
ATOM   2977  O   LEU A 195     -16.722 -29.093  -7.284  1.00 56.37           O  
ANISOU 2977  O   LEU A 195     9624   4942   6851  -1629  -1504    994       O  
ATOM   2978  CB  LEU A 195     -16.874 -32.160  -7.473  1.00 50.12           C  
ANISOU 2978  CB  LEU A 195     8572   4399   6071  -1553  -1244    955       C  
ATOM   2979  CG  LEU A 195     -17.752 -33.162  -8.224  1.00 55.59           C  
ANISOU 2979  CG  LEU A 195     9206   5163   6752  -1477  -1146    949       C  
ATOM   2980  CD1 LEU A 195     -17.837 -34.476  -7.472  1.00 61.51           C  
ANISOU 2980  CD1 LEU A 195     9874   5977   7520  -1409  -1064    891       C  
ATOM   2981  CD2 LEU A 195     -19.144 -32.591  -8.447  1.00 40.68           C  
ANISOU 2981  CD2 LEU A 195     7414   3188   4855  -1359  -1187    925       C  
ATOM   2982  H   LEU A 195     -14.571 -32.337  -8.467  1.00 56.42           H  
ATOM   2983  HA  LEU A 195     -16.766 -30.913  -9.090  1.00 54.11           H  
ATOM   2984  HB2 LEU A 195     -16.211 -32.662  -6.976  1.00 60.14           H  
ATOM   2985  HB3 LEU A 195     -17.444 -31.671  -6.859  1.00 60.14           H  
ATOM   2986  HG  LEU A 195     -17.358 -33.339  -9.092  1.00 66.71           H  
ATOM   2987 HD11 LEU A 195     -18.221 -34.314  -6.596  1.00 73.81           H  
ATOM   2988 HD12 LEU A 195     -18.399 -35.089  -7.971  1.00 73.81           H  
ATOM   2989 HD13 LEU A 195     -16.945 -34.845  -7.379  1.00 73.81           H  
ATOM   2990 HD21 LEU A 195     -19.071 -31.777  -8.970  1.00 48.82           H  
ATOM   2991 HD22 LEU A 195     -19.681 -33.243  -8.923  1.00 48.82           H  
ATOM   2992 HD23 LEU A 195     -19.547 -32.396  -7.586  1.00 48.82           H  
ATOM   2993  N   PHE A 196     -14.554 -29.697  -7.270  1.00 45.74           N  
ANISOU 2993  N   PHE A 196     8118   3738   5524  -1846  -1465   1074       N  
ATOM   2994  CA  PHE A 196     -14.102 -28.473  -6.618  1.00 49.08           C  
ANISOU 2994  CA  PHE A 196     8648   4049   5950  -1899  -1599   1078       C  
ATOM   2995  C   PHE A 196     -12.876 -27.937  -7.347  1.00 66.15           C  
ANISOU 2995  C   PHE A 196    10765   6256   8115  -2080  -1632   1187       C  
ATOM   2996  O   PHE A 196     -11.741 -28.164  -6.927  1.00 64.82           O  
ANISOU 2996  O   PHE A 196    10519   6142   7965  -2178  -1635   1216       O  
ATOM   2997  CB  PHE A 196     -13.777 -28.723  -5.143  1.00 48.91           C  
ANISOU 2997  CB  PHE A 196     8640   4000   5945  -1861  -1630   1007       C  
ATOM   2998  CG  PHE A 196     -14.925 -29.287  -4.355  1.00 52.27           C  
ANISOU 2998  CG  PHE A 196     9103   4391   6365  -1684  -1592    904       C  
ATOM   2999  CD1 PHE A 196     -15.832 -28.451  -3.722  1.00 46.99           C  
ANISOU 2999  CD1 PHE A 196     8584   3591   5681  -1569  -1672    839       C  
ATOM   3000  CD2 PHE A 196     -15.095 -30.657  -4.247  1.00 48.15           C  
ANISOU 3000  CD2 PHE A 196     8468   3971   5854  -1629  -1475    874       C  
ATOM   3001  CE1 PHE A 196     -16.890 -28.976  -2.996  1.00 50.94           C  
ANISOU 3001  CE1 PHE A 196     9110   4069   6175  -1402  -1629    750       C  
ATOM   3002  CE2 PHE A 196     -16.146 -31.185  -3.525  1.00 47.45           C  
ANISOU 3002  CE2 PHE A 196     8409   3856   5762  -1469  -1440    787       C  
ATOM   3003  CZ  PHE A 196     -17.046 -30.344  -2.900  1.00 46.63           C  
ANISOU 3003  CZ  PHE A 196     8446   3629   5642  -1355  -1514    726       C  
ATOM   3004  H   PHE A 196     -13.927 -30.266  -7.420  1.00 54.89           H  
ATOM   3005  HA  PHE A 196     -14.803 -27.804  -6.667  1.00 58.89           H  
ATOM   3006  HB2 PHE A 196     -13.042 -29.354  -5.088  1.00 58.70           H  
ATOM   3007  HB3 PHE A 196     -13.520 -27.883  -4.733  1.00 58.70           H  
ATOM   3008  HD2 PHE A 196     -14.493 -31.228  -4.667  1.00 57.77           H  
ATOM   3009  HD1 PHE A 196     -15.731 -27.528  -3.786  1.00 56.39           H  
ATOM   3010  HE2 PHE A 196     -16.250 -32.107  -3.461  1.00 56.94           H  
ATOM   3011  HE1 PHE A 196     -17.493 -28.407  -2.576  1.00 61.12           H  
ATOM   3012  HZ  PHE A 196     -17.754 -30.699  -2.413  1.00 55.95           H  
ATOM   3013  N   GLU A 197     -13.120 -27.232  -8.447  1.00 85.90           N  
ANISOU 3013  N   GLU A 197    13307   8733  10596  -2124  -1656   1251       N  
ATOM   3014  CA  GLU A 197     -12.048 -26.717  -9.292  1.00 92.01           C  
ANISOU 3014  CA  GLU A 197    14037   9556  11368  -2295  -1679   1364       C  
ATOM   3015  C   GLU A 197     -11.112 -25.789  -8.527  1.00 94.64           C  
ANISOU 3015  C   GLU A 197    14422   9817  11719  -2396  -1805   1390       C  
ATOM   3016  O   GLU A 197      -9.907 -25.764  -8.777  1.00 87.44           O  
ANISOU 3016  O   GLU A 197    13422   8982  10820  -2540  -1805   1473       O  
ATOM   3017  CB  GLU A 197     -12.630 -25.953 -10.484  1.00 98.67           C  
ANISOU 3017  CB  GLU A 197    14948  10358  12183  -2310  -1706   1421       C  
ATOM   3018  CG  GLU A 197     -13.548 -26.774 -11.380  1.00100.89           C  
ANISOU 3018  CG  GLU A 197    15185  10708  12440  -2224  -1595   1409       C  
ATOM   3019  CD  GLU A 197     -15.003 -26.349 -11.287  1.00105.23           C  
ANISOU 3019  CD  GLU A 197    15857  11144  12982  -2077  -1639   1345       C  
ATOM   3020  OE1 GLU A 197     -15.461 -25.998 -10.178  1.00110.13           O  
ANISOU 3020  OE1 GLU A 197    16564  11661  13619  -1985  -1704   1266       O  
ATOM   3021  OE2 GLU A 197     -15.691 -26.363 -12.330  1.00 98.64           O  
ANISOU 3021  OE2 GLU A 197    15030  10325  12122  -2053  -1607   1375       O  
ATOM   3022  H   GLU A 197     -13.908 -27.035  -8.729  1.00103.07           H  
ATOM   3023  HA  GLU A 197     -11.526 -27.460  -9.633  1.00110.42           H  
ATOM   3024  HB2 GLU A 197     -13.143 -25.201 -10.150  1.00118.40           H  
ATOM   3025  HB3 GLU A 197     -11.898 -25.630 -11.032  1.00118.40           H  
ATOM   3026  HG2 GLU A 197     -13.264 -26.671 -12.301  1.00121.07           H  
ATOM   3027  HG3 GLU A 197     -13.492 -27.706 -11.118  1.00121.07           H  
ATOM   3028  N   GLU A 198     -11.674 -25.035  -7.589  1.00 67.21           N  
ANISOU 3028  N   GLU A 198    11093   6199   8245  -2317  -1914   1319       N  
ATOM   3029  CA  GLU A 198     -10.952 -23.948  -6.936  1.00 65.36           C  
ANISOU 3029  CA  GLU A 198    10948   5867   8018  -2407  -2059   1342       C  
ATOM   3030  C   GLU A 198      -9.990 -24.414  -5.846  1.00 69.80           C  
ANISOU 3030  C   GLU A 198    11448   6471   8604  -2454  -2072   1324       C  
ATOM   3031  O   GLU A 198      -8.959 -23.781  -5.614  1.00 74.96           O  
ANISOU 3031  O   GLU A 198    12107   7106   9270  -2586  -2165   1385       O  
ATOM   3032  CB  GLU A 198     -11.953 -22.954  -6.349  1.00 57.49           C  
ANISOU 3032  CB  GLU A 198    10143   4697   7005  -2295  -2170   1269       C  
ATOM   3033  CG  GLU A 198     -12.820 -22.268  -7.397  1.00 66.57           C  
ANISOU 3033  CG  GLU A 198    11369   5787   8137  -2264  -2188   1299       C  
ATOM   3034  CD  GLU A 198     -12.005 -21.593  -8.483  1.00 65.04           C  
ANISOU 3034  CD  GLU A 198    11151   5619   7943  -2437  -2229   1428       C  
ATOM   3035  OE1 GLU A 198     -10.942 -21.023  -8.160  1.00 67.41           O  
ANISOU 3035  OE1 GLU A 198    11459   5900   8255  -2569  -2318   1482       O  
ATOM   3036  OE2 GLU A 198     -12.421 -21.643  -9.660  1.00 55.74           O  
ANISOU 3036  OE2 GLU A 198     9946   4483   6751  -2444  -2174   1478       O  
ATOM   3037  H   GLU A 198     -12.482 -25.134  -7.310  1.00 80.65           H  
ATOM   3038  HA  GLU A 198     -10.430 -23.479  -7.606  1.00 78.43           H  
ATOM   3039  HB2 GLU A 198     -12.542 -23.425  -5.739  1.00 68.99           H  
ATOM   3040  HB3 GLU A 198     -11.466 -22.265  -5.870  1.00 68.99           H  
ATOM   3041  HG2 GLU A 198     -13.390 -22.931  -7.818  1.00 79.88           H  
ATOM   3042  HG3 GLU A 198     -13.363 -21.591  -6.964  1.00 79.88           H  
ATOM   3043  N   ASN A 199     -10.328 -25.514  -5.182  1.00 87.35           N  
ANISOU 3043  N   ASN A 199    13611   8747  10832  -2348  -1983   1243       N  
ATOM   3044  CA  ASN A 199      -9.521 -26.021  -4.080  1.00 82.63           C  
ANISOU 3044  CA  ASN A 199    12957   8184  10255  -2376  -1995   1217       C  
ATOM   3045  C   ASN A 199      -9.277 -27.516  -4.227  1.00 74.48           C  
ANISOU 3045  C   ASN A 199    11749   7307   9241  -2358  -1843   1212       C  
ATOM   3046  O   ASN A 199      -9.866 -28.320  -3.502  1.00 61.09           O  
ANISOU 3046  O   ASN A 199    10048   5618   7545  -2237  -1790   1124       O  
ATOM   3047  CB  ASN A 199     -10.205 -25.723  -2.744  1.00 85.17           C  
ANISOU 3047  CB  ASN A 199    13421   8381  10560  -2248  -2072   1105       C  
ATOM   3048  CG  ASN A 199     -10.452 -24.241  -2.535  1.00 90.69           C  
ANISOU 3048  CG  ASN A 199    14304   8918  11237  -2255  -2225   1102       C  
ATOM   3049  OD1 ASN A 199      -9.538 -23.424  -2.654  1.00 96.27           O  
ANISOU 3049  OD1 ASN A 199    15034   9594  11951  -2397  -2327   1178       O  
ATOM   3050  ND2 ASN A 199     -11.695 -23.885  -2.234  1.00 87.57           N  
ANISOU 3050  ND2 ASN A 199    14039   8417  10815  -2100  -2243   1017       N  
ATOM   3051  H   ASN A 199     -11.025 -25.987  -5.352  1.00104.82           H  
ATOM   3052  HA  ASN A 199      -8.660 -25.574  -4.085  1.00 99.16           H  
ATOM   3053  HB2 ASN A 199     -11.062 -26.177  -2.719  1.00102.21           H  
ATOM   3054  HB3 ASN A 199      -9.640 -26.039  -2.021  1.00102.21           H  
ATOM   3055 HD21 ASN A 199     -12.310 -24.483  -2.167  1.00105.08           H  
ATOM   3056 HD22 ASN A 199     -11.886 -23.056  -2.106  1.00105.08           H  
ATOM   3057  N   PRO A 200      -8.404 -27.898  -5.173  1.00 67.37           N  
ANISOU 3057  N   PRO A 200    10707   6535   8356  -2478  -1773   1308       N  
ATOM   3058  CA  PRO A 200      -8.123 -29.321  -5.363  1.00 64.05           C  
ANISOU 3058  CA  PRO A 200    10119   6264   7952  -2463  -1627   1307       C  
ATOM   3059  C   PRO A 200      -7.269 -29.868  -4.230  1.00 64.29           C  
ANISOU 3059  C   PRO A 200    10079   6335   8015  -2491  -1641   1286       C  
ATOM   3060  O   PRO A 200      -6.804 -29.105  -3.382  1.00 60.85           O  
ANISOU 3060  O   PRO A 200     9718   5816   7585  -2539  -1767   1284       O  
ATOM   3061  CB  PRO A 200      -7.331 -29.344  -6.669  1.00 57.11           C  
ANISOU 3061  CB  PRO A 200     9126   5500   7073  -2592  -1565   1424       C  
ATOM   3062  CG  PRO A 200      -6.623 -28.032  -6.685  1.00 64.85           C  
ANISOU 3062  CG  PRO A 200    10173   6409   8057  -2720  -1700   1498       C  
ATOM   3063  CD  PRO A 200      -7.575 -27.052  -6.051  1.00 63.06           C  
ANISOU 3063  CD  PRO A 200    10145   6005   7811  -2635  -1824   1426       C  
ATOM   3064  HA  PRO A 200      -8.940 -29.836  -5.453  1.00 76.85           H  
ATOM   3065  HB2 PRO A 200      -6.698 -30.080  -6.659  1.00 68.53           H  
ATOM   3066  HB3 PRO A 200      -7.938 -29.419  -7.422  1.00 68.53           H  
ATOM   3067  HG2 PRO A 200      -5.805 -28.097  -6.168  1.00 77.82           H  
ATOM   3068  HG3 PRO A 200      -6.429 -27.778  -7.601  1.00 77.82           H  
ATOM   3069  HD2 PRO A 200      -7.087 -26.397  -5.528  1.00 75.68           H  
ATOM   3070  HD3 PRO A 200      -8.124 -26.628  -6.729  1.00 75.68           H  
ATOM   3071  N   ILE A 201      -7.070 -31.181  -4.228  1.00 66.71           N  
ANISOU 3071  N   ILE A 201    10244   6763   8340  -2462  -1517   1272       N  
ATOM   3072  CA  ILE A 201      -6.167 -31.822  -3.287  1.00 65.17           C  
ANISOU 3072  CA  ILE A 201     9954   6629   8181  -2498  -1518   1265       C  
ATOM   3073  C   ILE A 201      -5.047 -32.464  -4.082  1.00 66.27           C  
ANISOU 3073  C   ILE A 201     9903   6931   8347  -2608  -1422   1361       C  
ATOM   3074  O   ILE A 201      -5.286 -33.056  -5.134  1.00 62.44           O  
ANISOU 3074  O   ILE A 201     9344   6534   7848  -2590  -1302   1386       O  
ATOM   3075  CB  ILE A 201      -6.886 -32.893  -2.455  1.00 63.08           C  
ANISOU 3075  CB  ILE A 201     9681   6367   7918  -2358  -1455   1161       C  
ATOM   3076  CG1 ILE A 201      -8.234 -32.349  -1.973  1.00 61.12           C  
ANISOU 3076  CG1 ILE A 201     9612   5976   7635  -2223  -1512   1069       C  
ATOM   3077  CG2 ILE A 201      -5.997 -33.349  -1.308  1.00 64.34           C  
ANISOU 3077  CG2 ILE A 201     9775   6560   8112  -2395  -1490   1150       C  
ATOM   3078  CD1 ILE A 201      -8.934 -33.188  -0.916  1.00 63.49           C  
ANISOU 3078  CD1 ILE A 201     9933   6257   7934  -2087  -1480    965       C  
ATOM   3079  H   ILE A 201      -7.452 -31.728  -4.770  1.00 80.05           H  
ATOM   3080  HA  ILE A 201      -5.789 -31.159  -2.687  1.00 78.21           H  
ATOM   3081  HB  ILE A 201      -7.056 -33.658  -3.028  1.00 75.69           H  
ATOM   3082 HG12 ILE A 201      -8.093 -31.466  -1.597  1.00 73.34           H  
ATOM   3083 HG13 ILE A 201      -8.830 -32.285  -2.736  1.00 73.34           H  
ATOM   3084 HG21 ILE A 201      -5.794 -32.586  -0.744  1.00 77.21           H  
ATOM   3085 HG22 ILE A 201      -6.467 -34.025  -0.794  1.00 77.21           H  
ATOM   3086 HG23 ILE A 201      -5.177 -33.719  -1.671  1.00 77.21           H  
ATOM   3087 HD11 ILE A 201      -8.363 -33.252  -0.135  1.00 76.19           H  
ATOM   3088 HD12 ILE A 201      -9.773 -32.762  -0.680  1.00 76.19           H  
ATOM   3089 HD13 ILE A 201      -9.102 -34.073  -1.277  1.00 76.19           H  
ATOM   3090  N   ASN A 202      -3.823 -32.332  -3.583  1.00 80.51           N  
ANISOU 3090  N   ASN A 202    11628   8777  10185  -2718  -1476   1417       N  
ATOM   3091  CA  ASN A 202      -2.662 -32.859  -4.279  1.00 85.81           C  
ANISOU 3091  CA  ASN A 202    12111   9609  10885  -2823  -1390   1516       C  
ATOM   3092  C   ASN A 202      -2.282 -34.235  -3.760  1.00 87.32           C  
ANISOU 3092  C   ASN A 202    12156   9912  11112  -2780  -1293   1485       C  
ATOM   3093  O   ASN A 202      -2.047 -34.420  -2.565  1.00 86.86           O  
ANISOU 3093  O   ASN A 202    12104   9820  11077  -2764  -1357   1441       O  
ATOM   3094  CB  ASN A 202      -1.479 -31.906  -4.134  1.00 86.12           C  
ANISOU 3094  CB  ASN A 202    12130   9643  10947  -2978  -1504   1613       C  
ATOM   3095  CG  ASN A 202      -0.410 -32.150  -5.177  1.00 88.82           C  
ANISOU 3095  CG  ASN A 202    12296  10143  11307  -3091  -1415   1734       C  
ATOM   3096  OD1 ASN A 202       0.065 -33.271  -5.348  1.00 81.52           O  
ANISOU 3096  OD1 ASN A 202    11208   9360  10406  -3076  -1291   1746       O  
ATOM   3097  ND2 ASN A 202      -0.040 -31.101  -5.897  1.00 95.11           N  
ANISOU 3097  ND2 ASN A 202    13126  10920  12091  -3200  -1476   1826       N  
ATOM   3098  H   ASN A 202      -3.641 -31.940  -2.839  1.00 96.61           H  
ATOM   3099  HA  ASN A 202      -2.869 -32.940  -5.223  1.00102.98           H  
ATOM   3100  HB2 ASN A 202      -1.793 -30.993  -4.232  1.00103.34           H  
ATOM   3101  HB3 ASN A 202      -1.079 -32.028  -3.258  1.00103.34           H  
ATOM   3102 HD21 ASN A 202      -0.404 -30.334  -5.758  1.00114.13           H  
ATOM   3103 HD22 ASN A 202       0.564 -31.186  -6.503  1.00114.13           H  
ATOM   3104  N   ALA A 203      -2.220 -35.200  -4.670  1.00 93.14           N  
ANISOU 3104  N   ALA A 203    12763  10781  11847  -2759  -1139   1510       N  
ATOM   3105  CA  ALA A 203      -1.810 -36.550  -4.319  1.00 92.64           C  
ANISOU 3105  CA  ALA A 203    12548  10835  11818  -2719  -1037   1489       C  
ATOM   3106  C   ALA A 203      -0.321 -36.568  -3.996  1.00 95.84           C  
ANISOU 3106  C   ALA A 203    12806  11336  12273  -2835  -1061   1573       C  
ATOM   3107  O   ALA A 203       0.152 -37.465  -3.301  1.00 99.74           O  
ANISOU 3107  O   ALA A 203    13191  11898  12807  -2813  -1029   1554       O  
ATOM   3108  CB  ALA A 203      -2.120 -37.509  -5.458  1.00 95.56           C  
ANISOU 3108  CB  ALA A 203    12828  11317  12164  -2668   -869   1497       C  
ATOM   3109  H   ALA A 203      -2.411 -35.096  -5.502  1.00111.77           H  
ATOM   3110  HA  ALA A 203      -2.298 -36.841  -3.532  1.00111.17           H  
ATOM   3111  HB1 ALA A 203      -1.638 -37.224  -6.250  1.00114.67           H  
ATOM   3112  HB2 ALA A 203      -1.839 -38.402  -5.203  1.00114.67           H  
ATOM   3113  HB3 ALA A 203      -3.074 -37.498  -5.629  1.00114.67           H  
ATOM   3114  N   SER A 204       0.398 -35.562  -4.497  1.00122.74           N  
ANISOU 3114  N   SER A 204    16210  14746  15680  -2959  -1124   1670       N  
ATOM   3115  CA  SER A 204       1.849 -35.457  -4.339  1.00119.87           C  
ANISOU 3115  CA  SER A 204    15701  14480  15364  -3082  -1151   1769       C  
ATOM   3116  C   SER A 204       2.513 -36.818  -4.558  1.00118.85           C  
ANISOU 3116  C   SER A 204    15361  14529  15269  -3055  -1000   1789       C  
ATOM   3117  O   SER A 204       2.420 -37.389  -5.645  1.00126.04           O  
ANISOU 3117  O   SER A 204    16193  15541  16156  -3027   -856   1812       O  
ATOM   3118  CB  SER A 204       2.197 -34.884  -2.961  1.00118.05           C  
ANISOU 3118  CB  SER A 204    15543  14150  15161  -3121  -1318   1749       C  
ATOM   3119  OG  SER A 204       1.805 -35.767  -1.926  1.00116.55           O  
ANISOU 3119  OG  SER A 204    15354  13943  14986  -3019  -1308   1652       O  
ATOM   3120  H   SER A 204       0.057 -34.911  -4.944  1.00147.29           H  
ATOM   3121  HA  SER A 204       2.194 -34.847  -5.010  1.00143.84           H  
ATOM   3122  HB2 SER A 204       3.156 -34.746  -2.910  1.00141.66           H  
ATOM   3123  HB3 SER A 204       1.735 -34.040  -2.845  1.00141.66           H  
ATOM   3124  HG  SER A 204       0.976 -35.896  -1.957  1.00139.86           H  
ATOM   3125  N   GLY A 205       3.180 -37.329  -3.525  1.00 73.29           N  
ANISOU 3125  N   GLY A 205     9502   8794   9549  -3059  -1034   1781       N  
ATOM   3126  CA  GLY A 205       3.633 -38.707  -3.501  1.00 75.47           C  
ANISOU 3126  CA  GLY A 205     9597   9217   9862  -3004   -901   1775       C  
ATOM   3127  C   GLY A 205       3.172 -39.375  -2.219  1.00 81.83           C  
ANISOU 3127  C   GLY A 205    10441   9962  10689  -2915   -943   1675       C  
ATOM   3128  O   GLY A 205       3.977 -39.941  -1.479  1.00 80.28           O  
ANISOU 3128  O   GLY A 205    10123   9836  10545  -2928   -955   1691       O  
ATOM   3129  H   GLY A 205       3.384 -36.885  -2.817  1.00 87.94           H  
ATOM   3130  HA2 GLY A 205       3.267 -39.191  -4.258  1.00 90.56           H  
ATOM   3131  HA3 GLY A 205       4.601 -38.740  -3.544  1.00 90.56           H  
ATOM   3132  N   VAL A 206       1.871 -39.298  -1.953  1.00 76.60           N  
ANISOU 3132  N   VAL A 206     9948   9173   9986  -2822   -967   1575       N  
ATOM   3133  CA  VAL A 206       1.298 -39.885  -0.747  1.00 72.78           C  
ANISOU 3133  CA  VAL A 206     9519   8622   9512  -2731  -1006   1475       C  
ATOM   3134  C   VAL A 206       1.245 -41.400  -0.877  1.00 64.73           C  
ANISOU 3134  C   VAL A 206     8358   7721   8516  -2644   -859   1446       C  
ATOM   3135  O   VAL A 206       0.771 -41.930  -1.883  1.00 71.86           O  
ANISOU 3135  O   VAL A 206     9232   8679   9392  -2593   -730   1441       O  
ATOM   3136  CB  VAL A 206      -0.129 -39.345  -0.469  1.00 60.71           C  
ANISOU 3136  CB  VAL A 206     8212   6926   7929  -2646  -1067   1379       C  
ATOM   3137  CG1 VAL A 206      -0.792 -40.102   0.679  1.00 60.45           C  
ANISOU 3137  CG1 VAL A 206     8226   6841   7901  -2538  -1081   1277       C  
ATOM   3138  CG2 VAL A 206      -0.086 -37.861  -0.150  1.00 59.33           C  
ANISOU 3138  CG2 VAL A 206     8188   6622   7732  -2718  -1226   1397       C  
ATOM   3139  H   VAL A 206       1.296 -38.908  -2.460  1.00 91.92           H  
ATOM   3140  HA  VAL A 206       1.859 -39.665   0.013  1.00 87.33           H  
ATOM   3141  HB  VAL A 206      -0.673 -39.465  -1.263  1.00 72.85           H  
ATOM   3142 HG11 VAL A 206      -0.255 -39.995   1.479  1.00 72.54           H  
ATOM   3143 HG12 VAL A 206      -1.680 -39.739   0.825  1.00 72.54           H  
ATOM   3144 HG13 VAL A 206      -0.853 -41.041   0.444  1.00 72.54           H  
ATOM   3145 HG21 VAL A 206       0.292 -37.386  -0.907  1.00 71.20           H  
ATOM   3146 HG22 VAL A 206      -0.988 -37.548   0.019  1.00 71.20           H  
ATOM   3147 HG23 VAL A 206       0.465 -37.723   0.636  1.00 71.20           H  
ATOM   3148  N   ASP A 207       1.737 -42.091   0.145  1.00 61.88           N  
ANISOU 3148  N   ASP A 207     7913   7396   8201  -2628   -884   1429       N  
ATOM   3149  CA  ASP A 207       1.690 -43.544   0.173  1.00 66.11           C  
ANISOU 3149  CA  ASP A 207     8319   8035   8766  -2542   -759   1398       C  
ATOM   3150  C   ASP A 207       0.364 -43.999   0.767  1.00 66.64           C  
ANISOU 3150  C   ASP A 207     8518   7997   8805  -2426   -765   1286       C  
ATOM   3151  O   ASP A 207       0.326 -44.624   1.828  1.00 62.08           O  
ANISOU 3151  O   ASP A 207     7925   7407   8255  -2381   -799   1240       O  
ATOM   3152  CB  ASP A 207       2.861 -44.103   0.979  1.00 63.34           C  
ANISOU 3152  CB  ASP A 207     7805   7778   8482  -2576   -785   1439       C  
ATOM   3153  CG  ASP A 207       3.067 -45.593   0.758  1.00 69.33           C  
ANISOU 3153  CG  ASP A 207     8389   8675   9277  -2495   -639   1432       C  
ATOM   3154  OD1 ASP A 207       2.120 -46.274   0.309  1.00 69.30           O  
ANISOU 3154  OD1 ASP A 207     8421   8666   9244  -2403   -541   1373       O  
ATOM   3155  OD2 ASP A 207       4.182 -46.084   1.030  1.00 76.58           O  
ANISOU 3155  OD2 ASP A 207     9133   9709  10254  -2522   -624   1488       O  
ATOM   3156  H   ASP A 207       2.105 -41.738   0.838  1.00 74.25           H  
ATOM   3157  HA  ASP A 207       1.752 -43.885  -0.733  1.00 79.33           H  
ATOM   3158  HB2 ASP A 207       3.675 -43.645   0.714  1.00 76.00           H  
ATOM   3159  HB3 ASP A 207       2.692 -43.960   1.924  1.00 76.00           H  
ATOM   3160  N   ALA A 208      -0.718 -43.687   0.056  1.00 70.60           N  
ANISOU 3160  N   ALA A 208     9146   8428   9251  -2378   -730   1248       N  
ATOM   3161  CA  ALA A 208      -2.061 -44.094   0.447  1.00 68.48           C  
ANISOU 3161  CA  ALA A 208     9002   8064   8952  -2262   -722   1149       C  
ATOM   3162  C   ALA A 208      -2.084 -45.579   0.786  1.00 64.56           C  
ANISOU 3162  C   ALA A 208     8386   7652   8490  -2189   -631   1118       C  
ATOM   3163  O   ALA A 208      -2.419 -45.951   1.905  1.00 65.22           O  
ANISOU 3163  O   ALA A 208     8512   7682   8589  -2138   -686   1060       O  
ATOM   3164  CB  ALA A 208      -3.049 -43.788  -0.672  1.00 68.82           C  
ANISOU 3164  CB  ALA A 208     9142   8067   8938  -2222   -662   1135       C  
ATOM   3165  H   ALA A 208      -0.696 -43.231  -0.673  1.00 84.72           H  
ATOM   3166  HA  ALA A 208      -2.330 -43.597   1.235  1.00 82.17           H  
ATOM   3167  HB1 ALA A 208      -2.784 -44.274  -1.468  1.00 82.58           H  
ATOM   3168  HB2 ALA A 208      -3.936 -44.065  -0.394  1.00 82.58           H  
ATOM   3169  HB3 ALA A 208      -3.040 -42.834  -0.848  1.00 82.58           H  
ATOM   3170  N   LYS A 209      -1.701 -46.408  -0.183  1.00 59.60           N  
ANISOU 3170  N   LYS A 209     7612   7160   7873  -2183   -492   1160       N  
ATOM   3171  CA  LYS A 209      -1.642 -47.862  -0.021  1.00 61.40           C  
ANISOU 3171  CA  LYS A 209     7710   7484   8135  -2112   -392   1140       C  
ATOM   3172  C   LYS A 209      -1.180 -48.277   1.372  1.00 63.33           C  
ANISOU 3172  C   LYS A 209     7903   7726   8435  -2097   -470   1118       C  
ATOM   3173  O   LYS A 209      -1.877 -49.009   2.072  1.00 69.02           O  
ANISOU 3173  O   LYS A 209     8661   8417   9149  -1962   -461   1026       O  
ATOM   3174  CB  LYS A 209      -0.705 -48.456  -1.076  1.00 66.18           C  
ANISOU 3174  CB  LYS A 209     8128   8261   8756  -2135   -258   1212       C  
ATOM   3175  CG  LYS A 209      -0.595 -49.974  -1.061  1.00 67.92           C  
ANISOU 3175  CG  LYS A 209     8213   8593   9001  -2003   -137   1166       C  
ATOM   3176  CD  LYS A 209       0.272 -50.458  -2.212  1.00 80.07           C  
ANISOU 3176  CD  LYS A 209     9586  10296  10541  -2022      3   1237       C  
ATOM   3177  CE  LYS A 209       0.417 -51.968  -2.217  1.00 84.13           C  
ANISOU 3177  CE  LYS A 209     9976  10912  11078  -1869    122   1180       C  
ATOM   3178  NZ  LYS A 209       1.277 -52.415  -3.346  1.00 83.19           N  
ANISOU 3178  NZ  LYS A 209     9702  10954  10952  -1875    265   1244       N  
ATOM   3179  H   LYS A 209      -1.464 -46.145  -0.966  1.00 71.52           H  
ATOM   3180  HA  LYS A 209      -2.528 -48.231  -0.165  1.00 73.68           H  
ATOM   3181  HB2 LYS A 209      -1.024 -48.195  -1.954  1.00 79.41           H  
ATOM   3182  HB3 LYS A 209       0.185 -48.097  -0.934  1.00 79.41           H  
ATOM   3183  HG2 LYS A 209      -0.188 -50.260  -0.228  1.00 81.51           H  
ATOM   3184  HG3 LYS A 209      -1.478 -50.362  -1.157  1.00 81.51           H  
ATOM   3185  HD2 LYS A 209      -0.134 -50.191  -3.051  1.00 96.08           H  
ATOM   3186  HD3 LYS A 209       1.157 -50.070  -2.129  1.00 96.08           H  
ATOM   3187  HE2 LYS A 209       0.828 -52.255  -1.387  1.00100.96           H  
ATOM   3188  HE3 LYS A 209      -0.458 -52.375  -2.318  1.00100.96           H  
ATOM   3189  HZ1 LYS A 209       2.087 -52.054  -3.273  1.00 99.83           H  
ATOM   3190  HZ2 LYS A 209       1.353 -53.302  -3.338  1.00 99.83           H  
ATOM   3191  HZ3 LYS A 209       0.917 -52.163  -4.120  1.00 99.83           H  
ATOM   3192  N   ALA A 210      -0.020 -47.776   1.782  1.00 56.93           N  
ANISOU 3192  N   ALA A 210     7015   6953   7663  -2193   -545   1182       N  
ATOM   3193  CA  ALA A 210       0.545 -48.118   3.082  1.00 56.01           C  
ANISOU 3193  CA  ALA A 210     6842   6842   7598  -2198   -631   1176       C  
ATOM   3194  C   ALA A 210      -0.324 -47.630   4.243  1.00 49.73           C  
ANISOU 3194  C   ALA A 210     6238   5885   6771  -2169   -761   1096       C  
ATOM   3195  O   ALA A 210      -0.488 -48.339   5.232  1.00 55.60           O  
ANISOU 3195  O   ALA A 210     6972   6623   7531  -2095   -784   1045       O  
ATOM   3196  CB  ALA A 210       1.961 -47.563   3.204  1.00 63.50           C  
ANISOU 3196  CB  ALA A 210     7680   7860   8587  -2305   -691   1263       C  
ATOM   3197  H   ALA A 210       0.462 -47.232   1.322  1.00 68.32           H  
ATOM   3198  HA  ALA A 210       0.604 -49.084   3.148  1.00 67.22           H  
ATOM   3199  HB1 ALA A 210       1.931 -46.598   3.110  1.00 76.20           H  
ATOM   3200  HB2 ALA A 210       2.320 -47.800   4.073  1.00 76.20           H  
ATOM   3201  HB3 ALA A 210       2.512 -47.946   2.503  1.00 76.20           H  
ATOM   3202  N   ILE A 211      -0.891 -46.434   4.118  1.00 43.26           N  
ANISOU 3202  N   ILE A 211     5597   4944   5897  -2193   -835   1075       N  
ATOM   3203  CA  ILE A 211      -1.680 -45.849   5.202  1.00 39.63           C  
ANISOU 3203  CA  ILE A 211     5329   4332   5398  -2155   -957    998       C  
ATOM   3204  C   ILE A 211      -3.034 -46.540   5.343  1.00 42.46           C  
ANISOU 3204  C   ILE A 211     5774   4634   5723  -2021   -897    909       C  
ATOM   3205  O   ILE A 211      -3.478 -46.817   6.456  1.00 39.00           O  
ANISOU 3205  O   ILE A 211     5401   4149   5268  -1932   -944    836       O  
ATOM   3206  CB  ILE A 211      -1.877 -44.329   4.994  1.00 36.33           C  
ANISOU 3206  CB  ILE A 211     5072   3803   4930  -2206  -1052   1002       C  
ATOM   3207  CG1 ILE A 211      -0.555 -43.597   5.226  1.00 39.77           C  
ANISOU 3207  CG1 ILE A 211     5446   4271   5393  -2332  -1147   1081       C  
ATOM   3208  CG2 ILE A 211      -2.927 -43.765   5.953  1.00 37.52           C  
ANISOU 3208  CG2 ILE A 211     5437   3794   5025  -2133  -1150    908       C  
ATOM   3209  CD1 ILE A 211      -0.304 -42.458   4.268  1.00 48.71           C  
ANISOU 3209  CD1 ILE A 211     6618   5385   6504  -2414  -1165   1142       C  
ATOM   3210  H   ILE A 211      -0.834 -45.939   3.417  1.00 51.92           H  
ATOM   3211  HA  ILE A 211      -1.199 -45.972   6.035  1.00 47.56           H  
ATOM   3212  HB  ILE A 211      -2.167 -44.172   4.082  1.00 43.60           H  
ATOM   3213 HG12 ILE A 211      -0.555 -43.233   6.125  1.00 47.72           H  
ATOM   3214 HG13 ILE A 211       0.173 -44.231   5.128  1.00 47.72           H  
ATOM   3215 HG21 ILE A 211      -2.637 -43.920   6.866  1.00 45.02           H  
ATOM   3216 HG22 ILE A 211      -3.022 -42.813   5.793  1.00 45.02           H  
ATOM   3217 HG23 ILE A 211      -3.772 -44.214   5.794  1.00 45.02           H  
ATOM   3218 HD11 ILE A 211      -1.016 -41.806   4.360  1.00 58.45           H  
ATOM   3219 HD12 ILE A 211       0.549 -42.049   4.481  1.00 58.45           H  
ATOM   3220 HD13 ILE A 211      -0.288 -42.805   3.362  1.00 58.45           H  
ATOM   3221  N   LEU A 212      -3.687 -46.816   4.218  1.00 57.13           N  
ANISOU 3221  N   LEU A 212     7627   6522   7557  -1961   -779    900       N  
ATOM   3222  CA  LEU A 212      -5.001 -47.446   4.237  1.00 49.33           C  
ANISOU 3222  CA  LEU A 212     6708   5506   6529  -1790   -707    806       C  
ATOM   3223  C   LEU A 212      -4.910 -48.949   4.506  1.00 47.91           C  
ANISOU 3223  C   LEU A 212     6386   5439   6379  -1676   -608    772       C  
ATOM   3224  O   LEU A 212      -5.762 -49.501   5.202  1.00 52.20           O  
ANISOU 3224  O   LEU A 212     6981   5950   6902  -1549   -599    696       O  
ATOM   3225  CB  LEU A 212      -5.756 -47.187   2.924  1.00 46.91           C  
ANISOU 3225  CB  LEU A 212     6455   5185   6184  -1773   -630    811       C  
ATOM   3226  CG  LEU A 212      -6.245 -45.764   2.593  1.00 48.33           C  
ANISOU 3226  CG  LEU A 212     6809   5230   6325  -1845   -719    828       C  
ATOM   3227  CD1 LEU A 212      -6.609 -44.956   3.832  1.00 37.34           C  
ANISOU 3227  CD1 LEU A 212     5576   3698   4913  -1833   -857    777       C  
ATOM   3228  CD2 LEU A 212      -5.234 -44.996   1.763  1.00 54.87           C  
ANISOU 3228  CD2 LEU A 212     7578   6106   7162  -1978   -731    919       C  
ATOM   3229  H   LEU A 212      -3.389 -46.648   3.429  1.00 68.55           H  
ATOM   3230  HA  LEU A 212      -5.520 -47.052   4.955  1.00 59.20           H  
ATOM   3231  HB2 LEU A 212      -5.176 -47.456   2.195  1.00 56.29           H  
ATOM   3232  HB3 LEU A 212      -6.542 -47.756   2.923  1.00 56.29           H  
ATOM   3233  HG  LEU A 212      -7.051 -45.841   2.059  1.00 58.00           H  
ATOM   3234 HD11 LEU A 212      -5.826 -44.880   4.400  1.00 44.80           H  
ATOM   3235 HD12 LEU A 212      -6.908 -44.075   3.558  1.00 44.80           H  
ATOM   3236 HD13 LEU A 212      -7.320 -45.413   4.309  1.00 44.80           H  
ATOM   3237 HD21 LEU A 212      -5.084 -45.471   0.930  1.00 65.84           H  
ATOM   3238 HD22 LEU A 212      -5.584 -44.110   1.580  1.00 65.84           H  
ATOM   3239 HD23 LEU A 212      -4.404 -44.929   2.260  1.00 65.84           H  
ATOM   3240  N   SER A 213      -3.890 -49.613   3.967  1.00 67.48           N  
ANISOU 3240  N   SER A 213     8686   8049   8905  -1717   -534    831       N  
ATOM   3241  CA  SER A 213      -3.753 -51.060   4.154  1.00 62.29           C  
ANISOU 3241  CA  SER A 213     7895   7493   8281  -1605   -442    802       C  
ATOM   3242  C   SER A 213      -3.186 -51.458   5.513  1.00 61.20           C  
ANISOU 3242  C   SER A 213     7705   7366   8181  -1595   -517    794       C  
ATOM   3243  O   SER A 213      -3.393 -52.587   5.957  1.00 72.65           O  
ANISOU 3243  O   SER A 213     9096   8860   9649  -1480   -466    752       O  
ATOM   3244  CB  SER A 213      -2.879 -51.671   3.059  1.00 61.15           C  
ANISOU 3244  CB  SER A 213     7578   7486   8169  -1632   -326    862       C  
ATOM   3245  OG  SER A 213      -3.527 -51.607   1.801  1.00 67.87           O  
ANISOU 3245  OG  SER A 213     8473   8339   8974  -1609   -237    854       O  
ATOM   3246  H   SER A 213      -3.268 -49.255   3.493  1.00 80.98           H  
ATOM   3247  HA  SER A 213      -4.633 -51.461   4.080  1.00 74.75           H  
ATOM   3248  HB2 SER A 213      -2.045 -51.179   3.010  1.00 73.38           H  
ATOM   3249  HB3 SER A 213      -2.703 -52.600   3.277  1.00 73.38           H  
ATOM   3250  HG  SER A 213      -3.037 -51.946   1.208  1.00 81.44           H  
ATOM   3251  N   ALA A 214      -2.468 -50.547   6.166  1.00 56.62           N  
ANISOU 3251  N   ALA A 214     7154   6746   7615  -1718   -644    840       N  
ATOM   3252  CA  ALA A 214      -1.811 -50.864   7.434  1.00 62.11           C  
ANISOU 3252  CA  ALA A 214     7798   7458   8345  -1726   -729    843       C  
ATOM   3253  C   ALA A 214      -2.815 -51.385   8.457  1.00 60.65           C  
ANISOU 3253  C   ALA A 214     7711   7211   8120  -1587   -744    750       C  
ATOM   3254  O   ALA A 214      -4.001 -51.073   8.386  1.00 70.09           O  
ANISOU 3254  O   ALA A 214     9052   8321   9258  -1516   -733    688       O  
ATOM   3255  CB  ALA A 214      -1.074 -49.647   7.982  1.00 67.18           C  
ANISOU 3255  CB  ALA A 214     8497   8037   8993  -1886   -885    897       C  
ATOM   3256  H   ALA A 214      -2.346 -49.739   5.898  1.00 67.95           H  
ATOM   3257  HA  ALA A 214      -1.155 -51.562   7.280  1.00 74.54           H  
ATOM   3258  HB1 ALA A 214      -1.712 -48.931   8.126  1.00 80.62           H  
ATOM   3259  HB2 ALA A 214      -0.649 -49.886   8.820  1.00 80.62           H  
ATOM   3260  HB3 ALA A 214      -0.404 -49.368   7.338  1.00 80.62           H  
ATOM   3261  N   ARG A 215      -2.334 -52.189   9.399  1.00 71.96           N  
ANISOU 3261  N   ARG A 215     9059   8695   9585  -1547   -767    748       N  
ATOM   3262  CA  ARG A 215      -3.204 -52.812  10.390  1.00 76.05           C  
ANISOU 3262  CA  ARG A 215     9651   9176  10069  -1417   -773    673       C  
ATOM   3263  C   ARG A 215      -3.286 -51.980  11.659  1.00 75.35           C  
ANISOU 3263  C   ARG A 215     9707   8991   9932  -1453   -920    648       C  
ATOM   3264  O   ARG A 215      -2.598 -52.245  12.646  1.00 71.60           O  
ANISOU 3264  O   ARG A 215     9187   8542   9477  -1476   -997    665       O  
ATOM   3265  CB  ARG A 215      -2.725 -54.225  10.706  1.00 88.41           C  
ANISOU 3265  CB  ARG A 215    11057  10846  11690  -1340   -713    684       C  
ATOM   3266  CG  ARG A 215      -2.946 -55.192   9.559  1.00 93.62           C  
ANISOU 3266  CG  ARG A 215    11613  11579  12378  -1262   -562    680       C  
ATOM   3267  CD  ARG A 215      -2.825 -56.630  10.017  1.00 98.39           C  
ANISOU 3267  CD  ARG A 215    12108  12251  13025  -1153   -511    667       C  
ATOM   3268  NE  ARG A 215      -1.495 -56.933  10.540  1.00105.06           N  
ANISOU 3268  NE  ARG A 215    12810  13172  13935  -1208   -560    730       N  
ATOM   3269  CZ  ARG A 215      -0.467 -57.338   9.800  1.00107.46           C  
ANISOU 3269  CZ  ARG A 215    12945  13579  14306  -1239   -499    789       C  
ATOM   3270  NH1 ARG A 215      -0.597 -57.494   8.488  1.00110.31           N  
ANISOU 3270  NH1 ARG A 215    13267  13978  14667  -1221   -382    790       N  
ATOM   3271  NH2 ARG A 215       0.702 -57.588  10.375  1.00103.19           N  
ANISOU 3271  NH2 ARG A 215    12273  13107  13828  -1284   -555    851       N  
ATOM   3272  H   ARG A 215      -1.502 -52.392   9.486  1.00 86.35           H  
ATOM   3273  HA  ARG A 215      -4.098 -52.878  10.021  1.00 91.26           H  
ATOM   3274  HB2 ARG A 215      -1.774 -54.200  10.898  1.00106.10           H  
ATOM   3275  HB3 ARG A 215      -3.211 -54.558  11.477  1.00106.10           H  
ATOM   3276  HG2 ARG A 215      -3.836 -55.061   9.198  1.00112.34           H  
ATOM   3277  HG3 ARG A 215      -2.278 -55.034   8.874  1.00112.34           H  
ATOM   3278  HD2 ARG A 215      -3.472 -56.795  10.721  1.00118.07           H  
ATOM   3279  HD3 ARG A 215      -2.995 -57.218   9.264  1.00118.07           H  
ATOM   3280  HE  ARG A 215      -1.369 -56.843  11.386  1.00126.07           H  
ATOM   3281 HH11 ARG A 215      -1.353 -57.334   8.109  1.00132.37           H  
ATOM   3282 HH12 ARG A 215       0.073 -57.756   8.017  1.00132.37           H  
ATOM   3283 HH21 ARG A 215       0.793 -57.488  11.224  1.00123.83           H  
ATOM   3284 HH22 ARG A 215       1.368 -57.849   9.899  1.00123.83           H  
ATOM   3285  N   LEU A 216      -4.141 -50.966  11.606  1.00 64.08           N  
ANISOU 3285  N   LEU A 216     8457   7450   8439  -1455   -960    606       N  
ATOM   3286  CA  LEU A 216      -4.369 -50.065  12.723  1.00 64.17           C  
ANISOU 3286  CA  LEU A 216     8641   7352   8389  -1475  -1095    567       C  
ATOM   3287  C   LEU A 216      -5.863 -49.776  12.787  1.00 61.83           C  
ANISOU 3287  C   LEU A 216     8509   6967   8016  -1353  -1060    486       C  
ATOM   3288  O   LEU A 216      -6.621 -50.221  11.923  1.00 65.40           O  
ANISOU 3288  O   LEU A 216     8933   7444   8472  -1276   -944    472       O  
ATOM   3289  CB  LEU A 216      -3.571 -48.773  12.524  1.00 65.67           C  
ANISOU 3289  CB  LEU A 216     8885   7478   8587  -1645  -1215    619       C  
ATOM   3290  CG  LEU A 216      -2.050 -48.956  12.468  1.00 65.09           C  
ANISOU 3290  CG  LEU A 216     8638   7499   8595  -1780  -1259    713       C  
ATOM   3291  CD1 LEU A 216      -1.399 -47.920  11.565  1.00 62.16           C  
ANISOU 3291  CD1 LEU A 216     8260   7105   8252  -1943  -1302    789       C  
ATOM   3292  CD2 LEU A 216      -1.456 -48.892  13.867  1.00 65.90           C  
ANISOU 3292  CD2 LEU A 216     8769   7581   8687  -1817  -1399    711       C  
ATOM   3293  H   LEU A 216      -4.613 -50.776  10.912  1.00 76.89           H  
ATOM   3294  HA  LEU A 216      -4.091 -50.485  13.552  1.00 77.00           H  
ATOM   3295  HB2 LEU A 216      -3.848 -48.364  11.689  1.00 78.80           H  
ATOM   3296  HB3 LEU A 216      -3.767 -48.172  13.260  1.00 78.80           H  
ATOM   3297  HG  LEU A 216      -1.855 -49.832  12.103  1.00 78.11           H  
ATOM   3298 HD11 LEU A 216      -1.594 -47.035  11.909  1.00 74.59           H  
ATOM   3299 HD12 LEU A 216      -0.441 -48.068  11.556  1.00 74.59           H  
ATOM   3300 HD13 LEU A 216      -1.757 -48.014  10.669  1.00 74.59           H  
ATOM   3301 HD21 LEU A 216      -1.844 -49.599  14.406  1.00 79.08           H  
ATOM   3302 HD22 LEU A 216      -0.495 -49.010  13.807  1.00 79.08           H  
ATOM   3303 HD23 LEU A 216      -1.660 -48.028  14.257  1.00 79.08           H  
ATOM   3304  N   SER A 217      -6.290 -49.049  13.814  1.00 41.87           N  
ANISOU 3304  N   SER A 217     6153   4338   5417  -1331  -1161    433       N  
ATOM   3305  CA  SER A 217      -7.682 -48.630  13.919  1.00 41.47           C  
ANISOU 3305  CA  SER A 217     6263   4201   5291  -1214  -1134    360       C  
ATOM   3306  C   SER A 217      -8.088 -47.836  12.683  1.00 46.31           C  
ANISOU 3306  C   SER A 217     6928   4757   5909  -1251  -1105    373       C  
ATOM   3307  O   SER A 217      -7.244 -47.229  12.024  1.00 46.32           O  
ANISOU 3307  O   SER A 217     6899   4751   5950  -1390  -1150    433       O  
ATOM   3308  CB  SER A 217      -7.885 -47.757  15.153  1.00 55.84           C  
ANISOU 3308  CB  SER A 217     8274   5913   7030  -1202  -1261    305       C  
ATOM   3309  OG  SER A 217      -9.197 -47.216  15.166  1.00 58.03           O  
ANISOU 3309  OG  SER A 217     8708   6105   7237  -1088  -1235    239       O  
ATOM   3310  H   SER A 217      -5.793 -48.786  14.464  1.00 50.24           H  
ATOM   3311  HA  SER A 217      -8.255 -49.410  13.991  1.00 49.76           H  
ATOM   3312  HB2 SER A 217      -7.757 -48.297  15.948  1.00 67.01           H  
ATOM   3313  HB3 SER A 217      -7.243 -47.031  15.136  1.00 67.01           H  
ATOM   3314  HG  SER A 217      -9.303 -46.737  15.847  1.00 69.64           H  
ATOM   3315  N   LYS A 218      -9.382 -47.834  12.381  1.00 32.58           N  
ANISOU 3315  N   LYS A 218     5264   2984   4131  -1130  -1033    325       N  
ATOM   3316  CA  LYS A 218      -9.902 -47.077  11.254  1.00 31.15           C  
ANISOU 3316  CA  LYS A 218     5145   2743   3946  -1150  -1010    335       C  
ATOM   3317  C   LYS A 218      -9.651 -45.603  11.492  1.00 34.40           C  
ANISOU 3317  C   LYS A 218     5726   3020   4324  -1240  -1146    331       C  
ATOM   3318  O   LYS A 218      -9.123 -44.899  10.626  1.00 38.53           O  
ANISOU 3318  O   LYS A 218     6250   3512   4877  -1363  -1180    386       O  
ATOM   3319  CB  LYS A 218     -11.400 -47.320  11.106  1.00 28.79           C  
ANISOU 3319  CB  LYS A 218     4905   2426   3607   -992   -925    282       C  
ATOM   3320  CG  LYS A 218     -11.754 -48.720  10.653  1.00 24.70           C  
ANISOU 3320  CG  LYS A 218     4233   2026   3127   -914   -794    291       C  
ATOM   3321  CD  LYS A 218     -13.252 -48.978  10.785  1.00 24.05           C  
ANISOU 3321  CD  LYS A 218     4209   1926   3002   -758   -729    242       C  
ATOM   3322  CE  LYS A 218     -13.617 -50.423  10.492  1.00 33.84           C  
ANISOU 3322  CE  LYS A 218     5304   3274   4278   -684   -616    250       C  
ATOM   3323  NZ  LYS A 218     -15.096 -50.596  10.391  1.00 44.09           N  
ANISOU 3323  NZ  LYS A 218     6649   4559   5547   -554   -555    220       N  
ATOM   3324  H   LYS A 218      -9.982 -48.268  12.818  1.00 39.10           H  
ATOM   3325  HA  LYS A 218      -9.455 -47.346  10.437  1.00 37.38           H  
ATOM   3326  HB2 LYS A 218     -11.827 -47.170  11.964  1.00 34.55           H  
ATOM   3327  HB3 LYS A 218     -11.754 -46.699  10.450  1.00 34.55           H  
ATOM   3328  HG2 LYS A 218     -11.506 -48.828   9.722  1.00 29.64           H  
ATOM   3329  HG3 LYS A 218     -11.283 -49.364  11.205  1.00 29.64           H  
ATOM   3330  HD2 LYS A 218     -13.530 -48.775  11.692  1.00 28.86           H  
ATOM   3331  HD3 LYS A 218     -13.728 -48.413  10.156  1.00 28.86           H  
ATOM   3332  HE2 LYS A 218     -13.221 -50.689   9.647  1.00 40.60           H  
ATOM   3333  HE3 LYS A 218     -13.292 -50.988  11.210  1.00 40.60           H  
ATOM   3334  HZ1 LYS A 218     -15.417 -50.088   9.735  1.00 52.91           H  
ATOM   3335  HZ2 LYS A 218     -15.291 -51.448  10.219  1.00 52.91           H  
ATOM   3336  HZ3 LYS A 218     -15.483 -50.360  11.157  1.00 52.91           H  
ATOM   3337  N   SER A 219     -10.028 -45.147  12.681  1.00 55.75           N  
ANISOU 3337  N   SER A 219     8578   5642   6963  -1178  -1226    268       N  
ATOM   3338  CA  SER A 219      -9.855 -43.758  13.067  1.00 54.75           C  
ANISOU 3338  CA  SER A 219     8640   5369   6794  -1247  -1369    249       C  
ATOM   3339  C   SER A 219      -8.396 -43.349  12.927  1.00 56.70           C  
ANISOU 3339  C   SER A 219     8831   5619   7094  -1446  -1472    323       C  
ATOM   3340  O   SER A 219      -8.089 -42.288  12.388  1.00 62.32           O  
ANISOU 3340  O   SER A 219     9609   6260   7810  -1540  -1540    357       O  
ATOM   3341  CB  SER A 219     -10.321 -43.562  14.507  1.00 57.61           C  
ANISOU 3341  CB  SER A 219     9150   5667   7071  -1144  -1434    166       C  
ATOM   3342  OG  SER A 219     -11.635 -44.067  14.677  1.00 67.46           O  
ANISOU 3342  OG  SER A 219    10419   6939   8275   -959  -1326    110       O  
ATOM   3343  H   SER A 219     -10.393 -45.633  13.290  1.00 66.90           H  
ATOM   3344  HA  SER A 219     -10.391 -43.191  12.490  1.00 65.71           H  
ATOM   3345  HB2 SER A 219      -9.720 -44.037  15.102  1.00 69.13           H  
ATOM   3346  HB3 SER A 219     -10.316 -42.615  14.716  1.00 69.13           H  
ATOM   3347  HG  SER A 219     -11.885 -43.956  15.471  1.00 80.96           H  
ATOM   3348  N   ARG A 220      -7.499 -44.204  13.406  1.00 53.66           N  
ANISOU 3348  N   ARG A 220     8300   5341   6747  -1489  -1471    356       N  
ATOM   3349  CA  ARG A 220      -6.069 -43.923  13.348  1.00 62.99           C  
ANISOU 3349  CA  ARG A 220     9401   6546   7988  -1675  -1567    436       C  
ATOM   3350  C   ARG A 220      -5.573 -43.836  11.906  1.00 60.66           C  
ANISOU 3350  C   ARG A 220     8980   6306   7762  -1783  -1506    525       C  
ATOM   3351  O   ARG A 220      -4.744 -42.987  11.578  1.00 65.75           O  
ANISOU 3351  O   ARG A 220     9607   6955   8419  -1888  -1568    584       O  
ATOM   3352  CB  ARG A 220      -5.284 -44.991  14.110  1.00 60.68           C  
ANISOU 3352  CB  ARG A 220     8956   6373   7728  -1677  -1563    457       C  
ATOM   3353  CG  ARG A 220      -5.472 -44.926  15.615  1.00 70.85           C  
ANISOU 3353  CG  ARG A 220    10372   7606   8942  -1614  -1657    387       C  
ATOM   3354  CD  ARG A 220      -4.661 -46.000  16.330  1.00 70.30           C  
ANISOU 3354  CD  ARG A 220    10146   7657   8909  -1621  -1658    417       C  
ATOM   3355  NE  ARG A 220      -4.801 -45.912  17.781  1.00 64.08           N  
ANISOU 3355  NE  ARG A 220     9488   6818   8041  -1569  -1756    355       N  
ATOM   3356  CZ  ARG A 220      -4.214 -46.735  18.646  1.00 79.04           C  
ANISOU 3356  CZ  ARG A 220    11291   8795   9944  -1564  -1782    371       C  
ATOM   3357  NH1 ARG A 220      -3.440 -47.724  18.217  1.00 88.90           N  
ANISOU 3357  NH1 ARG A 220    12312  10179  11288  -1601  -1717    445       N  
ATOM   3358  NH2 ARG A 220      -4.404 -46.569  19.947  1.00 81.09           N  
ANISOU 3358  NH2 ARG A 220    11691   9002  10115  -1516  -1874    312       N  
ATOM   3359  H   ARG A 220      -7.694 -44.957  13.772  1.00 64.39           H  
ATOM   3360  HA  ARG A 220      -5.900 -43.067  13.774  1.00 75.59           H  
ATOM   3361  HB2 ARG A 220      -5.576 -45.867  13.812  1.00 72.82           H  
ATOM   3362  HB3 ARG A 220      -4.339 -44.878  13.923  1.00 72.82           H  
ATOM   3363  HG2 ARG A 220      -5.177 -44.060  15.937  1.00 85.02           H  
ATOM   3364  HG3 ARG A 220      -6.408 -45.062  15.827  1.00 85.02           H  
ATOM   3365  HD2 ARG A 220      -4.972 -46.875  16.048  1.00 84.36           H  
ATOM   3366  HD3 ARG A 220      -3.723 -45.892  16.109  1.00 84.36           H  
ATOM   3367  HE  ARG A 220      -5.297 -45.286  18.099  1.00 76.89           H  
ATOM   3368 HH11 ARG A 220      -3.313 -47.836  17.374  1.00106.68           H  
ATOM   3369 HH12 ARG A 220      -3.064 -48.252  18.783  1.00106.68           H  
ATOM   3370 HH21 ARG A 220      -4.905 -45.930  20.231  1.00 97.30           H  
ATOM   3371 HH22 ARG A 220      -4.027 -47.100  20.508  1.00 97.30           H  
ATOM   3372  N   ARG A 221      -6.088 -44.714  11.050  1.00 40.98           N  
ANISOU 3372  N   ARG A 221     6370   3908   5291  -1695  -1349    529       N  
ATOM   3373  CA  ARG A 221      -5.716 -44.717   9.639  1.00 38.73           C  
ANISOU 3373  CA  ARG A 221     5973   3686   5058  -1778  -1273    606       C  
ATOM   3374  C   ARG A 221      -6.208 -43.446   8.958  1.00 39.49           C  
ANISOU 3374  C   ARG A 221     6211   3679   5115  -1799  -1309    607       C  
ATOM   3375  O   ARG A 221      -5.476 -42.830   8.184  1.00 41.51           O  
ANISOU 3375  O   ARG A 221     6411   3969   5391  -1899  -1319    678       O  
ATOM   3376  CB  ARG A 221      -6.272 -45.956   8.931  1.00 40.19           C  
ANISOU 3376  CB  ARG A 221     6025   3986   5258  -1657  -1101    593       C  
ATOM   3377  CG  ARG A 221      -5.458 -47.217   9.180  1.00 38.96           C  
ANISOU 3377  CG  ARG A 221     5670   3975   5158  -1647  -1041    621       C  
ATOM   3378  CD  ARG A 221      -5.931 -48.369   8.317  1.00 35.47           C  
ANISOU 3378  CD  ARG A 221     5108   3635   4735  -1544   -880    613       C  
ATOM   3379  NE  ARG A 221      -7.129 -49.010   8.849  1.00 45.44           N  
ANISOU 3379  NE  ARG A 221     6430   4878   5958  -1380   -830    532       N  
ATOM   3380  CZ  ARG A 221      -7.858 -49.902   8.185  1.00 46.16           C  
ANISOU 3380  CZ  ARG A 221     6463   5023   6052  -1277   -707    510       C  
ATOM   3381  NH1 ARG A 221      -8.931 -50.438   8.749  1.00 40.58           N  
ANISOU 3381  NH1 ARG A 221     5807   4299   5313  -1140   -674    447       N  
ATOM   3382  NH2 ARG A 221      -7.518 -50.257   6.952  1.00 45.27           N  
ANISOU 3382  NH2 ARG A 221     6244   4985   5971  -1313   -619    554       N  
ATOM   3383  H   ARG A 221      -6.658 -45.322  11.263  1.00 49.17           H  
ATOM   3384  HA  ARG A 221      -4.749 -44.740   9.568  1.00 46.48           H  
ATOM   3385  HB2 ARG A 221      -7.175 -46.118   9.247  1.00 48.23           H  
ATOM   3386  HB3 ARG A 221      -6.282 -45.793   7.975  1.00 48.23           H  
ATOM   3387  HG2 ARG A 221      -4.527 -47.043   8.970  1.00 46.75           H  
ATOM   3388  HG3 ARG A 221      -5.549 -47.477  10.110  1.00 46.75           H  
ATOM   3389  HD2 ARG A 221      -6.137 -48.036   7.429  1.00 42.57           H  
ATOM   3390  HD3 ARG A 221      -5.229 -49.036   8.267  1.00 42.57           H  
ATOM   3391  HE  ARG A 221      -7.385 -48.792   9.641  1.00 54.53           H  
ATOM   3392 HH11 ARG A 221      -9.157 -50.210   9.547  1.00 48.70           H  
ATOM   3393 HH12 ARG A 221      -9.403 -51.013   8.316  1.00 48.70           H  
ATOM   3394 HH21 ARG A 221      -6.822 -49.912   6.582  1.00 54.32           H  
ATOM   3395 HH22 ARG A 221      -7.992 -50.833   6.524  1.00 54.32           H  
ATOM   3396  N   LEU A 222      -7.444 -43.054   9.254  1.00 36.00           N  
ANISOU 3396  N   LEU A 222     5938   3129   4613  -1682  -1317    528       N  
ATOM   3397  CA  LEU A 222      -7.983 -41.791   8.759  1.00 42.24           C  
ANISOU 3397  CA  LEU A 222     6865   3827   5358  -1665  -1355    517       C  
ATOM   3398  C   LEU A 222      -7.097 -40.631   9.199  1.00 49.16           C  
ANISOU 3398  C   LEU A 222     7805   4654   6220  -1766  -1492    546       C  
ATOM   3399  O   LEU A 222      -6.581 -39.865   8.371  1.00 49.04           O  
ANISOU 3399  O   LEU A 222     7768   4646   6218  -1859  -1513    611       O  
ATOM   3400  CB  LEU A 222      -9.408 -41.585   9.280  1.00 37.62           C  
ANISOU 3400  CB  LEU A 222     6449   3137   4709  -1506  -1352    422       C  
ATOM   3401  CG  LEU A 222     -10.047 -40.212   9.068  1.00 31.89           C  
ANISOU 3401  CG  LEU A 222     5886   2300   3929  -1465  -1411    398       C  
ATOM   3402  CD1 LEU A 222     -10.187 -39.896   7.587  1.00 36.64           C  
ANISOU 3402  CD1 LEU A 222     6436   2930   4554  -1505  -1350    457       C  
ATOM   3403  CD2 LEU A 222     -11.397 -40.167   9.762  1.00 31.41           C  
ANISOU 3403  CD2 LEU A 222     5969   2156   3808  -1291  -1400    303       C  
ATOM   3404  H   LEU A 222      -7.992 -43.503   9.741  1.00 43.20           H  
ATOM   3405  HA  LEU A 222      -8.009 -41.808   7.789  1.00 50.69           H  
ATOM   3406  HB2 LEU A 222      -9.982 -42.236   8.847  1.00 45.15           H  
ATOM   3407  HB3 LEU A 222      -9.404 -41.752  10.236  1.00 45.15           H  
ATOM   3408  HG  LEU A 222      -9.481 -39.534   9.468  1.00 38.26           H  
ATOM   3409 HD11 LEU A 222     -10.747 -40.571   7.172  1.00 43.96           H  
ATOM   3410 HD12 LEU A 222     -10.595 -39.021   7.489  1.00 43.96           H  
ATOM   3411 HD13 LEU A 222      -9.307 -39.899   7.179  1.00 43.96           H  
ATOM   3412 HD21 LEU A 222     -11.269 -40.324  10.710  1.00 37.69           H  
ATOM   3413 HD22 LEU A 222     -11.794 -39.293   9.621  1.00 37.69           H  
ATOM   3414 HD23 LEU A 222     -11.968 -40.855   9.386  1.00 37.69           H  
ATOM   3415  N   GLU A 223      -6.921 -40.518  10.512  1.00 84.46           N  
ANISOU 3415  N   GLU A 223    12357   9073  10659  -1749  -1588    498       N  
ATOM   3416  CA  GLU A 223      -6.119 -39.459  11.105  1.00 84.28           C  
ANISOU 3416  CA  GLU A 223    12414   8994  10616  -1837  -1731    519       C  
ATOM   3417  C   GLU A 223      -4.704 -39.467  10.541  1.00 80.80           C  
ANISOU 3417  C   GLU A 223    11804   8652  10243  -2000  -1747    630       C  
ATOM   3418  O   GLU A 223      -4.090 -38.415  10.371  1.00 88.24           O  
ANISOU 3418  O   GLU A 223    12790   9556  11182  -2094  -1838    680       O  
ATOM   3419  CB  GLU A 223      -6.088 -39.613  12.628  1.00 88.94           C  
ANISOU 3419  CB  GLU A 223    13094   9537  11161  -1791  -1818    453       C  
ATOM   3420  CG  GLU A 223      -7.406 -39.266  13.301  1.00 95.49           C  
ANISOU 3420  CG  GLU A 223    14124  10254  11906  -1629  -1826    344       C  
ATOM   3421  CD  GLU A 223      -7.449 -39.687  14.757  1.00106.31           C  
ANISOU 3421  CD  GLU A 223    15566  11602  13225  -1568  -1882    276       C  
ATOM   3422  OE1 GLU A 223      -6.378 -39.726  15.398  1.00110.05           O  
ANISOU 3422  OE1 GLU A 223    15996  12104  13714  -1668  -1972    311       O  
ATOM   3423  OE2 GLU A 223      -8.555 -39.981  15.259  1.00107.10           O  
ANISOU 3423  OE2 GLU A 223    15765  11660  13268  -1418  -1836    190       O  
ATOM   3424  H   GLU A 223      -7.263 -41.056  11.090  1.00101.35           H  
ATOM   3425  HA  GLU A 223      -6.522 -38.601  10.897  1.00101.14           H  
ATOM   3426  HB2 GLU A 223      -5.877 -40.534  12.845  1.00106.73           H  
ATOM   3427  HB3 GLU A 223      -5.406 -39.025  12.989  1.00106.73           H  
ATOM   3428  HG2 GLU A 223      -7.537 -38.306  13.263  1.00114.59           H  
ATOM   3429  HG3 GLU A 223      -8.127 -39.719  12.837  1.00114.59           H  
ATOM   3430  N   ASN A 224      -4.194 -40.658  10.243  1.00 51.89           N  
ANISOU 3430  N   ASN A 224     7951   5121   6645  -2029  -1656    672       N  
ATOM   3431  CA  ASN A 224      -2.877 -40.791   9.628  1.00 53.86           C  
ANISOU 3431  CA  ASN A 224     8016   5486   6962  -2165  -1646    781       C  
ATOM   3432  C   ASN A 224      -2.871 -40.300   8.191  1.00 49.36           C  
ANISOU 3432  C   ASN A 224     7406   4944   6405  -2212  -1579    842       C  
ATOM   3433  O   ASN A 224      -1.944 -39.609   7.774  1.00 60.54           O  
ANISOU 3433  O   ASN A 224     8775   6386   7842  -2330  -1629    924       O  
ATOM   3434  CB  ASN A 224      -2.409 -42.246   9.669  1.00 58.08           C  
ANISOU 3434  CB  ASN A 224     8352   6157   7559  -2163  -1554    805       C  
ATOM   3435  CG  ASN A 224      -1.505 -42.543  10.856  1.00 60.12           C  
ANISOU 3435  CG  ASN A 224     8560   6445   7838  -2211  -1651    818       C  
ATOM   3436  OD1 ASN A 224      -0.604 -43.376  10.762  1.00 58.58           O  
ANISOU 3436  OD1 ASN A 224     8170   6376   7709  -2260  -1610    880       O  
ATOM   3437  ND2 ASN A 224      -1.733 -41.855  11.973  1.00 65.55           N  
ANISOU 3437  ND2 ASN A 224     9423   7017   8466  -2190  -1780    760       N  
ATOM   3438  H   ASN A 224      -4.591 -41.407  10.386  1.00 62.27           H  
ATOM   3439  HA  ASN A 224      -2.241 -40.258  10.129  1.00 64.63           H  
ATOM   3440  HB2 ASN A 224      -3.184 -42.826   9.730  1.00 69.70           H  
ATOM   3441  HB3 ASN A 224      -1.912 -42.441   8.858  1.00 69.70           H  
ATOM   3442 HD21 ASN A 224      -2.367 -41.275  11.999  1.00 78.66           H  
ATOM   3443 HD22 ASN A 224      -1.245 -41.991  12.668  1.00 78.66           H  
ATOM   3444  N   LEU A 225      -3.897 -40.660   7.427  1.00 43.65           N  
ANISOU 3444  N   LEU A 225     6700   4217   5666  -2123  -1469    807       N  
ATOM   3445  CA  LEU A 225      -3.957 -40.244   6.035  1.00 51.27           C  
ANISOU 3445  CA  LEU A 225     7633   5210   6635  -2161  -1403    862       C  
ATOM   3446  C   LEU A 225      -4.088 -38.731   5.921  1.00 59.89           C  
ANISOU 3446  C   LEU A 225     8883   6188   7685  -2199  -1512    870       C  
ATOM   3447  O   LEU A 225      -3.400 -38.110   5.111  1.00 57.27           O  
ANISOU 3447  O   LEU A 225     8502   5888   7369  -2305  -1525    953       O  
ATOM   3448  CB  LEU A 225      -5.108 -40.922   5.292  1.00 42.37           C  
ANISOU 3448  CB  LEU A 225     6510   4094   5494  -2051  -1274    820       C  
ATOM   3449  CG  LEU A 225      -5.100 -40.600   3.794  1.00 39.95           C  
ANISOU 3449  CG  LEU A 225     6159   3834   5188  -2096  -1200    884       C  
ATOM   3450  CD1 LEU A 225      -4.633 -41.800   2.976  1.00 38.71           C  
ANISOU 3450  CD1 LEU A 225     5806   3828   5072  -2114  -1060    933       C  
ATOM   3451  CD2 LEU A 225      -6.461 -40.098   3.329  1.00 45.43           C  
ANISOU 3451  CD2 LEU A 225     7001   4429   5830  -1998  -1185    830       C  
ATOM   3452  H   LEU A 225      -4.562 -41.139   7.688  1.00 52.38           H  
ATOM   3453  HA  LEU A 225      -3.131 -40.502   5.597  1.00 61.52           H  
ATOM   3454  HB2 LEU A 225      -5.030 -41.883   5.395  1.00 50.84           H  
ATOM   3455  HB3 LEU A 225      -5.950 -40.614   5.663  1.00 50.84           H  
ATOM   3456  HG  LEU A 225      -4.463 -39.884   3.641  1.00 47.94           H  
ATOM   3457 HD11 LEU A 225      -5.237 -42.543   3.134  1.00 46.45           H  
ATOM   3458 HD12 LEU A 225      -4.640 -41.562   2.035  1.00 46.45           H  
ATOM   3459 HD13 LEU A 225      -3.734 -42.039   3.251  1.00 46.45           H  
ATOM   3460 HD21 LEU A 225      -6.685 -39.293   3.822  1.00 54.51           H  
ATOM   3461 HD22 LEU A 225      -6.419 -39.905   2.380  1.00 54.51           H  
ATOM   3462 HD23 LEU A 225      -7.125 -40.785   3.498  1.00 54.51           H  
ATOM   3463  N   ILE A 226      -4.964 -38.134   6.724  1.00 65.70           N  
ANISOU 3463  N   ILE A 226     9807   6789   8365  -2111  -1590    786       N  
ATOM   3464  CA  ILE A 226      -5.168 -36.686   6.641  1.00 66.35           C  
ANISOU 3464  CA  ILE A 226    10050   6754   8406  -2134  -1696    787       C  
ATOM   3465  C   ILE A 226      -3.901 -35.919   7.029  1.00 72.18           C  
ANISOU 3465  C   ILE A 226    10780   7485   9161  -2277  -1824    856       C  
ATOM   3466  O   ILE A 226      -3.720 -34.766   6.635  1.00 73.58           O  
ANISOU 3466  O   ILE A 226    11037   7597   9322  -2343  -1903    897       O  
ATOM   3467  CB  ILE A 226      -6.408 -36.231   7.456  1.00 62.20           C  
ANISOU 3467  CB  ILE A 226     9729   6091   7814  -1991  -1744    678       C  
ATOM   3468  CG1 ILE A 226      -7.672 -36.653   6.696  1.00 60.62           C  
ANISOU 3468  CG1 ILE A 226     9541   5892   7601  -1869  -1625    637       C  
ATOM   3469  CG2 ILE A 226      -6.397 -34.713   7.707  1.00 64.49           C  
ANISOU 3469  CG2 ILE A 226    10192   6250   8061  -2022  -1884    676       C  
ATOM   3470  CD1 ILE A 226      -8.965 -36.067   7.201  1.00 69.87           C  
ANISOU 3470  CD1 ILE A 226    10900   6937   8709  -1723  -1656    545       C  
ATOM   3471  H   ILE A 226      -5.445 -38.532   7.314  1.00 78.83           H  
ATOM   3472  HA  ILE A 226      -5.351 -36.468   5.714  1.00 79.62           H  
ATOM   3473  HB  ILE A 226      -6.398 -36.686   8.313  1.00 74.64           H  
ATOM   3474 HG12 ILE A 226      -7.575 -36.385   5.769  1.00 72.75           H  
ATOM   3475 HG13 ILE A 226      -7.751 -37.618   6.746  1.00 72.75           H  
ATOM   3476 HG21 ILE A 226      -6.401 -34.253   6.853  1.00 77.39           H  
ATOM   3477 HG22 ILE A 226      -7.186 -34.472   8.217  1.00 77.39           H  
ATOM   3478 HG23 ILE A 226      -5.597 -34.482   8.205  1.00 77.39           H  
ATOM   3479 HD11 ILE A 226      -8.917 -35.100   7.143  1.00 83.84           H  
ATOM   3480 HD12 ILE A 226      -9.695 -36.396   6.654  1.00 83.84           H  
ATOM   3481 HD13 ILE A 226      -9.094 -36.338   8.124  1.00 83.84           H  
ATOM   3482  N   ALA A 227      -3.009 -36.570   7.770  1.00 77.06           N  
ANISOU 3482  N   ALA A 227    11293   8173   9813  -2328  -1847    876       N  
ATOM   3483  CA  ALA A 227      -1.732 -35.957   8.121  1.00 76.96           C  
ANISOU 3483  CA  ALA A 227    11248   8171   9824  -2469  -1965    954       C  
ATOM   3484  C   ALA A 227      -0.927 -35.645   6.860  1.00 71.21           C  
ANISOU 3484  C   ALA A 227    10390   7528   9139  -2593  -1928   1070       C  
ATOM   3485  O   ALA A 227      -0.110 -34.724   6.852  1.00 79.71           O  
ANISOU 3485  O   ALA A 227    11485   8579  10222  -2711  -2035   1142       O  
ATOM   3486  CB  ALA A 227      -0.936 -36.863   9.054  1.00 72.90           C  
ANISOU 3486  CB  ALA A 227    10618   7735   9345  -2494  -1982    961       C  
ATOM   3487  H   ALA A 227      -3.118 -37.364   8.081  1.00 92.47           H  
ATOM   3488  HA  ALA A 227      -1.899 -35.122   8.585  1.00 92.36           H  
ATOM   3489  HB1 ALA A 227      -0.770 -37.708   8.608  1.00 87.48           H  
ATOM   3490  HB2 ALA A 227      -0.094 -36.432   9.270  1.00 87.48           H  
ATOM   3491  HB3 ALA A 227      -1.449 -37.012   9.864  1.00 87.48           H  
ATOM   3492  N   GLN A 228      -1.167 -36.408   5.796  1.00 62.70           N  
ANISOU 3492  N   GLN A 228     9187   6551   8086  -2565  -1776   1091       N  
ATOM   3493  CA  GLN A 228      -0.495 -36.176   4.519  1.00 67.64           C  
ANISOU 3493  CA  GLN A 228     9692   7266   8741  -2667  -1720   1197       C  
ATOM   3494  C   GLN A 228      -1.136 -35.025   3.745  1.00 69.49           C  
ANISOU 3494  C   GLN A 228    10068   7402   8932  -2672  -1754   1203       C  
ATOM   3495  O   GLN A 228      -0.501 -34.430   2.875  1.00 69.98           O  
ANISOU 3495  O   GLN A 228    10079   7502   9007  -2780  -1762   1297       O  
ATOM   3496  CB  GLN A 228      -0.512 -37.440   3.652  1.00 69.45           C  
ANISOU 3496  CB  GLN A 228     9744   7642   9004  -2630  -1542   1215       C  
ATOM   3497  CG  GLN A 228       0.124 -38.670   4.288  1.00 79.29           C  
ANISOU 3497  CG  GLN A 228    10830   8998  10299  -2619  -1494   1216       C  
ATOM   3498  CD  GLN A 228       1.545 -38.423   4.760  1.00 77.88           C  
ANISOU 3498  CD  GLN A 228    10549   8878  10166  -2744  -1582   1301       C  
ATOM   3499  OE1 GLN A 228       2.507 -38.810   4.096  1.00 78.70           O  
ANISOU 3499  OE1 GLN A 228    10466   9119  10316  -2816  -1513   1392       O  
ATOM   3500  NE2 GLN A 228       1.684 -37.781   5.914  1.00 68.22           N  
ANISOU 3500  NE2 GLN A 228     9446   7552   8924  -2767  -1736   1274       N  
ATOM   3501  H   GLN A 228      -1.717 -37.069   5.787  1.00 75.24           H  
ATOM   3502  HA  GLN A 228       0.431 -35.942   4.689  1.00 81.16           H  
ATOM   3503  HB2 GLN A 228      -1.434 -37.661   3.447  1.00 83.34           H  
ATOM   3504  HB3 GLN A 228      -0.032 -37.255   2.829  1.00 83.34           H  
ATOM   3505  HG2 GLN A 228      -0.404 -38.936   5.057  1.00 95.15           H  
ATOM   3506  HG3 GLN A 228       0.146 -39.387   3.636  1.00 95.15           H  
ATOM   3507 HE21 GLN A 228       0.988 -37.528   6.352  1.00 81.87           H  
ATOM   3508 HE22 GLN A 228       2.469 -37.618   6.223  1.00 81.87           H  
ATOM   3509  N   LEU A 229      -2.394 -34.722   4.057  1.00 56.12           N  
ANISOU 3509  N   LEU A 229     8548   5587   7187  -2552  -1773   1106       N  
ATOM   3510  CA  LEU A 229      -3.124 -33.657   3.373  1.00 52.57           C  
ANISOU 3510  CA  LEU A 229     8240   5038   6698  -2537  -1807   1103       C  
ATOM   3511  C   LEU A 229      -3.165 -32.384   4.220  1.00 58.91           C  
ANISOU 3511  C   LEU A 229     9231   5687   7463  -2555  -1979   1078       C  
ATOM   3512  O   LEU A 229      -3.977 -32.278   5.138  1.00 55.28           O  
ANISOU 3512  O   LEU A 229     8914   5127   6963  -2443  -2023    979       O  
ATOM   3513  CB  LEU A 229      -4.555 -34.105   3.060  1.00 52.12           C  
ANISOU 3513  CB  LEU A 229     8248   4947   6608  -2383  -1710   1018       C  
ATOM   3514  CG  LEU A 229      -4.736 -35.392   2.250  1.00 47.76           C  
ANISOU 3514  CG  LEU A 229     7539   4527   6082  -2343  -1541   1028       C  
ATOM   3515  CD1 LEU A 229      -6.171 -35.480   1.761  1.00 42.15           C  
ANISOU 3515  CD1 LEU A 229     6919   3761   5333  -2211  -1475    962       C  
ATOM   3516  CD2 LEU A 229      -3.759 -35.478   1.080  1.00 49.52           C  
ANISOU 3516  CD2 LEU A 229     7605   4874   6337  -2467  -1478   1142       C  
ATOM   3517  H   LEU A 229      -2.851 -35.122   4.666  1.00 67.34           H  
ATOM   3518  HA  LEU A 229      -2.680 -33.451   2.535  1.00 63.09           H  
ATOM   3519  HB2 LEU A 229      -5.019 -34.233   3.902  1.00 62.54           H  
ATOM   3520  HB3 LEU A 229      -4.989 -33.394   2.564  1.00 62.54           H  
ATOM   3521  HG  LEU A 229      -4.573 -36.153   2.829  1.00 57.31           H  
ATOM   3522 HD11 LEU A 229      -6.361 -34.710   1.202  1.00 50.58           H  
ATOM   3523 HD12 LEU A 229      -6.280 -36.296   1.248  1.00 50.58           H  
ATOM   3524 HD13 LEU A 229      -6.765 -35.487   2.527  1.00 50.58           H  
ATOM   3525 HD21 LEU A 229      -2.853 -35.458   1.424  1.00 59.43           H  
ATOM   3526 HD22 LEU A 229      -3.914 -36.307   0.600  1.00 59.43           H  
ATOM   3527 HD23 LEU A 229      -3.907 -34.722   0.490  1.00 59.43           H  
ATOM   3528  N   PRO A 230      -2.295 -31.405   3.912  1.00 90.64           N  
ANISOU 3528  N   PRO A 230    13258   9688  11493  -2695  -2078   1169       N  
ATOM   3529  CA  PRO A 230      -2.266 -30.178   4.716  1.00 90.11           C  
ANISOU 3529  CA  PRO A 230    13375   9471  11390  -2720  -2252   1150       C  
ATOM   3530  C   PRO A 230      -3.454 -29.260   4.440  1.00 87.98           C  
ANISOU 3530  C   PRO A 230    13297   9064  11068  -2629  -2286   1092       C  
ATOM   3531  O   PRO A 230      -3.811 -29.040   3.282  1.00 88.26           O  
ANISOU 3531  O   PRO A 230    13313   9117  11104  -2637  -2225   1130       O  
ATOM   3532  CB  PRO A 230      -0.965 -29.507   4.272  1.00 96.38           C  
ANISOU 3532  CB  PRO A 230    14095  10306  12220  -2905  -2331   1280       C  
ATOM   3533  CG  PRO A 230      -0.784 -29.950   2.873  1.00 96.58           C  
ANISOU 3533  CG  PRO A 230    13962  10459  12276  -2948  -2195   1357       C  
ATOM   3534  CD  PRO A 230      -1.319 -31.355   2.809  1.00 89.25           C  
ANISOU 3534  CD  PRO A 230    12926   9626  11358  -2832  -2035   1294       C  
ATOM   3535  HA  PRO A 230      -2.222 -30.386   5.663  1.00108.13           H  
ATOM   3536  HB2 PRO A 230      -1.059 -28.543   4.319  1.00115.66           H  
ATOM   3537  HB3 PRO A 230      -0.231 -29.811   4.829  1.00115.66           H  
ATOM   3538  HG2 PRO A 230      -1.285 -29.368   2.281  1.00115.90           H  
ATOM   3539  HG3 PRO A 230       0.160 -29.935   2.648  1.00115.90           H  
ATOM   3540  HD2 PRO A 230      -1.761 -31.510   1.959  1.00107.09           H  
ATOM   3541  HD3 PRO A 230      -0.606 -31.995   2.960  1.00107.09           H  
ATOM   3542  N   GLY A 231      -4.054 -28.736   5.505  1.00 56.60           N  
ANISOU 3542  N   GLY A 231     9505   4954   7045  -2540  -2383   1002       N  
ATOM   3543  CA  GLY A 231      -5.162 -27.805   5.390  1.00 52.62           C  
ANISOU 3543  CA  GLY A 231     9191   4312   6489  -2444  -2427    943       C  
ATOM   3544  C   GLY A 231      -6.520 -28.478   5.298  1.00 54.56           C  
ANISOU 3544  C   GLY A 231     9459   4558   6711  -2264  -2306    848       C  
ATOM   3545  O   GLY A 231      -7.538 -27.804   5.141  1.00 59.07           O  
ANISOU 3545  O   GLY A 231    10171   5027   7244  -2166  -2325    798       O  
ATOM   3546  H   GLY A 231      -3.831 -28.910   6.317  1.00 67.92           H  
ATOM   3547  HA2 GLY A 231      -5.167 -27.218   6.163  1.00 63.14           H  
ATOM   3548  HA3 GLY A 231      -5.040 -27.260   4.597  1.00 63.14           H  
ATOM   3549  N   GLU A 232      -6.534 -29.805   5.389  1.00 65.18           N  
ANISOU 3549  N   GLU A 232    10665   6020   8083  -2221  -2184    827       N  
ATOM   3550  CA  GLU A 232      -7.776 -30.574   5.386  1.00 65.95           C  
ANISOU 3550  CA  GLU A 232    10770   6126   8161  -2054  -2068    742       C  
ATOM   3551  C   GLU A 232      -8.123 -31.047   6.794  1.00 59.36           C  
ANISOU 3551  C   GLU A 232    10004   5256   7296  -1945  -2087    644       C  
ATOM   3552  O   GLU A 232      -7.272 -31.580   7.506  1.00 60.49           O  
ANISOU 3552  O   GLU A 232    10075   5451   7457  -2006  -2110    656       O  
ATOM   3553  CB  GLU A 232      -7.652 -31.780   4.451  1.00 68.80           C  
ANISOU 3553  CB  GLU A 232    10935   6637   8568  -2072  -1914    785       C  
ATOM   3554  CG  GLU A 232      -7.816 -31.451   2.972  1.00 66.44           C  
ANISOU 3554  CG  GLU A 232    10595   6369   8281  -2118  -1860    854       C  
ATOM   3555  CD  GLU A 232      -9.210 -30.958   2.628  1.00 73.51           C  
ANISOU 3555  CD  GLU A 232    11622   7172   9137  -1987  -1848    796       C  
ATOM   3556  OE1 GLU A 232     -10.185 -31.690   2.898  1.00 76.89           O  
ANISOU 3556  OE1 GLU A 232    12056   7605   9552  -1847  -1768    721       O  
ATOM   3557  OE2 GLU A 232      -9.329 -29.841   2.080  1.00 80.84           O  
ANISOU 3557  OE2 GLU A 232    12642   8023  10049  -2025  -1920    830       O  
ATOM   3558  H   GLU A 232      -5.826 -30.290   5.456  1.00 78.22           H  
ATOM   3559  HA  GLU A 232      -8.499 -30.013   5.065  1.00 79.14           H  
ATOM   3560  HB2 GLU A 232      -6.774 -32.176   4.568  1.00 82.56           H  
ATOM   3561  HB3 GLU A 232      -8.336 -32.427   4.686  1.00 82.56           H  
ATOM   3562  HG2 GLU A 232      -7.184 -30.755   2.732  1.00 79.73           H  
ATOM   3563  HG3 GLU A 232      -7.643 -32.250   2.450  1.00 79.73           H  
ATOM   3564  N   LYS A 233      -9.379 -30.854   7.187  1.00 62.78           N  
ANISOU 3564  N   LYS A 233    10570   5603   7679  -1783  -2075    551       N  
ATOM   3565  CA  LYS A 233      -9.843 -31.265   8.508  1.00 76.97           C  
ANISOU 3565  CA  LYS A 233    12445   7365   9434  -1661  -2084    454       C  
ATOM   3566  C   LYS A 233     -10.444 -32.665   8.461  1.00 78.74           C  
ANISOU 3566  C   LYS A 233    12556   7686   9677  -1565  -1938    417       C  
ATOM   3567  O   LYS A 233     -10.859 -33.139   7.401  1.00 81.36           O  
ANISOU 3567  O   LYS A 233    12794   8081  10040  -1552  -1833    447       O  
ATOM   3568  CB  LYS A 233     -10.872 -30.268   9.049  1.00 84.37           C  
ANISOU 3568  CB  LYS A 233    13594   8160  10303  -1526  -2149    372       C  
ATOM   3569  CG  LYS A 233     -10.293 -28.897   9.366  1.00 90.97           C  
ANISOU 3569  CG  LYS A 233    14571   8881  11112  -1609  -2312    394       C  
ATOM   3570  CD  LYS A 233     -11.357 -27.946   9.893  1.00 89.09           C  
ANISOU 3570  CD  LYS A 233    14543   8504  10804  -1460  -2368    309       C  
ATOM   3571  CE  LYS A 233     -10.773 -26.576  10.210  1.00 92.37           C  
ANISOU 3571  CE  LYS A 233    15110   8795  11190  -1543  -2538    331       C  
ATOM   3572  NZ  LYS A 233     -11.804 -25.609  10.687  1.00 89.28           N  
ANISOU 3572  NZ  LYS A 233    14927   8265  10730  -1393  -2594    247       N  
ATOM   3573  H   LYS A 233      -9.986 -30.484   6.703  1.00 75.33           H  
ATOM   3574  HA  LYS A 233      -9.090 -31.281   9.118  1.00 92.36           H  
ATOM   3575  HB2 LYS A 233     -11.570 -30.149   8.386  1.00101.25           H  
ATOM   3576  HB3 LYS A 233     -11.253 -30.625   9.866  1.00101.25           H  
ATOM   3577  HG2 LYS A 233      -9.605 -28.989  10.043  1.00109.16           H  
ATOM   3578  HG3 LYS A 233      -9.918 -28.513   8.557  1.00109.16           H  
ATOM   3579  HD2 LYS A 233     -12.048 -27.835   9.222  1.00106.91           H  
ATOM   3580  HD3 LYS A 233     -11.736 -28.311  10.708  1.00106.91           H  
ATOM   3581  HE2 LYS A 233     -10.104 -26.670  10.906  1.00110.84           H  
ATOM   3582  HE3 LYS A 233     -10.368 -26.211   9.407  1.00110.84           H  
ATOM   3583  HZ1 LYS A 233     -12.188 -25.915  11.429  1.00107.13           H  
ATOM   3584  HZ2 LYS A 233     -11.425 -24.822  10.861  1.00107.13           H  
ATOM   3585  HZ3 LYS A 233     -12.428 -25.498  10.063  1.00107.13           H  
ATOM   3586  N   LYS A 234     -10.477 -33.320   9.618  1.00 67.26           N  
ANISOU 3586  N   LYS A 234    11116   6240   8200  -1501  -1937    355       N  
ATOM   3587  CA  LYS A 234     -11.051 -34.656   9.738  1.00 61.92           C  
ANISOU 3587  CA  LYS A 234    10345   5644   7537  -1406  -1812    316       C  
ATOM   3588  C   LYS A 234     -12.498 -34.675   9.271  1.00 45.49           C  
ANISOU 3588  C   LYS A 234     8316   3534   5433  -1251  -1727    268       C  
ATOM   3589  O   LYS A 234     -12.911 -35.567   8.533  1.00 43.14           O  
ANISOU 3589  O   LYS A 234     7905   3316   5172  -1222  -1611    285       O  
ATOM   3590  CB  LYS A 234     -10.997 -35.134  11.189  1.00 62.85           C  
ANISOU 3590  CB  LYS A 234    10515   5750   7616  -1344  -1845    247       C  
ATOM   3591  CG  LYS A 234      -9.833 -36.051  11.535  1.00 60.99           C  
ANISOU 3591  CG  LYS A 234    10135   5612   7428  -1458  -1848    291       C  
ATOM   3592  CD  LYS A 234     -10.270 -37.127  12.529  1.00 66.89           C  
ANISOU 3592  CD  LYS A 234    10876   6389   8152  -1351  -1798    220       C  
ATOM   3593  CE  LYS A 234     -10.893 -36.554  13.804  1.00 69.95           C  
ANISOU 3593  CE  LYS A 234    11459   6672   8446  -1227  -1870    125       C  
ATOM   3594  NZ  LYS A 234      -9.885 -35.968  14.729  1.00 70.76           N  
ANISOU 3594  NZ  LYS A 234    11630   6733   8522  -1319  -2011    133       N  
ATOM   3595  H   LYS A 234     -10.169 -33.008  10.357  1.00 80.71           H  
ATOM   3596  HA  LYS A 234     -10.544 -35.276   9.191  1.00 74.30           H  
ATOM   3597  HB2 LYS A 234     -10.936 -34.357  11.766  1.00 75.42           H  
ATOM   3598  HB3 LYS A 234     -11.815 -35.618  11.383  1.00 75.42           H  
ATOM   3599  HG2 LYS A 234      -9.516 -36.488  10.729  1.00 73.19           H  
ATOM   3600  HG3 LYS A 234      -9.122 -35.531  11.940  1.00 73.19           H  
ATOM   3601  HD2 LYS A 234     -10.931 -37.697  12.105  1.00 80.27           H  
ATOM   3602  HD3 LYS A 234      -9.496 -37.652  12.785  1.00 80.27           H  
ATOM   3603  HE2 LYS A 234     -11.520 -35.854  13.562  1.00 83.94           H  
ATOM   3604  HE3 LYS A 234     -11.355 -37.264  14.276  1.00 83.94           H  
ATOM   3605  HZ1 LYS A 234      -9.449 -35.306  14.324  1.00 84.91           H  
ATOM   3606  HZ2 LYS A 234     -10.288 -35.648  15.455  1.00 84.91           H  
ATOM   3607  HZ3 LYS A 234      -9.299 -36.591  14.975  1.00 84.91           H  
ATOM   3608  N   ASN A 235     -13.261 -33.680   9.709  1.00 52.50           N  
ANISOU 3608  N   ASN A 235     9377   4309   6262  -1148  -1788    210       N  
ATOM   3609  CA  ASN A 235     -14.676 -33.591   9.380  1.00 52.19           C  
ANISOU 3609  CA  ASN A 235     9393   4237   6199   -988  -1718    163       C  
ATOM   3610  C   ASN A 235     -14.901 -33.019   7.989  1.00 51.45           C  
ANISOU 3610  C   ASN A 235     9275   4137   6136  -1035  -1703    225       C  
ATOM   3611  O   ASN A 235     -16.041 -32.834   7.566  1.00 52.21           O  
ANISOU 3611  O   ASN A 235     9412   4206   6219   -916  -1655    199       O  
ATOM   3612  CB  ASN A 235     -15.396 -32.731  10.419  1.00 71.47           C  
ANISOU 3612  CB  ASN A 235    12027   6566   8562   -851  -1786     77       C  
ATOM   3613  CG  ASN A 235     -15.424 -33.379  11.789  1.00 76.75           C  
ANISOU 3613  CG  ASN A 235    12728   7246   9185   -770  -1782      7       C  
ATOM   3614  OD1 ASN A 235     -15.745 -34.560  11.923  1.00 77.78           O  
ANISOU 3614  OD1 ASN A 235    12763   7457   9332   -713  -1681     -9       O  
ATOM   3615  ND2 ASN A 235     -15.074 -32.612  12.814  1.00 75.25           N  
ANISOU 3615  ND2 ASN A 235    12681   6974   8937   -766  -1894    -34       N  
ATOM   3616  H   ASN A 235     -12.978 -33.037  10.204  1.00 63.00           H  
ATOM   3617  HA  ASN A 235     -15.063 -34.480   9.406  1.00 62.63           H  
ATOM   3618  HB2 ASN A 235     -14.938 -31.880  10.498  1.00 85.76           H  
ATOM   3619  HB3 ASN A 235     -16.312 -32.591  10.134  1.00 85.76           H  
ATOM   3620 HD21 ASN A 235     -14.847 -31.793  12.680  1.00 90.30           H  
ATOM   3621 HD22 ASN A 235     -15.074 -32.933  13.611  1.00 90.30           H  
ATOM   3622  N   GLY A 236     -13.811 -32.741   7.279  1.00 37.47           N  
ANISOU 3622  N   GLY A 236     7434   2398   4405  -1207  -1744    310       N  
ATOM   3623  CA  GLY A 236     -13.901 -32.242   5.921  1.00 37.69           C  
ANISOU 3623  CA  GLY A 236     7431   2430   4458  -1267  -1729    377       C  
ATOM   3624  C   GLY A 236     -14.592 -33.262   5.042  1.00 43.45           C  
ANISOU 3624  C   GLY A 236     8042   3250   5217  -1211  -1590    390       C  
ATOM   3625  O   GLY A 236     -14.649 -34.445   5.384  1.00 56.84           O  
ANISOU 3625  O   GLY A 236     9647   5022   6929  -1173  -1509    368       O  
ATOM   3626  H   GLY A 236     -13.006 -32.835   7.567  1.00 44.96           H  
ATOM   3627  HA2 GLY A 236     -14.409 -31.416   5.905  1.00 45.22           H  
ATOM   3628  HA3 GLY A 236     -13.012 -32.073   5.571  1.00 45.22           H  
ATOM   3629  N   LEU A 237     -15.125 -32.800   3.916  1.00 48.85           N  
ANISOU 3629  N   LEU A 237     8733   3922   5907  -1208  -1570    427       N  
ATOM   3630  CA  LEU A 237     -15.828 -33.671   2.983  1.00 50.50           C  
ANISOU 3630  CA  LEU A 237     8841   4208   6138  -1158  -1450    444       C  
ATOM   3631  C   LEU A 237     -14.939 -34.845   2.581  1.00 45.00           C  
ANISOU 3631  C   LEU A 237     7975   3642   5483  -1260  -1369    495       C  
ATOM   3632  O   LEU A 237     -15.358 -36.005   2.631  1.00 43.64           O  
ANISOU 3632  O   LEU A 237     7720   3536   5323  -1194  -1273    473       O  
ATOM   3633  CB  LEU A 237     -16.251 -32.880   1.742  1.00 44.28           C  
ANISOU 3633  CB  LEU A 237     8084   3391   5350  -1179  -1461    494       C  
ATOM   3634  CG  LEU A 237     -17.039 -33.655   0.682  1.00 44.97           C  
ANISOU 3634  CG  LEU A 237     8084   3550   5453  -1129  -1350    517       C  
ATOM   3635  CD1 LEU A 237     -18.511 -33.716   1.040  1.00 44.28           C  
ANISOU 3635  CD1 LEU A 237     8063   3414   5347   -944  -1322    450       C  
ATOM   3636  CD2 LEU A 237     -16.851 -33.049  -0.698  1.00 47.24           C  
ANISOU 3636  CD2 LEU A 237     8358   3845   5744  -1225  -1362    598       C  
ATOM   3637  H   LEU A 237     -15.093 -31.977   3.668  1.00 58.62           H  
ATOM   3638  HA  LEU A 237     -16.626 -34.022   3.408  1.00 60.59           H  
ATOM   3639  HB2 LEU A 237     -16.806 -32.138   2.029  1.00 53.14           H  
ATOM   3640  HB3 LEU A 237     -15.451 -32.536   1.314  1.00 53.14           H  
ATOM   3641  HG  LEU A 237     -16.705 -34.565   0.651  1.00 53.97           H  
ATOM   3642 HD11 LEU A 237     -18.859 -32.812   1.096  1.00 53.14           H  
ATOM   3643 HD12 LEU A 237     -18.983 -34.211   0.352  1.00 53.14           H  
ATOM   3644 HD13 LEU A 237     -18.609 -34.162   1.896  1.00 53.14           H  
ATOM   3645 HD21 LEU A 237     -15.909 -33.073  -0.928  1.00 56.68           H  
ATOM   3646 HD22 LEU A 237     -17.363 -33.564  -1.341  1.00 56.68           H  
ATOM   3647 HD23 LEU A 237     -17.165 -32.131  -0.684  1.00 56.68           H  
ATOM   3648  N   PHE A 238     -13.704 -34.534   2.203  1.00 36.90           N  
ANISOU 3648  N   PHE A 238     6894   2650   4477  -1420  -1410    566       N  
ATOM   3649  CA  PHE A 238     -12.752 -35.553   1.782  1.00 37.76           C  
ANISOU 3649  CA  PHE A 238     6835   2887   4626  -1522  -1335    622       C  
ATOM   3650  C   PHE A 238     -12.452 -36.518   2.924  1.00 36.76           C  
ANISOU 3650  C   PHE A 238     6659   2798   4512  -1491  -1315    575       C  
ATOM   3651  O   PHE A 238     -12.418 -37.734   2.730  1.00 40.57           O  
ANISOU 3651  O   PHE A 238     7020   3374   5020  -1480  -1216    580       O  
ATOM   3652  CB  PHE A 238     -11.457 -34.905   1.289  1.00 35.33           C  
ANISOU 3652  CB  PHE A 238     6482   2605   4335  -1694  -1392    709       C  
ATOM   3653  CG  PHE A 238     -10.583 -35.837   0.510  1.00 37.02           C  
ANISOU 3653  CG  PHE A 238     6518   2962   4587  -1793  -1298    780       C  
ATOM   3654  CD1 PHE A 238     -10.904 -36.175  -0.793  1.00 37.48           C  
ANISOU 3654  CD1 PHE A 238     6513   3084   4643  -1797  -1205    823       C  
ATOM   3655  CD2 PHE A 238      -9.447 -36.386   1.081  1.00 43.12           C  
ANISOU 3655  CD2 PHE A 238     7185   3806   5392  -1875  -1301    805       C  
ATOM   3656  CE1 PHE A 238     -10.107 -37.038  -1.515  1.00 34.05           C  
ANISOU 3656  CE1 PHE A 238     5919   2783   4234  -1877  -1111    884       C  
ATOM   3657  CE2 PHE A 238      -8.646 -37.251   0.363  1.00 45.01           C  
ANISOU 3657  CE2 PHE A 238     7254   4182   5665  -1954  -1206    869       C  
ATOM   3658  CZ  PHE A 238      -8.977 -37.575  -0.935  1.00 38.00           C  
ANISOU 3658  CZ  PHE A 238     6310   3357   4770  -1953  -1108    907       C  
ATOM   3659  H   PHE A 238     -13.391 -33.733   2.181  1.00 44.28           H  
ATOM   3660  HA  PHE A 238     -13.133 -36.061   1.049  1.00 45.32           H  
ATOM   3661  HB2 PHE A 238     -11.680 -34.156   0.715  1.00 42.39           H  
ATOM   3662  HB3 PHE A 238     -10.951 -34.594   2.056  1.00 42.39           H  
ATOM   3663  HD1 PHE A 238     -11.666 -35.814  -1.187  1.00 44.98           H  
ATOM   3664  HD2 PHE A 238      -9.221 -36.170   1.957  1.00 51.74           H  
ATOM   3665  HE1 PHE A 238     -10.331 -37.256  -2.391  1.00 40.86           H  
ATOM   3666  HE2 PHE A 238      -7.884 -37.613   0.754  1.00 54.01           H  
ATOM   3667  HZ  PHE A 238      -8.437 -38.157  -1.421  1.00 45.60           H  
ATOM   3668  N   GLY A 239     -12.235 -35.965   4.114  1.00 38.10           N  
ANISOU 3668  N   GLY A 239     6926   2890   4659  -1479  -1414    531       N  
ATOM   3669  CA  GLY A 239     -11.983 -36.766   5.296  1.00 35.42           C  
ANISOU 3669  CA  GLY A 239     6561   2573   4323  -1446  -1413    483       C  
ATOM   3670  C   GLY A 239     -13.131 -37.713   5.569  1.00 43.50           C  
ANISOU 3670  C   GLY A 239     7583   3610   5337  -1293  -1320    418       C  
ATOM   3671  O   GLY A 239     -12.922 -38.890   5.855  1.00 34.20           O  
ANISOU 3671  O   GLY A 239     6302   2508   4185  -1287  -1255    413       O  
ATOM   3672  H   GLY A 239     -12.228 -35.117   4.259  1.00 45.72           H  
ATOM   3673  HA2 GLY A 239     -11.173 -37.285   5.174  1.00 42.50           H  
ATOM   3674  HA3 GLY A 239     -11.868 -36.187   6.066  1.00 42.50           H  
ATOM   3675  N   ASN A 240     -14.350 -37.195   5.472  1.00 35.57           N  
ANISOU 3675  N   ASN A 240     6686   2531   4296  -1167  -1317    373       N  
ATOM   3676  CA  ASN A 240     -15.541 -38.008   5.652  1.00 32.57           C  
ANISOU 3676  CA  ASN A 240     6304   2164   3908  -1014  -1230    321       C  
ATOM   3677  C   ASN A 240     -15.642 -39.087   4.580  1.00 36.90           C  
ANISOU 3677  C   ASN A 240     6708   2815   4498  -1037  -1115    370       C  
ATOM   3678  O   ASN A 240     -16.002 -40.225   4.875  1.00 37.00           O  
ANISOU 3678  O   ASN A 240     6657   2879   4524   -972  -1040    347       O  
ATOM   3679  CB  ASN A 240     -16.792 -37.123   5.651  1.00 31.29           C  
ANISOU 3679  CB  ASN A 240     6275   1909   3704   -879  -1252    277       C  
ATOM   3680  CG  ASN A 240     -17.048 -36.469   7.002  1.00 33.74           C  
ANISOU 3680  CG  ASN A 240     6731   2128   3960   -789  -1330    200       C  
ATOM   3681  OD1 ASN A 240     -16.442 -36.836   8.009  1.00 38.00           O  
ANISOU 3681  OD1 ASN A 240     7274   2677   4489   -809  -1359    172       O  
ATOM   3682  ND2 ASN A 240     -17.957 -35.499   7.030  1.00 32.95           N  
ANISOU 3682  ND2 ASN A 240     6755   1941   3822   -685  -1365    165       N  
ATOM   3683  H   ASN A 240     -14.513 -36.368   5.302  1.00 42.68           H  
ATOM   3684  HA  ASN A 240     -15.491 -38.450   6.514  1.00 39.08           H  
ATOM   3685  HB2 ASN A 240     -16.680 -36.419   4.993  1.00 37.55           H  
ATOM   3686  HB3 ASN A 240     -17.564 -37.666   5.429  1.00 37.55           H  
ATOM   3687 HD21 ASN A 240     -18.366 -35.272   6.308  1.00 39.54           H  
ATOM   3688 HD22 ASN A 240     -18.137 -35.099   7.769  1.00 39.54           H  
ATOM   3689  N   LEU A 241     -15.310 -38.739   3.339  1.00 34.25           N  
ANISOU 3689  N   LEU A 241     6325   2510   4179  -1131  -1103    437       N  
ATOM   3690  CA  LEU A 241     -15.291 -39.728   2.262  1.00 32.46           C  
ANISOU 3690  CA  LEU A 241     5968   2386   3981  -1163   -998    485       C  
ATOM   3691  C   LEU A 241     -14.293 -40.847   2.559  1.00 33.86           C  
ANISOU 3691  C   LEU A 241     6012   2657   4194  -1238   -951    505       C  
ATOM   3692  O   LEU A 241     -14.612 -42.033   2.414  1.00 39.82           O  
ANISOU 3692  O   LEU A 241     6686   3477   4966  -1194   -862    500       O  
ATOM   3693  CB  LEU A 241     -14.960 -39.066   0.921  1.00 29.61           C  
ANISOU 3693  CB  LEU A 241     5588   2043   3620  -1261  -1001    558       C  
ATOM   3694  CG  LEU A 241     -16.078 -38.197   0.336  1.00 31.78           C  
ANISOU 3694  CG  LEU A 241     5967   2242   3867  -1183  -1025    549       C  
ATOM   3695  CD1 LEU A 241     -15.545 -37.292  -0.770  1.00 32.96           C  
ANISOU 3695  CD1 LEU A 241     6123   2391   4011  -1299  -1061    622       C  
ATOM   3696  CD2 LEU A 241     -17.229 -39.060  -0.178  1.00 30.76           C  
ANISOU 3696  CD2 LEU A 241     5803   2149   3737  -1074   -934    534       C  
ATOM   3697  H   LEU A 241     -15.094 -37.943   3.095  1.00 41.10           H  
ATOM   3698  HA  LEU A 241     -16.172 -40.126   2.187  1.00 38.96           H  
ATOM   3699  HB2 LEU A 241     -14.182 -38.499   1.041  1.00 35.53           H  
ATOM   3700  HB3 LEU A 241     -14.761 -39.761   0.275  1.00 35.53           H  
ATOM   3701  HG  LEU A 241     -16.428 -37.627   1.038  1.00 38.14           H  
ATOM   3702 HD11 LEU A 241     -15.172 -37.843  -1.476  1.00 39.56           H  
ATOM   3703 HD12 LEU A 241     -16.275 -36.757  -1.119  1.00 39.56           H  
ATOM   3704 HD13 LEU A 241     -14.858 -36.715  -0.402  1.00 39.56           H  
ATOM   3705 HD21 LEU A 241     -17.587 -39.580   0.558  1.00 36.92           H  
ATOM   3706 HD22 LEU A 241     -17.918 -38.482  -0.542  1.00 36.92           H  
ATOM   3707 HD23 LEU A 241     -16.894 -39.652  -0.870  1.00 36.92           H  
ATOM   3708  N   ILE A 242     -13.089 -40.474   2.982  1.00 30.94           N  
ANISOU 3708  N   ILE A 242     5621   2298   3839  -1352  -1016    532       N  
ATOM   3709  CA  ILE A 242     -12.089 -41.461   3.379  1.00 28.94           C  
ANISOU 3709  CA  ILE A 242     5238   2133   3624  -1422   -985    553       C  
ATOM   3710  C   ILE A 242     -12.638 -42.295   4.533  1.00 29.25           C  
ANISOU 3710  C   ILE A 242     5298   2155   3660  -1314   -971    484       C  
ATOM   3711  O   ILE A 242     -12.519 -43.519   4.534  1.00 27.15           O  
ANISOU 3711  O   ILE A 242     4912   1982   3421  -1294   -888    486       O  
ATOM   3712  CB  ILE A 242     -10.759 -40.794   3.790  1.00 32.87           C  
ANISOU 3712  CB  ILE A 242     5718   2634   4136  -1554  -1077    594       C  
ATOM   3713  CG1 ILE A 242     -10.125 -40.092   2.582  1.00 31.14           C  
ANISOU 3713  CG1 ILE A 242     5458   2451   3925  -1669  -1079    677       C  
ATOM   3714  CG2 ILE A 242      -9.788 -41.819   4.391  1.00 40.69           C  
ANISOU 3714  CG2 ILE A 242     6575   3715   5170  -1610  -1056    610       C  
ATOM   3715  CD1 ILE A 242      -9.389 -41.018   1.598  1.00 30.79           C  
ANISOU 3715  CD1 ILE A 242     5236   2547   3917  -1746   -971    747       C  
ATOM   3716  H   ILE A 242     -12.826 -39.657   3.049  1.00 37.13           H  
ATOM   3717  HA  ILE A 242     -11.913 -42.054   2.632  1.00 34.73           H  
ATOM   3718  HB  ILE A 242     -10.950 -40.124   4.465  1.00 39.44           H  
ATOM   3719 HG12 ILE A 242     -10.825 -39.638   2.087  1.00 37.37           H  
ATOM   3720 HG13 ILE A 242      -9.482 -39.441   2.906  1.00 37.37           H  
ATOM   3721 HG21 ILE A 242      -9.604 -42.505   3.730  1.00 48.83           H  
ATOM   3722 HG22 ILE A 242      -8.966 -41.367   4.637  1.00 48.83           H  
ATOM   3723 HG23 ILE A 242     -10.196 -42.216   5.176  1.00 48.83           H  
ATOM   3724 HD11 ILE A 242     -10.018 -41.668   1.247  1.00 36.95           H  
ATOM   3725 HD12 ILE A 242      -9.026 -40.484   0.874  1.00 36.95           H  
ATOM   3726 HD13 ILE A 242      -8.672 -41.471   2.068  1.00 36.95           H  
ATOM   3727  N   ALA A 243     -13.260 -41.628   5.499  1.00 28.44           N  
ANISOU 3727  N   ALA A 243     5338   1951   3516  -1225  -1044    419       N  
ATOM   3728  CA  ALA A 243     -13.846 -42.307   6.648  1.00 28.40           C  
ANISOU 3728  CA  ALA A 243     5372   1924   3495  -1111  -1033    351       C  
ATOM   3729  C   ALA A 243     -14.931 -43.279   6.192  1.00 34.33           C  
ANISOU 3729  C   ALA A 243     6042   2755   4247   -975   -907    331       C  
ATOM   3730  O   ALA A 243     -15.114 -44.339   6.789  1.00 28.64           O  
ANISOU 3730  O   ALA A 243     5231   2123   3530   -892   -842    301       O  
ATOM   3731  CB  ALA A 243     -14.413 -41.296   7.630  1.00 30.95           C  
ANISOU 3731  CB  ALA A 243     5867   2134   3759  -1021  -1121    282       C  
ATOM   3732  H   ALA A 243     -13.356 -40.774   5.513  1.00 34.12           H  
ATOM   3733  HA  ALA A 243     -13.156 -42.816   7.102  1.00 34.08           H  
ATOM   3734  HB1 ALA A 243     -15.098 -40.774   7.184  1.00 37.14           H  
ATOM   3735  HB2 ALA A 243     -14.797 -41.771   8.384  1.00 37.14           H  
ATOM   3736  HB3 ALA A 243     -13.698 -40.715   7.933  1.00 37.14           H  
ATOM   3737  N   LEU A 244     -15.643 -42.917   5.128  1.00 26.97           N  
ANISOU 3737  N   LEU A 244     5144   1793   3312   -958   -879    354       N  
ATOM   3738  CA  LEU A 244     -16.627 -43.813   4.529  1.00 26.84           C  
ANISOU 3738  CA  LEU A 244     5044   1853   3298   -852   -770    347       C  
ATOM   3739  C   LEU A 244     -15.924 -45.022   3.910  1.00 31.92           C  
ANISOU 3739  C   LEU A 244     5507   2640   3981   -910   -680    384       C  
ATOM   3740  O   LEU A 244     -16.341 -46.163   4.113  1.00 27.13           O  
ANISOU 3740  O   LEU A 244     4804   2119   3385   -823   -601    360       O  
ATOM   3741  CB  LEU A 244     -17.449 -43.082   3.460  1.00 25.51           C  
ANISOU 3741  CB  LEU A 244     4957   1618   3118   -838   -776    373       C  
ATOM   3742  CG  LEU A 244     -18.726 -43.764   2.957  1.00 27.99           C  
ANISOU 3742  CG  LEU A 244     5224   1981   3429   -711   -691    361       C  
ATOM   3743  CD1 LEU A 244     -19.687 -44.088   4.094  1.00 24.25           C  
ANISOU 3743  CD1 LEU A 244     4774   1504   2937   -549   -673    298       C  
ATOM   3744  CD2 LEU A 244     -19.403 -42.871   1.929  1.00 26.12           C  
ANISOU 3744  CD2 LEU A 244     5080   1665   3180   -714   -720    394       C  
ATOM   3745  H   LEU A 244     -15.576 -42.156   4.734  1.00 32.37           H  
ATOM   3746  HA  LEU A 244     -17.233 -44.131   5.216  1.00 32.20           H  
ATOM   3747  HB2 LEU A 244     -17.711 -42.221   3.822  1.00 30.61           H  
ATOM   3748  HB3 LEU A 244     -16.879 -42.942   2.688  1.00 30.61           H  
ATOM   3749  HG  LEU A 244     -18.488 -44.596   2.519  1.00 33.58           H  
ATOM   3750 HD11 LEU A 244     -19.935 -43.264   4.542  1.00 29.10           H  
ATOM   3751 HD12 LEU A 244     -20.477 -44.516   3.727  1.00 29.10           H  
ATOM   3752 HD13 LEU A 244     -19.247 -44.685   4.718  1.00 29.10           H  
ATOM   3753 HD21 LEU A 244     -18.795 -42.726   1.188  1.00 31.35           H  
ATOM   3754 HD22 LEU A 244     -20.210 -43.308   1.615  1.00 31.35           H  
ATOM   3755 HD23 LEU A 244     -19.626 -42.024   2.346  1.00 31.35           H  
ATOM   3756  N   SER A 245     -14.856 -44.770   3.157  1.00 25.77           N  
ANISOU 3756  N   SER A 245     4683   1885   3224  -1057   -692    445       N  
ATOM   3757  CA  SER A 245     -14.102 -45.859   2.532  1.00 27.53           C  
ANISOU 3757  CA  SER A 245     4736   2243   3479  -1108   -604    480       C  
ATOM   3758  C   SER A 245     -13.401 -46.760   3.551  1.00 29.72           C  
ANISOU 3758  C   SER A 245     4912   2595   3784  -1094   -590    458       C  
ATOM   3759  O   SER A 245     -13.203 -47.948   3.300  1.00 29.93           O  
ANISOU 3759  O   SER A 245     4805   2730   3836  -1066   -502    459       O  
ATOM   3760  CB  SER A 245     -13.072 -45.306   1.542  1.00 34.51           C  
ANISOU 3760  CB  SER A 245     5593   3144   4375  -1267   -617    558       C  
ATOM   3761  OG  SER A 245     -12.069 -44.566   2.213  1.00 44.82           O  
ANISOU 3761  OG  SER A 245     6930   4405   5695  -1376   -714    583       O  
ATOM   3762  H   SER A 245     -14.548 -43.984   2.992  1.00 30.93           H  
ATOM   3763  HA  SER A 245     -14.720 -46.413   2.030  1.00 33.03           H  
ATOM   3764  HB2 SER A 245     -12.657 -46.046   1.073  1.00 41.41           H  
ATOM   3765  HB3 SER A 245     -13.523 -44.724   0.910  1.00 41.41           H  
ATOM   3766  HG  SER A 245     -12.414 -43.921   2.624  1.00 53.79           H  
ATOM   3767  N   LEU A 246     -13.023 -46.196   4.695  1.00 40.70           N  
ANISOU 3767  N   LEU A 246     6373   3924   5168  -1113   -681    437       N  
ATOM   3768  CA  LEU A 246     -12.325 -46.958   5.731  1.00 32.18           C  
ANISOU 3768  CA  LEU A 246     5208   2909   4111  -1107   -685    421       C  
ATOM   3769  C   LEU A 246     -13.214 -47.936   6.501  1.00 39.71           C  
ANISOU 3769  C   LEU A 246     6138   3898   5052   -954   -630    363       C  
ATOM   3770  O   LEU A 246     -12.749 -49.005   6.901  1.00 40.10           O  
ANISOU 3770  O   LEU A 246     6068   4038   5132   -936   -586    363       O  
ATOM   3771  CB  LEU A 246     -11.639 -46.010   6.720  1.00 39.87           C  
ANISOU 3771  CB  LEU A 246     6276   3799   5072  -1183   -814    419       C  
ATOM   3772  CG  LEU A 246     -10.279 -45.456   6.290  1.00 34.20           C  
ANISOU 3772  CG  LEU A 246     5513   3092   4390  -1362   -872    494       C  
ATOM   3773  CD1 LEU A 246      -9.860 -44.341   7.224  1.00 39.35           C  
ANISOU 3773  CD1 LEU A 246     6301   3628   5021  -1433  -1020    485       C  
ATOM   3774  CD2 LEU A 246      -9.227 -46.557   6.266  1.00 37.31           C  
ANISOU 3774  CD2 LEU A 246     5713   3628   4837  -1404   -812    533       C  
ATOM   3775  H   LEU A 246     -13.160 -45.372   4.898  1.00 48.84           H  
ATOM   3776  HA  LEU A 246     -11.628 -47.480   5.303  1.00 38.62           H  
ATOM   3777  HB2 LEU A 246     -12.225 -45.252   6.871  1.00 47.84           H  
ATOM   3778  HB3 LEU A 246     -11.506 -46.486   7.555  1.00 47.84           H  
ATOM   3779  HG  LEU A 246     -10.354 -45.089   5.395  1.00 41.04           H  
ATOM   3780 HD11 LEU A 246      -9.796 -44.692   8.126  1.00 47.22           H  
ATOM   3781 HD12 LEU A 246      -8.997 -43.999   6.940  1.00 47.22           H  
ATOM   3782 HD13 LEU A 246     -10.523 -43.634   7.190  1.00 47.22           H  
ATOM   3783 HD21 LEU A 246      -9.502 -47.242   5.637  1.00 44.78           H  
ATOM   3784 HD22 LEU A 246      -8.379 -46.176   5.990  1.00 44.78           H  
ATOM   3785 HD23 LEU A 246      -9.147 -46.936   7.155  1.00 44.78           H  
ATOM   3786  N   GLY A 247     -14.477 -47.574   6.717  1.00 36.18           N  
ANISOU 3786  N   GLY A 247     5799   3383   4565   -844   -632    320       N  
ATOM   3787  CA  GLY A 247     -15.385 -48.410   7.486  1.00 22.89           C  
ANISOU 3787  CA  GLY A 247     4097   1734   2866   -703   -582    275       C  
ATOM   3788  C   GLY A 247     -16.230 -47.662   8.495  1.00 29.25           C  
ANISOU 3788  C   GLY A 247     5050   2450   3615   -606   -636    223       C  
ATOM   3789  O   GLY A 247     -17.120 -48.237   9.123  1.00 28.45           O  
ANISOU 3789  O   GLY A 247     4941   2376   3494   -481   -591    192       O  
ATOM   3790  H   GLY A 247     -14.830 -46.846   6.426  1.00 43.42           H  
ATOM   3791  HA2 GLY A 247     -15.983 -48.869   6.876  1.00 27.47           H  
ATOM   3792  HA3 GLY A 247     -14.870 -49.079   7.964  1.00 27.47           H  
ATOM   3793  N   LEU A 248     -15.956 -46.374   8.644  1.00 24.26           N  
ANISOU 3793  N   LEU A 248     4554   1709   2956   -662   -733    217       N  
ATOM   3794  CA  LEU A 248     -16.582 -45.578   9.686  1.00 24.89           C  
ANISOU 3794  CA  LEU A 248     4791   1693   2974   -573   -796    160       C  
ATOM   3795  C   LEU A 248     -17.943 -45.070   9.230  1.00 24.81           C  
ANISOU 3795  C   LEU A 248     4865   1624   2938   -461   -768    142       C  
ATOM   3796  O   LEU A 248     -18.352 -45.323   8.097  1.00 37.40           O  
ANISOU 3796  O   LEU A 248     6396   3250   4563   -467   -710    177       O  
ATOM   3797  CB  LEU A 248     -15.664 -44.414  10.053  1.00 26.14           C  
ANISOU 3797  CB  LEU A 248     5071   1747   3115   -685   -925    159       C  
ATOM   3798  CG  LEU A 248     -14.241 -44.869  10.390  1.00 27.90           C  
ANISOU 3798  CG  LEU A 248     5193   2033   3373   -813   -961    192       C  
ATOM   3799  CD1 LEU A 248     -13.233 -43.741  10.259  1.00 30.11           C  
ANISOU 3799  CD1 LEU A 248     5556   2222   3661   -970  -1084    223       C  
ATOM   3800  CD2 LEU A 248     -14.218 -45.454  11.788  1.00 31.86           C  
ANISOU 3800  CD2 LEU A 248     5694   2571   3841   -738   -970    147       C  
ATOM   3801  H   LEU A 248     -15.406 -45.934   8.150  1.00 29.12           H  
ATOM   3802  HA  LEU A 248     -16.710 -46.126  10.476  1.00 29.87           H  
ATOM   3803  HB2 LEU A 248     -15.614 -43.802   9.302  1.00 31.37           H  
ATOM   3804  HB3 LEU A 248     -16.026 -43.958  10.830  1.00 31.37           H  
ATOM   3805  HG  LEU A 248     -13.982 -45.570   9.772  1.00 33.48           H  
ATOM   3806 HD11 LEU A 248     -13.478 -43.027  10.868  1.00 36.13           H  
ATOM   3807 HD12 LEU A 248     -12.352 -44.079  10.482  1.00 36.13           H  
ATOM   3808 HD13 LEU A 248     -13.242 -43.416   9.345  1.00 36.13           H  
ATOM   3809 HD21 LEU A 248     -14.821 -46.212  11.822  1.00 38.23           H  
ATOM   3810 HD22 LEU A 248     -13.314 -45.740  11.995  1.00 38.23           H  
ATOM   3811 HD23 LEU A 248     -14.503 -44.775  12.419  1.00 38.23           H  
ATOM   3812  N   THR A 249     -18.645 -44.380  10.126  1.00 25.43           N  
ANISOU 3812  N   THR A 249     5084   1621   2957   -352   -808     87       N  
ATOM   3813  CA  THR A 249     -19.947 -43.797   9.817  1.00 30.07           C  
ANISOU 3813  CA  THR A 249     5758   2147   3519   -230   -789     69       C  
ATOM   3814  C   THR A 249     -19.865 -42.273   9.873  1.00 28.47           C  
ANISOU 3814  C   THR A 249     5750   1785   3282   -253   -901     45       C  
ATOM   3815  O   THR A 249     -20.179 -41.669  10.898  1.00 30.01           O  
ANISOU 3815  O   THR A 249     6082   1905   3417   -164   -949    -15       O  
ATOM   3816  CB  THR A 249     -21.036 -44.274  10.808  1.00 25.37           C  
ANISOU 3816  CB  THR A 249     5165   1595   2878    -51   -728     24       C  
ATOM   3817  OG1 THR A 249     -20.920 -45.687  11.018  1.00 28.43           O  
ANISOU 3817  OG1 THR A 249     5389   2119   3295    -45   -646     44       O  
ATOM   3818  CG2 THR A 249     -22.429 -43.949  10.273  1.00 26.46           C  
ANISOU 3818  CG2 THR A 249     5334   1708   3011     75   -683     26       C  
ATOM   3819  H   THR A 249     -18.383 -44.233  10.932  1.00 30.52           H  
ATOM   3820  HA  THR A 249     -20.213 -44.058   8.922  1.00 36.08           H  
ATOM   3821  HB  THR A 249     -20.921 -43.815  11.655  1.00 30.44           H  
ATOM   3822  HG1 THR A 249     -21.510 -45.947  11.556  1.00 34.12           H  
ATOM   3823 HG21 THR A 249     -22.568 -44.393   9.421  1.00 31.75           H  
ATOM   3824 HG22 THR A 249     -23.104 -44.252  10.900  1.00 31.75           H  
ATOM   3825 HG23 THR A 249     -22.521 -42.992  10.148  1.00 31.75           H  
ATOM   3826  N   PRO A 250     -19.439 -41.637   8.770  1.00 40.66           N  
ANISOU 3826  N   PRO A 250     7315   3273   4860   -373   -944     94       N  
ATOM   3827  CA  PRO A 250     -19.332 -40.180   8.828  1.00 36.24           C  
ANISOU 3827  CA  PRO A 250     6905   2597   4267   -395  -1047     76       C  
ATOM   3828  C   PRO A 250     -20.691 -39.513   8.683  1.00 41.40           C  
ANISOU 3828  C   PRO A 250     7640   3203   4889   -239  -1029     47       C  
ATOM   3829  O   PRO A 250     -21.627 -40.124   8.166  1.00 34.29           O  
ANISOU 3829  O   PRO A 250     6675   2346   4009   -153   -945     63       O  
ATOM   3830  CB  PRO A 250     -18.458 -39.838   7.614  1.00 35.31           C  
ANISOU 3830  CB  PRO A 250     6720   2502   4195   -566  -1071    150       C  
ATOM   3831  CG  PRO A 250     -18.031 -41.153   7.020  1.00 41.81           C  
ANISOU 3831  CG  PRO A 250     7386   3427   5073   -637   -989    200       C  
ATOM   3832  CD  PRO A 250     -19.041 -42.144   7.449  1.00 37.11           C  
ANISOU 3832  CD  PRO A 250     6733   2898   4469   -483   -895    165       C  
ATOM   3833  HA  PRO A 250     -18.899 -39.891   9.647  1.00 43.48           H  
ATOM   3834  HB2 PRO A 250     -18.979 -39.329   6.973  1.00 42.37           H  
ATOM   3835  HB3 PRO A 250     -17.685 -39.329   7.904  1.00 42.37           H  
ATOM   3836  HG2 PRO A 250     -18.013 -41.082   6.053  1.00 50.17           H  
ATOM   3837  HG3 PRO A 250     -17.154 -41.392   7.360  1.00 50.17           H  
ATOM   3838  HD2 PRO A 250     -19.798 -42.145   6.842  1.00 44.53           H  
ATOM   3839  HD3 PRO A 250     -18.643 -43.025   7.528  1.00 44.53           H  
ATOM   3840  N   ASN A 251     -20.780 -38.269   9.137  1.00 47.41           N  
ANISOU 3840  N   ASN A 251     8536   3875   5600   -206  -1111      8       N  
ATOM   3841  CA  ASN A 251     -21.987 -37.468   8.994  1.00 42.63           C  
ANISOU 3841  CA  ASN A 251     8014   3219   4967    -65  -1106    -18       C  
ATOM   3842  C   ASN A 251     -21.707 -36.330   8.021  1.00 40.48           C  
ANISOU 3842  C   ASN A 251     7783   2888   4709   -161  -1177     23       C  
ATOM   3843  O   ASN A 251     -20.755 -35.573   8.209  1.00 57.41           O  
ANISOU 3843  O   ASN A 251     9992   4981   6841   -272  -1272     27       O  
ATOM   3844  CB  ASN A 251     -22.403 -36.913  10.354  1.00 46.53           C  
ANISOU 3844  CB  ASN A 251     8643   3653   5382     71  -1141   -101       C  
ATOM   3845  CG  ASN A 251     -23.830 -36.411  10.366  1.00 49.31           C  
ANISOU 3845  CG  ASN A 251     9050   3980   5705    257  -1102   -131       C  
ATOM   3846  OD1 ASN A 251     -24.441 -36.206   9.316  1.00 39.12           O  
ANISOU 3846  OD1 ASN A 251     7717   2693   4453    268  -1077    -89       O  
ATOM   3847  ND2 ASN A 251     -24.373 -36.212  11.561  1.00 48.85           N  
ANISOU 3847  ND2 ASN A 251     9085   3902   5575    407  -1095   -202       N  
ATOM   3848  H   ASN A 251     -20.141 -37.858   9.539  1.00 56.89           H  
ATOM   3849  HA  ASN A 251     -22.707 -38.014   8.643  1.00 51.16           H  
ATOM   3850  HB2 ASN A 251     -22.326 -37.614  11.019  1.00 55.83           H  
ATOM   3851  HB3 ASN A 251     -21.822 -36.171  10.584  1.00 55.83           H  
ATOM   3852 HD21 ASN A 251     -23.916 -36.367  12.272  1.00 58.62           H  
ATOM   3853 HD22 ASN A 251     -25.182 -35.927  11.623  1.00 58.62           H  
ATOM   3854  N   PHE A 252     -22.531 -36.207   6.984  1.00 38.32           N  
ANISOU 3854  N   PHE A 252     7474   2623   4462   -121  -1137     58       N  
ATOM   3855  CA  PHE A 252     -22.267 -35.253   5.908  1.00 44.03           C  
ANISOU 3855  CA  PHE A 252     8223   3302   5204   -220  -1195    109       C  
ATOM   3856  C   PHE A 252     -23.092 -33.970   6.007  1.00 41.83           C  
ANISOU 3856  C   PHE A 252     8080   2924   4891   -114  -1252     76       C  
ATOM   3857  O   PHE A 252     -23.009 -33.110   5.131  1.00 44.92           O  
ANISOU 3857  O   PHE A 252     8505   3268   5294   -180  -1305    117       O  
ATOM   3858  CB  PHE A 252     -22.519 -35.913   4.549  1.00 34.57           C  
ANISOU 3858  CB  PHE A 252     6901   2178   4057   -268  -1124    178       C  
ATOM   3859  CG  PHE A 252     -21.472 -36.919   4.160  1.00 36.27           C  
ANISOU 3859  CG  PHE A 252     6992   2483   4308   -411  -1085    225       C  
ATOM   3860  CD1 PHE A 252     -20.282 -36.508   3.585  1.00 33.23           C  
ANISOU 3860  CD1 PHE A 252     6587   2101   3937   -583  -1136    277       C  
ATOM   3861  CD2 PHE A 252     -21.679 -38.275   4.364  1.00 28.86           C  
ANISOU 3861  CD2 PHE A 252     5951   1626   3389   -370   -996    221       C  
ATOM   3862  CE1 PHE A 252     -19.315 -37.426   3.222  1.00 29.91           C  
ANISOU 3862  CE1 PHE A 252     6044   1771   3551   -707  -1093    321       C  
ATOM   3863  CE2 PHE A 252     -20.713 -39.198   4.003  1.00 28.09           C  
ANISOU 3863  CE2 PHE A 252     5740   1608   3325   -496   -959    262       C  
ATOM   3864  CZ  PHE A 252     -19.530 -38.772   3.433  1.00 28.63           C  
ANISOU 3864  CZ  PHE A 252     5785   1685   3407   -661  -1004    311       C  
ATOM   3865  H   PHE A 252     -23.251 -36.665   6.878  1.00 45.98           H  
ATOM   3866  HA  PHE A 252     -21.331 -35.001   5.943  1.00 52.83           H  
ATOM   3867  HB2 PHE A 252     -23.374 -36.370   4.577  1.00 41.49           H  
ATOM   3868  HB3 PHE A 252     -22.536 -35.225   3.866  1.00 41.49           H  
ATOM   3869  HD1 PHE A 252     -20.130 -35.601   3.441  1.00 39.87           H  
ATOM   3870  HD2 PHE A 252     -22.473 -38.567   4.749  1.00 34.63           H  
ATOM   3871  HE1 PHE A 252     -18.519 -37.137   2.838  1.00 35.90           H  
ATOM   3872  HE2 PHE A 252     -20.860 -40.106   4.145  1.00 33.71           H  
ATOM   3873  HZ  PHE A 252     -18.881 -39.392   3.189  1.00 34.35           H  
ATOM   3874  N   LYS A 253     -23.878 -33.831   7.070  1.00 57.94           N  
ANISOU 3874  N   LYS A 253    10197   4933   6883     52  -1241      4       N  
ATOM   3875  CA  LYS A 253     -24.772 -32.683   7.189  1.00 63.41           C  
ANISOU 3875  CA  LYS A 253    11011   5538   7543    176  -1282    -30       C  
ATOM   3876  C   LYS A 253     -23.992 -31.382   7.385  1.00 60.09           C  
ANISOU 3876  C   LYS A 253    10729   5011   7093     88  -1411    -40       C  
ATOM   3877  O   LYS A 253     -24.360 -30.343   6.837  1.00 62.08           O  
ANISOU 3877  O   LYS A 253    11057   5186   7344    102  -1465    -27       O  
ATOM   3878  CB  LYS A 253     -25.804 -32.900   8.308  1.00 63.74           C  
ANISOU 3878  CB  LYS A 253    11093   5590   7536    385  -1224   -102       C  
ATOM   3879  CG  LYS A 253     -25.637 -32.035   9.556  1.00 63.91           C  
ANISOU 3879  CG  LYS A 253    11276   5528   7480    451  -1297   -179       C  
ATOM   3880  CD  LYS A 253     -26.854 -32.159  10.459  1.00 64.87           C  
ANISOU 3880  CD  LYS A 253    11429   5669   7549    678  -1225   -241       C  
ATOM   3881  CE  LYS A 253     -26.951 -30.992  11.423  1.00 64.79           C  
ANISOU 3881  CE  LYS A 253    11601   5559   7457    767  -1302   -314       C  
ATOM   3882  NZ  LYS A 253     -28.200 -31.055  12.226  1.00 65.84           N  
ANISOU 3882  NZ  LYS A 253    11757   5722   7536    998  -1220   -369       N  
ATOM   3883  H   LYS A 253     -23.914 -34.381   7.730  1.00 69.52           H  
ATOM   3884  HA  LYS A 253     -25.266 -32.597   6.358  1.00 76.09           H  
ATOM   3885  HB2 LYS A 253     -26.687 -32.720   7.948  1.00 76.49           H  
ATOM   3886  HB3 LYS A 253     -25.755 -33.827   8.591  1.00 76.49           H  
ATOM   3887  HG2 LYS A 253     -24.857 -32.329  10.051  1.00 76.69           H  
ATOM   3888  HG3 LYS A 253     -25.543 -31.106   9.294  1.00 76.69           H  
ATOM   3889  HD2 LYS A 253     -27.657 -32.172   9.914  1.00 77.84           H  
ATOM   3890  HD3 LYS A 253     -26.786 -32.977  10.976  1.00 77.84           H  
ATOM   3891  HE2 LYS A 253     -26.197 -31.015  12.032  1.00 77.75           H  
ATOM   3892  HE3 LYS A 253     -26.954 -30.161  10.922  1.00 77.75           H  
ATOM   3893  HZ1 LYS A 253     -28.220 -31.809  12.699  1.00 79.00           H  
ATOM   3894  HZ2 LYS A 253     -28.238 -30.363  12.785  1.00 79.00           H  
ATOM   3895  HZ3 LYS A 253     -28.909 -31.032  11.689  1.00 79.00           H  
ATOM   3896  N   SER A 254     -22.914 -31.443   8.160  1.00 65.83           N  
ANISOU 3896  N   SER A 254    11488   5729   7796     -3  -1465    -58       N  
ATOM   3897  CA  SER A 254     -22.083 -30.268   8.399  1.00 68.75           C  
ANISOU 3897  CA  SER A 254    11984   5999   8138    -99  -1597    -60       C  
ATOM   3898  C   SER A 254     -21.405 -29.804   7.113  1.00 67.69           C  
ANISOU 3898  C   SER A 254    11808   5856   8056   -271  -1645     27       C  
ATOM   3899  O   SER A 254     -21.233 -28.607   6.889  1.00 75.97           O  
ANISOU 3899  O   SER A 254    12966   6809   9091   -311  -1744     39       O  
ATOM   3900  CB  SER A 254     -21.023 -30.570   9.461  1.00 79.49           C  
ANISOU 3900  CB  SER A 254    13366   7367   9469   -174  -1644    -86       C  
ATOM   3901  OG  SER A 254     -20.305 -31.752   9.145  1.00 86.55           O  
ANISOU 3901  OG  SER A 254    14104   8367  10413   -286  -1585    -39       O  
ATOM   3902  H   SER A 254     -22.641 -32.154   8.559  1.00 79.00           H  
ATOM   3903  HA  SER A 254     -22.641 -29.544   8.725  1.00 82.50           H  
ATOM   3904  HB2 SER A 254     -20.402 -29.827   9.506  1.00 95.38           H  
ATOM   3905  HB3 SER A 254     -21.461 -30.688  10.318  1.00 95.38           H  
ATOM   3906  HG  SER A 254     -19.728 -31.904   9.736  1.00103.86           H  
ATOM   3907  N   ASN A 255     -21.026 -30.761   6.272  1.00 49.87           N  
ANISOU 3907  N   ASN A 255     9395   3700   5852   -369  -1573     90       N  
ATOM   3908  CA  ASN A 255     -20.316 -30.465   5.031  1.00 44.99           C  
ANISOU 3908  CA  ASN A 255     8719   3097   5277   -535  -1602    179       C  
ATOM   3909  C   ASN A 255     -21.194 -29.792   3.981  1.00 44.44           C  
ANISOU 3909  C   ASN A 255     8678   2987   5219   -489  -1602    208       C  
ATOM   3910  O   ASN A 255     -20.698 -29.051   3.131  1.00 45.52           O  
ANISOU 3910  O   ASN A 255     8833   3091   5371   -607  -1663    270       O  
ATOM   3911  CB  ASN A 255     -19.746 -31.750   4.432  1.00 46.27           C  
ANISOU 3911  CB  ASN A 255     8707   3389   5487   -633  -1512    232       C  
ATOM   3912  CG  ASN A 255     -18.817 -32.477   5.380  1.00 51.34           C  
ANISOU 3912  CG  ASN A 255     9305   4077   6126   -690  -1512    213       C  
ATOM   3913  OD1 ASN A 255     -19.057 -33.630   5.737  1.00 59.20           O  
ANISOU 3913  OD1 ASN A 255    10216   5146   7131   -632  -1425    190       O  
ATOM   3914  ND2 ASN A 255     -17.744 -31.810   5.788  1.00 43.37           N  
ANISOU 3914  ND2 ASN A 255     8349   3023   5106   -806  -1614    227       N  
ATOM   3915  H   ASN A 255     -21.170 -31.600   6.398  1.00 59.84           H  
ATOM   3916  HA  ASN A 255     -19.575 -29.871   5.226  1.00 53.99           H  
ATOM   3917  HB2 ASN A 255     -20.477 -32.348   4.212  1.00 55.53           H  
ATOM   3918  HB3 ASN A 255     -19.244 -31.530   3.631  1.00 55.53           H  
ATOM   3919 HD21 ASN A 255     -17.607 -31.007   5.513  1.00 52.04           H  
ATOM   3920 HD22 ASN A 255     -17.186 -32.181   6.327  1.00 52.04           H  
ATOM   3921  N   PHE A 256     -22.493 -30.064   4.036  1.00 41.50           N  
ANISOU 3921  N   PHE A 256     8304   2621   4842   -320  -1533    170       N  
ATOM   3922  CA  PHE A 256     -23.425 -29.594   3.016  1.00 45.33           C  
ANISOU 3922  CA  PHE A 256     8797   3082   5346   -266  -1523    203       C  
ATOM   3923  C   PHE A 256     -24.509 -28.681   3.584  1.00 52.04           C  
ANISOU 3923  C   PHE A 256     9778   3833   6162    -92  -1558    141       C  
ATOM   3924  O   PHE A 256     -25.456 -28.322   2.882  1.00 44.88           O  
ANISOU 3924  O   PHE A 256     8877   2905   5271    -15  -1544    160       O  
ATOM   3925  CB  PHE A 256     -24.066 -30.793   2.318  1.00 38.06           C  
ANISOU 3925  CB  PHE A 256     7729   2269   4461   -227  -1405    234       C  
ATOM   3926  CG  PHE A 256     -23.117 -31.562   1.445  1.00 35.22           C  
ANISOU 3926  CG  PHE A 256     7245   2002   4135   -395  -1369    305       C  
ATOM   3927  CD1 PHE A 256     -22.748 -31.075   0.204  1.00 35.65           C  
ANISOU 3927  CD1 PHE A 256     7285   2055   4206   -516  -1400    380       C  
ATOM   3928  CD2 PHE A 256     -22.601 -32.777   1.864  1.00 35.69           C  
ANISOU 3928  CD2 PHE A 256     7202   2153   4206   -427  -1301    298       C  
ATOM   3929  CE1 PHE A 256     -21.878 -31.779  -0.602  1.00 36.07           C  
ANISOU 3929  CE1 PHE A 256     7223   2202   4282   -661  -1358    445       C  
ATOM   3930  CE2 PHE A 256     -21.733 -33.486   1.063  1.00 40.32           C  
ANISOU 3930  CE2 PHE A 256     7673   2827   4820   -572  -1263    361       C  
ATOM   3931  CZ  PHE A 256     -21.370 -32.986  -0.173  1.00 40.95           C  
ANISOU 3931  CZ  PHE A 256     7737   2910   4911   -687  -1287    434       C  
ATOM   3932  H   PHE A 256     -22.865 -30.524   4.661  1.00 49.80           H  
ATOM   3933  HA  PHE A 256     -22.931 -29.091   2.350  1.00 54.40           H  
ATOM   3934  HB2 PHE A 256     -24.408 -31.401   2.992  1.00 45.67           H  
ATOM   3935  HB3 PHE A 256     -24.793 -30.478   1.759  1.00 45.67           H  
ATOM   3936  HD1 PHE A 256     -23.088 -30.261  -0.089  1.00 42.78           H  
ATOM   3937  HD2 PHE A 256     -22.842 -33.117   2.695  1.00 42.83           H  
ATOM   3938  HE1 PHE A 256     -21.636 -31.441  -1.433  1.00 43.29           H  
ATOM   3939  HE2 PHE A 256     -21.390 -34.300   1.354  1.00 48.38           H  
ATOM   3940  HZ  PHE A 256     -20.784 -33.463  -0.714  1.00 49.13           H  
ATOM   3941  N   ASP A 257     -24.365 -28.313   4.854  1.00 73.13           N  
ANISOU 3941  N   ASP A 257    12554   6447   8783    -27  -1602     68       N  
ATOM   3942  CA  ASP A 257     -25.296 -27.398   5.512  1.00 77.85           C  
ANISOU 3942  CA  ASP A 257    13291   6951   9338    142  -1637      2       C  
ATOM   3943  C   ASP A 257     -26.726 -27.931   5.466  1.00 71.26           C  
ANISOU 3943  C   ASP A 257    12393   6167   8513    330  -1531    -18       C  
ATOM   3944  O   ASP A 257     -27.681 -27.171   5.294  1.00 76.85           O  
ANISOU 3944  O   ASP A 257    13168   6815   9218    451  -1544    -31       O  
ATOM   3945  CB  ASP A 257     -25.237 -26.004   4.875  1.00 82.88           C  
ANISOU 3945  CB  ASP A 257    14042   7471   9976     93  -1746     30       C  
ATOM   3946  CG  ASP A 257     -23.907 -25.312   5.100  1.00 82.32           C  
ANISOU 3946  CG  ASP A 257    14054   7335   9887    -73  -1866     46       C  
ATOM   3947  OD1 ASP A 257     -23.730 -24.704   6.176  1.00 75.94           O  
ANISOU 3947  OD1 ASP A 257    13380   6448   9026    -24  -1937    -18       O  
ATOM   3948  OD2 ASP A 257     -23.043 -25.368   4.198  1.00 79.88           O  
ANISOU 3948  OD2 ASP A 257    13677   7057   9616   -250  -1890    126       O  
ATOM   3949  H   ASP A 257     -23.728 -28.583   5.364  1.00 87.75           H  
ATOM   3950  HA  ASP A 257     -25.042 -27.310   6.444  1.00 93.42           H  
ATOM   3951  HB2 ASP A 257     -25.373 -26.087   3.918  1.00 99.45           H  
ATOM   3952  HB3 ASP A 257     -25.932 -25.449   5.262  1.00 99.45           H  
ATOM   3953  N   LEU A 258     -26.864 -29.242   5.615  1.00 55.06           N  
ANISOU 3953  N   LEU A 258    10211   4229   6479    353  -1427    -14       N  
ATOM   3954  CA  LEU A 258     -28.172 -29.881   5.601  1.00 57.56           C  
ANISOU 3954  CA  LEU A 258    10448   4610   6811    522  -1324    -22       C  
ATOM   3955  C   LEU A 258     -28.899 -29.622   6.912  1.00 58.07           C  
ANISOU 3955  C   LEU A 258    10599   4650   6814    715  -1303   -107       C  
ATOM   3956  O   LEU A 258     -28.272 -29.446   7.958  1.00 54.96           O  
ANISOU 3956  O   LEU A 258    10292   4224   6365    708  -1343   -163       O  
ATOM   3957  CB  LEU A 258     -28.017 -31.385   5.371  1.00 61.14           C  
ANISOU 3957  CB  LEU A 258    10739   5191   7300    477  -1227     12       C  
ATOM   3958  CG  LEU A 258     -27.279 -31.762   4.082  1.00 56.18           C  
ANISOU 3958  CG  LEU A 258    10018   4603   6724    291  -1233     95       C  
ATOM   3959  CD1 LEU A 258     -27.007 -33.261   4.017  1.00 53.88           C  
ANISOU 3959  CD1 LEU A 258     9581   4429   6460    247  -1143    119       C  
ATOM   3960  CD2 LEU A 258     -28.065 -31.308   2.860  1.00 41.03           C  
ANISOU 3960  CD2 LEU A 258     8081   2669   4841    308  -1237    151       C  
ATOM   3961  H   LEU A 258     -26.209 -29.789   5.727  1.00 66.07           H  
ATOM   3962  HA  LEU A 258     -28.703 -29.513   4.877  1.00 69.07           H  
ATOM   3963  HB2 LEU A 258     -27.522 -31.762   6.114  1.00 73.37           H  
ATOM   3964  HB3 LEU A 258     -28.900 -31.784   5.331  1.00 73.37           H  
ATOM   3965  HG  LEU A 258     -26.423 -31.306   4.069  1.00 67.41           H  
ATOM   3966 HD11 LEU A 258     -27.852 -33.736   4.043  1.00 64.65           H  
ATOM   3967 HD12 LEU A 258     -26.540 -33.461   3.191  1.00 64.65           H  
ATOM   3968 HD13 LEU A 258     -26.460 -33.515   4.777  1.00 64.65           H  
ATOM   3969 HD21 LEU A 258     -28.173 -30.345   2.893  1.00 49.24           H  
ATOM   3970 HD22 LEU A 258     -27.576 -31.559   2.060  1.00 49.24           H  
ATOM   3971 HD23 LEU A 258     -28.934 -31.740   2.866  1.00 49.24           H  
ATOM   3972  N   ALA A 259     -30.226 -29.596   6.850  1.00 80.70           N  
ANISOU 3972  N   ALA A 259    13439   7536   9689    889  -1241   -113       N  
ATOM   3973  CA  ALA A 259     -31.038 -29.342   8.031  1.00 81.62           C  
ANISOU 3973  CA  ALA A 259    13625   7643   9744   1090  -1206   -188       C  
ATOM   3974  C   ALA A 259     -31.002 -30.557   8.950  1.00 81.91           C  
ANISOU 3974  C   ALA A 259    13581   7785   9755   1140  -1115   -215       C  
ATOM   3975  O   ALA A 259     -30.869 -30.425  10.168  1.00 82.65           O  
ANISOU 3975  O   ALA A 259    13763   7866   9776   1216  -1119   -285       O  
ATOM   3976  CB  ALA A 259     -32.469 -29.027   7.627  1.00 77.69           C  
ANISOU 3976  CB  ALA A 259    13095   7152   9273   1257  -1158   -173       C  
ATOM   3977  H   ALA A 259     -30.681 -29.723   6.132  1.00 96.84           H  
ATOM   3978  HA  ALA A 259     -30.680 -28.581   8.513  1.00 97.94           H  
ATOM   3979  HB1 ALA A 259     -32.834 -29.784   7.143  1.00 93.23           H  
ATOM   3980  HB2 ALA A 259     -32.993 -28.862   8.427  1.00 93.23           H  
ATOM   3981  HB3 ALA A 259     -32.470 -28.240   7.061  1.00 93.23           H  
ATOM   3982  N   GLU A 260     -31.110 -31.740   8.349  1.00 74.50           N  
ANISOU 3982  N   GLU A 260    12482   6951   8875   1096  -1038   -158       N  
ATOM   3983  CA  GLU A 260     -31.211 -32.987   9.101  1.00 73.73           C  
ANISOU 3983  CA  GLU A 260    12290   6961   8762   1152   -944   -171       C  
ATOM   3984  C   GLU A 260     -29.957 -33.852   8.944  1.00 74.70           C  
ANISOU 3984  C   GLU A 260    12355   7120   8909    968   -955   -146       C  
ATOM   3985  O   GLU A 260     -29.082 -33.562   8.128  1.00 72.70           O  
ANISOU 3985  O   GLU A 260    12109   6826   8689    797  -1023   -108       O  
ATOM   3986  CB  GLU A 260     -32.456 -33.765   8.661  1.00 71.07           C  
ANISOU 3986  CB  GLU A 260    11806   6725   8474   1270   -839   -123       C  
ATOM   3987  CG  GLU A 260     -32.952 -34.790   9.682  1.00 80.59           C  
ANISOU 3987  CG  GLU A 260    12935   8038   9648   1398   -734   -144       C  
ATOM   3988  CD  GLU A 260     -34.447 -34.701   9.929  1.00 86.96           C  
ANISOU 3988  CD  GLU A 260    13691   8901  10450   1608   -656   -139       C  
ATOM   3989  OE1 GLU A 260     -34.936 -33.595  10.245  1.00 89.38           O  
ANISOU 3989  OE1 GLU A 260    14105   9139  10717   1714   -686   -181       O  
ATOM   3990  OE2 GLU A 260     -35.134 -35.739   9.813  1.00 82.85           O  
ANISOU 3990  OE2 GLU A 260    13019   8494   9966   1666   -564    -90       O  
ATOM   3991  H   GLU A 260     -31.128 -31.847   7.496  1.00 89.41           H  
ATOM   3992  HA  GLU A 260     -31.309 -32.777  10.043  1.00 88.47           H  
ATOM   3993  HB2 GLU A 260     -33.177 -33.135   8.503  1.00 85.29           H  
ATOM   3994  HB3 GLU A 260     -32.252 -34.241   7.841  1.00 85.29           H  
ATOM   3995  HG2 GLU A 260     -32.755 -35.681   9.355  1.00 96.71           H  
ATOM   3996  HG3 GLU A 260     -32.499 -34.639  10.526  1.00 96.71           H  
ATOM   3997  N   ASP A 261     -29.894 -34.919   9.733  1.00 96.04           N  
ANISOU 3997  N   ASP A 261    14993   9905  11593   1008   -884   -163       N  
ATOM   3998  CA  ASP A 261     -28.719 -35.779   9.813  1.00 93.84           C  
ANISOU 3998  CA  ASP A 261    14665   9661  11330    856   -891   -149       C  
ATOM   3999  C   ASP A 261     -28.548 -36.631   8.554  1.00 90.60           C  
ANISOU 3999  C   ASP A 261    14112   9311  11002    738   -857    -68       C  
ATOM   4000  O   ASP A 261     -29.509 -37.232   8.070  1.00 86.30           O  
ANISOU 4000  O   ASP A 261    13464   8833  10493    819   -783    -28       O  
ATOM   4001  CB  ASP A 261     -28.844 -36.686  11.042  1.00 93.98           C  
ANISOU 4001  CB  ASP A 261    14658   9749  11302    955   -821   -190       C  
ATOM   4002  CG  ASP A 261     -27.605 -36.669  11.911  1.00100.53           C  
ANISOU 4002  CG  ASP A 261    15569  10544  12086    857   -886   -233       C  
ATOM   4003  OD1 ASP A 261     -26.515 -36.975  11.393  1.00100.81           O  
ANISOU 4003  OD1 ASP A 261    15563  10575  12165    676   -929   -198       O  
ATOM   4004  OD2 ASP A 261     -27.723 -36.347  13.113  1.00105.74           O  
ANISOU 4004  OD2 ASP A 261    16328  11184  12664    960   -894   -301       O  
ATOM   4005  H   ASP A 261     -30.537 -35.171  10.246  1.00115.25           H  
ATOM   4006  HA  ASP A 261     -27.926 -35.230   9.919  1.00112.61           H  
ATOM   4007  HB2 ASP A 261     -29.592 -36.387  11.580  1.00112.78           H  
ATOM   4008  HB3 ASP A 261     -28.990 -37.598  10.747  1.00112.78           H  
ATOM   4009  N   ALA A 262     -27.323 -36.676   8.032  1.00 40.49           N  
ANISOU 4009  N   ALA A 262     7757   2947   4681    546   -912    -39       N  
ATOM   4010  CA  ALA A 262     -26.997 -37.492   6.860  1.00 35.30           C  
ANISOU 4010  CA  ALA A 262     6972   2351   4090    422   -880     35       C  
ATOM   4011  C   ALA A 262     -25.788 -38.384   7.139  1.00 36.67           C  
ANISOU 4011  C   ALA A 262     7091   2568   4275    290   -875     42       C  
ATOM   4012  O   ALA A 262     -24.677 -38.106   6.687  1.00 36.17           O  
ANISOU 4012  O   ALA A 262     7032   2484   4226    126   -932     67       O  
ATOM   4013  CB  ALA A 262     -26.729 -36.610   5.651  1.00 30.63           C  
ANISOU 4013  CB  ALA A 262     6406   1708   3524    311   -943     81       C  
ATOM   4014  H   ALA A 262     -26.652 -36.237   8.343  1.00 48.59           H  
ATOM   4015  HA  ALA A 262     -27.753 -38.065   6.654  1.00 42.36           H  
ATOM   4016  HB1 ALA A 262     -25.982 -36.024   5.848  1.00 36.76           H  
ATOM   4017  HB2 ALA A 262     -26.517 -37.174   4.890  1.00 36.76           H  
ATOM   4018  HB3 ALA A 262     -27.522 -36.084   5.462  1.00 36.76           H  
ATOM   4019  N   LYS A 263     -26.015 -39.452   7.894  1.00 38.83           N  
ANISOU 4019  N   LYS A 263     7307   2906   4542    366   -806     25       N  
ATOM   4020  CA  LYS A 263     -24.966 -40.412   8.212  1.00 39.06           C  
ANISOU 4020  CA  LYS A 263     7276   2979   4586    258   -795     33       C  
ATOM   4021  C   LYS A 263     -24.902 -41.517   7.168  1.00 39.03           C  
ANISOU 4021  C   LYS A 263     7114   3073   4644    180   -728    100       C  
ATOM   4022  O   LYS A 263     -25.939 -42.026   6.743  1.00 30.76           O  
ANISOU 4022  O   LYS A 263     5982   2091   3616    270   -660    125       O  
ATOM   4023  CB  LYS A 263     -25.240 -41.042   9.569  1.00 45.05           C  
ANISOU 4023  CB  LYS A 263     8035   3781   5302    378   -750    -18       C  
ATOM   4024  CG  LYS A 263     -25.039 -40.112  10.736  1.00 50.51           C  
ANISOU 4024  CG  LYS A 263     8886   4387   5919    434   -819    -92       C  
ATOM   4025  CD  LYS A 263     -25.860 -40.562  11.909  1.00 47.64           C  
ANISOU 4025  CD  LYS A 263     8535   4067   5500    617   -752   -139       C  
ATOM   4026  CE  LYS A 263     -25.316 -40.011  13.196  1.00 50.68           C  
ANISOU 4026  CE  LYS A 263     9059   4395   5803    638   -816   -213       C  
ATOM   4027  NZ  LYS A 263     -26.421 -39.910  14.165  1.00 58.07           N  
ANISOU 4027  NZ  LYS A 263    10043   5356   6665    851   -755   -263       N  
ATOM   4028  H   LYS A 263     -26.779 -39.646   8.238  1.00 46.60           H  
ATOM   4029  HA  LYS A 263     -24.108 -39.962   8.243  1.00 46.87           H  
ATOM   4030  HB2 LYS A 263     -26.160 -41.347   9.590  1.00 54.06           H  
ATOM   4031  HB3 LYS A 263     -24.642 -41.797   9.687  1.00 54.06           H  
ATOM   4032  HG2 LYS A 263     -24.104 -40.115  10.996  1.00 60.61           H  
ATOM   4033  HG3 LYS A 263     -25.320 -39.217  10.489  1.00 60.61           H  
ATOM   4034  HD2 LYS A 263     -26.771 -40.248  11.803  1.00 57.17           H  
ATOM   4035  HD3 LYS A 263     -25.841 -41.531  11.961  1.00 57.17           H  
ATOM   4036  HE2 LYS A 263     -24.641 -40.609  13.552  1.00 60.82           H  
ATOM   4037  HE3 LYS A 263     -24.949 -39.125  13.046  1.00 60.82           H  
ATOM   4038  HZ1 LYS A 263     -26.774 -40.715  14.308  1.00 69.68           H  
ATOM   4039  HZ2 LYS A 263     -26.120 -39.585  14.936  1.00 69.68           H  
ATOM   4040  HZ3 LYS A 263     -27.054 -39.369  13.849  1.00 69.68           H  
ATOM   4041  N   LEU A 264     -23.687 -41.895   6.775  1.00 26.34           N  
ANISOU 4041  N   LEU A 264     5443   1501   3065     13   -743    128       N  
ATOM   4042  CA  LEU A 264     -23.488 -42.953   5.790  1.00 24.91           C  
ANISOU 4042  CA  LEU A 264     5099   1435   2932    -66   -674    183       C  
ATOM   4043  C   LEU A 264     -22.548 -44.054   6.270  1.00 24.61           C  
ANISOU 4043  C   LEU A 264     4939   1501   2910   -136   -635    180       C  
ATOM   4044  O   LEU A 264     -21.473 -43.797   6.803  1.00 24.62           O  
ANISOU 4044  O   LEU A 264     4975   1477   2903   -224   -689    167       O  
ATOM   4045  CB  LEU A 264     -22.964 -42.368   4.476  1.00 25.18           C  
ANISOU 4045  CB  LEU A 264     5157   1420   2989   -203   -717    237       C  
ATOM   4046  CG  LEU A 264     -23.943 -41.537   3.642  1.00 27.63           C  
ANISOU 4046  CG  LEU A 264     5533   1668   3296   -147   -739    259       C  
ATOM   4047  CD1 LEU A 264     -23.344 -41.219   2.286  1.00 25.79           C  
ANISOU 4047  CD1 LEU A 264     5269   1450   3081   -291   -756    317       C  
ATOM   4048  CD2 LEU A 264     -25.270 -42.243   3.462  1.00 25.04           C  
ANISOU 4048  CD2 LEU A 264     5137   1398   2980    -11   -667    267       C  
ATOM   4049  H   LEU A 264     -22.955 -41.550   7.068  1.00 31.61           H  
ATOM   4050  HA  LEU A 264     -24.347 -43.365   5.604  1.00 29.90           H  
ATOM   4051  HB2 LEU A 264     -22.208 -41.797   4.682  1.00 30.21           H  
ATOM   4052  HB3 LEU A 264     -22.666 -43.103   3.917  1.00 30.21           H  
ATOM   4053  HG  LEU A 264     -24.111 -40.697   4.099  1.00 33.15           H  
ATOM   4054 HD11 LEU A 264     -23.155 -42.050   1.822  1.00 30.95           H  
ATOM   4055 HD12 LEU A 264     -23.980 -40.693   1.776  1.00 30.95           H  
ATOM   4056 HD13 LEU A 264     -22.525 -40.716   2.413  1.00 30.95           H  
ATOM   4057 HD21 LEU A 264     -25.664 -42.401   4.334  1.00 30.05           H  
ATOM   4058 HD22 LEU A 264     -25.856 -41.682   2.930  1.00 30.05           H  
ATOM   4059 HD23 LEU A 264     -25.118 -43.087   3.009  1.00 30.05           H  
ATOM   4060  N   GLN A 265     -22.980 -45.291   6.068  1.00 25.09           N  
ANISOU 4060  N   GLN A 265     4857   1679   2998    -97   -546    197       N  
ATOM   4061  CA  GLN A 265     -22.152 -46.455   6.344  1.00 29.07           C  
ANISOU 4061  CA  GLN A 265     5233   2285   3526   -158   -503    202       C  
ATOM   4062  C   GLN A 265     -22.359 -47.485   5.247  1.00 22.71           C  
ANISOU 4062  C   GLN A 265     4296   1570   2763   -186   -431    243       C  
ATOM   4063  O   GLN A 265     -23.471 -47.969   5.050  1.00 29.54           O  
ANISOU 4063  O   GLN A 265     5118   2472   3636    -94   -383    250       O  
ATOM   4064  CB  GLN A 265     -22.514 -47.068   7.696  1.00 28.28           C  
ANISOU 4064  CB  GLN A 265     5109   2234   3403    -50   -472    165       C  
ATOM   4065  CG  GLN A 265     -21.302 -47.560   8.464  1.00 30.42           C  
ANISOU 4065  CG  GLN A 265     5337   2544   3677   -125   -488    153       C  
ATOM   4066  CD  GLN A 265     -21.639 -48.528   9.580  1.00 35.06           C  
ANISOU 4066  CD  GLN A 265     5860   3210   4251    -32   -439    135       C  
ATOM   4067  OE1 GLN A 265     -22.806 -48.740   9.912  1.00 32.61           O  
ANISOU 4067  OE1 GLN A 265     5546   2921   3921     94   -393    128       O  
ATOM   4068  NE2 GLN A 265     -20.608 -49.128  10.168  1.00 45.03           N  
ANISOU 4068  NE2 GLN A 265     7065   4519   5524    -97   -450    134       N  
ATOM   4069  H   GLN A 265     -23.761 -45.485   5.766  1.00 30.11           H  
ATOM   4070  HA  GLN A 265     -21.217 -46.198   6.359  1.00 34.88           H  
ATOM   4071  HB2 GLN A 265     -22.960 -46.398   8.237  1.00 33.94           H  
ATOM   4072  HB3 GLN A 265     -23.105 -47.824   7.552  1.00 33.94           H  
ATOM   4073  HG2 GLN A 265     -20.705 -48.013   7.848  1.00 36.50           H  
ATOM   4074  HG3 GLN A 265     -20.851 -46.797   8.859  1.00 36.50           H  
ATOM   4075 HE21 GLN A 265     -19.806 -48.957   9.908  1.00 54.03           H  
ATOM   4076 HE22 GLN A 265     -20.742 -49.687  10.807  1.00 54.03           H  
ATOM   4077  N   LEU A 266     -21.284 -47.823   4.540  1.00 23.38           N  
ANISOU 4077  N   LEU A 266     4317   1693   2874   -314   -425    270       N  
ATOM   4078  CA  LEU A 266     -21.365 -48.729   3.397  1.00 24.15           C  
ANISOU 4078  CA  LEU A 266     4309   1866   3002   -348   -362    303       C  
ATOM   4079  C   LEU A 266     -21.816 -50.130   3.800  1.00 20.03           C  
ANISOU 4079  C   LEU A 266     3672   1436   2503   -275   -293    293       C  
ATOM   4080  O   LEU A 266     -22.398 -50.855   2.993  1.00 27.78           O  
ANISOU 4080  O   LEU A 266     4590   2463   3502   -259   -248    311       O  
ATOM   4081  CB  LEU A 266     -20.007 -48.823   2.691  1.00 20.98           C  
ANISOU 4081  CB  LEU A 266     3860   1497   2617   -490   -360    331       C  
ATOM   4082  CG  LEU A 266     -19.415 -47.547   2.088  1.00 23.51           C  
ANISOU 4082  CG  LEU A 266     4273   1739   2921   -594   -425    360       C  
ATOM   4083  CD1 LEU A 266     -17.955 -47.729   1.680  1.00 22.11           C  
ANISOU 4083  CD1 LEU A 266     4025   1613   2762   -731   -418    393       C  
ATOM   4084  CD2 LEU A 266     -20.243 -47.133   0.898  1.00 25.69           C  
ANISOU 4084  CD2 LEU A 266     4593   1984   3183   -586   -422    389       C  
ATOM   4085  H   LEU A 266     -20.489 -47.538   4.704  1.00 28.06           H  
ATOM   4086  HA  LEU A 266     -22.009 -48.378   2.762  1.00 28.98           H  
ATOM   4087  HB2 LEU A 266     -19.361 -49.156   3.334  1.00 25.18           H  
ATOM   4088  HB3 LEU A 266     -20.092 -49.463   1.968  1.00 25.18           H  
ATOM   4089  HG  LEU A 266     -19.457 -46.836   2.746  1.00 28.21           H  
ATOM   4090 HD11 LEU A 266     -17.898 -48.436   1.018  1.00 26.53           H  
ATOM   4091 HD12 LEU A 266     -17.627 -46.897   1.304  1.00 26.53           H  
ATOM   4092 HD13 LEU A 266     -17.436 -47.966   2.464  1.00 26.53           H  
ATOM   4093 HD21 LEU A 266     -21.153 -46.969   1.189  1.00 30.82           H  
ATOM   4094 HD22 LEU A 266     -19.865 -46.325   0.517  1.00 30.82           H  
ATOM   4095 HD23 LEU A 266     -20.229 -47.847   0.240  1.00 30.82           H  
ATOM   4096  N   SER A 267     -21.543 -50.513   5.043  1.00 22.72           N  
ANISOU 4096  N   SER A 267     3992   1799   2841   -237   -293    267       N  
ATOM   4097  CA  SER A 267     -21.894 -51.847   5.517  1.00 21.07           C  
ANISOU 4097  CA  SER A 267     3677   1674   2656   -176   -234    265       C  
ATOM   4098  C   SER A 267     -23.373 -51.915   5.867  1.00 19.20           C  
ANISOU 4098  C   SER A 267     3452   1437   2406    -50   -213    265       C  
ATOM   4099  O   SER A 267     -23.949 -52.997   5.959  1.00 25.84           O  
ANISOU 4099  O   SER A 267     4204   2343   3272     -2   -165    278       O  
ATOM   4100  CB  SER A 267     -21.069 -52.218   6.749  1.00 19.36           C  
ANISOU 4100  CB  SER A 267     3435   1484   2436   -181   -246    245       C  
ATOM   4101  OG  SER A 267     -21.611 -51.630   7.921  1.00 36.59           O  
ANISOU 4101  OG  SER A 267     5701   3628   4575    -94   -274    217       O  
ATOM   4102  H   SER A 267     -21.155 -50.020   5.631  1.00 27.26           H  
ATOM   4103  HA  SER A 267     -21.713 -52.496   4.819  1.00 25.29           H  
ATOM   4104  HB2 SER A 267     -21.071 -53.182   6.851  1.00 23.23           H  
ATOM   4105  HB3 SER A 267     -20.161 -51.899   6.628  1.00 23.23           H  
ATOM   4106  HG  SER A 267     -21.149 -51.842   8.589  1.00 43.91           H  
ATOM   4107  N   LYS A 268     -23.980 -50.753   6.071  1.00 27.67           N  
ANISOU 4107  N   LYS A 268     4634   2436   3442      5   -251    253       N  
ATOM   4108  CA  LYS A 268     -25.375 -50.681   6.480  1.00 28.25           C  
ANISOU 4108  CA  LYS A 268     4719   2513   3502    136   -230    256       C  
ATOM   4109  C   LYS A 268     -26.292 -51.056   5.325  1.00 26.22           C  
ANISOU 4109  C   LYS A 268     4406   2281   3277    147   -204    296       C  
ATOM   4110  O   LYS A 268     -26.062 -50.667   4.181  1.00 35.42           O  
ANISOU 4110  O   LYS A 268     5597   3413   4450     74   -226    311       O  
ATOM   4111  CB  LYS A 268     -25.695 -49.276   6.989  1.00 35.35           C  
ANISOU 4111  CB  LYS A 268     5761   3319   4353    199   -280    227       C  
ATOM   4112  CG  LYS A 268     -26.967 -49.179   7.808  1.00 41.99           C  
ANISOU 4112  CG  LYS A 268     6615   4174   5167    356   -250    221       C  
ATOM   4113  CD  LYS A 268     -26.911 -47.993   8.764  1.00 54.80           C  
ANISOU 4113  CD  LYS A 268     8384   5711   6726    423   -297    171       C  
ATOM   4114  CE  LYS A 268     -28.281 -47.371   8.981  1.00 43.69           C  
ANISOU 4114  CE  LYS A 268     7027   4281   5294    578   -281    170       C  
ATOM   4115  NZ  LYS A 268     -29.309 -48.379   9.358  1.00 41.51           N  
ANISOU 4115  NZ  LYS A 268     6626   4115   5031    676   -200    204       N  
ATOM   4116  H   LYS A 268     -23.603 -49.986   5.977  1.00 33.20           H  
ATOM   4117  HA  LYS A 268     -25.528 -51.307   7.205  1.00 33.90           H  
ATOM   4118  HB2 LYS A 268     -24.961 -48.974   7.547  1.00 42.42           H  
ATOM   4119  HB3 LYS A 268     -25.790 -48.684   6.226  1.00 42.42           H  
ATOM   4120  HG2 LYS A 268     -27.724 -49.058   7.214  1.00 50.39           H  
ATOM   4121  HG3 LYS A 268     -27.075 -49.989   8.332  1.00 50.39           H  
ATOM   4122  HD2 LYS A 268     -26.575 -48.292   9.623  1.00 65.76           H  
ATOM   4123  HD3 LYS A 268     -26.326 -47.314   8.394  1.00 65.76           H  
ATOM   4124  HE2 LYS A 268     -28.223 -46.718   9.696  1.00 52.43           H  
ATOM   4125  HE3 LYS A 268     -28.568 -46.941   8.160  1.00 52.43           H  
ATOM   4126  HZ1 LYS A 268     -29.073 -48.785  10.114  1.00 49.81           H  
ATOM   4127  HZ2 LYS A 268     -30.096 -47.981   9.477  1.00 49.81           H  
ATOM   4128  HZ3 LYS A 268     -29.387 -48.989   8.714  1.00 49.81           H  
ATOM   4129  N   ASP A 269     -27.338 -51.812   5.640  1.00 38.14           N  
ANISOU 4129  N   ASP A 269     5840   3850   4801    235   -160    317       N  
ATOM   4130  CA  ASP A 269     -28.230 -52.366   4.628  1.00 39.26           C  
ANISOU 4130  CA  ASP A 269     5914   4025   4978    239   -142    360       C  
ATOM   4131  C   ASP A 269     -28.999 -51.277   3.884  1.00 33.47           C  
ANISOU 4131  C   ASP A 269     5256   3229   4233    272   -177    376       C  
ATOM   4132  O   ASP A 269     -29.412 -51.468   2.742  1.00 41.66           O  
ANISOU 4132  O   ASP A 269     6266   4271   5292    237   -185    409       O  
ATOM   4133  CB  ASP A 269     -29.210 -53.344   5.283  1.00 33.33           C  
ANISOU 4133  CB  ASP A 269     5066   3351   4248    325    -96    388       C  
ATOM   4134  CG  ASP A 269     -30.164 -52.658   6.246  1.00 49.97           C  
ANISOU 4134  CG  ASP A 269     7211   5453   6323    458    -87    389       C  
ATOM   4135  OD1 ASP A 269     -29.764 -51.649   6.865  1.00 62.93           O  
ANISOU 4135  OD1 ASP A 269     8957   7034   7918    488   -111    347       O  
ATOM   4136  OD2 ASP A 269     -31.313 -53.128   6.385  1.00 57.82           O  
ANISOU 4136  OD2 ASP A 269     8129   6502   7337    535    -55    432       O  
ATOM   4137  H   ASP A 269     -27.555 -52.022   6.446  1.00 45.77           H  
ATOM   4138  HA  ASP A 269     -27.704 -52.859   3.979  1.00 47.11           H  
ATOM   4139  HB2 ASP A 269     -29.739 -53.773   4.592  1.00 40.00           H  
ATOM   4140  HB3 ASP A 269     -28.709 -54.010   5.780  1.00 40.00           H  
ATOM   4141  N   THR A 270     -29.174 -50.130   4.532  1.00 20.82           N  
ANISOU 4141  N   THR A 270     3756   1562   2594    342   -205    352       N  
ATOM   4142  CA  THR A 270     -29.968 -49.043   3.972  1.00 31.43           C  
ANISOU 4142  CA  THR A 270     5178   2837   3928    395   -242    367       C  
ATOM   4143  C   THR A 270     -29.097 -48.021   3.247  1.00 36.76           C  
ANISOU 4143  C   THR A 270     5964   3419   4586    297   -303    355       C  
ATOM   4144  O   THR A 270     -29.580 -46.955   2.862  1.00 38.80           O  
ANISOU 4144  O   THR A 270     6312   3599   4832    334   -347    363       O  
ATOM   4145  CB  THR A 270     -30.766 -48.313   5.073  1.00 27.68           C  
ANISOU 4145  CB  THR A 270     4762   2335   3419    546   -237    347       C  
ATOM   4146  OG1 THR A 270     -29.889 -47.973   6.152  1.00 27.42           O  
ANISOU 4146  OG1 THR A 270     4804   2271   3345    543   -249    292       O  
ATOM   4147  CG2 THR A 270     -31.906 -49.186   5.593  1.00 26.80           C  
ANISOU 4147  CG2 THR A 270     4533   2322   3327    652   -175    381       C  
ATOM   4148  H   THR A 270     -28.839 -49.956   5.305  1.00 24.98           H  
ATOM   4149  HA  THR A 270     -30.600 -49.409   3.333  1.00 37.72           H  
ATOM   4150  HB  THR A 270     -31.149 -47.502   4.705  1.00 33.22           H  
ATOM   4151  HG1 THR A 270     -29.276 -47.470   5.876  1.00 32.91           H  
ATOM   4152 HG21 THR A 270     -31.550 -50.008   5.966  1.00 32.16           H  
ATOM   4153 HG22 THR A 270     -32.397 -48.713   6.284  1.00 32.16           H  
ATOM   4154 HG23 THR A 270     -32.513 -49.406   4.869  1.00 32.16           H  
ATOM   4155  N   TYR A 271     -27.821 -48.346   3.050  1.00 20.93           N  
ANISOU 4155  N   TYR A 271     3946   1423   2582    173   -307    342       N  
ATOM   4156  CA  TYR A 271     -26.869 -47.379   2.509  1.00 21.37           C  
ANISOU 4156  CA  TYR A 271     4100   1399   2622     69   -363    338       C  
ATOM   4157  C   TYR A 271     -27.274 -46.803   1.162  1.00 23.50           C  
ANISOU 4157  C   TYR A 271     4410   1626   2895     32   -395    380       C  
ATOM   4158  O   TYR A 271     -27.258 -45.591   0.989  1.00 24.41           O  
ANISOU 4158  O   TYR A 271     4642   1643   2990     27   -455    382       O  
ATOM   4159  CB  TYR A 271     -25.470 -47.972   2.372  1.00 20.95           C  
ANISOU 4159  CB  TYR A 271     3995   1388   2578    -60   -350    333       C  
ATOM   4160  CG  TYR A 271     -24.533 -47.015   1.673  1.00 22.30           C  
ANISOU 4160  CG  TYR A 271     4248   1489   2735   -179   -405    347       C  
ATOM   4161  CD1 TYR A 271     -24.033 -45.900   2.334  1.00 22.28           C  
ANISOU 4161  CD1 TYR A 271     4361   1394   2708   -194   -470    325       C  
ATOM   4162  CD2 TYR A 271     -24.174 -47.205   0.343  1.00 21.37           C  
ANISOU 4162  CD2 TYR A 271     4098   1397   2625   -278   -394    386       C  
ATOM   4163  CE1 TYR A 271     -23.188 -45.010   1.700  1.00 22.89           C  
ANISOU 4163  CE1 TYR A 271     4513   1407   2779   -314   -527    349       C  
ATOM   4164  CE2 TYR A 271     -23.330 -46.320  -0.301  1.00 21.98           C  
ANISOU 4164  CE2 TYR A 271     4245   1419   2688   -392   -440    411       C  
ATOM   4165  CZ  TYR A 271     -22.845 -45.223   0.380  1.00 26.13           C  
ANISOU 4165  CZ  TYR A 271     4877   1852   3198   -414   -508    397       C  
ATOM   4166  OH  TYR A 271     -22.002 -44.350  -0.263  1.00 23.45           O  
ANISOU 4166  OH  TYR A 271     4603   1457   2848   -539   -560    433       O  
ATOM   4167  H   TYR A 271     -27.482 -49.118   3.220  1.00 25.11           H  
ATOM   4168  HA  TYR A 271     -26.807 -46.637   3.131  1.00 25.65           H  
ATOM   4169  HB2 TYR A 271     -25.112 -48.157   3.255  1.00 25.14           H  
ATOM   4170  HB3 TYR A 271     -25.517 -48.788   1.850  1.00 25.14           H  
ATOM   4171  HD1 TYR A 271     -24.266 -45.753   3.222  1.00 26.73           H  
ATOM   4172  HD2 TYR A 271     -24.503 -47.942  -0.119  1.00 25.65           H  
ATOM   4173  HE1 TYR A 271     -22.857 -44.270   2.157  1.00 27.47           H  
ATOM   4174  HE2 TYR A 271     -23.093 -46.461  -1.190  1.00 26.38           H  
ATOM   4175  HH  TYR A 271     -21.880 -44.600  -1.055  1.00 28.13           H  
ATOM   4176  N   ASP A 272     -27.602 -47.663   0.204  1.00 21.13           N  
ANISOU 4176  N   ASP A 272     4021   1393   2616      0   -362    413       N  
ATOM   4177  CA  ASP A 272     -27.980 -47.199  -1.124  1.00 21.43           C  
ANISOU 4177  CA  ASP A 272     4095   1398   2649    -42   -394    457       C  
ATOM   4178  C   ASP A 272     -29.148 -46.214  -1.048  1.00 24.54           C  
ANISOU 4178  C   ASP A 272     4565   1721   3039     69   -437    472       C  
ATOM   4179  O   ASP A 272     -29.110 -45.138  -1.657  1.00 30.50           O  
ANISOU 4179  O   ASP A 272     5422   2390   3778     39   -495    493       O  
ATOM   4180  CB  ASP A 272     -28.313 -48.390  -2.025  1.00 20.82           C  
ANISOU 4180  CB  ASP A 272     3914   1407   2590    -73   -354    483       C  
ATOM   4181  CG  ASP A 272     -27.079 -49.200  -2.389  1.00 30.55           C  
ANISOU 4181  CG  ASP A 272     5092   2697   3820   -186   -316    470       C  
ATOM   4182  OD1 ASP A 272     -26.029 -48.586  -2.669  1.00 29.72           O  
ANISOU 4182  OD1 ASP A 272     5040   2558   3694   -279   -334    471       O  
ATOM   4183  OD2 ASP A 272     -27.152 -50.446  -2.385  1.00 25.37           O  
ANISOU 4183  OD2 ASP A 272     4338   2116   3184   -181   -270    463       O  
ATOM   4184  H   ASP A 272     -27.614 -48.518   0.298  1.00 25.36           H  
ATOM   4185  HA  ASP A 272     -27.226 -46.732  -1.517  1.00 25.72           H  
ATOM   4186  HB2 ASP A 272     -28.932 -48.975  -1.562  1.00 24.99           H  
ATOM   4187  HB3 ASP A 272     -28.713 -48.064  -2.846  1.00 24.99           H  
ATOM   4188  N   ASP A 273     -30.166 -46.571  -0.270  1.00 31.68           N  
ANISOU 4188  N   ASP A 273     5418   2661   3959    199   -408    466       N  
ATOM   4189  CA  ASP A 273     -31.317 -45.700  -0.062  1.00 27.12           C  
ANISOU 4189  CA  ASP A 273     4896   2028   3381    329   -437    479       C  
ATOM   4190  C   ASP A 273     -30.913 -44.408   0.647  1.00 30.58           C  
ANISOU 4190  C   ASP A 273     5479   2354   3786    364   -485    439       C  
ATOM   4191  O   ASP A 273     -31.393 -43.327   0.305  1.00 32.81           O  
ANISOU 4191  O   ASP A 273     5859   2544   4061    410   -540    453       O  
ATOM   4192  CB  ASP A 273     -32.384 -46.433   0.747  1.00 26.14           C  
ANISOU 4192  CB  ASP A 273     4670   1984   3277    460   -383    484       C  
ATOM   4193  CG  ASP A 273     -33.025 -47.565  -0.031  1.00 37.19           C  
ANISOU 4193  CG  ASP A 273     5941   3475   4714    434   -358    534       C  
ATOM   4194  OD1 ASP A 273     -33.500 -47.317  -1.160  1.00 35.34           O  
ANISOU 4194  OD1 ASP A 273     5717   3221   4489    406   -397    578       O  
ATOM   4195  OD2 ASP A 273     -33.041 -48.706   0.477  1.00 46.80           O  
ANISOU 4195  OD2 ASP A 273     7053   4778   5949    436   -306    531       O  
ATOM   4196  H   ASP A 273     -30.214 -47.319   0.151  1.00 38.02           H  
ATOM   4197  HA  ASP A 273     -31.698 -45.465  -0.922  1.00 32.55           H  
ATOM   4198  HB2 ASP A 273     -31.977 -46.808   1.543  1.00 31.37           H  
ATOM   4199  HB3 ASP A 273     -33.082 -45.805   0.994  1.00 31.37           H  
ATOM   4200  N   ASP A 274     -30.028 -44.528   1.632  1.00 23.53           N  
ANISOU 4200  N   ASP A 274     4604   1462   2875    341   -472    389       N  
ATOM   4201  CA  ASP A 274     -29.534 -43.366   2.366  1.00 24.37           C  
ANISOU 4201  CA  ASP A 274     4857   1458   2946    360   -527    344       C  
ATOM   4202  C   ASP A 274     -28.755 -42.449   1.432  1.00 33.49           C  
ANISOU 4202  C   ASP A 274     6113   2517   4096    230   -601    366       C  
ATOM   4203  O   ASP A 274     -28.834 -41.222   1.530  1.00 44.33           O  
ANISOU 4203  O   ASP A 274     7585   3810   5449    254   -658    346       O  
ATOM   4204  CB  ASP A 274     -28.622 -43.795   3.520  1.00 24.09           C  
ANISOU 4204  CB  ASP A 274     4811   1452   2891    334   -506    293       C  
ATOM   4205  CG  ASP A 274     -29.346 -44.615   4.571  1.00 39.89           C  
ANISOU 4205  CG  ASP A 274     6727   3543   4888    462   -436    275       C  
ATOM   4206  OD1 ASP A 274     -30.566 -44.420   4.746  1.00 39.91           O  
ANISOU 4206  OD1 ASP A 274     6723   3550   4889    602   -416    285       O  
ATOM   4207  OD2 ASP A 274     -28.690 -45.456   5.223  1.00 41.84           O  
ANISOU 4207  OD2 ASP A 274     6907   3858   5133    423   -401    255       O  
ATOM   4208  H   ASP A 274     -29.696 -45.276   1.897  1.00 28.24           H  
ATOM   4209  HA  ASP A 274     -30.284 -42.871   2.732  1.00 29.25           H  
ATOM   4210  HB2 ASP A 274     -27.898 -44.335   3.165  1.00 28.91           H  
ATOM   4211  HB3 ASP A 274     -28.265 -43.003   3.951  1.00 28.91           H  
ATOM   4212  N   LEU A 275     -28.001 -43.056   0.521  1.00 24.95           N  
ANISOU 4212  N   LEU A 275     4961   1491   3027     88   -586    399       N  
ATOM   4213  CA  LEU A 275     -27.184 -42.298  -0.406  1.00 24.69           C  
ANISOU 4213  CA  LEU A 275     4988   1407   2986    -49   -639    427       C  
ATOM   4214  C   LEU A 275     -28.118 -41.553  -1.333  1.00 29.34           C  
ANISOU 4214  C   LEU A 275     5604   1969   3576    -10   -671    462       C  
ATOM   4215  O   LEU A 275     -27.934 -40.363  -1.577  1.00 26.22           O  
ANISOU 4215  O   LEU A 275     5290   1506   3166    -38   -731    461       O  
ATOM   4216  CB  LEU A 275     -26.242 -43.207  -1.199  1.00 23.97           C  
ANISOU 4216  CB  LEU A 275     4813   1392   2903   -194   -601    460       C  
ATOM   4217  CG  LEU A 275     -25.404 -42.502  -2.274  1.00 29.90           C  
ANISOU 4217  CG  LEU A 275     5594   2128   3640   -337   -638    497       C  
ATOM   4218  CD1 LEU A 275     -24.572 -41.372  -1.669  1.00 32.96           C  
ANISOU 4218  CD1 LEU A 275     6064   2446   4013   -386   -702    472       C  
ATOM   4219  CD2 LEU A 275     -24.510 -43.494  -3.006  1.00 25.15           C  
ANISOU 4219  CD2 LEU A 275     4907   1608   3041   -461   -586    528       C  
ATOM   4220  H   LEU A 275     -27.948 -43.909   0.423  1.00 29.94           H  
ATOM   4221  HA  LEU A 275     -26.652 -41.651   0.083  1.00 29.63           H  
ATOM   4222  HB2 LEU A 275     -25.626 -43.628  -0.579  1.00 28.76           H  
ATOM   4223  HB3 LEU A 275     -26.772 -43.888  -1.643  1.00 28.76           H  
ATOM   4224  HG  LEU A 275     -26.004 -42.109  -2.927  1.00 35.88           H  
ATOM   4225 HD11 LEU A 275     -23.976 -41.743  -0.999  1.00 39.55           H  
ATOM   4226 HD12 LEU A 275     -24.056 -40.949  -2.372  1.00 39.55           H  
ATOM   4227 HD13 LEU A 275     -25.168 -40.726  -1.260  1.00 39.55           H  
ATOM   4228 HD21 LEU A 275     -25.066 -44.166  -3.430  1.00 30.18           H  
ATOM   4229 HD22 LEU A 275     -23.995 -43.019  -3.677  1.00 30.18           H  
ATOM   4230 HD23 LEU A 275     -23.914 -43.913  -2.366  1.00 30.18           H  
ATOM   4231  N   ASP A 276     -29.131 -42.252  -1.833  1.00 24.84           N  
ANISOU 4231  N   ASP A 276     4966   1448   3026     55   -638    496       N  
ATOM   4232  CA  ASP A 276     -30.157 -41.604  -2.637  1.00 30.19           C  
ANISOU 4232  CA  ASP A 276     5661   2102   3709    109   -671    532       C  
ATOM   4233  C   ASP A 276     -30.809 -40.444  -1.872  1.00 28.83           C  
ANISOU 4233  C   ASP A 276     5569   1853   3530    237   -708    497       C  
ATOM   4234  O   ASP A 276     -30.996 -39.349  -2.418  1.00 37.00           O  
ANISOU 4234  O   ASP A 276     6672   2827   4560    230   -764    511       O  
ATOM   4235  CB  ASP A 276     -31.210 -42.623  -3.076  1.00 24.88           C  
ANISOU 4235  CB  ASP A 276     4894   1499   3062    171   -635    574       C  
ATOM   4236  CG  ASP A 276     -30.656 -43.647  -4.055  1.00 29.93           C  
ANISOU 4236  CG  ASP A 276     5468   2206   3698     42   -608    608       C  
ATOM   4237  OD1 ASP A 276     -29.597 -43.382  -4.660  1.00 32.05           O  
ANISOU 4237  OD1 ASP A 276     5767   2467   3943    -90   -620    612       O  
ATOM   4238  OD2 ASP A 276     -31.280 -44.716  -4.222  1.00 38.76           O  
ANISOU 4238  OD2 ASP A 276     6472   3417   4836     73   -565    619       O  
ATOM   4239  H   ASP A 276     -29.246 -43.097  -1.723  1.00 29.81           H  
ATOM   4240  HA  ASP A 276     -29.745 -41.239  -3.436  1.00 36.23           H  
ATOM   4241  HB2 ASP A 276     -31.535 -43.098  -2.296  1.00 29.86           H  
ATOM   4242  HB3 ASP A 276     -31.941 -42.156  -3.511  1.00 29.86           H  
ATOM   4243  N   ASN A 277     -31.142 -40.683  -0.606  1.00 29.10           N  
ANISOU 4243  N   ASN A 277     5602   1893   3564    357   -676    452       N  
ATOM   4244  CA  ASN A 277     -31.685 -39.632   0.249  1.00 29.76           C  
ANISOU 4244  CA  ASN A 277     5769   1909   3630    486   -701    407       C  
ATOM   4245  C   ASN A 277     -30.763 -38.423   0.305  1.00 30.42           C  
ANISOU 4245  C   ASN A 277     5972   1900   3684    402   -773    375       C  
ATOM   4246  O   ASN A 277     -31.222 -37.286   0.208  1.00 40.31           O  
ANISOU 4246  O   ASN A 277     7305   3082   4929    457   -822    367       O  
ATOM   4247  CB  ASN A 277     -31.937 -40.135   1.674  1.00 34.12           C  
ANISOU 4247  CB  ASN A 277     6306   2491   4167    611   -649    357       C  
ATOM   4248  CG  ASN A 277     -33.124 -41.070   1.767  1.00 36.49           C  
ANISOU 4248  CG  ASN A 277     6492   2878   4496    734   -584    393       C  
ATOM   4249  OD1 ASN A 277     -33.888 -41.225   0.816  1.00 31.69           O  
ANISOU 4249  OD1 ASN A 277     5824   2297   3920    741   -588    453       O  
ATOM   4250  ND2 ASN A 277     -33.299 -41.682   2.933  1.00 31.12           N  
ANISOU 4250  ND2 ASN A 277     5780   2243   3800    831   -527    363       N  
ATOM   4251  H   ASN A 277     -31.062 -41.447  -0.218  1.00 34.93           H  
ATOM   4252  HA  ASN A 277     -32.534 -39.340  -0.117  1.00 35.71           H  
ATOM   4253  HB2 ASN A 277     -31.153 -40.614   1.983  1.00 40.95           H  
ATOM   4254  HB3 ASN A 277     -32.109 -39.374   2.251  1.00 40.95           H  
ATOM   4255 HD21 ASN A 277     -32.752 -41.536   3.581  1.00 37.34           H  
ATOM   4256 HD22 ASN A 277     -33.958 -42.224   3.040  1.00 37.34           H  
ATOM   4257  N   LEU A 278     -29.466 -38.667   0.468  1.00 27.97           N  
ANISOU 4257  N   LEU A 278     5672   1594   3361    269   -781    361       N  
ATOM   4258  CA  LEU A 278     -28.495 -37.580   0.435  1.00 28.84           C  
ANISOU 4258  CA  LEU A 278     5882   1627   3448    165   -856    345       C  
ATOM   4259  C   LEU A 278     -28.491 -36.883  -0.927  1.00 31.43           C  
ANISOU 4259  C   LEU A 278     6229   1930   3785     79   -902    403       C  
ATOM   4260  O   LEU A 278     -28.581 -35.660  -1.002  1.00 40.07           O  
ANISOU 4260  O   LEU A 278     7420   2939   4865     89   -970    396       O  
ATOM   4261  CB  LEU A 278     -27.092 -38.095   0.766  1.00 28.29           C  
ANISOU 4261  CB  LEU A 278     5792   1585   3372     29   -853    335       C  
ATOM   4262  CG  LEU A 278     -25.960 -37.068   0.655  1.00 29.20           C  
ANISOU 4262  CG  LEU A 278     5989   1637   3470   -103   -933    336       C  
ATOM   4263  CD1 LEU A 278     -26.174 -35.901   1.606  1.00 30.46           C  
ANISOU 4263  CD1 LEU A 278     6281   1697   3597    -17  -1000    278       C  
ATOM   4264  CD2 LEU A 278     -24.615 -37.724   0.913  1.00 28.64           C  
ANISOU 4264  CD2 LEU A 278     5867   1613   3402   -237   -922    340       C  
ATOM   4265  H   LEU A 278     -29.126 -39.446   0.598  1.00 33.56           H  
ATOM   4266  HA  LEU A 278     -28.737 -36.923   1.105  1.00 34.60           H  
ATOM   4267  HB2 LEU A 278     -27.095 -38.424   1.679  1.00 33.95           H  
ATOM   4268  HB3 LEU A 278     -26.882 -38.824   0.161  1.00 33.95           H  
ATOM   4269  HG  LEU A 278     -25.947 -36.715  -0.248  1.00 35.04           H  
ATOM   4270 HD11 LEU A 278     -26.203 -36.237   2.516  1.00 36.56           H  
ATOM   4271 HD12 LEU A 278     -25.441 -35.275   1.508  1.00 36.56           H  
ATOM   4272 HD13 LEU A 278     -27.013 -35.466   1.387  1.00 36.56           H  
ATOM   4273 HD21 LEU A 278     -24.475 -38.425   0.257  1.00 34.37           H  
ATOM   4274 HD22 LEU A 278     -23.918 -37.054   0.836  1.00 34.37           H  
ATOM   4275 HD23 LEU A 278     -24.615 -38.102   1.806  1.00 34.37           H  
ATOM   4276  N   LEU A 279     -28.400 -37.670  -1.998  1.00 32.40           N  
ANISOU 4276  N   LEU A 279     6263   2125   3925     -4   -867    460       N  
ATOM   4277  CA  LEU A 279     -28.291 -37.137  -3.353  1.00 29.01           C  
ANISOU 4277  CA  LEU A 279     5844   1685   3493   -100   -904    519       C  
ATOM   4278  C   LEU A 279     -29.480 -36.256  -3.708  1.00 29.92           C  
ANISOU 4278  C   LEU A 279     6011   1743   3616      7   -944    533       C  
ATOM   4279  O   LEU A 279     -29.324 -35.257  -4.409  1.00 30.86           O  
ANISOU 4279  O   LEU A 279     6196   1805   3725    -50  -1006    562       O  
ATOM   4280  CB  LEU A 279     -28.169 -38.273  -4.375  1.00 28.01           C  
ANISOU 4280  CB  LEU A 279     5614   1656   3374   -181   -849    570       C  
ATOM   4281  CG  LEU A 279     -26.856 -39.061  -4.398  1.00 29.57           C  
ANISOU 4281  CG  LEU A 279     5756   1915   3563   -316   -810    572       C  
ATOM   4282  CD1 LEU A 279     -26.925 -40.145  -5.451  1.00 26.50           C  
ANISOU 4282  CD1 LEU A 279     5279   1617   3175   -371   -756    617       C  
ATOM   4283  CD2 LEU A 279     -25.659 -38.163  -4.663  1.00 28.11           C  
ANISOU 4283  CD2 LEU A 279     5626   1695   3360   -451   -861    587       C  
ATOM   4284  H   LEU A 279     -28.399 -38.529  -1.964  1.00 38.89           H  
ATOM   4285  HA  LEU A 279     -27.490 -36.594  -3.413  1.00 34.81           H  
ATOM   4286  HB2 LEU A 279     -28.880 -38.910  -4.202  1.00 33.62           H  
ATOM   4287  HB3 LEU A 279     -28.289 -37.895  -5.260  1.00 33.62           H  
ATOM   4288  HG  LEU A 279     -26.727 -39.487  -3.536  1.00 35.48           H  
ATOM   4289 HD11 LEU A 279     -27.072 -39.734  -6.317  1.00 31.80           H  
ATOM   4290 HD12 LEU A 279     -26.089 -40.635  -5.455  1.00 31.80           H  
ATOM   4291 HD13 LEU A 279     -27.659 -40.743  -5.240  1.00 31.80           H  
ATOM   4292 HD21 LEU A 279     -25.605 -37.496  -3.961  1.00 33.73           H  
ATOM   4293 HD22 LEU A 279     -24.854 -38.704  -4.669  1.00 33.73           H  
ATOM   4294 HD23 LEU A 279     -25.774 -37.731  -5.524  1.00 33.73           H  
ATOM   4295  N   ALA A 280     -30.666 -36.626  -3.233  1.00 36.33           N  
ANISOU 4295  N   ALA A 280     6786   2571   4446    164   -909    519       N  
ATOM   4296  CA  ALA A 280     -31.854 -35.807  -3.464  1.00 35.53           C  
ANISOU 4296  CA  ALA A 280     6722   2420   4358    283   -943    533       C  
ATOM   4297  C   ALA A 280     -31.662 -34.371  -2.964  1.00 40.23           C  
ANISOU 4297  C   ALA A 280     7450   2902   4933    311  -1013    494       C  
ATOM   4298  O   ALA A 280     -32.124 -33.419  -3.592  1.00 40.22           O  
ANISOU 4298  O   ALA A 280     7505   2839   4937    328  -1068    521       O  
ATOM   4299  CB  ALA A 280     -33.060 -36.438  -2.804  1.00 30.43           C  
ANISOU 4299  CB  ALA A 280     6006   1819   3735    454   -887    523       C  
ATOM   4300  H   ALA A 280     -30.810 -37.341  -2.777  1.00 43.60           H  
ATOM   4301  HA  ALA A 280     -32.025 -35.768  -4.418  1.00 42.64           H  
ATOM   4302  HB1 ALA A 280     -32.897 -36.507  -1.850  1.00 36.51           H  
ATOM   4303  HB2 ALA A 280     -33.837 -35.881  -2.968  1.00 36.51           H  
ATOM   4304  HB3 ALA A 280     -33.200 -37.321  -3.180  1.00 36.51           H  
ATOM   4305  N   GLN A 281     -30.976 -34.227  -1.834  1.00 39.79           N  
ANISOU 4305  N   GLN A 281     7448   2816   4853    314  -1017    430       N  
ATOM   4306  CA  GLN A 281     -30.761 -32.921  -1.217  1.00 42.95           C  
ANISOU 4306  CA  GLN A 281     7985   3108   5228    343  -1089    384       C  
ATOM   4307  C   GLN A 281     -29.612 -32.138  -1.851  1.00 46.64           C  
ANISOU 4307  C   GLN A 281     8520   3520   5680    169  -1166    411       C  
ATOM   4308  O   GLN A 281     -29.762 -30.950  -2.141  1.00 57.59           O  
ANISOU 4308  O   GLN A 281    10005   4817   7061    173  -1240    418       O  
ATOM   4309  CB  GLN A 281     -30.500 -33.083   0.285  1.00 39.14           C  
ANISOU 4309  CB  GLN A 281     7540   2616   4715    416  -1069    304       C  
ATOM   4310  CG  GLN A 281     -31.730 -33.499   1.082  1.00 35.51           C  
ANISOU 4310  CG  GLN A 281     7040   2193   4258    617  -1002    271       C  
ATOM   4311  CD  GLN A 281     -31.395 -34.241   2.363  1.00 43.57           C  
ANISOU 4311  CD  GLN A 281     8045   3257   5251    662   -951    213       C  
ATOM   4312  OE1 GLN A 281     -30.290 -34.127   2.893  1.00 54.21           O  
ANISOU 4312  OE1 GLN A 281     9450   4578   6570    568   -986    179       O  
ATOM   4313  NE2 GLN A 281     -32.356 -35.012   2.865  1.00 57.47           N  
ANISOU 4313  NE2 GLN A 281     9724   5091   7020    806   -871    207       N  
ATOM   4314  H   GLN A 281     -30.621 -34.879  -1.399  1.00 47.75           H  
ATOM   4315  HA  GLN A 281     -31.569 -32.393  -1.320  1.00 51.55           H  
ATOM   4316  HB2 GLN A 281     -29.820 -33.762   0.413  1.00 46.97           H  
ATOM   4317  HB3 GLN A 281     -30.189 -32.236   0.641  1.00 46.97           H  
ATOM   4318  HG2 GLN A 281     -32.233 -32.705   1.321  1.00 42.61           H  
ATOM   4319  HG3 GLN A 281     -32.276 -34.084   0.534  1.00 42.61           H  
ATOM   4320 HE21 GLN A 281     -33.116 -35.068   2.465  1.00 68.96           H  
ATOM   4321 HE22 GLN A 281     -32.218 -35.454   3.590  1.00 68.96           H  
ATOM   4322  N   ILE A 282     -28.474 -32.793  -2.065  1.00 41.06           N  
ANISOU 4322  N   ILE A 282     7760   2871   4970     19  -1148    430       N  
ATOM   4323  CA  ILE A 282     -27.263 -32.087  -2.491  1.00 34.44           C  
ANISOU 4323  CA  ILE A 282     6976   1994   4117   -148  -1216    458       C  
ATOM   4324  C   ILE A 282     -27.013 -32.086  -4.004  1.00 37.59           C  
ANISOU 4324  C   ILE A 282     7329   2429   4523   -273  -1221    541       C  
ATOM   4325  O   ILE A 282     -26.173 -31.332  -4.492  1.00 40.69           O  
ANISOU 4325  O   ILE A 282     7770   2785   4904   -399  -1282    576       O  
ATOM   4326  CB  ILE A 282     -26.010 -32.632  -1.776  1.00 33.49           C  
ANISOU 4326  CB  ILE A 282     6829   1911   3986   -247  -1204    434       C  
ATOM   4327  CG1 ILE A 282     -25.812 -34.124  -2.063  1.00 35.30           C  
ANISOU 4327  CG1 ILE A 282     6918   2261   4232   -286  -1109    456       C  
ATOM   4328  CG2 ILE A 282     -26.123 -32.396  -0.278  1.00 33.89           C  
ANISOU 4328  CG2 ILE A 282     6954   1909   4015   -140  -1221    351       C  
ATOM   4329  CD1 ILE A 282     -24.400 -34.598  -1.801  1.00 33.31           C  
ANISOU 4329  CD1 ILE A 282     6624   2055   3978   -428  -1102    461       C  
ATOM   4330  H   ILE A 282     -28.374 -33.642  -1.971  1.00 49.27           H  
ATOM   4331  HA  ILE A 282     -27.356 -31.159  -2.224  1.00 41.33           H  
ATOM   4332  HB  ILE A 282     -25.235 -32.151  -2.105  1.00 40.19           H  
ATOM   4333 HG12 ILE A 282     -26.409 -34.636  -1.495  1.00 42.35           H  
ATOM   4334 HG13 ILE A 282     -26.016 -34.295  -2.996  1.00 42.35           H  
ATOM   4335 HG21 ILE A 282     -26.910 -32.855   0.055  1.00 40.67           H  
ATOM   4336 HG22 ILE A 282     -25.329 -32.744   0.157  1.00 40.67           H  
ATOM   4337 HG23 ILE A 282     -26.200 -31.443  -0.113  1.00 40.67           H  
ATOM   4338 HD11 ILE A 282     -24.183 -34.443  -0.868  1.00 39.98           H  
ATOM   4339 HD12 ILE A 282     -24.343 -35.545  -2.001  1.00 39.98           H  
ATOM   4340 HD13 ILE A 282     -23.790 -34.102  -2.370  1.00 39.98           H  
ATOM   4341  N   GLY A 283     -27.733 -32.929  -4.740  1.00 36.23           N  
ANISOU 4341  N   GLY A 283     7067   2332   4368   -239  -1160    576       N  
ATOM   4342  CA  GLY A 283     -27.617 -32.973  -6.189  1.00 33.11           C  
ANISOU 4342  CA  GLY A 283     6635   1977   3969   -342  -1162    652       C  
ATOM   4343  C   GLY A 283     -26.927 -34.227  -6.694  1.00 32.36           C  
ANISOU 4343  C   GLY A 283     6429   1997   3869   -446  -1088    680       C  
ATOM   4344  O   GLY A 283     -25.945 -34.692  -6.113  1.00 31.41           O  
ANISOU 4344  O   GLY A 283     6278   1910   3745   -513  -1062    658       O  
ATOM   4345  H   GLY A 283     -28.301 -33.490  -4.418  1.00 43.48           H  
ATOM   4346  HA2 GLY A 283     -28.502 -32.932  -6.583  1.00 39.73           H  
ATOM   4347  HA3 GLY A 283     -27.112 -32.203  -6.493  1.00 39.73           H  
ATOM   4348  N   ASP A 284     -27.441 -34.760  -7.797  1.00 36.78           N  
ANISOU 4348  N   ASP A 284     6932   2617   4426   -458  -1058    729       N  
ATOM   4349  CA  ASP A 284     -26.964 -36.014  -8.365  1.00 31.51           C  
ANISOU 4349  CA  ASP A 284     6163   2059   3748   -538   -984    753       C  
ATOM   4350  C   ASP A 284     -25.544 -35.904  -8.910  1.00 30.66           C  
ANISOU 4350  C   ASP A 284     6047   1988   3615   -708   -982    789       C  
ATOM   4351  O   ASP A 284     -24.911 -36.904  -9.239  1.00 34.77           O  
ANISOU 4351  O   ASP A 284     6488   2600   4125   -781   -916    802       O  
ATOM   4352  CB  ASP A 284     -27.903 -36.454  -9.485  1.00 30.18           C  
ANISOU 4352  CB  ASP A 284     5958   1936   3574   -512   -970    799       C  
ATOM   4353  CG  ASP A 284     -29.231 -36.962  -8.964  1.00 37.49           C  
ANISOU 4353  CG  ASP A 284     6849   2864   4532   -354   -951    775       C  
ATOM   4354  OD1 ASP A 284     -29.238 -37.992  -8.261  1.00 33.11           O  
ANISOU 4354  OD1 ASP A 284     6230   2360   3992   -314   -893    741       O  
ATOM   4355  OD2 ASP A 284     -30.266 -36.339  -9.269  1.00 45.28           O  
ANISOU 4355  OD2 ASP A 284     7869   3804   5530   -271   -994    795       O  
ATOM   4356  H   ASP A 284     -28.084 -34.404  -8.244  1.00 44.14           H  
ATOM   4357  HA  ASP A 284     -26.972 -36.698  -7.677  1.00 37.81           H  
ATOM   4358  HB2 ASP A 284     -28.077 -35.698 -10.066  1.00 36.22           H  
ATOM   4359  HB3 ASP A 284     -27.483 -37.170  -9.987  1.00 36.22           H  
ATOM   4360  N   GLN A 285     -25.069 -34.673  -9.028  1.00 33.30           N  
ANISOU 4360  N   GLN A 285     6462   2250   3939   -768  -1054    808       N  
ATOM   4361  CA  GLN A 285     -23.696 -34.395  -9.441  1.00 32.40           C  
ANISOU 4361  CA  GLN A 285     6340   2163   3806   -929  -1062    850       C  
ATOM   4362  C   GLN A 285     -22.652 -35.003  -8.495  1.00 32.24           C  
ANISOU 4362  C   GLN A 285     6268   2185   3799   -975  -1025    816       C  
ATOM   4363  O   GLN A 285     -21.492 -35.161  -8.878  1.00 32.95           O  
ANISOU 4363  O   GLN A 285     6309   2332   3876  -1106  -1003    855       O  
ATOM   4364  CB  GLN A 285     -23.421 -32.876  -9.586  1.00 33.97           C  
ANISOU 4364  CB  GLN A 285     6644   2263   3998   -979  -1162    877       C  
ATOM   4365  CG  GLN A 285     -24.568 -31.878  -9.241  1.00 46.22           C  
ANISOU 4365  CG  GLN A 285     8300   3699   5563   -852  -1236    849       C  
ATOM   4366  CD  GLN A 285     -24.142 -30.706  -8.351  1.00 57.56           C  
ANISOU 4366  CD  GLN A 285     9841   5024   7004   -856  -1324    819       C  
ATOM   4367  OE1 GLN A 285     -24.972 -30.129  -7.641  1.00 61.87           O  
ANISOU 4367  OE1 GLN A 285    10463   5482   7562   -729  -1366    770       O  
ATOM   4368  NE2 GLN A 285     -22.866 -30.335  -8.399  1.00 62.18           N  
ANISOU 4368  NE2 GLN A 285    10432   5615   7580  -1000  -1355    851       N  
ATOM   4369  H   GLN A 285     -25.530 -33.965  -8.872  1.00 39.95           H  
ATOM   4370  HA  GLN A 285     -23.559 -34.795 -10.314  1.00 38.88           H  
ATOM   4371  HB2 GLN A 285     -22.673 -32.654  -9.010  1.00 40.76           H  
ATOM   4372  HB3 GLN A 285     -23.170 -32.707 -10.508  1.00 40.76           H  
ATOM   4373  HG2 GLN A 285     -24.916 -31.509 -10.068  1.00 55.47           H  
ATOM   4374  HG3 GLN A 285     -25.270 -32.360  -8.777  1.00 55.47           H  
ATOM   4375 HE21 GLN A 285     -22.317 -30.749  -8.916  1.00 74.62           H  
ATOM   4376 HE22 GLN A 285     -22.590 -29.681  -7.914  1.00 74.62           H  
ATOM   4377  N   TYR A 286     -23.053 -35.335  -7.269  1.00 31.23           N  
ANISOU 4377  N   TYR A 286     6144   2029   3694   -869  -1017    748       N  
ATOM   4378  CA  TYR A 286     -22.112 -35.832  -6.259  1.00 32.55           C  
ANISOU 4378  CA  TYR A 286     6272   2223   3874   -905   -995    713       C  
ATOM   4379  C   TYR A 286     -22.053 -37.356  -6.175  1.00 29.40           C  
ANISOU 4379  C   TYR A 286     5762   1925   3485   -892   -897    699       C  
ATOM   4380  O   TYR A 286     -21.270 -37.900  -5.402  1.00 33.45           O  
ANISOU 4380  O   TYR A 286     6229   2470   4011   -924   -872    675       O  
ATOM   4381  CB  TYR A 286     -22.473 -35.274  -4.882  1.00 31.12           C  
ANISOU 4381  CB  TYR A 286     6172   1950   3703   -802  -1048    643       C  
ATOM   4382  CG  TYR A 286     -22.278 -33.782  -4.752  1.00 42.14           C  
ANISOU 4382  CG  TYR A 286     7686   3239   5087   -829  -1152    648       C  
ATOM   4383  CD1 TYR A 286     -21.028 -33.251  -4.476  1.00 48.38           C  
ANISOU 4383  CD1 TYR A 286     8497   4012   5873   -953  -1204    665       C  
ATOM   4384  CD2 TYR A 286     -23.344 -32.905  -4.896  1.00 34.31           C  
ANISOU 4384  CD2 TYR A 286     6784   2161   4090   -729  -1202    638       C  
ATOM   4385  CE1 TYR A 286     -20.843 -31.890  -4.352  1.00 48.17           C  
ANISOU 4385  CE1 TYR A 286     8584   3882   5835   -983  -1308    671       C  
ATOM   4386  CE2 TYR A 286     -23.167 -31.543  -4.773  1.00 34.86           C  
ANISOU 4386  CE2 TYR A 286     6969   2126   4149   -752  -1302    641       C  
ATOM   4387  CZ  TYR A 286     -21.913 -31.040  -4.501  1.00 44.15           C  
ANISOU 4387  CZ  TYR A 286     8172   3284   5320   -881  -1357    657       C  
ATOM   4388  OH  TYR A 286     -21.721 -29.680  -4.375  1.00 54.28           O  
ANISOU 4388  OH  TYR A 286     9576   4457   6591   -910  -1465    662       O  
ATOM   4389  H   TYR A 286     -23.866 -35.281  -6.994  1.00 37.48           H  
ATOM   4390  HA  TYR A 286     -21.223 -35.515  -6.482  1.00 39.06           H  
ATOM   4391  HB2 TYR A 286     -23.407 -35.467  -4.702  1.00 37.35           H  
ATOM   4392  HB3 TYR A 286     -21.915 -35.704  -4.215  1.00 37.35           H  
ATOM   4393  HD1 TYR A 286     -20.301 -33.822  -4.375  1.00 58.06           H  
ATOM   4394  HD2 TYR A 286     -24.192 -33.241  -5.079  1.00 41.17           H  
ATOM   4395  HE1 TYR A 286     -19.997 -31.548  -4.168  1.00 57.80           H  
ATOM   4396  HE2 TYR A 286     -23.890 -30.967  -4.873  1.00 41.83           H  
ATOM   4397  HH  TYR A 286     -22.449 -29.276  -4.487  1.00 65.13           H  
ATOM   4398  N   ALA A 287     -22.883 -38.033  -6.960  1.00 28.78           N  
ANISOU 4398  N   ALA A 287     5642   1893   3400   -845   -849    716       N  
ATOM   4399  CA  ALA A 287     -22.951 -39.492  -6.939  1.00 31.44           C  
ANISOU 4399  CA  ALA A 287     5883   2319   3745   -826   -763    704       C  
ATOM   4400  C   ALA A 287     -21.585 -40.131  -7.185  1.00 27.35           C  
ANISOU 4400  C   ALA A 287     5287   1884   3220   -957   -710    728       C  
ATOM   4401  O   ALA A 287     -21.123 -40.964  -6.395  1.00 33.51           O  
ANISOU 4401  O   ALA A 287     6010   2701   4021   -953   -668    697       O  
ATOM   4402  CB  ALA A 287     -23.957 -39.974  -7.970  1.00 27.21           C  
ANISOU 4402  CB  ALA A 287     5325   1818   3195   -783   -736    732       C  
ATOM   4403  H   ALA A 287     -23.424 -37.668  -7.520  1.00 34.54           H  
ATOM   4404  HA  ALA A 287     -23.260 -39.778  -6.066  1.00 37.73           H  
ATOM   4405  HB1 ALA A 287     -23.676 -39.674  -8.849  1.00 32.65           H  
ATOM   4406  HB2 ALA A 287     -23.992 -40.943  -7.946  1.00 32.65           H  
ATOM   4407  HB3 ALA A 287     -24.828 -39.605  -7.757  1.00 32.65           H  
ATOM   4408  N   ASP A 288     -20.941 -39.735  -8.276  1.00 28.04           N  
ANISOU 4408  N   ASP A 288     5370   2004   3279  -1069   -712    787       N  
ATOM   4409  CA  ASP A 288     -19.672 -40.332  -8.673  1.00 36.75           C  
ANISOU 4409  CA  ASP A 288     6390   3200   4372  -1190   -651    821       C  
ATOM   4410  C   ASP A 288     -18.602 -40.214  -7.591  1.00 29.74           C  
ANISOU 4410  C   ASP A 288     5478   2307   3516  -1239   -667    803       C  
ATOM   4411  O   ASP A 288     -17.731 -41.081  -7.454  1.00 35.60           O  
ANISOU 4411  O   ASP A 288     6129   3129   4268  -1295   -605    808       O  
ATOM   4412  CB  ASP A 288     -19.183 -39.698  -9.972  1.00 38.53           C  
ANISOU 4412  CB  ASP A 288     6628   3455   4558  -1297   -658    894       C  
ATOM   4413  CG  ASP A 288     -19.957 -40.191 -11.179  1.00 49.39           C  
ANISOU 4413  CG  ASP A 288     8001   4874   5892  -1275   -619    917       C  
ATOM   4414  OD1 ASP A 288     -21.204 -40.160 -11.137  1.00 50.57           O  
ANISOU 4414  OD1 ASP A 288     8195   4973   6047  -1170   -648    892       O  
ATOM   4415  OD2 ASP A 288     -19.321 -40.629 -12.161  1.00 46.76           O  
ANISOU 4415  OD2 ASP A 288     7621   4629   5518  -1360   -559    962       O  
ATOM   4416  H   ASP A 288     -21.220 -39.118  -8.806  1.00 33.65           H  
ATOM   4417  HA  ASP A 288     -19.815 -41.277  -8.843  1.00 44.10           H  
ATOM   4418  HB2 ASP A 288     -19.292 -38.736  -9.917  1.00 46.24           H  
ATOM   4419  HB3 ASP A 288     -18.248 -39.921 -10.102  1.00 46.24           H  
ATOM   4420  N   LEU A 289     -18.685 -39.138  -6.820  1.00 29.99           N  
ANISOU 4420  N   LEU A 289     5594   2242   3561  -1217   -755    782       N  
ATOM   4421  CA  LEU A 289     -17.747 -38.888  -5.737  1.00 31.22           C  
ANISOU 4421  CA  LEU A 289     5746   2377   3741  -1262   -793    763       C  
ATOM   4422  C   LEU A 289     -17.845 -39.983  -4.672  1.00 29.56           C  
ANISOU 4422  C   LEU A 289     5484   2192   3556  -1191   -748    705       C  
ATOM   4423  O   LEU A 289     -16.833 -40.480  -4.180  1.00 38.15           O  
ANISOU 4423  O   LEU A 289     6501   3330   4663  -1257   -726    707       O  
ATOM   4424  CB  LEU A 289     -18.034 -37.520  -5.121  1.00 35.59           C  
ANISOU 4424  CB  LEU A 289     6422   2808   4291  -1231   -903    741       C  
ATOM   4425  CG  LEU A 289     -17.210 -37.067  -3.917  1.00 37.25           C  
ANISOU 4425  CG  LEU A 289     6661   2974   4517  -1267   -968    714       C  
ATOM   4426  CD1 LEU A 289     -15.735 -36.970  -4.266  1.00 31.46           C  
ANISOU 4426  CD1 LEU A 289     5856   2303   3793  -1429   -970    779       C  
ATOM   4427  CD2 LEU A 289     -17.739 -35.728  -3.423  1.00 41.72           C  
ANISOU 4427  CD2 LEU A 289     7370   3412   5071  -1214  -1074    686       C  
ATOM   4428  H   LEU A 289     -19.285 -38.528  -6.907  1.00 35.99           H  
ATOM   4429  HA  LEU A 289     -16.842 -38.883  -6.088  1.00 37.47           H  
ATOM   4430  HB2 LEU A 289     -17.907 -36.852  -5.813  1.00 42.70           H  
ATOM   4431  HB3 LEU A 289     -18.963 -37.511  -4.842  1.00 42.70           H  
ATOM   4432  HG  LEU A 289     -17.309 -37.715  -3.201  1.00 44.69           H  
ATOM   4433 HD11 LEU A 289     -15.623 -36.326  -4.983  1.00 37.75           H  
ATOM   4434 HD12 LEU A 289     -15.244 -36.681  -3.481  1.00 37.75           H  
ATOM   4435 HD13 LEU A 289     -15.421 -37.842  -4.551  1.00 37.75           H  
ATOM   4436 HD21 LEU A 289     -18.668 -35.832  -3.165  1.00 50.06           H  
ATOM   4437 HD22 LEU A 289     -17.213 -35.444  -2.658  1.00 50.06           H  
ATOM   4438 HD23 LEU A 289     -17.663 -35.076  -4.137  1.00 50.06           H  
ATOM   4439  N   PHE A 290     -19.073 -40.352  -4.323  1.00 27.36           N  
ANISOU 4439  N   PHE A 290     5236   1880   3278  -1056   -734    658       N  
ATOM   4440  CA  PHE A 290     -19.309 -41.413  -3.348  1.00 26.34           C  
ANISOU 4440  CA  PHE A 290     5064   1774   3171   -978   -690    607       C  
ATOM   4441  C   PHE A 290     -19.044 -42.793  -3.941  1.00 25.46           C  
ANISOU 4441  C   PHE A 290     4839   1768   3065  -1011   -593    627       C  
ATOM   4442  O   PHE A 290     -18.544 -43.700  -3.253  1.00 24.87           O  
ANISOU 4442  O   PHE A 290     4700   1736   3014  -1017   -554    606       O  
ATOM   4443  CB  PHE A 290     -20.741 -41.327  -2.814  1.00 26.51           C  
ANISOU 4443  CB  PHE A 290     5149   1733   3191   -819   -705    559       C  
ATOM   4444  CG  PHE A 290     -20.974 -40.153  -1.903  1.00 26.86           C  
ANISOU 4444  CG  PHE A 290     5304   1673   3227   -762   -790    520       C  
ATOM   4445  CD1 PHE A 290     -20.741 -40.257  -0.543  1.00 26.80           C  
ANISOU 4445  CD1 PHE A 290     5322   1637   3223   -719   -809    467       C  
ATOM   4446  CD2 PHE A 290     -21.413 -38.942  -2.410  1.00 27.81           C  
ANISOU 4446  CD2 PHE A 290     5512   1725   3331   -753   -852    536       C  
ATOM   4447  CE1 PHE A 290     -20.949 -39.176   0.296  1.00 28.33           C  
ANISOU 4447  CE1 PHE A 290     5631   1736   3399   -663   -888    425       C  
ATOM   4448  CE2 PHE A 290     -21.623 -37.859  -1.577  1.00 30.53           C  
ANISOU 4448  CE2 PHE A 290     5968   1971   3663   -698   -931    497       C  
ATOM   4449  CZ  PHE A 290     -21.390 -37.976  -0.222  1.00 29.26           C  
ANISOU 4449  CZ  PHE A 290     5835   1782   3499   -651   -948    439       C  
ATOM   4450  H   PHE A 290     -19.792 -40.001  -4.638  1.00 32.83           H  
ATOM   4451  HA  PHE A 290     -18.705 -41.290  -2.599  1.00 31.61           H  
ATOM   4452  HB2 PHE A 290     -21.350 -41.247  -3.564  1.00 31.81           H  
ATOM   4453  HB3 PHE A 290     -20.938 -42.135  -2.315  1.00 31.81           H  
ATOM   4454  HD1 PHE A 290     -20.444 -41.064  -0.188  1.00 32.16           H  
ATOM   4455  HD2 PHE A 290     -21.571 -38.857  -3.322  1.00 33.38           H  
ATOM   4456  HE1 PHE A 290     -20.792 -39.259   1.209  1.00 34.00           H  
ATOM   4457  HE2 PHE A 290     -21.920 -37.052  -1.930  1.00 36.64           H  
ATOM   4458  HZ  PHE A 290     -21.531 -37.249   0.340  1.00 35.11           H  
ATOM   4459  N   LEU A 291     -19.384 -42.961  -5.215  1.00 25.43           N  
ANISOU 4459  N   LEU A 291     4820   1806   3038  -1032   -558    666       N  
ATOM   4460  CA  LEU A 291     -19.062 -44.204  -5.904  1.00 24.81           C  
ANISOU 4460  CA  LEU A 291     4648   1827   2953  -1072   -467    685       C  
ATOM   4461  C   LEU A 291     -17.552 -44.460  -5.867  1.00 28.78           C  
ANISOU 4461  C   LEU A 291     5071   2400   3465  -1193   -434    713       C  
ATOM   4462  O   LEU A 291     -17.108 -45.590  -5.630  1.00 29.38           O  
ANISOU 4462  O   LEU A 291     5039   2567   3558  -1180   -362    688       O  
ATOM   4463  CB  LEU A 291     -19.581 -44.167  -7.341  1.00 26.86           C  
ANISOU 4463  CB  LEU A 291     4921   2114   3170  -1088   -447    725       C  
ATOM   4464  CG  LEU A 291     -21.101 -43.982  -7.469  1.00 36.98           C  
ANISOU 4464  CG  LEU A 291     6263   3338   4447   -971   -481    708       C  
ATOM   4465  CD1 LEU A 291     -21.526 -43.751  -8.914  1.00 40.53           C  
ANISOU 4465  CD1 LEU A 291     6737   3809   4853  -1001   -480    754       C  
ATOM   4466  CD2 LEU A 291     -21.850 -45.163  -6.883  1.00 43.86           C  
ANISOU 4466  CD2 LEU A 291     7084   4237   5343   -866   -437    662       C  
ATOM   4467  H   LEU A 291     -19.797 -42.380  -5.696  1.00 30.52           H  
ATOM   4468  HA  LEU A 291     -19.500 -44.939  -5.447  1.00 29.77           H  
ATOM   4469  HB2 LEU A 291     -19.156 -43.428  -7.805  1.00 32.23           H  
ATOM   4470  HB3 LEU A 291     -19.349 -45.002  -7.776  1.00 32.23           H  
ATOM   4471  HG  LEU A 291     -21.357 -43.196  -6.962  1.00 44.37           H  
ATOM   4472 HD11 LEU A 291     -21.263 -44.518  -9.446  1.00 48.64           H  
ATOM   4473 HD12 LEU A 291     -22.489 -43.640  -8.945  1.00 48.64           H  
ATOM   4474 HD13 LEU A 291     -21.090 -42.951  -9.246  1.00 48.64           H  
ATOM   4475 HD21 LEU A 291     -21.623 -45.246  -5.944  1.00 52.63           H  
ATOM   4476 HD22 LEU A 291     -22.803 -45.011  -6.982  1.00 52.63           H  
ATOM   4477 HD23 LEU A 291     -21.592 -45.967  -7.359  1.00 52.63           H  
ATOM   4478  N   ALA A 292     -16.762 -43.411  -6.086  1.00 26.18           N  
ANISOU 4478  N   ALA A 292     4762   2056   3129  -1285   -482    752       N  
ATOM   4479  CA  ALA A 292     -15.308 -43.524  -5.969  1.00 26.68           C  
ANISOU 4479  CA  ALA A 292     4742   2187   3209  -1400   -461    788       C  
ATOM   4480  C   ALA A 292     -14.871 -44.025  -4.584  1.00 29.33           C  
ANISOU 4480  C   ALA A 292     5039   2517   3589  -1380   -472    745       C  
ATOM   4481  O   ALA A 292     -13.996 -44.895  -4.465  1.00 30.80           O  
ANISOU 4481  O   ALA A 292     5117   2790   3796  -1429   -412    758       O  
ATOM   4482  CB  ALA A 292     -14.650 -42.187  -6.277  1.00 28.00           C  
ANISOU 4482  CB  ALA A 292     4949   2323   3367  -1493   -532    838       C  
ATOM   4483  H   ALA A 292     -17.041 -42.626  -6.302  1.00 31.41           H  
ATOM   4484  HA  ALA A 292     -14.993 -44.165  -6.626  1.00 32.02           H  
ATOM   4485  HB1 ALA A 292     -14.973 -41.524  -5.647  1.00 33.60           H  
ATOM   4486  HB2 ALA A 292     -13.688 -42.282  -6.195  1.00 33.60           H  
ATOM   4487  HB3 ALA A 292     -14.881 -41.923  -7.182  1.00 33.60           H  
ATOM   4488  N   ALA A 293     -15.489 -43.479  -3.541  1.00 26.17           N  
ANISOU 4488  N   ALA A 293     4726   2018   3199  -1302   -548    695       N  
ATOM   4489  CA  ALA A 293     -15.196 -43.889  -2.171  1.00 26.34           C  
ANISOU 4489  CA  ALA A 293     4733   2023   3252  -1273   -569    651       C  
ATOM   4490  C   ALA A 293     -15.504 -45.371  -1.985  1.00 24.81           C  
ANISOU 4490  C   ALA A 293     4426   1928   3073  -1179   -473    606       C  
ATOM   4491  O   ALA A 293     -14.698 -46.124  -1.417  1.00 29.95           O  
ANISOU 4491  O   ALA A 293     4973   2656   3752  -1193   -440    594       O  
ATOM   4492  CB  ALA A 293     -16.001 -43.051  -1.185  1.00 26.00           C  
ANISOU 4492  CB  ALA A 293     4816   1864   3201  -1178   -654    595       C  
ATOM   4493  H   ALA A 293     -16.086 -42.863  -3.601  1.00 31.40           H  
ATOM   4494  HA  ALA A 293     -14.254 -43.749  -1.990  1.00 31.61           H  
ATOM   4495  HB1 ALA A 293     -16.946 -43.177  -1.362  1.00 31.21           H  
ATOM   4496  HB2 ALA A 293     -15.792 -43.339  -0.283  1.00 31.21           H  
ATOM   4497  HB3 ALA A 293     -15.764 -42.117  -1.298  1.00 31.21           H  
ATOM   4498  N   LYS A 294     -16.668 -45.793  -2.469  1.00 24.01           N  
ANISOU 4498  N   LYS A 294     4337   1830   2954  -1080   -432    583       N  
ATOM   4499  CA  LYS A 294     -17.031 -47.203  -2.381  1.00 24.34           C  
ANISOU 4499  CA  LYS A 294     4272   1967   3010   -989   -347    542       C  
ATOM   4500  C   LYS A 294     -15.987 -48.075  -3.086  1.00 26.90           C  
ANISOU 4500  C   LYS A 294     4470   2410   3341  -1061   -267    567       C  
ATOM   4501  O   LYS A 294     -15.517 -49.076  -2.527  1.00 30.11           O  
ANISOU 4501  O   LYS A 294     4776   2889   3777  -1031   -221    540       O  
ATOM   4502  CB  LYS A 294     -18.421 -47.442  -2.971  1.00 26.82           C  
ANISOU 4502  CB  LYS A 294     4620   2266   3305   -894   -327    528       C  
ATOM   4503  CG  LYS A 294     -19.147 -48.649  -2.390  1.00 26.34           C  
ANISOU 4503  CG  LYS A 294     4487   2255   3265   -775   -278    478       C  
ATOM   4504  CD  LYS A 294     -19.051 -49.846  -3.312  1.00 28.27           C  
ANISOU 4504  CD  LYS A 294     4635   2597   3508   -781   -196    480       C  
ATOM   4505  CE  LYS A 294     -19.777 -51.049  -2.747  1.00 22.72           C  
ANISOU 4505  CE  LYS A 294     3867   1935   2832   -674   -158    437       C  
ATOM   4506  NZ  LYS A 294     -19.002 -51.701  -1.665  1.00 30.34           N  
ANISOU 4506  NZ  LYS A 294     4756   2942   3831   -663   -139    411       N  
ATOM   4507  H   LYS A 294     -17.256 -45.292  -2.847  1.00 28.81           H  
ATOM   4508  HA  LYS A 294     -17.055 -47.464  -1.447  1.00 29.21           H  
ATOM   4509  HB2 LYS A 294     -18.969 -46.659  -2.804  1.00 32.19           H  
ATOM   4510  HB3 LYS A 294     -18.334 -47.583  -3.927  1.00 32.19           H  
ATOM   4511  HG2 LYS A 294     -18.745 -48.886  -1.540  1.00 31.60           H  
ATOM   4512  HG3 LYS A 294     -20.085 -48.431  -2.270  1.00 31.60           H  
ATOM   4513  HD2 LYS A 294     -19.453 -49.624  -4.167  1.00 33.92           H  
ATOM   4514  HD3 LYS A 294     -18.118 -50.084  -3.432  1.00 33.92           H  
ATOM   4515  HE2 LYS A 294     -20.629 -50.765  -2.381  1.00 27.27           H  
ATOM   4516  HE3 LYS A 294     -19.916 -51.699  -3.453  1.00 27.27           H  
ATOM   4517  HZ1 LYS A 294     -18.865 -51.125  -1.000  1.00 36.41           H  
ATOM   4518  HZ2 LYS A 294     -19.450 -52.403  -1.351  1.00 36.41           H  
ATOM   4519  HZ3 LYS A 294     -18.216 -51.976  -1.977  1.00 36.41           H  
ATOM   4520  N   ASN A 295     -15.618 -47.694  -4.307  1.00 23.60           N  
ANISOU 4520  N   ASN A 295     4061   2014   2893  -1150   -248    623       N  
ATOM   4521  CA  ASN A 295     -14.575 -48.418  -5.030  1.00 23.84           C  
ANISOU 4521  CA  ASN A 295     3976   2161   2920  -1215   -165    651       C  
ATOM   4522  C   ASN A 295     -13.285 -48.532  -4.212  1.00 29.04           C  
ANISOU 4522  C   ASN A 295     4548   2864   3621  -1274   -169    663       C  
ATOM   4523  O   ASN A 295     -12.695 -49.617  -4.103  1.00 26.85           O  
ANISOU 4523  O   ASN A 295     4150   2683   3368  -1250    -98    645       O  
ATOM   4524  CB  ASN A 295     -14.299 -47.766  -6.389  1.00 24.68           C  
ANISOU 4524  CB  ASN A 295     4117   2280   2978  -1315   -152    720       C  
ATOM   4525  CG  ASN A 295     -15.472 -47.903  -7.347  1.00 24.34           C  
ANISOU 4525  CG  ASN A 295     4139   2221   2890  -1257   -136    711       C  
ATOM   4526  OD1 ASN A 295     -16.312 -48.787  -7.193  1.00 23.49           O  
ANISOU 4526  OD1 ASN A 295     4012   2124   2789  -1149   -108    655       O  
ATOM   4527  ND2 ASN A 295     -15.531 -47.031  -8.342  1.00 26.48           N  
ANISOU 4527  ND2 ASN A 295     4484   2463   3115  -1333   -159    772       N  
ATOM   4528  H   ASN A 295     -15.953 -47.027  -4.735  1.00 28.32           H  
ATOM   4529  HA  ASN A 295     -14.890 -49.320  -5.199  1.00 28.60           H  
ATOM   4530  HB2 ASN A 295     -14.127 -46.820  -6.257  1.00 29.61           H  
ATOM   4531  HB3 ASN A 295     -13.528 -48.192  -6.794  1.00 29.61           H  
ATOM   4532 HD21 ASN A 295     -14.924 -46.426  -8.420  1.00 31.78           H  
ATOM   4533 HD22 ASN A 295     -16.176 -47.069  -8.909  1.00 31.78           H  
ATOM   4534  N   LEU A 296     -12.866 -47.415  -3.622  1.00 24.90           N  
ANISOU 4534  N   LEU A 296     4088   2264   3109  -1351   -260    693       N  
ATOM   4535  CA  LEU A 296     -11.687 -47.406  -2.760  1.00 25.37           C  
ANISOU 4535  CA  LEU A 296     4075   2354   3211  -1416   -288    709       C  
ATOM   4536  C   LEU A 296     -11.824 -48.438  -1.637  1.00 24.51           C  
ANISOU 4536  C   LEU A 296     3902   2275   3136  -1310   -269    641       C  
ATOM   4537  O   LEU A 296     -10.913 -49.243  -1.395  1.00 24.55           O  
ANISOU 4537  O   LEU A 296     3779   2373   3174  -1323   -222    647       O  
ATOM   4538  CB  LEU A 296     -11.481 -46.008  -2.175  1.00 26.23           C  
ANISOU 4538  CB  LEU A 296     4299   2345   3323  -1500   -412    738       C  
ATOM   4539  CG  LEU A 296     -10.354 -45.830  -1.154  1.00 26.85           C  
ANISOU 4539  CG  LEU A 296     4327   2430   3442  -1576   -473    754       C  
ATOM   4540  CD1 LEU A 296      -9.032 -46.269  -1.751  1.00 27.48           C  
ANISOU 4540  CD1 LEU A 296     4252   2642   3548  -1678   -408    824       C  
ATOM   4541  CD2 LEU A 296     -10.271 -44.382  -0.675  1.00 27.81           C  
ANISOU 4541  CD2 LEU A 296     4583   2427   3557  -1645   -605    771       C  
ATOM   4542  H   LEU A 296     -13.247 -46.648  -3.705  1.00 29.88           H  
ATOM   4543  HA  LEU A 296     -10.904 -47.633  -3.287  1.00 30.44           H  
ATOM   4544  HB2 LEU A 296     -11.298 -45.399  -2.908  1.00 31.48           H  
ATOM   4545  HB3 LEU A 296     -12.304 -45.741  -1.738  1.00 31.48           H  
ATOM   4546  HG  LEU A 296     -10.535 -46.390  -0.384  1.00 32.21           H  
ATOM   4547 HD11 LEU A 296      -8.845 -45.728  -2.534  1.00 32.98           H  
ATOM   4548 HD12 LEU A 296      -8.333 -46.149  -1.090  1.00 32.98           H  
ATOM   4549 HD13 LEU A 296      -9.095 -47.204  -2.001  1.00 32.98           H  
ATOM   4550 HD21 LEU A 296     -11.113 -44.139  -0.260  1.00 33.38           H  
ATOM   4551 HD22 LEU A 296      -9.550 -44.304  -0.032  1.00 33.38           H  
ATOM   4552 HD23 LEU A 296     -10.099 -43.807  -1.437  1.00 33.38           H  
ATOM   4553  N   SER A 297     -12.971 -48.412  -0.962  1.00 23.83           N  
ANISOU 4553  N   SER A 297     3901   2113   3041  -1202   -303    583       N  
ATOM   4554  CA  SER A 297     -13.265 -49.384   0.092  1.00 23.03           C  
ANISOU 4554  CA  SER A 297     3750   2038   2965  -1096   -284    525       C  
ATOM   4555  C   SER A 297     -13.072 -50.817  -0.415  1.00 22.46           C  
ANISOU 4555  C   SER A 297     3546   2078   2910  -1051   -179    513       C  
ATOM   4556  O   SER A 297     -12.372 -51.639   0.208  1.00 23.76           O  
ANISOU 4556  O   SER A 297     3609   2307   3112  -1038   -155    503       O  
ATOM   4557  CB  SER A 297     -14.701 -49.209   0.595  1.00 22.44           C  
ANISOU 4557  CB  SER A 297     3777   1883   2868   -979   -313    474       C  
ATOM   4558  OG  SER A 297     -14.898 -49.903   1.815  1.00 27.21           O  
ANISOU 4558  OG  SER A 297     4348   2500   3489   -893   -313    428       O  
ATOM   4559  H   SER A 297     -13.598 -47.839  -1.094  1.00 28.60           H  
ATOM   4560  HA  SER A 297     -12.661 -49.241   0.837  1.00 27.64           H  
ATOM   4561  HB2 SER A 297     -14.873 -48.265   0.738  1.00 26.93           H  
ATOM   4562  HB3 SER A 297     -15.313 -49.561  -0.070  1.00 26.93           H  
ATOM   4563  HG  SER A 297     -15.688 -49.800   2.080  1.00 32.65           H  
ATOM   4564  N   ASP A 298     -13.698 -51.113  -1.552  1.00 23.49           N  
ANISOU 4564  N   ASP A 298     3685   2228   3013  -1027   -123    514       N  
ATOM   4565  CA  ASP A 298     -13.563 -52.437  -2.157  1.00 24.48           C  
ANISOU 4565  CA  ASP A 298     3707   2447   3146   -983    -27    498       C  
ATOM   4566  C   ASP A 298     -12.104 -52.796  -2.386  1.00 28.18           C  
ANISOU 4566  C   ASP A 298     4059   3010   3638  -1054     20    532       C  
ATOM   4567  O   ASP A 298     -11.693 -53.916  -2.101  1.00 38.53           O  
ANISOU 4567  O   ASP A 298     5270   4388   4981  -1004     72    509       O  
ATOM   4568  CB  ASP A 298     -14.320 -52.534  -3.480  1.00 24.37           C  
ANISOU 4568  CB  ASP A 298     3736   2437   3087   -969     14    501       C  
ATOM   4569  CG  ASP A 298     -15.826 -52.539  -3.295  1.00 34.03           C  
ANISOU 4569  CG  ASP A 298     5040   3592   4300   -877    -17    467       C  
ATOM   4570  OD1 ASP A 298     -16.291 -52.597  -2.136  1.00 27.55           O  
ANISOU 4570  OD1 ASP A 298     4232   2731   3503   -813    -56    437       O  
ATOM   4571  OD2 ASP A 298     -16.548 -52.494  -4.315  1.00 29.54           O  
ANISOU 4571  OD2 ASP A 298     4516   3013   3693   -869     -3    474       O  
ATOM   4572  H   ASP A 298     -14.202 -50.571  -1.990  1.00 28.19           H  
ATOM   4573  HA  ASP A 298     -13.938 -53.096  -1.552  1.00 29.37           H  
ATOM   4574  HB2 ASP A 298     -14.089 -51.771  -4.033  1.00 29.25           H  
ATOM   4575  HB3 ASP A 298     -14.070 -53.357  -3.929  1.00 29.25           H  
ATOM   4576  N   ALA A 299     -11.320 -51.854  -2.900  1.00 30.77           N  
ANISOU 4576  N   ALA A 299     4395   3345   3951  -1170      2    594       N  
ATOM   4577  CA  ALA A 299      -9.891 -52.104  -3.083  1.00 27.37           C  
ANISOU 4577  CA  ALA A 299     3840   3013   3546  -1244     46    640       C  
ATOM   4578  C   ALA A 299      -9.202 -52.444  -1.760  1.00 29.72           C  
ANISOU 4578  C   ALA A 299     4063   3325   3903  -1235      8    630       C  
ATOM   4579  O   ALA A 299      -8.445 -53.417  -1.681  1.00 29.92           O  
ANISOU 4579  O   ALA A 299     3962   3442   3963  -1209     70    629       O  
ATOM   4580  CB  ALA A 299      -9.225 -50.920  -3.733  1.00 34.49           C  
ANISOU 4580  CB  ALA A 299     4767   3912   4426  -1382     18    720       C  
ATOM   4581  H   ALA A 299     -11.584 -51.074  -3.148  1.00 36.93           H  
ATOM   4582  HA  ALA A 299      -9.783 -52.865  -3.674  1.00 32.84           H  
ATOM   4583  HB1 ALA A 299      -9.342 -50.142  -3.166  1.00 41.39           H  
ATOM   4584  HB2 ALA A 299      -8.280 -51.111  -3.842  1.00 41.39           H  
ATOM   4585  HB3 ALA A 299      -9.634 -50.764  -4.598  1.00 41.39           H  
ATOM   4586  N   ILE A 300      -9.464 -51.648  -0.726  1.00 24.12           N  
ANISOU 4586  N   ILE A 300     3438   2524   3202  -1251    -95    622       N  
ATOM   4587  CA  ILE A 300      -8.877 -51.916   0.585  1.00 27.11           C  
ANISOU 4587  CA  ILE A 300     3765   2910   3627  -1244   -145    611       C  
ATOM   4588  C   ILE A 300      -9.208 -53.327   1.068  1.00 35.88           C  
ANISOU 4588  C   ILE A 300     4805   4066   4762  -1119    -88    556       C  
ATOM   4589  O   ILE A 300      -8.337 -54.022   1.594  1.00 41.60           O  
ANISOU 4589  O   ILE A 300     5417   4857   5532  -1115    -74    565       O  
ATOM   4590  CB  ILE A 300      -9.313 -50.876   1.640  1.00 30.23           C  
ANISOU 4590  CB  ILE A 300     4290   3187   4009  -1259   -265    594       C  
ATOM   4591  CG1 ILE A 300      -8.671 -49.527   1.326  1.00 29.89           C  
ANISOU 4591  CG1 ILE A 300     4301   3097   3957  -1403   -339    659       C  
ATOM   4592  CG2 ILE A 300      -8.889 -51.308   3.055  1.00 24.91           C  
ANISOU 4592  CG2 ILE A 300     3575   2520   3369  -1229   -314    571       C  
ATOM   4593  CD1 ILE A 300      -9.426 -48.344   1.870  1.00 28.27           C  
ANISOU 4593  CD1 ILE A 300     4271   2751   3719  -1406   -446    637       C  
ATOM   4594  H   ILE A 300      -9.972 -50.954  -0.756  1.00 28.94           H  
ATOM   4595  HA  ILE A 300      -7.912 -51.858   0.503  1.00 32.54           H  
ATOM   4596  HB  ILE A 300     -10.278 -50.782   1.613  1.00 36.28           H  
ATOM   4597 HG12 ILE A 300      -7.780 -49.509   1.710  1.00 35.86           H  
ATOM   4598 HG13 ILE A 300      -8.615 -49.425   0.363  1.00 35.86           H  
ATOM   4599 HG21 ILE A 300      -7.924 -51.395   3.082  1.00 29.89           H  
ATOM   4600 HG22 ILE A 300      -9.179 -50.634   3.690  1.00 29.89           H  
ATOM   4601 HG23 ILE A 300      -9.305 -52.159   3.263  1.00 29.89           H  
ATOM   4602 HD11 ILE A 300      -9.481 -48.422   2.835  1.00 33.92           H  
ATOM   4603 HD12 ILE A 300      -8.955 -47.531   1.628  1.00 33.92           H  
ATOM   4604 HD13 ILE A 300     -10.318 -48.337   1.487  1.00 33.92           H  
ATOM   4605  N   LEU A 301     -10.455 -53.755   0.888  1.00 50.33           N  
ANISOU 4605  N   LEU A 301     6697   5859   6567  -1021    -61    506       N  
ATOM   4606  CA  LEU A 301     -10.829 -55.122   1.267  1.00 51.76           C  
ANISOU 4606  CA  LEU A 301     6816   6077   6773   -910    -10    461       C  
ATOM   4607  C   LEU A 301     -10.213 -56.191   0.349  1.00 42.44           C  
ANISOU 4607  C   LEU A 301     5522   4992   5610   -894     89    465       C  
ATOM   4608  O   LEU A 301      -9.778 -57.264   0.800  1.00 38.46           O  
ANISOU 4608  O   LEU A 301     4925   4540   5148   -839    121    450       O  
ATOM   4609  CB  LEU A 301     -12.353 -55.263   1.276  1.00 50.30           C  
ANISOU 4609  CB  LEU A 301     6723   5829   6559   -819    -13    417       C  
ATOM   4610  CG  LEU A 301     -13.071 -54.320   2.245  1.00 62.86           C  
ANISOU 4610  CG  LEU A 301     8427   7328   8128   -804    -99    403       C  
ATOM   4611  CD1 LEU A 301     -14.575 -54.341   2.021  1.00 69.22           C  
ANISOU 4611  CD1 LEU A 301     9312   8084   8905   -720    -92    374       C  
ATOM   4612  CD2 LEU A 301     -12.744 -54.676   3.689  1.00 52.48           C  
ANISOU 4612  CD2 LEU A 301     7082   6018   6840   -771   -139    387       C  
ATOM   4613  H   LEU A 301     -11.094 -53.286   0.556  1.00 60.39           H  
ATOM   4614  HA  LEU A 301     -10.513 -55.291   2.168  1.00 62.11           H  
ATOM   4615  HB2 LEU A 301     -12.687 -55.078   0.384  1.00 60.36           H  
ATOM   4616  HB3 LEU A 301     -12.579 -56.172   1.527  1.00 60.36           H  
ATOM   4617  HG  LEU A 301     -12.761 -53.415   2.087  1.00 75.43           H  
ATOM   4618 HD11 LEU A 301     -14.902 -55.244   2.161  1.00 83.07           H  
ATOM   4619 HD12 LEU A 301     -14.996 -53.735   2.650  1.00 83.07           H  
ATOM   4620 HD13 LEU A 301     -14.762 -54.059   1.112  1.00 83.07           H  
ATOM   4621 HD21 LEU A 301     -11.786 -54.599   3.823  1.00 62.97           H  
ATOM   4622 HD22 LEU A 301     -13.211 -54.063   4.278  1.00 62.97           H  
ATOM   4623 HD23 LEU A 301     -13.030 -55.586   3.862  1.00 62.97           H  
ATOM   4624  N   LEU A 302     -10.179 -55.888  -0.942  1.00 33.06           N  
ANISOU 4624  N   LEU A 302     4349   3828   4385   -936    138    486       N  
ATOM   4625  CA  LEU A 302      -9.734 -56.842  -1.949  1.00 39.09           C  
ANISOU 4625  CA  LEU A 302     5030   4677   5145   -909    239    482       C  
ATOM   4626  C   LEU A 302      -8.250 -57.152  -1.772  1.00 43.28           C  
ANISOU 4626  C   LEU A 302     5422   5300   5720   -948    272    520       C  
ATOM   4627  O   LEU A 302      -7.842 -58.321  -1.807  1.00 54.19           O  
ANISOU 4627  O   LEU A 302     6713   6744   7133   -877    335    497       O  
ATOM   4628  CB  LEU A 302     -10.024 -56.293  -3.350  1.00 44.34           C  
ANISOU 4628  CB  LEU A 302     5755   5345   5746   -955    276    502       C  
ATOM   4629  CG  LEU A 302     -10.016 -57.240  -4.556  1.00 51.92           C  
ANISOU 4629  CG  LEU A 302     6683   6372   6674   -907    378    479       C  
ATOM   4630  CD1 LEU A 302     -10.761 -58.531  -4.278  1.00 45.88           C  
ANISOU 4630  CD1 LEU A 302     5915   5587   5928   -789    396    411       C  
ATOM   4631  CD2 LEU A 302     -10.641 -56.537  -5.747  1.00 59.15           C  
ANISOU 4631  CD2 LEU A 302     7697   7263   7514   -950    385    495       C  
ATOM   4632  H   LEU A 302     -10.413 -55.126  -1.265  1.00 39.67           H  
ATOM   4633  HA  LEU A 302     -10.229 -57.670  -1.841  1.00 46.91           H  
ATOM   4634  HB2 LEU A 302     -10.904 -55.885  -3.327  1.00 53.20           H  
ATOM   4635  HB3 LEU A 302      -9.367 -55.605  -3.536  1.00 53.20           H  
ATOM   4636  HG  LEU A 302      -9.099 -57.461  -4.781  1.00 62.31           H  
ATOM   4637 HD11 LEU A 302     -11.683 -58.323  -4.060  1.00 55.05           H  
ATOM   4638 HD12 LEU A 302     -10.726 -59.092  -5.069  1.00 55.05           H  
ATOM   4639 HD13 LEU A 302     -10.339 -58.985  -3.531  1.00 55.05           H  
ATOM   4640 HD21 LEU A 302     -10.125 -55.741  -5.950  1.00 70.98           H  
ATOM   4641 HD22 LEU A 302     -10.634 -57.139  -6.507  1.00 70.98           H  
ATOM   4642 HD23 LEU A 302     -11.554 -56.293  -5.526  1.00 70.98           H  
ATOM   4643  N   SER A 303      -7.445 -56.115  -1.556  1.00 42.76           N  
ANISOU 4643  N   SER A 303     5341   5242   5664  -1058    223    581       N  
ATOM   4644  CA  SER A 303      -6.019 -56.314  -1.326  1.00 44.31           C  
ANISOU 4644  CA  SER A 303     5395   5531   5909  -1105    243    631       C  
ATOM   4645  C   SER A 303      -5.807 -57.158  -0.074  1.00 41.63           C  
ANISOU 4645  C   SER A 303     4991   5195   5630  -1035    212    603       C  
ATOM   4646  O   SER A 303      -4.854 -57.929   0.009  1.00 46.15           O  
ANISOU 4646  O   SER A 303     5431   5855   6251  -1012    259    619       O  
ATOM   4647  CB  SER A 303      -5.292 -54.975  -1.181  1.00 48.65           C  
ANISOU 4647  CB  SER A 303     5951   6073   6463  -1250    171    708       C  
ATOM   4648  OG  SER A 303      -5.167 -54.610   0.183  1.00 59.62           O  
ANISOU 4648  OG  SER A 303     7359   7405   7889  -1272     62    707       O  
ATOM   4649  H   SER A 303      -7.698 -55.293  -1.537  1.00 51.31           H  
ATOM   4650  HA  SER A 303      -5.636 -56.788  -2.081  1.00 53.17           H  
ATOM   4651  HB2 SER A 303      -4.406 -55.054  -1.569  1.00 58.38           H  
ATOM   4652  HB3 SER A 303      -5.797 -54.290  -1.646  1.00 58.38           H  
ATOM   4653  HG  SER A 303      -4.766 -53.874   0.247  1.00 71.55           H  
ATOM   4654  N   ASP A 304      -6.703 -57.010   0.898  1.00 68.76           N  
ANISOU 4654  N   ASP A 304     8522   8540   9064   -997    135    563       N  
ATOM   4655  CA  ASP A 304      -6.616 -57.780   2.134  1.00 71.12           C  
ANISOU 4655  CA  ASP A 304     8776   8836   9409   -931    100    538       C  
ATOM   4656  C   ASP A 304      -6.923 -59.256   1.903  1.00 71.38           C  
ANISOU 4656  C   ASP A 304     8757   8902   9463   -811    179    492       C  
ATOM   4657  O   ASP A 304      -6.162 -60.121   2.341  1.00 72.83           O  
ANISOU 4657  O   ASP A 304     8830   9142   9699   -772    198    499       O  
ATOM   4658  CB  ASP A 304      -7.560 -57.219   3.199  1.00 70.47           C  
ANISOU 4658  CB  ASP A 304     8817   8652   9304   -915      6    508       C  
ATOM   4659  CG  ASP A 304      -7.398 -57.912   4.541  1.00 82.45           C  
ANISOU 4659  CG  ASP A 304    10293  10172  10860   -859    -37    493       C  
ATOM   4660  OD1 ASP A 304      -6.243 -58.144   4.956  1.00 88.25           O  
ANISOU 4660  OD1 ASP A 304    10921  10968  11644   -895    -52    530       O  
ATOM   4661  OD2 ASP A 304      -8.425 -58.230   5.179  1.00 89.93           O  
ANISOU 4661  OD2 ASP A 304    11312  11066  11791   -781    -56    450       O  
ATOM   4662  H   ASP A 304      -7.372 -56.470   0.865  1.00 82.51           H  
ATOM   4663  HA  ASP A 304      -5.711 -57.716   2.477  1.00 85.34           H  
ATOM   4664  HB2 ASP A 304      -7.373 -56.275   3.323  1.00 84.56           H  
ATOM   4665  HB3 ASP A 304      -8.477 -57.341   2.906  1.00 84.56           H  
ATOM   4666  N   ILE A 305      -8.036 -59.557   1.235  1.00 48.16           N  
ANISOU 4666  N   ILE A 305     5895   5921   6481   -753    217    448       N  
ATOM   4667  CA  ILE A 305      -8.347 -60.966   0.967  1.00 48.82           C  
ANISOU 4667  CA  ILE A 305     5941   6025   6584   -647    281    405       C  
ATOM   4668  C   ILE A 305      -7.349 -61.616   0.009  1.00 56.79           C  
ANISOU 4668  C   ILE A 305     6845   7125   7606   -635    376    414       C  
ATOM   4669  O   ILE A 305      -7.086 -62.813   0.116  1.00 61.05           O  
ANISOU 4669  O   ILE A 305     7316   7694   8184   -551    416    389       O  
ATOM   4670  CB  ILE A 305      -9.788 -61.190   0.453  1.00 38.37           C  
ANISOU 4670  CB  ILE A 305     4724   4637   5217   -592    291    359       C  
ATOM   4671  CG1 ILE A 305     -10.015 -60.476  -0.882  1.00 54.09           C  
ANISOU 4671  CG1 ILE A 305     6775   6631   7148   -645    327    368       C  
ATOM   4672  CG2 ILE A 305     -10.790 -60.764   1.520  1.00 26.90           C  
ANISOU 4672  CG2 ILE A 305     3354   3106   3759   -576    211    349       C  
ATOM   4673  CD1 ILE A 305     -11.433 -60.629  -1.435  1.00 61.23           C  
ANISOU 4673  CD1 ILE A 305     7781   7473   8010   -600    326    331       C  
ATOM   4674  H   ILE A 305      -8.609 -58.991   0.935  1.00 57.79           H  
ATOM   4675  HA  ILE A 305      -8.275 -61.445   1.808  1.00 58.59           H  
ATOM   4676  HB  ILE A 305      -9.904 -62.141   0.303  1.00 46.04           H  
ATOM   4677 HG12 ILE A 305      -9.845 -59.529  -0.762  1.00 64.91           H  
ATOM   4678 HG13 ILE A 305      -9.400 -60.840  -1.538  1.00 64.91           H  
ATOM   4679 HG21 ILE A 305     -10.659 -59.823   1.717  1.00 32.27           H  
ATOM   4680 HG22 ILE A 305     -11.689 -60.910   1.185  1.00 32.27           H  
ATOM   4681 HG23 ILE A 305     -10.645 -61.294   2.319  1.00 32.27           H  
ATOM   4682 HD11 ILE A 305     -12.062 -60.259  -0.797  1.00 73.47           H  
ATOM   4683 HD12 ILE A 305     -11.496 -60.152  -2.277  1.00 73.47           H  
ATOM   4684 HD13 ILE A 305     -11.617 -61.571  -1.574  1.00 73.47           H  
ATOM   4685  N   LEU A 306      -6.796 -60.841  -0.922  1.00 61.96           N  
ANISOU 4685  N   LEU A 306     7489   7827   8227   -713    412    453       N  
ATOM   4686  CA  LEU A 306      -5.754 -61.367  -1.806  1.00 66.86           C  
ANISOU 4686  CA  LEU A 306     8001   8551   8853   -701    511    470       C  
ATOM   4687  C   LEU A 306      -4.408 -61.487  -1.094  1.00 63.30           C  
ANISOU 4687  C   LEU A 306     7404   8175   8472   -725    503    521       C  
ATOM   4688  O   LEU A 306      -3.607 -62.364  -1.418  1.00 62.66           O  
ANISOU 4688  O   LEU A 306     7211   8175   8421   -665    580    521       O  
ATOM   4689  CB  LEU A 306      -5.617 -60.500  -3.062  1.00 62.84           C  
ANISOU 4689  CB  LEU A 306     7523   8076   8276   -781    558    504       C  
ATOM   4690  CG  LEU A 306      -6.424 -60.925  -4.299  1.00 56.87           C  
ANISOU 4690  CG  LEU A 306     6850   7309   7450   -728    626    455       C  
ATOM   4691  CD1 LEU A 306      -7.753 -61.594  -3.956  1.00 46.54           C  
ANISOU 4691  CD1 LEU A 306     5637   5906   6141   -644    586    386       C  
ATOM   4692  CD2 LEU A 306      -6.681 -59.717  -5.186  1.00 65.83           C  
ANISOU 4692  CD2 LEU A 306     8064   8435   8513   -827    621    496       C  
ATOM   4693  H   LEU A 306      -7.002 -60.018  -1.062  1.00 74.35           H  
ATOM   4694  HA  LEU A 306      -6.014 -62.257  -2.092  1.00 80.24           H  
ATOM   4695  HB2 LEU A 306      -5.894 -59.599  -2.837  1.00 75.41           H  
ATOM   4696  HB3 LEU A 306      -4.683 -60.491  -3.321  1.00 75.41           H  
ATOM   4697  HG  LEU A 306      -5.898 -61.559  -4.810  1.00 68.25           H  
ATOM   4698 HD11 LEU A 306      -8.297 -60.973  -3.447  1.00 55.85           H  
ATOM   4699 HD12 LEU A 306      -8.206 -61.834  -4.779  1.00 55.85           H  
ATOM   4700 HD13 LEU A 306      -7.578 -62.390  -3.430  1.00 55.85           H  
ATOM   4701 HD21 LEU A 306      -5.830 -59.345  -5.466  1.00 78.99           H  
ATOM   4702 HD22 LEU A 306      -7.190 -59.999  -5.962  1.00 78.99           H  
ATOM   4703 HD23 LEU A 306      -7.182 -59.057  -4.683  1.00 78.99           H  
ATOM   4704  N   ARG A 307      -4.161 -60.610  -0.126  1.00120.13           N  
ANISOU 4704  N   ARG A 307    14605  15345  15693   -808    406    563       N  
ATOM   4705  CA  ARG A 307      -2.931 -60.660   0.658  1.00129.12           C  
ANISOU 4705  CA  ARG A 307    15611  16549  16901   -841    375    617       C  
ATOM   4706  C   ARG A 307      -3.159 -60.102   2.060  1.00129.13           C  
ANISOU 4706  C   ARG A 307    15664  16476  16923   -884    246    624       C  
ATOM   4707  O   ARG A 307      -2.649 -60.640   3.043  1.00133.24           O  
ANISOU 4707  O   ARG A 307    16111  17015  17500   -854    206    633       O  
ATOM   4708  CB  ARG A 307      -1.813 -59.875  -0.033  1.00129.45           C  
ANISOU 4708  CB  ARG A 307    15561  16682  16942   -951    408    699       C  
ATOM   4709  CG  ARG A 307      -1.319 -60.491  -1.336  1.00134.98           C  
ANISOU 4709  CG  ARG A 307    16181  17484  17622   -902    547    702       C  
ATOM   4710  CD  ARG A 307      -0.170 -59.687  -1.922  1.00140.60           C  
ANISOU 4710  CD  ARG A 307    16787  18299  18336  -1017    579    799       C  
ATOM   4711  NE  ARG A 307       0.268 -60.206  -3.216  1.00141.74           N  
ANISOU 4711  NE  ARG A 307    16862  18548  18444   -967    723    802       N  
ATOM   4712  CZ  ARG A 307       1.172 -59.616  -3.993  1.00143.90           C  
ANISOU 4712  CZ  ARG A 307    17045  18930  18702  -1053    784    886       C  
ATOM   4713  NH1 ARG A 307       1.744 -58.479  -3.617  1.00144.97           N  
ANISOU 4713  NH1 ARG A 307    17146  19075  18861  -1203    703    978       N  
ATOM   4714  NH2 ARG A 307       1.505 -60.165  -5.154  1.00144.52           N  
ANISOU 4714  NH2 ARG A 307    17070  19106  18735   -989    924    880       N  
ATOM   4715  H   ARG A 307      -4.693 -59.972   0.097  1.00144.15           H  
ATOM   4716  HA  ARG A 307      -2.645 -61.583   0.743  1.00154.95           H  
ATOM   4717  HB2 ARG A 307      -2.139 -58.984  -0.235  1.00155.34           H  
ATOM   4718  HB3 ARG A 307      -1.056 -59.817   0.570  1.00155.34           H  
ATOM   4719  HG2 ARG A 307      -1.005 -61.393  -1.167  1.00161.98           H  
ATOM   4720  HG3 ARG A 307      -2.044 -60.502  -1.981  1.00161.98           H  
ATOM   4721  HD2 ARG A 307      -0.456 -58.769  -2.047  1.00168.72           H  
ATOM   4722  HD3 ARG A 307       0.584 -59.722  -1.313  1.00168.72           H  
ATOM   4723  HE  ARG A 307      -0.082 -60.940  -3.493  1.00170.09           H  
ATOM   4724 HH11 ARG A 307       1.531 -58.120  -2.865  1.00173.97           H  
ATOM   4725 HH12 ARG A 307       2.327 -58.103  -4.124  1.00173.97           H  
ATOM   4726 HH21 ARG A 307       1.137 -60.901  -5.403  1.00173.43           H  
ATOM   4727 HH22 ARG A 307       2.089 -59.784  -5.658  1.00173.43           H  
ATOM   4728  N   LYS A 314      -7.081 -70.899  -4.458  1.00 68.92           N  
ANISOU 4728  N   LYS A 314     8302   8711   9173    101    848     33       N  
ATOM   4729  CA  LYS A 314      -8.238 -71.433  -3.752  1.00 74.16           C  
ANISOU 4729  CA  LYS A 314     9042   9266   9870    116    757     12       C  
ATOM   4730  C   LYS A 314      -9.409 -70.453  -3.867  1.00 70.19           C  
ANISOU 4730  C   LYS A 314     8638   8717   9313     26    701     27       C  
ATOM   4731  O   LYS A 314      -9.643 -69.871  -4.929  1.00 64.18           O  
ANISOU 4731  O   LYS A 314     7938   7974   8473    -13    736     17       O  
ATOM   4732  CB  LYS A 314      -7.879 -71.697  -2.281  1.00 77.77           C  
ANISOU 4732  CB  LYS A 314     9415   9715  10421    129    698     52       C  
ATOM   4733  CG  LYS A 314      -7.427 -70.452  -1.511  1.00 72.26           C  
ANISOU 4733  CG  LYS A 314     8652   9068   9734     34    665    123       C  
ATOM   4734  CD  LYS A 314      -7.089 -70.762  -0.061  1.00 82.69           C  
ANISOU 4734  CD  LYS A 314     9900  10380  11137     48    600    159       C  
ATOM   4735  CE  LYS A 314      -5.875 -71.673   0.050  1.00 82.36           C  
ANISOU 4735  CE  LYS A 314     9743  10392  11160    131    645    161       C  
ATOM   4736  NZ  LYS A 314      -5.520 -71.980   1.462  1.00 69.95           N  
ANISOU 4736  NZ  LYS A 314     8099   8812   9666    143    575    202       N  
ATOM   4737  HA  LYS A 314      -8.502 -72.274  -4.157  1.00 88.99           H  
ATOM   4738  HB2 LYS A 314      -8.660 -72.056  -1.830  1.00 93.33           H  
ATOM   4739  HB3 LYS A 314      -7.156 -72.343  -2.248  1.00 93.33           H  
ATOM   4740  HG2 LYS A 314      -6.634 -70.088  -1.934  1.00 86.71           H  
ATOM   4741  HG3 LYS A 314      -8.141 -69.796  -1.521  1.00 86.71           H  
ATOM   4742  HD2 LYS A 314      -6.891 -69.934   0.405  1.00 99.22           H  
ATOM   4743  HD3 LYS A 314      -7.843 -71.208   0.355  1.00 99.22           H  
ATOM   4744  HE2 LYS A 314      -6.066 -72.511  -0.401  1.00 98.84           H  
ATOM   4745  HE3 LYS A 314      -5.114 -71.238  -0.364  1.00 98.84           H  
ATOM   4746  HZ1 LYS A 314      -6.201 -72.388   1.865  1.00 83.94           H  
ATOM   4747  HZ2 LYS A 314      -4.808 -72.514   1.487  1.00 83.94           H  
ATOM   4748  HZ3 LYS A 314      -5.333 -71.228   1.899  1.00 83.94           H  
ATOM   4749  N   ALA A 315     -10.142 -70.283  -2.771  1.00 40.40           N  
ANISOU 4749  N   ALA A 315     4881   4888   5580     -1    615     54       N  
ATOM   4750  CA  ALA A 315     -11.192 -69.284  -2.669  1.00 31.15           C  
ANISOU 4750  CA  ALA A 315     3786   3678   4369    -76    559     77       C  
ATOM   4751  C   ALA A 315     -10.768 -68.290  -1.587  1.00 29.95           C  
ANISOU 4751  C   ALA A 315     3579   3555   4246   -137    519    134       C  
ATOM   4752  O   ALA A 315     -10.935 -68.569  -0.400  1.00 27.83           O  
ANISOU 4752  O   ALA A 315     3285   3259   4029   -120    464    152       O  
ATOM   4753  CB  ALA A 315     -12.499 -69.948  -2.290  1.00 33.03           C  
ANISOU 4753  CB  ALA A 315     4095   3828   4626    -48    495     59       C  
ATOM   4754  H   ALA A 315     -10.044 -70.750  -2.055  1.00 48.48           H  
ATOM   4755  HA  ALA A 315     -11.300 -68.817  -3.512  1.00 37.37           H  
ATOM   4756  HB1 ALA A 315     -12.390 -70.393  -1.435  1.00 39.63           H  
ATOM   4757  HB2 ALA A 315     -13.190 -69.271  -2.225  1.00 39.63           H  
ATOM   4758  HB3 ALA A 315     -12.733 -70.596  -2.973  1.00 39.63           H  
ATOM   4759  N   PRO A 316     -10.208 -67.129  -1.983  1.00 27.37           N  
ANISOU 4759  N   PRO A 316     3238   3280   3879   -212    541    167       N  
ATOM   4760  CA  PRO A 316      -9.657 -66.223  -0.964  1.00 23.38           C  
ANISOU 4760  CA  PRO A 316     2682   2799   3403   -274    495    219       C  
ATOM   4761  C   PRO A 316     -10.703 -65.719   0.041  1.00 28.77           C  
ANISOU 4761  C   PRO A 316     3432   3412   4088   -294    409    231       C  
ATOM   4762  O   PRO A 316     -10.417 -65.647   1.245  1.00 34.96           O  
ANISOU 4762  O   PRO A 316     4176   4195   4913   -297    360    255       O  
ATOM   4763  CB  PRO A 316      -9.071 -65.070  -1.793  1.00 25.50           C  
ANISOU 4763  CB  PRO A 316     2947   3121   3620   -359    530    252       C  
ATOM   4764  CG  PRO A 316      -9.795 -65.119  -3.101  1.00 35.38           C  
ANISOU 4764  CG  PRO A 316     4286   4354   4802   -352    571    218       C  
ATOM   4765  CD  PRO A 316     -10.080 -66.572  -3.344  1.00 34.23           C  
ANISOU 4765  CD  PRO A 316     4145   4186   4675   -251    600    161       C  
ATOM   4766  HA  PRO A 316      -8.940 -66.662  -0.481  1.00 28.06           H  
ATOM   4767  HB2 PRO A 316      -9.236 -64.227  -1.343  1.00 30.60           H  
ATOM   4768  HB3 PRO A 316      -8.120 -65.211  -1.922  1.00 30.60           H  
ATOM   4769  HG2 PRO A 316     -10.621 -64.615  -3.037  1.00 42.46           H  
ATOM   4770  HG3 PRO A 316      -9.228 -64.760  -3.802  1.00 42.46           H  
ATOM   4771  HD2 PRO A 316     -10.912 -66.677  -3.831  1.00 41.07           H  
ATOM   4772  HD3 PRO A 316      -9.339 -66.989  -3.811  1.00 41.07           H  
ATOM   4773  N   LEU A 317     -11.901 -65.401  -0.440  1.00 19.67           N  
ANISOU 4773  N   LEU A 317     2379   2207   2889   -302    392    215       N  
ATOM   4774  CA  LEU A 317     -12.966 -64.922   0.435  1.00 23.31           C  
ANISOU 4774  CA  LEU A 317     2901   2610   3347   -308    321    226       C  
ATOM   4775  C   LEU A 317     -13.319 -65.970   1.487  1.00 27.56           C  
ANISOU 4775  C   LEU A 317     3410   3123   3938   -241    292    221       C  
ATOM   4776  O   LEU A 317     -13.234 -65.708   2.696  1.00 29.85           O  
ANISOU 4776  O   LEU A 317     3683   3409   4249   -244    245    245       O  
ATOM   4777  CB  LEU A 317     -14.212 -64.555  -0.378  1.00 18.63           C  
ANISOU 4777  CB  LEU A 317     2405   1971   2702   -316    313    214       C  
ATOM   4778  CG  LEU A 317     -15.421 -64.094   0.445  1.00 23.59           C  
ANISOU 4778  CG  LEU A 317     3091   2544   3326   -307    250    227       C  
ATOM   4779  CD1 LEU A 317     -15.154 -62.728   1.059  1.00 17.97           C  
ANISOU 4779  CD1 LEU A 317     2404   1829   2595   -360    211    255       C  
ATOM   4780  CD2 LEU A 317     -16.700 -64.079  -0.385  1.00 24.65           C  
ANISOU 4780  CD2 LEU A 317     3302   2639   3426   -297    242    217       C  
ATOM   4781  H   LEU A 317     -12.123 -65.453  -1.269  1.00 23.61           H  
ATOM   4782  HA  LEU A 317     -12.662 -64.125   0.896  1.00 27.98           H  
ATOM   4783  HB2 LEU A 317     -13.981 -63.834  -0.985  1.00 22.36           H  
ATOM   4784  HB3 LEU A 317     -14.486 -65.333  -0.888  1.00 22.36           H  
ATOM   4785  HG  LEU A 317     -15.554 -64.720   1.174  1.00 28.30           H  
ATOM   4786 HD11 LEU A 317     -14.989 -62.089   0.348  1.00 21.57           H  
ATOM   4787 HD12 LEU A 317     -15.930 -62.456   1.574  1.00 21.57           H  
ATOM   4788 HD13 LEU A 317     -14.378 -62.789   1.638  1.00 21.57           H  
ATOM   4789 HD21 LEU A 317     -16.874 -64.975  -0.712  1.00 29.58           H  
ATOM   4790 HD22 LEU A 317     -17.435 -63.782   0.174  1.00 29.58           H  
ATOM   4791 HD23 LEU A 317     -16.585 -63.470  -1.131  1.00 29.58           H  
ATOM   4792  N   SER A 318     -13.718 -67.152   1.021  1.00 22.02           N  
ANISOU 4792  N   SER A 318     2712   2402   3254   -184    313    191       N  
ATOM   4793  CA  SER A 318     -14.118 -68.238   1.909  1.00 22.42           C  
ANISOU 4793  CA  SER A 318     2741   2421   3356   -126    283    193       C  
ATOM   4794  C   SER A 318     -13.036 -68.509   2.944  1.00 20.80           C  
ANISOU 4794  C   SER A 318     2449   2251   3201   -112    273    215       C  
ATOM   4795  O   SER A 318     -13.321 -68.672   4.134  1.00 31.83           O  
ANISOU 4795  O   SER A 318     3837   3634   4623    -97    226    239       O  
ATOM   4796  CB  SER A 318     -14.397 -69.511   1.108  1.00 23.43           C  
ANISOU 4796  CB  SER A 318     2883   2521   3500    -73    308    155       C  
ATOM   4797  OG  SER A 318     -15.641 -69.430   0.435  1.00 25.58           O  
ANISOU 4797  OG  SER A 318     3237   2748   3735    -84    291    144       O  
ATOM   4798  H   SER A 318     -13.766 -67.350   0.185  1.00 26.43           H  
ATOM   4799  HA  SER A 318     -14.931 -67.988   2.376  1.00 26.90           H  
ATOM   4800  HB2 SER A 318     -13.692 -69.631   0.452  1.00 28.12           H  
ATOM   4801  HB3 SER A 318     -14.416 -70.267   1.715  1.00 28.12           H  
ATOM   4802  HG  SER A 318     -15.639 -68.778  -0.095  1.00 30.70           H  
ATOM   4803  N   ALA A 319     -11.792 -68.552   2.480  1.00 20.48           N  
ANISOU 4803  N   ALA A 319     2344   2265   3174   -116    319    210       N  
ATOM   4804  CA  ALA A 319     -10.646 -68.737   3.362  1.00 21.84           C  
ANISOU 4804  CA  ALA A 319     2422   2480   3397   -108    308    237       C  
ATOM   4805  C   ALA A 319     -10.565 -67.638   4.416  1.00 25.51           C  
ANISOU 4805  C   ALA A 319     2891   2952   3848   -169    248    276       C  
ATOM   4806  O   ALA A 319     -10.370 -67.929   5.598  1.00 35.88           O  
ANISOU 4806  O   ALA A 319     4172   4266   5196   -152    201    299       O  
ATOM   4807  CB  ALA A 319      -9.356 -68.797   2.554  1.00 20.56           C  
ANISOU 4807  CB  ALA A 319     2181   2387   3245   -109    374    234       C  
ATOM   4808  H   ALA A 319     -11.583 -68.474   1.650  1.00 24.58           H  
ATOM   4809  HA  ALA A 319     -10.744 -69.584   3.826  1.00 26.21           H  
ATOM   4810  HB1 ALA A 319      -9.252 -67.966   2.065  1.00 24.68           H  
ATOM   4811  HB2 ALA A 319      -8.610 -68.921   3.161  1.00 24.68           H  
ATOM   4812  HB3 ALA A 319      -9.407 -69.542   1.934  1.00 24.68           H  
ATOM   4813  N   SER A 320     -10.706 -66.379   4.001  1.00 26.78           N  
ANISOU 4813  N   SER A 320     3103   3115   3957   -238    244    283       N  
ATOM   4814  CA  SER A 320     -10.674 -65.279   4.965  1.00 21.29           C  
ANISOU 4814  CA  SER A 320     2434   2412   3242   -294    180    311       C  
ATOM   4815  C   SER A 320     -11.791 -65.414   5.997  1.00 25.71           C  
ANISOU 4815  C   SER A 320     3055   2922   3792   -256    129    310       C  
ATOM   4816  O   SER A 320     -11.567 -65.184   7.189  1.00 28.07           O  
ANISOU 4816  O   SER A 320     3348   3223   4096   -262     76    331       O  
ATOM   4817  CB  SER A 320     -10.743 -63.919   4.265  1.00 21.69           C  
ANISOU 4817  CB  SER A 320     2545   2458   3239   -371    179    317       C  
ATOM   4818  OG  SER A 320     -12.006 -63.701   3.664  1.00 33.65           O  
ANISOU 4818  OG  SER A 320     4153   3924   4711   -358    186    295       O  
ATOM   4819  H   SER A 320     -10.819 -66.139   3.183  1.00 32.14           H  
ATOM   4820  HA  SER A 320      -9.831 -65.317   5.443  1.00 25.55           H  
ATOM   4821  HB2 SER A 320     -10.583 -63.221   4.920  1.00 26.03           H  
ATOM   4822  HB3 SER A 320     -10.060 -63.886   3.577  1.00 26.03           H  
ATOM   4823  HG  SER A 320     -12.159 -64.296   3.092  1.00 40.39           H  
ATOM   4824  N   MET A 321     -12.984 -65.799   5.552  1.00 18.91           N  
ANISOU 4824  N   MET A 321     2250   2022   2914   -218    145    291       N  
ATOM   4825  CA  MET A 321     -14.088 -66.024   6.486  1.00 17.64           C  
ANISOU 4825  CA  MET A 321     2131   1825   2746   -178    108    299       C  
ATOM   4826  C   MET A 321     -13.751 -67.157   7.464  1.00 24.54           C  
ANISOU 4826  C   MET A 321     2942   2710   3671   -130     90    317       C  
ATOM   4827  O   MET A 321     -13.972 -67.032   8.673  1.00 27.89           O  
ANISOU 4827  O   MET A 321     3377   3133   4086   -119     47    340       O  
ATOM   4828  CB  MET A 321     -15.386 -66.338   5.733  1.00 17.21           C  
ANISOU 4828  CB  MET A 321     2130   1734   2675   -151    126    285       C  
ATOM   4829  CG  MET A 321     -15.873 -65.210   4.830  1.00 22.18           C  
ANISOU 4829  CG  MET A 321     2829   2346   3251   -193    134    275       C  
ATOM   4830  SD  MET A 321     -16.076 -63.645   5.701  1.00 23.40           S  
ANISOU 4830  SD  MET A 321     3049   2486   3357   -226     84    290       S  
ATOM   4831  CE  MET A 321     -17.701 -63.860   6.428  1.00 17.33           C  
ANISOU 4831  CE  MET A 321     2325   1688   2574   -160     64    303       C  
ATOM   4832  H   MET A 321     -13.180 -65.936   4.726  1.00 22.70           H  
ATOM   4833  HA  MET A 321     -14.233 -65.210   6.993  1.00 21.17           H  
ATOM   4834  HB2 MET A 321     -15.242 -67.119   5.177  1.00 20.65           H  
ATOM   4835  HB3 MET A 321     -16.085 -66.520   6.380  1.00 20.65           H  
ATOM   4836  HG2 MET A 321     -15.227 -65.074   4.119  1.00 26.61           H  
ATOM   4837  HG3 MET A 321     -16.732 -65.456   4.454  1.00 26.61           H  
ATOM   4838  HE1 MET A 321     -17.684 -64.632   7.015  1.00 20.80           H  
ATOM   4839  HE2 MET A 321     -17.928 -63.064   6.934  1.00 20.80           H  
ATOM   4840  HE3 MET A 321     -18.349 -63.997   5.719  1.00 20.80           H  
ATOM   4841  N   ILE A 322     -13.210 -68.257   6.946  1.00 18.73           N  
ANISOU 4841  N   ILE A 322     2147   1984   2985    -98    123    306       N  
ATOM   4842  CA  ILE A 322     -12.827 -69.381   7.798  1.00 18.80           C  
ANISOU 4842  CA  ILE A 322     2096   1997   3049    -50    104    325       C  
ATOM   4843  C   ILE A 322     -11.758 -68.950   8.803  1.00 20.85           C  
ANISOU 4843  C   ILE A 322     2304   2298   3320    -75     66    354       C  
ATOM   4844  O   ILE A 322     -11.791 -69.349   9.969  1.00 19.66           O  
ANISOU 4844  O   ILE A 322     2140   2147   3184    -52     22    383       O  
ATOM   4845  CB  ILE A 322     -12.319 -70.579   6.964  1.00 18.61           C  
ANISOU 4845  CB  ILE A 322     2023   1970   3077     -4    146    302       C  
ATOM   4846  CG1 ILE A 322     -13.463 -71.162   6.136  1.00 19.96           C  
ANISOU 4846  CG1 ILE A 322     2255   2089   3238     20    163    276       C  
ATOM   4847  CG2 ILE A 322     -11.749 -71.679   7.862  1.00 18.96           C  
ANISOU 4847  CG2 ILE A 322     2002   2017   3187     46    120    326       C  
ATOM   4848  CD1 ILE A 322     -13.007 -72.000   4.949  1.00 21.70           C  
ANISOU 4848  CD1 ILE A 322     2462   2302   3482     56    213    234       C  
ATOM   4849  H   ILE A 322     -13.056 -68.378   6.109  1.00 22.47           H  
ATOM   4850  HA  ILE A 322     -13.604 -69.674   8.298  1.00 22.56           H  
ATOM   4851  HB  ILE A 322     -11.622 -70.271   6.363  1.00 22.33           H  
ATOM   4852 HG12 ILE A 322     -14.004 -71.730   6.708  1.00 23.95           H  
ATOM   4853 HG13 ILE A 322     -14.003 -70.433   5.794  1.00 23.95           H  
ATOM   4854 HG21 ILE A 322     -12.445 -71.988   8.462  1.00 22.76           H  
ATOM   4855 HG22 ILE A 322     -11.442 -72.412   7.306  1.00 22.76           H  
ATOM   4856 HG23 ILE A 322     -11.008 -71.317   8.372  1.00 22.76           H  
ATOM   4857 HD11 ILE A 322     -12.475 -72.743   5.273  1.00 26.04           H  
ATOM   4858 HD12 ILE A 322     -13.788 -72.331   4.478  1.00 26.04           H  
ATOM   4859 HD13 ILE A 322     -12.475 -71.445   4.358  1.00 26.04           H  
ATOM   4860  N   LYS A 323     -10.819 -68.124   8.353  1.00 25.10           N  
ANISOU 4860  N   LYS A 323     2815   2873   3850   -128     77    352       N  
ATOM   4861  CA  LYS A 323      -9.770 -67.623   9.235  1.00 27.49           C  
ANISOU 4861  CA  LYS A 323     3068   3214   4163   -166     30    383       C  
ATOM   4862  C   LYS A 323     -10.378 -66.757  10.329  1.00 28.10           C  
ANISOU 4862  C   LYS A 323     3223   3268   4186   -192    -34    395       C  
ATOM   4863  O   LYS A 323     -10.016 -66.879  11.499  1.00 36.70           O  
ANISOU 4863  O   LYS A 323     4294   4368   5281   -189    -89    421       O  
ATOM   4864  CB  LYS A 323      -8.726 -66.825   8.452  1.00 25.42           C  
ANISOU 4864  CB  LYS A 323     2761   2997   3901   -231     53    387       C  
ATOM   4865  CG  LYS A 323      -7.679 -66.160   9.333  1.00 28.44           C  
ANISOU 4865  CG  LYS A 323     3097   3416   4294   -291    -10    426       C  
ATOM   4866  CD  LYS A 323      -6.588 -65.498   8.514  1.00 44.53           C  
ANISOU 4866  CD  LYS A 323     5069   5506   6342   -360     16    445       C  
ATOM   4867  CE  LYS A 323      -5.898 -64.409   9.319  1.00 56.51           C  
ANISOU 4867  CE  LYS A 323     6587   7037   7848   -450    -68    482       C  
ATOM   4868  NZ  LYS A 323      -6.782 -63.224   9.527  1.00 60.27           N  
ANISOU 4868  NZ  LYS A 323     7200   7451   8251   -497   -112    464       N  
ATOM   4869  H   LYS A 323     -10.766 -67.839   7.543  1.00 30.12           H  
ATOM   4870  HA  LYS A 323      -9.323 -68.374   9.656  1.00 32.99           H  
ATOM   4871  HB2 LYS A 323      -8.266 -67.425   7.844  1.00 30.51           H  
ATOM   4872  HB3 LYS A 323      -9.177 -66.129   7.949  1.00 30.51           H  
ATOM   4873  HG2 LYS A 323      -8.105 -65.478   9.876  1.00 34.13           H  
ATOM   4874  HG3 LYS A 323      -7.267 -66.830   9.900  1.00 34.13           H  
ATOM   4875  HD2 LYS A 323      -5.925 -66.160   8.264  1.00 53.43           H  
ATOM   4876  HD3 LYS A 323      -6.978 -65.094   7.723  1.00 53.43           H  
ATOM   4877  HE2 LYS A 323      -5.654 -64.761  10.189  1.00 67.82           H  
ATOM   4878  HE3 LYS A 323      -5.106 -64.115   8.843  1.00 67.82           H  
ATOM   4879  HZ1 LYS A 323      -7.517 -63.467   9.967  1.00 72.33           H  
ATOM   4880  HZ2 LYS A 323      -6.353 -62.604  10.000  1.00 72.33           H  
ATOM   4881  HZ3 LYS A 323      -7.017 -62.878   8.742  1.00 72.33           H  
ATOM   4882  N   ARG A 324     -11.298 -65.881   9.940  1.00 18.83           N  
ANISOU 4882  N   ARG A 324     2140   2060   2954   -213    -28    375       N  
ATOM   4883  CA  ARG A 324     -12.032 -65.068  10.900  1.00 19.30           C  
ANISOU 4883  CA  ARG A 324     2287   2091   2954   -218    -78    378       C  
ATOM   4884  C   ARG A 324     -12.677 -65.965  11.957  1.00 23.85           C  
ANISOU 4884  C   ARG A 324     2864   2663   3535   -153    -95    396       C  
ATOM   4885  O   ARG A 324     -12.499 -65.756  13.162  1.00 32.77           O  
ANISOU 4885  O   ARG A 324     4010   3801   4640   -153   -148    414       O  
ATOM   4886  CB  ARG A 324     -13.098 -64.235  10.180  1.00 23.51           C  
ANISOU 4886  CB  ARG A 324     2911   2585   3436   -226    -57    354       C  
ATOM   4887  CG  ARG A 324     -13.897 -63.322  11.088  1.00 19.37           C  
ANISOU 4887  CG  ARG A 324     2483   2030   2846   -216   -100    351       C  
ATOM   4888  CD  ARG A 324     -15.030 -62.626  10.347  1.00 26.24           C  
ANISOU 4888  CD  ARG A 324     3433   2863   3676   -207    -76    332       C  
ATOM   4889  NE  ARG A 324     -14.552 -61.669   9.351  1.00 31.19           N  
ANISOU 4889  NE  ARG A 324     4085   3476   4291   -275    -74    321       N  
ATOM   4890  CZ  ARG A 324     -15.345 -60.894   8.616  1.00 31.99           C  
ANISOU 4890  CZ  ARG A 324     4258   3540   4357   -281    -63    308       C  
ATOM   4891  NH1 ARG A 324     -16.662 -60.953   8.760  1.00 35.16           N  
ANISOU 4891  NH1 ARG A 324     4707   3919   4734   -219    -52    304       N  
ATOM   4892  NH2 ARG A 324     -14.822 -60.053   7.734  1.00 31.73           N  
ANISOU 4892  NH2 ARG A 324     4246   3496   4314   -350    -64    306       N  
ATOM   4893  H   ARG A 324     -11.518 -65.739   9.120  1.00 22.60           H  
ATOM   4894  HA  ARG A 324     -11.419 -64.462  11.345  1.00 23.15           H  
ATOM   4895  HB2 ARG A 324     -12.662 -63.680   9.514  1.00 28.21           H  
ATOM   4896  HB3 ARG A 324     -13.722 -64.837   9.745  1.00 28.21           H  
ATOM   4897  HG2 ARG A 324     -14.283 -63.847  11.807  1.00 23.24           H  
ATOM   4898  HG3 ARG A 324     -13.309 -62.641  11.451  1.00 23.24           H  
ATOM   4899  HD2 ARG A 324     -15.565 -63.293   9.889  1.00 31.49           H  
ATOM   4900  HD3 ARG A 324     -15.577 -62.144  10.987  1.00 31.49           H  
ATOM   4901  HE  ARG A 324     -13.703 -61.603   9.233  1.00 37.43           H  
ATOM   4902 HH11 ARG A 324     -17.008 -61.496   9.330  1.00 42.19           H  
ATOM   4903 HH12 ARG A 324     -17.170 -60.449   8.283  1.00 42.19           H  
ATOM   4904 HH21 ARG A 324     -13.969 -60.009   7.636  1.00 38.08           H  
ATOM   4905 HH22 ARG A 324     -15.336 -59.552   7.260  1.00 38.08           H  
ATOM   4906  N   TYR A 325     -13.407 -66.974  11.491  1.00 25.75           N  
ANISOU 4906  N   TYR A 325     3089   2891   3805   -104    -54    394       N  
ATOM   4907  CA  TYR A 325     -14.075 -67.942  12.363  1.00 23.22           C  
ANISOU 4907  CA  TYR A 325     2761   2565   3496    -48    -66    422       C  
ATOM   4908  C   TYR A 325     -13.095 -68.627  13.340  1.00 29.38           C  
ANISOU 4908  C   TYR A 325     3476   3373   4314    -38   -105    453       C  
ATOM   4909  O   TYR A 325     -13.308 -68.654  14.565  1.00 26.94           O  
ANISOU 4909  O   TYR A 325     3187   3073   3975    -22   -146    482       O  
ATOM   4910  CB  TYR A 325     -14.780 -68.975  11.473  1.00 19.34           C  
ANISOU 4910  CB  TYR A 325     2255   2050   3046    -14    -23    416       C  
ATOM   4911  CG  TYR A 325     -15.548 -70.055  12.192  1.00 22.69           C  
ANISOU 4911  CG  TYR A 325     2668   2462   3490     33    -36    454       C  
ATOM   4912  CD1 TYR A 325     -14.923 -71.232  12.593  1.00 22.86           C  
ANISOU 4912  CD1 TYR A 325     2628   2485   3573     60    -51    477       C  
ATOM   4913  CD2 TYR A 325     -16.909 -69.918  12.435  1.00 17.17           C  
ANISOU 4913  CD2 TYR A 325     2018   1752   2755     51    -32    472       C  
ATOM   4914  CE1 TYR A 325     -15.627 -72.229  13.240  1.00 21.13           C  
ANISOU 4914  CE1 TYR A 325     2402   2250   3375     95    -68    521       C  
ATOM   4915  CE2 TYR A 325     -17.622 -70.908  13.082  1.00 17.20           C  
ANISOU 4915  CE2 TYR A 325     2005   1752   2780     84    -42    519       C  
ATOM   4916  CZ  TYR A 325     -16.976 -72.062  13.481  1.00 29.90           C  
ANISOU 4916  CZ  TYR A 325     3558   3355   4447    102    -62    544       C  
ATOM   4917  OH  TYR A 325     -17.679 -73.052  14.122  1.00 33.25           O  
ANISOU 4917  OH  TYR A 325     3969   3771   4894    127    -78    600       O  
ATOM   4918  H   TYR A 325     -13.534 -67.124  10.654  1.00 30.90           H  
ATOM   4919  HA  TYR A 325     -14.751 -67.484  12.886  1.00 27.86           H  
ATOM   4920  HB2 TYR A 325     -15.407 -68.507  10.901  1.00 23.21           H  
ATOM   4921  HB3 TYR A 325     -14.110 -69.414  10.926  1.00 23.21           H  
ATOM   4922  HD1 TYR A 325     -14.014 -71.344  12.433  1.00 27.43           H  
ATOM   4923  HD2 TYR A 325     -17.345 -69.140  12.169  1.00 20.61           H  
ATOM   4924  HE1 TYR A 325     -15.196 -73.007  13.510  1.00 25.35           H  
ATOM   4925  HE2 TYR A 325     -18.531 -70.800  13.245  1.00 20.64           H  
ATOM   4926  HH  TYR A 325     -18.484 -72.826  14.205  1.00 39.90           H  
ATOM   4927  N   ASP A 326     -12.009 -69.165  12.793  1.00 30.03           N  
ANISOU 4927  N   ASP A 326     3479   3472   4458    -43    -92    450       N  
ATOM   4928  CA  ASP A 326     -11.015 -69.869  13.599  1.00 27.28           C  
ANISOU 4928  CA  ASP A 326     3057   3151   4159    -28   -130    483       C  
ATOM   4929  C   ASP A 326     -10.365 -68.944  14.636  1.00 33.31           C  
ANISOU 4929  C   ASP A 326     3832   3942   4882    -74   -196    502       C  
ATOM   4930  O   ASP A 326     -10.264 -69.296  15.818  1.00 35.22           O  
ANISOU 4930  O   ASP A 326     4070   4194   5116    -57   -247    536       O  
ATOM   4931  CB  ASP A 326      -9.944 -70.501  12.700  1.00 28.06           C  
ANISOU 4931  CB  ASP A 326     3063   3269   4331    -17    -95    473       C  
ATOM   4932  CG  ASP A 326     -10.416 -71.788  12.030  1.00 32.38           C  
ANISOU 4932  CG  ASP A 326     3597   3779   4927     46    -53    460       C  
ATOM   4933  OD1 ASP A 326     -11.424 -72.373  12.481  1.00 33.08           O  
ANISOU 4933  OD1 ASP A 326     3727   3833   5009     76    -67    476       O  
ATOM   4934  OD2 ASP A 326      -9.770 -72.222  11.052  1.00 30.61           O  
ANISOU 4934  OD2 ASP A 326     3322   3562   4745     66     -8    435       O  
ATOM   4935  H   ASP A 326     -11.824 -69.137  11.953  1.00 36.03           H  
ATOM   4936  HA  ASP A 326     -11.457 -70.586  14.080  1.00 32.74           H  
ATOM   4937  HB2 ASP A 326      -9.704 -69.871  12.003  1.00 33.68           H  
ATOM   4938  HB3 ASP A 326      -9.165 -70.713  13.238  1.00 33.68           H  
ATOM   4939  N   GLU A 327      -9.933 -67.765  14.193  1.00 25.37           N  
ANISOU 4939  N   GLU A 327     2848   2945   3848   -136   -201    482       N  
ATOM   4940  CA  GLU A 327      -9.378 -66.764  15.102  1.00 28.45           C  
ANISOU 4940  CA  GLU A 327     3270   3348   4193   -192   -274    494       C  
ATOM   4941  C   GLU A 327     -10.361 -66.473  16.225  1.00 29.51           C  
ANISOU 4941  C   GLU A 327     3502   3460   4250   -165   -310    496       C  
ATOM   4942  O   GLU A 327      -9.998 -66.462  17.406  1.00 37.56           O  
ANISOU 4942  O   GLU A 327     4531   4494   5245   -168   -375    520       O  
ATOM   4943  CB  GLU A 327      -9.069 -65.458  14.366  1.00 27.38           C  
ANISOU 4943  CB  GLU A 327     3169   3206   4029   -266   -275    472       C  
ATOM   4944  CG  GLU A 327      -7.616 -65.288  13.953  1.00 27.70           C  
ANISOU 4944  CG  GLU A 327     3109   3290   4124   -327   -288    494       C  
ATOM   4945  CD  GLU A 327      -7.286 -63.855  13.562  1.00 46.35           C  
ANISOU 4945  CD  GLU A 327     5520   5642   6449   -419   -316    487       C  
ATOM   4946  OE1 GLU A 327      -8.214 -63.022  13.490  1.00 46.12           O  
ANISOU 4946  OE1 GLU A 327     5606   5563   6353   -427   -318    457       O  
ATOM   4947  OE2 GLU A 327      -6.094 -63.562  13.334  1.00 58.74           O  
ANISOU 4947  OE2 GLU A 327     7009   7253   8058   -485   -338    517       O  
ATOM   4948  H   GLU A 327      -9.950 -67.519  13.369  1.00 30.45           H  
ATOM   4949  HA  GLU A 327      -8.555 -67.101  15.491  1.00 34.14           H  
ATOM   4950  HB2 GLU A 327      -9.609 -65.422  13.561  1.00 32.86           H  
ATOM   4951  HB3 GLU A 327      -9.298 -64.715  14.946  1.00 32.86           H  
ATOM   4952  HG2 GLU A 327      -7.044 -65.537  14.696  1.00 33.24           H  
ATOM   4953  HG3 GLU A 327      -7.436 -65.857  13.189  1.00 33.24           H  
ATOM   4954  N   HIS A 328     -11.610 -66.231  15.838  1.00 22.41           N  
ANISOU 4954  N   HIS A 328     2675   2529   3309   -136   -266    472       N  
ATOM   4955  CA  HIS A 328     -12.679 -65.971  16.791  1.00 19.35           C  
ANISOU 4955  CA  HIS A 328     2376   2129   2845    -96   -280    474       C  
ATOM   4956  C   HIS A 328     -12.732 -67.057  17.862  1.00 24.43           C  
ANISOU 4956  C   HIS A 328     2984   2798   3500    -50   -301    519       C  
ATOM   4957  O   HIS A 328     -12.701 -66.759  19.062  1.00 32.90           O  
ANISOU 4957  O   HIS A 328     4105   3884   4511    -45   -352    533       O  
ATOM   4958  CB  HIS A 328     -14.020 -65.859  16.057  1.00 21.13           C  
ANISOU 4958  CB  HIS A 328     2648   2329   3051    -61   -218    455       C  
ATOM   4959  CG  HIS A 328     -15.194 -65.639  16.960  1.00 24.19           C  
ANISOU 4959  CG  HIS A 328     3111   2716   3364     -9   -217    464       C  
ATOM   4960  ND1 HIS A 328     -15.954 -64.491  16.924  1.00 22.89           N  
ANISOU 4960  ND1 HIS A 328     3041   2528   3129      0   -211    435       N  
ATOM   4961  CD2 HIS A 328     -15.747 -66.424  17.916  1.00 28.74           C  
ANISOU 4961  CD2 HIS A 328     3679   3316   3926     42   -217    504       C  
ATOM   4962  CE1 HIS A 328     -16.920 -64.574  17.821  1.00 23.15           C  
ANISOU 4962  CE1 HIS A 328     3117   2576   3103     61   -201    453       C  
ATOM   4963  NE2 HIS A 328     -16.815 -65.738  18.438  1.00 20.35           N  
ANISOU 4963  NE2 HIS A 328     2699   2253   2779     82   -203    498       N  
ATOM   4964  H   HIS A 328     -11.865 -66.212  15.017  1.00 26.89           H  
ATOM   4965  HA  HIS A 328     -12.508 -65.124  17.232  1.00 23.21           H  
ATOM   4966  HB2 HIS A 328     -13.977 -65.111  15.441  1.00 25.35           H  
ATOM   4967  HB3 HIS A 328     -14.176 -66.680  15.565  1.00 25.35           H  
ATOM   4968  HD1 HIS A 328     -15.819 -63.822  16.400  1.00 27.47           H  
ATOM   4969  HD2 HIS A 328     -15.454 -67.269  18.174  1.00 34.49           H  
ATOM   4970  HE1 HIS A 328     -17.563 -63.924  17.991  1.00 27.78           H  
ATOM   4971  HE2 HIS A 328     -17.333 -66.020  19.063  1.00 24.42           H  
ATOM   4972  N   HIS A 329     -12.794 -68.316  17.443  1.00 27.57           N  
ANISOU 4972  N   HIS A 329     3306   3197   3971    -17   -266    541       N  
ATOM   4973  CA  HIS A 329     -12.880 -69.397  18.430  1.00 29.39           C  
ANISOU 4973  CA  HIS A 329     3506   3444   4217     23   -290    592       C  
ATOM   4974  C   HIS A 329     -11.613 -69.622  19.278  1.00 30.17           C  
ANISOU 4974  C   HIS A 329     3555   3571   4337      4   -359    621       C  
ATOM   4975  O   HIS A 329     -11.722 -69.875  20.487  1.00 28.74           O  
ANISOU 4975  O   HIS A 329     3396   3408   4115     22   -403    659       O  
ATOM   4976  CB  HIS A 329     -13.394 -70.685  17.783  1.00 27.54           C  
ANISOU 4976  CB  HIS A 329     3220   3189   4054     63   -245    609       C  
ATOM   4977  CG  HIS A 329     -14.883 -70.702  17.625  1.00 36.40           C  
ANISOU 4977  CG  HIS A 329     4393   4295   5140     90   -203    614       C  
ATOM   4978  ND1 HIS A 329     -15.512 -70.394  16.437  1.00 37.73           N  
ANISOU 4978  ND1 HIS A 329     4581   4438   5316     84   -155    578       N  
ATOM   4979  CD2 HIS A 329     -15.870 -70.936  18.523  1.00 35.65           C  
ANISOU 4979  CD2 HIS A 329     4332   4216   4999    122   -203    657       C  
ATOM   4980  CE1 HIS A 329     -16.821 -70.466  16.603  1.00 37.66           C  
ANISOU 4980  CE1 HIS A 329     4608   4427   5274    110   -132    599       C  
ATOM   4981  NE2 HIS A 329     -17.065 -70.792  17.859  1.00 38.20           N  
ANISOU 4981  NE2 HIS A 329     4682   4523   5310    135   -156    649       N  
ATOM   4982  H   HIS A 329     -12.789 -68.570  16.622  1.00 33.08           H  
ATOM   4983  HA  HIS A 329     -13.566 -69.134  19.063  1.00 35.27           H  
ATOM   4984  HB2 HIS A 329     -12.998 -70.776  16.902  1.00 33.04           H  
ATOM   4985  HB3 HIS A 329     -13.143 -71.440  18.339  1.00 33.04           H  
ATOM   4986  HD1 HIS A 329     -15.114 -70.199  15.700  1.00 45.27           H  
ATOM   4987  HD2 HIS A 329     -15.759 -71.165  19.417  1.00 42.78           H  
ATOM   4988  HE1 HIS A 329     -17.462 -70.312  15.947  1.00 45.19           H  
ATOM   4989  HE2 HIS A 329     -17.845 -70.899  18.206  1.00 45.84           H  
ATOM   4990  N   GLN A 330     -10.427 -69.504  18.679  1.00 28.25           N  
ANISOU 4990  N   GLN A 330     3243   3337   4152    -33   -371    610       N  
ATOM   4991  CA  GLN A 330      -9.190 -69.562  19.464  1.00 33.60           C  
ANISOU 4991  CA  GLN A 330     3867   4047   4850    -60   -445    642       C  
ATOM   4992  C   GLN A 330      -9.206 -68.484  20.549  1.00 33.61           C  
ANISOU 4992  C   GLN A 330     3960   4056   4753    -97   -515    640       C  
ATOM   4993  O   GLN A 330      -9.001 -68.767  21.741  1.00 36.27           O  
ANISOU 4993  O   GLN A 330     4308   4412   5059    -87   -577    677       O  
ATOM   4994  CB  GLN A 330      -7.952 -69.381  18.575  1.00 33.92           C  
ANISOU 4994  CB  GLN A 330     3816   4108   4963   -101   -441    633       C  
ATOM   4995  CG  GLN A 330      -7.638 -70.571  17.672  1.00 46.33           C  
ANISOU 4995  CG  GLN A 330     5291   5679   6634    -52   -383    636       C  
ATOM   4996  CD  GLN A 330      -6.385 -70.363  16.838  1.00 60.95           C  
ANISOU 4996  CD  GLN A 330     7044   7567   8549    -84   -368    632       C  
ATOM   4997  OE1 GLN A 330      -6.023 -69.231  16.510  1.00 63.39           O  
ANISOU 4997  OE1 GLN A 330     7368   7890   8826   -153   -377    617       O  
ATOM   4998  NE2 GLN A 330      -5.711 -71.459  16.494  1.00 60.25           N  
ANISOU 4998  NE2 GLN A 330     6852   7491   8548    -32   -346    650       N  
ATOM   4999  H   GLN A 330     -10.311 -69.391  17.835  1.00 33.90           H  
ATOM   5000  HA  GLN A 330      -9.127 -70.428  19.898  1.00 40.32           H  
ATOM   5001  HB2 GLN A 330      -8.090 -68.609  18.005  1.00 40.70           H  
ATOM   5002  HB3 GLN A 330      -7.181 -69.233  19.144  1.00 40.70           H  
ATOM   5003  HG2 GLN A 330      -7.505 -71.359  18.222  1.00 55.60           H  
ATOM   5004  HG3 GLN A 330      -8.382 -70.712  17.065  1.00 55.60           H  
ATOM   5005 HE21 GLN A 330      -5.993 -72.233  16.744  1.00 72.30           H  
ATOM   5006 HE22 GLN A 330      -4.995 -71.394  16.023  1.00 72.30           H  
ATOM   5007  N   ASP A 331      -9.469 -67.249  20.126  1.00 23.36           N  
ANISOU 5007  N   ASP A 331     2737   2738   3400   -137   -507    595       N  
ATOM   5008  CA  ASP A 331      -9.516 -66.117  21.043  1.00 21.97           C  
ANISOU 5008  CA  ASP A 331     2669   2554   3125   -170   -575    579       C  
ATOM   5009  C   ASP A 331     -10.565 -66.337  22.124  1.00 21.93           C  
ANISOU 5009  C   ASP A 331     2746   2551   3034   -107   -574    590       C  
ATOM   5010  O   ASP A 331     -10.326 -66.057  23.296  1.00 24.80           O  
ANISOU 5010  O   ASP A 331     3166   2928   3328   -113   -645    602       O  
ATOM   5011  CB  ASP A 331      -9.829 -64.826  20.285  1.00 21.75           C  
ANISOU 5011  CB  ASP A 331     2718   2489   3058   -210   -557    527       C  
ATOM   5012  CG  ASP A 331      -8.666 -64.346  19.437  1.00 29.94           C  
ANISOU 5012  CG  ASP A 331     3688   3531   4157   -291   -576    525       C  
ATOM   5013  OD1 ASP A 331      -7.573 -64.945  19.525  1.00 30.07           O  
ANISOU 5013  OD1 ASP A 331     3596   3587   4244   -314   -607    563       O  
ATOM   5014  OD2 ASP A 331      -8.840 -63.363  18.685  1.00 33.47           O  
ANISOU 5014  OD2 ASP A 331     4186   3947   4583   -331   -561    492       O  
ATOM   5015  H   ASP A 331      -9.624 -67.041  19.306  1.00 28.03           H  
ATOM   5016  HA  ASP A 331      -8.652 -66.016  21.473  1.00 26.37           H  
ATOM   5017  HB2 ASP A 331     -10.585 -64.981  19.697  1.00 26.10           H  
ATOM   5018  HB3 ASP A 331     -10.042 -64.128  20.924  1.00 26.10           H  
ATOM   5019  N   LEU A 332     -11.731 -66.836  21.726  1.00 21.26           N  
ANISOU 5019  N   LEU A 332     2669   2459   2951    -49   -495    590       N  
ATOM   5020  CA  LEU A 332     -12.805 -67.085  22.683  1.00 23.44           C  
ANISOU 5020  CA  LEU A 332     3008   2749   3148     13   -479    611       C  
ATOM   5021  C   LEU A 332     -12.376 -68.078  23.757  1.00 31.88           C  
ANISOU 5021  C   LEU A 332     4035   3853   4225     30   -526    673       C  
ATOM   5022  O   LEU A 332     -12.539 -67.815  24.954  1.00 39.23           O  
ANISOU 5022  O   LEU A 332     5038   4806   5061     45   -568    687       O  
ATOM   5023  CB  LEU A 332     -14.064 -67.587  21.970  1.00 24.57           C  
ANISOU 5023  CB  LEU A 332     3139   2883   3313     62   -390    616       C  
ATOM   5024  CG  LEU A 332     -15.282 -67.871  22.858  1.00 26.05           C  
ANISOU 5024  CG  LEU A 332     3375   3098   3427    126   -360    651       C  
ATOM   5025  CD1 LEU A 332     -15.685 -66.632  23.654  1.00 22.30           C  
ANISOU 5025  CD1 LEU A 332     3023   2627   2823    144   -378    616       C  
ATOM   5026  CD2 LEU A 332     -16.452 -68.363  22.016  1.00 20.00           C  
ANISOU 5026  CD2 LEU A 332     2579   2322   2700    159   -282    662       C  
ATOM   5027  H   LEU A 332     -11.924 -67.038  20.913  1.00 25.51           H  
ATOM   5028  HA  LEU A 332     -13.029 -66.251  23.124  1.00 28.12           H  
ATOM   5029  HB2 LEU A 332     -14.331 -66.919  21.319  1.00 29.48           H  
ATOM   5030  HB3 LEU A 332     -13.844 -68.413  21.511  1.00 29.48           H  
ATOM   5031  HG  LEU A 332     -15.055 -68.570  23.490  1.00 31.27           H  
ATOM   5032 HD11 LEU A 332     -15.906 -65.918  23.035  1.00 26.76           H  
ATOM   5033 HD12 LEU A 332     -16.455 -66.846  24.202  1.00 26.76           H  
ATOM   5034 HD13 LEU A 332     -14.942 -66.364  24.217  1.00 26.76           H  
ATOM   5035 HD21 LEU A 332     -16.191 -69.179  21.561  1.00 24.00           H  
ATOM   5036 HD22 LEU A 332     -17.208 -68.535  22.597  1.00 24.00           H  
ATOM   5037 HD23 LEU A 332     -16.682 -67.680  21.366  1.00 24.00           H  
ATOM   5038  N   THR A 333     -11.819 -69.211  23.335  1.00 34.34           N  
ANISOU 5038  N   THR A 333     4236   4168   4644     30   -521    708       N  
ATOM   5039  CA  THR A 333     -11.350 -70.203  24.297  1.00 25.38           C  
ANISOU 5039  CA  THR A 333     3056   3060   3528     47   -572    773       C  
ATOM   5040  C   THR A 333     -10.292 -69.605  25.234  1.00 31.56           C  
ANISOU 5040  C   THR A 333     3862   3864   4264      3   -672    778       C  
ATOM   5041  O   THR A 333     -10.391 -69.753  26.465  1.00 29.85           O  
ANISOU 5041  O   THR A 333     3693   3674   3973     18   -721    815       O  
ATOM   5042  CB  THR A 333     -10.818 -71.475  23.600  1.00 36.97           C  
ANISOU 5042  CB  THR A 333     4403   4516   5128     61   -556    803       C  
ATOM   5043  OG1 THR A 333      -9.775 -71.133  22.678  1.00 46.53           O  
ANISOU 5043  OG1 THR A 333     5550   5720   6409     21   -561    769       O  
ATOM   5044  CG2 THR A 333     -11.955 -72.192  22.859  1.00 41.04           C  
ANISOU 5044  CG2 THR A 333     4910   5004   5679    102   -475    806       C  
ATOM   5045  H   THR A 333     -11.704 -69.428  22.511  1.00 41.21           H  
ATOM   5046  HA  THR A 333     -12.103 -70.470  24.848  1.00 30.46           H  
ATOM   5047  HB  THR A 333     -10.465 -72.081  24.270  1.00 44.37           H  
ATOM   5048  HG1 THR A 333     -10.069 -70.606  22.094  1.00 55.84           H  
ATOM   5049 HG21 THR A 333     -12.336 -71.603  22.189  1.00 49.25           H  
ATOM   5050 HG22 THR A 333     -11.616 -72.989  22.424  1.00 49.25           H  
ATOM   5051 HG23 THR A 333     -12.650 -72.446  23.487  1.00 49.25           H  
ATOM   5052  N   LEU A 334      -9.301 -68.919  24.664  1.00 23.30           N  
ANISOU 5052  N   LEU A 334     2785   2810   3256    -57   -706    746       N  
ATOM   5053  CA  LEU A 334      -8.285 -68.259  25.487  1.00 24.98           C  
ANISOU 5053  CA  LEU A 334     3022   3040   3430   -113   -813    752       C  
ATOM   5054  C   LEU A 334      -8.937 -67.351  26.533  1.00 29.35           C  
ANISOU 5054  C   LEU A 334     3728   3590   3834   -108   -849    727       C  
ATOM   5055  O   LEU A 334      -8.723 -67.520  27.740  1.00 37.69           O  
ANISOU 5055  O   LEU A 334     4823   4671   4826   -103   -919    761       O  
ATOM   5056  CB  LEU A 334      -7.314 -67.444  24.622  1.00 25.14           C  
ANISOU 5056  CB  LEU A 334     3000   3050   3504   -188   -836    721       C  
ATOM   5057  CG  LEU A 334      -6.261 -66.626  25.385  1.00 31.48           C  
ANISOU 5057  CG  LEU A 334     3829   3864   4269   -266   -958    729       C  
ATOM   5058  CD1 LEU A 334      -5.263 -67.526  26.102  1.00 27.24           C  
ANISOU 5058  CD1 LEU A 334     3193   3368   3788   -269  -1034    798       C  
ATOM   5059  CD2 LEU A 334      -5.539 -65.670  24.452  1.00 25.49           C  
ANISOU 5059  CD2 LEU A 334     3043   3091   3552   -348   -970    700       C  
ATOM   5060  H   LEU A 334      -9.195 -68.820  23.816  1.00 27.95           H  
ATOM   5061  HA  LEU A 334      -7.771 -68.935  25.956  1.00 29.98           H  
ATOM   5062  HB2 LEU A 334      -6.839 -68.055  24.038  1.00 30.17           H  
ATOM   5063  HB3 LEU A 334      -7.831 -66.822  24.085  1.00 30.17           H  
ATOM   5064  HG  LEU A 334      -6.712 -66.093  26.058  1.00 37.78           H  
ATOM   5065 HD11 LEU A 334      -4.810 -68.080  25.447  1.00 32.69           H  
ATOM   5066 HD12 LEU A 334      -4.618 -66.972  26.570  1.00 32.69           H  
ATOM   5067 HD13 LEU A 334      -5.740 -68.085  26.736  1.00 32.69           H  
ATOM   5068 HD21 LEU A 334      -6.187 -65.064  24.059  1.00 30.59           H  
ATOM   5069 HD22 LEU A 334      -4.883 -65.169  24.960  1.00 30.59           H  
ATOM   5070 HD23 LEU A 334      -5.099 -66.182  23.755  1.00 30.59           H  
ATOM   5071  N   LEU A 335      -9.742 -66.405  26.056  1.00 24.11           N  
ANISOU 5071  N   LEU A 335     3153   2894   3113   -102   -799    668       N  
ATOM   5072  CA  LEU A 335     -10.431 -65.455  26.923  1.00 24.50           C  
ANISOU 5072  CA  LEU A 335     3357   2934   3018    -81   -820    632       C  
ATOM   5073  C   LEU A 335     -11.161 -66.173  28.055  1.00 24.77           C  
ANISOU 5073  C   LEU A 335     3427   3008   2976    -11   -807    676       C  
ATOM   5074  O   LEU A 335     -11.018 -65.807  29.226  1.00 28.26           O  
ANISOU 5074  O   LEU A 335     3961   3466   3310     -9   -876    678       O  
ATOM   5075  CB  LEU A 335     -11.421 -64.613  26.111  1.00 23.88           C  
ANISOU 5075  CB  LEU A 335     3348   2816   2908    -57   -744    573       C  
ATOM   5076  CG  LEU A 335     -12.195 -63.550  26.898  1.00 24.71           C  
ANISOU 5076  CG  LEU A 335     3620   2904   2866    -18   -755    526       C  
ATOM   5077  CD1 LEU A 335     -11.275 -62.430  27.364  1.00 25.26           C  
ANISOU 5077  CD1 LEU A 335     3781   2937   2878    -90   -870    487       C  
ATOM   5078  CD2 LEU A 335     -13.336 -62.996  26.065  1.00 23.69           C  
ANISOU 5078  CD2 LEU A 335     3534   2744   2722     27   -663    483       C  
ATOM   5079  H   LEU A 335      -9.907 -66.291  25.220  1.00 28.93           H  
ATOM   5080  HA  LEU A 335      -9.779 -64.856  27.317  1.00 29.40           H  
ATOM   5081  HB2 LEU A 335     -10.930 -64.156  25.411  1.00 28.65           H  
ATOM   5082  HB3 LEU A 335     -12.073 -65.210  25.711  1.00 28.65           H  
ATOM   5083  HG  LEU A 335     -12.579 -63.965  27.686  1.00 29.66           H  
ATOM   5084 HD11 LEU A 335     -10.869 -62.011  26.589  1.00 30.31           H  
ATOM   5085 HD12 LEU A 335     -11.798 -61.777  27.857  1.00 30.31           H  
ATOM   5086 HD13 LEU A 335     -10.588 -62.804  27.937  1.00 30.31           H  
ATOM   5087 HD21 LEU A 335     -13.937 -63.720  25.832  1.00 28.42           H  
ATOM   5088 HD22 LEU A 335     -13.809 -62.326  26.584  1.00 28.42           H  
ATOM   5089 HD23 LEU A 335     -12.973 -62.595  25.260  1.00 28.42           H  
ATOM   5090  N   LYS A 336     -11.928 -67.203  27.704  1.00 26.28           N  
ANISOU 5090  N   LYS A 336     3549   3217   3220     43   -722    716       N  
ATOM   5091  CA  LYS A 336     -12.651 -67.990  28.700  1.00 24.42           C  
ANISOU 5091  CA  LYS A 336     3330   3026   2923    102   -702    775       C  
ATOM   5092  C   LYS A 336     -11.716 -68.549  29.764  1.00 28.72           C  
ANISOU 5092  C   LYS A 336     3855   3601   3457     80   -798    830       C  
ATOM   5093  O   LYS A 336     -11.963 -68.384  30.964  1.00 30.92           O  
ANISOU 5093  O   LYS A 336     4223   3912   3614    104   -832    847       O  
ATOM   5094  CB  LYS A 336     -13.408 -69.131  28.025  1.00 23.69           C  
ANISOU 5094  CB  LYS A 336     3144   2937   2920    140   -615    820       C  
ATOM   5095  CG  LYS A 336     -14.807 -68.752  27.575  1.00 27.41           C  
ANISOU 5095  CG  LYS A 336     3660   3405   3349    189   -519    796       C  
ATOM   5096  CD  LYS A 336     -15.417 -69.827  26.698  1.00 22.45           C  
ANISOU 5096  CD  LYS A 336     2935   2768   2828    205   -450    835       C  
ATOM   5097  CE  LYS A 336     -16.808 -69.448  26.226  1.00 22.00           C  
ANISOU 5097  CE  LYS A 336     2910   2712   2735    248   -362    820       C  
ATOM   5098  NZ  LYS A 336     -17.359 -70.497  25.329  1.00 23.85           N  
ANISOU 5098  NZ  LYS A 336     3054   2930   3077    251   -311    858       N  
ATOM   5099  H   LYS A 336     -12.047 -67.466  26.894  1.00 31.54           H  
ATOM   5100  HA  LYS A 336     -13.300 -67.420  29.142  1.00 29.31           H  
ATOM   5101  HB2 LYS A 336     -12.911 -69.416  27.242  1.00 28.43           H  
ATOM   5102  HB3 LYS A 336     -13.487 -69.868  28.651  1.00 28.43           H  
ATOM   5103  HG2 LYS A 336     -15.374 -68.637  28.354  1.00 32.89           H  
ATOM   5104  HG3 LYS A 336     -14.767 -67.929  27.064  1.00 32.89           H  
ATOM   5105  HD2 LYS A 336     -14.857 -69.957  25.917  1.00 26.94           H  
ATOM   5106  HD3 LYS A 336     -15.483 -70.652  27.204  1.00 26.94           H  
ATOM   5107  HE2 LYS A 336     -17.396 -69.359  26.992  1.00 26.40           H  
ATOM   5108  HE3 LYS A 336     -16.765 -68.613  25.733  1.00 26.40           H  
ATOM   5109  HZ1 LYS A 336     -17.406 -71.273  25.762  1.00 28.62           H  
ATOM   5110  HZ2 LYS A 336     -18.174 -70.267  25.057  1.00 28.62           H  
ATOM   5111  HZ3 LYS A 336     -16.833 -70.595  24.617  1.00 28.62           H  
ATOM   5112  N   ALA A 337     -10.647 -69.210  29.324  1.00 31.99           N  
ANISOU 5112  N   ALA A 337     4153   4007   3995     39   -841    859       N  
ATOM   5113  CA  ALA A 337      -9.663 -69.759  30.257  1.00 26.78           C  
ANISOU 5113  CA  ALA A 337     3459   3375   3342     17   -942    917       C  
ATOM   5114  C   ALA A 337      -9.166 -68.678  31.212  1.00 27.45           C  
ANISOU 5114  C   ALA A 337     3658   3467   3306    -23  -1041    886       C  
ATOM   5115  O   ALA A 337      -9.192 -68.848  32.440  1.00 40.93           O  
ANISOU 5115  O   ALA A 337     5429   5207   4915     -8  -1096    924       O  
ATOM   5116  CB  ALA A 337      -8.494 -70.370  29.502  1.00 26.10           C  
ANISOU 5116  CB  ALA A 337     3230   3278   3410    -20   -972    938       C  
ATOM   5117  H   ALA A 337     -10.468 -69.353  28.495  1.00 38.39           H  
ATOM   5118  HA  ALA A 337     -10.081 -70.459  30.784  1.00 32.14           H  
ATOM   5119  HB1 ALA A 337      -8.073 -69.682  28.963  1.00 31.32           H  
ATOM   5120  HB2 ALA A 337      -7.857 -70.727  30.141  1.00 31.32           H  
ATOM   5121  HB3 ALA A 337      -8.824 -71.082  28.931  1.00 31.32           H  
ATOM   5122  N   LEU A 338      -8.726 -67.560  30.642  1.00 35.70           N  
ANISOU 5122  N   LEU A 338     4737   4477   4352    -77  -1067    820       N  
ATOM   5123  CA  LEU A 338      -8.249 -66.443  31.450  1.00 35.34           C  
ANISOU 5123  CA  LEU A 338     4812   4421   4194   -125  -1172    783       C  
ATOM   5124  C   LEU A 338      -9.298 -66.046  32.496  1.00 43.05           C  
ANISOU 5124  C   LEU A 338     5948   5412   4998    -61  -1153    762       C  
ATOM   5125  O   LEU A 338      -8.995 -66.009  33.693  1.00 48.82           O  
ANISOU 5125  O   LEU A 338     6753   6167   5628    -65  -1239    783       O  
ATOM   5126  CB  LEU A 338      -7.876 -65.243  30.567  1.00 30.36           C  
ANISOU 5126  CB  LEU A 338     4209   3739   3588   -189  -1187    713       C  
ATOM   5127  CG  LEU A 338      -6.817 -65.462  29.476  1.00 37.00           C  
ANISOU 5127  CG  LEU A 338     4896   4575   4587   -255  -1197    731       C  
ATOM   5128  CD1 LEU A 338      -6.696 -64.224  28.596  1.00 38.23           C  
ANISOU 5128  CD1 LEU A 338     5096   4681   4748   -315  -1195    667       C  
ATOM   5129  CD2 LEU A 338      -5.457 -65.830  30.059  1.00 33.09           C  
ANISOU 5129  CD2 LEU A 338     4319   4110   4142   -316  -1319    790       C  
ATOM   5130  H   LEU A 338      -8.693 -67.424  29.793  1.00 42.84           H  
ATOM   5131  HA  LEU A 338      -7.450 -66.721  31.924  1.00 42.41           H  
ATOM   5132  HB2 LEU A 338      -8.682 -64.936  30.123  1.00 36.44           H  
ATOM   5133  HB3 LEU A 338      -7.545 -64.538  31.145  1.00 36.44           H  
ATOM   5134  HG  LEU A 338      -7.103 -66.197  28.911  1.00 44.40           H  
ATOM   5135 HD11 LEU A 338      -6.435 -63.469  29.147  1.00 45.87           H  
ATOM   5136 HD12 LEU A 338      -6.023 -64.385  27.916  1.00 45.87           H  
ATOM   5137 HD13 LEU A 338      -7.553 -64.048  28.178  1.00 45.87           H  
ATOM   5138 HD21 LEU A 338      -5.545 -66.650  30.570  1.00 39.70           H  
ATOM   5139 HD22 LEU A 338      -4.827 -65.957  29.333  1.00 39.70           H  
ATOM   5140 HD23 LEU A 338      -5.157 -65.110  30.637  1.00 39.70           H  
ATOM   5141  N   VAL A 339     -10.524 -65.754  32.055  1.00 37.53           N  
ANISOU 5141  N   VAL A 339     5299   4702   4259      2  -1040    723       N  
ATOM   5142  CA  VAL A 339     -11.570 -65.287  32.976  1.00 38.33           C  
ANISOU 5142  CA  VAL A 339     5547   4823   4193     76  -1007    700       C  
ATOM   5143  C   VAL A 339     -11.877 -66.322  34.058  1.00 44.77           C  
ANISOU 5143  C   VAL A 339     6352   5706   4951    124  -1002    781       C  
ATOM   5144  O   VAL A 339     -12.170 -65.963  35.196  1.00 46.61           O  
ANISOU 5144  O   VAL A 339     6711   5969   5029    160  -1030    775       O  
ATOM   5145  CB  VAL A 339     -12.861 -64.854  32.241  1.00 38.44           C  
ANISOU 5145  CB  VAL A 339     5594   4821   4191    142   -881    655       C  
ATOM   5146  CG1 VAL A 339     -13.932 -64.422  33.241  1.00 36.62           C  
ANISOU 5146  CG1 VAL A 339     5503   4624   3785    232   -837    638       C  
ATOM   5147  CG2 VAL A 339     -12.558 -63.704  31.294  1.00 32.39           C  
ANISOU 5147  CG2 VAL A 339     4866   3983   3459     93   -898    576       C  
ATOM   5148  H   VAL A 339     -10.776 -65.815  31.235  1.00 45.04           H  
ATOM   5149  HA  VAL A 339     -11.232 -64.501  33.432  1.00 45.99           H  
ATOM   5150  HB  VAL A 339     -13.206 -65.598  31.722  1.00 46.13           H  
ATOM   5151 HG11 VAL A 339     -13.595 -63.675  33.760  1.00 43.94           H  
ATOM   5152 HG12 VAL A 339     -14.728 -64.156  32.756  1.00 43.94           H  
ATOM   5153 HG13 VAL A 339     -14.135 -65.168  33.827  1.00 43.94           H  
ATOM   5154 HG21 VAL A 339     -11.899 -63.996  30.645  1.00 38.87           H  
ATOM   5155 HG22 VAL A 339     -13.376 -63.445  30.841  1.00 38.87           H  
ATOM   5156 HG23 VAL A 339     -12.211 -62.957  31.806  1.00 38.87           H  
ATOM   5157  N   ARG A 340     -11.806 -67.603  33.715  1.00 42.10           N  
ANISOU 5157  N   ARG A 340     5871   5391   4733    126   -968    858       N  
ATOM   5158  CA  ARG A 340     -11.912 -68.634  34.740  1.00 48.77           C  
ANISOU 5158  CA  ARG A 340     6699   6294   5539    155   -984    948       C  
ATOM   5159  C   ARG A 340     -10.779 -68.502  35.741  1.00 55.67           C  
ANISOU 5159  C   ARG A 340     7614   7179   6358    104  -1126    965       C  
ATOM   5160  O   ARG A 340     -11.001 -68.586  36.946  1.00 60.16           O  
ANISOU 5160  O   ARG A 340     8273   7794   6793    133  -1158    997       O  
ATOM   5161  CB  ARG A 340     -11.896 -70.032  34.128  1.00 43.14           C  
ANISOU 5161  CB  ARG A 340     5827   5584   4980    157   -943   1026       C  
ATOM   5162  CG  ARG A 340     -13.246 -70.483  33.613  1.00 53.78           C  
ANISOU 5162  CG  ARG A 340     7147   6943   6345    215   -813   1046       C  
ATOM   5163  CD  ARG A 340     -13.910 -71.487  34.543  1.00 56.94           C  
ANISOU 5163  CD  ARG A 340     7540   7402   6692    258   -787   1146       C  
ATOM   5164  NE  ARG A 340     -15.194 -71.934  34.002  1.00 55.28           N  
ANISOU 5164  NE  ARG A 340     7290   7203   6512    302   -669   1175       N  
ATOM   5165  CZ  ARG A 340     -16.392 -71.588  34.472  1.00 52.47           C  
ANISOU 5165  CZ  ARG A 340     7002   6899   6036    360   -589   1183       C  
ATOM   5166  NH1 ARG A 340     -16.514 -70.792  35.530  1.00 54.54           N  
ANISOU 5166  NH1 ARG A 340     7390   7205   6127    393   -605   1158       N  
ATOM   5167  NH2 ARG A 340     -17.484 -72.056  33.883  1.00 44.33           N  
ANISOU 5167  NH2 ARG A 340     5912   5878   5054    389   -491   1219       N  
ATOM   5168  H   ARG A 340     -11.700 -67.897  32.914  1.00 50.52           H  
ATOM   5169  HA  ARG A 340     -12.750 -68.524  35.216  1.00 58.53           H  
ATOM   5170  HB2 ARG A 340     -11.276 -70.040  33.383  1.00 51.77           H  
ATOM   5171  HB3 ARG A 340     -11.608 -70.666  34.803  1.00 51.77           H  
ATOM   5172  HG2 ARG A 340     -13.830 -69.712  33.535  1.00 64.54           H  
ATOM   5173  HG3 ARG A 340     -13.131 -70.903  32.747  1.00 64.54           H  
ATOM   5174  HD2 ARG A 340     -13.334 -72.261  34.644  1.00 68.33           H  
ATOM   5175  HD3 ARG A 340     -14.069 -71.071  35.405  1.00 68.33           H  
ATOM   5176  HE  ARG A 340     -15.174 -72.464  33.325  1.00 66.34           H  
ATOM   5177 HH11 ARG A 340     -15.813 -70.481  35.919  1.00 65.45           H  
ATOM   5178 HH12 ARG A 340     -17.296 -70.582  35.822  1.00 65.45           H  
ATOM   5179 HH21 ARG A 340     -17.415 -72.575  33.201  1.00 53.20           H  
ATOM   5180 HH22 ARG A 340     -18.260 -71.843  34.185  1.00 53.20           H  
ATOM   5181  N   GLN A 341      -9.562 -68.292  35.251  1.00119.45           N  
ANISOU 5181  N   GLN A 341    15629  15222  14537     28  -1214    949       N  
ATOM   5182  CA  GLN A 341      -8.420 -68.192  36.159  1.00120.00           C  
ANISOU 5182  CA  GLN A 341    15722  15302  14569    -30  -1362    974       C  
ATOM   5183  C   GLN A 341      -8.401 -66.940  37.048  1.00122.39           C  
ANISOU 5183  C   GLN A 341    16212  15595  14694    -45  -1440    908       C  
ATOM   5184  O   GLN A 341      -8.219 -67.051  38.260  1.00134.31           O  
ANISOU 5184  O   GLN A 341    17803  17141  16089    -41  -1519    940       O  
ATOM   5185  CB  GLN A 341      -7.115 -68.289  35.381  1.00115.63           C  
ANISOU 5185  CB  GLN A 341    15035  14722  14176   -108  -1433    983       C  
ATOM   5186  CG  GLN A 341      -6.911 -69.635  34.748  1.00115.02           C  
ANISOU 5186  CG  GLN A 341    14785  14655  14261    -88  -1385   1054       C  
ATOM   5187  CD  GLN A 341      -5.760 -69.632  33.773  1.00114.84           C  
ANISOU 5187  CD  GLN A 341    14627  14611  14396   -147  -1422   1050       C  
ATOM   5188  OE1 GLN A 341      -5.357 -68.583  33.263  1.00114.83           O  
ANISOU 5188  OE1 GLN A 341    14650  14582  14397   -205  -1447    989       O  
ATOM   5189  NE2 GLN A 341      -5.213 -70.804  33.514  1.00114.81           N  
ANISOU 5189  NE2 GLN A 341    14479  14620  14524   -133  -1425   1119       N  
ATOM   5190  H   GLN A 341      -9.371 -68.205  34.417  1.00143.35           H  
ATOM   5191  HA  GLN A 341      -8.450 -68.957  36.755  1.00144.00           H  
ATOM   5192  HB2 GLN A 341      -7.117 -67.623  34.676  1.00138.75           H  
ATOM   5193  HB3 GLN A 341      -6.374 -68.128  35.987  1.00138.75           H  
ATOM   5194  HG2 GLN A 341      -6.719 -70.287  35.440  1.00138.02           H  
ATOM   5195  HG3 GLN A 341      -7.715 -69.885  34.266  1.00138.02           H  
ATOM   5196 HE21 GLN A 341      -5.515 -71.513  33.894  1.00137.77           H  
ATOM   5197 HE22 GLN A 341      -4.553 -70.858  32.965  1.00137.77           H  
ATOM   5198  N   GLN A 342      -8.595 -65.761  36.459  1.00 54.65           N  
ANISOU 5198  N   GLN A 342     7710   6963   6090    -60  -1423    815       N  
ATOM   5199  CA  GLN A 342      -8.267 -64.503  37.144  1.00 50.79           C  
ANISOU 5199  CA  GLN A 342     7395   6441   5464    -97  -1529    745       C  
ATOM   5200  C   GLN A 342      -9.459 -63.631  37.561  1.00 60.86           C  
ANISOU 5200  C   GLN A 342     8853   7704   6566    -13  -1460    669       C  
ATOM   5201  O   GLN A 342      -9.315 -62.749  38.410  1.00 69.93           O  
ANISOU 5201  O   GLN A 342    10173   8831   7566    -20  -1548    615       O  
ATOM   5202  CB  GLN A 342      -7.330 -63.677  36.264  1.00 48.90           C  
ANISOU 5202  CB  GLN A 342     7120   6137   5323   -197  -1601    700       C  
ATOM   5203  CG  GLN A 342      -6.371 -64.536  35.470  1.00 48.48           C  
ANISOU 5203  CG  GLN A 342     6856   6100   5466   -255  -1616    768       C  
ATOM   5204  CD  GLN A 342      -5.374 -63.734  34.670  1.00 52.34           C  
ANISOU 5204  CD  GLN A 342     7299   6541   6047   -360  -1689    738       C  
ATOM   5205  OE1 GLN A 342      -5.135 -62.558  34.941  1.00 60.55           O  
ANISOU 5205  OE1 GLN A 342     8471   7533   7003   -415  -1777    679       O  
ATOM   5206  NE2 GLN A 342      -4.781 -64.373  33.672  1.00 57.81           N  
ANISOU 5206  NE2 GLN A 342     7806   7247   6912   -389  -1654    781       N  
ATOM   5207  H   GLN A 342      -8.914 -65.658  35.666  1.00 65.58           H  
ATOM   5208  HA  GLN A 342      -7.779 -64.722  37.954  1.00 60.95           H  
ATOM   5209  HB2 GLN A 342      -7.859 -63.159  35.637  1.00 58.68           H  
ATOM   5210  HB3 GLN A 342      -6.807 -63.085  36.826  1.00 58.68           H  
ATOM   5211  HG2 GLN A 342      -5.876 -65.102  36.082  1.00 58.18           H  
ATOM   5212  HG3 GLN A 342      -6.879 -65.083  34.850  1.00 58.18           H  
ATOM   5213 HE21 GLN A 342      -4.973 -65.196  33.513  1.00 69.37           H  
ATOM   5214 HE22 GLN A 342      -4.203 -63.964  33.183  1.00 69.37           H  
ATOM   5215  N   LEU A 343     -10.623 -63.864  36.965  1.00 63.40           N  
ANISOU 5215  N   LEU A 343     9144   8040   6907     68  -1307    663       N  
ATOM   5216  CA  LEU A 343     -11.831 -63.118  37.328  1.00 53.97           C  
ANISOU 5216  CA  LEU A 343     8103   6847   5557    165  -1225    600       C  
ATOM   5217  C   LEU A 343     -13.082 -64.000  37.232  1.00 56.90           C  
ANISOU 5217  C   LEU A 343     8402   7285   5932    261  -1069    658       C  
ATOM   5218  O   LEU A 343     -13.930 -63.797  36.363  1.00 64.51           O  
ANISOU 5218  O   LEU A 343     9336   8233   6942    306   -960    631       O  
ATOM   5219  CB  LEU A 343     -11.981 -61.858  36.460  1.00 60.17           C  
ANISOU 5219  CB  LEU A 343     8960   7547   6354    152  -1215    501       C  
ATOM   5220  CG  LEU A 343     -11.257 -60.600  36.958  1.00 75.31           C  
ANISOU 5220  CG  LEU A 343    11047   9394   8174     94  -1356    422       C  
ATOM   5221  CD1 LEU A 343      -9.905 -60.417  36.270  1.00 76.54           C  
ANISOU 5221  CD1 LEU A 343    11111   9498   8471    -44  -1472    430       C  
ATOM   5222  CD2 LEU A 343     -12.139 -59.377  36.793  1.00 73.28           C  
ANISOU 5222  CD2 LEU A 343    10952   9078   7813    164  -1306    321       C  
ATOM   5223  H   LEU A 343     -10.744 -64.448  36.345  1.00 76.09           H  
ATOM   5224  HA  LEU A 343     -11.748 -62.829  38.250  1.00 64.77           H  
ATOM   5225  HB2 LEU A 343     -11.638 -62.056  35.575  1.00 72.20           H  
ATOM   5226  HB3 LEU A 343     -12.925 -61.642  36.398  1.00 72.20           H  
ATOM   5227  HG  LEU A 343     -11.085 -60.705  37.907  1.00 90.37           H  
ATOM   5228 HD11 LEU A 343     -10.047 -60.334  35.314  1.00 91.84           H  
ATOM   5229 HD12 LEU A 343      -9.483 -59.614  36.612  1.00 91.84           H  
ATOM   5230 HD13 LEU A 343      -9.348 -61.189  36.456  1.00 91.84           H  
ATOM   5231 HD21 LEU A 343     -12.952 -59.502  37.308  1.00 87.94           H  
ATOM   5232 HD22 LEU A 343     -11.660 -58.597  37.115  1.00 87.94           H  
ATOM   5233 HD23 LEU A 343     -12.356 -59.269  35.854  1.00 87.94           H  
ATOM   5234  N   PRO A 344     -13.195 -64.994  38.132  1.00 44.69           N  
ANISOU 5234  N   PRO A 344     6827   5815   4340    288  -1066    745       N  
ATOM   5235  CA  PRO A 344     -14.337 -65.920  38.117  1.00 45.69           C  
ANISOU 5235  CA  PRO A 344     6877   6009   4475    365   -931    818       C  
ATOM   5236  C   PRO A 344     -15.686 -65.257  38.416  1.00 39.93           C  
ANISOU 5236  C   PRO A 344     6259   5312   3599    476   -817    776       C  
ATOM   5237  O   PRO A 344     -16.711 -65.760  37.958  1.00 52.65           O  
ANISOU 5237  O   PRO A 344     7789   6960   5254    530   -692    818       O  
ATOM   5238  CB  PRO A 344     -13.986 -66.937  39.215  1.00 51.65           C  
ANISOU 5238  CB  PRO A 344     7609   6832   5185    358   -984    918       C  
ATOM   5239  CG  PRO A 344     -12.519 -66.794  39.427  1.00 51.96           C  
ANISOU 5239  CG  PRO A 344     7650   6830   5263    263  -1145    908       C  
ATOM   5240  CD  PRO A 344     -12.204 -65.368  39.157  1.00 48.25           C  
ANISOU 5240  CD  PRO A 344     7300   6290   4744    237  -1198    791       C  
ATOM   5241  HA  PRO A 344     -14.388 -66.377  37.263  1.00 54.83           H  
ATOM   5242  HB2 PRO A 344     -14.473 -66.723  40.026  1.00 61.98           H  
ATOM   5243  HB3 PRO A 344     -14.203 -67.833  38.911  1.00 61.98           H  
ATOM   5244  HG2 PRO A 344     -12.300 -67.023  40.344  1.00 62.35           H  
ATOM   5245  HG3 PRO A 344     -12.044 -67.370  38.809  1.00 62.35           H  
ATOM   5246  HD2 PRO A 344     -12.328 -64.835  39.958  1.00 57.90           H  
ATOM   5247  HD3 PRO A 344     -11.304 -65.280  38.806  1.00 57.90           H  
ATOM   5248  N   GLU A 345     -15.687 -64.154  39.162  1.00 54.21           N  
ANISOU 5248  N   GLU A 345     8252   7106   5240    510   -860    694       N  
ATOM   5249  CA  GLU A 345     -16.934 -63.465  39.494  1.00 64.94           C  
ANISOU 5249  CA  GLU A 345     9726   8496   6450    631   -751    647       C  
ATOM   5250  C   GLU A 345     -17.572 -62.937  38.215  1.00 60.10           C  
ANISOU 5250  C   GLU A 345     9067   7831   5938    654   -665    595       C  
ATOM   5251  O   GLU A 345     -18.794 -62.963  38.063  1.00 65.11           O  
ANISOU 5251  O   GLU A 345     9684   8513   6541    748   -533    610       O  
ATOM   5252  CB  GLU A 345     -16.711 -62.292  40.464  1.00 66.52           C  
ANISOU 5252  CB  GLU A 345    10152   8669   6452    666   -829    552       C  
ATOM   5253  CG  GLU A 345     -15.509 -62.409  41.394  1.00 74.58           C  
ANISOU 5253  CG  GLU A 345    11238   9685   7414    586   -989    564       C  
ATOM   5254  CD  GLU A 345     -14.231 -61.896  40.757  1.00 79.01           C  
ANISOU 5254  CD  GLU A 345    11786  10143   8091    460  -1132    515       C  
ATOM   5255  OE1 GLU A 345     -14.118 -60.670  40.547  1.00 83.40           O  
ANISOU 5255  OE1 GLU A 345    12474  10615   8598    456  -1178    409       O  
ATOM   5256  OE2 GLU A 345     -13.340 -62.718  40.465  1.00 75.01           O  
ANISOU 5256  OE2 GLU A 345    11135   9638   7725    367  -1198    586       O  
ATOM   5257  H   GLU A 345     -14.982 -63.785  39.488  1.00 65.05           H  
ATOM   5258  HA  GLU A 345     -17.549 -64.091  39.908  1.00 77.92           H  
ATOM   5259  HB2 GLU A 345     -16.594 -61.483  39.942  1.00 79.82           H  
ATOM   5260  HB3 GLU A 345     -17.500 -62.203  41.021  1.00 79.82           H  
ATOM   5261  HG2 GLU A 345     -15.676 -61.889  42.195  1.00 89.50           H  
ATOM   5262  HG3 GLU A 345     -15.377 -63.342  41.625  1.00 89.50           H  
ATOM   5263  N   LYS A 346     -16.729 -62.476  37.293  1.00 84.54           N  
ANISOU 5263  N   LYS A 346    12135  10832   9153    564   -741    543       N  
ATOM   5264  CA  LYS A 346     -17.187 -61.839  36.062  1.00 85.84           C  
ANISOU 5264  CA  LYS A 346    12274  10935   9405    573   -681    486       C  
ATOM   5265  C   LYS A 346     -17.516 -62.854  34.958  1.00 84.22           C  
ANISOU 5265  C   LYS A 346    11872  10749   9379    549   -599    558       C  
ATOM   5266  O   LYS A 346     -18.051 -62.481  33.916  1.00 85.90           O  
ANISOU 5266  O   LYS A 346    12050  10923   9663    563   -535    526       O  
ATOM   5267  CB  LYS A 346     -16.133 -60.850  35.539  1.00 80.42           C  
ANISOU 5267  CB  LYS A 346    11652  10141   8764    480   -800    404       C  
ATOM   5268  CG  LYS A 346     -15.948 -59.596  36.388  1.00 81.81           C  
ANISOU 5268  CG  LYS A 346    12047  10267   8769    505   -883    310       C  
ATOM   5269  CD  LYS A 346     -15.107 -58.556  35.666  1.00 81.74           C  
ANISOU 5269  CD  LYS A 346    12092  10143   8821    411   -987    235       C  
ATOM   5270  CE  LYS A 346     -14.620 -57.472  36.625  1.00 83.30           C  
ANISOU 5270  CE  LYS A 346    12508  10280   8861    403  -1113    153       C  
ATOM   5271  NZ  LYS A 346     -13.497 -56.683  36.055  1.00 83.39           N  
ANISOU 5271  NZ  LYS A 346    12545  10188   8950    272  -1250    110       N  
ATOM   5272  H   LYS A 346     -15.873 -62.520  37.361  1.00101.44           H  
ATOM   5273  HA  LYS A 346     -17.995 -61.338  36.253  1.00103.01           H  
ATOM   5274  HB2 LYS A 346     -15.277 -61.304  35.499  1.00 96.51           H  
ATOM   5275  HB3 LYS A 346     -16.392 -60.565  34.649  1.00 96.51           H  
ATOM   5276  HG2 LYS A 346     -16.816 -59.207  36.578  1.00 98.17           H  
ATOM   5277  HG3 LYS A 346     -15.498 -59.831  37.214  1.00 98.17           H  
ATOM   5278  HD2 LYS A 346     -14.332 -58.987  35.274  1.00 98.08           H  
ATOM   5279  HD3 LYS A 346     -15.642 -58.134  34.976  1.00 98.08           H  
ATOM   5280  HE2 LYS A 346     -15.351 -56.863  36.815  1.00 99.95           H  
ATOM   5281  HE3 LYS A 346     -14.310 -57.888  37.445  1.00 99.95           H  
ATOM   5282  HZ1 LYS A 346     -13.757 -56.285  35.302  1.00100.06           H  
ATOM   5283  HZ2 LYS A 346     -13.236 -56.061  36.636  1.00100.06           H  
ATOM   5284  HZ3 LYS A 346     -12.809 -57.218  35.876  1.00100.06           H  
ATOM   5285  N   TYR A 347     -17.193 -64.127  35.173  1.00 36.91           N  
ANISOU 5285  N   TYR A 347     5759   4808   3458    512   -607    654       N  
ATOM   5286  CA  TYR A 347     -17.363 -65.136  34.123  1.00 35.33           C  
ANISOU 5286  CA  TYR A 347     5383   4611   3432    481   -550    717       C  
ATOM   5287  C   TYR A 347     -18.817 -65.293  33.667  1.00 38.07           C  
ANISOU 5287  C   TYR A 347     5688   4995   3782    562   -412    741       C  
ATOM   5288  O   TYR A 347     -19.111 -65.187  32.476  1.00 41.19           O  
ANISOU 5288  O   TYR A 347     6018   5348   4285    548   -367    719       O  
ATOM   5289  CB  TYR A 347     -16.822 -66.501  34.563  1.00 30.32           C  
ANISOU 5289  CB  TYR A 347     4642   4019   2860    440   -587    819       C  
ATOM   5290  CG  TYR A 347     -16.763 -67.508  33.429  1.00 27.16           C  
ANISOU 5290  CG  TYR A 347     4076   3598   2647    399   -553    868       C  
ATOM   5291  CD1 TYR A 347     -17.895 -68.215  33.036  1.00 26.67           C  
ANISOU 5291  CD1 TYR A 347     3935   3570   2627    443   -447    926       C  
ATOM   5292  CD2 TYR A 347     -15.579 -67.748  32.746  1.00 27.49           C  
ANISOU 5292  CD2 TYR A 347     4040   3587   2819    318   -628    858       C  
ATOM   5293  CE1 TYR A 347     -17.847 -69.124  31.999  1.00 25.74           C  
ANISOU 5293  CE1 TYR A 347     3684   3423   2672    406   -425    964       C  
ATOM   5294  CE2 TYR A 347     -15.525 -68.664  31.701  1.00 25.78           C  
ANISOU 5294  CE2 TYR A 347     3685   3349   2763    291   -593    895       C  
ATOM   5295  CZ  TYR A 347     -16.666 -69.348  31.336  1.00 27.39           C  
ANISOU 5295  CZ  TYR A 347     3831   3576   3001    335   -495    944       C  
ATOM   5296  OH  TYR A 347     -16.647 -70.265  30.306  1.00 30.67           O  
ANISOU 5296  OH  TYR A 347     4126   3961   3568    310   -468    974       O  
ATOM   5297  H   TYR A 347     -16.876 -64.433  35.912  1.00 44.30           H  
ATOM   5298  HA  TYR A 347     -16.848 -64.858  33.349  1.00 42.40           H  
ATOM   5299  HB2 TYR A 347     -15.923 -66.387  34.909  1.00 36.39           H  
ATOM   5300  HB3 TYR A 347     -17.400 -66.861  35.254  1.00 36.39           H  
ATOM   5301  HD1 TYR A 347     -18.700 -68.068  33.478  1.00 32.00           H  
ATOM   5302  HD2 TYR A 347     -14.809 -67.287  32.989  1.00 32.99           H  
ATOM   5303  HE1 TYR A 347     -18.614 -69.588  31.751  1.00 30.89           H  
ATOM   5304  HE2 TYR A 347     -14.725 -68.816  31.253  1.00 30.94           H  
ATOM   5305  HH  TYR A 347     -15.874 -70.315  29.981  1.00 36.81           H  
ATOM   5306  N   LYS A 348     -19.712 -65.570  34.612  1.00 47.13           N  
ANISOU 5306  N   LYS A 348     6869   6227   4813    643   -345    792       N  
ATOM   5307  CA  LYS A 348     -21.130 -65.748  34.306  1.00 44.24           C  
ANISOU 5307  CA  LYS A 348     6451   5913   4444    721   -215    832       C  
ATOM   5308  C   LYS A 348     -21.646 -64.508  33.592  1.00 38.90           C  
ANISOU 5308  C   LYS A 348     5846   5186   3750    767   -175    735       C  
ATOM   5309  O   LYS A 348     -22.344 -64.588  32.581  1.00 38.11           O  
ANISOU 5309  O   LYS A 348     5664   5073   3743    777   -107    744       O  
ATOM   5310  CB  LYS A 348     -21.926 -65.967  35.595  1.00 41.33           C  
ANISOU 5310  CB  LYS A 348     6134   5653   3918    808   -153    892       C  
ATOM   5311  CG  LYS A 348     -23.205 -66.781  35.424  1.00 38.21           C  
ANISOU 5311  CG  LYS A 348     5621   5338   3557    855    -33    995       C  
ATOM   5312  CD  LYS A 348     -24.225 -66.459  36.510  1.00 44.67           C  
ANISOU 5312  CD  LYS A 348     6514   6264   4194    972     58   1022       C  
ATOM   5313  CE  LYS A 348     -23.806 -67.006  37.862  1.00 58.69           C  
ANISOU 5313  CE  LYS A 348     8338   8109   5853    969     19   1084       C  
ATOM   5314  NZ  LYS A 348     -24.310 -66.161  38.980  1.00 52.27           N  
ANISOU 5314  NZ  LYS A 348     7675   7364   4819   1084     67   1045       N  
ATOM   5315  H   LYS A 348     -19.522 -65.659  35.446  1.00 56.56           H  
ATOM   5316  HA  LYS A 348     -21.249 -66.518  33.727  1.00 53.09           H  
ATOM   5317  HB2 LYS A 348     -21.363 -66.436  36.231  1.00 49.60           H  
ATOM   5318  HB3 LYS A 348     -22.176 -65.102  35.956  1.00 49.60           H  
ATOM   5319  HG2 LYS A 348     -23.602 -66.576  34.564  1.00 45.85           H  
ATOM   5320  HG3 LYS A 348     -22.992 -67.726  35.478  1.00 45.85           H  
ATOM   5321  HD2 LYS A 348     -24.315 -65.496  36.588  1.00 53.61           H  
ATOM   5322  HD3 LYS A 348     -25.078 -66.856  36.274  1.00 53.61           H  
ATOM   5323  HE2 LYS A 348     -24.167 -67.900  37.971  1.00 70.43           H  
ATOM   5324  HE3 LYS A 348     -22.837 -67.028  37.911  1.00 70.43           H  
ATOM   5325  HZ1 LYS A 348     -25.199 -66.128  38.960  1.00 62.72           H  
ATOM   5326  HZ2 LYS A 348     -24.051 -66.503  39.760  1.00 62.72           H  
ATOM   5327  HZ3 LYS A 348     -23.988 -65.334  38.905  1.00 62.72           H  
ATOM   5328  N   GLU A 349     -21.285 -63.357  34.142  1.00 34.94           N  
ANISOU 5328  N   GLU A 349     5505   4648   3125    795   -227    644       N  
ATOM   5329  CA  GLU A 349     -21.611 -62.065  33.559  1.00 42.41           C  
ANISOU 5329  CA  GLU A 349     6545   5525   4044    835   -214    543       C  
ATOM   5330  C   GLU A 349     -21.214 -61.958  32.087  1.00 43.21           C  
ANISOU 5330  C   GLU A 349     6563   5542   4312    753   -236    517       C  
ATOM   5331  O   GLU A 349     -22.055 -61.730  31.217  1.00 36.32           O  
ANISOU 5331  O   GLU A 349     5648   4659   3492    790   -161    510       O  
ATOM   5332  CB  GLU A 349     -20.906 -60.974  34.363  1.00 50.29           C  
ANISOU 5332  CB  GLU A 349     7731   6472   4906    840   -310    450       C  
ATOM   5333  CG  GLU A 349     -21.023 -59.604  33.776  1.00 60.80           C  
ANISOU 5333  CG  GLU A 349     9176   7709   6217    865   -325    343       C  
ATOM   5334  CD  GLU A 349     -20.586 -58.527  34.742  1.00 66.72           C  
ANISOU 5334  CD  GLU A 349    10136   8412   6803    894   -409    252       C  
ATOM   5335  OE1 GLU A 349     -19.423 -58.573  35.185  1.00 71.55           O  
ANISOU 5335  OE1 GLU A 349    10785   8992   7407    802   -532    244       O  
ATOM   5336  OE2 GLU A 349     -21.411 -57.645  35.063  1.00 60.38           O  
ANISOU 5336  OE2 GLU A 349     9461   7602   5879   1013   -356    191       O  
ATOM   5337  H   GLU A 349     -20.838 -63.298  34.874  1.00 41.93           H  
ATOM   5338  HA  GLU A 349     -22.567 -61.919  33.625  1.00 50.89           H  
ATOM   5339  HB2 GLU A 349     -21.290 -60.946  35.253  1.00 60.35           H  
ATOM   5340  HB3 GLU A 349     -19.962 -61.190  34.420  1.00 60.35           H  
ATOM   5341  HG2 GLU A 349     -20.461 -59.548  32.988  1.00 72.96           H  
ATOM   5342  HG3 GLU A 349     -21.948 -59.439  33.538  1.00 72.96           H  
ATOM   5343  N   ILE A 350     -19.924 -62.121  31.824  1.00 32.23           N  
ANISOU 5343  N   ILE A 350     5147   4099   3001    642   -340    505       N  
ATOM   5344  CA  ILE A 350     -19.370 -61.936  30.488  1.00 26.23           C  
ANISOU 5344  CA  ILE A 350     4320   3262   2384    559   -369    476       C  
ATOM   5345  C   ILE A 350     -19.939 -62.900  29.442  1.00 29.87           C  
ANISOU 5345  C   ILE A 350     4621   3744   2983    549   -289    538       C  
ATOM   5346  O   ILE A 350     -20.257 -62.482  28.330  1.00 32.09           O  
ANISOU 5346  O   ILE A 350     4879   3979   3333    541   -257    506       O  
ATOM   5347  CB  ILE A 350     -17.823 -62.052  30.529  1.00 26.27           C  
ANISOU 5347  CB  ILE A 350     4310   3227   2445    445   -492    468       C  
ATOM   5348  CG1 ILE A 350     -17.237 -60.907  31.361  1.00 27.39           C  
ANISOU 5348  CG1 ILE A 350     4623   3324   2459    438   -589    395       C  
ATOM   5349  CG2 ILE A 350     -17.221 -62.019  29.125  1.00 25.29           C  
ANISOU 5349  CG2 ILE A 350     4095   3041   2472    360   -508    453       C  
ATOM   5350  CD1 ILE A 350     -15.768 -61.072  31.702  1.00 27.75           C  
ANISOU 5350  CD1 ILE A 350     4655   3350   2538    331   -719    404       C  
ATOM   5351  H   ILE A 350     -19.338 -62.344  32.412  1.00 38.68           H  
ATOM   5352  HA  ILE A 350     -19.584 -61.037  30.194  1.00 31.48           H  
ATOM   5353  HB  ILE A 350     -17.586 -62.894  30.948  1.00 31.52           H  
ATOM   5354 HG12 ILE A 350     -17.333 -60.080  30.864  1.00 32.86           H  
ATOM   5355 HG13 ILE A 350     -17.728 -60.847  32.195  1.00 32.86           H  
ATOM   5356 HG21 ILE A 350     -17.459 -61.180  28.700  1.00 30.34           H  
ATOM   5357 HG22 ILE A 350     -16.256 -62.093  29.194  1.00 30.34           H  
ATOM   5358 HG23 ILE A 350     -17.575 -62.762  28.612  1.00 30.34           H  
ATOM   5359 HD11 ILE A 350     -15.257 -61.121  30.879  1.00 33.30           H  
ATOM   5360 HD12 ILE A 350     -15.479 -60.309  32.227  1.00 33.30           H  
ATOM   5361 HD13 ILE A 350     -15.652 -61.888  32.213  1.00 33.30           H  
ATOM   5362  N   PHE A 351     -20.085 -64.173  29.801  1.00 38.03           N  
ANISOU 5362  N   PHE A 351     5553   4842   4053    548   -263    628       N  
ATOM   5363  CA  PHE A 351     -20.327 -65.219  28.809  1.00 28.95           C  
ANISOU 5363  CA  PHE A 351     4256   3695   3050    513   -220    686       C  
ATOM   5364  C   PHE A 351     -21.747 -65.778  28.774  1.00 32.09           C  
ANISOU 5364  C   PHE A 351     4594   4155   3445    582   -116    753       C  
ATOM   5365  O   PHE A 351     -22.056 -66.591  27.902  1.00 31.37           O  
ANISOU 5365  O   PHE A 351     4391   4057   3471    553    -84    798       O  
ATOM   5366  CB  PHE A 351     -19.345 -66.371  29.029  1.00 23.97           C  
ANISOU 5366  CB  PHE A 351     3537   3072   2498    447   -280    745       C  
ATOM   5367  CG  PHE A 351     -17.908 -65.984  28.836  1.00 25.38           C  
ANISOU 5367  CG  PHE A 351     3732   3195   2716    368   -380    695       C  
ATOM   5368  CD1 PHE A 351     -17.420 -65.700  27.568  1.00 23.22           C  
ANISOU 5368  CD1 PHE A 351     3414   2861   2548    312   -388    652       C  
ATOM   5369  CD2 PHE A 351     -17.041 -65.911  29.918  1.00 24.80           C  
ANISOU 5369  CD2 PHE A 351     3714   3136   2573    346   -466    699       C  
ATOM   5370  CE1 PHE A 351     -16.095 -65.343  27.383  1.00 23.34           C  
ANISOU 5370  CE1 PHE A 351     3429   2836   2603    236   -475    618       C  
ATOM   5371  CE2 PHE A 351     -15.715 -65.555  29.738  1.00 24.91           C  
ANISOU 5371  CE2 PHE A 351     3729   3105   2630    267   -563    664       C  
ATOM   5372  CZ  PHE A 351     -15.244 -65.271  28.470  1.00 25.34           C  
ANISOU 5372  CZ  PHE A 351     3728   3105   2794    212   -565    626       C  
ATOM   5373  H   PHE A 351     -20.049 -64.458  30.612  1.00 45.63           H  
ATOM   5374  HA  PHE A 351     -20.144 -64.849  27.931  1.00 34.74           H  
ATOM   5375  HB2 PHE A 351     -19.445 -66.698  29.936  1.00 28.76           H  
ATOM   5376  HB3 PHE A 351     -19.548 -67.080  28.399  1.00 28.76           H  
ATOM   5377  HD1 PHE A 351     -17.990 -65.746  26.834  1.00 27.87           H  
ATOM   5378  HD2 PHE A 351     -17.355 -66.100  30.773  1.00 29.76           H  
ATOM   5379  HE1 PHE A 351     -15.779 -65.153  26.530  1.00 28.01           H  
ATOM   5380  HE2 PHE A 351     -15.143 -65.507  30.469  1.00 29.89           H  
ATOM   5381  HZ  PHE A 351     -14.353 -65.033  28.348  1.00 30.40           H  
ATOM   5382  N   PHE A 352     -22.609 -65.360  29.701  1.00 40.12           N  
ANISOU 5382  N   PHE A 352     5682   5233   4328    672    -64    763       N  
ATOM   5383  CA  PHE A 352     -23.963 -65.914  29.752  1.00 39.74           C  
ANISOU 5383  CA  PHE A 352     5563   5261   4277    735     37    843       C  
ATOM   5384  C   PHE A 352     -25.122 -64.924  29.873  1.00 38.04           C  
ANISOU 5384  C   PHE A 352     5413   5077   3962    843    119    812       C  
ATOM   5385  O   PHE A 352     -26.220 -65.225  29.410  1.00 42.03           O  
ANISOU 5385  O   PHE A 352     5836   5623   4509    878    197    866       O  
ATOM   5386  CB  PHE A 352     -24.070 -66.915  30.904  1.00 46.19           C  
ANISOU 5386  CB  PHE A 352     6346   6162   5041    746     46    942       C  
ATOM   5387  CG  PHE A 352     -23.180 -68.118  30.753  1.00 41.69           C  
ANISOU 5387  CG  PHE A 352     5687   5568   4585    654    -20    997       C  
ATOM   5388  CD1 PHE A 352     -23.574 -69.198  29.983  1.00 47.27           C  
ANISOU 5388  CD1 PHE A 352     6265   6269   5425    615      5   1070       C  
ATOM   5389  CD2 PHE A 352     -21.955 -68.172  31.389  1.00 42.38           C  
ANISOU 5389  CD2 PHE A 352     5820   5634   4646    611   -113    978       C  
ATOM   5390  CE1 PHE A 352     -22.755 -70.304  29.847  1.00 43.19           C  
ANISOU 5390  CE1 PHE A 352     5676   5722   5012    543    -57   1116       C  
ATOM   5391  CE2 PHE A 352     -21.139 -69.274  31.254  1.00 45.13           C  
ANISOU 5391  CE2 PHE A 352     6083   5961   5103    539   -173   1031       C  
ATOM   5392  CZ  PHE A 352     -21.537 -70.341  30.484  1.00 44.80           C  
ANISOU 5392  CZ  PHE A 352     5921   5909   5192    510   -142   1097       C  
ATOM   5393  H   PHE A 352     -22.440 -64.767  30.301  1.00 48.14           H  
ATOM   5394  HA  PHE A 352     -24.108 -66.412  28.932  1.00 47.69           H  
ATOM   5395  HB2 PHE A 352     -23.826 -66.468  31.730  1.00 55.43           H  
ATOM   5396  HB3 PHE A 352     -24.986 -67.230  30.960  1.00 55.43           H  
ATOM   5397  HD1 PHE A 352     -24.396 -69.178  29.549  1.00 56.72           H  
ATOM   5398  HD2 PHE A 352     -21.676 -67.455  31.911  1.00 50.85           H  
ATOM   5399  HE1 PHE A 352     -23.029 -71.024  29.325  1.00 51.83           H  
ATOM   5400  HE2 PHE A 352     -20.316 -69.296  31.686  1.00 54.16           H  
ATOM   5401  HZ  PHE A 352     -20.985 -71.084  30.394  1.00 53.76           H  
ATOM   5402  N   ASP A 353     -24.906 -63.762  30.482  1.00 63.46           N  
ANISOU 5402  N   ASP A 353     8780   8278   7055    897     97    727       N  
ATOM   5403  CA  ASP A 353     -26.042 -62.948  30.911  1.00 71.80           C  
ANISOU 5403  CA  ASP A 353     9907   9383   7992   1025    182    708       C  
ATOM   5404  C   ASP A 353     -26.932 -62.451  29.775  1.00 76.48           C  
ANISOU 5404  C   ASP A 353    10457   9947   8654   1060    241    690       C  
ATOM   5405  O   ASP A 353     -28.160 -62.512  29.878  1.00 85.25           O  
ANISOU 5405  O   ASP A 353    11519  11135   9737   1148    338    743       O  
ATOM   5406  CB  ASP A 353     -25.591 -61.764  31.753  1.00 64.36           C  
ANISOU 5406  CB  ASP A 353     9150   8406   6896   1079    137    608       C  
ATOM   5407  CG  ASP A 353     -26.759 -61.077  32.432  1.00 71.73           C  
ANISOU 5407  CG  ASP A 353    10161   9406   7685   1232    234    596       C  
ATOM   5408  OD1 ASP A 353     -27.832 -61.702  32.549  1.00 79.63           O  
ANISOU 5408  OD1 ASP A 353    11058  10509   8690   1291    337    688       O  
ATOM   5409  OD2 ASP A 353     -26.621 -59.917  32.848  1.00 83.24           O  
ANISOU 5409  OD2 ASP A 353    11783  10817   9028   1297    208    498       O  
ATOM   5410  H   ASP A 353     -24.133 -63.428  30.656  1.00 76.15           H  
ATOM   5411  HA  ASP A 353     -26.600 -63.500  31.481  1.00 86.16           H  
ATOM   5412  HB2 ASP A 353     -24.982 -62.075  32.440  1.00 77.23           H  
ATOM   5413  HB3 ASP A 353     -25.149 -61.116  31.182  1.00 77.23           H  
ATOM   5414  N   GLN A 354     -26.314 -61.924  28.721  1.00 47.29           N  
ANISOU 5414  N   GLN A 354     6778   6145   5043    993    181    620       N  
ATOM   5415  CA  GLN A 354     -27.016 -61.600  27.477  1.00 52.07           C  
ANISOU 5415  CA  GLN A 354     7330   6715   5737   1000    220    611       C  
ATOM   5416  C   GLN A 354     -27.741 -60.257  27.553  1.00 54.55           C  
ANISOU 5416  C   GLN A 354     7758   7011   5957   1115    258    543       C  
ATOM   5417  O   GLN A 354     -28.058 -59.664  26.522  1.00 61.97           O  
ANISOU 5417  O   GLN A 354     8696   7892   6957   1116    262    509       O  
ATOM   5418  CB  GLN A 354     -28.001 -62.721  27.115  1.00 49.37           C  
ANISOU 5418  CB  GLN A 354     6829   6452   5479   1002    293    724       C  
ATOM   5419  CG  GLN A 354     -28.200 -62.979  25.631  1.00 57.63           C  
ANISOU 5419  CG  GLN A 354     7780   7446   6669    937    289    733       C  
ATOM   5420  CD  GLN A 354     -28.678 -64.396  25.377  1.00 58.76           C  
ANISOU 5420  CD  GLN A 354     7772   7644   6909    890    316    845       C  
ATOM   5421  OE1 GLN A 354     -29.853 -64.628  25.091  1.00 62.72           O  
ANISOU 5421  OE1 GLN A 354     8194   8200   7437    931    381    910       O  
ATOM   5422  NE2 GLN A 354     -27.767 -65.356  25.504  1.00 54.19           N  
ANISOU 5422  NE2 GLN A 354     7153   7050   6385    804    262    871       N  
ATOM   5423  H   GLN A 354     -25.473 -61.741  28.700  1.00 56.74           H  
ATOM   5424  HA  GLN A 354     -26.364 -61.540  26.761  1.00 62.48           H  
ATOM   5425  HB2 GLN A 354     -27.682 -63.547  27.511  1.00 59.25           H  
ATOM   5426  HB3 GLN A 354     -28.868 -62.498  27.488  1.00 59.25           H  
ATOM   5427  HG2 GLN A 354     -28.868 -62.366  25.286  1.00 69.15           H  
ATOM   5428  HG3 GLN A 354     -27.358 -62.854  25.168  1.00 69.15           H  
ATOM   5429 HE21 GLN A 354     -26.959 -65.157  25.719  1.00 65.02           H  
ATOM   5430 HE22 GLN A 354     -27.987 -66.177  25.370  1.00 65.02           H  
ATOM   5431  N   SER A 355     -27.997 -59.778  28.766  1.00 43.11           N  
ANISOU 5431  N   SER A 355     6414   5608   4356   1217    285    521       N  
ATOM   5432  CA  SER A 355     -28.598 -58.462  28.949  1.00 40.27           C  
ANISOU 5432  CA  SER A 355     6185   5221   3894   1340    315    444       C  
ATOM   5433  C   SER A 355     -27.519 -57.437  29.277  1.00 38.25           C  
ANISOU 5433  C   SER A 355     6110   4858   3565   1313    211    330       C  
ATOM   5434  O   SER A 355     -27.809 -56.264  29.512  1.00 46.17           O  
ANISOU 5434  O   SER A 355     7257   5812   4472   1408    212    249       O  
ATOM   5435  CB  SER A 355     -29.633 -58.492  30.068  1.00 37.35           C  
ANISOU 5435  CB  SER A 355     5830   4970   3389   1487    419    485       C  
ATOM   5436  OG  SER A 355     -29.002 -58.506  31.337  1.00 43.13           O  
ANISOU 5436  OG  SER A 355     6669   5728   3990   1500    384    462       O  
ATOM   5437  H   SER A 355     -27.832 -60.195  29.500  1.00 51.73           H  
ATOM   5438  HA  SER A 355     -29.040 -58.191  28.129  1.00 48.32           H  
ATOM   5439  HB2 SER A 355     -30.194 -57.703  30.002  1.00 44.82           H  
ATOM   5440  HB3 SER A 355     -30.175 -59.292  29.976  1.00 44.82           H  
ATOM   5441  HG  SER A 355     -29.581 -58.523  31.946  1.00 51.75           H  
ATOM   5442  N   LYS A 356     -26.272 -57.895  29.293  1.00 57.74           N  
ANISOU 5442  N   LYS A 356     8569   7287   6080   1183    117    327       N  
ATOM   5443  CA  LYS A 356     -25.131 -57.028  29.528  1.00 58.58           C  
ANISOU 5443  CA  LYS A 356     8825   7293   6139   1127      1    234       C  
ATOM   5444  C   LYS A 356     -24.340 -56.909  28.231  1.00 52.00           C  
ANISOU 5444  C   LYS A 356     7942   6365   5451    997    -69    214       C  
ATOM   5445  O   LYS A 356     -24.673 -57.560  27.246  1.00 62.84           O  
ANISOU 5445  O   LYS A 356     9173   7757   6947    958    -25    269       O  
ATOM   5446  CB  LYS A 356     -24.262 -57.605  30.636  1.00 61.06           C  
ANISOU 5446  CB  LYS A 356     9166   7645   6389   1080    -59    252       C  
ATOM   5447  CG  LYS A 356     -24.898 -57.591  32.014  1.00 73.55           C  
ANISOU 5447  CG  LYS A 356    10830   9316   7800   1205     -2    261       C  
ATOM   5448  CD  LYS A 356     -24.048 -58.438  32.919  1.00 86.24           C  
ANISOU 5448  CD  LYS A 356    12421  10970   9375   1137    -61    307       C  
ATOM   5449  CE  LYS A 356     -24.526 -58.512  34.363  1.00 89.88           C  
ANISOU 5449  CE  LYS A 356    12968  11527   9656   1246    -14    323       C  
ATOM   5450  NZ  LYS A 356     -24.205 -57.296  35.144  1.00 88.41           N  
ANISOU 5450  NZ  LYS A 356    13006  11278   9308   1304    -79    210       N  
ATOM   5451  H   LYS A 356     -26.060 -58.719  29.168  1.00 69.28           H  
ATOM   5452  HA  LYS A 356     -25.435 -56.146  29.793  1.00 70.30           H  
ATOM   5453  HB2 LYS A 356     -24.055 -58.527  30.417  1.00 73.27           H  
ATOM   5454  HB3 LYS A 356     -23.442 -57.090  30.686  1.00 73.27           H  
ATOM   5455  HG2 LYS A 356     -24.921 -56.685  32.359  1.00 88.26           H  
ATOM   5456  HG3 LYS A 356     -25.790 -57.971  31.972  1.00 88.26           H  
ATOM   5457  HD2 LYS A 356     -24.031 -59.343  32.570  1.00103.48           H  
ATOM   5458  HD3 LYS A 356     -23.148 -58.075  32.927  1.00103.48           H  
ATOM   5459  HE2 LYS A 356     -25.489 -58.627  34.371  1.00107.86           H  
ATOM   5460  HE3 LYS A 356     -24.099 -59.268  34.797  1.00107.86           H  
ATOM   5461  HZ1 LYS A 356     -24.591 -56.585  34.773  1.00106.09           H  
ATOM   5462  HZ2 LYS A 356     -24.501 -57.383  35.979  1.00106.09           H  
ATOM   5463  HZ3 LYS A 356     -23.324 -57.169  35.162  1.00106.09           H  
ATOM   5464  N   ASN A 357     -23.303 -56.077  28.226  1.00 27.28           N  
ANISOU 5464  N   ASN A 357     4928   3136   2302    927   -178    140       N  
ATOM   5465  CA  ASN A 357     -22.520 -55.833  27.014  1.00 30.95           C  
ANISOU 5465  CA  ASN A 357     5354   3515   2891    804   -242    122       C  
ATOM   5466  C   ASN A 357     -21.263 -56.702  26.904  1.00 30.46           C  
ANISOU 5466  C   ASN A 357     5195   3463   2917    668   -310    162       C  
ATOM   5467  O   ASN A 357     -20.273 -56.306  26.292  1.00 32.11           O  
ANISOU 5467  O   ASN A 357     5412   3600   3189    560   -391    134       O  
ATOM   5468  CB  ASN A 357     -22.167 -54.346  26.914  1.00 37.03           C  
ANISOU 5468  CB  ASN A 357     6299   4165   3605    800   -322     27       C  
ATOM   5469  CG  ASN A 357     -23.373 -53.485  26.573  1.00 30.65           C  
ANISOU 5469  CG  ASN A 357     5561   3327   2757    924   -255     -9       C  
ATOM   5470  OD1 ASN A 357     -24.442 -53.996  26.237  1.00 27.07           O  
ANISOU 5470  OD1 ASN A 357     5005   2945   2336    999   -149     42       O  
ATOM   5471  ND2 ASN A 357     -23.205 -52.173  26.651  1.00 36.35           N  
ANISOU 5471  ND2 ASN A 357     6458   3940   3412    945   -322    -94       N  
ATOM   5472  H   ASN A 357     -23.029 -55.639  28.914  1.00 32.74           H  
ATOM   5473  HA  ASN A 357     -23.079 -56.045  26.249  1.00 37.14           H  
ATOM   5474  HB2 ASN A 357     -21.814 -54.046  27.766  1.00 44.43           H  
ATOM   5475  HB3 ASN A 357     -21.504 -54.223  26.217  1.00 44.43           H  
ATOM   5476 HD21 ASN A 357     -22.443 -51.850  26.884  1.00 43.62           H  
ATOM   5477 HD22 ASN A 357     -23.858 -51.644  26.468  1.00 43.62           H  
ATOM   5478  N   GLY A 358     -21.320 -57.896  27.484  1.00 34.77           N  
ANISOU 5478  N   GLY A 358     5641   4100   3469    674   -275    233       N  
ATOM   5479  CA  GLY A 358     -20.230 -58.849  27.377  1.00 29.45           C  
ANISOU 5479  CA  GLY A 358     4861   3443   2887    563   -330    279       C  
ATOM   5480  C   GLY A 358     -20.325 -59.638  26.087  1.00 29.18           C  
ANISOU 5480  C   GLY A 358     4669   3414   3003    510   -283    326       C  
ATOM   5481  O   GLY A 358     -20.970 -59.196  25.137  1.00 26.12           O  
ANISOU 5481  O   GLY A 358     4275   2994   2655    530   -238    308       O  
ATOM   5482  H   GLY A 358     -21.986 -58.178  27.949  1.00 41.72           H  
ATOM   5483  HA2 GLY A 358     -19.381 -58.379  27.394  1.00 35.34           H  
ATOM   5484  HA3 GLY A 358     -20.260 -59.467  28.124  1.00 35.34           H  
ATOM   5485  N   TYR A 359     -19.687 -60.804  26.046  1.00 28.11           N  
ANISOU 5485  N   TYR A 359     4415   3316   2952    448   -298    385       N  
ATOM   5486  CA  TYR A 359     -19.677 -61.618  24.837  1.00 22.42           C  
ANISOU 5486  CA  TYR A 359     3555   2593   2370    398   -262    422       C  
ATOM   5487  C   TYR A 359     -21.058 -62.194  24.539  1.00 22.05           C  
ANISOU 5487  C   TYR A 359     3444   2595   2341    471   -162    471       C  
ATOM   5488  O   TYR A 359     -21.460 -62.302  23.378  1.00 28.87           O  
ANISOU 5488  O   TYR A 359     4246   3435   3286    455   -125    474       O  
ATOM   5489  CB  TYR A 359     -18.656 -62.746  24.963  1.00 22.21           C  
ANISOU 5489  CB  TYR A 359     3427   2591   2422    329   -304    471       C  
ATOM   5490  CG  TYR A 359     -18.613 -63.652  23.762  1.00 21.30           C  
ANISOU 5490  CG  TYR A 359     3179   2470   2442    288   -268    504       C  
ATOM   5491  CD1 TYR A 359     -17.905 -63.292  22.624  1.00 23.52           C  
ANISOU 5491  CD1 TYR A 359     3435   2700   2801    218   -290    468       C  
ATOM   5492  CD2 TYR A 359     -19.277 -64.871  23.766  1.00 20.99           C  
ANISOU 5492  CD2 TYR A 359     3049   2477   2450    317   -214    573       C  
ATOM   5493  CE1 TYR A 359     -17.862 -64.121  21.520  1.00 20.13           C  
ANISOU 5493  CE1 TYR A 359     2898   2267   2484    188   -254    491       C  
ATOM   5494  CE2 TYR A 359     -19.242 -65.704  22.672  1.00 20.28           C  
ANISOU 5494  CE2 TYR A 359     2855   2372   2478    282   -189    595       C  
ATOM   5495  CZ  TYR A 359     -18.531 -65.325  21.550  1.00 19.85           C  
ANISOU 5495  CZ  TYR A 359     2784   2268   2490    223   -207    550       C  
ATOM   5496  OH  TYR A 359     -18.492 -66.150  20.451  1.00 20.42           O  
ANISOU 5496  OH  TYR A 359     2766   2326   2668    196   -179    565       O  
ATOM   5497  H   TYR A 359     -19.253 -61.146  26.705  1.00 33.74           H  
ATOM   5498  HA  TYR A 359     -19.417 -61.062  24.086  1.00 26.90           H  
ATOM   5499  HB2 TYR A 359     -17.774 -62.360  25.076  1.00 26.66           H  
ATOM   5500  HB3 TYR A 359     -18.881 -63.287  25.736  1.00 26.66           H  
ATOM   5501  HD1 TYR A 359     -17.454 -62.479  22.604  1.00 28.22           H  
ATOM   5502  HD2 TYR A 359     -19.756 -65.127  24.521  1.00 25.19           H  
ATOM   5503  HE1 TYR A 359     -17.385 -63.868  20.763  1.00 24.16           H  
ATOM   5504  HE2 TYR A 359     -19.692 -66.518  22.689  1.00 24.33           H  
ATOM   5505  HH  TYR A 359     -18.937 -66.847  20.599  1.00 24.51           H  
ATOM   5506  N   ALA A 360     -21.782 -62.562  25.590  1.00 27.35           N  
ANISOU 5506  N   ALA A 360     4127   3335   2932    546   -121    514       N  
ATOM   5507  CA  ALA A 360     -23.119 -63.123  25.438  1.00 23.13           C  
ANISOU 5507  CA  ALA A 360     3521   2858   2410    612    -29    575       C  
ATOM   5508  C   ALA A 360     -24.061 -62.092  24.826  1.00 22.49           C  
ANISOU 5508  C   ALA A 360     3492   2751   2303    674     19    532       C  
ATOM   5509  O   ALA A 360     -24.847 -62.405  23.931  1.00 28.22           O  
ANISOU 5509  O   ALA A 360     4138   3482   3102    680     69    564       O  
ATOM   5510  CB  ALA A 360     -23.649 -63.594  26.781  1.00 23.31           C  
ANISOU 5510  CB  ALA A 360     3553   2968   2335    681      6    632       C  
ATOM   5511  H   ALA A 360     -21.520 -62.497  26.406  1.00 32.83           H  
ATOM   5512  HA  ALA A 360     -23.079 -63.888  24.842  1.00 27.76           H  
ATOM   5513  HB1 ALA A 360     -23.685 -62.839  27.389  1.00 27.97           H  
ATOM   5514  HB2 ALA A 360     -24.538 -63.963  26.658  1.00 27.97           H  
ATOM   5515  HB3 ALA A 360     -23.054 -64.275  27.133  1.00 27.97           H  
ATOM   5516  N   GLY A 361     -23.968 -60.858  25.309  1.00 27.68           N  
ANISOU 5516  N   GLY A 361     4288   3373   2857    720     -6    459       N  
ATOM   5517  CA  GLY A 361     -24.753 -59.764  24.768  1.00 40.71           C  
ANISOU 5517  CA  GLY A 361     6005   4984   4479    785     27    411       C  
ATOM   5518  C   GLY A 361     -24.349 -59.466  23.339  1.00 36.41           C  
ANISOU 5518  C   GLY A 361     5432   4360   4042    703     -5    381       C  
ATOM   5519  O   GLY A 361     -25.181 -59.160  22.493  1.00 30.43           O  
ANISOU 5519  O   GLY A 361     4653   3590   3321    734     39    383       O  
ATOM   5520  H   GLY A 361     -23.450 -60.629  25.957  1.00 33.22           H  
ATOM   5521  HA2 GLY A 361     -25.694 -59.997  24.785  1.00 48.85           H  
ATOM   5522  HA3 GLY A 361     -24.618 -58.967  25.304  1.00 48.85           H  
ATOM   5523  N   TYR A 362     -23.049 -59.550  23.082  1.00 28.12           N  
ANISOU 5523  N   TYR A 362     4380   3264   3040    597    -81    358       N  
ATOM   5524  CA  TYR A 362     -22.498 -59.337  21.749  1.00 21.87           C  
ANISOU 5524  CA  TYR A 362     3556   2408   2347    509   -110    335       C  
ATOM   5525  C   TYR A 362     -23.047 -60.351  20.745  1.00 25.65           C  
ANISOU 5525  C   TYR A 362     3898   2915   2930    490    -54    392       C  
ATOM   5526  O   TYR A 362     -23.521 -59.973  19.674  1.00 26.90           O  
ANISOU 5526  O   TYR A 362     4049   3041   3132    486    -33    381       O  
ATOM   5527  CB  TYR A 362     -20.966 -59.397  21.807  1.00 26.52           C  
ANISOU 5527  CB  TYR A 362     4146   2964   2966    403   -194    316       C  
ATOM   5528  CG  TYR A 362     -20.263 -59.142  20.489  1.00 28.17           C  
ANISOU 5528  CG  TYR A 362     4320   3117   3266    309   -222    297       C  
ATOM   5529  CD1 TYR A 362     -20.536 -58.006  19.736  1.00 31.93           C  
ANISOU 5529  CD1 TYR A 362     4873   3527   3732    307   -228    253       C  
ATOM   5530  CD2 TYR A 362     -19.305 -60.028  20.011  1.00 20.36           C  
ANISOU 5530  CD2 TYR A 362     3225   2142   2369    226   -240    325       C  
ATOM   5531  CE1 TYR A 362     -19.883 -57.771  18.530  1.00 26.61           C  
ANISOU 5531  CE1 TYR A 362     4169   2810   3133    217   -250    243       C  
ATOM   5532  CE2 TYR A 362     -18.652 -59.804  18.814  1.00 25.73           C  
ANISOU 5532  CE2 TYR A 362     3871   2782   3122    145   -254    310       C  
ATOM   5533  CZ  TYR A 362     -18.941 -58.675  18.077  1.00 24.74           C  
ANISOU 5533  CZ  TYR A 362     3821   2598   2980    137   -259    272       C  
ATOM   5534  OH  TYR A 362     -18.285 -58.457  16.886  1.00 19.70           O  
ANISOU 5534  OH  TYR A 362     3149   1928   2407     53   -270    265       O  
ATOM   5535  H   TYR A 362     -22.454 -59.734  23.675  1.00 33.74           H  
ATOM   5536  HA  TYR A 362     -22.749 -58.451  21.444  1.00 26.25           H  
ATOM   5537  HB2 TYR A 362     -20.656 -58.730  22.438  1.00 31.82           H  
ATOM   5538  HB3 TYR A 362     -20.704 -60.280  22.112  1.00 31.82           H  
ATOM   5539  HD1 TYR A 362     -21.171 -57.398  20.039  1.00 38.32           H  
ATOM   5540  HD2 TYR A 362     -19.106 -60.793  20.503  1.00 24.43           H  
ATOM   5541  HE1 TYR A 362     -20.078 -57.009  18.033  1.00 31.93           H  
ATOM   5542  HE2 TYR A 362     -18.017 -60.411  18.508  1.00 30.87           H  
ATOM   5543  HH  TYR A 362     -17.745 -59.083  16.737  1.00 23.64           H  
ATOM   5544  N   ILE A 363     -22.998 -61.634  21.092  1.00 32.44           N  
ANISOU 5544  N   ILE A 363     4660   3834   3831    478    -37    454       N  
ATOM   5545  CA  ILE A 363     -23.450 -62.680  20.174  1.00 27.40           C  
ANISOU 5545  CA  ILE A 363     3903   3212   3294    453      2    506       C  
ATOM   5546  C   ILE A 363     -24.978 -62.829  20.121  1.00 37.89           C  
ANISOU 5546  C   ILE A 363     5197   4586   4612    530     73    553       C  
ATOM   5547  O   ILE A 363     -25.567 -62.692  19.050  1.00 46.06           O  
ANISOU 5547  O   ILE A 363     6204   5599   5698    524     94    553       O  
ATOM   5548  CB  ILE A 363     -22.757 -64.036  20.480  1.00 32.04           C  
ANISOU 5548  CB  ILE A 363     4401   3829   3942    405    -17    555       C  
ATOM   5549  CG1 ILE A 363     -21.426 -64.131  19.730  1.00 29.18           C  
ANISOU 5549  CG1 ILE A 363     4016   3419   3653    315    -68    520       C  
ATOM   5550  CG2 ILE A 363     -23.605 -65.216  20.033  1.00 30.25           C  
ANISOU 5550  CG2 ILE A 363     4070   3635   3789    410     28    625       C  
ATOM   5551  CD1 ILE A 363     -20.515 -62.927  19.883  1.00 38.02           C  
ANISOU 5551  CD1 ILE A 363     5228   4496   4723    283   -123    456       C  
ATOM   5552  H   ILE A 363     -22.709 -61.926  21.848  1.00 38.93           H  
ATOM   5553  HA  ILE A 363     -23.169 -62.424  19.282  1.00 32.87           H  
ATOM   5554  HB  ILE A 363     -22.592 -64.104  21.434  1.00 38.44           H  
ATOM   5555 HG12 ILE A 363     -20.943 -64.907  20.056  1.00 35.02           H  
ATOM   5556 HG13 ILE A 363     -21.613 -64.239  18.784  1.00 35.02           H  
ATOM   5557 HG21 ILE A 363     -23.753 -65.154  19.076  1.00 36.30           H  
ATOM   5558 HG22 ILE A 363     -23.136 -66.039  20.242  1.00 36.30           H  
ATOM   5559 HG23 ILE A 363     -24.453 -65.190  20.502  1.00 36.30           H  
ATOM   5560 HD11 ILE A 363     -20.301 -62.810  20.822  1.00 45.63           H  
ATOM   5561 HD12 ILE A 363     -19.703 -63.079  19.375  1.00 45.63           H  
ATOM   5562 HD13 ILE A 363     -20.973 -62.140  19.547  1.00 45.63           H  
ATOM   5563  N   ASP A 364     -25.618 -63.101  21.258  1.00 44.65           N  
ANISOU 5563  N   ASP A 364     6052   5512   5400    601    108    598       N  
ATOM   5564  CA  ASP A 364     -27.059 -63.381  21.270  1.00 42.22           C  
ANISOU 5564  CA  ASP A 364     5688   5266   5090    671    179    663       C  
ATOM   5565  C   ASP A 364     -27.909 -62.243  21.825  1.00 38.28           C  
ANISOU 5565  C   ASP A 364     5271   4789   4484    782    222    637       C  
ATOM   5566  O   ASP A 364     -29.139 -62.302  21.776  1.00 44.82           O  
ANISOU 5566  O   ASP A 364     6049   5672   5309    850    284    689       O  
ATOM   5567  CB  ASP A 364     -27.349 -64.664  22.049  1.00 41.15           C  
ANISOU 5567  CB  ASP A 364     5465   5206   4965    672    203    755       C  
ATOM   5568  CG  ASP A 364     -26.799 -65.893  21.358  1.00 48.30           C  
ANISOU 5568  CG  ASP A 364     6278   6084   5988    578    168    790       C  
ATOM   5569  OD1 ASP A 364     -27.037 -66.039  20.140  1.00 51.55           O  
ANISOU 5569  OD1 ASP A 364     6648   6456   6482    539    167    784       O  
ATOM   5570  OD2 ASP A 364     -26.112 -66.701  22.020  1.00 55.72           O  
ANISOU 5570  OD2 ASP A 364     7196   7040   6937    547    140    820       O  
ATOM   5571  H   ASP A 364     -25.245 -63.130  22.033  1.00 53.58           H  
ATOM   5572  HA  ASP A 364     -27.344 -63.530  20.355  1.00 50.67           H  
ATOM   5573  HB2 ASP A 364     -26.939 -64.602  22.925  1.00 49.38           H  
ATOM   5574  HB3 ASP A 364     -28.309 -64.772  22.136  1.00 49.38           H  
ATOM   5575  N   GLY A 365     -27.255 -61.219  22.361  1.00 50.79           N  
ANISOU 5575  N   GLY A 365     6983   6331   5984    803    185    560       N  
ATOM   5576  CA  GLY A 365     -27.945 -60.007  22.753  1.00 51.76           C  
ANISOU 5576  CA  GLY A 365     7209   6449   6007    912    215    515       C  
ATOM   5577  C   GLY A 365     -27.931 -59.054  21.576  1.00 61.46           C  
ANISOU 5577  C   GLY A 365     8485   7590   7279    892    188    457       C  
ATOM   5578  O   GLY A 365     -27.621 -59.455  20.452  1.00 65.95           O  
ANISOU 5578  O   GLY A 365     8987   8122   7951    803    165    467       O  
ATOM   5579  H   GLY A 365     -26.408 -61.205  22.508  1.00 60.95           H  
ATOM   5580  HA2 GLY A 365     -28.863 -60.205  22.995  1.00 62.11           H  
ATOM   5581  HA3 GLY A 365     -27.496 -59.593  23.507  1.00 62.11           H  
ATOM   5582  N   GLY A 366     -28.266 -57.794  21.830  1.00 47.57           N  
ANISOU 5582  N   GLY A 366     6847   5792   5436    977    190    396       N  
ATOM   5583  CA  GLY A 366     -28.098 -56.748  20.841  1.00 45.20           C  
ANISOU 5583  CA  GLY A 366     6619   5392   5162    954    148    336       C  
ATOM   5584  C   GLY A 366     -27.043 -55.780  21.331  1.00 53.70           C  
ANISOU 5584  C   GLY A 366     7849   6386   6170    928     69    251       C  
ATOM   5585  O   GLY A 366     -27.355 -54.822  22.039  1.00 67.28           O  
ANISOU 5585  O   GLY A 366     9696   8081   7786   1025     69    200       O  
ATOM   5586  H   GLY A 366     -28.595 -57.521  22.576  1.00 57.08           H  
ATOM   5587  HA2 GLY A 366     -27.814 -57.128  19.995  1.00 54.24           H  
ATOM   5588  HA3 GLY A 366     -28.933 -56.271  20.712  1.00 54.24           H  
ATOM   5589  N   ALA A 367     -25.789 -56.038  20.970  1.00 46.34           N  
ANISOU 5589  N   ALA A 367     6904   5412   5292    798     -1    237       N  
ATOM   5590  CA  ALA A 367     -24.678 -55.218  21.440  1.00 53.42           C  
ANISOU 5590  CA  ALA A 367     7930   6233   6134    749    -89    168       C  
ATOM   5591  C   ALA A 367     -23.723 -54.864  20.309  1.00 52.93           C  
ANISOU 5591  C   ALA A 367     7866   6091   6154    621   -156    147       C  
ATOM   5592  O   ALA A 367     -23.356 -55.711  19.494  1.00 51.36           O  
ANISOU 5592  O   ALA A 367     7546   5916   6053    538   -146    188       O  
ATOM   5593  CB  ALA A 367     -23.937 -55.925  22.562  1.00 46.05           C  
ANISOU 5593  CB  ALA A 367     6986   5351   5160    722   -116    183       C  
ATOM   5594  H   ALA A 367     -25.555 -56.684  20.452  1.00 55.61           H  
ATOM   5595  HA  ALA A 367     -25.033 -54.389  21.797  1.00 64.10           H  
ATOM   5596  HB1 ALA A 367     -23.593 -56.769  22.231  1.00 55.26           H  
ATOM   5597  HB2 ALA A 367     -23.204 -55.363  22.859  1.00 55.26           H  
ATOM   5598  HB3 ALA A 367     -24.552 -56.083  23.296  1.00 55.26           H  
ATOM   5599  N   SER A 368     -23.327 -53.597  20.275  1.00 78.08           N  
ANISOU 5599  N   SER A 368    11191   9180   9294    608   -223     83       N  
ATOM   5600  CA  SER A 368     -22.398 -53.104  19.276  1.00 74.31           C  
ANISOU 5600  CA  SER A 368    10726   8626   8883    484   -290     67       C  
ATOM   5601  C   SER A 368     -21.028 -53.726  19.475  1.00 72.59           C  
ANISOU 5601  C   SER A 368    10448   8427   8705    364   -346     83       C  
ATOM   5602  O   SER A 368     -20.663 -54.103  20.589  1.00 69.69           O  
ANISOU 5602  O   SER A 368    10094   8098   8286    377   -367     82       O  
ATOM   5603  CB  SER A 368     -22.280 -51.585  19.394  1.00 75.71           C  
ANISOU 5603  CB  SER A 368    11082   8691   8994    497   -362      0       C  
ATOM   5604  OG  SER A 368     -23.527 -50.954  19.167  1.00 91.93           O  
ANISOU 5604  OG  SER A 368    13193  10721  11016    617   -313    -15       O  
ATOM   5605  H   SER A 368     -23.588 -52.996  20.831  1.00 93.69           H  
ATOM   5606  HA  SER A 368     -22.719 -53.326  18.388  1.00 89.17           H  
ATOM   5607  HB2 SER A 368     -21.973 -51.362  20.287  1.00 90.85           H  
ATOM   5608  HB3 SER A 368     -21.642 -51.267  18.736  1.00 90.85           H  
ATOM   5609  HG  SER A 368     -23.443 -50.121  19.236  1.00110.32           H  
ATOM   5610  N   GLN A 369     -20.272 -53.831  18.387  1.00 52.74           N  
ANISOU 5610  N   GLN A 369     7867   5892   6280    250   -368    100       N  
ATOM   5611  CA  GLN A 369     -18.871 -54.210  18.468  1.00 48.49           C  
ANISOU 5611  CA  GLN A 369     7277   5364   5784    133   -428    113       C  
ATOM   5612  C   GLN A 369     -18.180 -53.200  19.383  1.00 52.00           C  
ANISOU 5612  C   GLN A 369     7863   5743   6150    105   -530     67       C  
ATOM   5613  O   GLN A 369     -17.288 -53.546  20.163  1.00 65.79           O  
ANISOU 5613  O   GLN A 369     9596   7515   7886     57   -585     74       O  
ATOM   5614  CB  GLN A 369     -18.245 -54.207  17.068  1.00 45.41           C  
ANISOU 5614  CB  GLN A 369     6812   4954   5487     26   -431    133       C  
ATOM   5615  CG  GLN A 369     -16.795 -54.685  17.001  1.00 67.31           C  
ANISOU 5615  CG  GLN A 369     9501   7754   8319    -90   -478    158       C  
ATOM   5616  CD  GLN A 369     -16.300 -54.853  15.571  1.00 70.71           C  
ANISOU 5616  CD  GLN A 369     9842   8188   8838   -176   -454    184       C  
ATOM   5617  OE1 GLN A 369     -17.051 -54.655  14.614  1.00 71.92           O  
ANISOU 5617  OE1 GLN A 369     9998   8322   9005   -154   -406    184       O  
ATOM   5618  NE2 GLN A 369     -15.031 -55.222  15.421  1.00 56.81           N  
ANISOU 5618  NE2 GLN A 369     7998   6457   7132   -272   -486    209       N  
ATOM   5619  H   GLN A 369     -20.551 -53.688  17.586  1.00 63.29           H  
ATOM   5620  HA  GLN A 369     -18.786 -55.096  18.852  1.00 58.19           H  
ATOM   5621  HB2 GLN A 369     -18.770 -54.788  16.496  1.00 54.49           H  
ATOM   5622  HB3 GLN A 369     -18.270 -53.302  16.722  1.00 54.49           H  
ATOM   5623  HG2 GLN A 369     -16.226 -54.034  17.441  1.00 80.77           H  
ATOM   5624  HG3 GLN A 369     -16.723 -55.543  17.447  1.00 80.77           H  
ATOM   5625 HE21 GLN A 369     -14.536 -55.352  16.112  1.00 68.18           H  
ATOM   5626 HE22 GLN A 369     -14.705 -55.330  14.633  1.00 68.18           H  
ATOM   5627  N   GLU A 370     -18.648 -51.956  19.315  1.00116.87           N  
ANISOU 5627  N   GLU A 370    16224  13871  14309    142   -560     19       N  
ATOM   5628  CA  GLU A 370     -18.087 -50.863  20.100  1.00122.18           C  
ANISOU 5628  CA  GLU A 370    17060  14460  14903    117   -667    -34       C  
ATOM   5629  C   GLU A 370     -18.527 -50.946  21.558  1.00120.61           C  
ANISOU 5629  C   GLU A 370    16947  14288  14591    227   -666    -66       C  
ATOM   5630  O   GLU A 370     -17.744 -50.671  22.465  1.00118.44           O  
ANISOU 5630  O   GLU A 370    16753  13989  14260    185   -756    -90       O  
ATOM   5631  CB  GLU A 370     -18.507 -49.520  19.493  1.00118.04           C  
ANISOU 5631  CB  GLU A 370    16670  13821  14357    129   -700    -75       C  
ATOM   5632  CG  GLU A 370     -17.977 -49.304  18.077  1.00117.54           C  
ANISOU 5632  CG  GLU A 370    16541  13726  14392      8   -713    -41       C  
ATOM   5633  CD  GLU A 370     -18.538 -48.059  17.417  1.00118.01           C  
ANISOU 5633  CD  GLU A 370    16727  13676  14434     30   -738    -71       C  
ATOM   5634  OE1 GLU A 370     -19.606 -47.576  17.853  1.00118.44           O  
ANISOU 5634  OE1 GLU A 370    16885  13699  14420    166   -711   -111       O  
ATOM   5635  OE2 GLU A 370     -17.914 -47.560  16.457  1.00118.02           O  
ANISOU 5635  OE2 GLU A 370    16723  13627  14492    -86   -782    -49       O  
ATOM   5636  H   GLU A 370     -19.302 -51.717  18.811  1.00140.24           H  
ATOM   5637  HA  GLU A 370     -17.119 -50.917  20.073  1.00146.62           H  
ATOM   5638  HB2 GLU A 370     -19.475 -49.480  19.458  1.00141.65           H  
ATOM   5639  HB3 GLU A 370     -18.166 -48.804  20.052  1.00141.65           H  
ATOM   5640  HG2 GLU A 370     -17.012 -49.214  18.113  1.00141.05           H  
ATOM   5641  HG3 GLU A 370     -18.219 -50.067  17.530  1.00141.05           H  
ATOM   5642  N   GLU A 371     -19.781 -51.327  21.779  1.00 31.90           N  
ANISOU 5642  N   GLU A 371     5693   3108   3321    364   -565    -60       N  
ATOM   5643  CA  GLU A 371     -20.299 -51.498  23.133  1.00 33.21           C  
ANISOU 5643  CA  GLU A 371     5925   3320   3374    479   -542    -80       C  
ATOM   5644  C   GLU A 371     -19.575 -52.658  23.797  1.00 41.10           C  
ANISOU 5644  C   GLU A 371     6820   4407   4389    426   -551    -33       C  
ATOM   5645  O   GLU A 371     -19.109 -52.550  24.936  1.00 40.42           O  
ANISOU 5645  O   GLU A 371     6820   4323   4216    431   -612    -57       O  
ATOM   5646  CB  GLU A 371     -21.801 -51.777  23.111  1.00 32.21           C  
ANISOU 5646  CB  GLU A 371     5762   3253   3222    629   -420    -63       C  
ATOM   5647  CG  GLU A 371     -22.672 -50.538  22.994  1.00 38.00           C  
ANISOU 5647  CG  GLU A 371     6640   3906   3892    735   -413   -121       C  
ATOM   5648  CD  GLU A 371     -24.116 -50.872  22.657  1.00 44.39           C  
ANISOU 5648  CD  GLU A 371     7371   4783   4714    863   -290    -85       C  
ATOM   5649  OE1 GLU A 371     -24.357 -51.919  22.019  1.00 45.57           O  
ANISOU 5649  OE1 GLU A 371     7350   5010   4956    828   -228    -15       O  
ATOM   5650  OE2 GLU A 371     -25.011 -50.088  23.034  1.00 48.45           O  
ANISOU 5650  OE2 GLU A 371     7994   5270   5145    999   -260   -126       O  
ATOM   5651  H   GLU A 371     -20.354 -51.493  21.160  1.00 38.28           H  
ATOM   5652  HA  GLU A 371     -20.138 -50.693  23.649  1.00 39.85           H  
ATOM   5653  HB2 GLU A 371     -21.999 -52.348  22.352  1.00 38.65           H  
ATOM   5654  HB3 GLU A 371     -22.044 -52.231  23.933  1.00 38.65           H  
ATOM   5655  HG2 GLU A 371     -22.662 -50.063  23.839  1.00 45.60           H  
ATOM   5656  HG3 GLU A 371     -22.322 -49.971  22.289  1.00 45.60           H  
ATOM   5657  N   PHE A 372     -19.484 -53.770  23.075  1.00 34.20           N  
ANISOU 5657  N   PHE A 372     5768   3601   3624    378   -496     32       N  
ATOM   5658  CA  PHE A 372     -18.781 -54.938  23.578  1.00 31.15           C  
ANISOU 5658  CA  PHE A 372     5272   3292   3271    328   -504     83       C  
ATOM   5659  C   PHE A 372     -17.329 -54.578  23.886  1.00 25.07           C  
ANISOU 5659  C   PHE A 372     4542   2479   2506    208   -628     67       C  
ATOM   5660  O   PHE A 372     -16.841 -54.823  24.996  1.00 29.37           O  
ANISOU 5660  O   PHE A 372     5120   3050   2988    205   -680     69       O  
ATOM   5661  CB  PHE A 372     -18.863 -56.102  22.584  1.00 28.56           C  
ANISOU 5661  CB  PHE A 372     4760   3022   3069    292   -434    147       C  
ATOM   5662  CG  PHE A 372     -17.999 -57.269  22.954  1.00 23.09           C  
ANISOU 5662  CG  PHE A 372     3954   2392   2428    233   -454    198       C  
ATOM   5663  CD1 PHE A 372     -18.076 -57.828  24.219  1.00 26.84           C  
ANISOU 5663  CD1 PHE A 372     4441   2924   2832    283   -457    219       C  
ATOM   5664  CD2 PHE A 372     -17.109 -57.808  22.041  1.00 22.47           C  
ANISOU 5664  CD2 PHE A 372     3758   2316   2465    133   -468    226       C  
ATOM   5665  CE1 PHE A 372     -17.279 -58.902  24.570  1.00 23.43           C  
ANISOU 5665  CE1 PHE A 372     3907   2545   2451    231   -483    270       C  
ATOM   5666  CE2 PHE A 372     -16.309 -58.883  22.384  1.00 30.25           C  
ANISOU 5666  CE2 PHE A 372     4637   3354   3501     91   -487    273       C  
ATOM   5667  CZ  PHE A 372     -16.395 -59.431  23.651  1.00 22.82           C  
ANISOU 5667  CZ  PHE A 372     3711   2463   2496    138   -499    296       C  
ATOM   5668  H   PHE A 372     -19.822 -53.871  22.290  1.00 41.04           H  
ATOM   5669  HA  PHE A 372     -19.200 -55.223  24.405  1.00 37.38           H  
ATOM   5670  HB2 PHE A 372     -19.781 -56.413  22.542  1.00 34.27           H  
ATOM   5671  HB3 PHE A 372     -18.581 -55.788  21.710  1.00 34.27           H  
ATOM   5672  HD1 PHE A 372     -18.669 -57.474  24.842  1.00 32.21           H  
ATOM   5673  HD2 PHE A 372     -17.047 -57.441  21.188  1.00 26.97           H  
ATOM   5674  HE1 PHE A 372     -17.340 -59.269  25.422  1.00 28.12           H  
ATOM   5675  HE2 PHE A 372     -15.714 -59.237  21.763  1.00 36.30           H  
ATOM   5676  HZ  PHE A 372     -15.859 -60.155  23.883  1.00 27.38           H  
ATOM   5677  N   TYR A 373     -16.654 -53.969  22.916  1.00 24.93           N  
ANISOU 5677  N   TYR A 373     4521   2395   2557    106   -677     57       N  
ATOM   5678  CA  TYR A 373     -15.268 -53.561  23.107  1.00 25.55           C  
ANISOU 5678  CA  TYR A 373     4624   2434   2651    -20   -798     52       C  
ATOM   5679  C   TYR A 373     -15.112 -52.639  24.313  1.00 37.35           C  
ANISOU 5679  C   TYR A 373     6305   3869   4017      0   -896     -5       C  
ATOM   5680  O   TYR A 373     -14.259 -52.878  25.153  1.00 39.17           O  
ANISOU 5680  O   TYR A 373     6541   4119   4222    -52   -976      5       O  
ATOM   5681  CB  TYR A 373     -14.708 -52.909  21.841  1.00 26.99           C  
ANISOU 5681  CB  TYR A 373     4785   2554   2916   -127   -828     55       C  
ATOM   5682  CG  TYR A 373     -14.331 -53.883  20.741  1.00 33.35           C  
ANISOU 5682  CG  TYR A 373     5400   3422   3848   -185   -764    114       C  
ATOM   5683  CD1 TYR A 373     -14.437 -55.259  20.921  1.00 33.18           C  
ANISOU 5683  CD1 TYR A 373     5245   3495   3869   -146   -697    159       C  
ATOM   5684  CD2 TYR A 373     -13.851 -53.422  19.526  1.00 26.44           C  
ANISOU 5684  CD2 TYR A 373     4489   2511   3046   -278   -773    126       C  
ATOM   5685  CE1 TYR A 373     -14.087 -56.140  19.917  1.00 29.16           C  
ANISOU 5685  CE1 TYR A 373     4579   3033   3470   -190   -643    203       C  
ATOM   5686  CE2 TYR A 373     -13.500 -54.292  18.521  1.00 34.50           C  
ANISOU 5686  CE2 TYR A 373     5349   3591   4170   -321   -711    173       C  
ATOM   5687  CZ  TYR A 373     -13.616 -55.650  18.719  1.00 31.99           C  
ANISOU 5687  CZ  TYR A 373     4906   3357   3890   -273   -647    207       C  
ATOM   5688  OH  TYR A 373     -13.263 -56.514  17.708  1.00 36.28           O  
ANISOU 5688  OH  TYR A 373     5304   3951   4531   -308   -587    245       O  
ATOM   5689  H   TYR A 373     -16.974 -53.782  22.140  1.00 29.92           H  
ATOM   5690  HA  TYR A 373     -14.738 -54.355  23.281  1.00 30.66           H  
ATOM   5691  HB2 TYR A 373     -15.377 -52.305  21.481  1.00 32.39           H  
ATOM   5692  HB3 TYR A 373     -13.911 -52.409  22.076  1.00 32.39           H  
ATOM   5693  HD1 TYR A 373     -14.755 -55.591  21.729  1.00 39.82           H  
ATOM   5694  HD2 TYR A 373     -13.769 -52.506  19.385  1.00 31.72           H  
ATOM   5695  HE1 TYR A 373     -14.166 -57.057  20.049  1.00 35.00           H  
ATOM   5696  HE2 TYR A 373     -13.182 -53.965  17.711  1.00 41.40           H  
ATOM   5697  HH  TYR A 373     -13.383 -57.308  17.955  1.00 43.54           H  
ATOM   5698  N   LYS A 374     -15.937 -51.603  24.422  1.00 78.22           N  
ANISOU 5698  N   LYS A 374    11639   8970   9109     81   -892    -67       N  
ATOM   5699  CA  LYS A 374     -15.875 -50.742  25.601  1.00 80.49           C  
ANISOU 5699  CA  LYS A 374    12124   9196   9261    119   -981   -132       C  
ATOM   5700  C   LYS A 374     -16.106 -51.540  26.887  1.00 74.84           C  
ANISOU 5700  C   LYS A 374    11408   8571   8458    201   -955   -122       C  
ATOM   5701  O   LYS A 374     -15.473 -51.274  27.909  1.00 81.14           O  
ANISOU 5701  O   LYS A 374    12309   9348   9172    173  -1056   -148       O  
ATOM   5702  CB  LYS A 374     -16.889 -49.605  25.509  1.00 76.45           C  
ANISOU 5702  CB  LYS A 374    11778   8596   8672    226   -961   -202       C  
ATOM   5703  CG  LYS A 374     -16.559 -48.561  24.463  1.00 76.55           C  
ANISOU 5703  CG  LYS A 374    11847   8495   8745    138  -1023   -220       C  
ATOM   5704  CD  LYS A 374     -17.694 -47.565  24.332  1.00 77.07           C  
ANISOU 5704  CD  LYS A 374    12062   8480   8742    265   -989   -282       C  
ATOM   5705  CE  LYS A 374     -17.481 -46.635  23.149  1.00 77.05           C  
ANISOU 5705  CE  LYS A 374    12095   8368   8811    181  -1037   -286       C  
ATOM   5706  NZ  LYS A 374     -18.582 -45.646  22.984  1.00 77.62           N  
ANISOU 5706  NZ  LYS A 374    12314   8354   8825    310  -1010   -343       N  
ATOM   5707  H   LYS A 374     -16.531 -51.380  23.841  1.00 93.86           H  
ATOM   5708  HA  LYS A 374     -14.990 -50.346  25.652  1.00 96.58           H  
ATOM   5709  HB2 LYS A 374     -17.756 -49.980  25.290  1.00 91.74           H  
ATOM   5710  HB3 LYS A 374     -16.933 -49.158  26.369  1.00 91.74           H  
ATOM   5711  HG2 LYS A 374     -15.758 -48.081  24.726  1.00 91.86           H  
ATOM   5712  HG3 LYS A 374     -16.429 -48.993  23.605  1.00 91.86           H  
ATOM   5713  HD2 LYS A 374     -18.527 -48.043  24.197  1.00 92.49           H  
ATOM   5714  HD3 LYS A 374     -17.743 -47.026  25.137  1.00 92.49           H  
ATOM   5715  HE2 LYS A 374     -16.654 -46.144  23.278  1.00 92.46           H  
ATOM   5716  HE3 LYS A 374     -17.429 -47.164  22.337  1.00 92.46           H  
ATOM   5717  HZ1 LYS A 374     -18.647 -45.139  23.713  1.00 93.15           H  
ATOM   5718  HZ2 LYS A 374     -18.418 -45.123  22.282  1.00 93.15           H  
ATOM   5719  HZ3 LYS A 374     -19.354 -46.069  22.855  1.00 93.15           H  
ATOM   5720  N   PHE A 375     -17.011 -52.513  26.838  1.00 48.27           N  
ANISOU 5720  N   PHE A 375     7929   5303   5109    296   -826    -79       N  
ATOM   5721  CA  PHE A 375     -17.251 -53.375  27.997  1.00 45.13           C  
ANISOU 5721  CA  PHE A 375     7512   5000   4634    366   -792    -52       C  
ATOM   5722  C   PHE A 375     -16.003 -54.178  28.394  1.00 50.61           C  
ANISOU 5722  C   PHE A 375     8114   5737   5377    253   -872     -1       C  
ATOM   5723  O   PHE A 375     -15.601 -54.144  29.559  1.00 61.21           O  
ANISOU 5723  O   PHE A 375     9545   7092   6621    256   -943    -15       O  
ATOM   5724  CB  PHE A 375     -18.443 -54.317  27.757  1.00 47.58           C  
ANISOU 5724  CB  PHE A 375     7700   5407   4972    471   -642      1       C  
ATOM   5725  CG  PHE A 375     -18.740 -55.241  28.918  1.00 54.62           C  
ANISOU 5725  CG  PHE A 375     8564   6402   5788    539   -601     43       C  
ATOM   5726  CD1 PHE A 375     -17.994 -56.394  29.114  1.00 52.38           C  
ANISOU 5726  CD1 PHE A 375     8150   6183   5571    464   -623    112       C  
ATOM   5727  CD2 PHE A 375     -19.773 -54.963  29.802  1.00 49.63           C  
ANISOU 5727  CD2 PHE A 375     8036   5805   5018    683   -538     18       C  
ATOM   5728  CE1 PHE A 375     -18.260 -57.243  30.174  1.00 52.92           C  
ANISOU 5728  CE1 PHE A 375     8195   6342   5569    521   -591    159       C  
ATOM   5729  CE2 PHE A 375     -20.045 -55.812  30.865  1.00 48.06           C  
ANISOU 5729  CE2 PHE A 375     7809   5708   4742    741   -497     66       C  
ATOM   5730  CZ  PHE A 375     -19.288 -56.952  31.048  1.00 57.93           C  
ANISOU 5730  CZ  PHE A 375     8934   7017   6062    655   -527    139       C  
ATOM   5731  H   PHE A 375     -17.498 -52.696  26.152  1.00 57.93           H  
ATOM   5732  HA  PHE A 375     -17.479 -52.810  28.751  1.00 54.15           H  
ATOM   5733  HB2 PHE A 375     -19.236 -53.781  27.595  1.00 57.10           H  
ATOM   5734  HB3 PHE A 375     -18.255 -54.867  26.981  1.00 57.10           H  
ATOM   5735  HD1 PHE A 375     -17.299 -56.595  28.530  1.00 62.86           H  
ATOM   5736  HD2 PHE A 375     -20.285 -54.195  29.684  1.00 59.56           H  
ATOM   5737  HE1 PHE A 375     -17.750 -58.011  30.295  1.00 63.50           H  
ATOM   5738  HE2 PHE A 375     -20.738 -55.614  31.453  1.00 57.67           H  
ATOM   5739  HZ  PHE A 375     -19.470 -57.523  31.760  1.00 69.52           H  
ATOM   5740  N   ILE A 376     -15.397 -54.900  27.449  1.00 28.80           N  
ANISOU 5740  N   ILE A 376     5179   3003   2762    159   -860     57       N  
ATOM   5741  CA  ILE A 376     -14.249 -55.762  27.788  1.00 32.65           C  
ANISOU 5741  CA  ILE A 376     5559   3540   3307     67   -924    113       C  
ATOM   5742  C   ILE A 376     -12.861 -55.103  27.750  1.00 35.24           C  
ANISOU 5742  C   ILE A 376     5918   3806   3664    -73  -1069    101       C  
ATOM   5743  O   ILE A 376     -11.912 -55.680  28.276  1.00 48.34           O  
ANISOU 5743  O   ILE A 376     7514   5506   5348   -139  -1140    143       O  
ATOM   5744  CB  ILE A 376     -14.200 -57.101  26.966  1.00 40.50           C  
ANISOU 5744  CB  ILE A 376     6339   4608   4442     47   -840    189       C  
ATOM   5745  CG1 ILE A 376     -14.392 -56.873  25.464  1.00 41.96           C  
ANISOU 5745  CG1 ILE A 376     6455   4758   4732     15   -784    185       C  
ATOM   5746  CG2 ILE A 376     -15.204 -58.114  27.516  1.00 36.44           C  
ANISOU 5746  CG2 ILE A 376     5777   4178   3892    157   -740    230       C  
ATOM   5747  CD1 ILE A 376     -13.109 -56.855  24.716  1.00 46.75           C  
ANISOU 5747  CD1 ILE A 376     6972   5346   5445   -117   -848    207       C  
ATOM   5748  H   ILE A 376     -15.622 -54.913  26.619  1.00 34.56           H  
ATOM   5749  HA  ILE A 376     -14.379 -56.031  28.711  1.00 39.18           H  
ATOM   5750  HB  ILE A 376     -13.315 -57.480  27.088  1.00 48.60           H  
ATOM   5751 HG12 ILE A 376     -14.939 -57.588  25.103  1.00 50.36           H  
ATOM   5752 HG13 ILE A 376     -14.831 -56.019  25.327  1.00 50.36           H  
ATOM   5753 HG21 ILE A 376     -16.096 -57.738  27.455  1.00 43.73           H  
ATOM   5754 HG22 ILE A 376     -15.151 -58.927  26.990  1.00 43.73           H  
ATOM   5755 HG23 ILE A 376     -14.986 -58.303  28.442  1.00 43.73           H  
ATOM   5756 HD11 ILE A 376     -12.662 -57.707  24.837  1.00 56.10           H  
ATOM   5757 HD12 ILE A 376     -13.294 -56.707  23.776  1.00 56.10           H  
ATOM   5758 HD13 ILE A 376     -12.554 -56.138  25.061  1.00 56.10           H  
ATOM   5759  N   LYS A 377     -12.732 -53.915  27.157  1.00 53.70           N  
ANISOU 5759  N   LYS A 377     8351   6048   6003   -122  -1118     52       N  
ATOM   5760  CA  LYS A 377     -11.448 -53.195  27.175  1.00 56.38           C  
ANISOU 5760  CA  LYS A 377     8731   6325   6366   -264  -1265     47       C  
ATOM   5761  C   LYS A 377     -10.883 -53.117  28.601  1.00 53.09           C  
ANISOU 5761  C   LYS A 377     8417   5910   5844   -279  -1383     34       C  
ATOM   5762  O   LYS A 377      -9.761 -53.557  28.845  1.00 60.78           O  
ANISOU 5762  O   LYS A 377     9303   6919   6873   -379  -1468     84       O  
ATOM   5763  CB  LYS A 377     -11.557 -51.777  26.586  1.00 56.75           C  
ANISOU 5763  CB  LYS A 377     8917   6252   6394   -301  -1315    -11       C  
ATOM   5764  CG  LYS A 377     -11.544 -51.691  25.059  1.00 55.81           C  
ANISOU 5764  CG  LYS A 377     8687   6118   6399   -356  -1253     17       C  
ATOM   5765  CD  LYS A 377     -11.875 -50.274  24.582  1.00 56.36           C  
ANISOU 5765  CD  LYS A 377     8917   6064   6433   -368  -1296    -41       C  
ATOM   5766  CE  LYS A 377     -12.134 -50.239  23.082  1.00 55.38           C  
ANISOU 5766  CE  LYS A 377     8694   5934   6412   -394  -1213    -13       C  
ATOM   5767  NZ  LYS A 377     -12.398 -48.889  22.529  1.00 55.93           N  
ANISOU 5767  NZ  LYS A 377     8909   5881   6460   -417  -1260    -57       N  
ATOM   5768  H   LYS A 377     -13.363 -53.505  26.741  1.00 64.43           H  
ATOM   5769  HA  LYS A 377     -10.811 -53.688  26.635  1.00 67.66           H  
ATOM   5770  HB2 LYS A 377     -12.389 -51.382  26.892  1.00 68.10           H  
ATOM   5771  HB3 LYS A 377     -10.811 -51.251  26.913  1.00 68.10           H  
ATOM   5772  HG2 LYS A 377     -10.661 -51.924  24.732  1.00 66.97           H  
ATOM   5773  HG3 LYS A 377     -12.209 -52.297  24.697  1.00 66.97           H  
ATOM   5774  HD2 LYS A 377     -12.673 -49.962  25.036  1.00 67.63           H  
ATOM   5775  HD3 LYS A 377     -11.127 -49.688  24.775  1.00 67.63           H  
ATOM   5776  HE2 LYS A 377     -11.357 -50.597  22.626  1.00 66.45           H  
ATOM   5777  HE3 LYS A 377     -12.908 -50.791  22.889  1.00 66.45           H  
ATOM   5778  HZ1 LYS A 377     -11.699 -48.358  22.678  1.00 67.11           H  
ATOM   5779  HZ2 LYS A 377     -12.540 -48.942  21.653  1.00 67.11           H  
ATOM   5780  HZ3 LYS A 377     -13.116 -48.536  22.918  1.00 67.11           H  
ATOM   5781  N   PRO A 378     -11.667 -52.576  29.552  1.00 50.09           N  
ANISOU 5781  N   PRO A 378     8222   5498   5310   -173  -1387    -31       N  
ATOM   5782  CA  PRO A 378     -11.157 -52.449  30.922  1.00 50.42           C  
ANISOU 5782  CA  PRO A 378     8384   5539   5234   -184  -1505    -50       C  
ATOM   5783  C   PRO A 378     -10.878 -53.803  31.565  1.00 61.72           C  
ANISOU 5783  C   PRO A 378     9680   7089   6681   -173  -1481     24       C  
ATOM   5784  O   PRO A 378      -9.882 -53.953  32.274  1.00 72.53           O  
ANISOU 5784  O   PRO A 378    11051   8470   8037   -255  -1604     49       O  
ATOM   5785  CB  PRO A 378     -12.301 -51.742  31.653  1.00 46.56           C  
ANISOU 5785  CB  PRO A 378     8105   5010   4577    -37  -1467   -135       C  
ATOM   5786  CG  PRO A 378     -13.515 -52.107  30.878  1.00 59.48           C  
ANISOU 5786  CG  PRO A 378     9657   6687   6255     75  -1294   -125       C  
ATOM   5787  CD  PRO A 378     -13.070 -52.138  29.456  1.00 56.49           C  
ANISOU 5787  CD  PRO A 378     9134   6285   6043    -28  -1279    -87       C  
ATOM   5788  HA  PRO A 378     -10.359 -51.899  30.946  1.00 60.50           H  
ATOM   5789  HB2 PRO A 378     -12.361 -52.070  32.564  1.00 55.88           H  
ATOM   5790  HB3 PRO A 378     -12.158 -50.783  31.639  1.00 55.88           H  
ATOM   5791  HG2 PRO A 378     -13.832 -52.980  31.158  1.00 71.37           H  
ATOM   5792  HG3 PRO A 378     -14.201 -51.434  31.009  1.00 71.37           H  
ATOM   5793  HD2 PRO A 378     -13.592 -52.781  28.951  1.00 67.78           H  
ATOM   5794  HD3 PRO A 378     -13.122 -51.251  29.065  1.00 67.78           H  
ATOM   5795  N   ILE A 379     -11.747 -54.776  31.311  1.00 41.87           N  
ANISOU 5795  N   ILE A 379     7050   4658   4200    -75  -1332     63       N  
ATOM   5796  CA  ILE A 379     -11.592 -56.111  31.881  1.00 37.77           C  
ANISOU 5796  CA  ILE A 379     6405   4246   3701    -56  -1302    138       C  
ATOM   5797  C   ILE A 379     -10.292 -56.753  31.406  1.00 43.76           C  
ANISOU 5797  C   ILE A 379     6991   5030   4608   -186  -1369    208       C  
ATOM   5798  O   ILE A 379      -9.590 -57.385  32.189  1.00 50.75           O  
ANISOU 5798  O   ILE A 379     7834   5964   5485   -220  -1441    256       O  
ATOM   5799  CB  ILE A 379     -12.796 -57.021  31.536  1.00 42.83           C  
ANISOU 5799  CB  ILE A 379     6946   4961   4368     59  -1131    174       C  
ATOM   5800  CG1 ILE A 379     -14.077 -56.435  32.132  1.00 43.51           C  
ANISOU 5800  CG1 ILE A 379     7190   5040   4300    198  -1060    116       C  
ATOM   5801  CG2 ILE A 379     -12.582 -58.439  32.073  1.00 43.18           C  
ANISOU 5801  CG2 ILE A 379     6857   5104   4445     67  -1110    261       C  
ATOM   5802  CD1 ILE A 379     -15.347 -57.084  31.637  1.00 42.75           C  
ANISOU 5802  CD1 ILE A 379     7002   5006   4237    304   -897    148       C  
ATOM   5803  H   ILE A 379     -12.439 -54.688  30.808  1.00 50.24           H  
ATOM   5804  HA  ILE A 379     -11.547 -56.033  32.847  1.00 45.33           H  
ATOM   5805  HB  ILE A 379     -12.890 -57.063  30.572  1.00 51.40           H  
ATOM   5806 HG12 ILE A 379     -14.048 -56.541  33.096  1.00 52.21           H  
ATOM   5807 HG13 ILE A 379     -14.121 -55.492  31.908  1.00 52.21           H  
ATOM   5808 HG21 ILE A 379     -12.482 -58.399  33.037  1.00 51.82           H  
ATOM   5809 HG22 ILE A 379     -13.351 -58.983  31.842  1.00 51.82           H  
ATOM   5810 HG23 ILE A 379     -11.781 -58.810  31.672  1.00 51.82           H  
ATOM   5811 HD11 ILE A 379     -15.329 -58.027  31.864  1.00 51.31           H  
ATOM   5812 HD12 ILE A 379     -16.107 -56.655  32.061  1.00 51.31           H  
ATOM   5813 HD13 ILE A 379     -15.402 -56.976  30.674  1.00 51.31           H  
ATOM   5814  N   LEU A 380      -9.962 -56.574  30.130  1.00 50.69           N  
ANISOU 5814  N   LEU A 380     7767   5876   5615   -255  -1346    217       N  
ATOM   5815  CA  LEU A 380      -8.745 -57.158  29.572  1.00 52.25           C  
ANISOU 5815  CA  LEU A 380     7789   6105   5957   -367  -1393    283       C  
ATOM   5816  C   LEU A 380      -7.509 -56.484  30.160  1.00 58.52           C  
ANISOU 5816  C   LEU A 380     8643   6862   6730   -488  -1569    283       C  
ATOM   5817  O   LEU A 380      -6.520 -57.145  30.472  1.00 55.22           O  
ANISOU 5817  O   LEU A 380     8113   6495   6373   -552  -1638    347       O  
ATOM   5818  CB  LEU A 380      -8.732 -57.029  28.045  1.00 47.47           C  
ANISOU 5818  CB  LEU A 380     7078   5479   5478   -407  -1320    289       C  
ATOM   5819  CG  LEU A 380      -9.819 -57.764  27.255  1.00 42.13           C  
ANISOU 5819  CG  LEU A 380     6318   4839   4850   -310  -1158    298       C  
ATOM   5820  CD1 LEU A 380      -9.885 -57.209  25.841  1.00 45.65           C  
ANISOU 5820  CD1 LEU A 380     6727   5239   5377   -353  -1110    281       C  
ATOM   5821  CD2 LEU A 380      -9.580 -59.263  27.222  1.00 34.69           C  
ANISOU 5821  CD2 LEU A 380     5200   3982   3997   -291  -1106    371       C  
ATOM   5822  H   LEU A 380     -10.425 -56.119  29.566  1.00 60.82           H  
ATOM   5823  HA  LEU A 380      -8.711 -58.101  29.797  1.00 62.70           H  
ATOM   5824  HB2 LEU A 380      -8.810 -56.087  27.825  1.00 56.96           H  
ATOM   5825  HB3 LEU A 380      -7.878 -57.359  27.725  1.00 56.96           H  
ATOM   5826  HG  LEU A 380     -10.678 -57.607  27.678  1.00 50.56           H  
ATOM   5827 HD11 LEU A 380      -9.025 -57.339  25.411  1.00 54.77           H  
ATOM   5828 HD12 LEU A 380     -10.575 -57.680  25.349  1.00 54.77           H  
ATOM   5829 HD13 LEU A 380     -10.095 -56.263  25.883  1.00 54.77           H  
ATOM   5830 HD21 LEU A 380      -9.578 -59.602  28.131  1.00 41.62           H  
ATOM   5831 HD22 LEU A 380     -10.291 -59.684  26.713  1.00 41.62           H  
ATOM   5832 HD23 LEU A 380      -8.724 -59.437  26.801  1.00 41.62           H  
ATOM   5833  N   GLU A 381      -7.576 -55.167  30.326  1.00118.00           N  
ANISOU 5833  N   GLU A 381    16356  14301  14177   -518  -1648    214       N  
ATOM   5834  CA  GLU A 381      -6.445 -54.407  30.849  1.00113.88           C  
ANISOU 5834  CA  GLU A 381    15910  13728  13633   -646  -1829    211       C  
ATOM   5835  C   GLU A 381      -6.193 -54.720  32.323  1.00118.38           C  
ANISOU 5835  C   GLU A 381    16561  14330  14088   -626  -1924    216       C  
ATOM   5836  O   GLU A 381      -5.047 -54.885  32.741  1.00123.00           O  
ANISOU 5836  O   GLU A 381    17089  14935  14710   -731  -2053    266       O  
ATOM   5837  CB  GLU A 381      -6.687 -52.910  30.658  1.00101.58           C  
ANISOU 5837  CB  GLU A 381    14546  12046  12005   -675  -1892    130       C  
ATOM   5838  CG  GLU A 381      -6.700 -52.469  29.202  1.00100.79           C  
ANISOU 5838  CG  GLU A 381    14370  11907  12021   -728  -1833    136       C  
ATOM   5839  CD  GLU A 381      -7.083 -51.014  29.052  1.00101.51           C  
ANISOU 5839  CD  GLU A 381    14667  11866  12036   -740  -1889     57       C  
ATOM   5840  OE1 GLU A 381      -7.339 -50.360  30.085  1.00102.65           O  
ANISOU 5840  OE1 GLU A 381    15017  11947  12037   -701  -1973    -10       O  
ATOM   5841  OE2 GLU A 381      -7.128 -50.520  27.909  1.00101.03           O  
ANISOU 5841  OE2 GLU A 381    14571  11761  12054   -786  -1853     60       O  
ATOM   5842  H   GLU A 381      -8.266 -54.688  30.142  1.00141.60           H  
ATOM   5843  HA  GLU A 381      -5.648 -54.647  30.352  1.00136.66           H  
ATOM   5844  HB2 GLU A 381      -7.547 -52.680  31.044  1.00121.90           H  
ATOM   5845  HB3 GLU A 381      -5.983 -52.419  31.110  1.00121.90           H  
ATOM   5846  HG2 GLU A 381      -5.814 -52.588  28.826  1.00120.95           H  
ATOM   5847  HG3 GLU A 381      -7.345 -53.003  28.713  1.00120.95           H  
ATOM   5848  N   LYS A 382      -7.266 -54.803  33.104  1.00 80.13           N  
ANISOU 5848  N   LYS A 382    11846   9497   9104   -492  -1859    170       N  
ATOM   5849  CA  LYS A 382      -7.163 -55.114  34.528  1.00 80.97           C  
ANISOU 5849  CA  LYS A 382    12044   9640   9080   -458  -1934    173       C  
ATOM   5850  C   LYS A 382      -6.631 -56.522  34.728  1.00 82.78           C  
ANISOU 5850  C   LYS A 382    12077   9977   9397   -470  -1918    274       C  
ATOM   5851  O   LYS A 382      -5.932 -56.813  35.699  1.00 90.29           O  
ANISOU 5851  O   LYS A 382    13045  10959  10302   -512  -2034    308       O  
ATOM   5852  CB  LYS A 382      -8.532 -54.996  35.199  1.00 82.51           C  
ANISOU 5852  CB  LYS A 382    12396   9843   9113   -296  -1833    112       C  
ATOM   5853  CG  LYS A 382      -9.027 -53.567  35.349  1.00 87.20           C  
ANISOU 5853  CG  LYS A 382    13226  10324   9581   -263  -1874      3       C  
ATOM   5854  CD  LYS A 382     -10.379 -53.512  36.041  1.00 83.67           C  
ANISOU 5854  CD  LYS A 382    12919   9902   8972    -86  -1761    -52       C  
ATOM   5855  CE  LYS A 382     -10.770 -52.080  36.364  1.00 81.40           C  
ANISOU 5855  CE  LYS A 382    12890   9496   8544    -44  -1821   -167       C  
ATOM   5856  NZ  LYS A 382     -11.902 -52.015  37.326  1.00 73.10           N  
ANISOU 5856  NZ  LYS A 382    11991   8478   7304    130  -1735   -220       N  
ATOM   5857  H   LYS A 382      -8.073 -54.683  32.832  1.00 96.16           H  
ATOM   5858  HA  LYS A 382      -6.554 -54.490  34.954  1.00 97.16           H  
ATOM   5859  HB2 LYS A 382      -9.183 -55.480  34.667  1.00 99.02           H  
ATOM   5860  HB3 LYS A 382      -8.479 -55.385  36.086  1.00 99.02           H  
ATOM   5861  HG2 LYS A 382      -8.393 -53.063  35.882  1.00104.64           H  
ATOM   5862  HG3 LYS A 382      -9.119 -53.167  34.470  1.00104.64           H  
ATOM   5863  HD2 LYS A 382     -11.056 -53.888  35.456  1.00100.41           H  
ATOM   5864  HD3 LYS A 382     -10.337 -54.011  36.871  1.00100.41           H  
ATOM   5865  HE2 LYS A 382     -10.010 -51.625  36.760  1.00 97.69           H  
ATOM   5866  HE3 LYS A 382     -11.040 -51.632  35.548  1.00 97.69           H  
ATOM   5867  HZ1 LYS A 382     -11.678 -52.417  38.087  1.00 87.72           H  
ATOM   5868  HZ2 LYS A 382     -12.108 -51.166  37.496  1.00 87.72           H  
ATOM   5869  HZ3 LYS A 382     -12.615 -52.423  36.983  1.00 87.72           H  
ATOM   5870  N   MET A 383      -6.973 -57.388  33.785  1.00 70.82           N  
ANISOU 5870  N   MET A 383    10382   8515   8011   -433  -1779    321       N  
ATOM   5871  CA  MET A 383      -6.642 -58.798  33.857  1.00 63.84           C  
ANISOU 5871  CA  MET A 383     9313   7724   7218   -422  -1742    413       C  
ATOM   5872  C   MET A 383      -5.156 -59.056  33.689  1.00 71.56           C  
ANISOU 5872  C   MET A 383    10152   8720   8319   -551  -1861    478       C  
ATOM   5873  O   MET A 383      -4.577 -59.862  34.417  1.00 72.22           O  
ANISOU 5873  O   MET A 383    10168   8861   8410   -563  -1923    543       O  
ATOM   5874  CB  MET A 383      -7.408 -59.524  32.767  1.00 49.84           C  
ANISOU 5874  CB  MET A 383     7404   5983   5552   -354  -1570    433       C  
ATOM   5875  CG  MET A 383      -7.355 -60.999  32.868  1.00 45.61           C  
ANISOU 5875  CG  MET A 383     6708   5530   5093   -315  -1514    517       C  
ATOM   5876  SD  MET A 383      -8.798 -61.650  32.032  1.00 50.47           S  
ANISOU 5876  SD  MET A 383     7262   6167   5745   -199  -1314    516       S  
ATOM   5877  CE  MET A 383      -9.016 -63.080  33.022  1.00 49.90           C  
ANISOU 5877  CE  MET A 383     7129   6181   5651   -134  -1293    600       C  
ATOM   5878  H   MET A 383      -7.409 -57.174  33.076  1.00 84.98           H  
ATOM   5879  HA  MET A 383      -6.930 -59.149  34.714  1.00 76.61           H  
ATOM   5880  HB2 MET A 383      -8.340 -59.258  32.812  1.00 59.81           H  
ATOM   5881  HB3 MET A 383      -7.038 -59.273  31.906  1.00 59.81           H  
ATOM   5882  HG2 MET A 383      -6.557 -61.334  32.430  1.00 54.73           H  
ATOM   5883  HG3 MET A 383      -7.380 -61.269  33.800  1.00 54.73           H  
ATOM   5884  HE1 MET A 383      -9.161 -62.807  33.942  1.00 59.88           H  
ATOM   5885  HE2 MET A 383      -9.786 -63.573  32.698  1.00 59.88           H  
ATOM   5886  HE3 MET A 383      -8.220 -63.631  32.961  1.00 59.88           H  
ATOM   5887  N   ASP A 384      -4.547 -58.380  32.721  1.00149.03           N  
ANISOU 5887  N   ASP A 384    19913  18484  18226   -647  -1892    469       N  
ATOM   5888  CA  ASP A 384      -3.118 -58.529  32.445  1.00151.05           C  
ANISOU 5888  CA  ASP A 384    20021  18764  18608   -775  -1998    536       C  
ATOM   5889  C   ASP A 384      -2.691 -59.933  32.014  1.00141.95           C  
ANISOU 5889  C   ASP A 384    18636  17699  17599   -752  -1928    624       C  
ATOM   5890  O   ASP A 384      -1.497 -60.207  31.869  1.00143.11           O  
ANISOU 5890  O   ASP A 384    18641  17881  17853   -839  -2008    690       O  
ATOM   5891  CB  ASP A 384      -2.302 -58.096  33.661  1.00127.41           C  
ANISOU 5891  CB  ASP A 384    17127  15755  15526   -853  -2189    545       C  
ATOM   5892  CG  ASP A 384      -2.300 -56.601  33.840  1.00128.37           C  
ANISOU 5892  CG  ASP A 384    17452  15774  15549   -921  -2295    468       C  
ATOM   5893  OD1 ASP A 384      -2.272 -55.879  32.818  1.00128.01           O  
ANISOU 5893  OD1 ASP A 384    17394  15674  15569   -974  -2268    444       O  
ATOM   5894  OD2 ASP A 384      -2.334 -56.136  34.996  1.00129.57           O  
ANISOU 5894  OD2 ASP A 384    17784  15893  15554   -920  -2407    430       O  
ATOM   5895  H   ASP A 384      -4.943 -57.820  32.201  1.00178.83           H  
ATOM   5896  HA  ASP A 384      -2.889 -57.928  31.719  1.00181.26           H  
ATOM   5897  HB2 ASP A 384      -2.683 -58.495  34.459  1.00152.89           H  
ATOM   5898  HB3 ASP A 384      -1.383 -58.387  33.548  1.00152.89           H  
ATOM   5899  N   GLY A 385      -3.658 -60.817  31.809  1.00 63.93           N  
ANISOU 5899  N   GLY A 385     8715   7852   7724   -634  -1783    626       N  
ATOM   5900  CA  GLY A 385      -3.366 -62.148  31.318  1.00 59.34           C  
ANISOU 5900  CA  GLY A 385     7932   7337   7279   -602  -1710    699       C  
ATOM   5901  C   GLY A 385      -2.722 -62.110  29.946  1.00 66.61           C  
ANISOU 5901  C   GLY A 385     8698   8260   8351   -661  -1667    716       C  
ATOM   5902  O   GLY A 385      -1.720 -62.784  29.706  1.00 70.57           O  
ANISOU 5902  O   GLY A 385     9030   8810   8971   -697  -1695    783       O  
ATOM   5903  H   GLY A 385      -4.493 -60.668  31.949  1.00 76.72           H  
ATOM   5904  HA2 GLY A 385      -2.762 -62.596  31.931  1.00 71.21           H  
ATOM   5905  HA3 GLY A 385      -4.187 -62.661  31.261  1.00 71.21           H  
ATOM   5906  N   THR A 386      -3.303 -61.325  29.041  1.00 60.73           N  
ANISOU 5906  N   THR A 386     8008   7464   7600   -665  -1594    657       N  
ATOM   5907  CA  THR A 386      -2.791 -61.216  27.681  1.00 55.29           C  
ANISOU 5907  CA  THR A 386     7188   6780   7040   -718  -1541    670       C  
ATOM   5908  C   THR A 386      -3.174 -59.877  27.043  1.00 53.72           C  
ANISOU 5908  C   THR A 386     7107   6507   6796   -766  -1536    605       C  
ATOM   5909  O   THR A 386      -4.311 -59.419  27.171  1.00 51.97           O  
ANISOU 5909  O   THR A 386     7033   6238   6476   -700  -1485    542       O  
ATOM   5910  CB  THR A 386      -3.311 -62.375  26.806  1.00 55.51           C  
ANISOU 5910  CB  THR A 386     7089   6846   7158   -627  -1388    687       C  
ATOM   5911  OG1 THR A 386      -2.946 -63.628  27.399  1.00 51.99           O  
ANISOU 5911  OG1 THR A 386     6540   6457   6758   -581  -1400    749       O  
ATOM   5912  CG2 THR A 386      -2.727 -62.299  25.406  1.00 60.50           C  
ANISOU 5912  CG2 THR A 386     7586   7490   7911   -677  -1331    700       C  
ATOM   5913  H   THR A 386      -3.998 -60.843  29.193  1.00 72.87           H  
ATOM   5914  HA  THR A 386      -1.823 -61.270  27.704  1.00 66.35           H  
ATOM   5915  HB  THR A 386      -4.277 -62.319  26.738  1.00 66.62           H  
ATOM   5916  HG1 THR A 386      -3.227 -64.263  26.925  1.00 62.39           H  
ATOM   5917 HG21 THR A 386      -1.760 -62.353  25.446  1.00 72.60           H  
ATOM   5918 HG22 THR A 386      -3.062 -63.032  24.867  1.00 72.60           H  
ATOM   5919 HG23 THR A 386      -2.978 -61.460  24.987  1.00 72.60           H  
ATOM   5920  N   GLU A 387      -2.212 -59.264  26.354  1.00 81.16           N  
ANISOU 5920  N   GLU A 387    10513   9977  10349   -880  -1588    629       N  
ATOM   5921  CA  GLU A 387      -2.400 -57.969  25.697  1.00 84.58           C  
ANISOU 5921  CA  GLU A 387    11048  10336  10754   -946  -1599    582       C  
ATOM   5922  C   GLU A 387      -2.509 -58.128  24.175  1.00 85.12           C  
ANISOU 5922  C   GLU A 387    10999  10421  10921   -944  -1471    590       C  
ATOM   5923  O   GLU A 387      -2.919 -57.205  23.464  1.00 87.77           O  
ANISOU 5923  O   GLU A 387    11416  10697  11236   -974  -1446    551       O  
ATOM   5924  CB  GLU A 387      -1.235 -57.041  26.051  1.00 88.18           C  
ANISOU 5924  CB  GLU A 387    11524  10766  11213  -1096  -1767    610       C  
ATOM   5925  CG  GLU A 387      -1.478 -55.569  25.739  1.00 88.57           C  
ANISOU 5925  CG  GLU A 387    11734  10714  11203  -1168  -1820    557       C  
ATOM   5926  CD  GLU A 387      -1.032 -55.168  24.341  1.00 88.02           C  
ANISOU 5926  CD  GLU A 387    11558  10648  11237  -1251  -1771    588       C  
ATOM   5927  OE1 GLU A 387       0.033 -55.640  23.887  1.00 84.96           O  
ANISOU 5927  OE1 GLU A 387    10978  10338  10965  -1320  -1776    667       O  
ATOM   5928  OE2 GLU A 387      -1.750 -54.376  23.696  1.00 83.51           O  
ANISOU 5928  OE2 GLU A 387    11094  10006  10631  -1245  -1724    538       O  
ATOM   5929  H   GLU A 387      -1.422 -59.587  26.250  1.00 97.40           H  
ATOM   5930  HA  GLU A 387      -3.221 -57.564  26.020  1.00101.50           H  
ATOM   5931  HB2 GLU A 387      -1.059 -57.114  27.003  1.00105.81           H  
ATOM   5932  HB3 GLU A 387      -0.453 -57.322  25.552  1.00105.81           H  
ATOM   5933  HG2 GLU A 387      -2.427 -55.384  25.813  1.00106.28           H  
ATOM   5934  HG3 GLU A 387      -0.986 -55.027  26.375  1.00106.28           H  
ATOM   5935  N   GLU A 388      -2.122 -59.301  23.683  1.00 64.58           N  
ANISOU 5935  N   GLU A 388     8214   7898   8425   -907  -1393    641       N  
ATOM   5936  CA  GLU A 388      -2.313 -59.671  22.282  1.00 59.57           C  
ANISOU 5936  CA  GLU A 388     7473   7288   7874   -881  -1258    644       C  
ATOM   5937  C   GLU A 388      -3.769 -59.414  21.878  1.00 60.22           C  
ANISOU 5937  C   GLU A 388     7682   7314   7886   -798  -1160    575       C  
ATOM   5938  O   GLU A 388      -4.061 -58.789  20.844  1.00 62.71           O  
ANISOU 5938  O   GLU A 388     8018   7597   8211   -824  -1106    552       O  
ATOM   5939  CB  GLU A 388      -1.945 -61.151  22.107  1.00 49.21           C  
ANISOU 5939  CB  GLU A 388     5984   6055   6657   -812  -1189    692       C  
ATOM   5940  CG  GLU A 388      -2.234 -61.766  20.742  1.00 55.04           C  
ANISOU 5940  CG  GLU A 388     6622   6818   7471   -760  -1043    687       C  
ATOM   5941  CD  GLU A 388      -1.236 -61.348  19.682  1.00 70.00           C  
ANISOU 5941  CD  GLU A 388     8400   8750   9448   -850  -1031    723       C  
ATOM   5942  OE1 GLU A 388      -1.350 -60.216  19.168  1.00 74.70           O  
ANISOU 5942  OE1 GLU A 388     9072   9302  10010   -925  -1044    702       O  
ATOM   5943  OE2 GLU A 388      -0.341 -62.159  19.356  1.00 72.58           O  
ANISOU 5943  OE2 GLU A 388     8556   9149   9871   -842  -1005    776       O  
ATOM   5944  H   GLU A 388      -1.739 -59.913  24.151  1.00 77.49           H  
ATOM   5945  HA  GLU A 388      -1.733 -59.136  21.718  1.00 71.49           H  
ATOM   5946  HB2 GLU A 388      -0.994 -61.249  22.271  1.00 59.05           H  
ATOM   5947  HB3 GLU A 388      -2.439 -61.666  22.764  1.00 59.05           H  
ATOM   5948  HG2 GLU A 388      -2.201 -62.733  20.818  1.00 66.04           H  
ATOM   5949  HG3 GLU A 388      -3.115 -61.486  20.449  1.00 66.04           H  
ATOM   5950  N   LEU A 389      -4.680 -59.888  22.722  1.00 38.82           N  
ANISOU 5950  N   LEU A 389     5053   4595   5102   -700  -1141    549       N  
ATOM   5951  CA  LEU A 389      -6.107 -59.660  22.536  1.00 32.39           C  
ANISOU 5951  CA  LEU A 389     4356   3735   4215   -614  -1057    491       C  
ATOM   5952  C   LEU A 389      -6.418 -58.167  22.484  1.00 31.65           C  
ANISOU 5952  C   LEU A 389     4424   3559   4042   -662  -1109    438       C  
ATOM   5953  O   LEU A 389      -7.251 -57.727  21.695  1.00 28.36           O  
ANISOU 5953  O   LEU A 389     4061   3103   3611   -631  -1036    402       O  
ATOM   5954  CB  LEU A 389      -6.895 -60.304  23.676  1.00 36.12           C  
ANISOU 5954  CB  LEU A 389     4892   4222   4611   -515  -1049    484       C  
ATOM   5955  CG  LEU A 389      -6.820 -61.828  23.761  1.00 35.33           C  
ANISOU 5955  CG  LEU A 389     4653   4188   4581   -453   -994    535       C  
ATOM   5956  CD1 LEU A 389      -7.426 -62.318  25.064  1.00 36.05           C  
ANISOU 5956  CD1 LEU A 389     4817   4296   4586   -380  -1013    542       C  
ATOM   5957  CD2 LEU A 389      -7.527 -62.469  22.577  1.00 34.07           C  
ANISOU 5957  CD2 LEU A 389     4422   4035   4487   -397   -862    529       C  
ATOM   5958  H   LEU A 389      -4.492 -60.352  23.421  1.00 46.58           H  
ATOM   5959  HA  LEU A 389      -6.392 -60.062  21.701  1.00 38.87           H  
ATOM   5960  HB2 LEU A 389      -6.561 -59.950  24.516  1.00 43.35           H  
ATOM   5961  HB3 LEU A 389      -7.829 -60.065  23.574  1.00 43.35           H  
ATOM   5962  HG  LEU A 389      -5.890 -62.102  23.740  1.00 42.39           H  
ATOM   5963 HD11 LEU A 389      -8.354 -62.040  25.104  1.00 43.26           H  
ATOM   5964 HD12 LEU A 389      -7.367 -63.285  25.095  1.00 43.26           H  
ATOM   5965 HD13 LEU A 389      -6.932 -61.932  25.805  1.00 43.26           H  
ATOM   5966 HD21 LEU A 389      -7.098 -62.175  21.758  1.00 40.88           H  
ATOM   5967 HD22 LEU A 389      -7.464 -63.433  22.657  1.00 40.88           H  
ATOM   5968 HD23 LEU A 389      -8.457 -62.196  22.580  1.00 40.88           H  
ATOM   5969  N   LEU A 390      -5.747 -57.392  23.333  1.00 43.38           N  
ANISOU 5969  N   LEU A 390     5992   5013   5476   -737  -1244    436       N  
ATOM   5970  CA  LEU A 390      -5.942 -55.943  23.366  1.00 43.73           C  
ANISOU 5970  CA  LEU A 390     6206   4965   5445   -789  -1315    385       C  
ATOM   5971  C   LEU A 390      -5.504 -55.294  22.057  1.00 51.21           C  
ANISOU 5971  C   LEU A 390     7101   5888   6468   -882  -1299    400       C  
ATOM   5972  O   LEU A 390      -6.188 -54.409  21.536  1.00 43.03           O  
ANISOU 5972  O   LEU A 390     6178   4780   5392   -876  -1278    356       O  
ATOM   5973  CB  LEU A 390      -5.195 -55.316  24.546  1.00 34.39           C  
ANISOU 5973  CB  LEU A 390     5121   3750   4196   -863  -1479    384       C  
ATOM   5974  CG  LEU A 390      -5.987 -55.255  25.851  1.00 46.85           C  
ANISOU 5974  CG  LEU A 390     6863   5304   5635   -768  -1508    332       C  
ATOM   5975  CD1 LEU A 390      -5.067 -55.037  27.045  1.00 56.15           C  
ANISOU 5975  CD1 LEU A 390     8094   6478   6762   -840  -1669    348       C  
ATOM   5976  CD2 LEU A 390      -7.035 -54.154  25.777  1.00 35.21           C  
ANISOU 5976  CD2 LEU A 390     5583   3735   4061   -716  -1490    252       C  
ATOM   5977  H   LEU A 390      -5.171 -57.681  23.903  1.00 52.05           H  
ATOM   5978  HA  LEU A 390      -6.887 -55.760  23.484  1.00 52.48           H  
ATOM   5979  HB2 LEU A 390      -4.393 -55.836  24.714  1.00 41.27           H  
ATOM   5980  HB3 LEU A 390      -4.951 -54.408  24.309  1.00 41.27           H  
ATOM   5981  HG  LEU A 390      -6.449 -56.098  25.980  1.00 56.23           H  
ATOM   5982 HD11 LEU A 390      -4.591 -54.200  26.927  1.00 67.38           H  
ATOM   5983 HD12 LEU A 390      -5.602 -55.003  27.853  1.00 67.38           H  
ATOM   5984 HD13 LEU A 390      -4.437 -55.773  27.095  1.00 67.38           H  
ATOM   5985 HD21 LEU A 390      -7.640 -54.343  25.042  1.00 42.26           H  
ATOM   5986 HD22 LEU A 390      -7.527 -54.129  26.613  1.00 42.26           H  
ATOM   5987 HD23 LEU A 390      -6.591 -53.304  25.630  1.00 42.26           H  
ATOM   5988  N   VAL A 391      -4.362 -55.731  21.536  1.00 50.48           N  
ANISOU 5988  N   VAL A 391     6837   5859   6483   -965  -1309    467       N  
ATOM   5989  CA  VAL A 391      -3.924 -55.302  20.214  1.00 42.81           C  
ANISOU 5989  CA  VAL A 391     5788   4890   5588  -1047  -1271    495       C  
ATOM   5990  C   VAL A 391      -5.046 -55.590  19.222  1.00 43.89           C  
ANISOU 5990  C   VAL A 391     5928   5020   5727   -953  -1125    461       C  
ATOM   5991  O   VAL A 391      -5.533 -54.676  18.537  1.00 46.04           O  
ANISOU 5991  O   VAL A 391     6292   5229   5973   -976  -1110    432       O  
ATOM   5992  CB  VAL A 391      -2.625 -56.027  19.784  1.00 48.99           C  
ANISOU 5992  CB  VAL A 391     6355   5770   6490  -1114  -1268    576       C  
ATOM   5993  CG1 VAL A 391      -2.281 -55.736  18.327  1.00 47.85           C  
ANISOU 5993  CG1 VAL A 391     6119   5646   6417  -1178  -1196    607       C  
ATOM   5994  CG2 VAL A 391      -1.476 -55.621  20.688  1.00 47.11           C  
ANISOU 5994  CG2 VAL A 391     6107   5536   6256  -1224  -1426    620       C  
ATOM   5995  H   VAL A 391      -3.823 -56.275  21.928  1.00 60.57           H  
ATOM   5996  HA  VAL A 391      -3.755 -54.347  20.221  1.00 51.37           H  
ATOM   5997  HB  VAL A 391      -2.753 -56.984  19.875  1.00 58.79           H  
ATOM   5998 HG11 VAL A 391      -2.155 -54.780  18.217  1.00 57.42           H  
ATOM   5999 HG12 VAL A 391      -1.464 -56.205  18.095  1.00 57.42           H  
ATOM   6000 HG13 VAL A 391      -3.009 -56.041  17.763  1.00 57.42           H  
ATOM   6001 HG21 VAL A 391      -1.693 -55.863  21.601  1.00 56.53           H  
ATOM   6002 HG22 VAL A 391      -0.673 -56.084  20.404  1.00 56.53           H  
ATOM   6003 HG23 VAL A 391      -1.347 -54.662  20.621  1.00 56.53           H  
ATOM   6004  N   LYS A 392      -5.479 -56.850  19.176  1.00 46.69           N  
ANISOU 6004  N   LYS A 392     6192   5437   6112   -850  -1027    465       N  
ATOM   6005  CA  LYS A 392      -6.575 -57.232  18.284  1.00 37.55           C  
ANISOU 6005  CA  LYS A 392     5034   4276   4958   -762   -896    437       C  
ATOM   6006  C   LYS A 392      -7.802 -56.349  18.470  1.00 36.63           C  
ANISOU 6006  C   LYS A 392     5098   4076   4743   -710   -894    375       C  
ATOM   6007  O   LYS A 392      -8.457 -55.970  17.501  1.00 31.89           O  
ANISOU 6007  O   LYS A 392     4528   3445   4144   -697   -830    355       O  
ATOM   6008  CB  LYS A 392      -6.985 -58.686  18.502  1.00 41.53           C  
ANISOU 6008  CB  LYS A 392     5448   4839   5491   -657   -817    447       C  
ATOM   6009  CG  LYS A 392      -6.116 -59.701  17.792  1.00 37.84           C  
ANISOU 6009  CG  LYS A 392     4796   4449   5134   -670   -765    496       C  
ATOM   6010  CD  LYS A 392      -6.960 -60.833  17.228  1.00 43.35           C  
ANISOU 6010  CD  LYS A 392     5442   5168   5861   -566   -647    486       C  
ATOM   6011  CE  LYS A 392      -6.097 -61.986  16.750  1.00 49.08           C  
ANISOU 6011  CE  LYS A 392     5998   5963   6688   -555   -604    527       C  
ATOM   6012  NZ  LYS A 392      -5.347 -62.617  17.871  1.00 51.17           N  
ANISOU 6012  NZ  LYS A 392     6201   6265   6974   -551   -675    567       N  
ATOM   6013  H   LYS A 392      -5.160 -57.496  19.646  1.00 56.03           H  
ATOM   6014  HA  LYS A 392      -6.278 -57.140  17.365  1.00 45.06           H  
ATOM   6015  HB2 LYS A 392      -6.946 -58.879  19.452  1.00 49.83           H  
ATOM   6016  HB3 LYS A 392      -7.893 -58.803  18.183  1.00 49.83           H  
ATOM   6017  HG2 LYS A 392      -5.651 -59.270  17.058  1.00 45.41           H  
ATOM   6018  HG3 LYS A 392      -5.480 -60.077  18.421  1.00 45.41           H  
ATOM   6019  HD2 LYS A 392      -7.554 -61.165  17.920  1.00 52.02           H  
ATOM   6020  HD3 LYS A 392      -7.474 -60.504  16.474  1.00 52.02           H  
ATOM   6021  HE2 LYS A 392      -6.663 -62.661  16.345  1.00 58.90           H  
ATOM   6022  HE3 LYS A 392      -5.454 -61.656  16.103  1.00 58.90           H  
ATOM   6023  HZ1 LYS A 392      -5.917 -62.933  18.478  1.00 61.40           H  
ATOM   6024  HZ2 LYS A 392      -4.850 -63.289  17.565  1.00 61.40           H  
ATOM   6025  HZ3 LYS A 392      -4.816 -62.017  18.258  1.00 61.40           H  
ATOM   6026  N   LEU A 393      -8.113 -56.035  19.721  1.00 41.53           N  
ANISOU 6026  N   LEU A 393     5839   4663   5276   -675   -965    346       N  
ATOM   6027  CA  LEU A 393      -9.254 -55.188  20.028  1.00 43.96           C  
ANISOU 6027  CA  LEU A 393     6323   4897   5485   -610   -964    285       C  
ATOM   6028  C   LEU A 393      -9.042 -53.815  19.400  1.00 51.79           C  
ANISOU 6028  C   LEU A 393     7409   5803   6465   -698  -1021    266       C  
ATOM   6029  O   LEU A 393      -9.945 -53.263  18.767  1.00 47.59           O  
ANISOU 6029  O   LEU A 393     6954   5221   5909   -655   -970    234       O  
ATOM   6030  CB  LEU A 393      -9.432 -55.063  21.543  1.00 40.41           C  
ANISOU 6030  CB  LEU A 393     5989   4433   4934   -563  -1038    257       C  
ATOM   6031  CG  LEU A 393     -10.755 -54.496  22.067  1.00 41.18           C  
ANISOU 6031  CG  LEU A 393     6252   4477   4918   -451  -1010    195       C  
ATOM   6032  CD1 LEU A 393     -10.965 -54.971  23.489  1.00 34.11           C  
ANISOU 6032  CD1 LEU A 393     5407   3615   3937   -380  -1037    188       C  
ATOM   6033  CD2 LEU A 393     -10.803 -52.983  22.012  1.00 37.83           C  
ANISOU 6033  CD2 LEU A 393     5999   3943   4433   -493  -1090    144       C  
ATOM   6034  H   LEU A 393      -7.676 -56.301  20.413  1.00 49.83           H  
ATOM   6035  HA  LEU A 393     -10.059 -55.578  19.653  1.00 52.76           H  
ATOM   6036  HB2 LEU A 393      -9.331 -55.947  21.929  1.00 48.50           H  
ATOM   6037  HB3 LEU A 393      -8.726 -54.489  21.880  1.00 48.50           H  
ATOM   6038  HG  LEU A 393     -11.483 -54.840  21.525  1.00 49.42           H  
ATOM   6039 HD11 LEU A 393     -10.230 -54.656  24.038  1.00 40.93           H  
ATOM   6040 HD12 LEU A 393     -11.803 -54.612  23.821  1.00 40.93           H  
ATOM   6041 HD13 LEU A 393     -10.994 -55.940  23.498  1.00 40.93           H  
ATOM   6042 HD21 LEU A 393     -10.696 -52.697  21.092  1.00 45.40           H  
ATOM   6043 HD22 LEU A 393     -11.659 -52.682  22.355  1.00 45.40           H  
ATOM   6044 HD23 LEU A 393     -10.085 -52.625  22.556  1.00 45.40           H  
ATOM   6045  N   ASN A 394      -7.838 -53.274  19.565  1.00 77.86           N  
ANISOU 6045  N   ASN A 394    10702   9091   9792   -824  -1132    294       N  
ATOM   6046  CA  ASN A 394      -7.490 -51.989  18.970  1.00 82.48           C  
ANISOU 6046  CA  ASN A 394    11367   9593  10376   -930  -1200    291       C  
ATOM   6047  C   ASN A 394      -7.695 -52.022  17.461  1.00 82.34           C  
ANISOU 6047  C   ASN A 394    11268   9592  10426   -947  -1100    314       C  
ATOM   6048  O   ASN A 394      -8.314 -51.117  16.901  1.00 78.74           O  
ANISOU 6048  O   ASN A 394    10921   9057   9938   -946  -1096    286       O  
ATOM   6049  CB  ASN A 394      -6.043 -51.612  19.305  1.00 80.08           C  
ANISOU 6049  CB  ASN A 394    11022   9293  10110  -1079  -1331    340       C  
ATOM   6050  CG  ASN A 394      -5.784 -50.119  19.187  1.00 86.43           C  
ANISOU 6050  CG  ASN A 394    11973   9984  10881  -1187  -1447    327       C  
ATOM   6051  OD1 ASN A 394      -5.672 -49.579  18.085  1.00 90.10           O  
ANISOU 6051  OD1 ASN A 394    12417  10425  11390  -1255  -1424    352       O  
ATOM   6052  ND2 ASN A 394      -5.678 -49.445  20.328  1.00 84.65           N  
ANISOU 6052  ND2 ASN A 394    11904   9685  10574  -1204  -1578    289       N  
ATOM   6053  H   ASN A 394      -7.202 -53.634  20.020  1.00 93.43           H  
ATOM   6054  HA  ASN A 394      -8.071 -51.304  19.337  1.00 98.97           H  
ATOM   6055  HB2 ASN A 394      -5.849 -51.879  20.217  1.00 96.09           H  
ATOM   6056  HB3 ASN A 394      -5.447 -52.069  18.691  1.00 96.09           H  
ATOM   6057 HD21 ASN A 394      -5.755 -49.857  21.079  1.00101.58           H  
ATOM   6058 HD22 ASN A 394      -5.531 -48.598  20.315  1.00101.58           H  
ATOM   6059  N   ARG A 395      -7.198 -53.069  16.804  1.00 81.10           N  
ANISOU 6059  N   ARG A 395    10925   9532  10356   -954  -1020    364       N  
ATOM   6060  CA  ARG A 395      -7.431 -53.213  15.363  1.00 74.49           C  
ANISOU 6060  CA  ARG A 395    10013   8719   9571   -959   -916    382       C  
ATOM   6061  C   ARG A 395      -8.896 -53.473  15.026  1.00 72.44           C  
ANISOU 6061  C   ARG A 395     9813   8438   9273   -831   -818    335       C  
ATOM   6062  O   ARG A 395      -9.286 -53.412  13.861  1.00 71.84           O  
ANISOU 6062  O   ARG A 395     9714   8361   9220   -830   -745    340       O  
ATOM   6063  CB  ARG A 395      -6.590 -54.344  14.769  1.00 71.94           C  
ANISOU 6063  CB  ARG A 395     9486   8506   9342   -978   -847    437       C  
ATOM   6064  CG  ARG A 395      -5.123 -54.003  14.590  1.00 79.21           C  
ANISOU 6064  CG  ARG A 395    10312   9464  10323  -1118   -916    502       C  
ATOM   6065  CD  ARG A 395      -4.253 -54.842  15.505  1.00 87.78           C  
ANISOU 6065  CD  ARG A 395    11287  10619  11447  -1119   -960    535       C  
ATOM   6066  NE  ARG A 395      -3.881 -56.120  14.898  1.00 88.36           N  
ANISOU 6066  NE  ARG A 395    11180  10794  11600  -1070   -856    568       N  
ATOM   6067  CZ  ARG A 395      -2.679 -56.407  14.401  1.00 88.59           C  
ANISOU 6067  CZ  ARG A 395    11048  10903  11711  -1141   -847    633       C  
ATOM   6068  NH1 ARG A 395      -1.695 -55.514  14.432  1.00 79.15           N  
ANISOU 6068  NH1 ARG A 395     9834   9705  10534  -1278   -942    684       N  
ATOM   6069  NH2 ARG A 395      -2.456 -57.603  13.872  1.00 92.77           N  
ANISOU 6069  NH2 ARG A 395    11431  11515  12304  -1073   -746    650       N  
ATOM   6070  H   ARG A 395      -6.732 -53.699  17.159  1.00 97.32           H  
ATOM   6071  HA  ARG A 395      -7.170 -52.389  14.923  1.00 89.39           H  
ATOM   6072  HB2 ARG A 395      -6.645 -55.113  15.357  1.00 86.33           H  
ATOM   6073  HB3 ARG A 395      -6.948 -54.572  13.897  1.00 86.33           H  
ATOM   6074  HG2 ARG A 395      -4.861 -54.179  13.673  1.00 95.06           H  
ATOM   6075  HG3 ARG A 395      -4.982 -53.068  14.807  1.00 95.06           H  
ATOM   6076  HD2 ARG A 395      -3.439 -54.354  15.704  1.00105.34           H  
ATOM   6077  HD3 ARG A 395      -4.739 -55.027  16.324  1.00105.34           H  
ATOM   6078  HE  ARG A 395      -4.484 -56.732  14.860  1.00106.04           H  
ATOM   6079 HH11 ARG A 395      -1.831 -54.736  14.773  1.00 94.98           H  
ATOM   6080 HH12 ARG A 395      -0.924 -55.713  14.109  1.00 94.98           H  
ATOM   6081 HH21 ARG A 395      -3.086 -58.188  13.849  1.00111.33           H  
ATOM   6082 HH22 ARG A 395      -1.681 -57.794  13.551  1.00111.33           H  
ATOM   6083  N   GLU A 396      -9.703 -53.762  16.043  1.00 55.64           N  
ANISOU 6083  N   GLU A 396     7758   6298   7083   -727   -818    295       N  
ATOM   6084  CA  GLU A 396     -11.104 -54.114  15.839  1.00 48.80           C  
ANISOU 6084  CA  GLU A 396     6929   5427   6186   -603   -725    262       C  
ATOM   6085  C   GLU A 396     -11.196 -55.410  15.039  1.00 44.82           C  
ANISOU 6085  C   GLU A 396     6270   5004   5755   -567   -618    292       C  
ATOM   6086  O   GLU A 396     -12.046 -55.560  14.160  1.00 43.70           O  
ANISOU 6086  O   GLU A 396     6124   4858   5621   -521   -540    283       O  
ATOM   6087  CB  GLU A 396     -11.855 -52.981  15.135  1.00 37.11           C  
ANISOU 6087  CB  GLU A 396     5569   3862   4668   -601   -723    234       C  
ATOM   6088  CG  GLU A 396     -11.356 -51.598  15.519  1.00 49.92           C  
ANISOU 6088  CG  GLU A 396     7328   5392   6247   -683   -844    217       C  
ATOM   6089  CD  GLU A 396     -12.270 -50.487  15.048  1.00 50.59           C  
ANISOU 6089  CD  GLU A 396     7557   5379   6284   -652   -848    181       C  
ATOM   6090  OE1 GLU A 396     -13.180 -50.759  14.236  1.00 63.25           O  
ANISOU 6090  OE1 GLU A 396     9136   6997   7901   -586   -757    179       O  
ATOM   6091  OE2 GLU A 396     -12.075 -49.336  15.493  1.00 53.80           O  
ANISOU 6091  OE2 GLU A 396     8108   5691   6641   -695   -950    155       O  
ATOM   6092  H   GLU A 396      -9.460 -53.761  16.868  1.00 66.76           H  
ATOM   6093  HA  GLU A 396     -11.522 -54.262  16.701  1.00 58.56           H  
ATOM   6094  HB2 GLU A 396     -11.749 -53.081  14.177  1.00 44.53           H  
ATOM   6095  HB3 GLU A 396     -12.795 -53.034  15.370  1.00 44.53           H  
ATOM   6096  HG2 GLU A 396     -11.292 -51.543  16.485  1.00 59.90           H  
ATOM   6097  HG3 GLU A 396     -10.483 -51.456  15.120  1.00 59.90           H  
ATOM   6098  N   ASP A 397     -10.306 -56.344  15.368  1.00 81.15           N  
ANISOU 6098  N   ASP A 397    10750   9675  10410   -588   -622    326       N  
ATOM   6099  CA  ASP A 397     -10.242 -57.645  14.708  1.00 84.57           C  
ANISOU 6099  CA  ASP A 397    11039  10179  10915   -552   -532    352       C  
ATOM   6100  C   ASP A 397     -10.355 -58.788  15.726  1.00 84.21           C  
ANISOU 6100  C   ASP A 397    10944  10178  10873   -478   -526    362       C  
ATOM   6101  O   ASP A 397     -10.098 -59.948  15.403  1.00 87.15           O  
ANISOU 6101  O   ASP A 397    11197  10605  11311   -452   -473    386       O  
ATOM   6102  CB  ASP A 397      -8.920 -57.773  13.940  1.00 92.76           C  
ANISOU 6102  CB  ASP A 397    11954  11264  12029   -646   -532    394       C  
ATOM   6103  CG  ASP A 397      -8.880 -58.997  13.039  1.00 98.85           C  
ANISOU 6103  CG  ASP A 397    12595  12096  12867   -603   -431    409       C  
ATOM   6104  OD1 ASP A 397      -9.960 -59.489  12.643  1.00 97.58           O  
ANISOU 6104  OD1 ASP A 397    12456  11924  12695   -525   -363    385       O  
ATOM   6105  OD2 ASP A 397      -7.768 -59.474  12.734  1.00100.33           O  
ANISOU 6105  OD2 ASP A 397    12659  12343  13119   -646   -424    445       O  
ATOM   6106  H   ASP A 397      -9.716 -56.244  15.985  1.00 97.38           H  
ATOM   6107  HA  ASP A 397     -10.973 -57.723  14.076  1.00101.48           H  
ATOM   6108  HB2 ASP A 397      -8.800 -56.987  13.385  1.00111.32           H  
ATOM   6109  HB3 ASP A 397      -8.191 -57.844  14.576  1.00111.32           H  
ATOM   6110  N   LEU A 398     -10.744 -58.462  16.955  1.00 24.88           N  
ANISOU 6110  N   LEU A 398     3528   2639   3285   -442   -582    343       N  
ATOM   6111  CA  LEU A 398     -10.689 -59.426  18.056  1.00 34.15           C  
ANISOU 6111  CA  LEU A 398     4664   3859   4455   -389   -595    363       C  
ATOM   6112  C   LEU A 398     -11.632 -60.630  17.930  1.00 45.95           C  
ANISOU 6112  C   LEU A 398     6102   5386   5970   -293   -505    373       C  
ATOM   6113  O   LEU A 398     -11.174 -61.771  17.861  1.00 54.85           O  
ANISOU 6113  O   LEU A 398     7115   6561   7166   -282   -481    407       O  
ATOM   6114  CB  LEU A 398     -10.928 -58.711  19.390  1.00 25.62           C  
ANISOU 6114  CB  LEU A 398     3718   2744   3271   -371   -674    338       C  
ATOM   6115  CG  LEU A 398     -11.183 -59.611  20.606  1.00 30.98           C  
ANISOU 6115  CG  LEU A 398     4388   3467   3916   -300   -680    356       C  
ATOM   6116  CD1 LEU A 398     -10.033 -60.578  20.818  1.00 26.91           C  
ANISOU 6116  CD1 LEU A 398     3738   3008   3479   -340   -711    408       C  
ATOM   6117  CD2 LEU A 398     -11.417 -58.800  21.870  1.00 29.91           C  
ANISOU 6117  CD2 LEU A 398     4404   3299   3663   -280   -755    325       C  
ATOM   6118  H   LEU A 398     -11.044 -57.688  17.180  1.00 29.85           H  
ATOM   6119  HA  LEU A 398      -9.788 -59.782  18.088  1.00 40.98           H  
ATOM   6120  HB2 LEU A 398     -10.148 -58.171  19.590  1.00 30.74           H  
ATOM   6121  HB3 LEU A 398     -11.702 -58.133  19.291  1.00 30.74           H  
ATOM   6122  HG  LEU A 398     -11.982 -60.135  20.441  1.00 37.18           H  
ATOM   6123 HD11 LEU A 398      -9.219 -60.072  20.966  1.00 32.29           H  
ATOM   6124 HD12 LEU A 398     -10.224 -61.131  21.592  1.00 32.29           H  
ATOM   6125 HD13 LEU A 398      -9.939 -61.134  20.029  1.00 32.29           H  
ATOM   6126 HD21 LEU A 398     -12.191 -58.230  21.740  1.00 35.89           H  
ATOM   6127 HD22 LEU A 398     -11.573 -59.407  22.610  1.00 35.89           H  
ATOM   6128 HD23 LEU A 398     -10.632 -58.257  22.046  1.00 35.89           H  
ATOM   6129  N   LEU A 399     -12.937 -60.378  17.933  1.00 26.14           N  
ANISOU 6129  N   LEU A 399     3674   2851   3405   -222   -460    348       N  
ATOM   6130  CA  LEU A 399     -13.931 -61.450  17.892  1.00 25.15           C  
ANISOU 6130  CA  LEU A 399     3504   2756   3297   -139   -384    366       C  
ATOM   6131  C   LEU A 399     -14.971 -61.129  16.831  1.00 27.31           C  
ANISOU 6131  C   LEU A 399     3805   3001   3571   -112   -318    346       C  
ATOM   6132  O   LEU A 399     -16.149 -60.929  17.130  1.00 27.02           O  
ANISOU 6132  O   LEU A 399     3830   2955   3480    -42   -289    338       O  
ATOM   6133  CB  LEU A 399     -14.595 -61.627  19.261  1.00 20.39           C  
ANISOU 6133  CB  LEU A 399     2960   2170   2615    -68   -397    374       C  
ATOM   6134  CG  LEU A 399     -13.768 -62.432  20.265  1.00 20.81           C  
ANISOU 6134  CG  LEU A 399     2960   2267   2682    -77   -447    411       C  
ATOM   6135  CD1 LEU A 399     -14.119 -62.050  21.690  1.00 24.78           C  
ANISOU 6135  CD1 LEU A 399     3565   2775   3074    -34   -489    406       C  
ATOM   6136  CD2 LEU A 399     -13.982 -63.923  20.050  1.00 22.39           C  
ANISOU 6136  CD2 LEU A 399     3045   2505   2955    -40   -393    457       C  
ATOM   6137  H   LEU A 399     -13.276 -59.589  17.958  1.00 31.36           H  
ATOM   6138  HA  LEU A 399     -13.497 -62.284  17.652  1.00 30.19           H  
ATOM   6139  HB2 LEU A 399     -14.753 -60.751  19.645  1.00 24.46           H  
ATOM   6140  HB3 LEU A 399     -15.440 -62.088  19.138  1.00 24.46           H  
ATOM   6141  HG  LEU A 399     -12.827 -62.240  20.126  1.00 24.98           H  
ATOM   6142 HD11 LEU A 399     -15.060 -62.230  21.842  1.00 29.73           H  
ATOM   6143 HD12 LEU A 399     -13.578 -62.577  22.300  1.00 29.73           H  
ATOM   6144 HD13 LEU A 399     -13.937 -61.106  21.818  1.00 29.73           H  
ATOM   6145 HD21 LEU A 399     -13.706 -64.154  19.149  1.00 26.86           H  
ATOM   6146 HD22 LEU A 399     -13.450 -64.414  20.696  1.00 26.86           H  
ATOM   6147 HD23 LEU A 399     -14.922 -64.128  20.171  1.00 26.86           H  
ATOM   6148  N   ARG A 400     -14.516 -61.061  15.585  1.00 33.24           N  
ANISOU 6148  N   ARG A 400     4507   3743   4380   -166   -296    342       N  
ATOM   6149  CA  ARG A 400     -15.384 -60.721  14.470  1.00 34.30           C  
ANISOU 6149  CA  ARG A 400     4667   3849   4516   -153   -244    326       C  
ATOM   6150  C   ARG A 400     -16.476 -61.754  14.273  1.00 23.29           C  
ANISOU 6150  C   ARG A 400     3230   2476   3143    -81   -180    344       C  
ATOM   6151  O   ARG A 400     -16.285 -62.941  14.540  1.00 30.99           O  
ANISOU 6151  O   ARG A 400     4124   3486   4163    -62   -166    371       O  
ATOM   6152  CB  ARG A 400     -14.580 -60.615  13.178  1.00 40.23           C  
ANISOU 6152  CB  ARG A 400     5364   4599   5323   -227   -228    325       C  
ATOM   6153  CG  ARG A 400     -13.445 -59.624  13.231  1.00 45.89           C  
ANISOU 6153  CG  ARG A 400     6106   5300   6032   -316   -291    322       C  
ATOM   6154  CD  ARG A 400     -13.945 -58.195  13.269  1.00 49.91           C  
ANISOU 6154  CD  ARG A 400     6747   5743   6473   -329   -330    294       C  
ATOM   6155  NE  ARG A 400     -14.559 -57.782  12.005  1.00 57.22           N  
ANISOU 6155  NE  ARG A 400     7696   6641   7402   -335   -285    286       N  
ATOM   6156  CZ  ARG A 400     -15.840 -57.452  11.843  1.00 54.68           C  
ANISOU 6156  CZ  ARG A 400     7446   6286   7043   -270   -259    269       C  
ATOM   6157  NH1 ARG A 400     -16.690 -57.473  12.865  1.00 55.37           N  
ANISOU 6157  NH1 ARG A 400     7586   6369   7082   -187   -263    258       N  
ATOM   6158  NH2 ARG A 400     -16.276 -57.092  10.643  1.00 50.21           N  
ANISOU 6158  NH2 ARG A 400     6896   5697   6485   -286   -227    267       N  
ATOM   6159  H   ARG A 400     -13.699 -61.210  15.359  1.00 39.89           H  
ATOM   6160  HA  ARG A 400     -15.803 -59.863  14.640  1.00 41.16           H  
ATOM   6161  HB2 ARG A 400     -14.202 -61.485  12.975  1.00 48.28           H  
ATOM   6162  HB3 ARG A 400     -15.176 -60.342  12.463  1.00 48.28           H  
ATOM   6163  HG2 ARG A 400     -12.920 -59.782  14.031  1.00 55.07           H  
ATOM   6164  HG3 ARG A 400     -12.892 -59.730  12.441  1.00 55.07           H  
ATOM   6165  HD2 ARG A 400     -14.611 -58.111  13.969  1.00 59.89           H  
ATOM   6166  HD3 ARG A 400     -13.198 -57.603  13.448  1.00 59.89           H  
ATOM   6167  HE  ARG A 400     -14.052 -57.750  11.311  1.00 68.66           H  
ATOM   6168 HH11 ARG A 400     -16.416 -57.704  13.647  1.00 66.44           H  
ATOM   6169 HH12 ARG A 400     -17.513 -57.256  12.744  1.00 66.44           H  
ATOM   6170 HH21 ARG A 400     -15.733 -57.075   9.976  1.00 60.25           H  
ATOM   6171 HH22 ARG A 400     -17.101 -56.878  10.532  1.00 60.25           H  
ATOM   6172  N   LYS A 401     -17.618 -61.280  13.794  1.00 24.34           N  
ANISOU 6172  N   LYS A 401     3416   2584   3248    -44   -149    332       N  
ATOM   6173  CA  LYS A 401     -18.738 -62.140  13.464  1.00 24.01           C  
ANISOU 6173  CA  LYS A 401     3334   2559   3229     11    -96    355       C  
ATOM   6174  C   LYS A 401     -18.739 -62.447  11.975  1.00 36.56           C  
ANISOU 6174  C   LYS A 401     4883   4137   4872    -24    -63    350       C  
ATOM   6175  O   LYS A 401     -18.064 -61.781  11.189  1.00 37.41           O  
ANISOU 6175  O   LYS A 401     5007   4224   4984    -82    -72    328       O  
ATOM   6176  CB  LYS A 401     -20.048 -61.455  13.827  1.00 25.60           C  
ANISOU 6176  CB  LYS A 401     3610   2749   3368     79    -82    353       C  
ATOM   6177  CG  LYS A 401     -20.089 -60.889  15.233  1.00 25.50           C  
ANISOU 6177  CG  LYS A 401     3668   2743   3280    121   -113    346       C  
ATOM   6178  CD  LYS A 401     -21.468 -61.062  15.835  1.00 29.90           C  
ANISOU 6178  CD  LYS A 401     4236   3329   3795    214    -72    371       C  
ATOM   6179  CE  LYS A 401     -21.790 -59.982  16.842  1.00 32.46           C  
ANISOU 6179  CE  LYS A 401     4671   3640   4021    273    -91    343       C  
ATOM   6180  NZ  LYS A 401     -23.260 -59.793  16.946  1.00 42.46           N  
ANISOU 6180  NZ  LYS A 401     5953   4926   5252    367    -38    361       N  
ATOM   6181  H   LYS A 401     -17.769 -60.445  13.649  1.00 29.21           H  
ATOM   6182  HA  LYS A 401     -18.671 -62.973  13.957  1.00 28.81           H  
ATOM   6183  HB2 LYS A 401     -20.197 -60.722  13.210  1.00 30.72           H  
ATOM   6184  HB3 LYS A 401     -20.768 -62.100  13.749  1.00 30.72           H  
ATOM   6185  HG2 LYS A 401     -19.449 -61.360  15.790  1.00 30.60           H  
ATOM   6186  HG3 LYS A 401     -19.882 -59.942  15.205  1.00 30.60           H  
ATOM   6187  HD2 LYS A 401     -22.130 -61.023  15.128  1.00 35.88           H  
ATOM   6188  HD3 LYS A 401     -21.512 -61.919  16.287  1.00 35.88           H  
ATOM   6189  HE2 LYS A 401     -21.450 -60.240  17.713  1.00 38.95           H  
ATOM   6190  HE3 LYS A 401     -21.392 -59.145  16.557  1.00 38.95           H  
ATOM   6191  HZ1 LYS A 401     -23.647 -60.552  17.207  1.00 50.95           H  
ATOM   6192  HZ2 LYS A 401     -23.444 -59.156  17.541  1.00 50.95           H  
ATOM   6193  HZ3 LYS A 401     -23.593 -59.556  16.156  1.00 50.95           H  
ATOM   6194  N   GLN A 402     -19.515 -63.450  11.588  1.00 38.65           N  
ANISOU 6194  N   GLN A 402     5098   4414   5174      9    -27    372       N  
ATOM   6195  CA  GLN A 402     -19.650 -63.804  10.184  1.00 34.01           C  
ANISOU 6195  CA  GLN A 402     4484   3812   4626    -17      1    364       C  
ATOM   6196  C   GLN A 402     -20.536 -62.801   9.454  1.00 43.43           C  
ANISOU 6196  C   GLN A 402     5744   4974   5782    -15      8    352       C  
ATOM   6197  O   GLN A 402     -20.319 -62.510   8.279  1.00 46.71           O  
ANISOU 6197  O   GLN A 402     6170   5372   6206    -57     17    335       O  
ATOM   6198  CB  GLN A 402     -20.238 -65.209  10.050  1.00 32.05           C  
ANISOU 6198  CB  GLN A 402     4174   3576   4428     12     22    392       C  
ATOM   6199  CG  GLN A 402     -19.305 -66.314  10.523  1.00 35.76           C  
ANISOU 6199  CG  GLN A 402     4576   4065   4947     10     16    403       C  
ATOM   6200  CD  GLN A 402     -18.136 -66.543   9.583  1.00 27.77           C  
ANISOU 6200  CD  GLN A 402     3530   3050   3973    -33     27    373       C  
ATOM   6201  OE1 GLN A 402     -16.991 -66.225   9.908  1.00 25.39           O  
ANISOU 6201  OE1 GLN A 402     3210   2765   3673    -60     12    365       O  
ATOM   6202  NE2 GLN A 402     -18.418 -67.110   8.415  1.00 29.81           N  
ANISOU 6202  NE2 GLN A 402     3778   3290   4258    -37     54    360       N  
ATOM   6203  H   GLN A 402     -19.976 -63.942  12.121  1.00 46.38           H  
ATOM   6204  HA  GLN A 402     -18.775 -63.799   9.766  1.00 40.81           H  
ATOM   6205  HB2 GLN A 402     -21.049 -65.260  10.579  1.00 38.46           H  
ATOM   6206  HB3 GLN A 402     -20.443 -65.374   9.116  1.00 38.46           H  
ATOM   6207  HG2 GLN A 402     -18.947 -66.075  11.392  1.00 42.91           H  
ATOM   6208  HG3 GLN A 402     -19.804 -67.143  10.587  1.00 42.91           H  
ATOM   6209 HE21 GLN A 402     -19.228 -67.327   8.226  1.00 35.77           H  
ATOM   6210 HE22 GLN A 402     -17.789 -67.261   7.847  1.00 35.77           H  
ATOM   6211  N   ARG A 403     -21.520 -62.259  10.162  1.00 93.30           N  
ANISOU 6211  N   ARG A 403    12106  11289  12055     40      3    364       N  
ATOM   6212  CA  ARG A 403     -22.521 -61.392   9.543  1.00 95.17           C  
ANISOU 6212  CA  ARG A 403    12399  11498  12263     60      8    361       C  
ATOM   6213  C   ARG A 403     -22.054 -59.939   9.436  1.00103.04           C  
ANISOU 6213  C   ARG A 403    13484  12452  13213     33    -21    328       C  
ATOM   6214  O   ARG A 403     -22.725 -59.018   9.905  1.00105.84           O  
ANISOU 6214  O   ARG A 403    13909  12785  13519     82    -33    322       O  
ATOM   6215  CB  ARG A 403     -23.863 -61.484  10.288  1.00 90.86           C  
ANISOU 6215  CB  ARG A 403    11852  10976  11695    143     24    394       C  
ATOM   6216  CG  ARG A 403     -23.751 -61.725  11.792  1.00 93.89           C  
ANISOU 6216  CG  ARG A 403    12231  11394  12049    188     22    408       C  
ATOM   6217  CD  ARG A 403     -23.708 -63.222  12.105  1.00 96.43           C  
ANISOU 6217  CD  ARG A 403    12461  11755  12422    185     36    448       C  
ATOM   6218  NE  ARG A 403     -22.650 -63.562  13.052  1.00 92.02           N  
ANISOU 6218  NE  ARG A 403    11892  11214  11859    171     15    443       N  
ATOM   6219  CZ  ARG A 403     -22.208 -64.797  13.274  1.00 87.40           C  
ANISOU 6219  CZ  ARG A 403    11234  10649  11324    156     14    470       C  
ATOM   6220  NH1 ARG A 403     -22.728 -65.831  12.623  1.00 82.52           N  
ANISOU 6220  NH1 ARG A 403    10558  10032  10765    152     31    498       N  
ATOM   6221  NH2 ARG A 403     -21.239 -65.001  14.156  1.00 80.08           N  
ANISOU 6221  NH2 ARG A 403    10300   9737  10390    146    -12    468       N  
ATOM   6222  H   ARG A 403     -21.633 -62.378  11.006  1.00111.96           H  
ATOM   6223  HA  ARG A 403     -22.675 -61.709   8.639  1.00114.20           H  
ATOM   6224  HB2 ARG A 403     -24.344 -60.652  10.161  1.00109.03           H  
ATOM   6225  HB3 ARG A 403     -24.375 -62.217   9.912  1.00109.03           H  
ATOM   6226  HG2 ARG A 403     -22.934 -61.320  12.123  1.00112.67           H  
ATOM   6227  HG3 ARG A 403     -24.523 -61.341  12.238  1.00112.67           H  
ATOM   6228  HD2 ARG A 403     -24.556 -63.490  12.492  1.00115.71           H  
ATOM   6229  HD3 ARG A 403     -23.547 -63.713  11.284  1.00115.71           H  
ATOM   6230  HE  ARG A 403     -22.288 -62.921  13.496  1.00110.43           H  
ATOM   6231 HH11 ARG A 403     -23.357 -65.705  12.050  1.00 99.02           H  
ATOM   6232 HH12 ARG A 403     -22.436 -66.625  12.774  1.00 99.02           H  
ATOM   6233 HH21 ARG A 403     -20.898 -64.336  14.581  1.00 96.10           H  
ATOM   6234 HH22 ARG A 403     -20.952 -65.798  14.303  1.00 96.10           H  
ATOM   6235  N   THR A 404     -20.899 -59.744   8.806  1.00112.21           N  
ANISOU 6235  N   THR A 404    14642  13602  14391    -45    -34    310       N  
ATOM   6236  CA  THR A 404     -20.406 -58.405   8.500  1.00112.03           C  
ANISOU 6236  CA  THR A 404    14700  13534  14334    -92    -68    289       C  
ATOM   6237  C   THR A 404     -19.458 -58.393   7.306  1.00116.49           C  
ANISOU 6237  C   THR A 404    15236  14098  14925   -179    -61    286       C  
ATOM   6238  O   THR A 404     -18.889 -59.416   6.930  1.00117.08           O  
ANISOU 6238  O   THR A 404    15229  14212  15043   -200    -32    291       O  
ATOM   6239  CB  THR A 404     -19.621 -57.784   9.685  1.00104.45           C  
ANISOU 6239  CB  THR A 404    13784  12561  13340   -104   -116    273       C  
ATOM   6240  OG1 THR A 404     -18.606 -58.695  10.128  1.00107.16           O  
ANISOU 6240  OG1 THR A 404    14047  12950  13721   -134   -116    282       O  
ATOM   6241  CG2 THR A 404     -20.535 -57.440  10.855  1.00102.13           C  
ANISOU 6241  CG2 THR A 404    13551  12260  12994    -14   -125    268       C  
ATOM   6242  H   THR A 404     -20.379 -60.376   8.542  1.00134.66           H  
ATOM   6243  HA  THR A 404     -21.158 -57.827   8.297  1.00134.44           H  
ATOM   6244  HB  THR A 404     -19.198 -56.964   9.385  1.00125.34           H  
ATOM   6245  HG1 THR A 404     -18.179 -58.360  10.769  1.00128.60           H  
ATOM   6246 HG21 THR A 404     -20.977 -58.242  11.176  1.00122.55           H  
ATOM   6247 HG22 THR A 404     -20.017 -57.055  11.578  1.00122.55           H  
ATOM   6248 HG23 THR A 404     -21.208 -56.801  10.573  1.00122.55           H  
ATOM   6249  N   PHE A 405     -19.324 -57.216   6.703  1.00 93.35           N  
ANISOU 6249  N   PHE A 405    12379  11124  11967   -225    -86    280       N  
ATOM   6250  CA  PHE A 405     -18.201 -56.892   5.833  1.00 85.30           C  
ANISOU 6250  CA  PHE A 405    11344  10106  10959   -320    -88    285       C  
ATOM   6251  C   PHE A 405     -17.940 -55.411   6.061  1.00 89.40           C  
ANISOU 6251  C   PHE A 405    11964  10565  11439   -363   -148    281       C  
ATOM   6252  O   PHE A 405     -18.872 -54.608   6.064  1.00 94.47           O  
ANISOU 6252  O   PHE A 405    12694  11153  12046   -323   -169    274       O  
ATOM   6253  CB  PHE A 405     -18.519 -57.170   4.364  1.00 87.21           C  
ANISOU 6253  CB  PHE A 405    11570  10358  11210   -341    -47    292       C  
ATOM   6254  CG  PHE A 405     -18.470 -58.628   3.989  1.00 90.61           C  
ANISOU 6254  CG  PHE A 405    11908  10839  11680   -319      4    291       C  
ATOM   6255  CD1 PHE A 405     -17.254 -59.279   3.837  1.00 84.81           C  
ANISOU 6255  CD1 PHE A 405    11097  10151  10977   -358     29    291       C  
ATOM   6256  CD2 PHE A 405     -19.638 -59.343   3.763  1.00 94.10           C  
ANISOU 6256  CD2 PHE A 405    12341  11281  12130   -259     23    293       C  
ATOM   6257  CE1 PHE A 405     -17.206 -60.618   3.486  1.00 86.87           C  
ANISOU 6257  CE1 PHE A 405    11286  10447  11273   -328     72    284       C  
ATOM   6258  CE2 PHE A 405     -19.595 -60.682   3.408  1.00 80.76           C  
ANISOU 6258  CE2 PHE A 405    10583   9625  10478   -242     58    289       C  
ATOM   6259  CZ  PHE A 405     -18.378 -61.319   3.271  1.00 82.47           C  
ANISOU 6259  CZ  PHE A 405    10735   9878  10722   -272     83    281       C  
ATOM   6260  H   PHE A 405     -19.888 -56.572   6.785  1.00112.02           H  
ATOM   6261  HA  PHE A 405     -17.416 -57.400   6.093  1.00102.36           H  
ATOM   6262  HB2 PHE A 405     -19.413 -56.845   4.172  1.00104.66           H  
ATOM   6263  HB3 PHE A 405     -17.874 -56.700   3.811  1.00104.66           H  
ATOM   6264  HD1 PHE A 405     -16.463 -58.813   3.982  1.00101.77           H  
ATOM   6265  HD2 PHE A 405     -20.460 -58.919   3.856  1.00112.92           H  
ATOM   6266  HE1 PHE A 405     -16.385 -61.044   3.392  1.00104.24           H  
ATOM   6267  HE2 PHE A 405     -20.385 -61.152   3.265  1.00 96.92           H  
ATOM   6268  HZ  PHE A 405     -18.346 -62.217   3.034  1.00 98.96           H  
ATOM   6269  N   ASP A 406     -16.680 -55.040   6.257  1.00129.12           N  
ANISOU 6269  N   ASP A 406    16982  15599  16477   -445   -180    288       N  
ATOM   6270  CA  ASP A 406     -16.364 -53.701   6.741  1.00129.04           C  
ANISOU 6270  CA  ASP A 406    17074  15522  16432   -489   -256    284       C  
ATOM   6271  C   ASP A 406     -16.636 -52.652   5.675  1.00130.09           C  
ANISOU 6271  C   ASP A 406    17285  15598  16543   -536   -271    296       C  
ATOM   6272  O   ASP A 406     -15.864 -52.496   4.729  1.00133.01           O  
ANISOU 6272  O   ASP A 406    17621  15988  16929   -627   -260    325       O  
ATOM   6273  CB  ASP A 406     -14.909 -53.621   7.188  1.00129.32           C  
ANISOU 6273  CB  ASP A 406    17065  15582  16489   -578   -296    299       C  
ATOM   6274  CG  ASP A 406     -14.567 -52.283   7.793  1.00135.70           C  
ANISOU 6274  CG  ASP A 406    17987  16312  17261   -631   -389    294       C  
ATOM   6275  OD1 ASP A 406     -15.447 -51.685   8.450  1.00127.48           O  
ANISOU 6275  OD1 ASP A 406    17056  15206  16174   -560   -423    262       O  
ATOM   6276  OD2 ASP A 406     -13.420 -51.828   7.602  1.00139.71           O  
ANISOU 6276  OD2 ASP A 406    18474  16822  17787   -742   -431    323       O  
ATOM   6277  H   ASP A 406     -15.994 -55.540   6.119  1.00154.94           H  
ATOM   6278  HA  ASP A 406     -16.925 -53.502   7.507  1.00154.85           H  
ATOM   6279  HB2 ASP A 406     -14.744 -54.304   7.856  1.00155.18           H  
ATOM   6280  HB3 ASP A 406     -14.333 -53.760   6.419  1.00155.18           H  
ATOM   6281  N   ASN A 407     -17.731 -51.921   5.858  1.00142.32           N  
ANISOU 6281  N   ASN A 407    18938  17081  18056   -470   -296    279       N  
ATOM   6282  CA  ASN A 407     -18.228 -50.992   4.852  1.00140.83           C  
ANISOU 6282  CA  ASN A 407    18828  16832  17847   -493   -311    293       C  
ATOM   6283  C   ASN A 407     -18.169 -51.592   3.455  1.00141.14           C  
ANISOU 6283  C   ASN A 407    18794  16925  17909   -535   -251    321       C  
ATOM   6284  O   ASN A 407     -17.436 -51.124   2.578  1.00145.20           O  
ANISOU 6284  O   ASN A 407    19310  17437  18422   -633   -258    351       O  
ATOM   6285  CB  ASN A 407     -17.465 -49.670   4.919  1.00143.35           C  
ANISOU 6285  CB  ASN A 407    19242  17075  18148   -585   -392    303       C  
ATOM   6286  CG  ASN A 407     -18.253 -48.575   5.627  1.00141.10           C  
ANISOU 6286  CG  ASN A 407    19104  16688  17820   -518   -457    273       C  
ATOM   6287  OD1 ASN A 407     -19.367 -48.802   6.097  1.00141.22           O  
ANISOU 6287  OD1 ASN A 407    19139  16700  17817   -396   -432    246       O  
ATOM   6288  ND2 ASN A 407     -17.678 -47.380   5.694  1.00125.11           N  
ANISOU 6288  ND2 ASN A 407    17182  14577  15777   -596   -540    278       N  
ATOM   6289  H   ASN A 407     -18.211 -51.946   6.571  1.00170.78           H  
ATOM   6290  HA  ASN A 407     -19.159 -50.801   5.046  1.00168.99           H  
ATOM   6291  HB2 ASN A 407     -16.637 -49.807   5.406  1.00172.01           H  
ATOM   6292  HB3 ASN A 407     -17.275 -49.369   4.017  1.00172.01           H  
ATOM   6293 HD21 ASN A 407     -16.900 -47.257   5.349  1.00150.13           H  
ATOM   6294 HD22 ASN A 407     -18.083 -46.729   6.084  1.00150.13           H  
ATOM   6295  N   GLY A 408     -18.949 -52.645   3.252  1.00 93.04           N  
ANISOU 6295  N   GLY A 408    12638  10880  11831   -461   -194    314       N  
ATOM   6296  CA  GLY A 408     -18.824 -53.405   2.031  1.00 94.04           C  
ANISOU 6296  CA  GLY A 408    12696  11061  11973   -494   -138    330       C  
ATOM   6297  C   GLY A 408     -20.009 -54.218   1.556  1.00 94.50           C  
ANISOU 6297  C   GLY A 408    12729  11140  12038   -420    -99    326       C  
ATOM   6298  O   GLY A 408     -20.809 -54.745   2.328  1.00 88.74           O  
ANISOU 6298  O   GLY A 408    11981  10418  11320   -335    -94    314       O  
ATOM   6299  H   GLY A 408     -19.548 -52.933   3.798  1.00111.64           H  
ATOM   6300  HA2 GLY A 408     -18.595 -52.791   1.316  1.00112.84           H  
ATOM   6301  HA3 GLY A 408     -18.081 -54.019   2.134  1.00112.84           H  
ATOM   6302  N   SER A 409     -20.097 -54.270   0.234  1.00 84.34           N  
ANISOU 6302  N   SER A 409    11443   9862  10739   -460    -77    342       N  
ATOM   6303  CA  SER A 409     -20.853 -55.258  -0.505  1.00 66.36           C  
ANISOU 6303  CA  SER A 409     9126   7617   8470   -423    -40    341       C  
ATOM   6304  C   SER A 409     -19.815 -55.722  -1.513  1.00 69.06           C  
ANISOU 6304  C   SER A 409     9424   8009   8808   -497      4    344       C  
ATOM   6305  O   SER A 409     -18.974 -54.927  -1.933  1.00 69.19           O  
ANISOU 6305  O   SER A 409     9465   8022   8804   -574     -2    362       O  
ATOM   6306  CB  SER A 409     -22.058 -54.626  -1.198  1.00 67.24           C  
ANISOU 6306  CB  SER A 409     9308   7684   8557   -398    -68    359       C  
ATOM   6307  OG  SER A 409     -22.509 -55.427  -2.276  1.00 70.16           O  
ANISOU 6307  OG  SER A 409     9652   8083   8924   -401    -41    363       O  
ATOM   6308  H   SER A 409     -19.701 -53.707  -0.281  1.00101.21           H  
ATOM   6309  HA  SER A 409     -21.129 -55.995   0.062  1.00 79.63           H  
ATOM   6310  HB2 SER A 409     -22.777 -54.532  -0.554  1.00 80.69           H  
ATOM   6311  HB3 SER A 409     -21.803 -53.755  -1.539  1.00 80.69           H  
ATOM   6312  HG  SER A 409     -23.171 -55.065  -2.646  1.00 84.20           H  
ATOM   6313  N   ILE A 410     -19.852 -56.990  -1.900  1.00 50.18           N  
ANISOU 6313  N   ILE A 410     6968   5664   6434   -472     49    327       N  
ATOM   6314  CA  ILE A 410     -18.711 -57.585  -2.587  1.00 49.25           C  
ANISOU 6314  CA  ILE A 410     6795   5602   6314   -520    102    321       C  
ATOM   6315  C   ILE A 410     -18.834 -57.542  -4.112  1.00 45.57           C  
ANISOU 6315  C   ILE A 410     6365   5148   5801   -558    128    328       C  
ATOM   6316  O   ILE A 410     -19.928 -57.646  -4.651  1.00 49.86           O  
ANISOU 6316  O   ILE A 410     6953   5666   6327   -531    109    328       O  
ATOM   6317  CB  ILE A 410     -18.497 -59.037  -2.122  1.00 52.14           C  
ANISOU 6317  CB  ILE A 410     7078   6009   6725   -467    138    293       C  
ATOM   6318  CG1 ILE A 410     -18.073 -59.039  -0.654  1.00 59.30           C  
ANISOU 6318  CG1 ILE A 410     7945   6917   7671   -445    116    293       C  
ATOM   6319  CG2 ILE A 410     -17.433 -59.725  -2.963  1.00 52.20           C  
ANISOU 6319  CG2 ILE A 410     7031   6074   6727   -496    200    281       C  
ATOM   6320  CD1 ILE A 410     -17.980 -60.405  -0.026  1.00 70.48           C  
ANISOU 6320  CD1 ILE A 410     9285   8361   9133   -389    138    274       C  
ATOM   6321  H   ILE A 410     -20.516 -57.523  -1.779  1.00 60.22           H  
ATOM   6322  HA  ILE A 410     -17.916 -57.085  -2.347  1.00 59.09           H  
ATOM   6323  HB  ILE A 410     -19.332 -59.523  -2.210  1.00 62.57           H  
ATOM   6324 HG12 ILE A 410     -17.199 -58.624  -0.584  1.00 71.16           H  
ATOM   6325 HG13 ILE A 410     -18.720 -58.526  -0.145  1.00 71.16           H  
ATOM   6326 HG21 ILE A 410     -16.598 -59.239  -2.875  1.00 62.64           H  
ATOM   6327 HG22 ILE A 410     -17.321 -60.636  -2.648  1.00 62.64           H  
ATOM   6328 HG23 ILE A 410     -17.718 -59.729  -3.891  1.00 62.64           H  
ATOM   6329 HD11 ILE A 410     -17.326 -60.932  -0.512  1.00 84.57           H  
ATOM   6330 HD12 ILE A 410     -17.706 -60.309   0.900  1.00 84.57           H  
ATOM   6331 HD13 ILE A 410     -18.849 -60.833  -0.071  1.00 84.57           H  
ATOM   6332  N   PRO A 411     -17.702 -57.364  -4.810  1.00 25.67           N  
ANISOU 6332  N   PRO A 411     3823   2673   3256   -624    169    340       N  
ATOM   6333  CA  PRO A 411     -17.645 -57.564  -6.263  1.00 32.59           C  
ANISOU 6333  CA  PRO A 411     4724   3580   4079   -654    211    341       C  
ATOM   6334  C   PRO A 411     -18.062 -58.978  -6.669  1.00 20.84           C  
ANISOU 6334  C   PRO A 411     3211   2112   2595   -592    244    298       C  
ATOM   6335  O   PRO A 411     -17.472 -59.953  -6.206  1.00 24.06           O  
ANISOU 6335  O   PRO A 411     3547   2554   3042   -556    280    271       O  
ATOM   6336  CB  PRO A 411     -16.167 -57.329  -6.588  1.00 34.52           C  
ANISOU 6336  CB  PRO A 411     4916   3889   4310   -722    263    363       C  
ATOM   6337  CG  PRO A 411     -15.688 -56.407  -5.523  1.00 41.49           C  
ANISOU 6337  CG  PRO A 411     5790   4746   5227   -760    216    391       C  
ATOM   6338  CD  PRO A 411     -16.493 -56.698  -4.295  1.00 31.60           C  
ANISOU 6338  CD  PRO A 411     4541   3445   4021   -685    168    364       C  
ATOM   6339  HA  PRO A 411     -18.193 -56.911  -6.725  1.00 39.11           H  
ATOM   6340  HB2 PRO A 411     -15.686 -58.171  -6.557  1.00 41.42           H  
ATOM   6341  HB3 PRO A 411     -16.085 -56.917  -7.462  1.00 41.42           H  
ATOM   6342  HG2 PRO A 411     -14.747 -56.571  -5.356  1.00 49.78           H  
ATOM   6343  HG3 PRO A 411     -15.825 -55.490  -5.807  1.00 49.78           H  
ATOM   6344  HD2 PRO A 411     -16.005 -57.295  -3.707  1.00 37.92           H  
ATOM   6345  HD3 PRO A 411     -16.729 -55.872  -3.844  1.00 37.92           H  
ATOM   6346  N   HIS A 412     -19.065 -59.081  -7.534  1.00 28.79           N  
ANISOU 6346  N   HIS A 412     4282   3092   3563   -582    224    295       N  
ATOM   6347  CA  HIS A 412     -19.601 -60.376  -7.949  1.00 30.08           C  
ANISOU 6347  CA  HIS A 412     4442   3259   3729   -531    235    255       C  
ATOM   6348  C   HIS A 412     -18.539 -61.303  -8.531  1.00 33.04           C  
ANISOU 6348  C   HIS A 412     4775   3692   4085   -525    312    219       C  
ATOM   6349  O   HIS A 412     -18.697 -62.530  -8.521  1.00 31.08           O  
ANISOU 6349  O   HIS A 412     4508   3442   3860   -471    324    178       O  
ATOM   6350  CB  HIS A 412     -20.712 -60.172  -8.981  1.00 36.53           C  
ANISOU 6350  CB  HIS A 412     5342   4043   4494   -542    195    265       C  
ATOM   6351  CG  HIS A 412     -20.208 -59.783 -10.336  1.00 42.66           C  
ANISOU 6351  CG  HIS A 412     6171   4853   5185   -598    231    272       C  
ATOM   6352  ND1 HIS A 412     -19.995 -60.701 -11.342  1.00 41.08           N  
ANISOU 6352  ND1 HIS A 412     5990   4684   4935   -588    274    233       N  
ATOM   6353  CD2 HIS A 412     -19.862 -58.578 -10.848  1.00 39.79           C  
ANISOU 6353  CD2 HIS A 412     5850   4496   4774   -665    231    316       C  
ATOM   6354  CE1 HIS A 412     -19.549 -60.077 -12.418  1.00 45.15           C  
ANISOU 6354  CE1 HIS A 412     6553   5233   5368   -644    305    254       C  
ATOM   6355  NE2 HIS A 412     -19.460 -58.787 -12.144  1.00 37.70           N  
ANISOU 6355  NE2 HIS A 412     5622   4276   4428   -695    279    309       N  
ATOM   6356  H   HIS A 412     -19.458 -58.409  -7.900  1.00 34.54           H  
ATOM   6357  HA  HIS A 412     -19.989 -60.816  -7.177  1.00 36.10           H  
ATOM   6358  HB2 HIS A 412     -21.208 -61.000  -9.075  1.00 43.83           H  
ATOM   6359  HB3 HIS A 412     -21.302 -59.468  -8.670  1.00 43.83           H  
ATOM   6360  HD1 HIS A 412     -20.136 -61.547 -11.281  1.00 49.30           H  
ATOM   6361  HD2 HIS A 412     -19.897 -57.760 -10.406  1.00 47.75           H  
ATOM   6362  HE1 HIS A 412     -19.333 -60.477 -13.229  1.00 54.18           H  
ATOM   6363  HE2 HIS A 412     -19.191 -58.178 -12.689  1.00 45.24           H  
ATOM   6364  N   GLN A 413     -17.456 -60.717  -9.031  1.00 26.16           N  
ANISOU 6364  N   GLN A 413     3891   2874   3176   -577    364    238       N  
ATOM   6365  CA  GLN A 413     -16.397 -61.490  -9.668  1.00 29.52           C  
ANISOU 6365  CA  GLN A 413     4273   3368   3575   -565    449    209       C  
ATOM   6366  C   GLN A 413     -15.782 -62.517  -8.711  1.00 33.65           C  
ANISOU 6366  C   GLN A 413     4703   3908   4174   -503    474    178       C  
ATOM   6367  O   GLN A 413     -15.421 -63.625  -9.125  1.00 33.86           O  
ANISOU 6367  O   GLN A 413     4710   3959   4195   -451    524    132       O  
ATOM   6368  CB  GLN A 413     -15.317 -60.554 -10.221  1.00 36.48           C  
ANISOU 6368  CB  GLN A 413     5137   4314   4411   -639    500    253       C  
ATOM   6369  CG  GLN A 413     -15.736 -59.812 -11.484  1.00 33.44           C  
ANISOU 6369  CG  GLN A 413     4846   3928   3933   -695    496    280       C  
ATOM   6370  CD  GLN A 413     -16.350 -58.450 -11.204  1.00 37.65           C  
ANISOU 6370  CD  GLN A 413     5435   4402   4468   -755    418    335       C  
ATOM   6371  OE1 GLN A 413     -16.784 -58.162 -10.088  1.00 34.20           O  
ANISOU 6371  OE1 GLN A 413     4987   3911   4097   -738    358    341       O  
ATOM   6372  NE2 GLN A 413     -16.385 -57.603 -12.224  1.00 47.46           N  
ANISOU 6372  NE2 GLN A 413     6744   5653   5634   -821    419    377       N  
ATOM   6373  H   GLN A 413     -17.310 -59.870  -9.014  1.00 31.39           H  
ATOM   6374  HA  GLN A 413     -16.776 -61.976 -10.417  1.00 35.42           H  
ATOM   6375  HB2 GLN A 413     -15.102 -59.892  -9.546  1.00 43.78           H  
ATOM   6376  HB3 GLN A 413     -14.528 -61.077 -10.432  1.00 43.78           H  
ATOM   6377  HG2 GLN A 413     -14.955 -59.678 -12.044  1.00 40.13           H  
ATOM   6378  HG3 GLN A 413     -16.394 -60.344 -11.958  1.00 40.13           H  
ATOM   6379 HE21 GLN A 413     -16.070 -57.838 -12.989  1.00 56.95           H  
ATOM   6380 HE22 GLN A 413     -16.722 -56.819 -12.120  1.00 56.95           H  
ATOM   6381  N   ILE A 414     -15.688 -62.160  -7.431  1.00 28.87           N  
ANISOU 6381  N   ILE A 414     4050   3285   3636   -505    435    201       N  
ATOM   6382  CA  ILE A 414     -15.050 -63.032  -6.444  1.00 29.31           C  
ANISOU 6382  CA  ILE A 414     4015   3358   3763   -454    451    183       C  
ATOM   6383  C   ILE A 414     -15.908 -64.273  -6.200  1.00 27.76           C  
ANISOU 6383  C   ILE A 414     3833   3116   3601   -380    426    141       C  
ATOM   6384  O   ILE A 414     -15.388 -65.374  -6.019  1.00 26.32           O  
ANISOU 6384  O   ILE A 414     3598   2948   3452   -325    459    109       O  
ATOM   6385  CB  ILE A 414     -14.788 -62.322  -5.092  1.00 29.59           C  
ANISOU 6385  CB  ILE A 414     4008   3383   3852   -477    405    218       C  
ATOM   6386  CG1 ILE A 414     -14.360 -60.865  -5.309  1.00 41.04           C  
ANISOU 6386  CG1 ILE A 414     5482   4844   5267   -565    394    267       C  
ATOM   6387  CG2 ILE A 414     -13.729 -63.093  -4.308  1.00 43.63           C  
ANISOU 6387  CG2 ILE A 414     5682   5204   5691   -442    435    211       C  
ATOM   6388  CD1 ILE A 414     -13.973 -60.122  -4.041  1.00 44.78           C  
ANISOU 6388  CD1 ILE A 414     5926   5303   5784   -595    343    298       C  
ATOM   6389  H   ILE A 414     -15.986 -61.421  -7.108  1.00 34.65           H  
ATOM   6390  HA  ILE A 414     -14.195 -63.326  -6.795  1.00 35.17           H  
ATOM   6391  HB  ILE A 414     -15.612 -62.326  -4.580  1.00 35.51           H  
ATOM   6392 HG12 ILE A 414     -13.592 -60.853  -5.902  1.00 49.25           H  
ATOM   6393 HG13 ILE A 414     -15.095 -60.384  -5.719  1.00 49.25           H  
ATOM   6394 HG21 ILE A 414     -12.910 -63.120  -4.827  1.00 52.36           H  
ATOM   6395 HG22 ILE A 414     -13.572 -62.642  -3.464  1.00 52.36           H  
ATOM   6396 HG23 ILE A 414     -14.050 -63.995  -4.148  1.00 52.36           H  
ATOM   6397 HD11 ILE A 414     -13.227 -60.579  -3.622  1.00 53.73           H  
ATOM   6398 HD12 ILE A 414     -13.718 -59.215  -4.272  1.00 53.73           H  
ATOM   6399 HD13 ILE A 414     -14.734 -60.109  -3.438  1.00 53.73           H  
ATOM   6400  N   HIS A 415     -17.224 -64.086  -6.187  1.00 20.30           N  
ANISOU 6400  N   HIS A 415     2954   2111   2648   -379    365    147       N  
ATOM   6401  CA  HIS A 415     -18.154 -65.205  -6.090  1.00 23.06           C  
ANISOU 6401  CA  HIS A 415     3321   2414   3025   -325    332    120       C  
ATOM   6402  C   HIS A 415     -18.096 -66.019  -7.374  1.00 26.41           C  
ANISOU 6402  C   HIS A 415     3792   2843   3400   -309    366     74       C  
ATOM   6403  O   HIS A 415     -18.100 -67.255  -7.344  1.00 26.29           O  
ANISOU 6403  O   HIS A 415     3767   2809   3414   -257    370     35       O  
ATOM   6404  CB  HIS A 415     -19.580 -64.707  -5.844  1.00 20.77           C  
ANISOU 6404  CB  HIS A 415     3080   2072   2737   -334    259    149       C  
ATOM   6405  CG  HIS A 415     -19.757 -64.013  -4.531  1.00 26.49           C  
ANISOU 6405  CG  HIS A 415     3772   2788   3504   -331    226    185       C  
ATOM   6406  ND1 HIS A 415     -19.268 -64.524  -3.347  1.00 22.64           N  
ANISOU 6406  ND1 HIS A 415     3216   2312   3075   -298    230    185       N  
ATOM   6407  CD2 HIS A 415     -20.369 -62.847  -4.211  1.00 20.82           C  
ANISOU 6407  CD2 HIS A 415     3089   2048   2772   -352    187    220       C  
ATOM   6408  CE1 HIS A 415     -19.569 -63.704  -2.357  1.00 17.29           C  
ANISOU 6408  CE1 HIS A 415     2536   1622   2410   -300    196    215       C  
ATOM   6409  NE2 HIS A 415     -20.238 -62.679  -2.854  1.00 27.94           N  
ANISOU 6409  NE2 HIS A 415     3949   2949   3718   -329    171    235       N  
ATOM   6410  H   HIS A 415     -17.606 -63.316  -6.234  1.00 24.36           H  
ATOM   6411  HA  HIS A 415     -17.896 -65.778  -5.350  1.00 27.67           H  
ATOM   6412  HB2 HIS A 415     -19.817 -64.081  -6.546  1.00 24.92           H  
ATOM   6413  HB3 HIS A 415     -20.184 -65.466  -5.863  1.00 24.92           H  
ATOM   6414  HD1 HIS A 415     -18.833 -65.262  -3.266  1.00 27.17           H  
ATOM   6415  HD2 HIS A 415     -20.797 -62.269  -4.800  1.00 24.98           H  
ATOM   6416  HE1 HIS A 415     -19.350 -63.828  -1.461  1.00 20.74           H  
ATOM   6417  HE2 HIS A 415     -20.542 -62.013  -2.402  1.00 33.53           H  
ATOM   6418  N   LEU A 416     -18.034 -65.315  -8.503  1.00 28.97           N  
ANISOU 6418  N   LEU A 416     4174   3189   3645   -355    388     78       N  
ATOM   6419  CA  LEU A 416     -17.923 -65.966  -9.805  1.00 27.03           C  
ANISOU 6419  CA  LEU A 416     3985   2954   3330   -341    425     32       C  
ATOM   6420  C   LEU A 416     -16.721 -66.907  -9.868  1.00 27.92           C  
ANISOU 6420  C   LEU A 416     4043   3112   3454   -286    504    -12       C  
ATOM   6421  O   LEU A 416     -16.840 -68.035 -10.346  1.00 41.48           O  
ANISOU 6421  O   LEU A 416     5796   4804   5160   -234    511    -67       O  
ATOM   6422  CB  LEU A 416     -17.811 -64.924 -10.923  1.00 39.96           C  
ANISOU 6422  CB  LEU A 416     5683   4626   4874   -404    448     56       C  
ATOM   6423  CG  LEU A 416     -18.797 -65.001 -12.097  1.00 37.50           C  
ANISOU 6423  CG  LEU A 416     5483   4281   4486   -420    409     41       C  
ATOM   6424  CD1 LEU A 416     -18.359 -64.064 -13.209  1.00 27.68           C  
ANISOU 6424  CD1 LEU A 416     4287   3088   3142   -478    452     66       C  
ATOM   6425  CD2 LEU A 416     -18.949 -66.411 -12.636  1.00 39.50           C  
ANISOU 6425  CD2 LEU A 416     5775   4509   4723   -363    414    -28       C  
ATOM   6426  H   LEU A 416     -18.054 -64.456  -8.541  1.00 34.77           H  
ATOM   6427  HA  LEU A 416     -18.723 -66.491  -9.964  1.00 32.43           H  
ATOM   6428  HB2 LEU A 416     -17.920 -64.047 -10.523  1.00 47.95           H  
ATOM   6429  HB3 LEU A 416     -16.920 -64.989 -11.301  1.00 47.95           H  
ATOM   6430  HG  LEU A 416     -19.669 -64.707 -11.791  1.00 45.01           H  
ATOM   6431 HD11 LEU A 416     -17.476 -64.326 -13.512  1.00 33.21           H  
ATOM   6432 HD12 LEU A 416     -18.992 -64.126 -13.941  1.00 33.21           H  
ATOM   6433 HD13 LEU A 416     -18.336 -63.157 -12.866  1.00 33.21           H  
ATOM   6434 HD21 LEU A 416     -19.276 -66.986 -11.926  1.00 47.40           H  
ATOM   6435 HD22 LEU A 416     -19.580 -66.402 -13.372  1.00 47.40           H  
ATOM   6436 HD23 LEU A 416     -18.084 -66.726 -12.944  1.00 47.40           H  
ATOM   6437  N   GLY A 417     -15.564 -66.444  -9.398  1.00 27.61           N  
ANISOU 6437  N   GLY A 417     3918   3136   3437   -298    558     14       N  
ATOM   6438  CA  GLY A 417     -14.371 -67.277  -9.368  1.00 26.50           C  
ANISOU 6438  CA  GLY A 417     3705   3047   3318   -239    635    -19       C  
ATOM   6439  C   GLY A 417     -14.601 -68.610  -8.679  1.00 27.20           C  
ANISOU 6439  C   GLY A 417     3773   3081   3479   -161    606    -59       C  
ATOM   6440  O   GLY A 417     -14.310 -69.676  -9.232  1.00 35.52           O  
ANISOU 6440  O   GLY A 417     4847   4130   4519    -95    644   -117       O  
ATOM   6441  H   GLY A 417     -15.447 -65.649  -9.092  1.00 33.13           H  
ATOM   6442  HA2 GLY A 417     -14.076 -67.448 -10.276  1.00 31.80           H  
ATOM   6443  HA3 GLY A 417     -13.664 -66.808  -8.899  1.00 31.80           H  
ATOM   6444  N   GLU A 418     -15.142 -68.552  -7.468  1.00 29.16           N  
ANISOU 6444  N   GLU A 418     3991   3287   3803   -167    537    -28       N  
ATOM   6445  CA  GLU A 418     -15.401 -69.758  -6.697  1.00 29.81           C  
ANISOU 6445  CA  GLU A 418     4051   3317   3959   -103    502    -51       C  
ATOM   6446  C   GLU A 418     -16.429 -70.628  -7.409  1.00 27.21           C  
ANISOU 6446  C   GLU A 418     3818   2916   3607    -81    460    -94       C  
ATOM   6447  O   GLU A 418     -16.272 -71.848  -7.476  1.00 24.55           O  
ANISOU 6447  O   GLU A 418     3489   2543   3296    -17    463   -139       O  
ATOM   6448  CB  GLU A 418     -15.886 -69.403  -5.294  1.00 21.85           C  
ANISOU 6448  CB  GLU A 418     2998   2284   3019   -122    438     -1       C  
ATOM   6449  CG  GLU A 418     -14.932 -68.509  -4.524  1.00 27.74           C  
ANISOU 6449  CG  GLU A 418     3664   3090   3787   -153    460     41       C  
ATOM   6450  CD  GLU A 418     -15.359 -68.302  -3.083  1.00 35.33           C  
ANISOU 6450  CD  GLU A 418     4592   4026   4808   -157    398     81       C  
ATOM   6451  OE1 GLU A 418     -16.186 -69.092  -2.583  1.00 38.91           O  
ANISOU 6451  OE1 GLU A 418     5059   4427   5299   -122    352     78       O  
ATOM   6452  OE2 GLU A 418     -14.862 -67.350  -2.449  1.00 39.76           O  
ANISOU 6452  OE2 GLU A 418     5115   4619   5373   -196    393    117       O  
ATOM   6453  H   GLU A 418     -15.367 -67.824  -7.070  1.00 35.00           H  
ATOM   6454  HA  GLU A 418     -14.579 -70.266  -6.614  1.00 35.77           H  
ATOM   6455  HB2 GLU A 418     -16.735 -68.939  -5.364  1.00 26.22           H  
ATOM   6456  HB3 GLU A 418     -16.000 -70.222  -4.786  1.00 26.22           H  
ATOM   6457  HG2 GLU A 418     -14.051 -68.916  -4.521  1.00 33.29           H  
ATOM   6458  HG3 GLU A 418     -14.896 -67.641  -4.955  1.00 33.29           H  
ATOM   6459  N   LEU A 419     -17.476 -69.996  -7.936  1.00 25.24           N  
ANISOU 6459  N   LEU A 419     3642   2640   3309   -134    413    -76       N  
ATOM   6460  CA  LEU A 419     -18.468 -70.695  -8.747  1.00 25.95           C  
ANISOU 6460  CA  LEU A 419     3827   2665   3366   -128    363   -111       C  
ATOM   6461  C   LEU A 419     -17.769 -71.537  -9.819  1.00 35.79           C  
ANISOU 6461  C   LEU A 419     5124   3919   4556    -78    422   -184       C  
ATOM   6462  O   LEU A 419     -17.924 -72.772  -9.870  1.00 36.14           O  
ANISOU 6462  O   LEU A 419     5201   3904   4627    -25    398   -231       O  
ATOM   6463  CB  LEU A 419     -19.429 -69.675  -9.381  1.00 33.95           C  
ANISOU 6463  CB  LEU A 419     4907   3672   4318   -196    321    -78       C  
ATOM   6464  CG  LEU A 419     -20.499 -70.151 -10.371  1.00 36.18           C  
ANISOU 6464  CG  LEU A 419     5295   3898   4553   -210    259   -102       C  
ATOM   6465  CD1 LEU A 419     -21.503 -70.991  -9.647  1.00 40.70           C  
ANISOU 6465  CD1 LEU A 419     5859   4400   5204   -198    174    -88       C  
ATOM   6466  CD2 LEU A 419     -21.175 -68.979 -11.076  1.00 23.45           C  
ANISOU 6466  CD2 LEU A 419     3739   2298   2874   -275    232    -64       C  
ATOM   6467  H   LEU A 419     -17.634 -69.157  -7.836  1.00 30.29           H  
ATOM   6468  HA  LEU A 419     -18.985 -71.289  -8.181  1.00 31.13           H  
ATOM   6469  HB2 LEU A 419     -19.900 -69.230  -8.659  1.00 40.74           H  
ATOM   6470  HB3 LEU A 419     -18.890 -69.020  -9.852  1.00 40.74           H  
ATOM   6471  HG  LEU A 419     -20.078 -70.705 -11.047  1.00 43.42           H  
ATOM   6472 HD11 LEU A 419     -21.915 -70.458  -8.949  1.00 48.84           H  
ATOM   6473 HD12 LEU A 419     -22.177 -71.290 -10.277  1.00 48.84           H  
ATOM   6474 HD13 LEU A 419     -21.052 -71.756  -9.257  1.00 48.84           H  
ATOM   6475 HD21 LEU A 419     -20.505 -68.474 -11.562  1.00 28.14           H  
ATOM   6476 HD22 LEU A 419     -21.842 -69.322 -11.690  1.00 28.14           H  
ATOM   6477 HD23 LEU A 419     -21.598 -68.412 -10.411  1.00 28.14           H  
ATOM   6478  N   HIS A 420     -16.966 -70.868 -10.644  1.00 31.75           N  
ANISOU 6478  N   HIS A 420     4617   3480   3965    -92    502   -192       N  
ATOM   6479  CA  HIS A 420     -16.225 -71.532 -11.711  1.00 34.29           C  
ANISOU 6479  CA  HIS A 420     4984   3827   4216    -37    576   -260       C  
ATOM   6480  C   HIS A 420     -15.360 -72.660 -11.172  1.00 33.88           C  
ANISOU 6480  C   HIS A 420     4871   3771   4230     55    616   -301       C  
ATOM   6481  O   HIS A 420     -15.349 -73.759 -11.723  1.00 41.26           O  
ANISOU 6481  O   HIS A 420     5873   4660   5145    121    620   -372       O  
ATOM   6482  CB  HIS A 420     -15.338 -70.526 -12.447  1.00 41.44           C  
ANISOU 6482  CB  HIS A 420     5871   4836   5040    -70    669   -240       C  
ATOM   6483  CG  HIS A 420     -15.962 -69.961 -13.684  1.00 48.11           C  
ANISOU 6483  CG  HIS A 420     6827   5681   5770   -123    657   -243       C  
ATOM   6484  ND1 HIS A 420     -16.310 -70.745 -14.762  1.00 58.82           N  
ANISOU 6484  ND1 HIS A 420     8299   7002   7047    -88    653   -313       N  
ATOM   6485  CD2 HIS A 420     -16.285 -68.690 -14.022  1.00 52.13           C  
ANISOU 6485  CD2 HIS A 420     7357   6220   6231   -207    643   -185       C  
ATOM   6486  CE1 HIS A 420     -16.824 -69.982 -15.710  1.00 67.07           C  
ANISOU 6486  CE1 HIS A 420     9427   8061   7995   -151    637   -294       C  
ATOM   6487  NE2 HIS A 420     -16.825 -68.732 -15.286  1.00 63.36           N  
ANISOU 6487  NE2 HIS A 420     8900   7628   7545   -223    631   -215       N  
ATOM   6488  H   HIS A 420     -16.833 -70.020 -10.604  1.00 38.10           H  
ATOM   6489  HA  HIS A 420     -16.851 -71.908 -12.349  1.00 41.14           H  
ATOM   6490  HB2 HIS A 420     -15.142 -69.787 -11.850  1.00 49.73           H  
ATOM   6491  HB3 HIS A 420     -14.514 -70.967 -12.706  1.00 49.73           H  
ATOM   6492  HD1 HIS A 420     -16.206 -71.598 -14.811  1.00 70.58           H  
ATOM   6493  HD2 HIS A 420     -16.169 -67.932 -13.496  1.00 62.56           H  
ATOM   6494  HE1 HIS A 420     -17.139 -70.277 -16.534  1.00 80.48           H  
ATOM   6495  HE2 HIS A 420     -17.113 -68.054 -15.729  1.00 76.03           H  
ATOM   6496  N   ALA A 421     -14.632 -72.383 -10.094  1.00 30.45           N  
ANISOU 6496  N   ALA A 421     4316   3380   3874     60    640   -258       N  
ATOM   6497  CA  ALA A 421     -13.738 -73.375  -9.510  1.00 28.68           C  
ANISOU 6497  CA  ALA A 421     4019   3159   3719    148    676   -285       C  
ATOM   6498  C   ALA A 421     -14.504 -74.635  -9.106  1.00 39.46           C  
ANISOU 6498  C   ALA A 421     5435   4412   5144    194    595   -319       C  
ATOM   6499  O   ALA A 421     -14.116 -75.749  -9.476  1.00 41.46           O  
ANISOU 6499  O   ALA A 421     5723   4632   5400    279    618   -384       O  
ATOM   6500  CB  ALA A 421     -12.998 -72.787  -8.317  1.00 33.40           C  
ANISOU 6500  CB  ALA A 421     4482   3814   4393    129    689   -220       C  
ATOM   6501  H   ALA A 421     -14.639 -71.628  -9.682  1.00 36.54           H  
ATOM   6502  HA  ALA A 421     -13.078 -73.630 -10.173  1.00 34.42           H  
ATOM   6503  HB1 ALA A 421     -13.646 -72.509  -7.650  1.00 40.08           H  
ATOM   6504  HB2 ALA A 421     -12.410 -73.463  -7.945  1.00 40.08           H  
ATOM   6505  HB3 ALA A 421     -12.478 -72.023  -8.613  1.00 40.08           H  
ATOM   6506  N   ILE A 422     -15.600 -74.460  -8.370  1.00 28.75           N  
ANISOU 6506  N   ILE A 422     4089   3000   3837    139    500   -273       N  
ATOM   6507  CA  ILE A 422     -16.397 -75.603  -7.940  1.00 35.11           C  
ANISOU 6507  CA  ILE A 422     4936   3702   4704    166    415   -287       C  
ATOM   6508  C   ILE A 422     -16.898 -76.382  -9.142  1.00 38.67           C  
ANISOU 6508  C   ILE A 422     5517   4084   5090    187    391   -359       C  
ATOM   6509  O   ILE A 422     -16.758 -77.606  -9.185  1.00 31.58           O  
ANISOU 6509  O   ILE A 422     4658   3118   4223    255    374   -410       O  
ATOM   6510  CB  ILE A 422     -17.617 -75.202  -7.091  1.00 25.75           C  
ANISOU 6510  CB  ILE A 422     3739   2479   3565     97    323   -218       C  
ATOM   6511  CG1 ILE A 422     -17.173 -74.530  -5.792  1.00 30.09           C  
ANISOU 6511  CG1 ILE A 422     4175   3084   4175     83    335   -153       C  
ATOM   6512  CG2 ILE A 422     -18.461 -76.442  -6.763  1.00 24.19           C  
ANISOU 6512  CG2 ILE A 422     3585   2177   3428    115    234   -224       C  
ATOM   6513  CD1 ILE A 422     -18.314 -73.948  -4.987  1.00 22.89           C  
ANISOU 6513  CD1 ILE A 422     3252   2153   3292     24    263    -86       C  
ATOM   6514  H   ILE A 422     -15.900 -73.697  -8.110  1.00 34.51           H  
ATOM   6515  HA  ILE A 422     -15.841 -76.194  -7.408  1.00 42.13           H  
ATOM   6516  HB  ILE A 422     -18.160 -74.577  -7.597  1.00 30.90           H  
ATOM   6517 HG12 ILE A 422     -16.724 -75.188  -5.238  1.00 36.11           H  
ATOM   6518 HG13 ILE A 422     -16.562 -73.808  -6.006  1.00 36.11           H  
ATOM   6519 HG21 ILE A 422     -17.915 -77.072  -6.267  1.00 29.02           H  
ATOM   6520 HG22 ILE A 422     -19.224 -76.172  -6.229  1.00 29.02           H  
ATOM   6521 HG23 ILE A 422     -18.763 -76.846  -7.592  1.00 29.02           H  
ATOM   6522 HD11 ILE A 422     -18.930 -74.659  -4.753  1.00 27.47           H  
ATOM   6523 HD12 ILE A 422     -17.956 -73.542  -4.182  1.00 27.47           H  
ATOM   6524 HD13 ILE A 422     -18.768 -73.278  -5.522  1.00 27.47           H  
ATOM   6525  N   LEU A 423     -17.497 -75.680 -10.103  1.00 34.69           N  
ANISOU 6525  N   LEU A 423     5091   3593   4497    129    383   -362       N  
ATOM   6526  CA  LEU A 423     -17.991 -76.351 -11.301  1.00 31.12           C  
ANISOU 6526  CA  LEU A 423     4777   3079   3970    142    352   -431       C  
ATOM   6527  C   LEU A 423     -16.874 -77.167 -11.946  1.00 39.15           C  
ANISOU 6527  C   LEU A 423     5823   4106   4946    244    438   -517       C  
ATOM   6528  O   LEU A 423     -17.030 -78.361 -12.176  1.00 43.90           O  
ANISOU 6528  O   LEU A 423     6504   4618   5559    301    397   -580       O  
ATOM   6529  CB  LEU A 423     -18.571 -75.347 -12.300  1.00 24.75           C  
ANISOU 6529  CB  LEU A 423     4039   2305   3059     69    346   -418       C  
ATOM   6530  CG  LEU A 423     -19.921 -74.721 -11.930  1.00 29.54           C  
ANISOU 6530  CG  LEU A 423     4649   2880   3695    -20    245   -345       C  
ATOM   6531  CD1 LEU A 423     -20.340 -73.743 -13.003  1.00 29.10           C  
ANISOU 6531  CD1 LEU A 423     4664   2860   3533    -81    245   -335       C  
ATOM   6532  CD2 LEU A 423     -21.009 -75.771 -11.725  1.00 30.16           C  
ANISOU 6532  CD2 LEU A 423     4782   2849   3829    -28    128   -349       C  
ATOM   6533  H   LEU A 423     -17.628 -74.831 -10.086  1.00 41.63           H  
ATOM   6534  HA  LEU A 423     -18.700 -76.963 -11.049  1.00 37.35           H  
ATOM   6535  HB2 LEU A 423     -17.936 -74.622 -12.405  1.00 29.69           H  
ATOM   6536  HB3 LEU A 423     -18.687 -75.798 -13.151  1.00 29.69           H  
ATOM   6537  HG  LEU A 423     -19.822 -74.229 -11.100  1.00 35.45           H  
ATOM   6538 HD11 LEU A 423     -20.420 -74.215 -13.846  1.00 34.92           H  
ATOM   6539 HD12 LEU A 423     -21.194 -73.353 -12.758  1.00 34.92           H  
ATOM   6540 HD13 LEU A 423     -19.667 -73.048 -13.075  1.00 34.92           H  
ATOM   6541 HD21 LEU A 423     -20.742 -76.366 -11.008  1.00 36.19           H  
ATOM   6542 HD22 LEU A 423     -21.839 -75.325 -11.494  1.00 36.19           H  
ATOM   6543 HD23 LEU A 423     -21.121 -76.273 -12.548  1.00 36.19           H  
ATOM   6544  N   ARG A 424     -15.738 -76.523 -12.197  1.00 46.04           N  
ANISOU 6544  N   ARG A 424     6630   5088   5775    269    554   -517       N  
ATOM   6545  CA  ARG A 424     -14.587 -77.190 -12.797  1.00 51.74           C  
ANISOU 6545  CA  ARG A 424     7359   5844   6455    376    655   -591       C  
ATOM   6546  C   ARG A 424     -14.180 -78.408 -11.986  1.00 47.27           C  
ANISOU 6546  C   ARG A 424     6754   5213   5992    468    638   -619       C  
ATOM   6547  O   ARG A 424     -13.775 -79.430 -12.541  1.00 58.21           O  
ANISOU 6547  O   ARG A 424     8209   6554   7352    567    666   -703       O  
ATOM   6548  CB  ARG A 424     -13.402 -76.228 -12.869  1.00 50.70           C  
ANISOU 6548  CB  ARG A 424     7116   5854   6293    376    779   -555       C  
ATOM   6549  CG  ARG A 424     -12.440 -76.504 -14.011  1.00 63.93           C  
ANISOU 6549  CG  ARG A 424     8827   7598   7866    460    900   -624       C  
ATOM   6550  CD  ARG A 424     -13.110 -76.310 -15.364  1.00 63.02           C  
ANISOU 6550  CD  ARG A 424     8866   7467   7612    426    890   -668       C  
ATOM   6551  NE  ARG A 424     -13.746 -75.000 -15.466  1.00 59.35           N  
ANISOU 6551  NE  ARG A 424     8399   7040   7112    299    855   -591       N  
ATOM   6552  CZ  ARG A 424     -13.100 -73.872 -15.748  1.00 65.47           C  
ANISOU 6552  CZ  ARG A 424     9107   7932   7836    252    938   -537       C  
ATOM   6553  NH1 ARG A 424     -11.790 -73.880 -15.959  1.00 58.84           N  
ANISOU 6553  NH1 ARG A 424     8185   7197   6974    315   1067   -544       N  
ATOM   6554  NH2 ARG A 424     -13.770 -72.730 -15.815  1.00 69.50           N  
ANISOU 6554  NH2 ARG A 424     9631   8455   8322    140    890   -469       N  
ATOM   6555  H   ARG A 424     -15.608 -75.691 -12.027  1.00 55.25           H  
ATOM   6556  HA  ARG A 424     -14.809 -77.477 -13.697  1.00 62.09           H  
ATOM   6557  HB2 ARG A 424     -13.741 -75.326 -12.980  1.00 60.84           H  
ATOM   6558  HB3 ARG A 424     -12.902 -76.290 -12.040  1.00 60.84           H  
ATOM   6559  HG2 ARG A 424     -11.690 -75.892 -13.953  1.00 76.72           H  
ATOM   6560  HG3 ARG A 424     -12.130 -77.422 -13.955  1.00 76.72           H  
ATOM   6561  HD2 ARG A 424     -12.443 -76.379 -16.064  1.00 75.62           H  
ATOM   6562  HD3 ARG A 424     -13.793 -76.988 -15.483  1.00 75.62           H  
ATOM   6563  HE  ARG A 424     -14.595 -74.954 -15.335  1.00 71.22           H  
ATOM   6564 HH11 ARG A 424     -11.351 -74.619 -15.915  1.00 70.61           H  
ATOM   6565 HH12 ARG A 424     -11.379 -73.146 -16.141  1.00 70.61           H  
ATOM   6566 HH21 ARG A 424     -14.619 -72.721 -15.679  1.00 83.40           H  
ATOM   6567 HH22 ARG A 424     -13.356 -71.999 -15.998  1.00 83.40           H  
ATOM   6568  N   ARG A 425     -14.289 -78.290 -10.667  1.00 44.33           N  
ANISOU 6568  N   ARG A 425     6278   4832   5733    439    591   -548       N  
ATOM   6569  CA  ARG A 425     -13.909 -79.379  -9.773  1.00 35.27           C  
ANISOU 6569  CA  ARG A 425     5085   3626   4692    517    567   -558       C  
ATOM   6570  C   ARG A 425     -14.842 -80.578  -9.870  1.00 39.90           C  
ANISOU 6570  C   ARG A 425     5791   4065   5305    533    459   -601       C  
ATOM   6571  O   ARG A 425     -14.393 -81.723  -9.856  1.00 45.67           O  
ANISOU 6571  O   ARG A 425     6552   4731   6071    631    459   -658       O  
ATOM   6572  CB  ARG A 425     -13.884 -78.884  -8.327  1.00 32.58           C  
ANISOU 6572  CB  ARG A 425     4612   3316   4452    469    535   -465       C  
ATOM   6573  CG  ARG A 425     -12.656 -79.306  -7.557  1.00 37.78           C  
ANISOU 6573  CG  ARG A 425     5153   4015   5187    552    590   -456       C  
ATOM   6574  CD  ARG A 425     -11.402 -78.688  -8.136  1.00 37.79           C  
ANISOU 6574  CD  ARG A 425     5083   4143   5133    588    717   -467       C  
ATOM   6575  NE  ARG A 425     -10.272 -78.808  -7.222  1.00 47.88           N  
ANISOU 6575  NE  ARG A 425     6218   5481   6495    641    759   -431       N  
ATOM   6576  CZ  ARG A 425      -9.011 -78.552  -7.552  1.00 53.17           C  
ANISOU 6576  CZ  ARG A 425     6797   6259   7145    693    868   -434       C  
ATOM   6577  NH1 ARG A 425      -8.704 -78.167  -8.785  1.00 56.95           N  
ANISOU 6577  NH1 ARG A 425     7318   6804   7518    702    957   -473       N  
ATOM   6578  NH2 ARG A 425      -8.051 -78.687  -6.648  1.00 62.39           N  
ANISOU 6578  NH2 ARG A 425     7830   7477   8400    735    889   -392       N  
ATOM   6579  H   ARG A 425     -14.580 -77.589 -10.263  1.00 53.19           H  
ATOM   6580  HA  ARG A 425     -13.015 -79.677 -10.002  1.00 42.33           H  
ATOM   6581  HB2 ARG A 425     -13.914 -77.914  -8.329  1.00 39.10           H  
ATOM   6582  HB3 ARG A 425     -14.660 -79.235  -7.864  1.00 39.10           H  
ATOM   6583  HG2 ARG A 425     -12.741 -79.016  -6.635  1.00 45.34           H  
ATOM   6584  HG3 ARG A 425     -12.567 -80.271  -7.600  1.00 45.34           H  
ATOM   6585  HD2 ARG A 425     -11.174 -79.143  -8.962  1.00 45.35           H  
ATOM   6586  HD3 ARG A 425     -11.558 -77.746  -8.304  1.00 45.35           H  
ATOM   6587  HE  ARG A 425     -10.432 -79.060  -6.416  1.00 57.46           H  
ATOM   6588 HH11 ARG A 425      -9.324 -78.078  -9.374  1.00 68.34           H  
ATOM   6589 HH12 ARG A 425      -7.886 -78.004  -8.993  1.00 68.34           H  
ATOM   6590 HH21 ARG A 425      -8.246 -78.938  -5.849  1.00 74.87           H  
ATOM   6591 HH22 ARG A 425      -7.234 -78.525  -6.861  1.00 74.87           H  
ATOM   6592  N   GLN A 426     -16.140 -80.313  -9.969  1.00 35.57           N  
ANISOU 6592  N   GLN A 426     5309   3464   4743    438    363   -570       N  
ATOM   6593  CA  GLN A 426     -17.140 -81.367  -9.855  1.00 37.27           C  
ANISOU 6593  CA  GLN A 426     5616   3541   5004    426    240   -584       C  
ATOM   6594  C   GLN A 426     -17.733 -81.789 -11.196  1.00 44.15           C  
ANISOU 6594  C   GLN A 426     6656   4342   5778    422    200   -661       C  
ATOM   6595  O   GLN A 426     -18.573 -82.683 -11.257  1.00 43.52           O  
ANISOU 6595  O   GLN A 426     6669   4140   5727    404     88   -677       O  
ATOM   6596  CB  GLN A 426     -18.251 -80.916  -8.904  1.00 29.21           C  
ANISOU 6596  CB  GLN A 426     4541   2505   4051    324    148   -483       C  
ATOM   6597  CG  GLN A 426     -17.834 -80.913  -7.433  1.00 24.99           C  
ANISOU 6597  CG  GLN A 426     3871   2000   3624    337    154   -413       C  
ATOM   6598  CD  GLN A 426     -17.522 -82.299  -6.906  1.00 25.67           C  
ANISOU 6598  CD  GLN A 426     3967   1993   3794    412    115   -436       C  
ATOM   6599  OE1 GLN A 426     -18.341 -83.211  -7.002  1.00 31.81           O  
ANISOU 6599  OE1 GLN A 426     4831   2656   4601    396     16   -445       O  
ATOM   6600  NE2 GLN A 426     -16.330 -82.462  -6.344  1.00 25.88           N  
ANISOU 6600  NE2 GLN A 426     3904   2067   3864    491    186   -440       N  
ATOM   6601  H   GLN A 426     -16.468 -79.530 -10.103  1.00 42.69           H  
ATOM   6602  HA  GLN A 426     -16.719 -82.149  -9.463  1.00 44.73           H  
ATOM   6603  HB2 GLN A 426     -18.518 -80.013  -9.140  1.00 35.05           H  
ATOM   6604  HB3 GLN A 426     -19.007 -81.517  -8.997  1.00 35.05           H  
ATOM   6605  HG2 GLN A 426     -17.038 -80.368  -7.333  1.00 29.98           H  
ATOM   6606  HG3 GLN A 426     -18.557 -80.545  -6.901  1.00 29.98           H  
ATOM   6607 HE21 GLN A 426     -15.784 -81.799  -6.296  1.00 31.06           H  
ATOM   6608 HE22 GLN A 426     -16.105 -83.229  -6.029  1.00 31.06           H  
ATOM   6609  N   GLU A 427     -17.276 -81.168 -12.273  1.00 52.54           N  
ANISOU 6609  N   GLU A 427     7760   5480   6722    434    286   -707       N  
ATOM   6610  CA  GLU A 427     -17.858 -81.403 -13.583  1.00 48.67           C  
ANISOU 6610  CA  GLU A 427     7435   4937   6121    420    247   -777       C  
ATOM   6611  C   GLU A 427     -17.614 -82.825 -14.083  1.00 53.73           C  
ANISOU 6611  C   GLU A 427     8202   5465   6749    520    223   -883       C  
ATOM   6612  O   GLU A 427     -18.453 -83.404 -14.775  1.00 45.68           O  
ANISOU 6612  O   GLU A 427     7331   4341   5685    492    124   -929       O  
ATOM   6613  CB  GLU A 427     -17.274 -80.402 -14.565  1.00 46.24           C  
ANISOU 6613  CB  GLU A 427     7135   4750   5685    419    360   -796       C  
ATOM   6614  CG  GLU A 427     -15.808 -80.634 -14.892  1.00 53.35           C  
ANISOU 6614  CG  GLU A 427     8001   5726   6546    541    505   -858       C  
ATOM   6615  CD  GLU A 427     -15.239 -79.551 -15.778  1.00 65.47           C  
ANISOU 6615  CD  GLU A 427     9524   7395   7959    524    619   -855       C  
ATOM   6616  OE1 GLU A 427     -16.004 -78.652 -16.181  1.00 61.71           O  
ANISOU 6616  OE1 GLU A 427     9082   6941   7426    420    579   -811       O  
ATOM   6617  OE2 GLU A 427     -14.025 -79.592 -16.062  1.00 71.74           O  
ANISOU 6617  OE2 GLU A 427    10268   8274   8715    615    749   -889       O  
ATOM   6618  H   GLU A 427     -16.627 -80.603 -12.271  1.00 63.05           H  
ATOM   6619  HA  GLU A 427     -18.816 -81.258 -13.536  1.00 58.41           H  
ATOM   6620  HB2 GLU A 427     -17.773 -80.453 -15.396  1.00 55.49           H  
ATOM   6621  HB3 GLU A 427     -17.355 -79.512 -14.189  1.00 55.49           H  
ATOM   6622  HG2 GLU A 427     -15.297 -80.648 -14.068  1.00 64.03           H  
ATOM   6623  HG3 GLU A 427     -15.716 -81.481 -15.355  1.00 64.03           H  
ATOM   6624  N   ASP A 428     -16.469 -83.392 -13.723  1.00 76.95           N  
ANISOU 6624  N   ASP A 428    11086   8421   9731    638    306   -920       N  
ATOM   6625  CA  ASP A 428     -16.109 -84.721 -14.196  1.00 87.92           C  
ANISOU 6625  CA  ASP A 428    12595   9703  11106    754    296  -1028       C  
ATOM   6626  C   ASP A 428     -17.060 -85.748 -13.599  1.00 86.71           C  
ANISOU 6626  C   ASP A 428    12506   9386  11054    718    135  -1013       C  
ATOM   6627  O   ASP A 428     -17.409 -86.736 -14.245  1.00 89.88           O  
ANISOU 6627  O   ASP A 428    13070   9658  11422    752     60  -1096       O  
ATOM   6628  CB  ASP A 428     -14.667 -85.068 -13.815  1.00 99.85           C  
ANISOU 6628  CB  ASP A 428    14008  11273  12658    894    419  -1057       C  
ATOM   6629  CG  ASP A 428     -13.720 -83.893 -13.967  1.00105.46           C  
ANISOU 6629  CG  ASP A 428    14589  12166  13314    899    570  -1022       C  
ATOM   6630  OD1 ASP A 428     -13.163 -83.711 -15.071  1.00103.41           O  
ANISOU 6630  OD1 ASP A 428    14388  11972  12930    957    670  -1089       O  
ATOM   6631  OD2 ASP A 428     -13.535 -83.148 -12.980  1.00100.29           O  
ANISOU 6631  OD2 ASP A 428    13776  11589  12739    843    585   -924       O  
ATOM   6632  H   ASP A 428     -15.884 -83.029 -13.206  1.00 92.34           H  
ATOM   6633  HA  ASP A 428     -16.188 -84.753 -15.163  1.00105.50           H  
ATOM   6634  HB2 ASP A 428     -14.645 -85.352 -12.887  1.00119.82           H  
ATOM   6635  HB3 ASP A 428     -14.352 -85.784 -14.388  1.00119.82           H  
ATOM   6636  N   PHE A 429     -17.489 -85.498 -12.365  1.00 49.76           N  
ANISOU 6636  N   PHE A 429     7701   4711   6492    644     80   -905       N  
ATOM   6637  CA  PHE A 429     -18.337 -86.442 -11.647  1.00 44.60           C  
ANISOU 6637  CA  PHE A 429     7081   3918   5946    604    -64   -868       C  
ATOM   6638  C   PHE A 429     -19.809 -86.277 -12.021  1.00 40.18           C  
ANISOU 6638  C   PHE A 429     6605   3298   5363    471   -195   -831       C  
ATOM   6639  O   PHE A 429     -20.603 -87.208 -11.881  1.00 49.33           O  
ANISOU 6639  O   PHE A 429     7845   4321   6578    434   -329   -825       O  
ATOM   6640  CB  PHE A 429     -18.171 -86.263 -10.137  1.00 47.22           C  
ANISOU 6640  CB  PHE A 429     7243   4292   6408    585    -64   -762       C  
ATOM   6641  CG  PHE A 429     -16.744 -86.318  -9.669  1.00 47.57           C  
ANISOU 6641  CG  PHE A 429     7182   4409   6485    702     56   -780       C  
ATOM   6642  CD1 PHE A 429     -16.033 -87.504  -9.709  1.00 44.12           C  
ANISOU 6642  CD1 PHE A 429     6797   3885   6082    828     62   -853       C  
ATOM   6643  CD2 PHE A 429     -16.118 -85.182  -9.182  1.00 39.16           C  
ANISOU 6643  CD2 PHE A 429     5966   3495   5420    687    155   -720       C  
ATOM   6644  CE1 PHE A 429     -14.719 -87.554  -9.275  1.00 50.22           C  
ANISOU 6644  CE1 PHE A 429     7460   4730   6891    940    169   -861       C  
ATOM   6645  CE2 PHE A 429     -14.809 -85.227  -8.747  1.00 45.49           C  
ANISOU 6645  CE2 PHE A 429     6660   4367   6255    786    256   -728       C  
ATOM   6646  CZ  PHE A 429     -14.108 -86.414  -8.794  1.00 52.18           C  
ANISOU 6646  CZ  PHE A 429     7548   5137   7140    915    265   -796       C  
ATOM   6647  H   PHE A 429     -17.301 -84.786 -11.921  1.00 59.71           H  
ATOM   6648  HA  PHE A 429     -18.068 -87.345 -11.874  1.00 53.52           H  
ATOM   6649  HB2 PHE A 429     -18.533 -85.400  -9.883  1.00 56.67           H  
ATOM   6650  HB3 PHE A 429     -18.658 -86.970  -9.684  1.00 56.67           H  
ATOM   6651  HD1 PHE A 429     -16.440 -88.275 -10.032  1.00 52.95           H  
ATOM   6652  HD2 PHE A 429     -16.585 -84.379  -9.148  1.00 47.00           H  
ATOM   6653  HE1 PHE A 429     -14.249 -88.356  -9.307  1.00 60.27           H  
ATOM   6654  HE2 PHE A 429     -14.399 -84.457  -8.424  1.00 54.58           H  
ATOM   6655  HZ  PHE A 429     -13.226 -86.447  -8.502  1.00 62.61           H  
ATOM   6656  N   TYR A 430     -20.162 -85.085 -12.491  1.00 46.88           N  
ANISOU 6656  N   TYR A 430     7430   4248   6134    397   -161   -799       N  
ATOM   6657  CA  TYR A 430     -21.534 -84.770 -12.869  1.00 44.79           C  
ANISOU 6657  CA  TYR A 430     7226   3948   5846    272   -277   -753       C  
ATOM   6658  C   TYR A 430     -21.538 -84.136 -14.259  1.00 50.88           C  
ANISOU 6658  C   TYR A 430     8101   4769   6464    261   -236   -816       C  
ATOM   6659  O   TYR A 430     -21.195 -82.964 -14.399  1.00 57.35           O  
ANISOU 6659  O   TYR A 430     8844   5716   7229    245   -141   -786       O  
ATOM   6660  CB  TYR A 430     -22.151 -83.812 -11.846  1.00 32.39           C  
ANISOU 6660  CB  TYR A 430     5502   2457   4348    179   -291   -622       C  
ATOM   6661  CG  TYR A 430     -22.281 -84.405 -10.458  1.00 34.07           C  
ANISOU 6661  CG  TYR A 430     5617   2626   4701    177   -339   -548       C  
ATOM   6662  CD1 TYR A 430     -23.400 -85.147 -10.105  1.00 34.75           C  
ANISOU 6662  CD1 TYR A 430     5737   2606   4860    104   -482   -495       C  
ATOM   6663  CD2 TYR A 430     -21.286 -84.228  -9.505  1.00 27.56           C  
ANISOU 6663  CD2 TYR A 430     4666   1872   3935    242   -246   -524       C  
ATOM   6664  CE1 TYR A 430     -23.527 -85.695  -8.842  1.00 33.80           C  
ANISOU 6664  CE1 TYR A 430     5529   2451   4862     98   -524   -419       C  
ATOM   6665  CE2 TYR A 430     -21.405 -84.770  -8.238  1.00 29.79           C  
ANISOU 6665  CE2 TYR A 430     4865   2118   4336    239   -292   -453       C  
ATOM   6666  CZ  TYR A 430     -22.525 -85.502  -7.912  1.00 34.83           C  
ANISOU 6666  CZ  TYR A 430     5542   2652   5040    168   -427   -400       C  
ATOM   6667  OH  TYR A 430     -22.636 -86.040  -6.650  1.00 31.88           O  
ANISOU 6667  OH  TYR A 430     5085   2248   4779    162   -470   -322       O  
ATOM   6668  H   TYR A 430     -19.615 -84.431 -12.601  1.00 56.26           H  
ATOM   6669  HA  TYR A 430     -22.063 -85.583 -12.895  1.00 53.75           H  
ATOM   6670  HB2 TYR A 430     -21.591 -83.022 -11.780  1.00 38.87           H  
ATOM   6671  HB3 TYR A 430     -23.038 -83.562 -12.147  1.00 38.87           H  
ATOM   6672  HD2 TYR A 430     -20.529 -83.734  -9.721  1.00 33.08           H  
ATOM   6673  HD1 TYR A 430     -24.076 -85.278 -10.730  1.00 41.70           H  
ATOM   6674  HE2 TYR A 430     -20.732 -84.643  -7.610  1.00 35.75           H  
ATOM   6675  HE1 TYR A 430     -24.283 -86.189  -8.620  1.00 40.56           H  
ATOM   6676  HH  TYR A 430     -21.959 -85.845  -6.194  1.00 38.25           H  
ATOM   6677  N   PRO A 431     -21.930 -84.905 -15.293  1.00 71.82           N  
ANISOU 6677  N   PRO A 431    10932   7314   9041    267   -313   -902       N  
ATOM   6678  CA  PRO A 431     -21.850 -84.417 -16.677  1.00 66.70           C  
ANISOU 6678  CA  PRO A 431    10402   6708   8232    270   -272   -973       C  
ATOM   6679  C   PRO A 431     -22.764 -83.218 -16.906  1.00 60.43           C  
ANISOU 6679  C   PRO A 431     9571   5987   7400    145   -309   -887       C  
ATOM   6680  O   PRO A 431     -22.457 -82.311 -17.695  1.00 66.91           O  
ANISOU 6680  O   PRO A 431    10409   6907   8107    142   -227   -902       O  
ATOM   6681  CB  PRO A 431     -22.326 -85.623 -17.495  1.00 72.11           C  
ANISOU 6681  CB  PRO A 431    11293   7235   8870    283   -391  -1067       C  
ATOM   6682  CG  PRO A 431     -23.239 -86.359 -16.570  1.00 77.58           C  
ANISOU 6682  CG  PRO A 431    11959   7812   9707    212   -541   -996       C  
ATOM   6683  CD  PRO A 431     -22.642 -86.193 -15.208  1.00 76.85           C  
ANISOU 6683  CD  PRO A 431    11678   7781   9740    249   -465   -922       C  
ATOM   6684  HA  PRO A 431     -20.937 -84.192 -16.915  1.00 80.04           H  
ATOM   6685  HB2 PRO A 431     -22.804 -85.319 -18.282  1.00 86.53           H  
ATOM   6686  HB3 PRO A 431     -21.567 -86.174 -17.742  1.00 86.53           H  
ATOM   6687  HG2 PRO A 431     -24.125 -85.966 -16.606  1.00 93.10           H  
ATOM   6688  HG3 PRO A 431     -23.269 -87.296 -16.819  1.00 93.10           H  
ATOM   6689  HD2 PRO A 431     -23.340 -86.149 -14.536  1.00 92.22           H  
ATOM   6690  HD3 PRO A 431     -22.017 -86.912 -15.023  1.00 92.22           H  
ATOM   6691  N   PHE A 432     -23.883 -83.212 -16.190  1.00 37.76           N  
ANISOU 6691  N   PHE A 432     6645   3073   4631     46   -430   -790       N  
ATOM   6692  CA  PHE A 432     -24.884 -82.171 -16.358  1.00 33.76           C  
ANISOU 6692  CA  PHE A 432     6103   2620   4104    -67   -483   -703       C  
ATOM   6693  C   PHE A 432     -24.349 -80.817 -15.891  1.00 41.47           C  
ANISOU 6693  C   PHE A 432     6933   3745   5078    -65   -358   -640       C  
ATOM   6694  O   PHE A 432     -24.838 -79.773 -16.319  1.00 38.16           O  
ANISOU 6694  O   PHE A 432     6505   3391   4602   -131   -361   -594       O  
ATOM   6695  CB  PHE A 432     -26.180 -82.545 -15.628  1.00 31.24           C  
ANISOU 6695  CB  PHE A 432     5742   2226   3902   -162   -635   -607       C  
ATOM   6696  CG  PHE A 432     -26.278 -82.006 -14.224  1.00 34.93           C  
ANISOU 6696  CG  PHE A 432     6022   2761   4490   -181   -603   -496       C  
ATOM   6697  CD1 PHE A 432     -26.826 -80.754 -13.982  1.00 40.72           C  
ANISOU 6697  CD1 PHE A 432     6658   3590   5223   -244   -588   -405       C  
ATOM   6698  CD2 PHE A 432     -25.842 -82.758 -13.145  1.00 34.08           C  
ANISOU 6698  CD2 PHE A 432     5843   2616   4491   -133   -591   -482       C  
ATOM   6699  CE1 PHE A 432     -26.923 -80.258 -12.693  1.00 38.38           C  
ANISOU 6699  CE1 PHE A 432     6203   3353   5026   -253   -558   -310       C  
ATOM   6700  CE2 PHE A 432     -25.940 -82.267 -11.855  1.00 40.96           C  
ANISOU 6700  CE2 PHE A 432     6552   3552   5460   -149   -562   -381       C  
ATOM   6701  CZ  PHE A 432     -26.481 -81.017 -11.630  1.00 37.54           C  
ANISOU 6701  CZ  PHE A 432     6030   3216   5019   -208   -544   -299       C  
ATOM   6702  H   PHE A 432     -24.085 -83.802 -15.599  1.00 45.32           H  
ATOM   6703  HA  PHE A 432     -25.092 -82.093 -17.302  1.00 40.51           H  
ATOM   6704  HB2 PHE A 432     -26.932 -82.197 -16.131  1.00 37.49           H  
ATOM   6705  HB3 PHE A 432     -26.240 -83.512 -15.577  1.00 37.49           H  
ATOM   6706  HD1 PHE A 432     -27.125 -80.238 -14.696  1.00 48.86           H  
ATOM   6707  HD2 PHE A 432     -25.476 -83.601 -13.290  1.00 40.90           H  
ATOM   6708  HE1 PHE A 432     -27.289 -79.416 -12.544  1.00 46.06           H  
ATOM   6709  HE2 PHE A 432     -25.640 -82.779 -11.139  1.00 49.15           H  
ATOM   6710  HZ  PHE A 432     -26.546 -80.686 -10.763  1.00 45.05           H  
ATOM   6711  N   LEU A 433     -23.346 -80.833 -15.016  1.00 45.86           N  
ANISOU 6711  N   LEU A 433     7377   4350   5697      7   -255   -637       N  
ATOM   6712  CA  LEU A 433     -22.672 -79.595 -14.629  1.00 44.32           C  
ANISOU 6712  CA  LEU A 433     7056   4289   5493     12   -135   -589       C  
ATOM   6713  C   LEU A 433     -21.759 -79.097 -15.755  1.00 43.84           C  
ANISOU 6713  C   LEU A 433     7057   4307   5295     57    -20   -660       C  
ATOM   6714  O   LEU A 433     -21.706 -77.894 -16.017  1.00 47.12           O  
ANISOU 6714  O   LEU A 433     7433   4816   5655     13     31   -616       O  
ATOM   6715  CB  LEU A 433     -21.868 -79.756 -13.331  1.00 35.34           C  
ANISOU 6715  CB  LEU A 433     5779   3182   4465     68    -70   -559       C  
ATOM   6716  CG  LEU A 433     -22.614 -80.009 -12.013  1.00 30.72           C  
ANISOU 6716  CG  LEU A 433     5101   2557   4015     26   -154   -469       C  
ATOM   6717  CD1 LEU A 433     -21.619 -80.041 -10.859  1.00 26.97           C  
ANISOU 6717  CD1 LEU A 433     4498   2130   3621     88    -74   -447       C  
ATOM   6718  CD2 LEU A 433     -23.693 -78.964 -11.733  1.00 30.94           C  
ANISOU 6718  CD2 LEU A 433     5074   2626   4054    -72   -206   -371       C  
ATOM   6719  H   LEU A 433     -23.039 -81.541 -14.635  1.00 55.03           H  
ATOM   6720  HA  LEU A 433     -23.344 -78.913 -14.473  1.00 53.18           H  
ATOM   6721  HB2 LEU A 433     -21.260 -80.502 -13.453  1.00 42.41           H  
ATOM   6722  HB3 LEU A 433     -21.348 -78.947 -13.205  1.00 42.41           H  
ATOM   6723  HG  LEU A 433     -23.045 -80.877 -12.058  1.00 36.87           H  
ATOM   6724 HD11 LEU A 433     -21.159 -79.188 -10.815  1.00 32.37           H  
ATOM   6725 HD12 LEU A 433     -22.100 -80.201 -10.032  1.00 32.37           H  
ATOM   6726 HD13 LEU A 433     -20.980 -80.754 -11.013  1.00 32.37           H  
ATOM   6727 HD21 LEU A 433     -24.342 -78.981 -12.454  1.00 37.12           H  
ATOM   6728 HD22 LEU A 433     -24.127 -79.175 -10.892  1.00 37.12           H  
ATOM   6729 HD23 LEU A 433     -23.279 -78.088 -11.681  1.00 37.12           H  
ATOM   6730  N   LYS A 434     -21.043 -80.011 -16.417  1.00 92.38           N  
ANISOU 6730  N   LYS A 434    13302  10416  11384    148     21   -765       N  
ATOM   6731  CA  LYS A 434     -20.249 -79.650 -17.598  1.00 95.48           C  
ANISOU 6731  CA  LYS A 434    13767  10882  11629    195    130   -835       C  
ATOM   6732  C   LYS A 434     -21.171 -78.993 -18.611  1.00 91.46           C  
ANISOU 6732  C   LYS A 434    13362  10377  11013    104     65   -821       C  
ATOM   6733  O   LYS A 434     -20.909 -77.880 -19.077  1.00 89.79           O  
ANISOU 6733  O   LYS A 434    13124  10270  10722     72    138   -789       O  
ATOM   6734  CB  LYS A 434     -19.565 -80.874 -18.240  1.00 86.52           C  
ANISOU 6734  CB  LYS A 434    12752   9684  10439    313    164   -961       C  
ATOM   6735  CG  LYS A 434     -18.360 -81.399 -17.498  1.00 86.67           C  
ANISOU 6735  CG  LYS A 434    12670   9727  10533    428    265   -985       C  
ATOM   6736  CD  LYS A 434     -17.643 -82.513 -18.229  1.00 88.43           C  
ANISOU 6736  CD  LYS A 434    13015   9896  10688    560    312  -1113       C  
ATOM   6737  CE  LYS A 434     -16.379 -82.859 -17.465  1.00 88.55           C  
ANISOU 6737  CE  LYS A 434    12902   9959  10783    676    424  -1121       C  
ATOM   6738  NZ  LYS A 434     -15.764 -84.146 -17.831  1.00 90.18           N  
ANISOU 6738  NZ  LYS A 434    13210  10083  10971    820    447  -1237       N  
ATOM   6739  H   LYS A 434     -21.000 -80.843 -16.205  1.00110.86           H  
ATOM   6740  HA  LYS A 434     -19.564 -79.012 -17.344  1.00114.58           H  
ATOM   6741  HB2 LYS A 434     -20.212 -81.595 -18.294  1.00103.83           H  
ATOM   6742  HB3 LYS A 434     -19.275 -80.631 -19.133  1.00103.83           H  
ATOM   6743  HG2 LYS A 434     -17.729 -80.672 -17.370  1.00104.00           H  
ATOM   6744  HG3 LYS A 434     -18.646 -81.743 -16.637  1.00104.00           H  
ATOM   6745  HD2 LYS A 434     -18.209 -83.299 -18.269  1.00106.12           H  
ATOM   6746  HD3 LYS A 434     -17.398 -82.218 -19.120  1.00106.12           H  
ATOM   6747  HE2 LYS A 434     -15.722 -82.164 -17.625  1.00106.25           H  
ATOM   6748  HE3 LYS A 434     -16.591 -82.894 -16.519  1.00106.25           H  
ATOM   6749  HZ1 LYS A 434     -15.543 -84.143 -18.693  1.00108.22           H  
ATOM   6750  HZ2 LYS A 434     -15.031 -84.282 -17.345  1.00108.22           H  
ATOM   6751  HZ3 LYS A 434     -16.337 -84.810 -17.682  1.00108.22           H  
ATOM   6752  N   ASP A 435     -22.266 -79.680 -18.923  1.00 43.04           N  
ANISOU 6752  N   ASP A 435     7342   4127   4883     56    -82   -837       N  
ATOM   6753  CA  ASP A 435     -23.192 -79.217 -19.954  1.00 41.99           C  
ANISOU 6753  CA  ASP A 435     7322   3984   4646    -29   -164   -829       C  
ATOM   6754  C   ASP A 435     -23.791 -77.832 -19.692  1.00 48.33           C  
ANISOU 6754  C   ASP A 435     8027   4869   5468   -125   -176   -714       C  
ATOM   6755  O   ASP A 435     -23.966 -77.047 -20.624  1.00 45.44           O  
ANISOU 6755  O   ASP A 435     7724   4555   4987   -168   -166   -707       O  
ATOM   6756  CB  ASP A 435     -24.306 -80.246 -20.133  1.00 51.02           C  
ANISOU 6756  CB  ASP A 435     8582   4981   5820    -75   -338   -849       C  
ATOM   6757  CG  ASP A 435     -23.769 -81.614 -20.498  1.00 60.90           C  
ANISOU 6757  CG  ASP A 435     9962   6134   7044     21   -342   -972       C  
ATOM   6758  OD1 ASP A 435     -22.694 -81.672 -21.132  1.00 66.95           O  
ANISOU 6758  OD1 ASP A 435    10780   6952   7706    118   -214  -1059       O  
ATOM   6759  OD2 ASP A 435     -24.407 -82.627 -20.145  1.00 65.84           O  
ANISOU 6759  OD2 ASP A 435    10635   6630   7751      2   -470   -978       O  
ATOM   6760  H   ASP A 435     -22.496 -80.420 -18.551  1.00 51.65           H  
ATOM   6761  HA  ASP A 435     -22.709 -79.166 -20.793  1.00 50.38           H  
ATOM   6762  HB2 ASP A 435     -24.800 -80.327 -19.303  1.00 61.22           H  
ATOM   6763  HB3 ASP A 435     -24.896 -79.954 -20.846  1.00 61.22           H  
ATOM   6764  N   ASN A 436     -24.101 -77.539 -18.431  1.00 50.54           N  
ANISOU 6764  N   ASN A 436     8159   5157   5886   -154   -196   -625       N  
ATOM   6765  CA  ASN A 436     -24.807 -76.305 -18.073  1.00 38.28           C  
ANISOU 6765  CA  ASN A 436     6518   3663   4364   -237   -224   -517       C  
ATOM   6766  C   ASN A 436     -23.959 -75.185 -17.450  1.00 36.51           C  
ANISOU 6766  C   ASN A 436     6161   3551   4159   -221    -98   -467       C  
ATOM   6767  O   ASN A 436     -24.510 -74.213 -16.932  1.00 36.35           O  
ANISOU 6767  O   ASN A 436     6061   3568   4184   -277   -122   -378       O  
ATOM   6768  CB  ASN A 436     -25.949 -76.631 -17.105  1.00 35.11           C  
ANISOU 6768  CB  ASN A 436     6048   3195   4095   -290   -347   -439       C  
ATOM   6769  CG  ASN A 436     -27.005 -77.524 -17.720  1.00 39.73           C  
ANISOU 6769  CG  ASN A 436     6754   3672   4669   -339   -497   -458       C  
ATOM   6770  OD1 ASN A 436     -27.969 -77.047 -18.315  1.00 43.65           O  
ANISOU 6770  OD1 ASN A 436     7295   4164   5125   -414   -585   -416       O  
ATOM   6771  ND2 ASN A 436     -26.835 -78.830 -17.571  1.00 45.98           N  
ANISOU 6771  ND2 ASN A 436     7601   4370   5500   -298   -536   -519       N  
ATOM   6772  H   ASN A 436     -23.913 -78.041 -17.758  1.00 60.65           H  
ATOM   6773  HA  ASN A 436     -25.208 -75.944 -18.879  1.00 45.94           H  
ATOM   6774  HB2 ASN A 436     -25.585 -77.087 -16.329  1.00 42.13           H  
ATOM   6775  HB3 ASN A 436     -26.377 -75.804 -16.832  1.00 42.13           H  
ATOM   6776 HD21 ASN A 436     -26.152 -79.128 -17.142  1.00 55.18           H  
ATOM   6777 HD22 ASN A 436     -27.408 -79.379 -17.903  1.00 55.18           H  
ATOM   6778  N   ARG A 437     -22.636 -75.307 -17.503  1.00 34.30           N  
ANISOU 6778  N   ARG A 437     5859   3327   3847   -145     30   -522       N  
ATOM   6779  CA  ARG A 437     -21.746 -74.364 -16.817  1.00 37.64           C  
ANISOU 6779  CA  ARG A 437     6149   3851   4303   -134    140   -473       C  
ATOM   6780  C   ARG A 437     -21.995 -72.893 -17.175  1.00 40.24           C  
ANISOU 6780  C   ARG A 437     6464   4253   4575   -207    153   -404       C  
ATOM   6781  O   ARG A 437     -22.213 -72.054 -16.289  1.00 44.52           O  
ANISOU 6781  O   ARG A 437     6904   4822   5191   -244    145   -325       O  
ATOM   6782  CB  ARG A 437     -20.290 -74.735 -17.103  1.00 38.74           C  
ANISOU 6782  CB  ARG A 437     6278   4045   4394    -44    274   -543       C  
ATOM   6783  CG  ARG A 437     -19.266 -73.785 -16.504  1.00 44.89           C  
ANISOU 6783  CG  ARG A 437     6922   4934   5201    -39    385   -493       C  
ATOM   6784  CD  ARG A 437     -17.903 -74.440 -16.377  1.00 59.61           C  
ANISOU 6784  CD  ARG A 437     8736   6840   7073     62    499   -549       C  
ATOM   6785  NE  ARG A 437     -17.400 -74.900 -17.671  1.00 69.57           N  
ANISOU 6785  NE  ARG A 437    10109   8120   8203    118    565   -635       N  
ATOM   6786  CZ  ARG A 437     -17.143 -76.168 -17.987  1.00 74.14           C  
ANISOU 6786  CZ  ARG A 437    10765   8638   8768    211    570   -728       C  
ATOM   6787  NH1 ARG A 437     -17.323 -77.146 -17.107  1.00 67.44           N  
ANISOU 6787  NH1 ARG A 437     9890   7699   8035    253    508   -744       N  
ATOM   6788  NH2 ARG A 437     -16.691 -76.460 -19.199  1.00 73.88           N  
ANISOU 6788  NH2 ARG A 437    10840   8631   8599    266    637   -806       N  
ATOM   6789  H   ARG A 437     -22.224 -75.929 -17.931  1.00 41.17           H  
ATOM   6790  HA  ARG A 437     -21.886 -74.455 -15.861  1.00 45.17           H  
ATOM   6791  HB2 ARG A 437     -20.119 -75.618 -16.740  1.00 46.48           H  
ATOM   6792  HB3 ARG A 437     -20.156 -74.745 -18.063  1.00 46.48           H  
ATOM   6793  HG2 ARG A 437     -19.176 -73.008 -17.078  1.00 53.87           H  
ATOM   6794  HG3 ARG A 437     -19.557 -73.517 -15.619  1.00 53.87           H  
ATOM   6795  HD2 ARG A 437     -17.272 -73.798 -16.017  1.00 71.53           H  
ATOM   6796  HD3 ARG A 437     -17.972 -75.208 -15.788  1.00 71.53           H  
ATOM   6797  HE  ARG A 437     -17.259 -74.305 -18.275  1.00 83.48           H  
ATOM   6798 HH11 ARG A 437     -17.616 -76.967 -16.318  1.00 80.93           H  
ATOM   6799 HH12 ARG A 437     -17.150 -77.960 -17.326  1.00 80.93           H  
ATOM   6800 HH21 ARG A 437     -16.569 -75.834 -19.776  1.00 88.65           H  
ATOM   6801 HH22 ARG A 437     -16.520 -77.276 -19.409  1.00 88.65           H  
ATOM   6802  N   GLU A 438     -21.958 -72.584 -18.468  1.00 47.82           N  
ANISOU 6802  N   GLU A 438     7532   5238   5399   -226    171   -434       N  
ATOM   6803  CA  GLU A 438     -22.177 -71.221 -18.939  1.00 49.21           C  
ANISOU 6803  CA  GLU A 438     7710   5476   5510   -297    179   -369       C  
ATOM   6804  C   GLU A 438     -23.536 -70.717 -18.464  1.00 45.64           C  
ANISOU 6804  C   GLU A 438     7237   4976   5128   -366     54   -289       C  
ATOM   6805  O   GLU A 438     -23.693 -69.557 -18.062  1.00 51.19           O  
ANISOU 6805  O   GLU A 438     7875   5719   5857   -408     58   -213       O  
ATOM   6806  CB  GLU A 438     -22.105 -71.183 -20.465  1.00 59.50           C  
ANISOU 6806  CB  GLU A 438     9156   6800   6650   -307    196   -416       C  
ATOM   6807  CG  GLU A 438     -20.731 -71.517 -21.016  1.00 74.02           C  
ANISOU 6807  CG  GLU A 438    11011   8711   8404   -234    338   -486       C  
ATOM   6808  CD  GLU A 438     -20.686 -71.467 -22.530  1.00 81.37           C  
ANISOU 6808  CD  GLU A 438    12090   9669   9158   -241    360   -531       C  
ATOM   6809  OE1 GLU A 438     -21.763 -71.522 -23.161  1.00 83.12           O  
ANISOU 6809  OE1 GLU A 438    12423   9829   9329   -293    244   -531       O  
ATOM   6810  OE2 GLU A 438     -19.573 -71.370 -23.090  1.00 80.19           O  
ANISOU 6810  OE2 GLU A 438    11943   9608   8917   -195    492   -563       O  
ATOM   6811  H   GLU A 438     -21.808 -73.151 -19.097  1.00 57.38           H  
ATOM   6812  HA  GLU A 438     -21.489 -70.639 -18.582  1.00 59.05           H  
ATOM   6813  HB2 GLU A 438     -22.734 -71.828 -20.824  1.00 71.40           H  
ATOM   6814  HB3 GLU A 438     -22.338 -70.292 -20.767  1.00 71.40           H  
ATOM   6815  HG2 GLU A 438     -20.088 -70.875 -20.675  1.00 88.83           H  
ATOM   6816  HG3 GLU A 438     -20.487 -72.413 -20.737  1.00 88.83           H  
ATOM   6817  N   LYS A 439     -24.509 -71.619 -18.496  1.00 35.82           N  
ANISOU 6817  N   LYS A 439     6048   3645   3918   -374    -58   -307       N  
ATOM   6818  CA  LYS A 439     -25.869 -71.328 -18.071  1.00 33.14           C  
ANISOU 6818  CA  LYS A 439     5681   3260   3650   -433   -181   -230       C  
ATOM   6819  C   LYS A 439     -25.888 -70.927 -16.600  1.00 36.84           C  
ANISOU 6819  C   LYS A 439     6003   3747   4250   -423   -164   -164       C  
ATOM   6820  O   LYS A 439     -26.505 -69.934 -16.228  1.00 35.74           O  
ANISOU 6820  O   LYS A 439     5811   3628   4141   -460   -194    -86       O  
ATOM   6821  CB  LYS A 439     -26.736 -72.566 -18.284  1.00 31.59           C  
ANISOU 6821  CB  LYS A 439     5558   2967   3478   -442   -299   -262       C  
ATOM   6822  CG  LYS A 439     -28.181 -72.294 -18.690  1.00 40.37           C  
ANISOU 6822  CG  LYS A 439     6709   4041   4589   -518   -438   -200       C  
ATOM   6823  CD  LYS A 439     -28.550 -73.041 -19.970  1.00 57.32           C  
ANISOU 6823  CD  LYS A 439     9018   6128   6632   -542   -519   -265       C  
ATOM   6824  CE  LYS A 439     -28.305 -74.544 -19.870  1.00 65.95           C  
ANISOU 6824  CE  LYS A 439    10167   7139   7753   -499   -544   -347       C  
ATOM   6825  NZ  LYS A 439     -27.859 -75.120 -21.166  1.00 67.23           N  
ANISOU 6825  NZ  LYS A 439    10498   7274   7770   -476   -535   -453       N  
ATOM   6826  H   LYS A 439     -24.401 -72.428 -18.767  1.00 42.99           H  
ATOM   6827  HA  LYS A 439     -26.230 -70.598 -18.599  1.00 39.77           H  
ATOM   6828  HB2 LYS A 439     -26.334 -73.105 -18.983  1.00 37.91           H  
ATOM   6829  HB3 LYS A 439     -26.757 -73.072 -17.456  1.00 37.91           H  
ATOM   6830  HG2 LYS A 439     -28.774 -72.592 -17.983  1.00 48.45           H  
ATOM   6831  HG3 LYS A 439     -28.296 -71.344 -18.848  1.00 48.45           H  
ATOM   6832  HD2 LYS A 439     -29.492 -72.902 -20.156  1.00 68.78           H  
ATOM   6833  HD3 LYS A 439     -28.014 -72.698 -20.702  1.00 68.78           H  
ATOM   6834  HE2 LYS A 439     -27.614 -74.711 -19.210  1.00 79.14           H  
ATOM   6835  HE3 LYS A 439     -29.130 -74.985 -19.611  1.00 79.14           H  
ATOM   6836  HZ1 LYS A 439     -27.100 -74.734 -21.424  1.00 80.67           H  
ATOM   6837  HZ2 LYS A 439     -27.724 -75.995 -21.079  1.00 80.67           H  
ATOM   6838  HZ3 LYS A 439     -28.480 -74.983 -21.789  1.00 80.67           H  
ATOM   6839  N   ILE A 440     -25.201 -71.708 -15.770  1.00 29.89           N  
ANISOU 6839  N   ILE A 440     5060   2857   3440   -366   -116   -197       N  
ATOM   6840  CA  ILE A 440     -25.131 -71.436 -14.337  1.00 26.51           C  
ANISOU 6840  CA  ILE A 440     4500   2446   3127   -351    -97   -141       C  
ATOM   6841  C   ILE A 440     -24.428 -70.112 -14.063  1.00 29.15           C  
ANISOU 6841  C   ILE A 440     4772   2861   3443   -359    -13   -104       C  
ATOM   6842  O   ILE A 440     -24.876 -69.335 -13.215  1.00 32.71           O  
ANISOU 6842  O   ILE A 440     5150   3325   3954   -377    -33    -36       O  
ATOM   6843  CB  ILE A 440     -24.415 -72.569 -13.574  1.00 24.48           C  
ANISOU 6843  CB  ILE A 440     4197   2163   2941   -287    -62   -186       C  
ATOM   6844  CG1 ILE A 440     -25.252 -73.843 -13.637  1.00 24.06           C  
ANISOU 6844  CG1 ILE A 440     4198   2016   2928   -290   -166   -205       C  
ATOM   6845  CG2 ILE A 440     -24.197 -72.194 -12.104  1.00 22.02           C  
ANISOU 6845  CG2 ILE A 440     3753   1883   2731   -271    -34   -128       C  
ATOM   6846  CD1 ILE A 440     -24.470 -75.108 -13.377  1.00 24.81           C  
ANISOU 6846  CD1 ILE A 440     4302   2067   3058   -222   -136   -274       C  
ATOM   6847  H   ILE A 440     -24.763 -72.406 -16.014  1.00 35.87           H  
ATOM   6848  HA  ILE A 440     -26.034 -71.369 -13.989  1.00 31.82           H  
ATOM   6849  HB  ILE A 440     -23.555 -72.735 -13.990  1.00 29.37           H  
ATOM   6850 HG12 ILE A 440     -25.954 -73.788 -12.970  1.00 28.87           H  
ATOM   6851 HG13 ILE A 440     -25.644 -73.915 -14.521  1.00 28.87           H  
ATOM   6852 HG21 ILE A 440     -25.058 -72.032 -11.688  1.00 26.43           H  
ATOM   6853 HG22 ILE A 440     -23.745 -72.927 -11.656  1.00 26.43           H  
ATOM   6854 HG23 ILE A 440     -23.651 -71.393 -12.060  1.00 26.43           H  
ATOM   6855 HD11 ILE A 440     -24.080 -75.061 -12.490  1.00 29.77           H  
ATOM   6856 HD12 ILE A 440     -25.071 -75.868 -13.435  1.00 29.77           H  
ATOM   6857 HD13 ILE A 440     -23.770 -75.189 -14.043  1.00 29.77           H  
ATOM   6858  N   GLU A 441     -23.328 -69.852 -14.767  1.00 29.50           N  
ANISOU 6858  N   GLU A 441     4845   2959   3403   -344     81   -146       N  
ATOM   6859  CA  GLU A 441     -22.662 -68.559 -14.625  1.00 31.89           C  
ANISOU 6859  CA  GLU A 441     5099   3335   3683   -368    150   -103       C  
ATOM   6860  C   GLU A 441     -23.622 -67.431 -14.973  1.00 36.99           C  
ANISOU 6860  C   GLU A 441     5780   3977   4300   -431     86    -38       C  
ATOM   6861  O   GLU A 441     -23.724 -66.447 -14.243  1.00 33.28           O  
ANISOU 6861  O   GLU A 441     5249   3524   3874   -450     84     22       O  
ATOM   6862  CB  GLU A 441     -21.420 -68.463 -15.513  1.00 38.23           C  
ANISOU 6862  CB  GLU A 441     5932   4204   4390   -353    258   -147       C  
ATOM   6863  CG  GLU A 441     -20.112 -68.801 -14.804  1.00 48.29           C  
ANISOU 6863  CG  GLU A 441     7110   5525   5712   -299    354   -170       C  
ATOM   6864  CD  GLU A 441     -19.739 -70.259 -14.916  1.00 60.96           C  
ANISOU 6864  CD  GLU A 441     8737   7097   7327   -223    374   -250       C  
ATOM   6865  OE1 GLU A 441     -19.744 -70.794 -16.044  1.00 63.25           O  
ANISOU 6865  OE1 GLU A 441     9132   7377   7525   -205    383   -310       O  
ATOM   6866  OE2 GLU A 441     -19.405 -70.857 -13.876  1.00 75.20           O  
ANISOU 6866  OE2 GLU A 441    10460   8884   9227   -178    379   -254       O  
ATOM   6867  H   GLU A 441     -22.954 -70.394 -15.321  1.00 35.40           H  
ATOM   6868  HA  GLU A 441     -22.383 -68.445 -13.703  1.00 38.27           H  
ATOM   6869  HB2 GLU A 441     -21.520 -69.079 -16.255  1.00 45.88           H  
ATOM   6870  HB3 GLU A 441     -21.347 -67.556 -15.848  1.00 45.88           H  
ATOM   6871  HG2 GLU A 441     -19.396 -68.278 -15.198  1.00 57.94           H  
ATOM   6872  HG3 GLU A 441     -20.200 -68.586 -13.862  1.00 57.94           H  
ATOM   6873  N   LYS A 442     -24.337 -67.586 -16.084  1.00 35.46           N  
ANISOU 6873  N   LYS A 442     5689   3755   4029   -460     27    -50       N  
ATOM   6874  CA  LYS A 442     -25.265 -66.551 -16.529  1.00 38.09           C  
ANISOU 6874  CA  LYS A 442     6061   4083   4330   -517    -41     14       C  
ATOM   6875  C   LYS A 442     -26.369 -66.235 -15.520  1.00 41.44           C  
ANISOU 6875  C   LYS A 442     6415   4471   4858   -522   -122     81       C  
ATOM   6876  O   LYS A 442     -26.893 -65.127 -15.523  1.00 39.17           O  
ANISOU 6876  O   LYS A 442     6126   4191   4567   -551   -154    143       O  
ATOM   6877  CB  LYS A 442     -25.877 -66.914 -17.884  1.00 46.91           C  
ANISOU 6877  CB  LYS A 442     7303   5173   5346   -547   -104    -12       C  
ATOM   6878  CG  LYS A 442     -25.092 -66.341 -19.049  1.00 45.00           C  
ANISOU 6878  CG  LYS A 442     7140   4988   4969   -570    -33    -30       C  
ATOM   6879  CD  LYS A 442     -25.101 -67.249 -20.264  1.00 51.41           C  
ANISOU 6879  CD  LYS A 442     8078   5783   5673   -563    -47   -103       C  
ATOM   6880  CE  LYS A 442     -23.814 -67.114 -21.064  1.00 59.53           C  
ANISOU 6880  CE  LYS A 442     9147   6887   6584   -546     79   -147       C  
ATOM   6881  NZ  LYS A 442     -24.069 -67.021 -22.524  1.00 65.15           N  
ANISOU 6881  NZ  LYS A 442    10001   7608   7144   -580     55   -166       N  
ATOM   6882  H   LYS A 442     -24.304 -68.277 -16.595  1.00 42.55           H  
ATOM   6883  HA  LYS A 442     -24.759 -65.733 -16.657  1.00 45.71           H  
ATOM   6884  HB2 LYS A 442     -25.890 -67.880 -17.977  1.00 56.29           H  
ATOM   6885  HB3 LYS A 442     -26.780 -66.563 -17.929  1.00 56.29           H  
ATOM   6886  HG2 LYS A 442     -25.483 -65.491 -19.307  1.00 54.00           H  
ATOM   6887  HG3 LYS A 442     -24.170 -66.213 -18.777  1.00 54.00           H  
ATOM   6888  HD2 LYS A 442     -25.185 -68.171 -19.974  1.00 61.69           H  
ATOM   6889  HD3 LYS A 442     -25.844 -67.009 -20.839  1.00 61.69           H  
ATOM   6890  HE2 LYS A 442     -23.350 -66.309 -20.787  1.00 71.43           H  
ATOM   6891  HE3 LYS A 442     -23.257 -67.892 -20.904  1.00 71.43           H  
ATOM   6892  HZ1 LYS A 442     -24.575 -66.310 -22.700  1.00 78.18           H  
ATOM   6893  HZ2 LYS A 442     -23.299 -66.943 -22.963  1.00 78.18           H  
ATOM   6894  HZ3 LYS A 442     -24.490 -67.752 -22.807  1.00 78.18           H  
ATOM   6895  N   ILE A 443     -26.710 -67.185 -14.650  1.00 33.39           N  
ANISOU 6895  N   ILE A 443     5340   3417   3931   -489   -152     73       N  
ATOM   6896  CA  ILE A 443     -27.749 -66.935 -13.654  1.00 29.71           C  
ANISOU 6896  CA  ILE A 443     4799   2930   3560   -487   -218    141       C  
ATOM   6897  C   ILE A 443     -27.237 -65.919 -12.641  1.00 31.71           C  
ANISOU 6897  C   ILE A 443     4973   3221   3853   -469   -158    177       C  
ATOM   6898  O   ILE A 443     -27.908 -64.931 -12.338  1.00 31.57           O  
ANISOU 6898  O   ILE A 443     4936   3205   3853   -478   -191    237       O  
ATOM   6899  CB  ILE A 443     -28.186 -68.215 -12.902  1.00 29.26           C  
ANISOU 6899  CB  ILE A 443     4694   2831   3591   -462   -260    133       C  
ATOM   6900  CG1 ILE A 443     -28.464 -69.349 -13.895  1.00 39.72           C  
ANISOU 6900  CG1 ILE A 443     6112   4106   4874   -479   -317     82       C  
ATOM   6901  CG2 ILE A 443     -29.405 -67.910 -12.029  1.00 34.96           C  
ANISOU 6901  CG2 ILE A 443     5341   3545   4398   -465   -328    216       C  
ATOM   6902  CD1 ILE A 443     -29.160 -70.570 -13.313  1.00 34.51           C  
ANISOU 6902  CD1 ILE A 443     5422   3390   4302   -475   -391     91       C  
ATOM   6903  H   ILE A 443     -26.360 -67.970 -14.616  1.00 40.07           H  
ATOM   6904  HA  ILE A 443     -28.529 -66.561 -14.093  1.00 35.65           H  
ATOM   6905  HB  ILE A 443     -27.459 -68.490 -12.322  1.00 35.11           H  
ATOM   6906 HG12 ILE A 443     -29.027 -69.004 -14.605  1.00 47.66           H  
ATOM   6907 HG13 ILE A 443     -27.618 -69.645 -14.266  1.00 47.66           H  
ATOM   6908 HG21 ILE A 443     -30.129 -67.602 -12.596  1.00 41.95           H  
ATOM   6909 HG22 ILE A 443     -29.670 -68.718 -11.563  1.00 41.95           H  
ATOM   6910 HG23 ILE A 443     -29.170 -67.220 -11.389  1.00 41.95           H  
ATOM   6911 HD11 ILE A 443     -30.018 -70.301 -12.950  1.00 41.42           H  
ATOM   6912 HD12 ILE A 443     -29.288 -71.225 -14.017  1.00 41.42           H  
ATOM   6913 HD13 ILE A 443     -28.605 -70.944 -12.611  1.00 41.42           H  
ATOM   6914  N   LEU A 444     -26.036 -66.164 -12.126  1.00 23.63           N  
ANISOU 6914  N   LEU A 444     3909   2226   2844   -440    -74    138       N  
ATOM   6915  CA  LEU A 444     -25.431 -65.272 -11.147  1.00 31.68           C  
ANISOU 6915  CA  LEU A 444     4860   3277   3898   -429    -24    166       C  
ATOM   6916  C   LEU A 444     -25.215 -63.901 -11.768  1.00 37.51           C  
ANISOU 6916  C   LEU A 444     5644   4039   4569   -470     -9    195       C  
ATOM   6917  O   LEU A 444     -25.417 -62.871 -11.122  1.00 30.61           O  
ANISOU 6917  O   LEU A 444     4744   3165   3722   -473    -20    241       O  
ATOM   6918  CB  LEU A 444     -24.090 -65.833 -10.664  1.00 24.25           C  
ANISOU 6918  CB  LEU A 444     3871   2367   2977   -398     59    120       C  
ATOM   6919  CG  LEU A 444     -23.359 -65.029  -9.580  1.00 20.82           C  
ANISOU 6919  CG  LEU A 444     3363   1964   2582   -391    102    146       C  
ATOM   6920  CD1 LEU A 444     -22.647 -65.966  -8.616  1.00 25.05           C  
ANISOU 6920  CD1 LEU A 444     3826   2509   3185   -345    138    119       C  
ATOM   6921  CD2 LEU A 444     -22.362 -64.035 -10.181  1.00 20.11           C  
ANISOU 6921  CD2 LEU A 444     3295   1919   2426   -430    161    149       C  
ATOM   6922  H   LEU A 444     -25.550 -66.843 -12.330  1.00 28.36           H  
ATOM   6923  HA  LEU A 444     -26.021 -65.178 -10.383  1.00 38.01           H  
ATOM   6924  HB2 LEU A 444     -24.244 -66.722 -10.307  1.00 29.10           H  
ATOM   6925  HB3 LEU A 444     -23.494 -65.894 -11.427  1.00 29.10           H  
ATOM   6926  HG  LEU A 444     -24.013 -64.523  -9.073  1.00 24.98           H  
ATOM   6927 HD11 LEU A 444     -22.003 -66.497  -9.110  1.00 30.06           H  
ATOM   6928 HD12 LEU A 444     -22.193 -65.437  -7.941  1.00 30.06           H  
ATOM   6929 HD13 LEU A 444     -23.302 -66.545  -8.197  1.00 30.06           H  
ATOM   6930 HD21 LEU A 444     -22.840 -63.416 -10.754  1.00 24.13           H  
ATOM   6931 HD22 LEU A 444     -21.926 -63.552  -9.462  1.00 24.13           H  
ATOM   6932 HD23 LEU A 444     -21.703 -64.524 -10.699  1.00 24.13           H  
ATOM   6933  N   THR A 445     -24.821 -63.902 -13.038  1.00 33.42           N  
ANISOU 6933  N   THR A 445     5201   3538   3960   -501     14    168       N  
ATOM   6934  CA  THR A 445     -24.404 -62.685 -13.722  1.00 29.02           C  
ANISOU 6934  CA  THR A 445     4688   3009   3329   -548     39    197       C  
ATOM   6935  C   THR A 445     -25.582 -62.034 -14.464  1.00 29.63           C  
ANISOU 6935  C   THR A 445     4837   3055   3367   -582    -45    243       C  
ATOM   6936  O   THR A 445     -25.450 -60.943 -15.018  1.00 29.47           O  
ANISOU 6936  O   THR A 445     4862   3045   3290   -624    -44    280       O  
ATOM   6937  CB  THR A 445     -23.207 -62.982 -14.682  1.00 21.77           C  
ANISOU 6937  CB  THR A 445     3806   2143   2324   -562    125    152       C  
ATOM   6938  OG1 THR A 445     -22.165 -62.023 -14.473  1.00 35.69           O  
ANISOU 6938  OG1 THR A 445     5534   3952   4074   -591    190    180       O  
ATOM   6939  CG2 THR A 445     -23.624 -62.964 -16.145  1.00 22.61           C  
ANISOU 6939  CG2 THR A 445     4021   2248   2321   -597     98    145       C  
ATOM   6940  H   THR A 445     -24.786 -64.606 -13.530  1.00 40.11           H  
ATOM   6941  HA  THR A 445     -24.093 -62.050 -13.058  1.00 34.82           H  
ATOM   6942  HB  THR A 445     -22.861 -63.866 -14.483  1.00 26.13           H  
ATOM   6943  HG1 THR A 445     -21.521 -62.181 -14.988  1.00 42.83           H  
ATOM   6944 HG21 THR A 445     -23.981 -62.093 -16.377  1.00 27.13           H  
ATOM   6945 HG22 THR A 445     -22.858 -63.152 -16.710  1.00 27.13           H  
ATOM   6946 HG23 THR A 445     -24.304 -63.637 -16.304  1.00 27.13           H  
ATOM   6947  N   PHE A 446     -26.735 -62.703 -14.455  1.00 74.05           N  
ANISOU 6947  N   PHE A 446    10468   8640   9027   -567   -124    248       N  
ATOM   6948  CA  PHE A 446     -27.948 -62.186 -15.098  1.00 77.39           C  
ANISOU 6948  CA  PHE A 446    10944   9035   9426   -594   -216    298       C  
ATOM   6949  C   PHE A 446     -28.299 -60.797 -14.564  1.00 74.27           C  
ANISOU 6949  C   PHE A 446    10527   8632   9060   -594   -235    364       C  
ATOM   6950  O   PHE A 446     -28.162 -60.543 -13.374  1.00 91.27           O  
ANISOU 6950  O   PHE A 446    12608  10784  11285   -557   -212    375       O  
ATOM   6951  CB  PHE A 446     -29.130 -63.133 -14.828  1.00 80.43           C  
ANISOU 6951  CB  PHE A 446    11303   9383   9875   -575   -299    306       C  
ATOM   6952  CG  PHE A 446     -30.226 -63.086 -15.870  1.00 82.97           C  
ANISOU 6952  CG  PHE A 446    11694   9679  10151   -613   -398    338       C  
ATOM   6953  CD1 PHE A 446     -30.166 -62.224 -16.957  1.00 81.40           C  
ANISOU 6953  CD1 PHE A 446    11581   9489   9856   -656   -410    357       C  
ATOM   6954  CD2 PHE A 446     -31.332 -63.914 -15.744  1.00 82.73           C  
ANISOU 6954  CD2 PHE A 446    11640   9618  10176   -611   -486    357       C  
ATOM   6955  CE1 PHE A 446     -31.184 -62.198 -17.898  1.00 88.94           C  
ANISOU 6955  CE1 PHE A 446    12601  10423  10771   -691   -510    389       C  
ATOM   6956  CE2 PHE A 446     -32.350 -63.890 -16.678  1.00 88.01           C  
ANISOU 6956  CE2 PHE A 446    12366  10264  10808   -651   -589    391       C  
ATOM   6957  CZ  PHE A 446     -32.277 -63.033 -17.755  1.00 92.47           C  
ANISOU 6957  CZ  PHE A 446    13020  10838  11276   -689   -602    406       C  
ATOM   6958  H   PHE A 446     -26.843 -63.469 -14.079  1.00 88.86           H  
ATOM   6959  HA  PHE A 446     -27.810 -62.126 -16.056  1.00 92.87           H  
ATOM   6960  HB2 PHE A 446     -28.796 -64.043 -14.794  1.00 96.52           H  
ATOM   6961  HB3 PHE A 446     -29.526 -62.898 -13.974  1.00 96.52           H  
ATOM   6962  HD1 PHE A 446     -29.432 -61.661 -17.058  1.00 97.67           H  
ATOM   6963  HD2 PHE A 446     -31.388 -64.495 -15.020  1.00 99.28           H  
ATOM   6964  HE1 PHE A 446     -31.133 -61.618 -18.623  1.00106.73           H  
ATOM   6965  HE2 PHE A 446     -33.084 -64.453 -16.580  1.00105.61           H  
ATOM   6966  HZ  PHE A 446     -32.961 -63.016 -18.384  1.00110.96           H  
ATOM   6967  N   ARG A 447     -28.743 -59.903 -15.444  1.00 72.33           N  
ANISOU 6967  N   ARG A 447    10351   8376   8754   -631   -281    407       N  
ATOM   6968  CA  ARG A 447     -29.195 -58.570 -15.041  1.00 74.90           C  
ANISOU 6968  CA  ARG A 447    10672   8680   9105   -625   -313    470       C  
ATOM   6969  C   ARG A 447     -30.390 -58.124 -15.881  1.00 79.74           C  
ANISOU 6969  C   ARG A 447    11342   9266   9691   -642   -410    525       C  
ATOM   6970  O   ARG A 447     -31.524 -58.540 -15.639  1.00 86.16           O  
ANISOU 6970  O   ARG A 447    12116  10061  10558   -614   -479    551       O  
ATOM   6971  CB  ARG A 447     -28.062 -57.551 -15.181  1.00 69.33           C  
ANISOU 6971  CB  ARG A 447    10000   7991   8352   -661   -252    477       C  
ATOM   6972  CG  ARG A 447     -27.078 -57.543 -14.021  1.00 61.23           C  
ANISOU 6972  CG  ARG A 447     8903   6981   7380   -638   -179    450       C  
ATOM   6973  CD  ARG A 447     -27.202 -56.296 -13.161  1.00 74.24           C  
ANISOU 6973  CD  ARG A 447    10542   8596   9072   -621   -199    493       C  
ATOM   6974  NE  ARG A 447     -28.436 -56.267 -12.377  1.00 85.29           N  
ANISOU 6974  NE  ARG A 447    11903   9961  10542   -556   -258    518       N  
ATOM   6975  CZ  ARG A 447     -28.623 -55.507 -11.300  1.00 86.82           C  
ANISOU 6975  CZ  ARG A 447    12072  10127  10788   -510   -267    537       C  
ATOM   6976  NH1 ARG A 447     -27.653 -54.711 -10.862  1.00 86.34           N  
ANISOU 6976  NH1 ARG A 447    12026  10059  10720   -532   -232    532       N  
ATOM   6977  NH2 ARG A 447     -29.780 -55.547 -10.652  1.00 77.54           N  
ANISOU 6977  NH2 ARG A 447    10856   8934   9670   -443   -311    562       N  
ATOM   6978  H   ARG A 447     -28.793 -60.044 -16.291  1.00 86.80           H  
ATOM   6979  HA  ARG A 447     -29.470 -58.593 -14.111  1.00 89.88           H  
ATOM   6980  HB2 ARG A 447     -27.564 -57.750 -15.989  1.00 83.20           H  
ATOM   6981  HB3 ARG A 447     -28.449 -56.663 -15.245  1.00 83.20           H  
ATOM   6982  HG2 ARG A 447     -27.247 -58.315 -13.457  1.00 73.47           H  
ATOM   6983  HG3 ARG A 447     -26.174 -57.578 -14.372  1.00 73.47           H  
ATOM   6984  HD2 ARG A 447     -26.454 -56.261 -12.544  1.00 89.09           H  
ATOM   6985  HD3 ARG A 447     -27.194 -55.514 -13.736  1.00 89.09           H  
ATOM   6986  HE  ARG A 447     -29.083 -56.774 -12.628  1.00102.35           H  
ATOM   6987 HH11 ARG A 447     -26.901 -54.681 -11.278  1.00103.61           H  
ATOM   6988 HH12 ARG A 447     -27.779 -54.223 -10.165  1.00103.61           H  
ATOM   6989 HH21 ARG A 447     -30.411 -56.061 -10.930  1.00 93.04           H  
ATOM   6990 HH22 ARG A 447     -29.900 -55.058  -9.955  1.00 93.04           H  
ATOM   6991  N   PRO A 503     -46.026 -71.918 -12.458  1.00100.41           N  
ANISOU 6991  N   PRO A 503    13689  11458  13003   1237   -840   1844       N  
ATOM   6992  CA  PRO A 503     -46.094 -70.616 -11.789  1.00101.71           C  
ANISOU 6992  CA  PRO A 503    13831  11590  13226   1339   -888   1879       C  
ATOM   6993  C   PRO A 503     -45.119 -70.491 -10.621  1.00102.11           C  
ANISOU 6993  C   PRO A 503    13891  11567  13337   1311   -834   1829       C  
ATOM   6994  O   PRO A 503     -44.178 -71.277 -10.516  1.00102.31           O  
ANISOU 6994  O   PRO A 503    13953  11548  13373   1170   -792   1747       O  
ATOM   6995  CB  PRO A 503     -47.539 -70.569 -11.294  1.00 99.30           C  
ANISOU 6995  CB  PRO A 503    13403  11459  12866   1530   -854   1947       C  
ATOM   6996  CG  PRO A 503     -48.293 -71.315 -12.341  1.00 94.74           C  
ANISOU 6996  CG  PRO A 503    12776  10984  12237   1504   -867   1986       C  
ATOM   6997  CD  PRO A 503     -47.365 -72.400 -12.844  1.00 96.78           C  
ANISOU 6997  CD  PRO A 503    13102  11171  12498   1324   -818   1928       C  
ATOM   6998  HA  PRO A 503     -45.942 -69.897 -12.421  1.00122.06           H  
ATOM   6999  HB2 PRO A 503     -47.609 -71.011 -10.433  1.00119.16           H  
ATOM   7000  HB3 PRO A 503     -47.840 -69.648 -11.238  1.00119.16           H  
ATOM   7001  HG2 PRO A 503     -49.090 -71.706 -11.949  1.00113.69           H  
ATOM   7002  HG3 PRO A 503     -48.531 -70.711 -13.062  1.00113.69           H  
ATOM   7003  HD2 PRO A 503     -47.560 -73.242 -12.405  1.00116.13           H  
ATOM   7004  HD3 PRO A 503     -47.430 -72.479 -13.809  1.00116.13           H  
ATOM   7005  N   ASN A 504     -45.354 -69.507  -9.759  1.00121.03           N  
ANISOU 7005  N   ASN A 504    16271  13982  15734   1461   -797   1853       N  
ATOM   7006  CA  ASN A 504     -44.468 -69.234  -8.634  1.00123.16           C  
ANISOU 7006  CA  ASN A 504    16569  14193  16032   1465   -731   1801       C  
ATOM   7007  C   ASN A 504     -44.427 -70.385  -7.643  1.00123.59           C  
ANISOU 7007  C   ASN A 504    16577  14302  16081   1441   -674   1765       C  
ATOM   7008  O   ASN A 504     -43.417 -70.606  -6.974  1.00123.01           O  
ANISOU 7008  O   ASN A 504    16529  14163  16047   1365   -640   1711       O  
ATOM   7009  CB  ASN A 504     -44.929 -67.972  -7.902  1.00122.62           C  
ANISOU 7009  CB  ASN A 504    16547  14151  15893   1675   -689   1807       C  
ATOM   7010  CG  ASN A 504     -43.877 -67.428  -6.952  1.00125.81           C  
ANISOU 7010  CG  ASN A 504    17037  14471  16296   1681   -628   1738       C  
ATOM   7011  OD1 ASN A 504     -43.175 -66.469  -7.272  1.00127.60           O  
ANISOU 7011  OD1 ASN A 504    17371  14604  16506   1678   -623   1710       O  
ATOM   7012  ND2 ASN A 504     -43.761 -68.041  -5.778  1.00126.65           N  
ANISOU 7012  ND2 ASN A 504    17107  14614  16399   1695   -577   1706       N  
ATOM   7013  H   ASN A 504     -46.030 -68.978  -9.804  1.00145.24           H  
ATOM   7014  HA  ASN A 504     -43.568 -69.083  -8.964  1.00147.79           H  
ATOM   7015  HB2 ASN A 504     -45.130 -67.283  -8.554  1.00147.15           H  
ATOM   7016  HB3 ASN A 504     -45.723 -68.180  -7.383  1.00147.15           H  
ATOM   7017 HD21 ASN A 504     -44.269 -68.709  -5.590  1.00151.98           H  
ATOM   7018 HD22 ASN A 504     -43.179 -67.769  -5.207  1.00151.98           H  
ATOM   7019  N   GLU A 505     -45.529 -71.120  -7.549  1.00109.72           N  
ANISOU 7019  N   GLU A 505    14732  12683  14275   1512   -647   1807       N  
ATOM   7020  CA  GLU A 505     -45.688 -72.093  -6.479  1.00107.59           C  
ANISOU 7020  CA  GLU A 505    14380  12500  13998   1526   -555   1807       C  
ATOM   7021  C   GLU A 505     -45.037 -73.437  -6.761  1.00104.63           C  
ANISOU 7021  C   GLU A 505    13999  12101  13653   1353   -515   1777       C  
ATOM   7022  O   GLU A 505     -44.830 -73.826  -7.913  1.00101.42           O  
ANISOU 7022  O   GLU A 505    13632  11659  13244   1246   -543   1767       O  
ATOM   7023  CB  GLU A 505     -47.168 -72.302  -6.169  1.00107.96           C  
ANISOU 7023  CB  GLU A 505    14289  12741  13991   1677   -511   1890       C  
ATOM   7024  CG  GLU A 505     -47.884 -71.049  -5.687  1.00111.43           C  
ANISOU 7024  CG  GLU A 505    14734  13234  14370   1884   -517   1911       C  
ATOM   7025  CD  GLU A 505     -47.103 -70.288  -4.629  1.00117.03           C  
ANISOU 7025  CD  GLU A 505    15538  13853  15074   1936   -485   1850       C  
ATOM   7026  OE1 GLU A 505     -46.876 -70.846  -3.535  1.00119.30           O  
ANISOU 7026  OE1 GLU A 505    15789  14174  15364   1937   -415   1835       O  
ATOM   7027  OE2 GLU A 505     -46.706 -69.133  -4.898  1.00118.74           O  
ANISOU 7027  OE2 GLU A 505    15867  13971  15279   1976   -524   1821       O  
ATOM   7028  H   GLU A 505     -46.196 -71.074  -8.090  1.00131.67           H  
ATOM   7029  HA  GLU A 505     -45.273 -71.734  -5.679  1.00129.11           H  
ATOM   7030  HB2 GLU A 505     -47.615 -72.606  -6.974  1.00129.56           H  
ATOM   7031  HB3 GLU A 505     -47.249 -72.975  -5.475  1.00129.56           H  
ATOM   7032  HG2 GLU A 505     -48.023 -70.456  -6.441  1.00133.72           H  
ATOM   7033  HG3 GLU A 505     -48.738 -71.302  -5.303  1.00133.72           H  
ATOM   7034  N   LYS A 506     -44.719 -74.135  -5.677  1.00 83.39           N  
ANISOU 7034  N   LYS A 506    11260   9440  10983   1336   -433   1764       N  
ATOM   7035  CA  LYS A 506     -44.172 -75.478  -5.756  1.00 69.24           C  
ANISOU 7035  CA  LYS A 506     9431   7649   9229   1187   -362   1749       C  
ATOM   7036  C   LYS A 506     -45.268 -76.528  -5.675  1.00 58.58           C  
ANISOU 7036  C   LYS A 506     7902   6464   7893   1195   -285   1851       C  
ATOM   7037  O   LYS A 506     -46.184 -76.440  -4.856  1.00 57.58           O  
ANISOU 7037  O   LYS A 506     7674   6460   7743   1321   -254   1916       O  
ATOM   7038  CB  LYS A 506     -43.125 -75.696  -4.664  1.00 65.06           C  
ANISOU 7038  CB  LYS A 506     8936   7055   8728   1144   -321   1686       C  
ATOM   7039  CG  LYS A 506     -41.732 -75.322  -5.125  1.00 67.85           C  
ANISOU 7039  CG  LYS A 506     9432   7256   9092   1032   -379   1587       C  
ATOM   7040  CD  LYS A 506     -40.692 -75.450  -4.027  1.00 69.65           C  
ANISOU 7040  CD  LYS A 506     9683   7434   9346    998   -350   1527       C  
ATOM   7041  CE  LYS A 506     -39.288 -75.316  -4.599  1.00 67.70           C  
ANISOU 7041  CE  LYS A 506     9548   7066   9109    866   -402   1437       C  
ATOM   7042  NZ  LYS A 506     -39.016 -76.319  -5.672  1.00 65.64           N  
ANISOU 7042  NZ  LYS A 506     9297   6811   8834    748   -347   1416       N  
ATOM   7043  H   LYS A 506     -44.813 -73.846  -4.873  1.00100.06           H  
ATOM   7044  HA  LYS A 506     -43.729 -75.581  -6.612  1.00 83.09           H  
ATOM   7045  HB2 LYS A 506     -43.346 -75.146  -3.896  1.00 78.07           H  
ATOM   7046  HB3 LYS A 506     -43.118 -76.633  -4.413  1.00 78.07           H  
ATOM   7047  HG2 LYS A 506     -41.473 -75.909  -5.852  1.00 81.42           H  
ATOM   7048  HG3 LYS A 506     -41.737 -74.401  -5.427  1.00 81.42           H  
ATOM   7049  HD2 LYS A 506     -40.825 -74.746  -3.373  1.00 83.58           H  
ATOM   7050  HD3 LYS A 506     -40.771 -76.321  -3.607  1.00 83.58           H  
ATOM   7051  HE2 LYS A 506     -39.184 -74.430  -4.981  1.00 81.24           H  
ATOM   7052  HE3 LYS A 506     -38.642 -75.451  -3.889  1.00 81.24           H  
ATOM   7053  HZ1 LYS A 506     -39.593 -76.213  -6.341  1.00 78.77           H  
ATOM   7054  HZ2 LYS A 506     -38.189 -76.213  -5.984  1.00 78.77           H  
ATOM   7055  HZ3 LYS A 506     -39.099 -77.143  -5.346  1.00 78.77           H  
ATOM   7056  N   VAL A 507     -45.147 -77.517  -6.550  1.00 32.07           N  
ANISOU 7056  N   VAL A 507     4497   3113   4577   1052   -254   1869       N  
ATOM   7057  CA  VAL A 507     -46.108 -78.603  -6.674  1.00 42.11           C  
ANISOU 7057  CA  VAL A 507     5582   4531   5885   1010   -198   1977       C  
ATOM   7058  C   VAL A 507     -46.458 -79.270  -5.348  1.00 49.71           C  
ANISOU 7058  C   VAL A 507     6403   5597   6887   1045   -108   2053       C  
ATOM   7059  O   VAL A 507     -45.623 -79.390  -4.452  1.00 43.10           O  
ANISOU 7059  O   VAL A 507     5632   4683   6060   1021    -86   1976       O  
ATOM   7060  CB  VAL A 507     -45.582 -79.679  -7.646  1.00 45.25           C  
ANISOU 7060  CB  VAL A 507     5938   4889   6364    811   -163   1979       C  
ATOM   7061  CG1 VAL A 507     -45.698 -79.183  -9.073  1.00 45.20           C  
ANISOU 7061  CG1 VAL A 507     5991   4854   6329    792   -222   1979       C  
ATOM   7062  CG2 VAL A 507     -44.137 -80.058  -7.312  1.00 50.97           C  
ANISOU 7062  CG2 VAL A 507     6755   5483   7128    698   -134   1863       C  
ATOM   7063  H   VAL A 507     -44.492 -77.582  -7.104  1.00 38.49           H  
ATOM   7064  HA  VAL A 507     -46.929 -78.247  -7.047  1.00 50.53           H  
ATOM   7065  HB  VAL A 507     -46.128 -80.476  -7.561  1.00 54.29           H  
ATOM   7066 HG11 VAL A 507     -45.172 -78.373  -9.169  1.00 54.24           H  
ATOM   7067 HG12 VAL A 507     -45.364 -79.868  -9.673  1.00 54.24           H  
ATOM   7068 HG13 VAL A 507     -46.630 -78.997  -9.267  1.00 54.24           H  
ATOM   7069 HG21 VAL A 507     -44.104 -80.407  -6.407  1.00 61.16           H  
ATOM   7070 HG22 VAL A 507     -43.835 -80.734  -7.939  1.00 61.16           H  
ATOM   7071 HG23 VAL A 507     -43.579 -79.268  -7.383  1.00 61.16           H  
ATOM   7072  N   LEU A 508     -47.712 -79.695  -5.240  1.00 48.29           N  
ANISOU 7072  N   LEU A 508     5999   5616   6733   1110    -43   2237       N  
ATOM   7073  CA  LEU A 508     -48.180 -80.446  -4.084  1.00 43.92           C  
ANISOU 7073  CA  LEU A 508     5278   5193   6214   1134     52   2347       C  
ATOM   7074  C   LEU A 508     -47.502 -81.811  -4.040  1.00 40.41           C  
ANISOU 7074  C   LEU A 508     4773   4690   5890    929    100   2353       C  
ATOM   7075  O   LEU A 508     -46.975 -82.277  -5.049  1.00 34.20           O  
ANISOU 7075  O   LEU A 508     4018   3813   5163    777     70   2310       O  
ATOM   7076  CB  LEU A 508     -49.696 -80.638  -4.166  1.00 46.54           C  
ANISOU 7076  CB  LEU A 508     5365   5787   6532   1228    100   2557       C  
ATOM   7077  CG  LEU A 508     -50.575 -79.438  -3.810  1.00 50.20           C  
ANISOU 7077  CG  LEU A 508     5839   6371   6863   1468     80   2562       C  
ATOM   7078  CD1 LEU A 508     -51.979 -79.620  -4.368  1.00 47.80           C  
ANISOU 7078  CD1 LEU A 508     5301   6334   6527   1530    101   2747       C  
ATOM   7079  CD2 LEU A 508     -50.620 -79.254  -2.303  1.00 49.99           C  
ANISOU 7079  CD2 LEU A 508     5815   6391   6787   1586    138   2545       C  
ATOM   7080  H   LEU A 508     -48.320 -79.557  -5.832  1.00 57.95           H  
ATOM   7081  HA  LEU A 508     -47.968 -79.964  -3.270  1.00 52.70           H  
ATOM   7082  HB2 LEU A 508     -49.918 -80.894  -5.075  1.00 55.85           H  
ATOM   7083  HB3 LEU A 508     -49.940 -81.358  -3.564  1.00 55.85           H  
ATOM   7084  HG  LEU A 508     -50.194 -78.637  -4.202  1.00 60.24           H  
ATOM   7085 HD11 LEU A 508     -52.368 -80.423  -3.989  1.00 57.36           H  
ATOM   7086 HD12 LEU A 508     -52.515 -78.848  -4.130  1.00 57.36           H  
ATOM   7087 HD13 LEU A 508     -51.926 -79.702  -5.334  1.00 57.36           H  
ATOM   7088 HD21 LEU A 508     -49.719 -79.102  -1.977  1.00 59.98           H  
ATOM   7089 HD22 LEU A 508     -51.180 -78.490  -2.095  1.00 59.98           H  
ATOM   7090 HD23 LEU A 508     -50.988 -80.055  -1.898  1.00 59.98           H  
ATOM   7091  N   PRO A 509     -47.502 -82.457  -2.864  1.00 44.73           N  
ANISOU 7091  N   PRO A 509     5237   5288   6470    928    171   2399       N  
ATOM   7092  CA  PRO A 509     -47.056 -83.852  -2.815  1.00 38.96           C  
ANISOU 7092  CA  PRO A 509     4418   4524   5861    738    209   2424       C  
ATOM   7093  C   PRO A 509     -47.997 -84.749  -3.612  1.00 36.55           C  
ANISOU 7093  C   PRO A 509     3882   4357   5650    631    222   2615       C  
ATOM   7094  O   PRO A 509     -49.200 -84.487  -3.663  1.00 37.28           O  
ANISOU 7094  O   PRO A 509     3815   4646   5705    729    241   2785       O  
ATOM   7095  CB  PRO A 509     -47.109 -84.188  -1.321  1.00 32.92           C  
ANISOU 7095  CB  PRO A 509     3597   3818   5092    798    279   2465       C  
ATOM   7096  CG  PRO A 509     -47.026 -82.871  -0.629  1.00 37.59           C  
ANISOU 7096  CG  PRO A 509     4336   4391   5556    986    257   2372       C  
ATOM   7097  CD  PRO A 509     -47.751 -81.913  -1.518  1.00 42.98           C  
ANISOU 7097  CD  PRO A 509     5029   5130   6171   1091    207   2399       C  
ATOM   7098  HA  PRO A 509     -46.148 -83.941  -3.145  1.00 46.75           H  
ATOM   7099  HB2 PRO A 509     -47.946 -84.632  -1.114  1.00 39.50           H  
ATOM   7100  HB3 PRO A 509     -46.354 -84.749  -1.084  1.00 39.50           H  
ATOM   7101  HG2 PRO A 509     -47.458 -82.929   0.237  1.00 45.11           H  
ATOM   7102  HG3 PRO A 509     -46.096 -82.612  -0.532  1.00 45.11           H  
ATOM   7103  HD2 PRO A 509     -48.701 -81.919  -1.320  1.00 51.57           H  
ATOM   7104  HD3 PRO A 509     -47.374 -81.023  -1.437  1.00 51.57           H  
ATOM   7105  N   LYS A 510     -47.448 -85.790  -4.229  1.00 56.39           N  
ANISOU 7105  N   LYS A 510     6380   6779   8264    432    201   2574       N  
ATOM   7106  CA  LYS A 510     -48.224 -86.674  -5.091  1.00 64.24           C  
ANISOU 7106  CA  LYS A 510     7183   7880   9348    292    182   2727       C  
ATOM   7107  C   LYS A 510     -49.383 -87.331  -4.346  1.00 64.22           C  
ANISOU 7107  C   LYS A 510     6930   8098   9375    299    233   2958       C  
ATOM   7108  O   LYS A 510     -50.422 -87.622  -4.940  1.00 71.65           O  
ANISOU 7108  O   LYS A 510     7680   9215  10330    248    215   3139       O  
ATOM   7109  CB  LYS A 510     -47.322 -87.754  -5.695  1.00 67.36           C  
ANISOU 7109  CB  LYS A 510     7646   8125   9823     87    143   2590       C  
ATOM   7110  CG  LYS A 510     -48.038 -88.680  -6.672  1.00 69.22           C  
ANISOU 7110  CG  LYS A 510     7727   8443  10131    -78    100   2701       C  
ATOM   7111  CD  LYS A 510     -47.102 -89.728  -7.256  1.00 74.59           C  
ANISOU 7111  CD  LYS A 510     8523   8970  10848   -251     65   2517       C  
ATOM   7112  CE  LYS A 510     -47.833 -90.644  -8.228  1.00 79.58           C  
ANISOU 7112  CE  LYS A 510     9038   9676  11522   -419     17   2592       C  
ATOM   7113  NZ  LYS A 510     -46.926 -91.671  -8.812  1.00 83.71           N  
ANISOU 7113  NZ  LYS A 510     9706  10055  12047   -561     -4   2387       N  
ATOM   7114  H   LYS A 510     -46.618 -86.008  -4.163  1.00 67.66           H  
ATOM   7115  HA  LYS A 510     -48.596 -86.154  -5.820  1.00 77.09           H  
ATOM   7116  HB2 LYS A 510     -46.596 -87.324  -6.173  1.00 80.83           H  
ATOM   7117  HB3 LYS A 510     -46.965 -88.300  -4.977  1.00 80.83           H  
ATOM   7118  HG2 LYS A 510     -48.755 -89.140  -6.208  1.00 83.07           H  
ATOM   7119  HG3 LYS A 510     -48.397 -88.154  -7.404  1.00 83.07           H  
ATOM   7120  HD2 LYS A 510     -46.384 -89.285  -7.736  1.00 89.51           H  
ATOM   7121  HD3 LYS A 510     -46.741 -90.271  -6.538  1.00 89.51           H  
ATOM   7122  HE2 LYS A 510     -48.547 -91.103  -7.758  1.00 95.49           H  
ATOM   7123  HE3 LYS A 510     -48.197 -90.114  -8.954  1.00 95.49           H  
ATOM   7124  HZ1 LYS A 510     -46.581 -92.175  -8.165  1.00100.46           H  
ATOM   7125  HZ2 LYS A 510     -47.378 -92.191  -9.374  1.00100.46           H  
ATOM   7126  HZ3 LYS A 510     -46.263 -91.275  -9.254  1.00100.46           H  
ATOM   7127  N   HIS A 511     -49.202 -87.554  -3.047  1.00 44.94           N  
ANISOU 7127  N   HIS A 511     4486   5664   6926    357    292   2955       N  
ATOM   7128  CA  HIS A 511     -50.192 -88.258  -2.239  1.00 49.47           C  
ANISOU 7128  CA  HIS A 511     4829   6448   7518    353    343   3166       C  
ATOM   7129  C   HIS A 511     -51.027 -87.299  -1.392  1.00 49.13           C  
ANISOU 7129  C   HIS A 511     4710   6606   7351    587    412   3282       C  
ATOM   7130  O   HIS A 511     -51.682 -87.714  -0.440  1.00 62.47           O  
ANISOU 7130  O   HIS A 511     6238   8475   9024    624    473   3431       O  
ATOM   7131  CB  HIS A 511     -49.498 -89.292  -1.346  1.00 48.41           C  
ANISOU 7131  CB  HIS A 511     4737   6207   7449    256    360   3089       C  
ATOM   7132  CG  HIS A 511     -48.767 -90.353  -2.111  1.00 50.29           C  
ANISOU 7132  CG  HIS A 511     5066   6276   7766     48    292   2948       C  
ATOM   7133  ND1 HIS A 511     -49.390 -91.483  -2.597  1.00 62.06           N  
ANISOU 7133  ND1 HIS A 511     6441   7835   9304   -123    251   3028       N  
ATOM   7134  CD2 HIS A 511     -47.467 -90.456  -2.473  1.00 50.31           C  
ANISOU 7134  CD2 HIS A 511     5282   6059   7773     -9    259   2711       C  
ATOM   7135  CE1 HIS A 511     -48.506 -92.235  -3.226  1.00 57.85           C  
ANISOU 7135  CE1 HIS A 511     6062   7118   8800   -263    204   2836       C  
ATOM   7136  NE2 HIS A 511     -47.331 -91.635  -3.166  1.00 53.49           N  
ANISOU 7136  NE2 HIS A 511     5697   6405   8223   -191    211   2654       N  
ATOM   7137  H   HIS A 511     -48.506 -87.305  -2.606  1.00 53.93           H  
ATOM   7138  HA  HIS A 511     -50.796 -88.734  -2.830  1.00 59.36           H  
ATOM   7139  HB2 HIS A 511     -48.854 -88.836  -0.782  1.00 58.09           H  
ATOM   7140  HB3 HIS A 511     -50.167 -89.729  -0.796  1.00 58.09           H  
ATOM   7141  HD1 HIS A 511     -50.225 -91.668  -2.505  1.00 74.47           H  
ATOM   7142  HD2 HIS A 511     -46.792 -89.844  -2.289  1.00 60.37           H  
ATOM   7143  HE1 HIS A 511     -48.681 -93.049  -3.641  1.00 69.42           H  
ATOM   7144  HE2 HIS A 511     -46.599 -91.934  -3.504  1.00 64.19           H  
ATOM   7145  N   SER A 512     -51.006 -86.017  -1.744  1.00 50.75           N  
ANISOU 7145  N   SER A 512     5048   6785   7450    749    392   3191       N  
ATOM   7146  CA  SER A 512     -51.834 -85.028  -1.062  1.00 57.45           C  
ANISOU 7146  CA  SER A 512     5861   7819   8148    991    436   3244       C  
ATOM   7147  C   SER A 512     -53.306 -85.285  -1.355  1.00 59.77           C  
ANISOU 7147  C   SER A 512     5874   8441   8395   1015    454   3483       C  
ATOM   7148  O   SER A 512     -53.668 -85.634  -2.477  1.00 53.12           O  
ANISOU 7148  O   SER A 512     4934   7650   7599    893    399   3565       O  
ATOM   7149  CB  SER A 512     -51.451 -83.616  -1.503  1.00 59.32           C  
ANISOU 7149  CB  SER A 512     6331   7925   8283   1141    375   3056       C  
ATOM   7150  OG  SER A 512     -52.438 -82.677  -1.116  1.00 55.94           O  
ANISOU 7150  OG  SER A 512     5855   7694   7707   1369    393   3098       O  
ATOM   7151  H   SER A 512     -50.521 -85.694  -2.375  1.00 60.90           H  
ATOM   7152  HA  SER A 512     -51.696 -85.097  -0.104  1.00 68.94           H  
ATOM   7153  HB2 SER A 512     -50.607 -83.374  -1.090  1.00 71.18           H  
ATOM   7154  HB3 SER A 512     -51.363 -83.600  -2.469  1.00 71.18           H  
ATOM   7155  HG  SER A 512     -52.215 -81.906  -1.364  1.00 67.13           H  
ATOM   7156  N   LEU A 513     -54.146 -85.109  -0.338  1.00 51.04           N  
ANISOU 7156  N   LEU A 513     4637   7574   7181   1167    526   3590       N  
ATOM   7157  CA  LEU A 513     -55.581 -85.344  -0.463  1.00 52.88           C  
ANISOU 7157  CA  LEU A 513     4588   8172   7331   1198    548   3810       C  
ATOM   7158  C   LEU A 513     -56.169 -84.535  -1.615  1.00 51.87           C  
ANISOU 7158  C   LEU A 513     4464   8124   7120   1281    478   3778       C  
ATOM   7159  O   LEU A 513     -56.947 -85.053  -2.420  1.00 50.41           O  
ANISOU 7159  O   LEU A 513     4074   8136   6942   1170    443   3931       O  
ATOM   7160  CB  LEU A 513     -56.286 -84.975   0.847  1.00 46.54           C  
ANISOU 7160  CB  LEU A 513     3704   7597   6381   1397    636   3862       C  
ATOM   7161  CG  LEU A 513     -55.974 -85.870   2.050  1.00 46.37           C  
ANISOU 7161  CG  LEU A 513     3615   7580   6423   1319    713   3946       C  
ATOM   7162  CD1 LEU A 513     -55.717 -85.041   3.304  1.00 51.70           C  
ANISOU 7162  CD1 LEU A 513     4440   8220   6984   1538    773   3821       C  
ATOM   7163  CD2 LEU A 513     -57.106 -86.858   2.287  1.00 48.27           C  
ANISOU 7163  CD2 LEU A 513     3525   8174   6643   1216    754   4224       C  
ATOM   7164  H   LEU A 513     -53.905 -84.849   0.445  1.00 61.24           H  
ATOM   7165  HA  LEU A 513     -55.738 -86.285  -0.639  1.00 63.45           H  
ATOM   7166  HB2 LEU A 513     -56.032 -84.070   1.085  1.00 55.84           H  
ATOM   7167  HB3 LEU A 513     -57.244 -85.013   0.699  1.00 55.84           H  
ATOM   7168  HG  LEU A 513     -55.170 -86.379   1.861  1.00 55.64           H  
ATOM   7169 HD11 LEU A 513     -56.508 -84.515   3.502  1.00 62.04           H  
ATOM   7170 HD12 LEU A 513     -55.523 -85.639   4.043  1.00 62.04           H  
ATOM   7171 HD13 LEU A 513     -54.961 -84.455   3.145  1.00 62.04           H  
ATOM   7172 HD21 LEU A 513     -57.212 -87.411   1.497  1.00 57.93           H  
ATOM   7173 HD22 LEU A 513     -56.886 -87.413   3.052  1.00 57.93           H  
ATOM   7174 HD23 LEU A 513     -57.923 -86.366   2.459  1.00 57.93           H  
ATOM   7175  N   LEU A 514     -55.770 -83.270  -1.697  1.00 58.04           N  
ANISOU 7175  N   LEU A 514     5482   8749   7821   1463    446   3576       N  
ATOM   7176  CA  LEU A 514     -56.307 -82.351  -2.694  1.00 65.74           C  
ANISOU 7176  CA  LEU A 514     6489   9782   8706   1574    375   3525       C  
ATOM   7177  C   LEU A 514     -55.920 -82.787  -4.103  1.00 63.81           C  
ANISOU 7177  C   LEU A 514     6256   9414   8574   1376    295   3536       C  
ATOM   7178  O   LEU A 514     -56.749 -82.779  -5.016  1.00 73.07           O  
ANISOU 7178  O   LEU A 514     7286  10772   9706   1362    250   3626       O  
ATOM   7179  CB  LEU A 514     -55.787 -80.937  -2.423  1.00 70.65           C  
ANISOU 7179  CB  LEU A 514     7392  10211   9240   1779    341   3302       C  
ATOM   7180  CG  LEU A 514     -56.667 -79.710  -2.688  1.00 75.72           C  
ANISOU 7180  CG  LEU A 514     8054  10989   9727   2011    302   3251       C  
ATOM   7181  CD1 LEU A 514     -58.146 -79.958  -2.418  1.00 76.56           C  
ANISOU 7181  CD1 LEU A 514     7875  11493   9721   2102    358   3420       C  
ATOM   7182  CD2 LEU A 514     -56.174 -78.562  -1.817  1.00 80.47           C  
ANISOU 7182  CD2 LEU A 514     8892  11428  10255   2193    293   3072       C  
ATOM   7183  H   LEU A 514     -55.182 -82.916  -1.180  1.00 69.64           H  
ATOM   7184  HA  LEU A 514     -57.275 -82.338  -2.632  1.00 78.88           H  
ATOM   7185  HB2 LEU A 514     -55.539 -80.896  -1.486  1.00 84.78           H  
ATOM   7186  HB3 LEU A 514     -54.987 -80.817  -2.959  1.00 84.78           H  
ATOM   7187  HG  LEU A 514     -56.572 -79.446  -3.616  1.00 90.86           H  
ATOM   7188 HD11 LEU A 514     -58.259 -80.208  -1.487  1.00 91.87           H  
ATOM   7189 HD12 LEU A 514     -58.642 -79.145  -2.604  1.00 91.87           H  
ATOM   7190 HD13 LEU A 514     -58.456 -80.674  -2.994  1.00 91.87           H  
ATOM   7191 HD21 LEU A 514     -55.252 -78.367  -2.046  1.00 96.56           H  
ATOM   7192 HD22 LEU A 514     -56.728 -77.782  -1.980  1.00 96.56           H  
ATOM   7193 HD23 LEU A 514     -56.236 -78.824  -0.885  1.00 96.56           H  
ATOM   7194  N   TYR A 515     -54.656 -83.165  -4.276  1.00 63.46           N  
ANISOU 7194  N   TYR A 515     6382   9068   8661   1221    276   3432       N  
ATOM   7195  CA  TYR A 515     -54.168 -83.626  -5.570  1.00 60.56           C  
ANISOU 7195  CA  TYR A 515     6046   8561   8404   1020    203   3424       C  
ATOM   7196  C   TYR A 515     -54.916 -84.890  -5.994  1.00 65.66           C  
ANISOU 7196  C   TYR A 515     6405   9416   9127    815    199   3656       C  
ATOM   7197  O   TYR A 515     -55.446 -84.961  -7.102  1.00 67.70           O  
ANISOU 7197  O   TYR A 515     6564   9783   9377    742    133   3734       O  
ATOM   7198  CB  TYR A 515     -52.661 -83.889  -5.512  1.00 53.80           C  
ANISOU 7198  CB  TYR A 515     5417   7365   7660    889    194   3248       C  
ATOM   7199  CG  TYR A 515     -52.026 -84.101  -6.868  1.00 61.23           C  
ANISOU 7199  CG  TYR A 515     6448   8136   8683    716    118   3178       C  
ATOM   7200  CD1 TYR A 515     -51.672 -83.021  -7.665  1.00 65.70           C  
ANISOU 7200  CD1 TYR A 515     7205   8581   9178    803     53   3040       C  
ATOM   7201  CD2 TYR A 515     -51.777 -85.380  -7.350  1.00 56.93           C  
ANISOU 7201  CD2 TYR A 515     5807   7546   8276    461    103   3237       C  
ATOM   7202  CE1 TYR A 515     -51.089 -83.208  -8.906  1.00 67.02           C  
ANISOU 7202  CE1 TYR A 515     7451   8607   9406    647    -11   2979       C  
ATOM   7203  CE2 TYR A 515     -51.195 -85.577  -8.589  1.00 57.65           C  
ANISOU 7203  CE2 TYR A 515     5987   7488   8427    305     34   3152       C  
ATOM   7204  CZ  TYR A 515     -50.853 -84.488  -9.362  1.00 65.16           C  
ANISOU 7204  CZ  TYR A 515     7112   8340   9304    401    -16   3034       C  
ATOM   7205  OH  TYR A 515     -50.273 -84.685 -10.594  1.00 64.91           O  
ANISOU 7205  OH  TYR A 515     7164   8176   9322    246    -78   2954       O  
ATOM   7206  H   TYR A 515     -54.060 -83.163  -3.656  1.00 76.15           H  
ATOM   7207  HA  TYR A 515     -54.331 -82.939  -6.235  1.00 72.67           H  
ATOM   7208  HB2 TYR A 515     -52.227 -83.127  -5.097  1.00 64.56           H  
ATOM   7209  HB3 TYR A 515     -52.503 -84.686  -4.983  1.00 64.56           H  
ATOM   7210  HD1 TYR A 515     -51.830 -82.156  -7.361  1.00 78.84           H  
ATOM   7211  HD2 TYR A 515     -52.006 -86.117  -6.831  1.00 68.31           H  
ATOM   7212  HE1 TYR A 515     -50.857 -82.475  -9.430  1.00 80.42           H  
ATOM   7213  HE2 TYR A 515     -51.035 -86.439  -8.898  1.00 69.17           H  
ATOM   7214  HH  TYR A 515     -50.188 -85.507 -10.744  1.00 77.89           H  
ATOM   7215  N   GLU A 516     -54.960 -85.877  -5.102  1.00 71.17           N  
ANISOU 7215  N   GLU A 516     6976  10174   9892    712    258   3766       N  
ATOM   7216  CA  GLU A 516     -55.687 -87.120  -5.354  1.00 77.09           C  
ANISOU 7216  CA  GLU A 516     7458  11127  10704    492    243   3992       C  
ATOM   7217  C   GLU A 516     -57.124 -86.822  -5.791  1.00 77.80           C  
ANISOU 7217  C   GLU A 516     7305  11600  10656    575    220   4158       C  
ATOM   7218  O   GLU A 516     -57.594 -87.324  -6.830  1.00 80.72           O  
ANISOU 7218  O   GLU A 516     7536  12087  11049    404    143   4272       O  
ATOM   7219  CB  GLU A 516     -55.686 -87.999  -4.098  1.00 79.71           C  
ANISOU 7219  CB  GLU A 516     7695  11508  11084    429    314   4071       C  
ATOM   7220  CG  GLU A 516     -54.301 -88.433  -3.618  1.00 82.69           C  
ANISOU 7220  CG  GLU A 516     8300  11532  11588    345    321   3865       C  
ATOM   7221  CD  GLU A 516     -53.773 -89.650  -4.354  1.00 84.38           C  
ANISOU 7221  CD  GLU A 516     8568  11563  11931     57    243   3769       C  
ATOM   7222  OE1 GLU A 516     -53.783 -89.645  -5.602  1.00 92.33           O  
ANISOU 7222  OE1 GLU A 516     9597  12529  12956    -50    175   3737       O  
ATOM   7223  OE2 GLU A 516     -53.337 -90.610  -3.682  1.00 70.09           O  
ANISOU 7223  OE2 GLU A 516     6807   9644  10180    -50    247   3691       O  
ATOM   7224  H   GLU A 516     -54.573 -85.852  -4.335  1.00 85.41           H  
ATOM   7225  HA  GLU A 516     -55.247 -87.609  -6.068  1.00 92.50           H  
ATOM   7226  HB2 GLU A 516     -56.104 -87.505  -3.375  1.00 95.65           H  
ATOM   7227  HB3 GLU A 516     -56.197 -88.802  -4.282  1.00 95.65           H  
ATOM   7228  HG2 GLU A 516     -53.676 -87.705  -3.757  1.00 99.23           H  
ATOM   7229  HG3 GLU A 516     -54.349 -88.652  -2.674  1.00 99.23           H  
ATOM   7230  N   TYR A 517     -57.806 -85.995  -4.997  1.00 65.99           N  
ANISOU 7230  N   TYR A 517     5775  10295   9003    831    281   4136       N  
ATOM   7231  CA  TYR A 517     -59.143 -85.517  -5.336  1.00 67.73           C  
ANISOU 7231  CA  TYR A 517     5813  10863   9060    952    269   4201       C  
ATOM   7232  C   TYR A 517     -59.179 -84.951  -6.751  1.00 71.25           C  
ANISOU 7232  C   TYR A 517     6325  11255   9491    952    172   4125       C  
ATOM   7233  O   TYR A 517     -60.040 -85.316  -7.556  1.00 73.74           O  
ANISOU 7233  O   TYR A 517     6435  11811   9771    845    119   4231       O  
ATOM   7234  CB  TYR A 517     -59.585 -84.415  -4.366  1.00 68.78           C  
ANISOU 7234  CB  TYR A 517     6016  11093   9023   1262    339   4102       C  
ATOM   7235  CG  TYR A 517     -60.356 -84.856  -3.136  1.00 72.96           C  
ANISOU 7235  CG  TYR A 517     6356  11899   9466   1303    432   4232       C  
ATOM   7236  CD1 TYR A 517     -60.952 -86.109  -3.051  1.00 78.60           C  
ANISOU 7236  CD1 TYR A 517     6810  12840  10212   1075    439   4438       C  
ATOM   7237  CD2 TYR A 517     -60.504 -83.992  -2.060  1.00 73.93           C  
ANISOU 7237  CD2 TYR A 517     6573  12055   9462   1561    501   4139       C  
ATOM   7238  CE1 TYR A 517     -61.658 -86.490  -1.925  1.00 77.51           C  
ANISOU 7238  CE1 TYR A 517     6524  12950   9975   1106    517   4550       C  
ATOM   7239  CE2 TYR A 517     -61.206 -84.362  -0.934  1.00 69.44           C  
ANISOU 7239  CE2 TYR A 517     5841  11744   8798   1604    586   4256       C  
ATOM   7240  CZ  TYR A 517     -61.782 -85.612  -0.871  1.00 78.09           C  
ANISOU 7240  CZ  TYR A 517     6686  13064   9920   1378    596   4465       C  
ATOM   7241  OH  TYR A 517     -62.482 -85.981   0.253  1.00 89.47           O  
ANISOU 7241  OH  TYR A 517     7984  14760  11251   1411    671   4579       O  
ATOM   7242  H   TYR A 517     -57.510 -85.695  -4.247  1.00 79.19           H  
ATOM   7243  HA  TYR A 517     -59.775 -86.251  -5.280  1.00 81.28           H  
ATOM   7244  HB2 TYR A 517     -58.792 -83.950  -4.056  1.00 82.53           H  
ATOM   7245  HB3 TYR A 517     -60.150 -83.794  -4.852  1.00 82.53           H  
ATOM   7246  HD1 TYR A 517     -60.869 -86.704  -3.762  1.00 94.31           H  
ATOM   7247  HD2 TYR A 517     -60.116 -83.147  -2.098  1.00 88.71           H  
ATOM   7248  HE1 TYR A 517     -62.048 -87.333  -1.880  1.00 93.01           H  
ATOM   7249  HE2 TYR A 517     -61.291 -83.772  -0.221  1.00 83.32           H  
ATOM   7250  HH  TYR A 517     -62.478 -85.355   0.813  1.00107.37           H  
ATOM   7251  N   PHE A 518     -58.250 -84.046  -7.047  1.00 66.53           N  
ANISOU 7251  N   PHE A 518     6018  10351   8911   1061    146   3931       N  
ATOM   7252  CA  PHE A 518     -58.193 -83.436  -8.369  1.00 67.56           C  
ANISOU 7252  CA  PHE A 518     6240  10407   9022   1069     54   3854       C  
ATOM   7253  C   PHE A 518     -58.055 -84.485  -9.466  1.00 66.17           C  
ANISOU 7253  C   PHE A 518     5949  10223   8969    773    -21   3969       C  
ATOM   7254  O   PHE A 518     -58.732 -84.403 -10.488  1.00 66.47           O  
ANISOU 7254  O   PHE A 518     5872  10430   8956    737    -92   4017       O  
ATOM   7255  CB  PHE A 518     -57.043 -82.432  -8.471  1.00 67.51           C  
ANISOU 7255  CB  PHE A 518     6579  10044   9030   1180     31   3629       C  
ATOM   7256  CG  PHE A 518     -56.657 -82.098  -9.888  1.00 66.77           C  
ANISOU 7256  CG  PHE A 518     6600   9808   8962   1107    -65   3564       C  
ATOM   7257  CD1 PHE A 518     -55.743 -82.882 -10.577  1.00 64.54           C  
ANISOU 7257  CD1 PHE A 518     6378   9317   8827    858   -101   3562       C  
ATOM   7258  CD2 PHE A 518     -57.211 -81.005 -10.532  1.00 68.95           C  
ANISOU 7258  CD2 PHE A 518     6930  10157   9113   1285   -121   3502       C  
ATOM   7259  CE1 PHE A 518     -55.394 -82.585 -11.878  1.00 65.19           C  
ANISOU 7259  CE1 PHE A 518     6564   9281   8922    786   -186   3505       C  
ATOM   7260  CE2 PHE A 518     -56.860 -80.701 -11.835  1.00 68.19           C  
ANISOU 7260  CE2 PHE A 518     6939   9938   9034   1216   -210   3451       C  
ATOM   7261  CZ  PHE A 518     -55.950 -81.492 -12.508  1.00 62.96           C  
ANISOU 7261  CZ  PHE A 518     6329   9083   8511    965   -239   3457       C  
ATOM   7262  H   PHE A 518     -57.644 -83.770  -6.503  1.00 79.84           H  
ATOM   7263  HA  PHE A 518     -59.020 -82.954  -8.525  1.00 81.07           H  
ATOM   7264  HB2 PHE A 518     -57.306 -81.608  -8.033  1.00 81.02           H  
ATOM   7265  HB3 PHE A 518     -56.262 -82.804  -8.031  1.00 81.02           H  
ATOM   7266  HD1 PHE A 518     -55.366 -83.621 -10.158  1.00 77.45           H  
ATOM   7267  HD2 PHE A 518     -57.825 -80.470 -10.084  1.00 82.74           H  
ATOM   7268  HE1 PHE A 518     -54.779 -83.119 -12.328  1.00 78.22           H  
ATOM   7269  HE2 PHE A 518     -57.238 -79.964 -12.258  1.00 81.83           H  
ATOM   7270  HZ  PHE A 518     -55.714 -81.288 -13.384  1.00 75.56           H  
ATOM   7271  N   THR A 519     -57.170 -85.459  -9.266  1.00 50.61           N  
ANISOU 7271  N   THR A 519     4025   8048   7156    557    -11   3998       N  
ATOM   7272  CA  THR A 519     -56.972 -86.492 -10.278  1.00 54.23           C  
ANISOU 7272  CA  THR A 519     4417   8456   7730    250    -86   4096       C  
ATOM   7273  C   THR A 519     -58.260 -87.269 -10.516  1.00 57.21           C  
ANISOU 7273  C   THR A 519     4480   9197   8062     86    -89   4209       C  
ATOM   7274  O   THR A 519     -58.677 -87.421 -11.669  1.00 58.37           O  
ANISOU 7274  O   THR A 519     4549   9435   8194    -53   -156   4196       O  
ATOM   7275  CB  THR A 519     -55.845 -87.491  -9.921  1.00 45.38           C  
ANISOU 7275  CB  THR A 519     3438   7029   6777     11    -39   4018       C  
ATOM   7276  OG1 THR A 519     -56.203 -88.231  -8.747  1.00 52.85           O  
ANISOU 7276  OG1 THR A 519     4245   8098   7737    -33     38   4108       O  
ATOM   7277  CG2 THR A 519     -54.514 -86.772  -9.708  1.00 41.79           C  
ANISOU 7277  CG2 THR A 519     3290   6225   6363    133    -25   3762       C  
ATOM   7278  H   THR A 519     -56.680 -85.544  -8.565  1.00 60.73           H  
ATOM   7279  HA  THR A 519     -56.729 -86.063 -11.114  1.00 65.07           H  
ATOM   7280  HB  THR A 519     -55.731 -88.111 -10.659  1.00 54.46           H  
ATOM   7281  HG1 THR A 519     -56.318 -87.706  -8.102  1.00 63.42           H  
ATOM   7282 HG21 THR A 519     -54.596 -86.133  -8.983  1.00 50.15           H  
ATOM   7283 HG22 THR A 519     -53.822 -87.414  -9.485  1.00 50.15           H  
ATOM   7284 HG23 THR A 519     -54.259 -86.301 -10.516  1.00 50.15           H  
ATOM   7285  N   VAL A 520     -58.900 -87.753  -9.448  1.00 63.69           N  
ANISOU 7285  N   VAL A 520     5116  10232   8852     91    -16   4313       N  
ATOM   7286  CA  VAL A 520     -60.143 -88.508  -9.650  1.00 64.19           C  
ANISOU 7286  CA  VAL A 520     4869  10654   8865    -86    -15   4417       C  
ATOM   7287  C   VAL A 520     -61.221 -87.658 -10.306  1.00 59.05           C  
ANISOU 7287  C   VAL A 520     4083  10304   8049     98    -73   4439       C  
ATOM   7288  O   VAL A 520     -61.853 -88.106 -11.259  1.00 62.06           O  
ANISOU 7288  O   VAL A 520     4362  10819   8399    -94   -126   4434       O  
ATOM   7289  CB  VAL A 520     -60.729 -89.158  -8.363  1.00 71.81           C  
ANISOU 7289  CB  VAL A 520     5743  11771   9769   -100     59   4483       C  
ATOM   7290  CG1 VAL A 520     -59.988 -90.445  -8.030  1.00 70.87           C  
ANISOU 7290  CG1 VAL A 520     5794  11355   9780   -358     48   4377       C  
ATOM   7291  CG2 VAL A 520     -60.751 -88.186  -7.190  1.00 72.99           C  
ANISOU 7291  CG2 VAL A 520     5891  12007   9835    250    135   4533       C  
ATOM   7292  H   VAL A 520     -58.650 -87.665  -8.630  1.00 76.43           H  
ATOM   7293  HA  VAL A 520     -59.949 -89.234 -10.263  1.00 77.02           H  
ATOM   7294  HB  VAL A 520     -61.650 -89.401  -8.545  1.00 86.17           H  
ATOM   7295 HG11 VAL A 520     -59.051 -90.241  -7.886  1.00 85.05           H  
ATOM   7296 HG12 VAL A 520     -60.371 -90.830  -7.226  1.00 85.05           H  
ATOM   7297 HG13 VAL A 520     -60.083 -91.064  -8.771  1.00 85.05           H  
ATOM   7298 HG21 VAL A 520     -61.300 -87.421  -7.425  1.00 87.59           H  
ATOM   7299 HG22 VAL A 520     -61.123 -88.635  -6.415  1.00 87.59           H  
ATOM   7300 HG23 VAL A 520     -59.844 -87.898  -7.003  1.00 87.59           H  
ATOM   7301  N   TYR A 521     -61.431 -86.442  -9.808  1.00 67.82           N  
ANISOU 7301  N   TYR A 521     5291  11455   9022    446    -40   4392       N  
ATOM   7302  CA  TYR A 521     -62.435 -85.565 -10.403  1.00 76.80           C  
ANISOU 7302  CA  TYR A 521     6373  12822   9987    621    -65   4353       C  
ATOM   7303  C   TYR A 521     -62.133 -85.325 -11.879  1.00 86.57           C  
ANISOU 7303  C   TYR A 521     7682  13949  11264    540   -176   4298       C  
ATOM   7304  O   TYR A 521     -63.004 -85.521 -12.722  1.00 93.47           O  
ANISOU 7304  O   TYR A 521     8389  15056  12070    442   -227   4333       O  
ATOM   7305  CB  TYR A 521     -62.535 -84.224  -9.658  1.00 79.32           C  
ANISOU 7305  CB  TYR A 521     6850  13115  10175    989     -4   4241       C  
ATOM   7306  CG  TYR A 521     -63.597 -84.160  -8.570  1.00 88.67           C  
ANISOU 7306  CG  TYR A 521     7872  14607  11211   1127     85   4301       C  
ATOM   7307  CD1 TYR A 521     -64.800 -84.848  -8.692  1.00 94.85           C  
ANISOU 7307  CD1 TYR A 521     8382  15750  11908    996     86   4420       C  
ATOM   7308  CD2 TYR A 521     -63.399 -83.395  -7.427  1.00 92.46           C  
ANISOU 7308  CD2 TYR A 521     8490  15014  11628   1379    164   4221       C  
ATOM   7309  CE1 TYR A 521     -65.767 -84.781  -7.707  1.00 97.51           C  
ANISOU 7309  CE1 TYR A 521     8583  16370  12096   1120    164   4473       C  
ATOM   7310  CE2 TYR A 521     -64.362 -83.325  -6.434  1.00 94.02           C  
ANISOU 7310  CE2 TYR A 521     8542  15499  11681   1508    243   4277       C  
ATOM   7311  CZ  TYR A 521     -65.542 -84.022  -6.578  1.00 97.44           C  
ANISOU 7311  CZ  TYR A 521     8700  16294  12028   1381    244   4410       C  
ATOM   7312  OH  TYR A 521     -66.504 -83.958  -5.595  1.00 97.91           O  
ANISOU 7312  OH  TYR A 521     8622  16645  11933   1504    319   4466       O  
ATOM   7313  H   TYR A 521     -61.012 -86.105  -9.137  1.00 81.39           H  
ATOM   7314  HA  TYR A 521     -63.300 -85.999 -10.346  1.00 92.16           H  
ATOM   7315  HB2 TYR A 521     -61.679 -84.040  -9.240  1.00 95.19           H  
ATOM   7316  HB3 TYR A 521     -62.737 -83.529 -10.303  1.00 95.19           H  
ATOM   7317  HD1 TYR A 521     -64.956 -85.363  -9.450  1.00113.83           H  
ATOM   7318  HD2 TYR A 521     -62.603 -82.925  -7.324  1.00110.96           H  
ATOM   7319  HE1 TYR A 521     -66.564 -85.251  -7.802  1.00117.01           H  
ATOM   7320  HE2 TYR A 521     -64.212 -82.812  -5.672  1.00112.82           H  
ATOM   7321  HH  TYR A 521     -66.242 -83.465  -4.968  1.00117.49           H  
ATOM   7322  N   ASN A 522     -60.902 -84.926 -12.189  1.00 90.40           N  
ANISOU 7322  N   ASN A 522     8427  14073  11847    567   -210   4204       N  
ATOM   7323  CA  ASN A 522     -60.524 -84.636 -13.567  1.00 83.25           C  
ANISOU 7323  CA  ASN A 522     7625  13038  10968    498   -314   4148       C  
ATOM   7324  C   ASN A 522     -60.663 -85.850 -14.481  1.00 78.58           C  
ANISOU 7324  C   ASN A 522     6859  12525  10471    136   -380   4216       C  
ATOM   7325  O   ASN A 522     -61.115 -85.721 -15.617  1.00 83.31           O  
ANISOU 7325  O   ASN A 522     7392  13240  11020     73   -459   4207       O  
ATOM   7326  CB  ASN A 522     -59.110 -84.065 -13.652  1.00 82.61           C  
ANISOU 7326  CB  ASN A 522     7887  12532  10969    555   -319   4009       C  
ATOM   7327  CG  ASN A 522     -58.799 -83.499 -15.027  1.00 85.29           C  
ANISOU 7327  CG  ASN A 522     8362  12752  11293    538   -415   3932       C  
ATOM   7328  OD1 ASN A 522     -59.697 -83.295 -15.845  1.00 87.82           O  
ANISOU 7328  OD1 ASN A 522     8540  13307  11519    552   -474   3969       O  
ATOM   7329  ND2 ASN A 522     -57.526 -83.237 -15.286  1.00 87.70           N  
ANISOU 7329  ND2 ASN A 522     8944  12695  11683    503   -425   3811       N  
ATOM   7330  H   ASN A 522     -60.267 -84.817 -11.619  1.00108.48           H  
ATOM   7331  HA  ASN A 522     -61.126 -83.955 -13.905  1.00 99.90           H  
ATOM   7332  HB2 ASN A 522     -59.017 -83.349 -13.004  1.00 99.13           H  
ATOM   7333  HB3 ASN A 522     -58.470 -84.769 -13.464  1.00 99.13           H  
ATOM   7334 HD21 ASN A 522     -56.926 -83.388 -14.689  1.00105.24           H  
ATOM   7335 HD22 ASN A 522     -57.300 -82.916 -16.051  1.00105.24           H  
ATOM   7336  N   GLU A 523     -60.287 -87.026 -13.988  1.00 72.17           N  
ANISOU 7336  N   GLU A 523     6030  11610   9783   -130   -318   4219       N  
ATOM   7337  CA  GLU A 523     -60.470 -88.248 -14.766  1.00 77.93           C  
ANISOU 7337  CA  GLU A 523     6649  12369  10590   -514   -341   4213       C  
ATOM   7338  C   GLU A 523     -61.957 -88.551 -14.911  1.00 90.11           C  
ANISOU 7338  C   GLU A 523     7923  14315  11998   -558   -356   4292       C  
ATOM   7339  O   GLU A 523     -62.406 -89.027 -15.953  1.00 94.18           O  
ANISOU 7339  O   GLU A 523     8404  14896  12482   -754   -420   4247       O  
ATOM   7340  CB  GLU A 523     -59.767 -89.438 -14.109  1.00 73.45           C  
ANISOU 7340  CB  GLU A 523     6190  11562  10156   -750   -281   4169       C  
ATOM   7341  CG  GLU A 523     -59.867 -90.729 -14.917  1.00 77.32           C  
ANISOU 7341  CG  GLU A 523     6765  11947  10664  -1057   -348   4019       C  
ATOM   7342  CD  GLU A 523     -59.272 -91.917 -14.190  1.00 80.63           C  
ANISOU 7342  CD  GLU A 523     7351  12117  11168  -1191   -322   3887       C  
ATOM   7343  OE1 GLU A 523     -58.760 -91.731 -13.069  1.00 82.48           O  
ANISOU 7343  OE1 GLU A 523     7639  12253  11445  -1063   -257   3916       O  
ATOM   7344  OE2 GLU A 523     -59.316 -93.039 -14.738  1.00 73.98           O  
ANISOU 7344  OE2 GLU A 523     6583  11181  10342  -1411   -361   3750       O  
ATOM   7345  H   GLU A 523     -59.928 -87.144 -13.216  1.00 86.61           H  
ATOM   7346  HA  GLU A 523     -60.096 -88.124 -15.652  1.00 93.51           H  
ATOM   7347  HB2 GLU A 523     -58.826 -89.227 -14.003  1.00 88.14           H  
ATOM   7348  HB3 GLU A 523     -60.168 -89.599 -13.241  1.00 88.14           H  
ATOM   7349  HG2 GLU A 523     -60.802 -90.921 -15.092  1.00 92.78           H  
ATOM   7350  HG3 GLU A 523     -59.388 -90.617 -15.753  1.00 92.78           H  
ATOM   7351  N   LEU A 524     -62.712 -88.264 -13.856  1.00 78.38           N  
ANISOU 7351  N   LEU A 524     6326  13055  10402   -360   -292   4368       N  
ATOM   7352  CA  LEU A 524     -64.132 -88.597 -13.804  1.00 83.11           C  
ANISOU 7352  CA  LEU A 524     6736  14000  10843   -396   -286   4415       C  
ATOM   7353  C   LEU A 524     -65.024 -87.501 -14.384  1.00 88.43           C  
ANISOU 7353  C   LEU A 524     7311  14937  11352   -155   -320   4428       C  
ATOM   7354  O   LEU A 524     -66.238 -87.677 -14.474  1.00 94.44           O  
ANISOU 7354  O   LEU A 524     7903  16003  11975   -175   -319   4465       O  
ATOM   7355  CB  LEU A 524     -64.537 -88.898 -12.356  1.00 85.00           C  
ANISOU 7355  CB  LEU A 524     6912  14352  11031   -322   -195   4480       C  
ATOM   7356  CG  LEU A 524     -65.996 -89.208 -11.996  1.00 81.97           C  
ANISOU 7356  CG  LEU A 524     6328  14337  10479   -329   -175   4544       C  
ATOM   7357  CD1 LEU A 524     -66.495 -90.470 -12.693  1.00 82.86           C  
ANISOU 7357  CD1 LEU A 524     6396  14481  10607   -676   -238   4506       C  
ATOM   7358  CD2 LEU A 524     -66.123 -89.331 -10.487  1.00 82.26           C  
ANISOU 7358  CD2 LEU A 524     6340  14435  10479   -219    -83   4606       C  
ATOM   7359  H   LEU A 524     -62.422 -87.872 -13.148  1.00 94.06           H  
ATOM   7360  HA  LEU A 524     -64.281 -89.402 -14.325  1.00 99.74           H  
ATOM   7361  HB2 LEU A 524     -64.017 -89.664 -12.065  1.00102.00           H  
ATOM   7362  HB3 LEU A 524     -64.283 -88.131 -11.820  1.00102.00           H  
ATOM   7363  HG  LEU A 524     -66.554 -88.469 -12.283  1.00 98.36           H  
ATOM   7364 HD11 LEU A 524     -65.943 -91.220 -12.420  1.00 99.43           H  
ATOM   7365 HD12 LEU A 524     -67.417 -90.627 -12.437  1.00 99.43           H  
ATOM   7366 HD13 LEU A 524     -66.433 -90.346 -13.653  1.00 99.43           H  
ATOM   7367 HD21 LEU A 524     -65.854 -88.493 -10.078  1.00 98.71           H  
ATOM   7368 HD22 LEU A 524     -67.046 -89.527 -10.263  1.00 98.71           H  
ATOM   7369 HD23 LEU A 524     -65.548 -90.049 -10.179  1.00 98.71           H  
ATOM   7370  N   THR A 525     -64.430 -86.382 -14.799  1.00139.37           N  
ANISOU 7370  N   THR A 525    13905  21242  17806     75   -358   4374       N  
ATOM   7371  CA  THR A 525     -65.190 -85.308 -15.444  1.00140.10           C  
ANISOU 7371  CA  THR A 525    13982  21508  17741    307   -396   4339       C  
ATOM   7372  C   THR A 525     -66.079 -85.856 -16.552  1.00142.26           C  
ANISOU 7372  C   THR A 525    14080  22016  17955     92   -463   4361       C  
ATOM   7373  O   THR A 525     -67.110 -85.271 -16.882  1.00145.05           O  
ANISOU 7373  O   THR A 525    14332  22626  18153    241   -475   4364       O  
ATOM   7374  CB  THR A 525     -64.273 -84.245 -16.076  1.00140.58           C  
ANISOU 7374  CB  THR A 525    14299  21285  17831    485   -454   4239       C  
ATOM   7375  OG1 THR A 525     -63.365 -84.876 -16.986  1.00142.13           O  
ANISOU 7375  OG1 THR A 525    14561  21269  18175    221   -536   4230       O  
ATOM   7376  CG2 THR A 525     -63.491 -83.514 -15.020  1.00132.83           C  
ANISOU 7376  CG2 THR A 525    13540  20057  16871    726   -384   4171       C  
ATOM   7377  H   THR A 525     -63.589 -86.220 -14.719  1.00167.24           H  
ATOM   7378  HA  THR A 525     -65.754 -84.873 -14.786  1.00168.12           H  
ATOM   7379  HB  THR A 525     -64.814 -83.599 -16.558  1.00168.70           H  
ATOM   7380  HG1 THR A 525     -62.894 -85.439 -16.578  1.00170.56           H  
ATOM   7381 HG21 THR A 525     -62.940 -84.139 -14.524  1.00159.39           H  
ATOM   7382 HG22 THR A 525     -62.918 -82.848 -15.433  1.00159.39           H  
ATOM   7383 HG23 THR A 525     -64.097 -83.071 -14.406  1.00159.39           H  
ATOM   7384  N   LYS A 526     -65.669 -86.990 -17.112  1.00156.07           N  
ANISOU 7384  N   LYS A 526    15821  23652  19827   -261   -504   4355       N  
ATOM   7385  CA  LYS A 526     -66.431 -87.659 -18.149  1.00157.45           C  
ANISOU 7385  CA  LYS A 526    15879  23994  19952   -504   -565   4344       C  
ATOM   7386  C   LYS A 526     -66.392 -89.168 -17.943  1.00162.12           C  
ANISOU 7386  C   LYS A 526    16475  24498  20625   -853   -550   4321       C  
ATOM   7387  O   LYS A 526     -65.399 -89.716 -17.459  1.00160.89           O  
ANISOU 7387  O   LYS A 526    16470  24050  20612   -962   -521   4279       O  
ATOM   7388  CB  LYS A 526     -65.870 -87.303 -19.526  1.00128.18           C  
ANISOU 7388  CB  LYS A 526    12266  20148  16288   -561   -666   4280       C  
ATOM   7389  CG  LYS A 526     -66.046 -85.855 -19.902  1.00128.50           C  
ANISOU 7389  CG  LYS A 526    12354  20253  16218   -219   -703   4269       C  
ATOM   7390  CD  LYS A 526     -65.496 -85.611 -21.285  1.00127.62           C  
ANISOU 7390  CD  LYS A 526    12345  20003  16142   -304   -813   4212       C  
ATOM   7391  CE  LYS A 526     -65.743 -84.182 -21.716  1.00128.20           C  
ANISOU 7391  CE  LYS A 526    12514  20108  16086     32   -851   4178       C  
ATOM   7392  NZ  LYS A 526     -65.260 -83.916 -23.094  1.00127.52           N  
ANISOU 7392  NZ  LYS A 526    12537  19900  16013    -48   -962   4129       N  
ATOM   7393  H   LYS A 526     -64.941 -87.395 -16.901  1.00187.29           H  
ATOM   7394  HA  LYS A 526     -67.355 -87.368 -18.110  1.00188.94           H  
ATOM   7395  HB2 LYS A 526     -64.920 -87.499 -19.536  1.00153.81           H  
ATOM   7396  HB3 LYS A 526     -66.322 -87.840 -20.196  1.00153.81           H  
ATOM   7397  HG2 LYS A 526     -66.990 -85.631 -19.901  1.00154.20           H  
ATOM   7398  HG3 LYS A 526     -65.563 -85.295 -19.274  1.00154.20           H  
ATOM   7399  HD2 LYS A 526     -64.539 -85.770 -21.284  1.00153.14           H  
ATOM   7400  HD3 LYS A 526     -65.936 -86.202 -21.916  1.00153.14           H  
ATOM   7401  HE2 LYS A 526     -66.696 -84.003 -21.691  1.00153.83           H  
ATOM   7402  HE3 LYS A 526     -65.276 -83.583 -21.112  1.00153.83           H  
ATOM   7403  HZ1 LYS A 526     -65.678 -84.450 -23.671  1.00153.02           H  
ATOM   7404  HZ2 LYS A 526     -65.420 -83.069 -23.314  1.00153.02           H  
ATOM   7405  HZ3 LYS A 526     -64.384 -84.067 -23.143  1.00153.02           H  
ATOM   7406  N   VAL A 527     -67.494 -89.824 -18.287  1.00111.79           N  
ANISOU 7406  N   VAL A 527     9962  18361  14153  -1007   -573   4329       N  
ATOM   7407  CA  VAL A 527     -67.533 -91.275 -18.402  1.00110.48           C  
ANISOU 7407  CA  VAL A 527     9843  18084  14050  -1339   -589   4262       C  
ATOM   7408  C   VAL A 527     -68.299 -91.628 -19.669  1.00108.46           C  
ANISOU 7408  C   VAL A 527     9507  17984  13719  -1510   -667   4222       C  
ATOM   7409  O   VAL A 527     -69.259 -90.947 -20.030  1.00103.82           O  
ANISOU 7409  O   VAL A 527     8750  17708  12987  -1375   -686   4286       O  
ATOM   7410  CB  VAL A 527     -68.219 -91.945 -17.198  1.00112.06           C  
ANISOU 7410  CB  VAL A 527     9948  18425  14203  -1368   -526   4321       C  
ATOM   7411  CG1 VAL A 527     -68.231 -93.462 -17.371  1.00113.31           C  
ANISOU 7411  CG1 VAL A 527    10183  18438  14433  -1697   -552   4229       C  
ATOM   7412  CG2 VAL A 527     -67.517 -91.568 -15.907  1.00106.33           C  
ANISOU 7412  CG2 VAL A 527     9294  17567  13538  -1186   -446   4365       C  
ATOM   7413  H   VAL A 527     -68.246 -89.444 -18.462  1.00134.15           H  
ATOM   7414  HA  VAL A 527     -66.630 -91.622 -18.477  1.00132.58           H  
ATOM   7415  HB  VAL A 527     -69.138 -91.639 -17.143  1.00134.47           H  
ATOM   7416 HG11 VAL A 527     -67.317 -93.779 -17.436  1.00135.98           H  
ATOM   7417 HG12 VAL A 527     -68.667 -93.864 -16.603  1.00135.98           H  
ATOM   7418 HG13 VAL A 527     -68.717 -93.683 -18.181  1.00135.98           H  
ATOM   7419 HG21 VAL A 527     -67.551 -90.605 -15.798  1.00127.59           H  
ATOM   7420 HG22 VAL A 527     -67.967 -92.002 -15.165  1.00127.59           H  
ATOM   7421 HG23 VAL A 527     -66.594 -91.864 -15.952  1.00127.59           H  
ATOM   7422  N   LEU A 540     -71.441 -86.645 -17.293  1.00 99.16           N  
ANISOU 7422  N   LEU A 540     7818  17951  11906    -27   -467   4531       N  
ATOM   7423  CA  LEU A 540     -71.821 -86.934 -15.915  1.00 96.48           C  
ANISOU 7423  CA  LEU A 540     7406  17729  11521     29   -374   4594       C  
ATOM   7424  C   LEU A 540     -72.249 -85.645 -15.216  1.00 97.55           C  
ANISOU 7424  C   LEU A 540     7539  18001  11524    436   -309   4590       C  
ATOM   7425  O   LEU A 540     -71.633 -84.592 -15.398  1.00100.30           O  
ANISOU 7425  O   LEU A 540     8049  18165  11894    678   -318   4518       O  
ATOM   7426  CB  LEU A 540     -70.653 -87.602 -15.177  1.00 88.61           C  
ANISOU 7426  CB  LEU A 540     6554  16416  10698   -108   -340   4589       C  
ATOM   7427  CG  LEU A 540     -70.903 -88.731 -14.163  1.00 84.76           C  
ANISOU 7427  CG  LEU A 540     6004  15973  10228   -299   -291   4645       C  
ATOM   7428  CD1 LEU A 540     -72.158 -89.557 -14.441  1.00 86.68           C  
ANISOU 7428  CD1 LEU A 540     6062  16510  10365   -504   -321   4684       C  
ATOM   7429  CD2 LEU A 540     -69.690 -89.653 -14.138  1.00 78.14           C  
ANISOU 7429  CD2 LEU A 540     5338  14760   9592   -550   -309   4596       C  
ATOM   7430  HA  LEU A 540     -72.573 -87.546 -15.912  1.00115.77           H  
ATOM   7431  HB2 LEU A 540     -70.060 -87.969 -15.851  1.00106.33           H  
ATOM   7432  HB3 LEU A 540     -70.180 -86.905 -14.697  1.00106.33           H  
ATOM   7433  HG  LEU A 540     -70.996 -88.341 -13.279  1.00101.71           H  
ATOM   7434 HD11 LEU A 540     -72.077 -89.968 -15.316  1.00104.02           H  
ATOM   7435 HD12 LEU A 540     -72.242 -90.243 -13.760  1.00104.02           H  
ATOM   7436 HD13 LEU A 540     -72.932 -88.973 -14.420  1.00104.02           H  
ATOM   7437 HD21 LEU A 540     -68.910 -89.140 -13.877  1.00 93.77           H  
ATOM   7438 HD22 LEU A 540     -69.848 -90.365 -13.498  1.00 93.77           H  
ATOM   7439 HD23 LEU A 540     -69.560 -90.027 -15.024  1.00 93.77           H  
ATOM   7440  N   SER A 541     -73.314 -85.730 -14.425  1.00 87.91           N  
ANISOU 7440  N   SER A 541     6154  17087  10162    510   -248   4654       N  
ATOM   7441  CA  SER A 541     -73.878 -84.552 -13.772  1.00 81.23           C  
ANISOU 7441  CA  SER A 541     5297  16398   9168    890   -186   4638       C  
ATOM   7442  C   SER A 541     -73.107 -84.174 -12.507  1.00 86.50           C  
ANISOU 7442  C   SER A 541     6113  16867   9884   1073   -102   4618       C  
ATOM   7443  O   SER A 541     -72.574 -85.035 -11.805  1.00 90.62           O  
ANISOU 7443  O   SER A 541     6654  17275  10504    893    -68   4664       O  
ATOM   7444  CB  SER A 541     -75.361 -84.774 -13.457  1.00 82.22           C  
ANISOU 7444  CB  SER A 541     5179  16952   9108    899   -156   4714       C  
ATOM   7445  OG  SER A 541     -75.536 -85.823 -12.525  1.00 82.11           O  
ANISOU 7445  OG  SER A 541     5076  17018   9105    702   -110   4797       O  
ATOM   7446  H   SER A 541     -73.731 -86.462 -14.249  1.00105.50           H  
ATOM   7447  HA  SER A 541     -73.818 -83.802 -14.384  1.00 97.47           H  
ATOM   7448  HB2 SER A 541     -75.728 -83.957 -13.084  1.00 98.66           H  
ATOM   7449  HB3 SER A 541     -75.825 -85.001 -14.278  1.00 98.66           H  
ATOM   7450  HG  SER A 541     -75.223 -86.538 -12.835  1.00 98.54           H  
ATOM   7451  N   GLY A 542     -73.051 -82.872 -12.236  1.00 87.23           N  
ANISOU 7451  N   GLY A 542     6329  16905   9908   1429    -74   4536       N  
ATOM   7452  CA  GLY A 542     -72.276 -82.334 -11.131  1.00 82.32           C  
ANISOU 7452  CA  GLY A 542     5888  16064   9327   1630     -3   4484       C  
ATOM   7453  C   GLY A 542     -72.643 -82.923  -9.780  1.00 84.66           C  
ANISOU 7453  C   GLY A 542     6072  16526   9568   1603     91   4570       C  
ATOM   7454  O   GLY A 542     -71.762 -83.243  -8.985  1.00 79.77           O  
ANISOU 7454  O   GLY A 542     5564  15692   9054   1560    135   4574       O  
ATOM   7455  H   GLY A 542     -73.465 -82.271 -12.690  1.00104.67           H  
ATOM   7456  HA2 GLY A 542     -71.334 -82.506 -11.289  1.00 98.79           H  
ATOM   7457  HA3 GLY A 542     -72.406 -81.374 -11.088  1.00 98.79           H  
ATOM   7458  N   GLU A 543     -73.939 -83.078  -9.517  1.00118.69           N  
ANISOU 7458  N   GLU A 543    10165  21222  13712   1625    118   4642       N  
ATOM   7459  CA  GLU A 543     -74.387 -83.663  -8.253  1.00116.76           C  
ANISOU 7459  CA  GLU A 543     9802  21165  13395   1591    198   4733       C  
ATOM   7460  C   GLU A 543     -73.966 -85.123  -8.163  1.00123.17           C  
ANISOU 7460  C   GLU A 543    10566  21891  14340   1209    178   4820       C  
ATOM   7461  O   GLU A 543     -73.445 -85.583  -7.133  1.00129.46           O  
ANISOU 7461  O   GLU A 543    11415  22579  15195   1163    231   4856       O  
ATOM   7462  CB  GLU A 543     -75.910 -83.546  -8.101  1.00124.25           C  
ANISOU 7462  CB  GLU A 543    10520  22560  14129   1678    218   4793       C  
ATOM   7463  CG  GLU A 543     -76.387 -82.114  -7.905  1.00125.60           C  
ANISOU 7463  CG  GLU A 543    10743  22826  14153   2081    252   4708       C  
ATOM   7464  CD  GLU A 543     -77.892 -81.997  -7.742  1.00129.15           C  
ANISOU 7464  CD  GLU A 543    10958  23729  14385   2175    274   4770       C  
ATOM   7465  OE1 GLU A 543     -78.601 -83.003  -7.952  1.00130.61           O  
ANISOU 7465  OE1 GLU A 543    10936  24159  14532   1914    251   4875       O  
ATOM   7466  OE2 GLU A 543     -78.368 -80.894  -7.405  1.00130.59           O  
ANISOU 7466  OE2 GLU A 543    11171  24017  14431   2508    309   4708       O  
ATOM   7467  H   GLU A 543     -74.576 -82.854 -10.049  1.00142.43           H  
ATOM   7468  HA  GLU A 543     -73.973 -83.184  -7.517  1.00140.11           H  
ATOM   7469  HB2 GLU A 543     -76.333 -83.895  -8.901  1.00149.10           H  
ATOM   7470  HB3 GLU A 543     -76.189 -84.062  -7.328  1.00149.10           H  
ATOM   7471  HG2 GLU A 543     -75.972 -81.751  -7.107  1.00150.72           H  
ATOM   7472  HG3 GLU A 543     -76.130 -81.589  -8.679  1.00150.72           H  
ATOM   7473  N   GLN A 544     -74.189 -85.852  -9.251  1.00117.21           N  
ANISOU 7473  N   GLN A 544     9728  21172  13635    935     94   4841       N  
ATOM   7474  CA  GLN A 544     -73.835 -87.262  -9.287  1.00120.19           C  
ANISOU 7474  CA  GLN A 544    10088  21438  14143    557     57   4893       C  
ATOM   7475  C   GLN A 544     -72.340 -87.455  -9.073  1.00123.43           C  
ANISOU 7475  C   GLN A 544    10713  21433  14754    495     61   4850       C  
ATOM   7476  O   GLN A 544     -71.947 -88.371  -8.374  1.00127.98           O  
ANISOU 7476  O   GLN A 544    11313  21897  15416    313     79   4889       O  
ATOM   7477  CB  GLN A 544     -74.260 -87.917 -10.599  1.00109.89           C  
ANISOU 7477  CB  GLN A 544     8696  20198  12858    284    -40   4887       C  
ATOM   7478  CG  GLN A 544     -75.754 -88.169 -10.723  1.00113.22           C  
ANISOU 7478  CG  GLN A 544     8883  21034  13101    237    -50   4950       C  
ATOM   7479  CD  GLN A 544     -76.142 -88.654 -12.105  1.00113.93           C  
ANISOU 7479  CD  GLN A 544     8907  21177  13204      1   -147   4927       C  
ATOM   7480  OE1 GLN A 544     -75.320 -88.662 -13.021  1.00111.97           O  
ANISOU 7480  OE1 GLN A 544     8789  20668  13085    -94   -205   4860       O  
ATOM   7481  NE2 GLN A 544     -77.392 -89.070 -12.262  1.00116.81           N  
ANISOU 7481  NE2 GLN A 544     9071  21882  13431   -100   -164   4982       N  
ATOM   7482  H   GLN A 544     -74.542 -85.555  -9.977  1.00140.65           H  
ATOM   7483  HA  GLN A 544     -74.297 -87.718  -8.566  1.00144.23           H  
ATOM   7484  HB2 GLN A 544     -73.997 -87.340 -11.333  1.00131.86           H  
ATOM   7485  HB3 GLN A 544     -73.810 -88.773 -10.679  1.00131.86           H  
ATOM   7486  HG2 GLN A 544     -76.016 -88.848 -10.081  1.00135.86           H  
ATOM   7487  HG3 GLN A 544     -76.231 -87.343 -10.548  1.00135.86           H  
ATOM   7488 HE21 GLN A 544     -77.936 -89.055 -11.596  1.00140.18           H  
ATOM   7489 HE22 GLN A 544     -77.658 -89.354 -13.029  1.00140.18           H  
ATOM   7490  N   LYS A 545     -71.513 -86.598  -9.669  1.00103.84           N  
ANISOU 7490  N   LYS A 545     8392  18716  12345    645     41   4764       N  
ATOM   7491  CA  LYS A 545     -70.065 -86.676  -9.464  1.00101.46           C  
ANISOU 7491  CA  LYS A 545     8298  18023  12229    611     47   4721       C  
ATOM   7492  C   LYS A 545     -69.737 -86.725  -7.971  1.00107.42           C  
ANISOU 7492  C   LYS A 545     9100  18730  12985    719    141   4756       C  
ATOM   7493  O   LYS A 545     -69.120 -87.685  -7.489  1.00107.69           O  
ANISOU 7493  O   LYS A 545     9176  18599  13142    508    147   4792       O  
ATOM   7494  CB  LYS A 545     -69.353 -85.487 -10.117  1.00 86.62           C  
ANISOU 7494  CB  LYS A 545     6597  15928  10387    837     19   4614       C  
ATOM   7495  CG  LYS A 545     -69.336 -85.523 -11.635  1.00 86.39           C  
ANISOU 7495  CG  LYS A 545     6563  15862  10399    698    -85   4578       C  
ATOM   7496  CD  LYS A 545     -68.654 -84.289 -12.209  1.00 85.03           C  
ANISOU 7496  CD  LYS A 545     6595  15464  10249    941   -121   4464       C  
ATOM   7497  CE  LYS A 545     -68.707 -84.292 -13.730  1.00 85.01           C  
ANISOU 7497  CE  LYS A 545     6580  15452  10268    812   -228   4436       C  
ATOM   7498  NZ  LYS A 545     -68.079 -83.093 -14.354  1.00 83.87           N  
ANISOU 7498  NZ  LYS A 545     6655  15078  10134   1037   -279   4323       N  
ATOM   7499  H   LYS A 545     -71.762 -85.964 -10.194  1.00124.60           H  
ATOM   7500  HA  LYS A 545     -69.731 -87.489  -9.873  1.00121.75           H  
ATOM   7501  HB2 LYS A 545     -69.801 -84.670  -9.846  1.00103.95           H  
ATOM   7502  HB3 LYS A 545     -68.432 -85.472  -9.812  1.00103.95           H  
ATOM   7503  HG2 LYS A 545     -68.848 -86.307 -11.932  1.00103.67           H  
ATOM   7504  HG3 LYS A 545     -70.248 -85.549 -11.965  1.00103.67           H  
ATOM   7505  HD2 LYS A 545     -69.107 -83.493 -11.889  1.00102.04           H  
ATOM   7506  HD3 LYS A 545     -67.723 -84.280 -11.936  1.00102.04           H  
ATOM   7507  HE2 LYS A 545     -68.239 -85.076 -14.058  1.00102.01           H  
ATOM   7508  HE3 LYS A 545     -69.635 -84.321 -14.011  1.00102.01           H  
ATOM   7509  HZ1 LYS A 545     -67.221 -83.045 -14.123  1.00100.65           H  
ATOM   7510  HZ2 LYS A 545     -68.138 -83.146 -15.240  1.00100.65           H  
ATOM   7511  HZ3 LYS A 545     -68.495 -82.355 -14.080  1.00100.65           H  
ATOM   7512  N   LYS A 546     -70.175 -85.698  -7.246  1.00145.00           N  
ANISOU 7512  N   LYS A 546    13865  23628  17602   1047    210   4732       N  
ATOM   7513  CA  LYS A 546     -69.997 -85.639  -5.799  1.00139.64           C  
ANISOU 7513  CA  LYS A 546    13223  22945  16890   1178    304   4759       C  
ATOM   7514  C   LYS A 546     -70.536 -86.908  -5.149  1.00139.76           C  
ANISOU 7514  C   LYS A 546    13078  23137  16888    930    315   4880       C  
ATOM   7515  O   LYS A 546     -69.878 -87.483  -4.275  1.00142.04           O  
ANISOU 7515  O   LYS A 546    13433  23269  17266    849    350   4914       O  
ATOM   7516  CB  LYS A 546     -70.687 -84.401  -5.213  1.00128.23           C  
ANISOU 7516  CB  LYS A 546    11779  21685  15257   1549    366   4704       C  
ATOM   7517  CG  LYS A 546     -70.050 -83.075  -5.611  1.00126.95           C  
ANISOU 7517  CG  LYS A 546    11843  21277  15116   1819    350   4548       C  
ATOM   7518  CD  LYS A 546     -70.814 -81.903  -5.030  1.00128.89           C  
ANISOU 7518  CD  LYS A 546    12100  21699  15174   2168    398   4481       C  
ATOM   7519  CE  LYS A 546     -70.156 -80.605  -5.437  1.00127.70           C  
ANISOU 7519  CE  LYS A 546    12211  21258  15052   2412    361   4309       C  
ATOM   7520  NZ  LYS A 546     -70.868 -79.420  -4.908  1.00129.66           N  
ANISOU 7520  NZ  LYS A 546    12496  21644  15124   2751    395   4229       N  
ATOM   7521  H   LYS A 546     -70.583 -85.015  -7.573  1.00174.00           H  
ATOM   7522  HA  LYS A 546     -69.049 -85.578  -5.599  1.00167.57           H  
ATOM   7523  HB2 LYS A 546     -71.608 -84.387  -5.514  1.00153.88           H  
ATOM   7524  HB3 LYS A 546     -70.661 -84.460  -4.245  1.00153.88           H  
ATOM   7525  HG2 LYS A 546     -69.141 -83.042  -5.276  1.00152.34           H  
ATOM   7526  HG3 LYS A 546     -70.057 -82.994  -6.578  1.00152.34           H  
ATOM   7527  HD2 LYS A 546     -71.723 -81.908  -5.368  1.00154.67           H  
ATOM   7528  HD3 LYS A 546     -70.810 -81.961  -4.062  1.00154.67           H  
ATOM   7529  HE2 LYS A 546     -69.248 -80.589  -5.095  1.00153.24           H  
ATOM   7530  HE3 LYS A 546     -70.147 -80.544  -6.405  1.00153.24           H  
ATOM   7531  HZ1 LYS A 546     -70.885 -79.447  -4.019  1.00155.59           H  
ATOM   7532  HZ2 LYS A 546     -70.454 -78.676  -5.167  1.00155.59           H  
ATOM   7533  HZ3 LYS A 546     -71.704 -79.406  -5.213  1.00155.59           H  
ATOM   7534  N   ALA A 547     -71.718 -87.352  -5.579  1.00 82.43           N  
ANISOU 7534  N   ALA A 547     5618  16184   9517    805    277   4935       N  
ATOM   7535  CA  ALA A 547     -72.239 -88.638  -5.110  1.00 88.54           C  
ANISOU 7535  CA  ALA A 547     6262  17090  10288    530    263   5024       C  
ATOM   7536  C   ALA A 547     -71.225 -89.764  -5.351  1.00 87.46           C  
ANISOU 7536  C   ALA A 547     6247  16614  10372    212    210   5004       C  
ATOM   7537  O   ALA A 547     -70.909 -90.530  -4.437  1.00 87.26           O  
ANISOU 7537  O   ALA A 547     6252  16495  10408     98    234   5037       O  
ATOM   7538  CB  ALA A 547     -73.593 -88.962  -5.770  1.00 90.55           C  
ANISOU 7538  CB  ALA A 547     6305  17690  10409    412    214   5065       C  
ATOM   7539  H   ALA A 547     -72.229 -86.937  -6.132  1.00 98.91           H  
ATOM   7540  HA  ALA A 547     -72.388 -88.579  -4.154  1.00106.24           H  
ATOM   7541  HB1 ALA A 547     -73.473 -89.004  -6.732  1.00108.66           H  
ATOM   7542  HB2 ALA A 547     -73.908 -89.817  -5.438  1.00108.66           H  
ATOM   7543  HB3 ALA A 547     -74.228 -88.265  -5.545  1.00108.66           H  
ATOM   7544  N   ILE A 548     -70.674 -89.820  -6.563  1.00101.27           N  
ANISOU 7544  N   ILE A 548     8080  18161  12236     86    140   4935       N  
ATOM   7545  CA  ILE A 548     -69.821 -90.929  -6.982  1.00107.33           C  
ANISOU 7545  CA  ILE A 548     8968  18611  13199   -231     80   4886       C  
ATOM   7546  C   ILE A 548     -68.549 -90.947  -6.145  1.00107.59           C  
ANISOU 7546  C   ILE A 548     9182  18324  13372   -177    127   4866       C  
ATOM   7547  O   ILE A 548     -68.100 -92.014  -5.723  1.00101.66           O  
ANISOU 7547  O   ILE A 548     8504  17386  12735   -393    116   4846       O  
ATOM   7548  CB  ILE A 548     -69.468 -90.868  -8.497  1.00 77.11           C  
ANISOU 7548  CB  ILE A 548     5205  14640   9454   -352     -3   4807       C  
ATOM   7549  CG1 ILE A 548     -70.723 -91.123  -9.342  1.00 80.21           C  
ANISOU 7549  CG1 ILE A 548     5420  15332   9723   -471    -59   4823       C  
ATOM   7550  CG2 ILE A 548     -68.395 -91.900  -8.846  1.00 78.36           C  
ANISOU 7550  CG2 ILE A 548     5541  14415   9818   -636    -51   4722       C  
ATOM   7551  CD1 ILE A 548     -70.494 -91.209 -10.848  1.00 82.03           C  
ANISOU 7551  CD1 ILE A 548     5700  15447  10020   -624   -147   4747       C  
ATOM   7552  H   ILE A 548     -70.782 -89.219  -7.169  1.00121.52           H  
ATOM   7553  HA  ILE A 548     -70.292 -91.761  -6.821  1.00128.79           H  
ATOM   7554  HB  ILE A 548     -69.128 -89.983  -8.703  1.00 92.54           H  
ATOM   7555 HG12 ILE A 548     -71.118 -91.963  -9.059  1.00 96.25           H  
ATOM   7556 HG13 ILE A 548     -71.351 -90.401  -9.184  1.00 96.25           H  
ATOM   7557 HG21 ILE A 548     -68.729 -92.786  -8.634  1.00 94.03           H  
ATOM   7558 HG22 ILE A 548     -68.196 -91.840  -9.794  1.00 94.03           H  
ATOM   7559 HG23 ILE A 548     -67.597 -91.714  -8.328  1.00 94.03           H  
ATOM   7560 HD11 ILE A 548     -69.881 -91.938 -11.033  1.00 98.43           H  
ATOM   7561 HD12 ILE A 548     -71.343 -91.371 -11.287  1.00 98.43           H  
ATOM   7562 HD13 ILE A 548     -70.115 -90.372 -11.158  1.00 98.43           H  
ATOM   7563  N   VAL A 549     -67.968 -89.775  -5.900  1.00121.30           N  
ANISOU 7563  N   VAL A 549    11005  19984  15098    117    179   4854       N  
ATOM   7564  CA  VAL A 549     -66.807 -89.717  -5.019  1.00107.84           C  
ANISOU 7564  CA  VAL A 549     9463  18002  13510    192    232   4843       C  
ATOM   7565  C   VAL A 549     -67.230 -90.179  -3.634  1.00115.60           C  
ANISOU 7565  C   VAL A 549    10376  19125  14422    211    293   4916       C  
ATOM   7566  O   VAL A 549     -66.658 -91.119  -3.090  1.00116.96           O  
ANISOU 7566  O   VAL A 549    10622  19103  14713     33    288   4909       O  
ATOM   7567  CB  VAL A 549     -66.199 -88.309  -4.881  1.00 92.37           C  
ANISOU 7567  CB  VAL A 549     7624  15944  11530    530    287   4797       C  
ATOM   7568  CG1 VAL A 549     -64.836 -88.403  -4.202  1.00 89.77           C  
ANISOU 7568  CG1 VAL A 549     7478  15273  11356    544    326   4776       C  
ATOM   7569  CG2 VAL A 549     -66.054 -87.633  -6.222  1.00 79.80           C  
ANISOU 7569  CG2 VAL A 549     6078  14284   9958    571    222   4722       C  
ATOM   7570  H   VAL A 549     -68.219 -89.018  -6.222  1.00145.55           H  
ATOM   7571  HA  VAL A 549     -66.121 -90.318  -5.348  1.00129.41           H  
ATOM   7572  HB  VAL A 549     -66.778 -87.763  -4.326  1.00110.85           H  
ATOM   7573 HG11 VAL A 549     -64.252 -88.958  -4.741  1.00107.72           H  
ATOM   7574 HG12 VAL A 549     -64.462 -87.511  -4.120  1.00107.72           H  
ATOM   7575 HG13 VAL A 549     -64.948 -88.797  -3.322  1.00107.72           H  
ATOM   7576 HG21 VAL A 549     -66.929 -87.554  -6.632  1.00 95.76           H  
ATOM   7577 HG22 VAL A 549     -65.669 -86.753  -6.091  1.00 95.76           H  
ATOM   7578 HG23 VAL A 549     -65.472 -88.169  -6.783  1.00 95.76           H  
ATOM   7579  N   ASP A 550     -68.245 -89.521  -3.076  1.00129.96           N  
ANISOU 7579  N   ASP A 550    12061  21277  16042    430    349   4969       N  
ATOM   7580  CA  ASP A 550     -68.738 -89.854  -1.741  1.00124.46           C  
ANISOU 7580  CA  ASP A 550    11282  20755  15250    473    408   5045       C  
ATOM   7581  C   ASP A 550     -69.077 -91.330  -1.621  1.00130.84           C  
ANISOU 7581  C   ASP A 550    12018  21576  16120    132    355   5077       C  
ATOM   7582  O   ASP A 550     -68.984 -91.909  -0.535  1.00139.54           O  
ANISOU 7582  O   ASP A 550    13121  22663  17234     88    389   5117       O  
ATOM   7583  CB  ASP A 550     -69.971 -89.012  -1.393  1.00113.85           C  
ANISOU 7583  CB  ASP A 550     9786  19804  13667    722    459   5083       C  
ATOM   7584  CG  ASP A 550     -69.618 -87.575  -1.068  1.00113.10           C  
ANISOU 7584  CG  ASP A 550     9810  19662  13500   1094    535   5012       C  
ATOM   7585  OD1 ASP A 550     -68.434 -87.305  -0.782  1.00110.73           O  
ANISOU 7585  OD1 ASP A 550     9700  19050  13323   1162    563   4958       O  
ATOM   7586  OD2 ASP A 550     -70.519 -86.713  -1.088  1.00114.95           O  
ANISOU 7586  OD2 ASP A 550     9965  20155  13557   1319    562   4990       O  
ATOM   7587  H   ASP A 550     -68.667 -88.873  -3.453  1.00155.95           H  
ATOM   7588  HA  ASP A 550     -68.046 -89.653  -1.091  1.00149.35           H  
ATOM   7589  HB2 ASP A 550     -70.577 -89.009  -2.150  1.00136.62           H  
ATOM   7590  HB3 ASP A 550     -70.409 -89.396  -0.617  1.00136.62           H  
ATOM   7591  N   LEU A 551     -69.437 -91.942  -2.742  1.00 91.45           N  
ANISOU 7591  N   LEU A 551     6982  16593  11170   -109    274   5043       N  
ATOM   7592  CA  LEU A 551     -69.924 -93.314  -2.730  1.00 85.36           C  
ANISOU 7592  CA  LEU A 551     6150  15850  10434   -431    227   5049       C  
ATOM   7593  C   LEU A 551     -68.848 -94.384  -2.951  1.00 83.46           C  
ANISOU 7593  C   LEU A 551     6102  15201  10410   -697    184   4952       C  
ATOM   7594  O   LEU A 551     -68.730 -95.308  -2.152  1.00 88.09           O  
ANISOU 7594  O   LEU A 551     6719  15703  11045   -838    197   4956       O  
ATOM   7595  CB  LEU A 551     -71.048 -93.440  -3.749  1.00 88.19           C  
ANISOU 7595  CB  LEU A 551     6350  16468  10689   -545    170   5058       C  
ATOM   7596  CG  LEU A 551     -72.322 -92.820  -3.178  1.00 88.48           C  
ANISOU 7596  CG  LEU A 551     6176  16946  10497   -344    218   5157       C  
ATOM   7597  CD1 LEU A 551     -73.296 -92.405  -4.262  1.00 86.20           C  
ANISOU 7597  CD1 LEU A 551     5747  16920  10086   -329    175   5157       C  
ATOM   7598  CD2 LEU A 551     -72.960 -93.798  -2.263  1.00 83.59           C  
ANISOU 7598  CD2 LEU A 551     5453  16475   9831   -505    230   5224       C  
ATOM   7599  H   LEU A 551     -69.409 -91.584  -3.524  1.00109.74           H  
ATOM   7600  HA  LEU A 551     -70.313 -93.484  -1.858  1.00102.44           H  
ATOM   7601  HB2 LEU A 551     -70.808 -92.965  -4.561  1.00105.82           H  
ATOM   7602  HB3 LEU A 551     -71.215 -94.376  -3.937  1.00105.82           H  
ATOM   7603  HG  LEU A 551     -72.089 -92.032  -2.662  1.00106.18           H  
ATOM   7604 HD11 LEU A 551     -73.544 -93.187  -4.779  1.00103.44           H  
ATOM   7605 HD12 LEU A 551     -74.084 -92.019  -3.847  1.00103.44           H  
ATOM   7606 HD13 LEU A 551     -72.869 -91.749  -4.836  1.00103.44           H  
ATOM   7607 HD21 LEU A 551     -72.342 -94.009  -1.546  1.00100.30           H  
ATOM   7608 HD22 LEU A 551     -73.769 -93.407  -1.898  1.00100.30           H  
ATOM   7609 HD23 LEU A 551     -73.176 -94.602  -2.761  1.00100.30           H  
ATOM   7610  N   LEU A 552     -68.063 -94.258  -4.018  1.00115.17           N  
ANISOU 7610  N   LEU A 552    10253  18961  14546   -756    136   4857       N  
ATOM   7611  CA  LEU A 552     -67.175 -95.332  -4.447  1.00117.70           C  
ANISOU 7611  CA  LEU A 552    10759  18911  15049  -1022     88   4735       C  
ATOM   7612  C   LEU A 552     -65.723 -95.034  -4.083  1.00113.67           C  
ANISOU 7612  C   LEU A 552    10458  18047  14684   -920    116   4671       C  
ATOM   7613  O   LEU A 552     -65.076 -95.803  -3.367  1.00109.53           O  
ANISOU 7613  O   LEU A 552    10056  17302  14257  -1014    133   4623       O  
ATOM   7614  CB  LEU A 552     -67.323 -95.534  -5.953  1.00112.96           C  
ANISOU 7614  CB  LEU A 552    10174  18269  14478  -1188      9   4656       C  
ATOM   7615  CG  LEU A 552     -68.735 -95.934  -6.385  1.00110.76           C  
ANISOU 7615  CG  LEU A 552     9696  18324  14064  -1318    -25   4709       C  
ATOM   7616  CD1 LEU A 552     -68.834 -95.998  -7.899  1.00109.79           C  
ANISOU 7616  CD1 LEU A 552     9590  18161  13963  -1452   -101   4631       C  
ATOM   7617  CD2 LEU A 552     -69.155 -97.266  -5.781  1.00109.54           C  
ANISOU 7617  CD2 LEU A 552     9524  18174  13924  -1555    -25   4711       C  
ATOM   7618  H   LEU A 552     -68.027 -93.556  -4.513  1.00138.20           H  
ATOM   7619  HA  LEU A 552     -67.434 -96.156  -4.004  1.00141.23           H  
ATOM   7620  HB2 LEU A 552     -67.098 -94.705  -6.404  1.00135.55           H  
ATOM   7621  HB3 LEU A 552     -66.716 -96.236  -6.236  1.00135.55           H  
ATOM   7622  HG  LEU A 552     -69.359 -95.259  -6.076  1.00132.91           H  
ATOM   7623 HD11 LEU A 552     -68.202 -96.656  -8.228  1.00131.74           H  
ATOM   7624 HD12 LEU A 552     -69.736 -96.253  -8.146  1.00131.74           H  
ATOM   7625 HD13 LEU A 552     -68.624 -95.124  -8.265  1.00131.74           H  
ATOM   7626 HD21 LEU A 552     -69.136 -97.194  -4.814  1.00131.45           H  
ATOM   7627 HD22 LEU A 552     -70.052 -97.480  -6.080  1.00131.45           H  
ATOM   7628 HD23 LEU A 552     -68.536 -97.954  -6.074  1.00131.45           H  
ATOM   7629  N   PHE A 553     -65.222 -93.904  -4.570  1.00 95.28           N  
ANISOU 7629  N   PHE A 553     8170  15669  12363   -722    122   4670       N  
ATOM   7630  CA  PHE A 553     -63.851 -93.491  -4.301  1.00 92.93           C  
ANISOU 7630  CA  PHE A 553     8063  15049  12197   -612    149   4615       C  
ATOM   7631  C   PHE A 553     -63.602 -93.278  -2.815  1.00 95.14           C  
ANISOU 7631  C   PHE A 553     8348  15344  12456   -438    230   4683       C  
ATOM   7632  O   PHE A 553     -62.459 -93.296  -2.375  1.00 98.03           O  
ANISOU 7632  O   PHE A 553     8882  15420  12945   -403    251   4624       O  
ATOM   7633  CB  PHE A 553     -63.526 -92.193  -5.038  1.00 85.36           C  
ANISOU 7633  CB  PHE A 553     7117  14091  11226   -405    150   4628       C  
ATOM   7634  CG  PHE A 553     -63.442 -92.339  -6.528  1.00 82.95           C  
ANISOU 7634  CG  PHE A 553     6851  13695  10973   -569     68   4545       C  
ATOM   7635  CD1 PHE A 553     -62.348 -92.955  -7.115  1.00 77.82           C  
ANISOU 7635  CD1 PHE A 553     6408  12673  10487   -750     22   4405       C  
ATOM   7636  CD2 PHE A 553     -64.445 -91.843  -7.345  1.00 78.75           C  
ANISOU 7636  CD2 PHE A 553     6160  13448  10314   -529     37   4591       C  
ATOM   7637  CE1 PHE A 553     -62.261 -93.080  -8.490  1.00 72.05           C  
ANISOU 7637  CE1 PHE A 553     5722  11862   9792   -894    -52   4320       C  
ATOM   7638  CE2 PHE A 553     -64.362 -91.970  -8.718  1.00 79.53           C  
ANISOU 7638  CE2 PHE A 553     6293  13469  10456   -680    -41   4516       C  
ATOM   7639  CZ  PHE A 553     -63.271 -92.590  -9.290  1.00 76.16           C  
ANISOU 7639  CZ  PHE A 553     6072  12674  10192   -865    -85   4385       C  
ATOM   7640  H   PHE A 553     -65.662 -93.354  -5.064  1.00114.34           H  
ATOM   7641  HA  PHE A 553     -63.243 -94.178  -4.615  1.00111.51           H  
ATOM   7642  HB2 PHE A 553     -64.220 -91.542  -4.844  1.00102.43           H  
ATOM   7643  HB3 PHE A 553     -62.670 -91.862  -4.724  1.00102.43           H  
ATOM   7644  HD1 PHE A 553     -61.665 -93.288  -6.579  1.00 93.39           H  
ATOM   7645  HD2 PHE A 553     -65.184 -91.425  -6.965  1.00 94.50           H  
ATOM   7646  HE1 PHE A 553     -61.525 -93.500  -8.874  1.00 86.46           H  
ATOM   7647  HE2 PHE A 553     -65.043 -91.637  -9.257  1.00 95.43           H  
ATOM   7648  HZ  PHE A 553     -63.216 -92.674 -10.215  1.00 91.39           H  
ATOM   7649  N   LYS A 554     -64.667 -93.055  -2.052  1.00 96.34           N  
ANISOU 7649  N   LYS A 554     8321  15840  12444   -322    274   4797       N  
ATOM   7650  CA  LYS A 554     -64.544 -92.798  -0.620  1.00 93.05           C  
ANISOU 7650  CA  LYS A 554     7898  15479  11979   -139    354   4866       C  
ATOM   7651  C   LYS A 554     -64.681 -94.081   0.189  1.00 97.73           C  
ANISOU 7651  C   LYS A 554     8488  16034  12609   -351    350   4862       C  
ATOM   7652  O   LYS A 554     -63.907 -94.326   1.115  1.00 96.00           O  
ANISOU 7652  O   LYS A 554     8379  15631  12467   -321    387   4844       O  
ATOM   7653  CB  LYS A 554     -65.594 -91.779  -0.172  1.00 84.09           C  
ANISOU 7653  CB  LYS A 554     6592  14733  10624    134    415   4973       C  
ATOM   7654  CG  LYS A 554     -65.255 -90.346  -0.554  1.00 83.03           C  
ANISOU 7654  CG  LYS A 554     6518  14588  10442    426    456   4957       C  
ATOM   7655  CD  LYS A 554     -65.029 -89.494   0.676  1.00 75.35           C  
ANISOU 7655  CD  LYS A 554     5597  13656   9377    728    561   4986       C  
ATOM   7656  CE  LYS A 554     -64.520 -88.112   0.322  1.00 75.00           C  
ANISOU 7656  CE  LYS A 554     5685  13503   9308   1001    609   4895       C  
ATOM   7657  NZ  LYS A 554     -65.625 -87.168   0.006  1.00 72.11           N  
ANISOU 7657  NZ  LYS A 554     5223  13427   8747   1206    623   4859       N  
ATOM   7658  H   LYS A 554     -65.477 -93.048  -2.340  1.00115.61           H  
ATOM   7659  HA  LYS A 554     -63.668 -92.423  -0.441  1.00111.67           H  
ATOM   7660  HB2 LYS A 554     -66.443 -92.003  -0.583  1.00100.90           H  
ATOM   7661  HB3 LYS A 554     -65.675 -91.817   0.794  1.00100.90           H  
ATOM   7662  HG2 LYS A 554     -64.443 -90.338  -1.084  1.00 99.64           H  
ATOM   7663  HG3 LYS A 554     -65.991 -89.965  -1.058  1.00 99.64           H  
ATOM   7664  HD2 LYS A 554     -65.867 -89.395   1.154  1.00 90.42           H  
ATOM   7665  HD3 LYS A 554     -64.369 -89.923   1.244  1.00 90.42           H  
ATOM   7666  HE2 LYS A 554     -64.024 -87.754   1.074  1.00 90.00           H  
ATOM   7667  HE3 LYS A 554     -63.946 -88.175  -0.458  1.00 90.00           H  
ATOM   7668  HZ1 LYS A 554     -66.166 -87.087   0.709  1.00 86.53           H  
ATOM   7669  HZ2 LYS A 554     -65.293 -86.368  -0.197  1.00 86.53           H  
ATOM   7670  HZ3 LYS A 554     -66.095 -87.471  -0.686  1.00 86.53           H  
ATOM   7671  N   THR A 555     -65.661 -94.903  -0.168  1.00102.49           N  
ANISOU 7671  N   THR A 555     8974  16812  13157   -565    308   4875       N  
ATOM   7672  CA  THR A 555     -65.916 -96.142   0.555  1.00104.93           C  
ANISOU 7672  CA  THR A 555     9274  17109  13486   -774    307   4878       C  
ATOM   7673  C   THR A 555     -64.910 -97.216   0.157  1.00103.81           C  
ANISOU 7673  C   THR A 555     9348  16564  13532  -1017    264   4732       C  
ATOM   7674  O   THR A 555     -64.531 -98.057   0.974  1.00104.31           O  
ANISOU 7674  O   THR A 555     9494  16483  13656  -1116    284   4707       O  
ATOM   7675  CB  THR A 555     -67.333 -96.659   0.278  1.00 96.24           C  
ANISOU 7675  CB  THR A 555     7974  16335  12256   -925    278   4942       C  
ATOM   7676  OG1 THR A 555     -67.522 -96.805  -1.135  1.00 96.75           O  
ANISOU 7676  OG1 THR A 555     8045  16363  12351  -1071    209   4873       O  
ATOM   7677  CG2 THR A 555     -68.369 -95.691   0.834  1.00 89.84           C  
ANISOU 7677  CG2 THR A 555