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

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


***  7jme_holo  ***

elNémo ID: 220606104349144714

Job options:

ID        	=	 220606104349144714
JOBID     	=	 7jme_holo
USERID    	=	 unknown
PRIVAT    	=	 0

NMODES    	=	 10
DQMIN     	=	 -100
DQMAX     	=	 100
DQSTEP    	=	 20
DOGRAPHS  	=	 on

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER 7jme_holo

HEADER    VIRAL PROTEIN/INHIBITOR                 31-JUL-20   7JME              
TITLE     STRUCTURE OF THE SARS-COV-2 NSP3 MACRO X DOMAIN IN COMPLEX WITH CYCLIC
TITLE    2 AMP                                                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NON-STRUCTURAL PROTEIN 3;                                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: NSP3,PL2-PRO,PAPAIN-LIKE PROTEASE,PAPAIN-LIKE PROTEINASE,PL-
COMPND   5 PRO;                                                                 
COMPND   6 EC: 3.4.19.121, 3.4.22.-;                                            
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS   
SOURCE   3 2;                                                                   
SOURCE   4 ORGANISM_COMMON: 2019-NCOV, SARS-COV-2, COVID-19 VIRUS;              
SOURCE   5 ORGANISM_TAXID: 2697049;                                             
SOURCE   6 GENE: REP, 1A-1B;                                                    
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;                            
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   9 EXPRESSION_SYSTEM_VARIANT: STAR                                      
KEYWDS    MACRO DOMAIN, CAMP, CYCLIC AMP, VIRAL PROTEIN, SARS-COV-2, VIRAL      
KEYWDS   2 PROTEIN-INHIBITOR COMPLEX                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.VUKSANOVIC,T.R.MELKONIAN,N.R.SILVAGGI                               
REVDAT   3   15-SEP-21 7JME    1       JRNL                                     
REVDAT   2   27-JAN-21 7JME    1       COMPND                                   
REVDAT   1   02-SEP-20 7JME    0                                                
JRNL        AUTH   R.S.VIRDI,R.V.BAVISOTTO,N.C.HOPPER,N.VUKSANOVIC,             
JRNL        AUTH 2 T.R.MELKONIAN,N.R.SILVAGGI,D.N.FRICK                         
JRNL        TITL   DISCOVERY OF DRUG-LIKE LIGANDS FOR THE MAC1 DOMAIN OF        
JRNL        TITL 2 SARS-COV-2 NSP3.                                             
JRNL        REF    SLAS DISCOV                   V.  25  1162 2020              
JRNL        REFN                   ESSN 2472-5560                               
JRNL        PMID   32981460                                                     
JRNL        DOI    10.1177/2472555220960428                                     
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.55 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.18.2_3874                                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : GEOSTD + MONOMER LIBRARY + CDL V1.2           
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.55                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 24.70                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 20433                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.159                           
REMARK   3   R VALUE            (WORKING SET) : 0.157                           
REMARK   3   FREE R VALUE                     : 0.182                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.780                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1998                            
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 24.7000 -  3.7300    0.86     1251   136  0.1718 0.1739        
REMARK   3     2  3.7300 -  2.9600    0.98     1393   151  0.1465 0.1737        
REMARK   3     3  2.9600 -  2.5900    0.99     1374   148  0.1521 0.1734        
REMARK   3     4  2.5900 -  2.3500    0.98     1366   149  0.1552 0.1873        
REMARK   3     5  2.3500 -  2.1800    0.96     1337   145  0.1464 0.1727        
REMARK   3     6  2.1800 -  2.0500    0.96     1331   143  0.1490 0.1937        
REMARK   3     7  2.0500 -  1.9500    0.95     1309   142  0.1539 0.1865        
REMARK   3     8  1.9500 -  1.8600    0.95     1326   145  0.1574 0.1704        
REMARK   3     9  1.8600 -  1.7900    0.96     1329   143  0.1545 0.1783        
REMARK   3    10  1.7900 -  1.7300    0.97     1331   145  0.1604 0.2243        
REMARK   3    11  1.7300 -  1.6800    0.95     1313   141  0.1610 0.2162        
REMARK   3    12  1.6800 -  1.6300    0.96     1312   143  0.1677 0.1898        
REMARK   3    13  1.6300 -  1.5900    0.95     1336   145  0.1749 0.2021        
REMARK   3    14  1.5900 -  1.5500    0.85     1145   124  0.1769 0.1956        
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)     : 0.102            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 16.758           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 13.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 20.33                          
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      :  0.008           1298                                  
REMARK   3   ANGLE     :  0.893           1775                                  
REMARK   3   CHIRALITY :  0.057            210                                  
REMARK   3   PLANARITY :  0.006            229                                  
REMARK   3   DIHEDRAL  : 20.316            463                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 7                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 208 THROUGH 242 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   6.1221  -9.2807   5.8167              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2208 T22:   0.1760                                     
REMARK   3      T33:   0.1226 T12:   0.0355                                     
REMARK   3      T13:   0.0101 T23:  -0.0518                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7290 L22:   2.4288                                     
REMARK   3      L33:   1.1193 L12:   0.6715                                     
REMARK   3      L13:   0.2428 L23:   0.7705                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0915 S12:   0.5641 S13:  -0.2525                       
REMARK   3      S21:  -0.4727 S22:   0.0469 S23:  -0.1523                       
REMARK   3      S31:   0.0939 S32:   0.3022 S33:  -0.0903                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 243 THROUGH 276 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  17.0405  -4.6609  23.1500              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0950 T22:   0.1892                                     
REMARK   3      T33:   0.1702 T12:  -0.0321                                     
REMARK   3      T13:  -0.0154 T23:  -0.0121                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.9037 L22:   2.2979                                     
REMARK   3      L33:   3.2871 L12:   0.1914                                     
REMARK   3      L13:   0.6003 L23:  -0.0425                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2490 S12:  -0.4594 S13:  -0.2315                       
REMARK   3      S21:   0.1808 S22:  -0.0261 S23:  -0.4144                       
REMARK   3      S31:   0.0077 S32:   0.3182 S33:  -0.1962                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 277 THROUGH 294 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  13.2456   0.1903  18.3053              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1184 T22:   0.1031                                     
REMARK   3      T33:   0.1101 T12:  -0.0293                                     
REMARK   3      T13:   0.0198 T23:  -0.0142                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2284 L22:   1.9951                                     
REMARK   3      L33:   3.4328 L12:   0.3718                                     
REMARK   3      L13:   0.7207 L23:   0.9818                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0388 S12:  -0.1791 S13:   0.1946                       
REMARK   3      S21:  -0.1186 S22:   0.0773 S23:  -0.1777                       
REMARK   3      S31:  -0.2174 S32:   0.4254 S33:  -0.1295                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 295 THROUGH 309 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   3.5880  -3.9039  24.4143              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0968 T22:   0.1718                                     
REMARK   3      T33:   0.0571 T12:   0.0043                                     
REMARK   3      T13:   0.0068 T23:  -0.0078                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.4839 L22:   4.0357                                     
REMARK   3      L33:   5.5516 L12:   0.9535                                     
REMARK   3      L13:  -2.5609 L23:  -1.0643                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0298 S12:  -0.5634 S13:  -0.0979                       
REMARK   3      S21:   0.2430 S22:  -0.0982 S23:   0.1255                       
REMARK   3      S31:  -0.1609 S32:  -0.0997 S33:   0.0679                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 310 THROUGH 322 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.5825   1.2684  18.1468              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1260 T22:   0.1158                                     
REMARK   3      T33:   0.1389 T12:   0.0441                                     
REMARK   3      T13:  -0.0194 T23:  -0.0509                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4575 L22:   7.6113                                     
REMARK   3      L33:   7.3301 L12:   1.5214                                     
REMARK   3      L13:  -0.7995 L23:  -3.2630                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0265 S12:  -0.2221 S13:   0.3698                       
REMARK   3      S21:   0.0192 S22:   0.0177 S23:   0.3018                       
REMARK   3      S31:  -0.4841 S32:  -0.4615 S33:  -0.1544                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 323 THROUGH 361 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -0.5402  -6.9292  13.6408              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0970 T22:   0.0615                                     
REMARK   3      T33:   0.0855 T12:   0.0252                                     
REMARK   3      T13:  -0.0096 T23:  -0.0146                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.6110 L22:   1.9134                                     
REMARK   3      L33:   3.1363 L12:   0.8468                                     
REMARK   3      L13:  -0.6623 L23:   0.7853                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0102 S12:   0.0624 S13:  -0.0878                       
REMARK   3      S21:  -0.0986 S22:  -0.0904 S23:   0.1677                       
REMARK   3      S31:   0.0276 S32:  -0.1077 S33:   0.0402                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 362 THROUGH 373 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.2568 -17.4146   9.7764              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2002 T22:   0.1029                                     
REMARK   3      T33:   0.2169 T12:   0.0084                                     
REMARK   3      T13:  -0.0369 T23:  -0.0365                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.7321 L22:   0.9079                                     
REMARK   3      L33:   6.7219 L12:   1.2662                                     
REMARK   3      L13:   2.6570 L23:  -1.2682                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0045 S12:   0.1824 S13:  -0.1137                       
REMARK   3      S21:  -0.2063 S22:   0.0274 S23:   0.4785                       
REMARK   3      S31:   0.2231 S32:  -0.3818 S33:   0.1050                       
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 7JME COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-AUG-20.                  
REMARK 100 THE DEPOSITION ID IS D_1000251058.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-JUL-20                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 21-ID-F                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97872                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 300 MM PLATE           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 20508                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.550                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 24.700                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.1                               
REMARK 200  DATA REDUNDANCY                : 3.400                              
REMARK 200  R MERGE                    (I) : 0.07640                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 10.9100                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.55                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.61                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.29100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 4.230                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 6WEY                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 38.42                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.00                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 4K, 0.1M MES PH 6.5, CRYSTALS    
REMARK 280  THEN SOAKED IN 35% PEG 4K, 20MM CAMP, VAPOR DIFFUSION, HANGING      
REMARK 280  DROP, TEMPERATURE 289.15K                                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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       16.51800            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A   206                                                      
REMARK 465     VAL A   207                                                      
REMARK 465     GLU A   374                                                      
REMARK 465     MET A   375                                                      
REMARK 465     LYS A   376                                                      
REMARK 465     SER A   377                                                      
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 233    CG   CD   CE   NZ                                   
REMARK 470     LYS A 235    CG   CD   CE   NZ                                   
REMARK 470     LYS A 280    CD   CE   NZ                                        
REMARK 470     LYS A 294    CE   NZ                                             
REMARK 470     LYS A 367    CE   NZ                                             
REMARK 470     LEU A 373    CG   CD1  CD2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A   597     O    HOH A   599              1.99            
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    HIS A 290     -131.55     53.02                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CMP A 401                 
DBREF  7JME A  207   377  UNP    P0DTD1   R1AB_SARS2    1025   1195             
SEQADV 7JME GLY A  206  UNP  P0DTD1              EXPRESSION TAG                 
SEQRES   1 A  172  GLY VAL ASN SER PHE SER GLY TYR LEU LYS LEU THR ASP          
SEQRES   2 A  172  ASN VAL TYR ILE LYS ASN ALA ASP ILE VAL GLU GLU ALA          
SEQRES   3 A  172  LYS LYS VAL LYS PRO THR VAL VAL VAL ASN ALA ALA ASN          
SEQRES   4 A  172  VAL TYR LEU LYS HIS GLY GLY GLY VAL ALA GLY ALA LEU          
SEQRES   5 A  172  ASN LYS ALA THR ASN ASN ALA MET GLN VAL GLU SER ASP          
SEQRES   6 A  172  ASP TYR ILE ALA THR ASN GLY PRO LEU LYS VAL GLY GLY          
SEQRES   7 A  172  SER CYS VAL LEU SER GLY HIS ASN LEU ALA LYS HIS CYS          
SEQRES   8 A  172  LEU HIS VAL VAL GLY PRO ASN VAL ASN LYS GLY GLU ASP          
SEQRES   9 A  172  ILE GLN LEU LEU LYS SER ALA TYR GLU ASN PHE ASN GLN          
SEQRES  10 A  172  HIS GLU VAL LEU LEU ALA PRO LEU LEU SER ALA GLY ILE          
SEQRES  11 A  172  PHE GLY ALA ASP PRO ILE HIS SER LEU ARG VAL CYS VAL          
SEQRES  12 A  172  ASP THR VAL ARG THR ASN VAL TYR LEU ALA VAL PHE ASP          
SEQRES  13 A  172  LYS ASN LEU TYR ASP LYS LEU VAL SER SER PHE LEU GLU          
SEQRES  14 A  172  MET LYS SER                                                  
HET    CMP  A 401      22                                                       
HETNAM     CMP ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE                             
HETSYN     CMP CYCLIC AMP; CAMP                                                 
FORMUL   2  CMP    C10 H12 N5 O6 P                                              
FORMUL   3  HOH   *135(H2 O)                                                    
HELIX    1 AA1 ASP A  226  LYS A  235  1                                  10    
HELIX    2 AA2 GLY A  251  THR A  261  1                                  11    
HELIX    3 AA3 ASN A  263  GLY A  277  1                                  15    
HELIX    4 AA4 ASN A  303  GLY A  307  5                                   5    
HELIX    5 AA5 GLN A  311  ASN A  319  1                                   9    
HELIX    6 AA6 PHE A  320  HIS A  323  5                                   4    
HELIX    7 AA7 ASP A  339  VAL A  351  1                                  13    
HELIX    8 AA8 ASP A  361  LEU A  373  1                                  13    
SHEET    1 AA1 4 LEU A 214  LYS A 215  0                                        
SHEET    2 AA1 4 VAL A 220  ASN A 224 -1  O  ILE A 222   N  LEU A 214           
SHEET    3 AA1 4 ASN A 354  VAL A 359  1  O  LEU A 357   N  TYR A 221           
SHEET    4 AA1 4 VAL A 325  ALA A 328  1  N  LEU A 326   O  TYR A 356           
SHEET    1 AA2 3 VAL A 238  ALA A 243  0                                        
SHEET    2 AA2 3 HIS A 295  VAL A 300  1  O  VAL A 299   N  ASN A 241           
SHEET    3 AA2 3 SER A 284  SER A 288 -1  N  LEU A 287   O  CYS A 296           
SITE     1 AC1 16 ALA A 242  LYS A 248  GLY A 250  GLY A 251                    
SITE     2 AC1 16 GLY A 252  VAL A 253  ALA A 254  SER A 332                    
SITE     3 AC1 16 ALA A 333  GLY A 334  ILE A 335  PHE A 336                    
SITE     4 AC1 16 HOH A 502  HOH A 548  HOH A 575  HOH A 592                    
CRYST1   37.210   33.036   60.476  90.00  96.35  90.00 P 1 21 1      2          
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      0.026874  0.000000  0.002991        0.00000                         
SCALE2      0.000000  0.030270  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016638        0.00000                         
ATOM      1  N   ASN A 208      12.070  -4.315   0.584  1.00 32.11           N  
ANISOU    1  N   ASN A 208     4527   4920   2752     48   1045   -374       N  
ATOM      2  CA  ASN A 208      10.651  -4.605   0.749  1.00 31.78           C  
ANISOU    2  CA  ASN A 208     4588   4817   2669     60    893   -351       C  
ATOM      3  C   ASN A 208      10.158  -5.591  -0.329  1.00 27.59           C  
ANISOU    3  C   ASN A 208     4155   4327   2002    113    844   -473       C  
ATOM      4  O   ASN A 208       9.075  -5.428  -0.874  1.00 29.10           O  
ANISOU    4  O   ASN A 208     4458   4522   2077     85    729   -418       O  
ATOM      5  CB  ASN A 208       9.822  -3.312   0.698  1.00 32.78           C  
ANISOU    5  CB  ASN A 208     4800   4916   2740    -23    819   -150       C  
ATOM      6  CG  ASN A 208      10.121  -2.360   1.858  1.00 38.15           C  
ANISOU    6  CG  ASN A 208     5392   5526   3577    -68    840    -34       C  
ATOM      7  OD1 ASN A 208      10.437  -2.778   2.980  1.00 28.66           O  
ANISOU    7  OD1 ASN A 208     4099   4265   2527    -39    852    -87       O  
ATOM      8  ND2 ASN A 208       9.984  -1.067   1.600  1.00 40.57           N  
ANISOU    8  ND2 ASN A 208     5727   5830   3857   -135    831    125       N  
ATOM      9  HA  ASN A 208      10.513  -5.015   1.617  1.00 38.17           H  
ATOM     10  HB2 ASN A 208      10.019  -2.845  -0.129  1.00 39.38           H  
ATOM     11  HB3 ASN A 208       8.880  -3.540   0.734  1.00 39.38           H  
ATOM     12 HD21 ASN A 208      10.139  -0.486   2.216  1.00 48.72           H  
ATOM     13 HD22 ASN A 208       9.740  -0.808   0.817  1.00 48.72           H  
ATOM     14  N   SER A 209      10.958  -6.626  -0.600  1.00 39.18           N  
ANISOU   14  N   SER A 209     5573   5802   3514    177    922   -639       N  
ATOM     15  CA  SER A 209      10.615  -7.651  -1.591  1.00 38.59           C  
ANISOU   15  CA  SER A 209     5592   5733   3338    222    890   -771       C  
ATOM     16  C   SER A 209       9.825  -8.778  -0.919  1.00 35.76           C  
ANISOU   16  C   SER A 209     5218   5258   3111    270    756   -876       C  
ATOM     17  O   SER A 209      10.262  -9.922  -0.800  1.00 45.68           O  
ANISOU   17  O   SER A 209     6393   6472   4492    341    760  -1024       O  
ATOM     18  CB  SER A 209      11.877  -8.172  -2.267  1.00 40.91           C  
ANISOU   18  CB  SER A 209     5819   6090   3634    244   1041   -898       C  
ATOM     19  OG  SER A 209      12.957  -8.229  -1.349  1.00 49.86           O  
ANISOU   19  OG  SER A 209     6774   7202   4968    264   1117   -933       O  
ATOM     20  H   SER A 209      11.717  -6.759  -0.218  1.00 47.06           H  
ATOM     21  HA  SER A 209      10.048  -7.251  -2.268  1.00 46.34           H  
ATOM     22  HB2 SER A 209      11.706  -9.064  -2.608  1.00 49.13           H  
ATOM     23  HB3 SER A 209      12.113  -7.577  -2.995  1.00 49.13           H  
ATOM     24  HG  SER A 209      13.654  -8.486  -1.741  1.00 59.86           H  
ATOM     25  N   PHE A 210       8.624  -8.423  -0.477  1.00 26.11           N  
ANISOU   25  N   PHE A 210     4043   3996   1882    245    612   -786       N  
ATOM     26  CA  PHE A 210       7.737  -9.390   0.153  1.00 20.95           C  
ANISOU   26  CA  PHE A 210     3372   3225   1362    332    447   -847       C  
ATOM     27  C   PHE A 210       7.160 -10.360  -0.875  1.00 25.20           C  
ANISOU   27  C   PHE A 210     3984   3761   1829    335    381   -962       C  
ATOM     28  O   PHE A 210       6.710  -9.960  -1.954  1.00 30.06           O  
ANISOU   28  O   PHE A 210     4711   4456   2255    265    368   -930       O  
ATOM     29  CB  PHE A 210       6.606  -8.668   0.871  1.00 19.26           C  
ANISOU   29  CB  PHE A 210     3200   2918   1200    311    309   -680       C  
ATOM     30  CG  PHE A 210       7.078  -7.740   1.975  1.00 20.70           C  
ANISOU   30  CG  PHE A 210     3294   3061   1512    271    361   -544       C  
ATOM     31  CD1 PHE A 210       7.185  -6.368   1.758  1.00 17.96           C  
ANISOU   31  CD1 PHE A 210     2988   2769   1066    188    422   -391       C  
ATOM     32  CD2 PHE A 210       7.412  -8.231   3.218  1.00 23.06           C  
ANISOU   32  CD2 PHE A 210     3477   3262   2023    313    340   -566       C  
ATOM     33  CE1 PHE A 210       7.613  -5.523   2.754  1.00 20.77           C  
ANISOU   33  CE1 PHE A 210     3263   3086   1543    148    470   -281       C  
ATOM     34  CE2 PHE A 210       7.847  -7.385   4.213  1.00 23.87           C  
ANISOU   34  CE2 PHE A 210     3506   3336   2229    271    382   -452       C  
ATOM     35  CZ  PHE A 210       7.935  -6.027   3.990  1.00 19.49           C  
ANISOU   35  CZ  PHE A 210     2984   2838   1585    188    448   -315       C  
ATOM     36  H   PHE A 210       8.299  -7.628  -0.530  1.00 31.37           H  
ATOM     37  HA  PHE A 210       8.241  -9.907   0.801  1.00 24.96           H  
ATOM     38  HB2 PHE A 210       6.116  -8.135   0.225  1.00 22.94           H  
ATOM     39  HB3 PHE A 210       6.018  -9.328   1.271  1.00 22.94           H  
ATOM     40  HD1 PHE A 210       6.964  -6.017   0.925  1.00 21.43           H  
ATOM     41  HD2 PHE A 210       7.342  -9.143   3.387  1.00 27.71           H  
ATOM     42  HE1 PHE A 210       7.686  -4.611   2.591  1.00 24.96           H  
ATOM     43  HE2 PHE A 210       8.085  -7.733   5.042  1.00 28.68           H  
ATOM     44  HZ  PHE A 210       8.209  -5.457   4.672  1.00 23.43           H  
ATOM     45  N   SER A 211       7.149 -11.643  -0.527  1.00 22.26           N  
ANISOU   45  N   SER A 211     3548   3293   1616    408    328  -1087       N  
ATOM     46  CA  SER A 211       6.667 -12.674  -1.437  1.00 24.78           C  
ANISOU   46  CA  SER A 211     3924   3598   1894    414    276  -1204       C  
ATOM     47  C   SER A 211       5.810 -13.673  -0.669  1.00 25.52           C  
ANISOU   47  C   SER A 211     3976   3540   2180    471    122  -1232       C  
ATOM     48  O   SER A 211       6.096 -14.009   0.493  1.00 23.30           O  
ANISOU   48  O   SER A 211     3602   3159   2091    520    101  -1219       O  
ATOM     49  CB  SER A 211       7.833 -13.398  -2.130  1.00 31.82           C  
ANISOU   49  CB  SER A 211     4788   4530   2772    437    420  -1344       C  
ATOM     50  OG  SER A 211       8.468 -14.306  -1.252  1.00 46.48           O  
ANISOU   50  OG  SER A 211     6512   6289   4858    522    419  -1416       O  
ATOM     51  H   SER A 211       7.417 -11.941   0.234  1.00 26.53           H  
ATOM     52  HA  SER A 211       6.112 -12.269  -2.121  1.00 29.77           H  
ATOM     53  HB2 SER A 211       7.488 -13.888  -2.893  1.00 38.22           H  
ATOM     54  HB3 SER A 211       8.481 -12.739  -2.423  1.00 38.22           H  
ATOM     55  HG  SER A 211       9.087 -14.708  -1.653  1.00 55.81           H  
ATOM     56  N   GLY A 212       4.732 -14.103  -1.304  1.00 23.15           N  
ANISOU   56  N   GLY A 212     3747   3221   1828    452     12  -1258       N  
ATOM     57  CA  GLY A 212       3.894 -15.116  -0.713  1.00 22.49           C  
ANISOU   57  CA  GLY A 212     3626   2996   1923    486   -115  -1284       C  
ATOM     58  C   GLY A 212       2.973 -14.622   0.359  1.00 20.57           C  
ANISOU   58  C   GLY A 212     3367   2658   1792    478   -226  -1158       C  
ATOM     59  O   GLY A 212       2.548 -15.432   1.198  1.00 20.74           O  
ANISOU   59  O   GLY A 212     3333   2549   1997    496   -292  -1157       O  
ATOM     60  H   GLY A 212       4.470 -13.823  -2.073  1.00 27.60           H  
ATOM     61  HA2 GLY A 212       3.350 -15.515  -1.410  1.00 26.81           H  
ATOM     62  HA3 GLY A 212       4.461 -15.801  -0.324  1.00 26.81           H  
ATOM     63  N   TYR A 213       2.653 -13.323   0.360  1.00 19.92           N  
ANISOU   63  N   TYR A 213     3336   2629   1602    443   -240  -1043       N  
ATOM     64  CA  TYR A 213       1.683 -12.782   1.297  1.00 18.32           C  
ANISOU   64  CA  TYR A 213     3128   2328   1503    427   -344   -930       C  
ATOM     65  C   TYR A 213       0.271 -12.861   0.729  1.00 18.77           C  
ANISOU   65  C   TYR A 213     3232   2358   1544    401   -482   -920       C  
ATOM     66  O   TYR A 213       0.064 -12.820  -0.490  1.00 22.87           O  
ANISOU   66  O   TYR A 213     3818   2967   1903    384   -503   -954       O  
ATOM     67  CB  TYR A 213       2.010 -11.324   1.673  1.00 17.44           C  
ANISOU   67  CB  TYR A 213     3049   2265   1311    404   -298   -802       C  
ATOM     68  CG  TYR A 213       3.167 -11.228   2.634  1.00 16.58           C  
ANISOU   68  CG  TYR A 213     2855   2144   1302    421   -182   -784       C  
ATOM     69  CD1 TYR A 213       4.459 -11.460   2.215  1.00 17.59           C  
ANISOU   69  CD1 TYR A 213     2952   2367   1364    452    -51   -870       C  
ATOM     70  CD2 TYR A 213       2.954 -10.923   3.987  1.00 14.96           C  
ANISOU   70  CD2 TYR A 213     2583   1830   1270    396   -204   -681       C  
ATOM     71  CE1 TYR A 213       5.514 -11.408   3.091  1.00 16.96           C  
ANISOU   71  CE1 TYR A 213     2770   2270   1403    467     37   -855       C  
ATOM     72  CE2 TYR A 213       4.006 -10.856   4.863  1.00 14.84           C  
ANISOU   72  CE2 TYR A 213     2487   1804   1347    404   -117   -658       C  
ATOM     73  CZ  TYR A 213       5.282 -11.086   4.414  1.00 15.34           C  
ANISOU   73  CZ  TYR A 213     2512   1959   1357    443     -6   -742       C  
ATOM     74  OH  TYR A 213       6.328 -11.051   5.284  1.00 17.03           O  
ANISOU   74  OH  TYR A 213     2632   2158   1681    457     61   -728       O  
ATOM     75  H   TYR A 213       2.988 -12.740  -0.176  1.00 23.72           H  
ATOM     76  HA  TYR A 213       1.715 -13.313   2.109  1.00 21.80           H  
ATOM     77  HB2 TYR A 213       2.244 -10.834   0.869  1.00 20.75           H  
ATOM     78  HB3 TYR A 213       1.234 -10.922   2.093  1.00 20.75           H  
ATOM     79  HD1 TYR A 213       4.620 -11.656   1.320  1.00 21.14           H  
ATOM     80  HD2 TYR A 213       2.090 -10.765   4.292  1.00 17.77           H  
ATOM     81  HE1 TYR A 213       6.377 -11.588   2.797  1.00 20.17           H  
ATOM     82  HE2 TYR A 213       3.855 -10.656   5.758  1.00 17.84           H  
ATOM     83  HH  TYR A 213       6.977 -11.481   4.970  1.00 20.47           H  
ATOM     84  N   LEU A 214      -0.688 -13.033   1.628  1.00 18.45           N  
ANISOU   84  N   LEU A 214     3144   2191   1676    390   -570   -876       N  
ATOM     85  CA  LEU A 214      -2.104 -12.949   1.309  1.00 17.93           C  
ANISOU   85  CA  LEU A 214     3091   2084   1638    365   -702   -854       C  
ATOM     86  C   LEU A 214      -2.606 -11.561   1.697  1.00 18.78           C  
ANISOU   86  C   LEU A 214     3220   2175   1739    335   -754   -727       C  
ATOM     87  O   LEU A 214      -2.416 -11.122   2.835  1.00 16.77           O  
ANISOU   87  O   LEU A 214     2926   1855   1591    320   -717   -664       O  
ATOM     88  CB  LEU A 214      -2.870 -14.039   2.054  1.00 21.63           C  
ANISOU   88  CB  LEU A 214     3477   2428   2313    357   -741   -884       C  
ATOM     89  CG  LEU A 214      -4.377 -14.110   1.862  1.00 21.25           C  
ANISOU   89  CG  LEU A 214     3411   2326   2337    332   -861   -876       C  
ATOM     90  CD1 LEU A 214      -4.732 -14.352   0.403  1.00 21.32           C  
ANISOU   90  CD1 LEU A 214     3484   2412   2202    344   -934   -953       C  
ATOM     91  CD2 LEU A 214      -4.954 -15.225   2.723  1.00 26.21           C  
ANISOU   91  CD2 LEU A 214     3955   2852   3154    311   -853   -891       C  
ATOM     92  H   LEU A 214      -0.538 -13.206   2.457  1.00 22.18           H  
ATOM     93  HA  LEU A 214      -2.256 -13.071   0.359  1.00 21.34           H  
ATOM     94  HB2 LEU A 214      -2.512 -14.895   1.773  1.00 25.99           H  
ATOM     95  HB3 LEU A 214      -2.715 -13.910   3.004  1.00 25.99           H  
ATOM     96  HG  LEU A 214      -4.766 -13.263   2.130  1.00 25.54           H  
ATOM     97 HD11 LEU A 214      -5.697 -14.397   0.316  1.00 25.61           H  
ATOM     98 HD12 LEU A 214      -4.385 -13.621  -0.132  1.00 25.61           H  
ATOM     99 HD13 LEU A 214      -4.335 -15.190   0.116  1.00 25.61           H  
ATOM    100 HD21 LEU A 214      -5.913 -15.264   2.587  1.00 31.49           H  
ATOM    101 HD22 LEU A 214      -4.548 -16.067   2.462  1.00 31.49           H  
ATOM    102 HD23 LEU A 214      -4.759 -15.038   3.654  1.00 31.49           H  
ATOM    103  N   LYS A 215      -3.207 -10.856   0.746  1.00 19.36           N  
ANISOU  103  N   LYS A 215     3359   2308   1688    321   -840   -682       N  
ATOM    104  CA  LYS A 215      -3.731  -9.512   1.000  1.00 17.53           C  
ANISOU  104  CA  LYS A 215     3146   2054   1461    294   -906   -549       C  
ATOM    105  C   LYS A 215      -5.070  -9.636   1.717  1.00 17.08           C  
ANISOU  105  C   LYS A 215     3002   1862   1625    278  -1012   -549       C  
ATOM    106  O   LYS A 215      -6.026 -10.184   1.163  1.00 23.30           O  
ANISOU  106  O   LYS A 215     3771   2628   2454    285  -1105   -603       O  
ATOM    107  CB  LYS A 215      -3.873  -8.754  -0.315  1.00 20.07           C  
ANISOU  107  CB  LYS A 215     3561   2480   1586    281   -959   -481       C  
ATOM    108  CG  LYS A 215      -4.185  -7.262  -0.152  1.00 22.93           C  
ANISOU  108  CG  LYS A 215     3943   2823   1945    253  -1006   -313       C  
ATOM    109  CD  LYS A 215      -4.110  -6.556  -1.511  1.00 25.67           C  
ANISOU  109  CD  LYS A 215     4389   3279   2086    231  -1029   -232       C  
ATOM    110  CE  LYS A 215      -4.126  -5.051  -1.339  1.00 38.50           C  
ANISOU  110  CE  LYS A 215     6030   4883   3714    199  -1033    -51       C  
ATOM    111  NZ  LYS A 215      -3.966  -4.334  -2.635  1.00 51.80           N  
ANISOU  111  NZ  LYS A 215     7813   6669   5201    168  -1041     39       N  
ATOM    112  H   LYS A 215      -3.327 -11.132  -0.059  1.00 23.27           H  
ATOM    113  HA  LYS A 215      -3.121  -9.021   1.573  1.00 20.86           H  
ATOM    114  HB2 LYS A 215      -3.040  -8.828  -0.807  1.00 24.13           H  
ATOM    115  HB3 LYS A 215      -4.596  -9.152  -0.825  1.00 24.13           H  
ATOM    116  HG2 LYS A 215      -5.080  -7.153   0.206  1.00 27.55           H  
ATOM    117  HG3 LYS A 215      -3.537  -6.856   0.445  1.00 27.55           H  
ATOM    118  HD2 LYS A 215      -3.288  -6.806  -1.961  1.00 30.84           H  
ATOM    119  HD3 LYS A 215      -4.875  -6.811  -2.051  1.00 30.84           H  
ATOM    120  HE2 LYS A 215      -4.972  -4.784  -0.948  1.00 46.23           H  
ATOM    121  HE3 LYS A 215      -3.395  -4.790  -0.757  1.00 46.23           H  
ATOM    122  HZ1 LYS A 215      -3.906  -3.457  -2.493  1.00 62.20           H  
ATOM    123  HZ2 LYS A 215      -3.226  -4.610  -3.047  1.00 62.20           H  
ATOM    124  HZ3 LYS A 215      -4.666  -4.494  -3.160  1.00 62.20           H  
ATOM    125  N   LEU A 216      -5.128  -9.187   2.964  1.00 15.42           N  
ANISOU  125  N   LEU A 216     2732   1563   1564    250   -982   -497       N  
ATOM    126  CA  LEU A 216      -6.365  -9.242   3.736  1.00 18.61           C  
ANISOU  126  CA  LEU A 216     3031   1846   2192    220  -1037   -494       C  
ATOM    127  C   LEU A 216      -7.225  -8.002   3.539  1.00 16.83           C  
ANISOU  127  C   LEU A 216     2798   1593   2003    204  -1155   -411       C  
ATOM    128  O   LEU A 216      -8.454  -8.105   3.489  1.00 19.91           O  
ANISOU  128  O   LEU A 216     3115   1919   2531    203  -1240   -433       O  
ATOM    129  CB  LEU A 216      -6.079  -9.378   5.231  1.00 16.49           C  
ANISOU  129  CB  LEU A 216     2680   1505   2081    180   -910   -463       C  
ATOM    130  CG  LEU A 216      -5.374 -10.675   5.669  1.00 17.30           C  
ANISOU  130  CG  LEU A 216     2756   1621   2198    190   -803   -513       C  
ATOM    131  CD1 LEU A 216      -5.174 -10.596   7.174  1.00 16.72           C  
ANISOU  131  CD1 LEU A 216     2599   1512   2243    135   -683   -438       C  
ATOM    132  CD2 LEU A 216      -6.136 -11.913   5.269  1.00 21.21           C  
ANISOU  132  CD2 LEU A 216     3215   2106   2740    200   -844   -588       C  
ATOM    133  H   LEU A 216      -4.463  -8.844   3.389  1.00 18.33           H  
ATOM    134  HA  LEU A 216      -6.851 -10.028   3.441  1.00 22.36           H  
ATOM    135  HB2 LEU A 216      -5.512  -8.638   5.499  1.00 19.83           H  
ATOM    136  HB3 LEU A 216      -6.924  -9.336   5.705  1.00 19.83           H  
ATOM    137  HG  LEU A 216      -4.517 -10.758   5.220  1.00 20.80           H  
ATOM    138 HD11 LEU A 216      -4.737 -11.407   7.478  1.00 20.10           H  
ATOM    139 HD12 LEU A 216      -4.622  -9.826   7.380  1.00 20.10           H  
ATOM    140 HD13 LEU A 216      -6.039 -10.506   7.603  1.00 20.10           H  
ATOM    141 HD21 LEU A 216      -5.654 -12.695   5.581  1.00 25.49           H  
ATOM    142 HD22 LEU A 216      -7.018 -11.885   5.673  1.00 25.49           H  
ATOM    143 HD23 LEU A 216      -6.216 -11.937   4.303  1.00 25.49           H  
ATOM    144  N   THR A 217      -6.589  -6.833   3.466  1.00 15.03           N  
ANISOU  144  N   THR A 217     2604   1418   1689    197  -1097   -280       N  
ATOM    145  CA  THR A 217      -7.273  -5.582   3.222  1.00 16.31           C  
ANISOU  145  CA  THR A 217     2755   1552   1888    191  -1190   -171       C  
ATOM    146  C   THR A 217      -6.382  -4.762   2.299  1.00 19.27           C  
ANISOU  146  C   THR A 217     3249   2040   2031    198  -1161    -58       C  
ATOM    147  O   THR A 217      -5.299  -5.205   1.920  1.00 20.24           O  
ANISOU  147  O   THR A 217     3442   2263   1984    204  -1057    -85       O  
ATOM    148  CB  THR A 217      -7.530  -4.804   4.517  1.00 14.71           C  
ANISOU  148  CB  THR A 217     2441   1251   1897    148  -1112   -108       C  
ATOM    149  OG1 THR A 217      -6.286  -4.324   5.060  1.00 17.45           O  
ANISOU  149  OG1 THR A 217     2806   1645   2180    124   -943    -30       O  
ATOM    150  CG2 THR A 217      -8.190  -5.689   5.552  1.00 17.07           C  
ANISOU  150  CG2 THR A 217     2637   1451   2397    117  -1089   -219       C  
ATOM    151  H   THR A 217      -5.739  -6.745   3.558  1.00 17.86           H  
ATOM    152  HA  THR A 217      -8.128  -5.765   2.803  1.00 19.60           H  
ATOM    153  HB  THR A 217      -8.116  -4.057   4.319  1.00 17.69           H  
ATOM    154  HG1 THR A 217      -6.204  -3.502   4.908  1.00 20.98           H  
ATOM    155 HG21 THR A 217      -8.363  -5.182   6.360  1.00 20.52           H  
ATOM    156 HG22 THR A 217      -9.031  -6.030   5.209  1.00 20.52           H  
ATOM    157 HG23 THR A 217      -7.611  -6.437   5.767  1.00 20.52           H  
ATOM    158  N   ASP A 218      -6.812  -3.542   1.981  1.00 19.08           N  
ANISOU  158  N   ASP A 218     3244   1992   2014    194  -1244     66       N  
ATOM    159  CA  ASP A 218      -6.031  -2.733   1.055  1.00 21.02           C  
ANISOU  159  CA  ASP A 218     3598   2339   2051    179  -1187    179       C  
ATOM    160  C   ASP A 218      -4.595  -2.554   1.526  1.00 20.31           C  
ANISOU  160  C   ASP A 218     3540   2314   1865    153  -1001    225       C  
ATOM    161  O   ASP A 218      -3.696  -2.381   0.691  1.00 23.05           O  
ANISOU  161  O   ASP A 218     3979   2776   2002    137   -918    261       O  
ATOM    162  CB  ASP A 218      -6.679  -1.366   0.846  1.00 26.47           C  
ANISOU  162  CB  ASP A 218     4267   2969   2823    166  -1252    305       C  
ATOM    163  CG  ASP A 218      -7.848  -1.417  -0.094  1.00 33.58           C  
ANISOU  163  CG  ASP A 218     5176   3846   3735    191  -1427    278       C  
ATOM    164  OD1 ASP A 218      -8.610  -0.437  -0.124  1.00 33.52           O  
ANISOU  164  OD1 ASP A 218     5127   3762   3848    191  -1509    349       O  
ATOM    165  OD2 ASP A 218      -8.004  -2.439  -0.801  1.00 32.84           O  
ANISOU  165  OD2 ASP A 218     5128   3811   3538    211  -1480    179       O  
ATOM    166  H   ASP A 218      -7.529  -3.172   2.279  1.00 22.93           H  
ATOM    167  HA  ASP A 218      -6.018  -3.193   0.201  1.00 25.26           H  
ATOM    168  HB2 ASP A 218      -6.994  -1.032   1.700  1.00 31.80           H  
ATOM    169  HB3 ASP A 218      -6.021  -0.758   0.474  1.00 31.80           H  
ATOM    170  N   ASN A 219      -4.362  -2.584   2.841  1.00 16.54           N  
ANISOU  170  N   ASN A 219     2945   1769   1569    133   -885    208       N  
ATOM    171  CA  ASN A 219      -3.043  -2.302   3.377  1.00 14.64           C  
ANISOU  171  CA  ASN A 219     2695   1582   1286    102   -696    249       C  
ATOM    172  C   ASN A 219      -2.483  -3.315   4.359  1.00 15.16           C  
ANISOU  172  C   ASN A 219     2683   1637   1441    105   -588    144       C  
ATOM    173  O   ASN A 219      -1.394  -3.079   4.881  1.00 15.68           O  
ANISOU  173  O   ASN A 219     2726   1740   1493     82   -447    173       O  
ATOM    174  CB  ASN A 219      -3.074  -0.926   4.074  1.00 18.79           C  
ANISOU  174  CB  ASN A 219     3173   2037   1931     60   -656    380       C  
ATOM    175  CG  ASN A 219      -3.912  -0.952   5.353  1.00 16.11           C  
ANISOU  175  CG  ASN A 219     2705   1568   1848     48   -670    338       C  
ATOM    176  OD1 ASN A 219      -5.155  -1.148   5.293  1.00 18.03           O  
ANISOU  176  OD1 ASN A 219     2910   1734   2208     69   -806    293       O  
ATOM    177  ND2 ASN A 219      -3.275  -0.705   6.484  1.00 18.57           N  
ANISOU  177  ND2 ASN A 219     2950   1857   2247      7   -533    350       N  
ATOM    178  H   ASN A 219      -4.956  -2.765   3.437  1.00 19.88           H  
ATOM    179  HA  ASN A 219      -2.427  -2.295   2.628  1.00 17.60           H  
ATOM    180  HB2 ASN A 219      -2.170  -0.667   4.309  1.00 22.59           H  
ATOM    181  HB3 ASN A 219      -3.461  -0.272   3.471  1.00 22.59           H  
ATOM    182 HD21 ASN A 219      -3.705  -0.708   7.229  1.00 22.31           H  
ATOM    183 HD22 ASN A 219      -2.431  -0.540   6.474  1.00 22.31           H  
ATOM    184  N   VAL A 220      -3.159  -4.430   4.603  1.00 12.96           N  
ANISOU  184  N   VAL A 220     2368   1305   1250    130   -656     25       N  
ATOM    185  CA  VAL A 220      -2.688  -5.447   5.533  1.00 11.95           C  
ANISOU  185  CA  VAL A 220     2185   1148   1210    131   -575    -64       C  
ATOM    186  C   VAL A 220      -2.507  -6.739   4.759  1.00 12.80           C  
ANISOU  186  C   VAL A 220     2342   1304   1218    180   -610   -193       C  
ATOM    187  O   VAL A 220      -3.446  -7.215   4.108  1.00 14.37           O  
ANISOU  187  O   VAL A 220     2568   1484   1409    200   -738   -258       O  
ATOM    188  CB  VAL A 220      -3.648  -5.679   6.708  1.00 14.28           C  
ANISOU  188  CB  VAL A 220     2392   1311   1722     99   -605    -93       C  
ATOM    189  CG1 VAL A 220      -3.143  -6.829   7.594  1.00 13.80           C  
ANISOU  189  CG1 VAL A 220     2305   1214   1725     96   -539   -173       C  
ATOM    190  CG2 VAL A 220      -3.810  -4.391   7.518  1.00 13.32           C  
ANISOU  190  CG2 VAL A 220     2215   1139   1706     48   -557     14       C  
ATOM    191  H   VAL A 220      -3.910  -4.624   4.233  1.00 15.37           H  
ATOM    192  HA  VAL A 220      -1.837  -5.155   5.896  1.00 14.17           H  
ATOM    193  HB  VAL A 220      -4.520  -5.931   6.365  1.00 17.17           H  
ATOM    194 HG11 VAL A 220      -3.752  -6.943   8.341  1.00 16.60           H  
ATOM    195 HG12 VAL A 220      -3.110  -7.643   7.067  1.00 16.60           H  
ATOM    196 HG13 VAL A 220      -2.256  -6.611   7.920  1.00 16.60           H  
ATOM    197 HG21 VAL A 220      -4.418  -4.555   8.255  1.00 16.02           H  
ATOM    198 HG22 VAL A 220      -2.942  -4.121   7.859  1.00 16.02           H  
ATOM    199 HG23 VAL A 220      -4.168  -3.698   6.941  1.00 16.02           H  
ATOM    200  N   TYR A 221      -1.312  -7.314   4.872  1.00 12.68           N  
ANISOU  200  N   TYR A 221     2328   1345   1146    200   -501   -242       N  
ATOM    201  CA  TYR A 221      -0.903  -8.546   4.218  1.00 15.01           C  
ANISOU  201  CA  TYR A 221     2658   1684   1362    252   -504   -379       C  
ATOM    202  C   TYR A 221      -0.428  -9.526   5.281  1.00 13.37           C  
ANISOU  202  C   TYR A 221     2388   1399   1293    267   -457   -447       C  
ATOM    203  O   TYR A 221       0.118  -9.117   6.305  1.00 11.90           O  
ANISOU  203  O   TYR A 221     2148   1184   1189    241   -381   -378       O  
ATOM    204  CB  TYR A 221       0.234  -8.265   3.217  1.00 16.16           C  
ANISOU  204  CB  TYR A 221     2862   1974   1302    266   -408   -382       C  
ATOM    205  CG  TYR A 221      -0.074  -7.202   2.188  1.00 16.71           C  
ANISOU  205  CG  TYR A 221     3020   2122   1207    237   -445   -286       C  
ATOM    206  CD1 TYR A 221      -0.483  -7.553   0.908  1.00 21.08           C  
ANISOU  206  CD1 TYR A 221     3674   2742   1592    254   -530   -350       C  
ATOM    207  CD2 TYR A 221       0.057  -5.849   2.485  1.00 18.22           C  
ANISOU  207  CD2 TYR A 221     3204   2314   1404    188   -403   -131       C  
ATOM    208  CE1 TYR A 221      -0.774  -6.589  -0.048  1.00 23.99           C  
ANISOU  208  CE1 TYR A 221     4146   3176   1794    222   -584   -248       C  
ATOM    209  CE2 TYR A 221      -0.219  -4.868   1.508  1.00 18.33           C  
ANISOU  209  CE2 TYR A 221     3317   2384   1264    160   -451    -27       C  
ATOM    210  CZ  TYR A 221      -0.634  -5.250   0.261  1.00 23.40           C  
ANISOU  210  CZ  TYR A 221     4068   3091   1733    177   -546    -80       C  
ATOM    211  OH  TYR A 221      -0.918  -4.301  -0.712  1.00 30.36           O  
ANISOU  211  OH  TYR A 221     5037   4021   2476    140   -599     35       O  
ATOM    212  H   TYR A 221      -0.681  -6.984   5.355  1.00 15.04           H  
ATOM    213  HA  TYR A 221      -1.644  -8.947   3.737  1.00 18.05           H  
ATOM    214  HB2 TYR A 221       1.015  -7.973   3.713  1.00 19.42           H  
ATOM    215  HB3 TYR A 221       0.432  -9.085   2.739  1.00 19.42           H  
ATOM    216  HD1 TYR A 221      -0.564  -8.452   0.686  1.00 25.33           H  
ATOM    217  HD2 TYR A 221       0.329  -5.588   3.336  1.00 21.90           H  
ATOM    218  HE1 TYR A 221      -1.063  -6.844  -0.894  1.00 28.83           H  
ATOM    219  HE2 TYR A 221      -0.118  -3.966   1.711  1.00 22.04           H  
ATOM    220  HH  TYR A 221      -1.279  -4.669  -1.375  1.00 36.46           H  
ATOM    221  N   ILE A 222      -0.621 -10.824   5.038  1.00 13.31           N  
ANISOU  221  N   ILE A 222     2394   1353   1310    309   -510   -580       N  
ATOM    222  CA  ILE A 222      -0.261 -11.825   6.036  1.00 12.75           C  
ANISOU  222  CA  ILE A 222     2258   1199   1388    315   -476   -613       C  
ATOM    223  C   ILE A 222       0.422 -13.017   5.370  1.00 13.89           C  
ANISOU  223  C   ILE A 222     2392   1386   1501    369   -449   -723       C  
ATOM    224  O   ILE A 222       0.138 -13.374   4.223  1.00 15.10           O  
ANISOU  224  O   ILE A 222     2583   1596   1557    389   -482   -797       O  
ATOM    225  CB  ILE A 222      -1.501 -12.254   6.838  1.00 15.27           C  
ANISOU  225  CB  ILE A 222     2509   1426   1866    256   -522   -562       C  
ATOM    226  CG1 ILE A 222      -1.112 -13.042   8.073  1.00 15.99           C  
ANISOU  226  CG1 ILE A 222     2534   1470   2073    228   -462   -525       C  
ATOM    227  CG2 ILE A 222      -2.476 -13.018   5.966  1.00 14.30           C  
ANISOU  227  CG2 ILE A 222     2392   1304   1738    266   -601   -631       C  
ATOM    228  CD1 ILE A 222      -2.180 -13.008   9.141  1.00 25.01           C  
ANISOU  228  CD1 ILE A 222     3615   2569   3317    147   -446   -444       C  
ATOM    229  H   ILE A 222      -0.954 -11.142   4.312  1.00 15.79           H  
ATOM    230  HA  ILE A 222       0.395 -11.452   6.646  1.00 15.15           H  
ATOM    231  HB  ILE A 222      -1.949 -11.449   7.142  1.00 18.36           H  
ATOM    232 HG12 ILE A 222      -0.965 -13.968   7.823  1.00 19.23           H  
ATOM    233 HG13 ILE A 222      -0.300 -12.666   8.446  1.00 19.23           H  
ATOM    234 HG21 ILE A 222      -3.252 -13.259   6.496  1.00 17.20           H  
ATOM    235 HG22 ILE A 222      -2.746 -12.454   5.224  1.00 17.20           H  
ATOM    236 HG23 ILE A 222      -2.042 -13.818   5.632  1.00 17.20           H  
ATOM    237 HD11 ILE A 222      -1.882 -13.531   9.902  1.00 30.04           H  
ATOM    238 HD12 ILE A 222      -2.328 -12.088   9.410  1.00 30.04           H  
ATOM    239 HD13 ILE A 222      -2.998 -13.384   8.782  1.00 30.04           H  
ATOM    240  N   LYS A 223       1.353 -13.615   6.108  1.00 13.66           N  
ANISOU  240  N   LYS A 223     2309   1325   1556    388   -391   -730       N  
ATOM    241  CA  LYS A 223       2.135 -14.745   5.639  1.00 14.80           C  
ANISOU  241  CA  LYS A 223     2430   1486   1707    441   -362   -834       C  
ATOM    242  C   LYS A 223       2.454 -15.671   6.796  1.00 14.43           C  
ANISOU  242  C   LYS A 223     2323   1342   1816    436   -367   -800       C  
ATOM    243  O   LYS A 223       2.765 -15.209   7.890  1.00 13.52           O  
ANISOU  243  O   LYS A 223     2183   1192   1760    409   -349   -712       O  
ATOM    244  CB  LYS A 223       3.447 -14.309   4.987  1.00 15.54           C  
ANISOU  244  CB  LYS A 223     2527   1693   1686    492   -264   -899       C  
ATOM    245  CG  LYS A 223       4.248 -15.446   4.322  1.00 17.07           C  
ANISOU  245  CG  LYS A 223     2688   1909   1888    544   -221  -1026       C  
ATOM    246  CD  LYS A 223       5.534 -14.902   3.754  1.00 17.87           C  
ANISOU  246  CD  LYS A 223     2768   2134   1887    575    -95  -1082       C  
ATOM    247  CE  LYS A 223       6.318 -15.960   3.000  1.00 19.63           C  
ANISOU  247  CE  LYS A 223     2958   2380   2120    621    -39  -1219       C  
ATOM    248  NZ  LYS A 223       7.552 -15.393   2.395  1.00 20.63           N  
ANISOU  248  NZ  LYS A 223     3053   2637   2148    633    109  -1273       N  
ATOM    249  H   LYS A 223       1.555 -13.375   6.908  1.00 16.21           H  
ATOM    250  HA  LYS A 223       1.599 -15.226   4.989  1.00 17.58           H  
ATOM    251  HB2 LYS A 223       3.246 -13.654   4.300  1.00 18.47           H  
ATOM    252  HB3 LYS A 223       4.012 -13.913   5.668  1.00 18.47           H  
ATOM    253  HG2 LYS A 223       4.461 -16.124   4.982  1.00 20.30           H  
ATOM    254  HG3 LYS A 223       3.729 -15.835   3.602  1.00 20.30           H  
ATOM    255  HD2 LYS A 223       5.330 -14.181   3.138  1.00 21.26           H  
ATOM    256  HD3 LYS A 223       6.089 -14.574   4.478  1.00 21.26           H  
ATOM    257  HE2 LYS A 223       6.576 -16.667   3.613  1.00 23.38           H  
ATOM    258  HE3 LYS A 223       5.767 -16.322   2.288  1.00 23.38           H  
ATOM    259  HZ1 LYS A 223       8.003 -16.031   1.968  1.00 24.58           H  
ATOM    260  HZ2 LYS A 223       7.339 -14.752   1.815  1.00 24.58           H  
ATOM    261  HZ3 LYS A 223       8.071 -15.047   3.030  1.00 24.58           H  
ATOM    262  N   ASN A 224       2.448 -16.974   6.529  1.00 15.43           N  
ANISOU  262  N   ASN A 224     2439   1430   1994    461   -392   -871       N  
ATOM    263  CA  ASN A 224       2.915 -17.946   7.505  1.00 15.48           C  
ANISOU  263  CA  ASN A 224     2407   1353   2123    467   -404   -846       C  
ATOM    264  C   ASN A 224       4.428 -18.024   7.359  1.00 16.20           C  
ANISOU  264  C   ASN A 224     2459   1476   2220    542   -353   -912       C  
ATOM    265  O   ASN A 224       4.953 -18.692   6.454  1.00 17.60           O  
ANISOU  265  O   ASN A 224     2626   1682   2379    599   -331  -1031       O  
ATOM    266  CB  ASN A 224       2.233 -19.288   7.259  1.00 16.42           C  
ANISOU  266  CB  ASN A 224     2536   1409   2295    464   -455   -896       C  
ATOM    267  CG  ASN A 224       2.776 -20.400   8.101  1.00 16.89           C  
ANISOU  267  CG  ASN A 224     2573   1382   2464    482   -478   -884       C  
ATOM    268  OD1 ASN A 224       2.851 -21.558   7.619  1.00 22.07           O  
ANISOU  268  OD1 ASN A 224     3230   1996   3160    520   -504   -972       O  
ATOM    269  ND2 ASN A 224       3.165 -20.117   9.322  1.00 18.10           N  
ANISOU  269  ND2 ASN A 224     2711   1503   2663    456   -476   -785       N  
ATOM    270  H   ASN A 224       2.178 -17.318   5.789  1.00 18.34           H  
ATOM    271  HA  ASN A 224       2.706 -17.671   8.411  1.00 18.40           H  
ATOM    272  HB2 ASN A 224       1.288 -19.199   7.459  1.00 19.53           H  
ATOM    273  HB3 ASN A 224       2.354 -19.534   6.329  1.00 19.53           H  
ATOM    274 HD21 ASN A 224       3.480 -20.738   9.827  1.00 21.76           H  
ATOM    275 HD22 ASN A 224       3.104 -19.312   9.617  1.00 21.76           H  
ATOM    276  N   ALA A 225       5.136 -17.326   8.240  1.00 15.38           N  
ANISOU  276  N   ALA A 225     2325   1372   2145    539   -328   -841       N  
ATOM    277  CA  ALA A 225       6.583 -17.209   8.130  1.00 16.13           C  
ANISOU  277  CA  ALA A 225     2361   1512   2255    608   -272   -902       C  
ATOM    278  C   ALA A 225       7.183 -16.764   9.452  1.00 17.62           C  
ANISOU  278  C   ALA A 225     2514   1660   2520    594   -286   -804       C  
ATOM    279  O   ALA A 225       6.517 -16.151  10.290  1.00 17.15           O  
ANISOU  279  O   ALA A 225     2488   1570   2459    521   -308   -691       O  
ATOM    280  CB  ALA A 225       6.962 -16.229   7.024  1.00 19.55           C  
ANISOU  280  CB  ALA A 225     2799   2079   2551    629   -175   -971       C  
ATOM    281  H   ALA A 225       4.800 -16.909   8.913  1.00 18.27           H  
ATOM    282  HA  ALA A 225       6.949 -18.085   7.932  1.00 19.39           H  
ATOM    283  HB1 ALA A 225       7.929 -16.167   6.975  1.00 23.50           H  
ATOM    284  HB2 ALA A 225       6.609 -16.553   6.181  1.00 23.50           H  
ATOM    285  HB3 ALA A 225       6.585 -15.360   7.229  1.00 23.50           H  
ATOM    286  N   ASP A 226       8.478 -17.075   9.600  1.00 16.47           N  
ANISOU  286  N   ASP A 226     2294   1520   2445    661   -272   -857       N  
ATOM    287  CA  ASP A 226       9.319 -16.566  10.685  1.00 15.61           C  
ANISOU  287  CA  ASP A 226     2133   1393   2403    663   -284   -789       C  
ATOM    288  C   ASP A 226       9.772 -15.155  10.346  1.00 16.35           C  
ANISOU  288  C   ASP A 226     2193   1594   2424    664   -182   -796       C  
ATOM    289  O   ASP A 226      10.401 -14.940   9.304  1.00 17.22           O  
ANISOU  289  O   ASP A 226     2255   1810   2478    708    -84   -900       O  
ATOM    290  CB  ASP A 226      10.513 -17.504  10.831  1.00 17.09           C  
ANISOU  290  CB  ASP A 226     2238   1549   2705    741   -317   -860       C  
ATOM    291  CG  ASP A 226      11.407 -17.177  12.002  1.00 22.83           C  
ANISOU  291  CG  ASP A 226     2908   2247   3519    747   -363   -795       C  
ATOM    292  OD1 ASP A 226      12.118 -18.108  12.439  1.00 28.52           O  
ANISOU  292  OD1 ASP A 226     3584   2903   4348    794   -441   -819       O  
ATOM    293  OD2 ASP A 226      11.392 -16.030  12.481  1.00 25.12           O  
ANISOU  293  OD2 ASP A 226     3199   2570   3773    704   -332   -722       O  
ATOM    294  H   ASP A 226       8.904 -17.597   9.066  1.00 19.80           H  
ATOM    295  HA  ASP A 226       8.832 -16.525  11.522  1.00 18.55           H  
ATOM    296  HB2 ASP A 226      10.185 -18.409  10.954  1.00 20.33           H  
ATOM    297  HB3 ASP A 226      11.050 -17.453  10.025  1.00 20.33           H  
ATOM    298  N   ILE A 227       9.438 -14.196  11.221  1.00 19.49           N  
ANISOU  298  N   ILE A 227     2619   1972   2816    604   -194   -685       N  
ATOM    299  CA  ILE A 227       9.754 -12.794  10.963  1.00 15.00           C  
ANISOU  299  CA  ILE A 227     2021   1511   2168    580    -91   -661       C  
ATOM    300  C   ILE A 227      11.257 -12.587  10.810  1.00 15.22           C  
ANISOU  300  C   ILE A 227     1917   1628   2239    630    -12   -724       C  
ATOM    301  O   ILE A 227      11.684 -11.716  10.047  1.00 15.52           O  
ANISOU  301  O   ILE A 227     1916   1804   2177    599    119   -731       O  
ATOM    302  CB  ILE A 227       9.184 -11.882  12.061  1.00 12.43           C  
ANISOU  302  CB  ILE A 227     1736   1148   1841    474   -115   -501       C  
ATOM    303  CG1 ILE A 227       9.229 -10.426  11.609  1.00 11.29           C  
ANISOU  303  CG1 ILE A 227     1573   1130   1585    402      2   -429       C  
ATOM    304  CG2 ILE A 227       9.914 -12.096  13.368  1.00 15.96           C  
ANISOU  304  CG2 ILE A 227     2140   1518   2405    478   -186   -456       C  
ATOM    305  CD1 ILE A 227       8.527  -9.476  12.590  1.00 15.28           C  
ANISOU  305  CD1 ILE A 227     2119   1594   2093    297    -13   -290       C  
ATOM    306  H   ILE A 227       9.030 -14.334  11.965  1.00 23.43           H  
ATOM    307  HA  ILE A 227       9.326 -12.552  10.127  1.00 18.04           H  
ATOM    308  HB  ILE A 227       8.254 -12.116  12.212  1.00 14.96           H  
ATOM    309 HG12 ILE A 227      10.155 -10.147  11.533  1.00 13.58           H  
ATOM    310 HG13 ILE A 227       8.787 -10.348  10.749  1.00 13.58           H  
ATOM    311 HG21 ILE A 227       9.514 -11.531  14.049  1.00 19.18           H  
ATOM    312 HG22 ILE A 227       9.837 -13.028  13.624  1.00 19.18           H  
ATOM    313 HG23 ILE A 227      10.848 -11.861  13.250  1.00 19.18           H  
ATOM    314 HD11 ILE A 227       8.567  -8.573  12.238  1.00 18.37           H  
ATOM    315 HD12 ILE A 227       7.603  -9.752  12.690  1.00 18.37           H  
ATOM    316 HD13 ILE A 227       8.979  -9.517  13.447  1.00 18.37           H  
ATOM    317  N   VAL A 228      12.078 -13.387  11.497  1.00 16.32           N  
ANISOU  317  N   VAL A 228     1987   1690   2526    697    -90   -764       N  
ATOM    318  CA  VAL A 228      13.536 -13.270  11.351  1.00 16.70           C  
ANISOU  318  CA  VAL A 228     1886   1817   2643    747    -23   -839       C  
ATOM    319  C   VAL A 228      13.953 -13.646   9.932  1.00 19.95           C  
ANISOU  319  C   VAL A 228     2259   2332   2991    784     91   -972       C  
ATOM    320  O   VAL A 228      14.720 -12.935   9.279  1.00 20.47           O  
ANISOU  320  O   VAL A 228     2242   2531   3005    771    235  -1022       O  
ATOM    321  CB  VAL A 228      14.263 -14.145  12.387  1.00 17.86           C  
ANISOU  321  CB  VAL A 228     1983   1860   2946    785   -159   -819       C  
ATOM    322  CG1 VAL A 228      15.773 -14.149  12.114  1.00 22.14           C  
ANISOU  322  CG1 VAL A 228     2359   2479   3575    839    -99   -915       C  
ATOM    323  CG2 VAL A 228      13.970 -13.683  13.786  1.00 22.98           C  
ANISOU  323  CG2 VAL A 228     2678   2425   3628    728   -260   -680       C  
ATOM    324  H   VAL A 228      11.822 -13.997  12.047  1.00 19.62           H  
ATOM    325  HA  VAL A 228      13.782 -12.345  11.513  1.00 20.08           H  
ATOM    326  HB  VAL A 228      13.939 -15.056  12.309  1.00 21.47           H  
ATOM    327 HG11 VAL A 228      16.216 -14.679  12.795  1.00 26.60           H  
ATOM    328 HG12 VAL A 228      15.935 -14.532  11.238  1.00 26.60           H  
ATOM    329 HG13 VAL A 228      16.101 -13.236  12.142  1.00 26.60           H  
ATOM    330 HG21 VAL A 228      14.442 -14.253  14.413  1.00 27.61           H  
ATOM    331 HG22 VAL A 228      14.267 -12.765  13.885  1.00 27.61           H  
ATOM    332 HG23 VAL A 228      13.014 -13.740  13.944  1.00 27.61           H  
ATOM    333  N   GLU A 229      13.435 -14.766   9.422  1.00 18.25           N  
ANISOU  333  N   GLU A 229     2108   2057   2769    812     37  -1026       N  
ATOM    334  CA  GLU A 229      13.777 -15.170   8.066  1.00 21.47           C  
ANISOU  334  CA  GLU A 229     2495   2552   3111    840    141  -1156       C  
ATOM    335  C   GLU A 229      13.235 -14.185   7.044  1.00 19.49           C  
ANISOU  335  C   GLU A 229     2312   2431   2660    782    268  -1157       C  
ATOM    336  O   GLU A 229      13.909 -13.901   6.039  1.00 22.83           O  
ANISOU  336  O   GLU A 229     2697   2980   2999    772    409  -1232       O  
ATOM    337  CB  GLU A 229      13.266 -16.580   7.807  1.00 23.25           C  
ANISOU  337  CB  GLU A 229     2776   2679   3381    877     48  -1210       C  
ATOM    338  CG  GLU A 229      13.894 -17.633   8.723  1.00 27.60           C  
ANISOU  338  CG  GLU A 229     3263   3108   4115    932    -76  -1211       C  
ATOM    339  CD  GLU A 229      15.416 -17.599   8.714  1.00 41.76           C  
ANISOU  339  CD  GLU A 229     4903   4953   6011    985    -23  -1291       C  
ATOM    340  OE1 GLU A 229      16.016 -17.510   9.808  1.00 44.12           O  
ANISOU  340  OE1 GLU A 229     5141   5197   6424    997   -107  -1230       O  
ATOM    341  OE2 GLU A 229      16.012 -17.650   7.615  1.00 42.08           O  
ANISOU  341  OE2 GLU A 229     4886   5090   6014   1008    101  -1415       O  
ATOM    342  H   GLU A 229      12.896 -15.295   9.833  1.00 21.91           H  
ATOM    343  HA  GLU A 229      14.742 -15.184   7.969  1.00 25.80           H  
ATOM    344  HB2 GLU A 229      12.306 -16.596   7.949  1.00 27.94           H  
ATOM    345  HB3 GLU A 229      13.469 -16.823   6.890  1.00 27.94           H  
ATOM    346  HG2 GLU A 229      13.597 -17.477   9.633  1.00 33.15           H  
ATOM    347  HG3 GLU A 229      13.613 -18.514   8.430  1.00 33.15           H  
ATOM    348  N   GLU A 230      12.016 -13.675   7.261  1.00 17.98           N  
ANISOU  348  N   GLU A 230     2233   2212   2385    733    217  -1068       N  
ATOM    349  CA  GLU A 230      11.490 -12.645   6.372  1.00 17.75           C  
ANISOU  349  CA  GLU A 230     2278   2310   2156    673    316  -1048       C  
ATOM    350  C   GLU A 230      12.397 -11.425   6.363  1.00 20.35           C  
ANISOU  350  C   GLU A 230     2530   2764   2438    619    456   -997       C  
ATOM    351  O   GLU A 230      12.683 -10.858   5.308  1.00 20.31           O  
ANISOU  351  O   GLU A 230     2542   2896   2280    577    592  -1026       O  
ATOM    352  CB  GLU A 230      10.067 -12.256   6.783  1.00 18.29           C  
ANISOU  352  CB  GLU A 230     2465   2308   2177    614    214   -918       C  
ATOM    353  CG  GLU A 230       9.004 -13.288   6.474  1.00 16.29           C  
ANISOU  353  CG  GLU A 230     2299   1962   1928    641    103   -974       C  
ATOM    354  CD  GLU A 230       8.839 -13.490   4.973  1.00 17.67           C  
ANISOU  354  CD  GLU A 230     2528   2240   1948    635    164  -1064       C  
ATOM    355  OE1 GLU A 230       8.429 -12.517   4.278  1.00 19.95           O  
ANISOU  355  OE1 GLU A 230     2890   2634   2056    587    214  -1024       O  
ATOM    356  OE2 GLU A 230       9.121 -14.582   4.475  1.00 19.73           O  
ANISOU  356  OE2 GLU A 230     2768   2476   2254    672    160  -1164       O  
ATOM    357  H   GLU A 230      11.490 -13.904   7.901  1.00 21.49           H  
ATOM    358  HA  GLU A 230      11.446 -13.002   5.471  1.00 21.12           H  
ATOM    359  HB2 GLU A 230      10.056 -12.104   7.741  1.00 21.99           H  
ATOM    360  HB3 GLU A 230       9.825 -11.441   6.315  1.00 21.99           H  
ATOM    361  HG2 GLU A 230       9.257 -14.137   6.870  1.00 19.48           H  
ATOM    362  HG3 GLU A 230       8.155 -12.992   6.838  1.00 19.48           H  
ATOM    363  N   ALA A 231      12.840 -10.985   7.537  1.00 16.94           N  
ANISOU  363  N   ALA A 231     2025   2282   2130    600    421   -902       N  
ATOM    364  CA  ALA A 231      13.680  -9.800   7.579  1.00 22.69           C  
ANISOU  364  CA  ALA A 231     2677   3117   2829    530    547   -840       C  
ATOM    365  C   ALA A 231      14.968 -10.025   6.807  1.00 21.87           C  
ANISOU  365  C   ALA A 231     2454   3119   2737    567    687   -987       C  
ATOM    366  O   ALA A 231      15.405  -9.148   6.055  1.00 26.63           O  
ANISOU  366  O   ALA A 231     3058   3841   3219    490    832   -955       O  
ATOM    367  CB  ALA A 231      13.966  -9.403   9.024  1.00 17.64           C  
ANISOU  367  CB  ALA A 231     1976   2398   2328    506    469   -734       C  
ATOM    368  H   ALA A 231      12.672 -11.345   8.300  1.00 20.15           H  
ATOM    369  HA  ALA A 231      13.206  -9.061   7.165  1.00 27.27           H  
ATOM    370  HB1 ALA A 231      14.525  -8.610   9.029  1.00 21.20           H  
ATOM    371  HB2 ALA A 231      13.127  -9.218   9.473  1.00 21.20           H  
ATOM    372  HB3 ALA A 231      14.425 -10.134   9.467  1.00 21.20           H  
ATOM    373  N   LYS A 232      15.576 -11.210   6.953  1.00 24.09           N  
ANISOU  373  N   LYS A 232     2663   3327   3163    657    618  -1088       N  
ATOM    374  CA  LYS A 232      16.836 -11.478   6.266  1.00 24.95           C  
ANISOU  374  CA  LYS A 232     2666   3508   3306    674    724  -1188       C  
ATOM    375  C   LYS A 232      16.658 -11.492   4.755  1.00 30.61           C  
ANISOU  375  C   LYS A 232     3470   4324   3836    641    848  -1247       C  
ATOM    376  O   LYS A 232      17.533 -11.027   4.020  1.00 39.76           O  
ANISOU  376  O   LYS A 232     4580   5590   4938    598    994  -1277       O  
ATOM    377  CB  LYS A 232      17.422 -12.810   6.739  1.00 27.36           C  
ANISOU  377  CB  LYS A 232     2885   3704   3808    776    608  -1282       C  
ATOM    378  CG  LYS A 232      17.825 -12.835   8.204  1.00 32.77           C  
ANISOU  378  CG  LYS A 232     3485   4292   4673    806    475  -1220       C  
ATOM    379  CD  LYS A 232      18.318 -14.229   8.582  1.00 37.57           C  
ANISOU  379  CD  LYS A 232     4037   4783   5454    900    343  -1299       C  
ATOM    380  CE  LYS A 232      18.810 -14.283  10.011  1.00 42.87           C  
ANISOU  380  CE  LYS A 232     4640   5359   6288    923    196  -1231       C  
ATOM    381  NZ  LYS A 232      19.226 -15.677  10.391  1.00 44.93           N  
ANISOU  381  NZ  LYS A 232     4869   5498   6706   1007     51  -1290       N  
ATOM    382  H   LYS A 232      15.283 -11.860   7.434  1.00 28.94           H  
ATOM    383  HA  LYS A 232      17.462 -10.771   6.490  1.00 29.97           H  
ATOM    384  HB2 LYS A 232      16.758 -13.505   6.606  1.00 32.87           H  
ATOM    385  HB3 LYS A 232      18.214 -13.003   6.214  1.00 32.87           H  
ATOM    386  HG2 LYS A 232      18.541 -12.199   8.358  1.00 39.36           H  
ATOM    387  HG3 LYS A 232      17.060 -12.615   8.758  1.00 39.36           H  
ATOM    388  HD2 LYS A 232      17.590 -14.863   8.488  1.00 45.11           H  
ATOM    389  HD3 LYS A 232      19.052 -14.478   7.999  1.00 45.11           H  
ATOM    390  HE2 LYS A 232      19.577 -13.697  10.111  1.00 51.48           H  
ATOM    391  HE3 LYS A 232      18.099 -14.003  10.608  1.00 51.48           H  
ATOM    392  HZ1 LYS A 232      19.511 -15.690  11.234  1.00 53.96           H  
ATOM    393  HZ2 LYS A 232      18.536 -16.233  10.310  1.00 53.96           H  
ATOM    394  HZ3 LYS A 232      19.884 -15.953   9.859  1.00 53.96           H  
ATOM    395  N   LYS A 233      15.540 -12.030   4.272  1.00 25.73           N  
ANISOU  395  N   LYS A 233     2985   3668   3122    655    785  -1264       N  
ATOM    396  CA  LYS A 233      15.300 -12.167   2.846  1.00 32.49           C  
ANISOU  396  CA  LYS A 233     3941   4607   3798    628    875  -1325       C  
ATOM    397  C   LYS A 233      14.694 -10.922   2.219  1.00 34.64           C  
ANISOU  397  C   LYS A 233     4337   4979   3844    525    951  -1211       C  
ATOM    398  O   LYS A 233      14.914 -10.672   1.027  1.00 34.46           O  
ANISOU  398  O   LYS A 233     4380   5054   3659    481   1064  -1234       O  
ATOM    399  CB  LYS A 233      14.380 -13.361   2.579  1.00 35.32           C  
ANISOU  399  CB  LYS A 233     4385   4872   4161    683    756  -1397       C  
ATOM    400  H   LYS A 233      14.898 -12.327   4.761  1.00 30.91           H  
ATOM    401  HA  LYS A 233      16.150 -12.334   2.408  1.00 39.03           H  
ATOM    402  N   VAL A 234      13.940 -10.137   2.987  1.00 30.84           N  
ANISOU  402  N   VAL A 234     3897   4471   3349    484    887  -1083       N  
ATOM    403  CA  VAL A 234      13.272  -8.963   2.445  1.00 31.38           C  
ANISOU  403  CA  VAL A 234     4091   4616   3214    386    931   -954       C  
ATOM    404  C   VAL A 234      14.123  -7.707   2.596  1.00 33.05           C  
ANISOU  404  C   VAL A 234     4242   4899   3418    306   1050   -844       C  
ATOM    405  O   VAL A 234      14.041  -6.807   1.755  1.00 37.73           O  
ANISOU  405  O   VAL A 234     4926   5569   3842    229   1122   -750       O  
ATOM    406  CB  VAL A 234      11.908  -8.783   3.134  1.00 39.00           C  
ANISOU  406  CB  VAL A 234     5136   5514   4169    382    788   -874       C  
ATOM    407  CG1 VAL A 234      11.255  -7.471   2.710  1.00 35.92           C  
ANISOU  407  CG1 VAL A 234     4865   5173   3609    275    806   -700       C  
ATOM    408  CG2 VAL A 234      10.993  -9.958   2.826  1.00 35.90           C  
ANISOU  408  CG2 VAL A 234     4819   5044   3777    452    657   -966       C  
ATOM    409  H   VAL A 234      13.801 -10.265   3.826  1.00 37.04           H  
ATOM    410  HA  VAL A 234      13.121  -9.097   1.497  1.00 37.69           H  
ATOM    411  HB  VAL A 234      12.049  -8.751   4.093  1.00 46.84           H  
ATOM    412 HG11 VAL A 234      10.386  -7.398   3.136  1.00 43.13           H  
ATOM    413 HG12 VAL A 234      11.821  -6.733   2.986  1.00 43.13           H  
ATOM    414 HG13 VAL A 234      11.152  -7.466   1.746  1.00 43.13           H  
ATOM    415 HG21 VAL A 234      10.142  -9.820   3.269  1.00 43.12           H  
ATOM    416 HG22 VAL A 234      10.862 -10.013   1.866  1.00 43.12           H  
ATOM    417 HG23 VAL A 234      11.407 -10.773   3.150  1.00 43.12           H  
ATOM    418  N   LYS A 235      14.931  -7.621   3.652  1.00 25.66           N  
ANISOU  418  N   LYS A 235     3156   3928   2666    324   1053   -845       N  
ATOM    419  CA  LYS A 235      15.700  -6.415   3.961  1.00 38.93           C  
ANISOU  419  CA  LYS A 235     4770   5655   4368    243   1140   -736       C  
ATOM    420  C   LYS A 235      14.747  -5.218   4.025  1.00 31.98           C  
ANISOU  420  C   LYS A 235     4008   4773   3368    150   1118   -557       C  
ATOM    421  O   LYS A 235      14.957  -4.224   3.313  1.00 33.31           O  
ANISOU  421  O   LYS A 235     4227   5005   3423     75   1192   -457       O  
ATOM    422  CB  LYS A 235      16.797  -6.185   2.942  1.00 30.19           C  
ANISOU  422  CB  LYS A 235     3626   4645   3201    214   1283   -777       C  
ATOM    423  H   LYS A 235      15.052  -8.261   4.214  1.00 30.83           H  
ATOM    424  HA  LYS A 235      16.148  -6.508   4.817  1.00 46.75           H  
ATOM    425  N   PRO A 236      13.700  -5.275   4.834  1.00 23.74           N  
ANISOU  425  N   PRO A 236     3011   3651   2356    152   1012   -512       N  
ATOM    426  CA  PRO A 236      12.700  -4.203   4.835  1.00 22.91           C  
ANISOU  426  CA  PRO A 236     3031   3519   2157     68    971   -337       C  
ATOM    427  C   PRO A 236      13.271  -2.914   5.400  1.00 18.88           C  
ANISOU  427  C   PRO A 236     2455   3007   1711    -11   1013   -204       C  
ATOM    428  O   PRO A 236      14.268  -2.891   6.132  1.00 21.85           O  
ANISOU  428  O   PRO A 236     2695   3381   2226     -3   1046   -237       O  
ATOM    429  CB  PRO A 236      11.589  -4.751   5.733  1.00 16.69           C  
ANISOU  429  CB  PRO A 236     2276   2588   1477    121    782   -303       C  
ATOM    430  CG  PRO A 236      12.277  -5.693   6.646  1.00 18.80           C  
ANISOU  430  CG  PRO A 236     2418   2801   1924    198    742   -405       C  
ATOM    431  CD  PRO A 236      13.395  -6.303   5.843  1.00 18.98           C  
ANISOU  431  CD  PRO A 236     2360   2926   1924    244    863   -567       C  
ATOM    432  HA  PRO A 236      12.354  -4.048   3.942  1.00 27.53           H  
ATOM    433  HB2 PRO A 236      11.174  -4.027   6.227  1.00 20.06           H  
ATOM    434  HB3 PRO A 236      10.925  -5.210   5.195  1.00 20.06           H  
ATOM    435  HG2 PRO A 236      12.627  -5.211   7.411  1.00 22.59           H  
ATOM    436  HG3 PRO A 236      11.655  -6.376   6.941  1.00 22.59           H  
ATOM    437  HD2 PRO A 236      14.168  -6.474   6.404  1.00 22.81           H  
ATOM    438  HD3 PRO A 236      13.105  -7.125   5.418  1.00 22.81           H  
ATOM    439  N   THR A 237      12.647  -1.810   4.998  1.00 18.36           N  
ANISOU  439  N   THR A 237     2482   2938   1555    -81    986    -53       N  
ATOM    440  CA  THR A 237      12.963  -0.533   5.630  1.00 16.38           C  
ANISOU  440  CA  THR A 237     2174   2659   1390   -148    979     74       C  
ATOM    441  C   THR A 237      12.730  -0.583   7.134  1.00 14.64           C  
ANISOU  441  C   THR A 237     1896   2336   1330   -149    909     88       C  
ATOM    442  O   THR A 237      13.543  -0.057   7.902  1.00 16.04           O  
ANISOU  442  O   THR A 237     1968   2508   1616   -175    917    106       O  
ATOM    443  CB  THR A 237      12.138   0.587   4.999  1.00 20.99           C  
ANISOU  443  CB  THR A 237     2861   3230   1885   -204    928    220       C  
ATOM    444  OG1 THR A 237      12.427   0.645   3.592  1.00 24.23           O  
ANISOU  444  OG1 THR A 237     3336   3733   2136   -208   1000    214       O  
ATOM    445  CG2 THR A 237      12.504   1.927   5.614  1.00 21.85           C  
ANISOU  445  CG2 THR A 237     2900   3306   2096   -261    912    329       C  
ATOM    446  H   THR A 237      12.052  -1.773   4.379  1.00 22.07           H  
ATOM    447  HA  THR A 237      13.901  -0.339   5.477  1.00 19.48           H  
ATOM    448  HB  THR A 237      11.195   0.417   5.147  1.00 25.23           H  
ATOM    449  HG1 THR A 237      11.866   0.189   3.164  1.00 29.11           H  
ATOM    450 HG21 THR A 237      11.987   2.635   5.199  1.00 26.26           H  
ATOM    451 HG22 THR A 237      12.316   1.917   6.566  1.00 26.26           H  
ATOM    452 HG23 THR A 237      13.448   2.107   5.481  1.00 26.26           H  
ATOM    453  N   VAL A 238      11.611  -1.168   7.577  1.00 13.47           N  
ANISOU  453  N   VAL A 238     1828   2097   1194   -119    837     88       N  
ATOM    454  CA  VAL A 238      11.259  -1.231   8.995  1.00 12.05           C  
ANISOU  454  CA  VAL A 238     1606   1806   1168   -114    744    116       C  
ATOM    455  C   VAL A 238      10.823  -2.648   9.342  1.00 13.10           C  
ANISOU  455  C   VAL A 238     1740   1878   1359    -20    627     21       C  
ATOM    456  O   VAL A 238       9.915  -3.213   8.706  1.00 12.33           O  
ANISOU  456  O   VAL A 238     1731   1762   1193     18    562     -2       O  
ATOM    457  CB  VAL A 238      10.133  -0.242   9.359  1.00 12.75           C  
ANISOU  457  CB  VAL A 238     1763   1810   1272   -173    668    244       C  
ATOM    458  CG1 VAL A 238       9.810  -0.319  10.847  1.00 11.73           C  
ANISOU  458  CG1 VAL A 238     1594   1576   1286   -182    594    257       C  
ATOM    459  CG2 VAL A 238      10.521   1.165   8.948  1.00 16.76           C  
ANISOU  459  CG2 VAL A 238     2236   2371   1762   -237    662    319       C  
ATOM    460  H   VAL A 238      11.032  -1.542   7.063  1.00 15.99           H  
ATOM    461  HA  VAL A 238      12.051  -1.014   9.511  1.00 14.50           H  
ATOM    462  HB  VAL A 238       9.327  -0.483   8.877  1.00 15.34           H  
ATOM    463 HG11 VAL A 238       9.108   0.318  11.051  1.00 14.11           H  
ATOM    464 HG12 VAL A 238       9.513  -1.218  11.060  1.00 14.11           H  
ATOM    465 HG13 VAL A 238      10.609  -0.106  11.355  1.00 14.11           H  
ATOM    466 HG21 VAL A 238       9.808   1.774   9.194  1.00 20.15           H  
ATOM    467 HG22 VAL A 238      11.340   1.413   9.405  1.00 20.15           H  
ATOM    468 HG23 VAL A 238      10.659   1.187   7.988  1.00 20.15           H  
ATOM    469  N   VAL A 239      11.411  -3.195  10.412  1.00 11.91           N  
ANISOU  469  N   VAL A 239     1501   1684   1341     10    585    -26       N  
ATOM    470  CA  VAL A 239      10.879  -4.382  11.063  1.00 10.54           C  
ANISOU  470  CA  VAL A 239     1346   1414   1246     76    456    -78       C  
ATOM    471  C   VAL A 239      10.397  -3.978  12.445  1.00  9.61           C  
ANISOU  471  C   VAL A 239     1237   1198   1217     19    385      5       C  
ATOM    472  O   VAL A 239      11.048  -3.178  13.131  1.00 10.40           O  
ANISOU  472  O   VAL A 239     1276   1312   1364    -37    426     50       O  
ATOM    473  CB  VAL A 239      11.921  -5.507  11.147  1.00 11.83           C  
ANISOU  473  CB  VAL A 239     1419   1591   1486    164    443   -204       C  
ATOM    474  CG1 VAL A 239      13.113  -5.095  12.037  1.00 15.19           C  
ANISOU  474  CG1 VAL A 239     1722   2033   2017    143    468   -199       C  
ATOM    475  CG2 VAL A 239      11.278  -6.796  11.650  1.00 11.90           C  
ANISOU  475  CG2 VAL A 239     1473   1485   1563    231    304   -250       C  
ATOM    476  H   VAL A 239      12.127  -2.888  10.776  1.00 14.33           H  
ATOM    477  HA  VAL A 239      10.126  -4.720  10.554  1.00 12.47           H  
ATOM    478  HB  VAL A 239      12.269  -5.674  10.258  1.00 14.23           H  
ATOM    479 HG11 VAL A 239      13.759  -5.818  12.054  1.00 18.26           H  
ATOM    480 HG12 VAL A 239      13.521  -4.296  11.668  1.00 18.26           H  
ATOM    481 HG13 VAL A 239      12.791  -4.918  12.934  1.00 18.26           H  
ATOM    482 HG21 VAL A 239      11.953  -7.491  11.689  1.00 14.31           H  
ATOM    483 HG22 VAL A 239      10.910  -6.641  12.534  1.00 14.31           H  
ATOM    484 HG23 VAL A 239      10.571  -7.055  11.038  1.00 14.31           H  
ATOM    485  N   VAL A 240       9.233  -4.443  12.804  1.00  8.55           N  
ANISOU  485  N   VAL A 240     1178    970   1098     22    293     21       N  
ATOM    486  CA  VAL A 240       8.645  -4.172  14.123  1.00  7.52           C  
ANISOU  486  CA  VAL A 240     1070    745   1042    -42    236     84       C  
ATOM    487  C   VAL A 240       9.059  -5.252  15.115  1.00  7.94           C  
ANISOU  487  C   VAL A 240     1109    732   1176     -7    148     41       C  
ATOM    488  O   VAL A 240       8.959  -6.443  14.836  1.00  8.18           O  
ANISOU  488  O   VAL A 240     1161    727   1221     67     85    -28       O  
ATOM    489  CB  VAL A 240       7.102  -4.065  14.046  1.00  6.87           C  
ANISOU  489  CB  VAL A 240     1071    591    948    -73    193    119       C  
ATOM    490  CG1 VAL A 240       6.511  -3.969  15.447  1.00  9.28           C  
ANISOU  490  CG1 VAL A 240     1397    798   1330   -144    151    157       C  
ATOM    491  CG2 VAL A 240       6.700  -2.929  13.126  1.00  9.08           C  
ANISOU  491  CG2 VAL A 240     1371    920   1159   -105    252    177       C  
ATOM    492  H   VAL A 240       8.736  -4.933  12.301  1.00 10.08           H  
ATOM    493  HA  VAL A 240       9.000  -3.326  14.437  1.00  8.84           H  
ATOM    494  HB  VAL A 240       6.724  -4.867  13.654  1.00  8.07           H  
ATOM    495 HG11 VAL A 240       5.549  -3.865  15.378  1.00 11.17           H  
ATOM    496 HG12 VAL A 240       6.722  -4.780  15.935  1.00 11.17           H  
ATOM    497 HG13 VAL A 240       6.895  -3.201  15.900  1.00 11.17           H  
ATOM    498 HG21 VAL A 240       5.732  -2.873  13.097  1.00 10.93           H  
ATOM    499 HG22 VAL A 240       7.069  -2.099  13.469  1.00 10.93           H  
ATOM    500 HG23 VAL A 240       7.048  -3.103  12.238  1.00 10.93           H  
ATOM    501  N   ASN A 241       9.523  -4.818  16.290  1.00  8.68           N  
ANISOU  501  N   ASN A 241     1174    802   1323    -64    135     84       N  
ATOM    502  CA  ASN A 241       9.731  -5.692  17.424  1.00  7.99           C  
ANISOU  502  CA  ASN A 241     1106    633   1299    -56     31     76       C  
ATOM    503  C   ASN A 241       8.566  -5.550  18.399  1.00  8.20           C  
ANISOU  503  C   ASN A 241     1224    566   1324   -148     -2    134       C  
ATOM    504  O   ASN A 241       8.154  -4.433  18.713  1.00  8.52           O  
ANISOU  504  O   ASN A 241     1271    687   1281   -210     48    151       O  
ATOM    505  CB  ASN A 241      11.045  -5.385  18.107  1.00  8.43           C  
ANISOU  505  CB  ASN A 241     1074    725   1403    -62     21     77       C  
ATOM    506  CG  ASN A 241      11.286  -6.293  19.278  1.00  9.47           C  
ANISOU  506  CG  ASN A 241     1242    768   1590    -53   -113     82       C  
ATOM    507  OD1 ASN A 241      10.875  -7.456  19.272  1.00 11.00           O  
ANISOU  507  OD1 ASN A 241     1497    882   1801      0   -196     56       O  
ATOM    508  ND2 ASN A 241      11.974  -5.756  20.288  1.00 10.81           N  
ANISOU  508  ND2 ASN A 241     1379    944   1783   -110   -142    117       N  
ATOM    509  H   ASN A 241       9.727  -3.998  16.449  1.00 10.45           H  
ATOM    510  HA  ASN A 241       9.760  -6.614  17.125  1.00  9.63           H  
ATOM    511  HB2 ASN A 241      11.771  -5.506  17.474  1.00 10.15           H  
ATOM    512  HB3 ASN A 241      11.034  -4.470  18.428  1.00 10.15           H  
ATOM    513 HD21 ASN A 241      12.145  -6.224  20.989  1.00 13.01           H  
ATOM    514 HD22 ASN A 241      12.246  -4.941  20.238  1.00 13.01           H  
ATOM    515  N   ALA A 242       8.055  -6.687  18.861  1.00  9.32           N  
ANISOU  515  N   ALA A 242     1417    671   1454   -117    -64    103       N  
ATOM    516  CA  ALA A 242       7.083  -6.735  19.949  1.00 10.71           C  
ANISOU  516  CA  ALA A 242     1588    894   1587   -151    -22    103       C  
ATOM    517  C   ALA A 242       7.903  -6.654  21.219  1.00  9.88           C  
ANISOU  517  C   ALA A 242     1486    791   1478   -180    -63    126       C  
ATOM    518  O   ALA A 242       8.446  -7.658  21.665  1.00 11.92           O  
ANISOU  518  O   ALA A 242     1779    997   1755   -163   -168    133       O  
ATOM    519  CB  ALA A 242       6.268  -8.008  19.884  1.00 10.40           C  
ANISOU  519  CB  ALA A 242     1578    826   1548   -125    -61     78       C  
ATOM    520  H   ALA A 242       8.260  -7.463  18.553  1.00 11.22           H  
ATOM    521  HA  ALA A 242       6.457  -5.995  19.902  1.00 12.88           H  
ATOM    522  HB1 ALA A 242       5.629  -8.011  20.614  1.00 12.52           H  
ATOM    523  HB2 ALA A 242       5.800  -8.040  19.035  1.00 12.52           H  
ATOM    524  HB3 ALA A 242       6.864  -8.769  19.963  1.00 12.52           H  
ATOM    525  N   ALA A 243       8.038  -5.461  21.789  1.00  9.69           N  
ANISOU  525  N   ALA A 243      987   1563   1132   -296     75    216       N  
ATOM    526  CA  ALA A 243       8.953  -5.176  22.878  1.00 10.46           C  
ANISOU  526  CA  ALA A 243     1074   1733   1166   -332     62    203       C  
ATOM    527  C   ALA A 243       8.226  -5.064  24.207  1.00 10.36           C  
ANISOU  527  C   ALA A 243     1028   1908   1002   -397     79    273       C  
ATOM    528  O   ALA A 243       6.991  -5.016  24.280  1.00 10.64           O  
ANISOU  528  O   ALA A 243     1034   2026    983   -404    131    316       O  
ATOM    529  CB  ALA A 243       9.722  -3.887  22.589  1.00  9.57           C  
ANISOU  529  CB  ALA A 243      998   1591   1047   -291    152     50       C  
ATOM    530  H   ALA A 243       7.587  -4.770  21.548  1.00 11.67           H  
ATOM    531  HA  ALA A 243       9.581  -5.912  22.952  1.00 12.58           H  
ATOM    532  HB1 ALA A 243      10.331  -3.711  23.324  1.00 11.52           H  
ATOM    533  HB2 ALA A 243      10.221  -3.994  21.765  1.00 11.52           H  
ATOM    534  HB3 ALA A 243       9.091  -3.155  22.501  1.00 11.52           H  
ATOM    535  N   ASN A 244       9.020  -5.036  25.272  1.00 13.21           N  
ANISOU  535  N   ASN A 244     1378   2361   1281   -445     33    284       N  
ATOM    536  CA  ASN A 244       8.550  -4.576  26.570  1.00 12.90           C  
ANISOU  536  CA  ASN A 244     1320   2536   1045   -496     77    290       C  
ATOM    537  C   ASN A 244       9.150  -3.202  26.869  1.00 14.04           C  
ANISOU  537  C   ASN A 244     1504   2710   1121   -470    152     89       C  
ATOM    538  O   ASN A 244       9.995  -2.694  26.145  1.00 11.69           O  
ANISOU  538  O   ASN A 244     1237   2270    934   -436    160    -17       O  
ATOM    539  CB  ASN A 244       8.851  -5.598  27.642  1.00 15.36           C  
ANISOU  539  CB  ASN A 244     1598   2961   1277   -587    -45    468       C  
ATOM    540  CG  ASN A 244      10.308  -5.942  27.720  1.00 19.33           C  
ANISOU  540  CG  ASN A 244     2100   3388   1856   -583   -170    471       C  
ATOM    541  OD1 ASN A 244      11.158  -5.048  27.686  1.00 23.06           O  
ANISOU  541  OD1 ASN A 244     2582   3854   2324   -559   -143    310       O  
ATOM    542  ND2 ASN A 244      10.616  -7.227  27.845  1.00 19.45           N  
ANISOU  542  ND2 ASN A 244     2095   3341   1953   -608   -312    656       N  
ATOM    543  H   ASN A 244       9.843  -5.283  25.265  1.00 15.89           H  
ATOM    544  HA  ASN A 244       7.586  -4.471  26.550  1.00 15.51           H  
ATOM    545  HB2 ASN A 244       8.580  -5.242  28.503  1.00 18.46           H  
ATOM    546  HB3 ASN A 244       8.360  -6.412  27.450  1.00 18.46           H  
ATOM    547 HD21 ASN A 244      11.440  -7.469  27.893  1.00 23.37           H  
ATOM    548 HD22 ASN A 244       9.992  -7.818  27.878  1.00 23.37           H  
ATOM    549  N   VAL A 245       8.741  -2.612  27.998  1.00 16.12           N  
ANISOU  549  N   VAL A 245     1764   3168   1192   -498    208     32       N  
ATOM    550  CA  VAL A 245       9.048  -1.197  28.182  1.00 14.07           C  
ANISOU  550  CA  VAL A 245     1560   2899    888   -466    293   -194       C  
ATOM    551  C   VAL A 245      10.520  -0.931  28.466  1.00 14.41           C  
ANISOU  551  C   VAL A 245     1618   2908    949   -524    206   -276       C  
ATOM    552  O   VAL A 245      10.984   0.172  28.188  1.00 14.80           O  
ANISOU  552  O   VAL A 245     1720   2854   1051   -512    260   -453       O  
ATOM    553  CB  VAL A 245       8.193  -0.587  29.315  1.00 18.91           C  
ANISOU  553  CB  VAL A 245     2172   3630   1384   -433    344   -260       C  
ATOM    554  CG1 VAL A 245       6.730  -0.531  28.888  1.00 19.02           C  
ANISOU  554  CG1 VAL A 245     2165   3606   1457   -340    423   -218       C  
ATOM    555  CG2 VAL A 245       8.364  -1.361  30.634  1.00 22.74           C  
ANISOU  555  CG2 VAL A 245     2607   4325   1707   -525    260   -147       C  
ATOM    556  H   VAL A 245       8.307  -2.991  28.636  1.00 19.38           H  
ATOM    557  HA  VAL A 245       8.825  -0.763  27.344  1.00 16.71           H  
ATOM    558  HB  VAL A 245       8.499   0.318  29.483  1.00 22.73           H  
ATOM    559 HG11 VAL A 245       6.205  -0.149  29.609  1.00 22.86           H  
ATOM    560 HG12 VAL A 245       6.653   0.021  28.094  1.00 22.86           H  
ATOM    561 HG13 VAL A 245       6.422  -1.431  28.696  1.00 22.86           H  
ATOM    562 HG21 VAL A 245       7.820  -0.941  31.319  1.00 27.32           H  
ATOM    563 HG22 VAL A 245       8.078  -2.278  30.501  1.00 27.32           H  
ATOM    564 HG23 VAL A 245       9.298  -1.340  30.894  1.00 27.32           H  
ATOM    565  N   TYR A 246      11.273  -1.915  28.953  1.00 14.87           N  
ANISOU  565  N   TYR A 246     1624   3038    987   -587     66   -142       N  
ATOM    566  CA  TYR A 246      12.709  -1.743  29.165  1.00 15.52           C  
ANISOU  566  CA  TYR A 246     1683   3106   1105   -636    -33   -208       C  
ATOM    567  C   TYR A 246      13.546  -2.349  28.054  1.00 17.33           C  
ANISOU  567  C   TYR A 246     1871   3153   1561   -599    -90   -146       C  
ATOM    568  O   TYR A 246      14.782  -2.421  28.162  1.00 17.09           O  
ANISOU  568  O   TYR A 246     1780   3126   1587   -631   -184   -169       O  
ATOM    569  CB  TYR A 246      13.121  -2.308  30.516  1.00 20.46           C  
ANISOU  569  CB  TYR A 246     2267   3960   1548   -714   -166   -115       C  
ATOM    570  CG  TYR A 246      12.765  -1.400  31.680  1.00 20.18           C  
ANISOU  570  CG  TYR A 246     2270   4111   1286   -755   -109   -260       C  
ATOM    571  CD1 TYR A 246      13.598  -0.343  32.038  1.00 23.08           C  
ANISOU  571  CD1 TYR A 246     2659   4463   1649   -790   -116   -468       C  
ATOM    572  CD2 TYR A 246      11.590  -1.585  32.388  1.00 19.72           C  
ANISOU  572  CD2 TYR A 246     2214   4160   1121   -730    -35   -186       C  
ATOM    573  CE1 TYR A 246      13.278   0.485  33.089  1.00 27.05           C  
ANISOU  573  CE1 TYR A 246     3201   5054   2022   -792    -63   -600       C  
ATOM    574  CE2 TYR A 246      11.265  -0.755  33.452  1.00 22.41           C  
ANISOU  574  CE2 TYR A 246     2578   4608   1328   -726     23   -324       C  
ATOM    575  CZ  TYR A 246      12.105   0.278  33.785  1.00 33.43           C  
ANISOU  575  CZ  TYR A 246     4013   5983   2706   -750      7   -534       C  
ATOM    576  OH  TYR A 246      11.786   1.111  34.849  1.00 32.86           O  
ANISOU  576  OH  TYR A 246     3979   6010   2497   -741     55   -683       O  
ATOM    577  H   TYR A 246      10.974  -2.692  29.169  1.00 17.67           H  
ATOM    578  HA  TYR A 246      12.900  -0.792  29.181  1.00 18.65           H  
ATOM    579  HB2 TYR A 246      12.671  -3.157  30.652  1.00 24.59           H  
ATOM    580  HB3 TYR A 246      14.082  -2.437  30.522  1.00 24.59           H  
ATOM    581  HD1 TYR A 246      14.382  -0.195  31.560  1.00 27.74           H  
ATOM    582  HD2 TYR A 246      11.012  -2.272  32.148  1.00 23.49           H  
ATOM    583  HE1 TYR A 246      13.848   1.180  33.328  1.00 32.49           H  
ATOM    584  HE2 TYR A 246      10.483  -0.898  33.936  1.00 26.92           H  
ATOM    585  HH  TYR A 246      11.051   0.881  35.184  1.00 39.47           H  
ATOM    586  N   LEU A 247      12.905  -2.712  26.955  1.00 12.87           N  
ANISOU  586  N   LEU A 247     1326   2444   1121   -529    -30    -91       N  
ATOM    587  CA  LEU A 247      13.585  -3.226  25.778  1.00 12.15           C  
ANISOU  587  CA  LEU A 247     1205   2187   1223   -478    -54    -69       C  
ATOM    588  C   LEU A 247      14.545  -4.353  26.131  1.00 13.89           C  
ANISOU  588  C   LEU A 247     1344   2430   1505   -479   -213     45       C  
ATOM    589  O   LEU A 247      15.707  -4.371  25.719  1.00 12.96           O  
ANISOU  589  O   LEU A 247     1159   2264   1500   -460   -250     -6       O  
ATOM    590  CB  LEU A 247      14.310  -2.116  25.018  1.00 13.23           C  
ANISOU  590  CB  LEU A 247     1356   2227   1443   -478     34   -227       C  
ATOM    591  CG  LEU A 247      13.433  -0.981  24.480  1.00 11.05           C  
ANISOU  591  CG  LEU A 247     1174   1873   1151   -452    180   -322       C  
ATOM    592  CD1 LEU A 247      14.299   0.036  23.727  1.00 12.79           C  
ANISOU  592  CD1 LEU A 247     1412   1978   1470   -479    252   -436       C  
ATOM    593  CD2 LEU A 247      12.318  -1.495  23.608  1.00 12.38           C  
ANISOU  593  CD2 LEU A 247     1373   1975   1356   -372    222   -237       C  
ATOM    594  H   LEU A 247      12.051  -2.669  26.864  1.00 15.27           H  
ATOM    595  HA  LEU A 247      12.906  -3.594  25.192  1.00 14.61           H  
ATOM    596  HB2 LEU A 247      14.960  -1.716  25.616  1.00 15.91           H  
ATOM    597  HB3 LEU A 247      14.760  -2.516  24.257  1.00 15.91           H  
ATOM    598  HG  LEU A 247      13.010  -0.534  25.230  1.00 13.29           H  
ATOM    599 HD11 LEU A 247      13.730   0.747  23.390  1.00 15.38           H  
ATOM    600 HD12 LEU A 247      14.958   0.402  24.337  1.00 15.38           H  
ATOM    601 HD13 LEU A 247      14.742  -0.411  22.989  1.00 15.38           H  
ATOM    602 HD21 LEU A 247      11.811  -0.742  23.267  1.00 14.89           H  
ATOM    603 HD22 LEU A 247      12.700  -1.998  22.871  1.00 14.89           H  
ATOM    604 HD23 LEU A 247      11.743  -2.069  24.137  1.00 14.89           H  
ATOM    605  N   LYS A 248      14.066  -5.293  26.966  1.00 15.05           N  
ANISOU  605  N   LYS A 248     1483   2662   1573   -503   -311    213       N  
ATOM    606  CA  LYS A 248      14.841  -6.488  27.289  1.00 15.51           C  
ANISOU  606  CA  LYS A 248     1477   2706   1710   -484   -482    361       C  
ATOM    607  C   LYS A 248      14.329  -7.621  26.409  1.00 15.28           C  
ANISOU  607  C   LYS A 248     1470   2492   1842   -419   -509    467       C  
ATOM    608  O   LYS A 248      13.187  -8.072  26.567  1.00 17.60           O  
ANISOU  608  O   LYS A 248     1810   2788   2088   -458   -498    580       O  
ATOM    609  CB  LYS A 248      14.724  -6.825  28.772  1.00 17.36           C  
ANISOU  609  CB  LYS A 248     1702   3139   1755   -563   -591    506       C  
ATOM    610  CG  LYS A 248      15.345  -5.812  29.686  1.00 18.36           C  
ANISOU  610  CG  LYS A 248     1806   3458   1713   -630   -598    381       C  
ATOM    611  CD  LYS A 248      16.864  -5.692  29.484  1.00 20.88           C  
ANISOU  611  CD  LYS A 248     2025   3752   2156   -605   -689    301       C  
ATOM    612  CE  LYS A 248      17.525  -4.825  30.532  1.00 28.18           C  
ANISOU  612  CE  LYS A 248     2922   4873   2911   -693   -735    189       C  
ATOM    613  NZ  LYS A 248      18.990  -4.703  30.269  1.00 32.04           N  
ANISOU  613  NZ  LYS A 248     3300   5323   3552   -668   -806    112       N  
ATOM    614  H   LYS A 248      13.299  -5.254  27.352  1.00 18.09           H  
ATOM    615  HA  LYS A 248      15.780  -6.343  27.094  1.00 18.64           H  
ATOM    616  HB2 LYS A 248      13.783  -6.889  29.002  1.00 20.87           H  
ATOM    617  HB3 LYS A 248      15.163  -7.674  28.933  1.00 20.87           H  
ATOM    618  HG2 LYS A 248      14.950  -4.943  29.513  1.00 22.07           H  
ATOM    619  HG3 LYS A 248      15.184  -6.073  30.606  1.00 22.07           H  
ATOM    620  HD2 LYS A 248      17.261  -6.575  29.532  1.00 25.09           H  
ATOM    621  HD3 LYS A 248      17.038  -5.297  28.615  1.00 25.09           H  
ATOM    622  HE2 LYS A 248      17.134  -3.937  30.512  1.00 33.85           H  
ATOM    623  HE3 LYS A 248      17.401  -5.223  31.407  1.00 33.85           H  
ATOM    624  HZ1 LYS A 248      19.384  -4.266  30.937  1.00 38.49           H  
ATOM    625  HZ2 LYS A 248      19.355  -5.512  30.198  1.00 38.49           H  
ATOM    626  HZ3 LYS A 248      19.128  -4.257  29.511  1.00 38.49           H  
ATOM    627  N   HIS A 249      15.153  -8.019  25.442  1.00 17.25           N  
ANISOU  627  N   HIS A 249     1681   2593   2282   -327   -532    407       N  
ATOM    628  CA  HIS A 249      14.754  -8.907  24.355  1.00 16.11           C  
ANISOU  628  CA  HIS A 249     1570   2254   2298   -253   -537    424       C  
ATOM    629  C   HIS A 249      15.189 -10.349  24.634  1.00 17.48           C  
ANISOU  629  C   HIS A 249     1716   2314   2610   -200   -718    577       C  
ATOM    630  O   HIS A 249      16.076 -10.907  23.974  1.00 24.90           O  
ANISOU  630  O   HIS A 249     2606   3130   3724    -85   -767    518       O  
ATOM    631  CB  HIS A 249      15.360  -8.419  23.035  1.00 14.87           C  
ANISOU  631  CB  HIS A 249     1394   2013   2242   -171   -430    240       C  
ATOM    632  CG  HIS A 249      15.248  -6.945  22.810  1.00 11.49           C  
ANISOU  632  CG  HIS A 249      988   1670   1708   -220   -275    109       C  
ATOM    633  ND1 HIS A 249      14.032  -6.294  22.775  1.00 12.34           N  
ANISOU  633  ND1 HIS A 249     1178   1805   1707   -264   -180    102       N  
ATOM    634  CD2 HIS A 249      16.198  -5.999  22.571  1.00 12.42           C  
ANISOU  634  CD2 HIS A 249     1056   1833   1832   -230   -202    -15       C  
ATOM    635  CE1 HIS A 249      14.245  -5.000  22.557  1.00 10.44           C  
ANISOU  635  CE1 HIS A 249      953   1598   1416   -287    -63    -20       C  
ATOM    636  NE2 HIS A 249      15.548  -4.800  22.406  1.00 11.06           N  
ANISOU  636  NE2 HIS A 249      958   1681   1563   -282    -72    -88       N  
ATOM    637  H   HIS A 249      15.977  -7.779  25.393  1.00 20.74           H  
ATOM    638  HA  HIS A 249      13.785  -8.888  24.302  1.00 19.37           H  
ATOM    639  HB2 HIS A 249      16.303  -8.646  23.025  1.00 17.88           H  
ATOM    640  HB3 HIS A 249      14.905  -8.863  22.302  1.00 17.88           H  
ATOM    641  HD2 HIS A 249      17.117  -6.139  22.527  1.00 14.94           H  
ATOM    642  HE1 HIS A 249      13.589  -4.343  22.517  1.00 12.56           H  
ATOM    643  N   GLY A 250      14.543 -10.960  25.614  1.00 27.56           N  
ANISOU  643  N   GLY A 250     3025   3633   3814   -281   -813    780       N  
ATOM    644  CA  GLY A 250      14.978 -12.255  26.110  1.00 25.34           C  
ANISOU  644  CA  GLY A 250     2729   3245   3654   -246  -1006    971       C  
ATOM    645  C   GLY A 250      14.158 -13.446  25.662  1.00 24.78           C  
ANISOU  645  C   GLY A 250     2735   2950   3733   -254  -1075   1090       C  
ATOM    646  O   GLY A 250      14.408 -14.560  26.135  1.00 28.36           O  
ANISOU  646  O   GLY A 250     3210   3287   4279   -248  -1179   1211       O  
ATOM    647  H   GLY A 250      13.848 -10.643  26.009  1.00 33.11           H  
ATOM    648  HA2 GLY A 250      15.891 -12.403  25.818  1.00 30.44           H  
ATOM    649  HA3 GLY A 250      14.955 -12.234  27.079  1.00 30.44           H  
ATOM    650  N   GLY A 251      13.202 -13.263  24.767  1.00 22.51           N  
ANISOU  650  N   GLY A 251     2500   2595   3456   -282   -962    990       N  
ATOM    651  CA  GLY A 251      12.408 -14.380  24.300  1.00 22.26           C  
ANISOU  651  CA  GLY A 251     2537   2347   3575   -314  -1039   1079       C  
ATOM    652  C   GLY A 251      11.330 -13.896  23.360  1.00 21.49           C  
ANISOU  652  C   GLY A 251     2475   2255   3436   -357   -905    947       C  
ATOM    653  O   GLY A 251      11.181 -12.695  23.108  1.00 16.55           O  
ANISOU  653  O   GLY A 251     1829   1790   2670   -351   -754    810       O  
ATOM    654  H   GLY A 251      12.994 -12.505  24.417  1.00 27.04           H  
ATOM    655  HA2 GLY A 251      12.974 -15.013  23.830  1.00 26.75           H  
ATOM    656  HA3 GLY A 251      11.991 -14.827  25.053  1.00 26.75           H  
ATOM    657  N   GLY A 252      10.569 -14.860  22.849  1.00 19.43           N  
ANISOU  657  N   GLY A 252     2268   1804   3310   -404   -979    998       N  
ATOM    658  CA  GLY A 252       9.538 -14.537  21.873  1.00 16.81           C  
ANISOU  658  CA  GLY A 252     1960   1474   2955   -442   -886    876       C  
ATOM    659  C   GLY A 252      10.155 -13.868  20.659  1.00 16.44           C  
ANISOU  659  C   GLY A 252     1917   1414   2917   -298   -785    612       C  
ATOM    660  O   GLY A 252      11.322 -14.095  20.320  1.00 17.99           O  
ANISOU  660  O   GLY A 252     2104   1519   3214   -167   -813    512       O  
ATOM    661  H   GLY A 252      10.629 -15.694  23.047  1.00 23.35           H  
ATOM    662  HA2 GLY A 252       9.086 -15.348  21.590  1.00 20.21           H  
ATOM    663  HA3 GLY A 252       8.887 -13.935  22.268  1.00 20.21           H  
ATOM    664  N   VAL A 253       9.352 -13.028  19.994  1.00 15.19           N  
ANISOU  664  N   VAL A 253     1761   1363   2648   -320   -663    512       N  
ATOM    665  CA  VAL A 253       9.817 -12.300  18.817  1.00 13.31           C  
ANISOU  665  CA  VAL A 253     1535   1139   2383   -205   -556    297       C  
ATOM    666  C   VAL A 253      11.052 -11.481  19.150  1.00 13.29           C  
ANISOU  666  C   VAL A 253     1487   1233   2330   -129   -480    239       C  
ATOM    667  O   VAL A 253      12.021 -11.454  18.381  1.00 14.32           O  
ANISOU  667  O   VAL A 253     1607   1315   2520    -20   -448     98       O  
ATOM    668  CB  VAL A 253       8.703 -11.394  18.256  1.00 13.57           C  
ANISOU  668  CB  VAL A 253     1575   1297   2286   -244   -448    251       C  
ATOM    669  CG1 VAL A 253       9.282 -10.350  17.290  1.00 15.93           C  
ANISOU  669  CG1 VAL A 253     1887   1653   2513   -141   -318     84       C  
ATOM    670  CG2 VAL A 253       7.647 -12.217  17.576  1.00 18.05           C  
ANISOU  670  CG2 VAL A 253     2171   1768   2920   -305   -532    253       C  
ATOM    671  H   VAL A 253       8.535 -12.864  20.206  1.00 18.27           H  
ATOM    672  HA  VAL A 253      10.051 -12.953  18.139  1.00 16.01           H  
ATOM    673  HB  VAL A 253       8.289 -10.919  18.994  1.00 16.32           H  
ATOM    674 HG11 VAL A 253       8.555  -9.831  16.912  1.00 19.15           H  
ATOM    675 HG12 VAL A 253       9.885  -9.768  17.778  1.00 19.15           H  
ATOM    676 HG13 VAL A 253       9.764 -10.808  16.583  1.00 19.15           H  
ATOM    677 HG21 VAL A 253       6.961 -11.626  17.229  1.00 21.70           H  
ATOM    678 HG22 VAL A 253       8.053 -12.715  16.850  1.00 21.70           H  
ATOM    679 HG23 VAL A 253       7.260 -12.830  18.221  1.00 21.70           H  
ATOM    680  N   ALA A 254      11.024 -10.764  20.281  1.00 12.28           N  
ANISOU  680  N   ALA A 254     1322   1262   2080   -195   -443    333       N  
ATOM    681  CA  ALA A 254      12.137  -9.872  20.599  1.00 12.48           C  
ANISOU  681  CA  ALA A 254     1301   1388   2053   -152   -377    261       C  
ATOM    682  C   ALA A 254      13.429 -10.651  20.752  1.00 13.22           C  
ANISOU  682  C   ALA A 254     1343   1398   2282    -72   -481    262       C  
ATOM    683  O   ALA A 254      14.484 -10.221  20.264  1.00 14.89           O  
ANISOU  683  O   ALA A 254     1502   1629   2525      4   -423    136       O  
ATOM    684  CB  ALA A 254      11.849  -9.093  21.873  1.00 13.56           C  
ANISOU  684  CB  ALA A 254     1418   1703   2032   -242   -345    343       C  
ATOM    685  H   ALA A 254      10.390 -10.778  20.862  1.00 14.77           H  
ATOM    686  HA  ALA A 254      12.238  -9.236  19.873  1.00 15.01           H  
ATOM    687  HB1 ALA A 254      12.598  -8.507  22.061  1.00 16.31           H  
ATOM    688  HB2 ALA A 254      11.042  -8.569  21.747  1.00 16.31           H  
ATOM    689  HB3 ALA A 254      11.726  -9.718  22.604  1.00 16.31           H  
ATOM    690  N   GLY A 255      13.375 -11.779  21.465  1.00 13.60           N  
ANISOU  690  N   GLY A 255     1394   1360   2414    -91   -635    418       N  
ATOM    691  CA  GLY A 255      14.579 -12.594  21.617  1.00 15.81           C  
ANISOU  691  CA  GLY A 255     1618   1541   2849     15   -756    432       C  
ATOM    692  C   GLY A 255      15.078 -13.134  20.293  1.00 17.50           C  
ANISOU  692  C   GLY A 255     1835   1591   3224    157   -742    257       C  
ATOM    693  O   GLY A 255      16.289 -13.195  20.054  1.00 18.71           O  
ANISOU  693  O   GLY A 255     1901   1743   3466    279   -744    163       O  
ATOM    694  H   GLY A 255      12.674 -12.086  21.859  1.00 16.30           H  
ATOM    695  HA2 GLY A 255      15.283 -12.057  22.014  1.00 19.01           H  
ATOM    696  HA3 GLY A 255      14.388 -13.345  22.202  1.00 19.01           H  
ATOM    697  N   ALA A 256      14.148 -13.527  19.413  1.00 16.29           N  
ANISOU  697  N   ALA A 256     1769   1318   3101    142   -726    199       N  
ATOM    698  CA  ALA A 256      14.517 -14.015  18.092  1.00 17.11           C  
ANISOU  698  CA  ALA A 256     1891   1289   3318    272   -704      0       C  
ATOM    699  C   ALA A 256      15.194 -12.925  17.268  1.00 15.63           C  
ANISOU  699  C   ALA A 256     1649   1258   3030    333   -526   -176       C  
ATOM    700  O   ALA A 256      16.259 -13.155  16.675  1.00 17.82           O  
ANISOU  700  O   ALA A 256     1859   1518   3395    470   -497   -314       O  
ATOM    701  CB  ALA A 256      13.272 -14.553  17.374  1.00 21.53           C  
ANISOU  701  CB  ALA A 256     2559   1725   3895    210   -735    -28       C  
ATOM    702  H   ALA A 256      13.301 -13.518  19.561  1.00 19.58           H  
ATOM    703  HA  ALA A 256      15.149 -14.744  18.189  1.00 20.56           H  
ATOM    704  HB1 ALA A 256      13.529 -14.878  16.497  1.00 25.87           H  
ATOM    705  HB2 ALA A 256      12.895 -15.278  17.898  1.00 25.87           H  
ATOM    706  HB3 ALA A 256      12.624 -13.837  17.286  1.00 25.87           H  
ATOM    707  N   LEU A 257      14.581 -11.735  17.202  1.00 14.01           N  
ANISOU  707  N   LEU A 257     1468   1207   2650    235   -401   -169       N  
ATOM    708  CA  LEU A 257      15.188 -10.632  16.466  1.00 13.70           C  
ANISOU  708  CA  LEU A 257     1390   1299   2517    264   -234   -295       C  
ATOM    709  C   LEU A 257      16.552 -10.295  17.039  1.00 16.60           C  
ANISOU  709  C   LEU A 257     1630   1755   2925    298   -220   -302       C  
ATOM    710  O   LEU A 257      17.525 -10.117  16.309  1.00 16.76           O  
ANISOU  710  O   LEU A 257     1571   1822   2974    379   -133   -427       O  
ATOM    711  CB  LEU A 257      14.286  -9.409  16.494  1.00 12.72           C  
ANISOU  711  CB  LEU A 257     1320   1287   2227    157   -130   -255       C  
ATOM    712  CG  LEU A 257      13.000  -9.503  15.653  1.00 13.02           C  
ANISOU  712  CG  LEU A 257     1454   1288   2205    136   -120   -273       C  
ATOM    713  CD1 LEU A 257      12.084  -8.316  15.936  1.00 13.89           C  
ANISOU  713  CD1 LEU A 257     1597   1505   2177     54    -39   -205       C  
ATOM    714  CD2 LEU A 257      13.288  -9.578  14.167  1.00 13.27           C  
ANISOU  714  CD2 LEU A 257     1512   1309   2219    223    -48   -431       C  
ATOM    715  H   LEU A 257      13.827 -11.548  17.571  1.00 16.85           H  
ATOM    716  HA  LEU A 257      15.294 -10.900  15.539  1.00 16.48           H  
ATOM    717  HB2 LEU A 257      14.018  -9.251  17.412  1.00 15.30           H  
ATOM    718  HB3 LEU A 257      14.792  -8.651  16.161  1.00 15.30           H  
ATOM    719  HG  LEU A 257      12.551 -10.325  15.905  1.00 15.66           H  
ATOM    720 HD11 LEU A 257      11.278  -8.405  15.404  1.00 16.71           H  
ATOM    721 HD12 LEU A 257      11.858  -8.310  16.880  1.00 16.71           H  
ATOM    722 HD13 LEU A 257      12.546  -7.497  15.701  1.00 16.71           H  
ATOM    723 HD21 LEU A 257      12.449  -9.654  13.686  1.00 15.95           H  
ATOM    724 HD22 LEU A 257      13.753  -8.771  13.894  1.00 15.95           H  
ATOM    725 HD23 LEU A 257      13.842 -10.355  13.990  1.00 15.95           H  
ATOM    726  N   ASN A 258      16.638 -10.188  18.355  1.00 13.69           N  
ANISOU  726  N   ASN A 258     1225   1435   2542    228   -304   -168       N  
ATOM    727  CA  ASN A 258      17.911  -9.841  18.975  1.00 13.74           C  
ANISOU  727  CA  ASN A 258     1097   1547   2577    244   -317   -172       C  
ATOM    728  C   ASN A 258      18.981 -10.887  18.678  1.00 16.29           C  
ANISOU  728  C   ASN A 258     1314   1792   3082    404   -397   -227       C  
ATOM    729  O   ASN A 258      20.137 -10.544  18.380  1.00 16.78           O  
ANISOU  729  O   ASN A 258     1238   1952   3186    461   -332   -323       O  
ATOM    730  CB  ASN A 258      17.728  -9.667  20.475  1.00 13.81           C  
ANISOU  730  CB  ASN A 258     1100   1636   2512    142   -419    -18       C  
ATOM    731  CG  ASN A 258      19.025  -9.313  21.169  1.00 14.85           C  
ANISOU  731  CG  ASN A 258     1084   1895   2661    143   -462    -24       C  
ATOM    732  OD1 ASN A 258      19.692  -8.365  20.798  1.00 15.78           O  
ANISOU  732  OD1 ASN A 258     1133   2111   2752    113   -348   -134       O  
ATOM    733  ND2 ASN A 258      19.412 -10.112  22.169  1.00 18.48           N  
ANISOU  733  ND2 ASN A 258     1490   2356   3175    171   -640    107       N  
ATOM    734  H   ASN A 258      15.988 -10.309  18.905  1.00 16.47           H  
ATOM    735  HA  ASN A 258      18.216  -8.995  18.611  1.00 16.52           H  
ATOM    736  HB2 ASN A 258      17.092  -8.953  20.638  1.00 16.40           H  
ATOM    737  HB3 ASN A 258      17.399 -10.497  20.854  1.00 16.40           H  
ATOM    738 HD21 ASN A 258      20.143  -9.948  22.592  1.00 22.21           H  
ATOM    739 HD22 ASN A 258      18.931 -10.789  22.390  1.00 22.21           H  
ATOM    740  N   LYS A 259      18.624 -12.167  18.799  1.00 17.68           N  
ANISOU  740  N   LYS A 259     1545   1790   3384    476   -542   -163       N  
ATOM    741  CA  LYS A 259      19.582 -13.234  18.543  1.00 21.61           C  
ANISOU  741  CA  LYS A 259     1962   2177   4072    652   -628   -221       C  
ATOM    742  C   LYS A 259      20.124 -13.153  17.124  1.00 20.66           C  
ANISOU  742  C   LYS A 259     1825   2091   3932    740   -464   -438       C  
ATOM    743  O   LYS A 259      21.318 -13.401  16.895  1.00 20.66           O  
ANISOU  743  O   LYS A 259     1719   2152   3979    838   -434   -507       O  
ATOM    744  CB  LYS A 259      18.930 -14.597  18.792  1.00 22.04           C  
ANISOU  744  CB  LYS A 259     2146   2009   4217    660   -779   -118       C  
ATOM    745  CG  LYS A 259      19.840 -15.786  18.522  1.00 26.80           C  
ANISOU  745  CG  LYS A 259     2728   2502   4953    802   -836   -178       C  
ATOM    746  CD  LYS A 259      19.115 -17.096  18.823  1.00 38.64           C  
ANISOU  746  CD  LYS A 259     4358   3774   6550    776   -984    -68       C  
ATOM    747  CE  LYS A 259      19.989 -18.294  18.482  1.00 50.25           C  
ANISOU  747  CE  LYS A 259     5810   5111   8170    936  -1039   -146       C  
ATOM    748  NZ  LYS A 259      19.212 -19.569  18.522  1.00 54.12           N  
ANISOU  748  NZ  LYS A 259     6435   5361   8767    901  -1165    -81       N  
ATOM    749  H   LYS A 259      17.841 -12.439  19.026  1.00 21.26           H  
ATOM    750  HA  LYS A 259      20.326 -13.142  19.158  1.00 25.97           H  
ATOM    751  HB2 LYS A 259      18.655 -14.643  19.721  1.00 26.48           H  
ATOM    752  HB3 LYS A 259      18.157 -14.681  18.212  1.00 26.48           H  
ATOM    753  HG2 LYS A 259      20.105 -15.787  17.589  1.00 32.20           H  
ATOM    754  HG3 LYS A 259      20.624 -15.730  19.090  1.00 32.20           H  
ATOM    755  HD2 LYS A 259      18.897 -17.135  19.768  1.00 46.40           H  
ATOM    756  HD3 LYS A 259      18.305 -17.147  18.293  1.00 46.40           H  
ATOM    757  HE2 LYS A 259      20.348 -18.184  17.588  1.00 60.33           H  
ATOM    758  HE3 LYS A 259      20.712 -18.357  19.125  1.00 60.33           H  
ATOM    759  HZ1 LYS A 259      19.742 -20.255  18.319  1.00 64.98           H  
ATOM    760  HZ2 LYS A 259      18.876 -19.695  19.337  1.00 64.98           H  
ATOM    761  HZ3 LYS A 259      18.544 -19.537  17.936  1.00 64.98           H  
ATOM    762  N   ALA A 260      19.268 -12.804  16.164  1.00 18.61           N  
ANISOU  762  N   ALA A 260     1670   1819   3580    700   -356   -529       N  
ATOM    763  CA  ALA A 260      19.681 -12.665  14.781  1.00 20.30           C  
ANISOU  763  CA  ALA A 260     1893   2110   3710    752   -199   -698       C  
ATOM    764  C   ALA A 260      20.631 -11.495  14.572  1.00 19.56           C  
ANISOU  764  C   ALA A 260     1672   2228   3530    720    -41   -738       C  
ATOM    765  O   ALA A 260      21.335 -11.464  13.562  1.00 23.99           O  
ANISOU  765  O   ALA A 260     2203   2877   4034    772     77   -839       O  
ATOM    766  CB  ALA A 260      18.443 -12.493  13.893  1.00 20.60           C  
ANISOU  766  CB  ALA A 260     2083   2114   3632    690   -144   -745       C  
ATOM    767  H   ALA A 260      18.433 -12.641  16.294  1.00 22.36           H  
ATOM    768  HA  ALA A 260      20.146 -13.471  14.509  1.00 24.40           H  
ATOM    769  HB1 ALA A 260      18.727 -12.399  12.970  1.00 24.76           H  
ATOM    770  HB2 ALA A 260      17.876 -13.274  13.987  1.00 24.76           H  
ATOM    771  HB3 ALA A 260      17.962 -11.698  14.173  1.00 24.76           H  
ATOM    772  N   THR A 261      20.666 -10.539  15.498  1.00 17.58           N  
ANISOU  772  N   THR A 261     1347   2069   3264    622    -39   -652       N  
ATOM    773  CA  THR A 261      21.644  -9.465  15.461  1.00 19.65           C  
ANISOU  773  CA  THR A 261     1484   2518   3464    554     87   -672       C  
ATOM    774  C   THR A 261      22.838  -9.770  16.366  1.00 20.27           C  
ANISOU  774  C   THR A 261     1394   2658   3650    596    -14   -627       C  
ATOM    775  O   THR A 261      23.695  -8.898  16.570  1.00 19.98           O  
ANISOU  775  O   THR A 261     1238   2777   3578    514     54   -625       O  
ATOM    776  CB  THR A 261      21.016  -8.119  15.853  1.00 19.30           C  
ANISOU  776  CB  THR A 261     1480   2543   3308    384    161   -615       C  
ATOM    777  OG1 THR A 261      20.875  -8.017  17.281  1.00 17.14           O  
ANISOU  777  OG1 THR A 261     1204   2272   3036    300     23   -490       O  
ATOM    778  CG2 THR A 261      19.668  -7.894  15.183  1.00 18.15           C  
ANISOU  778  CG2 THR A 261     1529   2323   3043    343    216   -607       C  
ATOM    779  H   THR A 261      20.125 -10.494  16.164  1.00 21.13           H  
ATOM    780  HA  THR A 261      21.957  -9.365  14.548  1.00 23.62           H  
ATOM    781  HB  THR A 261      21.610  -7.416  15.546  1.00 23.19           H  
ATOM    782  HG1 THR A 261      20.627  -8.754  17.598  1.00 20.60           H  
ATOM    783 HG21 THR A 261      19.304  -7.036  15.450  1.00 21.81           H  
ATOM    784 HG22 THR A 261      19.771  -7.906  14.218  1.00 21.81           H  
ATOM    785 HG23 THR A 261      19.048  -8.594  15.441  1.00 21.81           H  
ATOM    786  N   ASN A 262      22.882 -10.973  16.943  1.00 20.20           N  
ANISOU  786  N   ASN A 262     1387   2524   3763    705   -186   -572       N  
ATOM    787  CA  ASN A 262      23.933 -11.398  17.860  1.00 21.62           C  
ANISOU  787  CA  ASN A 262     1427   2754   4035    761   -311   -499       C  
ATOM    788  C   ASN A 262      24.126 -10.387  18.980  1.00 24.17           C  
ANISOU  788  C   ASN A 262     1662   3229   4292    610   -354   -407       C  
ATOM    789  O   ASN A 262      25.239  -9.968  19.297  1.00 22.20           O  
ANISOU  789  O   ASN A 262     1259   3134   4043    586   -346   -409       O  
ATOM    790  CB  ASN A 262      25.220 -11.653  17.103  1.00 25.36           C  
ANISOU  790  CB  ASN A 262     1771   3314   4550    874   -220   -602       C  
ATOM    791  CG  ASN A 262      25.010 -12.653  16.000  1.00 29.97           C  
ANISOU  791  CG  ASN A 262     2454   3761   5171   1011   -180   -712       C  
ATOM    792  OD1 ASN A 262      24.829 -12.284  14.847  1.00 26.84           O  
ANISOU  792  OD1 ASN A 262     2112   3410   4676    994    -22   -819       O  
ATOM    793  ND2 ASN A 262      24.982 -13.930  16.368  1.00 31.14           N  
ANISOU  793  ND2 ASN A 262     2645   3739   5450   1133   -333   -674       N  
ATOM    794  H   ASN A 262      22.290 -11.582  16.811  1.00 24.27           H  
ATOM    795  HA  ASN A 262      23.665 -12.230  18.281  1.00 25.77           H  
ATOM    796  HB2 ASN A 262      25.532 -10.823  16.710  1.00 30.47           H  
ATOM    797  HB3 ASN A 262      25.888 -12.003  17.712  1.00 30.47           H  
ATOM    798 HD21 ASN A 262      24.865 -14.545  15.778  1.00 37.41           H  
ATOM    799 HD22 ASN A 262      25.081 -14.141  17.196  1.00 37.41           H  
ATOM    800  N   ASN A 263      23.003  -9.998  19.574  1.00 23.01           N  
ANISOU  800  N   ASN A 263     1618   3045   4080    496   -404   -329       N  
ATOM    801  CA  ASN A 263      22.892  -9.156  20.753  1.00 20.14           C  
ANISOU  801  CA  ASN A 263     1241   2804   3607    333   -465   -238       C  
ATOM    802  C   ASN A 263      23.202  -7.693  20.468  1.00 19.45           C  
ANISOU  802  C   ASN A 263     1116   2855   3418    185   -298   -333       C  
ATOM    803  O   ASN A 263      23.207  -6.894  21.413  1.00 17.87           O  
ANISOU  803  O   ASN A 263      919   2754   3116     40   -337   -296       O  
ATOM    804  CB  ASN A 263      23.793  -9.652  21.890  1.00 20.61           C  
ANISOU  804  CB  ASN A 263     1186   2946   3699    366   -645   -131       C  
ATOM    805  CG  ASN A 263      23.166  -9.466  23.242  1.00 22.23           C  
ANISOU  805  CG  ASN A 263     1459   3207   3782    242   -784     15       C  
ATOM    806  OD1 ASN A 263      21.967  -9.716  23.420  1.00 24.05           O  
ANISOU  806  OD1 ASN A 263     1855   3339   3944    200   -799    101       O  
ATOM    807  ND2 ASN A 263      23.951  -9.002  24.197  1.00 28.64           N  
ANISOU  807  ND2 ASN A 263     2172   4200   4511    166   -858     42       N  
ATOM    808  H   ASN A 263      22.229 -10.232  19.283  1.00 27.65           H  
ATOM    809  HA  ASN A 263      21.973  -9.191  21.062  1.00 24.20           H  
ATOM    810  HB2 ASN A 263      23.968 -10.598  21.767  1.00 24.55           H  
ATOM    811  HB3 ASN A 263      24.627  -9.156  21.874  1.00 24.55           H  
ATOM    812 HD21 ASN A 263      23.638  -8.878  24.989  1.00 34.41           H  
ATOM    813 HD22 ASN A 263      24.775  -8.823  24.028  1.00 34.41           H  
ATOM    814  N   ALA A 264      23.430  -7.304  19.209  1.00 18.14           N  
ANISOU  814  N   ALA A 264      936   2693   3262    205   -116   -449       N  
ATOM    815  CA  ALA A 264      23.652  -5.895  18.906  1.00 17.43           C  
ANISOU  815  CA  ALA A 264      856   2692   3074     44     40   -496       C  
ATOM    816  C   ALA A 264      22.421  -5.057  19.231  1.00 16.52           C  
ANISOU  816  C   ALA A 264      924   2522   2831    -85     75   -463       C  
ATOM    817  O   ALA A 264      22.533  -3.911  19.713  1.00 17.76           O  
ANISOU  817  O   ALA A 264     1092   2735   2922   -240    112   -477       O  
ATOM    818  CB  ALA A 264      24.022  -5.718  17.438  1.00 21.72           C  
ANISOU  818  CB  ALA A 264     1411   3241   3602     88    220   -568       C  
ATOM    819  H   ALA A 264      23.459  -7.828  18.527  1.00 21.80           H  
ATOM    820  HA  ALA A 264      24.393  -5.582  19.449  1.00 20.73           H  
ATOM    821  HB1 ALA A 264      24.166  -4.775  17.260  1.00 26.10           H  
ATOM    822  HB2 ALA A 264      24.834  -6.217  17.254  1.00 26.10           H  
ATOM    823  HB3 ALA A 264      23.297  -6.052  16.887  1.00 26.10           H  
ATOM    824  N   MET A 265      21.239  -5.603  18.951  1.00 15.65           N  
ANISOU  824  N   MET A 265      976   2290   2679    -22     64   -422       N  
ATOM    825  CA  MET A 265      19.997  -4.906  19.276  1.00 15.47           C  
ANISOU  825  CA  MET A 265     1128   2223   2528   -115     93   -378       C  
ATOM    826  C   MET A 265      19.892  -4.665  20.778  1.00 13.20           C  
ANISOU  826  C   MET A 265      840   2002   2172   -205    -26   -317       C  
ATOM    827  O   MET A 265      19.525  -3.566  21.224  1.00 13.69           O  
ANISOU  827  O   MET A 265      973   2092   2137   -318     27   -344       O  
ATOM    828  CB  MET A 265      18.809  -5.729  18.778  1.00 14.98           C  
ANISOU  828  CB  MET A 265     1194   2045   2453    -32     73   -336       C  
ATOM    829  CG  MET A 265      17.483  -5.150  19.150  1.00 12.21           C  
ANISOU  829  CG  MET A 265      986   1670   1982   -104     94   -283       C  
ATOM    830  SD  MET A 265      16.139  -6.228  18.579  1.00 16.30           S  
ANISOU  830  SD  MET A 265     1613   2075   2506    -29     46   -229       S  
ATOM    831  CE  MET A 265      16.199  -5.829  16.827  1.00 16.41           C  
ANISOU  831  CE  MET A 265     1664   2062   2509     26    198   -337       C  
ATOM    832  H   MET A 265      21.128  -6.369  18.576  1.00 18.81           H  
ATOM    833  HA  MET A 265      19.981  -4.050  18.820  1.00 18.60           H  
ATOM    834  HB2 MET A 265      18.849  -5.782  17.811  1.00 18.01           H  
ATOM    835  HB3 MET A 265      18.862  -6.618  19.162  1.00 18.01           H  
ATOM    836  HG2 MET A 265      17.424  -5.066  20.115  1.00 14.68           H  
ATOM    837  HG3 MET A 265      17.380  -4.280  18.734  1.00 14.68           H  
ATOM    838  HE1 MET A 265      15.518  -6.340  16.363  1.00 19.73           H  
ATOM    839  HE2 MET A 265      16.034  -4.879  16.714  1.00 19.73           H  
ATOM    840  HE3 MET A 265      17.076  -6.056  16.481  1.00 19.73           H  
ATOM    841  N   GLN A 266      20.291  -5.660  21.583  1.00 14.22           N  
ANISOU  841  N   GLN A 266      889   2162   2350   -151   -190   -242       N  
ATOM    842  CA  GLN A 266      20.199  -5.500  23.032  1.00 15.12           C  
ANISOU  842  CA  GLN A 266     1005   2378   2361   -237   -313   -172       C  
ATOM    843  C   GLN A 266      21.137  -4.412  23.545  1.00 16.22           C  
ANISOU  843  C   GLN A 266     1050   2648   2465   -358   -303   -262       C  
ATOM    844  O   GLN A 266      20.759  -3.611  24.416  1.00 16.21           O  
ANISOU  844  O   GLN A 266     1117   2716   2328   -473   -311   -286       O  
ATOM    845  CB  GLN A 266      20.465  -6.832  23.721  1.00 18.45           C  
ANISOU  845  CB  GLN A 266     1364   2801   2843   -151   -504    -38       C  
ATOM    846  CG  GLN A 266      20.187  -6.782  25.223  1.00 16.64           C  
ANISOU  846  CG  GLN A 266     1161   2700   2460   -243   -634     70       C  
ATOM    847  CD  GLN A 266      18.742  -6.521  25.505  1.00 15.47           C  
ANISOU  847  CD  GLN A 266     1176   2539   2164   -308   -568    114       C  
ATOM    848  OE1 GLN A 266      17.910  -7.399  25.358  1.00 18.10           O  
ANISOU  848  OE1 GLN A 266     1580   2777   2522   -264   -597    227       O  
ATOM    849  NE2 GLN A 266      18.424  -5.281  25.862  1.00 16.56           N  
ANISOU  849  NE2 GLN A 266     1368   2763   2162   -414   -473     12       N  
ATOM    850  H   GLN A 266      20.609  -6.415  21.319  1.00 17.09           H  
ATOM    851  HA  GLN A 266      19.297  -5.226  23.258  1.00 18.17           H  
ATOM    852  HB2 GLN A 266      19.892  -7.510  23.330  1.00 22.17           H  
ATOM    853  HB3 GLN A 266      21.397  -7.073  23.595  1.00 22.17           H  
ATOM    854  HG2 GLN A 266      20.427  -7.633  25.622  1.00 19.79           H  
ATOM    855  HG3 GLN A 266      20.709  -6.070  25.623  1.00 19.79           H  
ATOM    856 HE21 GLN A 266      19.036  -4.680  25.919  1.00 19.91           H  
ATOM    857 HE22 GLN A 266      17.606  -5.080  26.035  1.00 19.91           H  
ATOM    858  N   VAL A 267      22.375  -4.375  23.050  1.00 16.71           N  
ANISOU  858  N   VAL A 267      944   2756   2649   -340   -288   -325       N  
ATOM    859  CA  VAL A 267      23.328  -3.370  23.513  1.00 17.95           C  
ANISOU  859  CA  VAL A 267     1012   3020   2788   -474   -289   -396       C  
ATOM    860  C   VAL A 267      22.849  -1.984  23.126  1.00 17.15           C  
ANISOU  860  C   VAL A 267     1047   2849   2619   -598   -128   -483       C  
ATOM    861  O   VAL A 267      22.910  -1.053  23.936  1.00 20.81           O  
ANISOU  861  O   VAL A 267     1565   3344   2998   -720   -152   -532       O  
ATOM    862  CB  VAL A 267      24.736  -3.655  22.962  1.00 19.51           C  
ANISOU  862  CB  VAL A 267     1032   3262   3119   -413   -282   -403       C  
ATOM    863  CG1 VAL A 267      25.710  -2.564  23.438  1.00 24.32           C  
ANISOU  863  CG1 VAL A 267     1582   3948   3709   -563   -286   -450       C  
ATOM    864  CG2 VAL A 267      25.212  -5.019  23.404  1.00 20.68           C  
ANISOU  864  CG2 VAL A 267     1056   3453   3348   -265   -454   -309       C  
ATOM    865  H   VAL A 267      22.683  -4.913  22.454  1.00 19.88           H  
ATOM    866  HA  VAL A 267      23.378  -3.419  24.480  1.00 21.36           H  
ATOM    867  HB  VAL A 267      24.709  -3.648  21.993  1.00 23.24           H  
ATOM    868 HG11 VAL A 267      26.597  -2.763  23.100  1.00 29.22           H  
ATOM    869 HG12 VAL A 267      25.412  -1.705  23.099  1.00 29.22           H  
ATOM    870 HG13 VAL A 267      25.720  -2.550  24.408  1.00 29.22           H  
ATOM    871 HG21 VAL A 267      26.099  -5.175  23.046  1.00 24.64           H  
ATOM    872 HG22 VAL A 267      25.236  -5.046  24.374  1.00 24.64           H  
ATOM    873 HG23 VAL A 267      24.597  -5.691  23.071  1.00 24.64           H  
ATOM    874  N   GLU A 268      22.327  -1.832  21.900  1.00 17.07           N  
ANISOU  874  N   GLU A 268     1109   2733   2646   -559     29   -502       N  
ATOM    875  CA  GLU A 268      21.772  -0.548  21.479  1.00 15.78           C  
ANISOU  875  CA  GLU A 268     1094   2474   2428   -654    170   -551       C  
ATOM    876  C   GLU A 268      20.563  -0.167  22.318  1.00 15.47           C  
ANISOU  876  C   GLU A 268     1204   2405   2269   -691    144   -562       C  
ATOM    877  O   GLU A 268      20.402   0.992  22.721  1.00 18.34           O  
ANISOU  877  O   GLU A 268     1650   2733   2585   -800    184   -640       O  
ATOM    878  CB  GLU A 268      21.397  -0.622  19.986  1.00 16.74           C  
ANISOU  878  CB  GLU A 268     1271   2504   2587   -580    321   -534       C  
ATOM    879  CG  GLU A 268      20.786   0.669  19.460  1.00 17.04           C  
ANISOU  879  CG  GLU A 268     1471   2427   2578   -654    451   -548       C  
ATOM    880  CD  GLU A 268      20.147   0.474  18.096  1.00 22.32           C  
ANISOU  880  CD  GLU A 268     2222   3025   3234   -562    565   -504       C  
ATOM    881  OE1 GLU A 268      19.721  -0.673  17.801  1.00 22.01           O  
ANISOU  881  OE1 GLU A 268     2161   3002   3200   -443    534   -483       O  
ATOM    882  OE2 GLU A 268      20.087   1.455  17.345  1.00 21.79           O  
ANISOU  882  OE2 GLU A 268     2247   2884   3150   -608    666   -484       O  
ATOM    883  H   GLU A 268      22.284  -2.451  21.304  1.00 20.52           H  
ATOM    884  HA  GLU A 268      22.441   0.144  21.595  1.00 18.97           H  
ATOM    885  HB2 GLU A 268      22.197  -0.807  19.470  1.00 20.13           H  
ATOM    886  HB3 GLU A 268      20.749  -1.333  19.860  1.00 20.13           H  
ATOM    887  HG2 GLU A 268      20.101   0.974  20.076  1.00 20.49           H  
ATOM    888  HG3 GLU A 268      21.481   1.341  19.378  1.00 20.49           H  
ATOM    889  N   SER A 269      19.709  -1.139  22.598  1.00 14.64           N  
ANISOU  889  N   SER A 269     1152   2300   2110   -584     77   -477       N  
ATOM    890  CA  SER A 269      18.505  -0.884  23.379  1.00 13.15           C  
ANISOU  890  CA  SER A 269     1098   2112   1787   -593     66   -464       C  
ATOM    891  C   SER A 269      18.858  -0.450  24.785  1.00 14.48           C  
ANISOU  891  C   SER A 269     1240   2410   1850   -697    -33   -520       C  
ATOM    892  O   SER A 269      18.237   0.468  25.325  1.00 18.06           O  
ANISOU  892  O   SER A 269     1799   2861   2203   -752     13   -605       O  
ATOM    893  CB  SER A 269      17.635  -2.148  23.407  1.00 14.16           C  
ANISOU  893  CB  SER A 269     1254   2233   1891   -486      3   -337       C  
ATOM    894  OG  SER A 269      17.154  -2.444  22.102  1.00 14.49           O  
ANISOU  894  OG  SER A 269     1342   2158   2006   -401     91   -317       O  
ATOM    895  H   SER A 269      19.800  -1.957  22.350  1.00 17.61           H  
ATOM    896  HA  SER A 269      17.994  -0.173  22.961  1.00 15.61           H  
ATOM    897  HB2 SER A 269      18.166  -2.893  23.727  1.00 17.02           H  
ATOM    898  HB3 SER A 269      16.880  -2.001  23.998  1.00 17.02           H  
ATOM    899  HG  SER A 269      16.560  -3.035  22.142  1.00 17.43           H  
ATOM    900  N   ASP A 270      19.857  -1.095  25.390  1.00 15.89           N  
ANISOU  900  N   ASP A 270     1278   2712   2048   -712   -175   -485       N  
ATOM    901  CA  ASP A 270      20.281  -0.718  26.739  1.00 17.25           C  
ANISOU  901  CA  ASP A 270     1416   3043   2096   -819   -294   -540       C  
ATOM    902  C   ASP A 270      20.747   0.728  26.774  1.00 18.17           C  
ANISOU  902  C   ASP A 270     1580   3100   2223   -927   -218   -694       C  
ATOM    903  O   ASP A 270      20.405   1.479  27.698  1.00 22.50           O  
ANISOU  903  O   ASP A 270     2218   3693   2638   -993   -229   -789       O  
ATOM    904  CB  ASP A 270      21.385  -1.642  27.240  1.00 18.63           C  
ANISOU  904  CB  ASP A 270     1440   3320   2317   -775   -462   -442       C  
ATOM    905  CG  ASP A 270      20.875  -3.048  27.570  1.00 20.41           C  
ANISOU  905  CG  ASP A 270     1650   3594   2510   -676   -580   -264       C  
ATOM    906  OD1 ASP A 270      19.653  -3.223  27.727  1.00 21.61           O  
ANISOU  906  OD1 ASP A 270     1933   3718   2561   -656   -533   -204       O  
ATOM    907  OD2 ASP A 270      21.717  -3.976  27.675  1.00 29.98           O  
ANISOU  907  OD2 ASP A 270     2742   4828   3820   -595   -707   -167       O  
ATOM    908  H   ASP A 270      20.301  -1.747  25.046  1.00 19.10           H  
ATOM    909  HA  ASP A 270      19.524  -0.817  27.337  1.00 20.52           H  
ATOM    910  HB2 ASP A 270      22.066  -1.723  26.553  1.00 22.17           H  
ATOM    911  HB3 ASP A 270      21.771  -1.266  28.046  1.00 22.17           H  
ATOM    912  N   ASP A 271      21.496   1.146  25.757  1.00 20.40           N  
ANISOU  912  N   ASP A 271     1813   3279   2658   -942   -133   -715       N  
ATOM    913  CA  ASP A 271      21.959   2.529  25.703  1.00 22.96           C  
ANISOU  913  CA  ASP A 271     2188   3520   3016  -1055    -66   -827       C  
ATOM    914  C   ASP A 271      20.789   3.477  25.491  1.00 22.07           C  
ANISOU  914  C   ASP A 271     2260   3264   2860  -1069     60   -905       C  
ATOM    915  O   ASP A 271      20.736   4.558  26.093  1.00 24.38           O  
ANISOU  915  O   ASP A 271     2642   3509   3113  -1145     66  -1019       O  
ATOM    916  CB  ASP A 271      22.990   2.679  24.590  1.00 25.27           C  
ANISOU  916  CB  ASP A 271     2380   3756   3465  -1071      3   -792       C  
ATOM    917  CG  ASP A 271      23.439   4.112  24.399  1.00 28.94           C  
ANISOU  917  CG  ASP A 271     2901   4115   3981  -1203     73   -872       C  
ATOM    918  OD1 ASP A 271      22.876   4.792  23.517  1.00 31.75           O  
ANISOU  918  OD1 ASP A 271     3373   4316   4375  -1206    209   -870       O  
ATOM    919  OD2 ASP A 271      24.328   4.555  25.146  1.00 37.09           O  
ANISOU  919  OD2 ASP A 271     3864   5210   5017  -1304    -21   -926       O  
ATOM    920  H   ASP A 271      21.747   0.657  25.095  1.00 24.51           H  
ATOM    921  HA  ASP A 271      22.388   2.762  26.541  1.00 27.59           H  
ATOM    922  HB2 ASP A 271      23.771   2.147  24.809  1.00 30.36           H  
ATOM    923  HB3 ASP A 271      22.602   2.372  23.756  1.00 30.36           H  
ATOM    924  N   TYR A 272      19.813   3.071  24.672  1.00 19.64           N  
ANISOU  924  N   TYR A 272     2015   2881   2568   -983    151   -848       N  
ATOM    925  CA  TYR A 272      18.637   3.908  24.487  1.00 17.28           C  
ANISOU  925  CA  TYR A 272     1887   2444   2237   -968    260   -912       C  
ATOM    926  C   TYR A 272      17.919   4.116  25.809  1.00 18.38           C  
ANISOU  926  C   TYR A 272     2100   2676   2210   -968    204  -1004       C  
ATOM    927  O   TYR A 272      17.536   5.242  26.148  1.00 21.02           O  
ANISOU  927  O   TYR A 272     2550   2914   2524   -976    257  -1110       O  
ATOM    928  CB  TYR A 272      17.698   3.289  23.451  1.00 15.77           C  
ANISOU  928  CB  TYR A 272     1744   2180   2066   -824    342   -787       C  
ATOM    929  CG  TYR A 272      16.357   4.009  23.434  1.00 19.22           C  
ANISOU  929  CG  TYR A 272     2341   2510   2450   -753    427   -821       C  
ATOM    930  CD1 TYR A 272      15.350   3.646  24.308  1.00 18.31           C  
ANISOU  930  CD1 TYR A 272     2260   2497   2199   -682    395   -823       C  
ATOM    931  CD2 TYR A 272      16.151   5.102  22.604  1.00 24.48           C  
ANISOU  931  CD2 TYR A 272     3114   2984   3203   -761    538   -847       C  
ATOM    932  CE1 TYR A 272      14.144   4.315  24.336  1.00 20.20           C  
ANISOU  932  CE1 TYR A 272     2612   2665   2397   -601    477   -868       C  
ATOM    933  CE2 TYR A 272      14.947   5.784  22.622  1.00 24.12           C  
ANISOU  933  CE2 TYR A 272     3200   2836   3127   -670    603   -881       C  
ATOM    934  CZ  TYR A 272      13.961   5.393  23.488  1.00 20.65           C  
ANISOU  934  CZ  TYR A 272     2770   2515   2560   -583    575   -904       C  
ATOM    935  OH  TYR A 272      12.755   6.074  23.533  1.00 22.59           O  
ANISOU  935  OH  TYR A 272     3104   2692   2788   -463    629   -916       O  
ATOM    936  H   TYR A 272      19.812   2.335  24.227  1.00 23.61           H  
ATOM    937  HA  TYR A 272      18.917   4.773  24.147  1.00 20.78           H  
ATOM    938  HB2 TYR A 272      18.097   3.360  22.570  1.00 18.96           H  
ATOM    939  HB3 TYR A 272      17.544   2.357  23.672  1.00 18.96           H  
ATOM    940  HD1 TYR A 272      15.488   2.934  24.890  1.00 22.00           H  
ATOM    941  HD2 TYR A 272      16.829   5.378  22.029  1.00 29.41           H  
ATOM    942  HE1 TYR A 272      13.467   4.047  24.914  1.00 24.27           H  
ATOM    943  HE2 TYR A 272      14.809   6.504  22.050  1.00 28.98           H  
ATOM    944  HH  TYR A 272      12.764   6.710  22.984  1.00 27.14           H  
ATOM    945  N   ILE A 273      17.718   3.035  26.570  1.00 20.15           N  
ANISOU  945  N   ILE A 273     2260   3084   2313   -923    101   -925       N  
ATOM    946  CA  ILE A 273      16.990   3.140  27.831  1.00 19.89           C  
ANISOU  946  CA  ILE A 273     2287   3189   2079   -921     63   -990       C  
ATOM    947  C   ILE A 273      17.768   3.987  28.833  1.00 21.27           C  
ANISOU  947  C   ILE A 273     2464   3412   2205  -1010      0  -1116       C  
ATOM    948  O   ILE A 273      17.188   4.787  29.576  1.00 24.79           O  
ANISOU  948  O   ILE A 273     3007   3858   2555   -997     36  -1230       O  
ATOM    949  CB  ILE A 273      16.697   1.733  28.388  1.00 21.60           C  
ANISOU  949  CB  ILE A 273     2434   3588   2186   -860    -38   -813       C  
ATOM    950  CG1 ILE A 273      15.737   0.981  27.469  1.00 19.47           C  
ANISOU  950  CG1 ILE A 273     2190   3225   1983   -735     36   -660       C  
ATOM    951  CG2 ILE A 273      16.162   1.823  29.814  1.00 24.82           C  
ANISOU  951  CG2 ILE A 273     2880   4203   2346   -891    -84   -869       C  
ATOM    952  CD1 ILE A 273      14.324   1.546  27.398  1.00 19.50           C  
ANISOU  952  CD1 ILE A 273     2304   3185   1920   -665    163   -704       C  
ATOM    953  H   ILE A 273      17.990   2.242  26.379  1.00 24.22           H  
ATOM    954  HA  ILE A 273      16.144   3.584  27.663  1.00 23.90           H  
ATOM    955  HB  ILE A 273      17.527   1.232  28.415  1.00 25.96           H  
ATOM    956 HG12 ILE A 273      16.100   0.996  26.569  1.00 23.40           H  
ATOM    957 HG13 ILE A 273      15.667   0.066  27.783  1.00 23.40           H  
ATOM    958 HG21 ILE A 273      15.943   0.932  30.126  1.00 29.82           H  
ATOM    959 HG22 ILE A 273      16.844   2.214  30.382  1.00 29.82           H  
ATOM    960 HG23 ILE A 273      15.368   2.380  29.819  1.00 29.82           H  
ATOM    961 HD11 ILE A 273      13.798   1.006  26.787  1.00 23.44           H  
ATOM    962 HD12 ILE A 273      13.929   1.521  28.284  1.00 23.44           H  
ATOM    963 HD13 ILE A 273      14.365   2.461  27.080  1.00 23.44           H  
ATOM    964  N   ALA A 274      19.089   3.815  28.887  1.00 20.68           N  
ANISOU  964  N   ALA A 274     2274   3380   2206  -1082    -98  -1089       N  
ATOM    965  CA  ALA A 274      19.886   4.590  29.835  1.00 23.57           C  
ANISOU  965  CA  ALA A 274     2635   3794   2529  -1175   -176  -1204       C  
ATOM    966  C   ALA A 274      19.774   6.084  29.581  1.00 25.25           C  
ANISOU  966  C   ALA A 274     2968   3801   2826  -1222    -80  -1355       C  
ATOM    967  O   ALA A 274      19.862   6.878  30.522  1.00 31.50           O  
ANISOU  967  O   ALA A 274     3818   4610   3540  -1272   -122  -1492       O  
ATOM    968  CB  ALA A 274      21.344   4.144  29.763  1.00 29.49           C  
ANISOU  968  CB  ALA A 274     3221   4611   3373  -1232   -294  -1136       C  
ATOM    969  H   ALA A 274      19.538   3.268  28.398  1.00 24.64           H  
ATOM    970  HA  ALA A 274      19.559   4.422  30.733  1.00 28.33           H  
ATOM    971  HB1 ALA A 274      21.866   4.669  30.390  1.00 35.43           H  
ATOM    972  HB2 ALA A 274      21.398   3.203  29.995  1.00 35.43           H  
ATOM    973  HB3 ALA A 274      21.673   4.281  28.861  1.00 35.43           H  
ATOM    974  N   THR A 275      19.566   6.486  28.337  1.00 22.88           N  
ANISOU  974  N   THR A 275     2711   3299   2682  -1202     41  -1324       N  
ATOM    975  CA  THR A 275      19.477   7.894  27.986  1.00 24.04           C  
ANISOU  975  CA  THR A 275     2978   3219   2935  -1239    120  -1422       C  
ATOM    976  C   THR A 275      18.053   8.433  28.055  1.00 23.73           C  
ANISOU  976  C   THR A 275     3094   3074   2848  -1119    213  -1480       C  
ATOM    977  O   THR A 275      17.855   9.590  28.438  1.00 25.59           O  
ANISOU  977  O   THR A 275     3440   3179   3104  -1126    223  -1608       O  
ATOM    978  CB  THR A 275      20.032   8.103  26.566  1.00 34.72           C  
ANISOU  978  CB  THR A 275     4302   4417   4475  -1275    199  -1320       C  
ATOM    979  OG1 THR A 275      21.437   7.811  26.554  1.00 40.60           O  
ANISOU  979  OG1 THR A 275     4889   5258   5279  -1379    116  -1282       O  
ATOM    980  CG2 THR A 275      19.808   9.527  26.087  1.00 36.26           C  
ANISOU  980  CG2 THR A 275     4638   4356   4784  -1303    277  -1374       C  
ATOM    981  H   THR A 275      19.470   5.955  27.668  1.00 27.27           H  
ATOM    982  HA  THR A 275      20.014   8.403  28.613  1.00 28.67           H  
ATOM    983  HB  THR A 275      19.568   7.510  25.956  1.00 41.70           H  
ATOM    984  HG1 THR A 275      21.745   7.913  25.779  1.00 48.76           H  
ATOM    985 HG21 THR A 275      20.193   9.645  25.205  1.00 43.55           H  
ATOM    986 HG22 THR A 275      18.857   9.717  26.043  1.00 43.55           H  
ATOM    987 HG23 THR A 275      20.225  10.153  26.700  1.00 43.55           H  
ATOM    988  N   ASN A 276      17.063   7.630  27.659  1.00 24.02           N  
ANISOU  988  N   ASN A 276     3136   3156   2835  -1001    274  -1387       N  
ATOM    989  CA  ASN A 276      15.709   8.115  27.479  1.00 21.37           C  
ANISOU  989  CA  ASN A 276     2919   2713   2488   -861    369  -1404       C  
ATOM    990  C   ASN A 276      14.710   7.554  28.477  1.00 21.35           C  
ANISOU  990  C   ASN A 276     2913   2905   2293   -765    357  -1420       C  
ATOM    991  O   ASN A 276      13.591   8.082  28.567  1.00 23.47           O  
ANISOU  991  O   ASN A 276     3262   3114   2541   -637    425  -1454       O  
ATOM    992  CB  ASN A 276      15.214   7.780  26.058  1.00 23.28           C  
ANISOU  992  CB  ASN A 276     3174   2833   2838   -785    462  -1264       C  
ATOM    993  CG  ASN A 276      16.080   8.387  24.979  1.00 25.54           C  
ANISOU  993  CG  ASN A 276     3471   2937   3298   -870    500  -1217       C  
ATOM    994  OD1 ASN A 276      16.998   7.743  24.459  1.00 30.46           O  
ANISOU  994  OD1 ASN A 276     3988   3616   3968   -949    481  -1141       O  
ATOM    995  ND2 ASN A 276      15.799   9.636  24.634  1.00 34.92           N  
ANISOU  995  ND2 ASN A 276     4777   3912   4580   -847    548  -1249       N  
ATOM    996  H   ASN A 276      17.159   6.792  27.489  1.00 28.86           H  
ATOM    997  HA  ASN A 276      15.722   9.079  27.586  1.00 25.47           H  
ATOM    998  HB2 ASN A 276      15.219   6.817  25.940  1.00 27.97           H  
ATOM    999  HB3 ASN A 276      14.313   8.123  25.948  1.00 27.97           H  
ATOM   1000 HD21 ASN A 276      16.262  10.029  24.024  1.00 41.94           H  
ATOM   1001 HD22 ASN A 276      15.154  10.054  25.019  1.00 41.94           H  
ATOM   1002  N   GLY A 277      15.069   6.516  29.230  1.00 21.30           N  
ANISOU 1002  N   GLY A 277     2302   3380   2411   -711      2  -1256       N  
ATOM   1003  CA  GLY A 277      14.141   5.861  30.119  1.00 19.48           C  
ANISOU 1003  CA  GLY A 277     2060   3295   2048   -624    -10  -1237       C  
ATOM   1004  C   GLY A 277      13.216   4.889  29.414  1.00 17.19           C  
ANISOU 1004  C   GLY A 277     1825   2966   1741   -555      6  -1105       C  
ATOM   1005  O   GLY A 277      13.192   4.795  28.193  1.00 18.56           O  
ANISOU 1005  O   GLY A 277     2056   2981   2016   -563     26  -1045       O  
ATOM   1006  H   GLY A 277      15.859   6.175  29.237  1.00 25.60           H  
ATOM   1007  HA2 GLY A 277      14.638   5.370  30.792  1.00 23.42           H  
ATOM   1008  HA3 GLY A 277      13.594   6.532  30.558  1.00 23.42           H  
ATOM   1009  N   PRO A 278      12.436   4.144  30.184  1.00 16.60           N  
ANISOU 1009  N   PRO A 278     1736   3041   1530   -497      1  -1053       N  
ATOM   1010  CA  PRO A 278      11.571   3.119  29.586  1.00 17.45           C  
ANISOU 1010  CA  PRO A 278     1894   3133   1605   -444     13   -916       C  
ATOM   1011  C   PRO A 278      10.485   3.724  28.711  1.00 17.07           C  
ANISOU 1011  C   PRO A 278     1921   2873   1692   -407     73   -952       C  
ATOM   1012  O   PRO A 278      10.071   4.874  28.903  1.00 20.31           O  
ANISOU 1012  O   PRO A 278     2343   3190   2182   -399     99  -1087       O  
ATOM   1013  CB  PRO A 278      10.970   2.401  30.805  1.00 18.01           C  
ANISOU 1013  CB  PRO A 278     1931   3410   1504   -420      7   -851       C  
ATOM   1014  CG  PRO A 278      11.056   3.402  31.932  1.00 21.09           C  
ANISOU 1014  CG  PRO A 278     2265   3883   1867   -445     20  -1012       C  
ATOM   1015  CD  PRO A 278      12.348   4.166  31.658  1.00 18.54           C  
ANISOU 1015  CD  PRO A 278     1920   3488   1637   -495    -13  -1103       C  
ATOM   1016  HA  PRO A 278      12.096   2.494  29.061  1.00 20.98           H  
ATOM   1017  HB2 PRO A 278      10.048   2.160  30.625  1.00 21.65           H  
ATOM   1018  HB3 PRO A 278      11.488   1.606  31.008  1.00 21.65           H  
ATOM   1019  HG2 PRO A 278      10.288   3.994  31.911  1.00 25.35           H  
ATOM   1020  HG3 PRO A 278      11.096   2.941  32.785  1.00 25.35           H  
ATOM   1021  HD2 PRO A 278      12.289   5.076  31.989  1.00 22.29           H  
ATOM   1022  HD3 PRO A 278      13.108   3.715  32.058  1.00 22.29           H  
ATOM   1023  N   LEU A 279      10.050   2.934  27.734  1.00 16.38           N  
ANISOU 1023  N   LEU A 279     1884   2678   1663   -354     83   -779       N  
ATOM   1024  CA  LEU A 279       8.895   3.300  26.930  1.00 16.88           C  
ANISOU 1024  CA  LEU A 279     2008   2571   1836   -297    121   -778       C  
ATOM   1025  C   LEU A 279       7.624   3.249  27.785  1.00 19.51           C  
ANISOU 1025  C   LEU A 279     2294   3036   2082   -261    155   -848       C  
ATOM   1026  O   LEU A 279       7.596   2.681  28.883  1.00 20.25           O  
ANISOU 1026  O   LEU A 279     2327   3355   2011   -293    157   -842       O  
ATOM   1027  CB  LEU A 279       8.749   2.359  25.732  1.00 13.95           C  
ANISOU 1027  CB  LEU A 279     1690   2089   1521   -259    115   -589       C  
ATOM   1028  CG  LEU A 279       9.902   2.351  24.728  1.00 16.35           C  
ANISOU 1028  CG  LEU A 279     2029   2284   1901   -288    102   -525       C  
ATOM   1029  CD1 LEU A 279       9.589   1.338  23.625  1.00 15.73           C  
ANISOU 1029  CD1 LEU A 279     1999   2123   1854   -237     98   -367       C  
ATOM   1030  CD2 LEU A 279      10.153   3.718  24.164  1.00 25.92           C  
ANISOU 1030  CD2 LEU A 279     3295   3326   3225   -332    121   -624       C  
ATOM   1031  H   LEU A 279      10.407   2.183  27.518  1.00 19.70           H  
ATOM   1032  HA  LEU A 279       9.009   4.201  26.590  1.00 20.30           H  
ATOM   1033  HB2 LEU A 279       8.659   1.454  26.070  1.00 16.77           H  
ATOM   1034  HB3 LEU A 279       7.950   2.613  25.246  1.00 16.77           H  
ATOM   1035  HG  LEU A 279      10.723   2.089  25.174  1.00 19.66           H  
ATOM   1036 HD11 LEU A 279      10.316   1.336  22.983  1.00 18.91           H  
ATOM   1037 HD12 LEU A 279       9.496   0.458  24.022  1.00 18.91           H  
ATOM   1038 HD13 LEU A 279       8.762   1.594  23.188  1.00 18.91           H  
ATOM   1039 HD21 LEU A 279      10.883   3.668  23.528  1.00 31.13           H  
ATOM   1040 HD22 LEU A 279       9.348   4.028  23.721  1.00 31.13           H  
ATOM   1041 HD23 LEU A 279      10.386   4.320  24.888  1.00 31.13           H  
ATOM   1042  N   LYS A 280       6.589   3.910  27.300  1.00 17.15           N  
ANISOU 1042  N   LYS A 280     2016   2613   1888   -195    179   -923       N  
ATOM   1043  CA  LYS A 280       5.239   3.764  27.818  1.00 18.32           C  
ANISOU 1043  CA  LYS A 280     2096   2885   1981   -147    221   -982       C  
ATOM   1044  C   LYS A 280       4.544   2.623  27.107  1.00 14.59           C  
ANISOU 1044  C   LYS A 280     1630   2400   1514   -133    224   -794       C  
ATOM   1045  O   LYS A 280       4.829   2.331  25.946  1.00 12.96           O  
ANISOU 1045  O   LYS A 280     1499   2020   1404   -116    190   -670       O  
ATOM   1046  CB  LYS A 280       4.437   5.044  27.604  1.00 21.04           C  
ANISOU 1046  CB  LYS A 280     2442   3087   2466    -54    220  -1138       C  
ATOM   1047  CG  LYS A 280       4.976   6.247  28.366  1.00 27.69           C  
ANISOU 1047  CG  LYS A 280     3282   3899   3338    -66    201  -1274       C  
ATOM   1048  H   LYS A 280       6.642   4.468  26.649  1.00 20.62           H  
ATOM   1049  HA  LYS A 280       5.275   3.581  28.769  1.00 22.02           H  
ATOM   1050  HB2 LYS A 280       4.448   5.263  26.659  1.00 25.28           H  
ATOM   1051  HB3 LYS A 280       3.525   4.892  27.899  1.00 25.28           H  
ATOM   1052  N   VAL A 281       3.637   1.957  27.821  1.00 14.90           N  
ANISOU 1052  N   VAL A 281     1588   2637   1436   -157    269   -779       N  
ATOM   1053  CA  VAL A 281       2.802   0.957  27.172  1.00 14.68           C  
ANISOU 1053  CA  VAL A 281     1557   2593   1430   -162    273   -631       C  
ATOM   1054  C   VAL A 281       2.002   1.654  26.090  1.00 12.57           C  
ANISOU 1054  C   VAL A 281     1295   2150   1330    -56    254   -699       C  
ATOM   1055  O   VAL A 281       1.413   2.718  26.311  1.00 15.23           O  
ANISOU 1055  O   VAL A 281     1581   2486   1721     23    268   -885       O  
ATOM   1056  CB  VAL A 281       1.904   0.253  28.194  1.00 14.00           C  
ANISOU 1056  CB  VAL A 281     1370   2764   1185   -238    338   -617       C  
ATOM   1057  CG1 VAL A 281       0.953  -0.739  27.515  1.00 15.32           C  
ANISOU 1057  CG1 VAL A 281     1522   2907   1391   -269    343   -482       C  
ATOM   1058  CG2 VAL A 281       2.767  -0.456  29.224  1.00 16.86           C  
ANISOU 1058  CG2 VAL A 281     1756   3283   1365   -338    332   -513       C  
ATOM   1059  H   VAL A 281       3.490   2.065  28.661  1.00 17.91           H  
ATOM   1060  HA  VAL A 281       3.357   0.272  26.766  1.00 17.66           H  
ATOM   1061  HB  VAL A 281       1.355   0.917  28.639  1.00 16.62           H  
ATOM   1062 HG11 VAL A 281       0.406  -1.166  28.193  1.00 18.42           H  
ATOM   1063 HG12 VAL A 281       0.389  -0.258  26.890  1.00 18.42           H  
ATOM   1064 HG13 VAL A 281       1.476  -1.406  27.044  1.00 18.42           H  
ATOM   1065 HG21 VAL A 281       2.191  -0.903  29.865  1.00 20.26           H  
ATOM   1066 HG22 VAL A 281       3.327  -1.107  28.773  1.00 20.26           H  
ATOM   1067 HG23 VAL A 281       3.320   0.199  29.678  1.00 20.26           H  
ATOM   1068  N   GLY A 282       1.981   1.061  24.898  1.00 12.13           N  
ANISOU 1068  N   GLY A 282     1308   1944   1355    -42    211   -555       N  
ATOM   1069  CA  GLY A 282       1.387   1.707  23.744  1.00 13.37           C  
ANISOU 1069  CA  GLY A 282     1498   1924   1656     60    167   -589       C  
ATOM   1070  C   GLY A 282       2.341   2.576  22.969  1.00 12.93           C  
ANISOU 1070  C   GLY A 282     1567   1653   1694     94    123   -587       C  
ATOM   1071  O   GLY A 282       1.976   3.062  21.891  1.00 14.41           O  
ANISOU 1071  O   GLY A 282     1818   1675   1984    171     73   -572       O  
ATOM   1072  H   GLY A 282       2.306   0.281  24.738  1.00 14.59           H  
ATOM   1073  HA2 GLY A 282       1.047   1.026  23.143  1.00 16.08           H  
ATOM   1074  HA3 GLY A 282       0.650   2.263  24.041  1.00 16.08           H  
ATOM   1075  N   GLY A 283       3.559   2.763  23.479  1.00 12.03           N  
ANISOU 1075  N   GLY A 283     1486   1549   1535     28    137   -595       N  
ATOM   1076  CA  GLY A 283       4.551   3.608  22.857  1.00 11.76           C  
ANISOU 1076  CA  GLY A 283     1553   1336   1579     17    113   -600       C  
ATOM   1077  C   GLY A 283       5.544   2.819  22.030  1.00 13.78           C  
ANISOU 1077  C   GLY A 283     1871   1546   1819    -39    104   -442       C  
ATOM   1078  O   GLY A 283       5.456   1.594  21.923  1.00 11.82           O  
ANISOU 1078  O   GLY A 283     1599   1376   1514    -51    102   -334       O  
ATOM   1079  H   GLY A 283       3.833   2.397  24.208  1.00 14.47           H  
ATOM   1080  HA2 GLY A 283       4.110   4.247  22.276  1.00 14.15           H  
ATOM   1081  HA3 GLY A 283       5.040   4.089  23.543  1.00 14.15           H  
ATOM   1082  N   SER A 284       6.505   3.559  21.471  1.00 12.89           N  
ANISOU 1082  N   SER A 284     1834   1305   1760    -80    100   -443       N  
ATOM   1083  CA  SER A 284       7.492   2.994  20.570  1.00 11.82           C  
ANISOU 1083  CA  SER A 284     1742   1135   1613   -130    105   -324       C  
ATOM   1084  C   SER A 284       8.730   3.874  20.514  1.00  9.97           C  
ANISOU 1084  C   SER A 284     1536    844   1407   -224    126   -369       C  
ATOM   1085  O   SER A 284       8.736   5.036  20.942  1.00 13.37           O  
ANISOU 1085  O   SER A 284     1992   1197   1892   -251    124   -479       O  
ATOM   1086  CB  SER A 284       6.927   2.844  19.156  1.00 10.90           C  
ANISOU 1086  CB  SER A 284     1713    892   1537    -81     82   -226       C  
ATOM   1087  OG  SER A 284       6.780   4.115  18.562  1.00 15.13           O  
ANISOU 1087  OG  SER A 284     2346   1252   2149    -75     64   -248       O  
ATOM   1088  H   SER A 284       6.602   4.403  21.604  1.00 15.51           H  
ATOM   1089  HA  SER A 284       7.753   2.129  20.923  1.00 14.22           H  
ATOM   1090  HB2 SER A 284       7.537   2.311  18.623  1.00 13.11           H  
ATOM   1091  HB3 SER A 284       6.061   2.411  19.202  1.00 13.11           H  
ATOM   1092  HG  SER A 284       5.999   4.399  18.682  1.00 18.19           H  
ATOM   1093  N   CYS A 285       9.803   3.273  20.016  1.00 12.22           N  
ANISOU 1093  N   CYS A 285     1806   1178   1659   -278    146   -298       N  
ATOM   1094  CA  CYS A 285      10.988   4.009  19.620  1.00 11.34           C  
ANISOU 1094  CA  CYS A 285     1713   1021   1574   -392    179   -317       C  
ATOM   1095  C   CYS A 285      11.546   3.361  18.358  1.00 12.15           C  
ANISOU 1095  C   CYS A 285     1839   1126   1652   -407    209   -208       C  
ATOM   1096  O   CYS A 285      11.368   2.155  18.110  1.00 12.14           O  
ANISOU 1096  O   CYS A 285     1806   1198   1608   -330    196   -148       O  
ATOM   1097  CB  CYS A 285      12.039   4.063  20.717  1.00 13.67           C  
ANISOU 1097  CB  CYS A 285     1892   1466   1834   -465    184   -414       C  
ATOM   1098  SG  CYS A 285      12.772   2.480  21.104  1.00 14.02           S  
ANISOU 1098  SG  CYS A 285     1812   1727   1788   -414    164   -361       S  
ATOM   1099  H   CYS A 285       9.868   2.423  19.897  1.00 14.70           H  
ATOM   1100  HA  CYS A 285      10.755   4.930  19.420  1.00 13.64           H  
ATOM   1101  HB2 CYS A 285      12.752   4.657  20.434  1.00 16.44           H  
ATOM   1102  HB3 CYS A 285      11.626   4.403  21.526  1.00 16.44           H  
ATOM   1103  HG  CYS A 285      13.695   2.649  21.851  1.00 16.86           H  
ATOM   1104  N   VAL A 286      12.266   4.168  17.586  1.00 13.78           N  
ANISOU 1104  N   VAL A 286     2101   1252   1880   -520    253   -192       N  
ATOM   1105  CA  VAL A 286      12.946   3.711  16.372  1.00 14.76           C  
ANISOU 1105  CA  VAL A 286     2237   1413   1959   -562    305   -112       C  
ATOM   1106  C   VAL A 286      14.436   3.618  16.674  1.00 13.04           C  
ANISOU 1106  C   VAL A 286     1882   1353   1720   -668    357   -177       C  
ATOM   1107  O   VAL A 286      15.078   4.615  17.061  1.00 15.55           O  
ANISOU 1107  O   VAL A 286     2184   1651   2075   -805    383   -241       O  
ATOM   1108  CB  VAL A 286      12.696   4.650  15.182  1.00 15.05           C  
ANISOU 1108  CB  VAL A 286     2414   1304   2001   -609    313    -24       C  
ATOM   1109  CG1 VAL A 286      13.480   4.138  13.953  1.00 20.36           C  
ANISOU 1109  CG1 VAL A 286     3084   2061   2590   -672    387     41       C  
ATOM   1110  CG2 VAL A 286      11.246   4.735  14.877  1.00 19.22           C  
ANISOU 1110  CG2 VAL A 286     3016   1737   2551   -465    229     27       C  
ATOM   1111  H   VAL A 286      12.380   5.006  17.746  1.00 16.57           H  
ATOM   1112  HA  VAL A 286      12.613   2.830  16.140  1.00 17.75           H  
ATOM   1113  HB  VAL A 286      13.002   5.543  15.404  1.00 18.10           H  
ATOM   1114 HG11 VAL A 286      13.298   4.718  13.197  1.00 24.47           H  
ATOM   1115 HG12 VAL A 286      14.428   4.147  14.157  1.00 24.47           H  
ATOM   1116 HG13 VAL A 286      13.194   3.233  13.751  1.00 24.47           H  
ATOM   1117 HG21 VAL A 286      11.116   5.328  14.121  1.00 23.10           H  
ATOM   1118 HG22 VAL A 286      10.916   3.849  14.662  1.00 23.10           H  
ATOM   1119 HG23 VAL A 286      10.779   5.083  15.653  1.00 23.10           H  
ATOM   1120  N   LEU A 287      14.995   2.433  16.437  1.00 11.91           N  
ANISOU 1120  N   LEU A 287     1637   1362   1528   -602    368   -171       N  
ATOM   1121  CA  LEU A 287      16.419   2.159  16.615  1.00 15.25           C  
ANISOU 1121  CA  LEU A 287     1895   1968   1931   -663    408   -243       C  
ATOM   1122  C   LEU A 287      16.909   1.472  15.352  1.00 12.28           C  
ANISOU 1122  C   LEU A 287     1498   1666   1504   -647    472   -211       C  
ATOM   1123  O   LEU A 287      16.165   1.288  14.391  1.00 13.16           O  
ANISOU 1123  O   LEU A 287     1733   1682   1585   -606    481   -131       O  
ATOM   1124  CB  LEU A 287      16.656   1.310  17.879  1.00 12.52           C  
ANISOU 1124  CB  LEU A 287     1420   1757   1579   -554    329   -301       C  
ATOM   1125  CG  LEU A 287      16.366   2.017  19.202  1.00 16.61           C  
ANISOU 1125  CG  LEU A 287     1932   2265   2115   -590    278   -365       C  
ATOM   1126  CD1 LEU A 287      16.494   1.042  20.340  1.00 16.85           C  
ANISOU 1126  CD1 LEU A 287     1862   2438   2101   -476    193   -383       C  
ATOM   1127  CD2 LEU A 287      17.310   3.194  19.377  1.00 18.53           C  
ANISOU 1127  CD2 LEU A 287     2119   2535   2387   -772    324   -459       C  
ATOM   1128  H   LEU A 287      14.553   1.748  16.163  1.00 14.33           H  
ATOM   1129  HA  LEU A 287      16.924   2.980  16.729  1.00 18.33           H  
ATOM   1130  HB2 LEU A 287      16.081   0.530  17.835  1.00 15.06           H  
ATOM   1131  HB3 LEU A 287      17.586   1.036  17.894  1.00 15.06           H  
ATOM   1132  HG  LEU A 287      15.460   2.362  19.205  1.00 19.97           H  
ATOM   1133 HD11 LEU A 287      16.313   1.503  21.173  1.00 20.25           H  
ATOM   1134 HD12 LEU A 287      15.855   0.323  20.213  1.00 20.25           H  
ATOM   1135 HD13 LEU A 287      17.396   0.684  20.349  1.00 20.25           H  
ATOM   1136 HD21 LEU A 287      17.127   3.622  20.228  1.00 22.27           H  
ATOM   1137 HD22 LEU A 287      18.224   2.871  19.359  1.00 22.27           H  
ATOM   1138 HD23 LEU A 287      17.167   3.824  18.653  1.00 22.27           H  
ATOM   1139  N   SER A 288      18.189   1.124  15.336  1.00 14.31           N  
ANISOU 1139  N   SER A 288     1582   2112   1743   -678    515   -290       N  
ATOM   1140  CA  SER A 288      18.754   0.497  14.152  1.00 15.18           C  
ANISOU 1140  CA  SER A 288     1644   2328   1796   -661    591   -297       C  
ATOM   1141  C   SER A 288      18.106  -0.855  13.904  1.00 14.62           C  
ANISOU 1141  C   SER A 288     1609   2229   1717   -452    524   -276       C  
ATOM   1142  O   SER A 288      17.750  -1.582  14.832  1.00 15.87           O  
ANISOU 1142  O   SER A 288     1747   2367   1916   -319    422   -278       O  
ATOM   1143  CB  SER A 288      20.263   0.315  14.313  1.00 18.59           C  
ANISOU 1143  CB  SER A 288     1841   3000   2224   -707    642   -420       C  
ATOM   1144  OG  SER A 288      20.763  -0.435  13.221  1.00 19.87           O  
ANISOU 1144  OG  SER A 288     1934   3288   2328   -653    715   -458       O  
ATOM   1145  H   SER A 288      18.741   1.237  15.986  1.00 17.21           H  
ATOM   1146  HA  SER A 288      18.592   1.067  13.383  1.00 18.26           H  
ATOM   1147  HB2 SER A 288      20.692   1.184  14.330  1.00 22.35           H  
ATOM   1148  HB3 SER A 288      20.443  -0.161  15.139  1.00 22.35           H  
ATOM   1149  HG  SER A 288      21.593  -0.540  13.301  1.00 23.88           H  
ATOM   1150  N   GLY A 289      17.985  -1.206  12.632  1.00 14.87           N  
ANISOU 1150  N   GLY A 289     1697   2265   1686   -438    582   -256       N  
ATOM   1151  CA  GLY A 289      17.577  -2.530  12.255  1.00 17.73           C  
ANISOU 1151  CA  GLY A 289     2077   2615   2046   -256    528   -272       C  
ATOM   1152  C   GLY A 289      18.718  -3.494  12.104  1.00 16.65           C  
ANISOU 1152  C   GLY A 289     1760   2656   1911   -153    546   -398       C  
ATOM   1153  O   GLY A 289      18.500  -4.675  11.821  1.00 16.50           O  
ANISOU 1153  O   GLY A 289     1750   2610   1908     12    491   -435       O  
ATOM   1154  H   GLY A 289      18.138  -0.681  11.968  1.00 17.87           H  
ATOM   1155  HA2 GLY A 289      16.976  -2.879  12.932  1.00 21.31           H  
ATOM   1156  HA3 GLY A 289      17.107  -2.486  11.408  1.00 21.31           H  
ATOM   1157  N   HIS A 290      19.956  -3.019  12.236  1.00 15.85           N  
ANISOU 1157  N   HIS A 290     1485   2738   1801   -246    621   -482       N  
ATOM   1158  CA  HIS A 290      21.143  -3.860  12.147  1.00 18.64           C  
ANISOU 1158  CA  HIS A 290     1622   3295   2166   -132    635   -630       C  
ATOM   1159  C   HIS A 290      21.048  -4.632  10.831  1.00 21.52           C  
ANISOU 1159  C   HIS A 290     2020   3690   2467    -46    692   -686       C  
ATOM   1160  O   HIS A 290      20.788  -4.021   9.785  1.00 23.41           O  
ANISOU 1160  O   HIS A 290     2356   3936   2601   -187    802   -641       O  
ATOM   1161  CB  HIS A 290      21.249  -4.702  13.414  1.00 21.70           C  
ANISOU 1161  CB  HIS A 290     1938   3660   2648     52    478   -651       C  
ATOM   1162  CG  HIS A 290      21.243  -3.897  14.679  1.00 22.02           C  
ANISOU 1162  CG  HIS A 290     1961   3689   2717    -45    424   -603       C  
ATOM   1163  ND1 HIS A 290      22.378  -3.284  15.174  1.00 29.11           N  
ANISOU 1163  ND1 HIS A 290     2663   4778   3621   -144    455   -694       N  
ATOM   1164  CD2 HIS A 290      20.238  -3.581  15.533  1.00 24.82           C  
ANISOU 1164  CD2 HIS A 290     2460   3882   3089    -65    346   -495       C  
ATOM   1165  CE1 HIS A 290      22.067  -2.633  16.286  1.00 22.91           C  
ANISOU 1165  CE1 HIS A 290     1917   3936   2853   -217    389   -647       C  
ATOM   1166  NE2 HIS A 290      20.778  -2.798  16.526  1.00 23.73           N  
ANISOU 1166  NE2 HIS A 290     2223   3832   2960   -166    329   -529       N  
ATOM   1167  H   HIS A 290      20.135  -2.191  12.381  1.00 19.06           H  
ATOM   1168  HA  HIS A 290      21.935  -3.303  12.094  1.00 22.41           H  
ATOM   1169  HB2 HIS A 290      20.495  -5.311  13.447  1.00 26.08           H  
ATOM   1170  HB3 HIS A 290      22.079  -5.203  13.386  1.00 26.08           H  
ATOM   1171  HD2 HIS A 290      19.349  -3.844  15.460  1.00 29.82           H  
ATOM   1172  HE1 HIS A 290      22.658  -2.142  16.811  1.00 27.53           H  
ATOM   1173  N   ASN A 291      21.254  -5.938  10.829  1.00 22.81           N  
ANISOU 1173  N   ASN A 291     2118   3867   2682    179    616   -785       N  
ATOM   1174  CA  ASN A 291      21.273  -6.717   9.603  1.00 20.46           C  
ANISOU 1174  CA  ASN A 291     1849   3591   2334    267    653   -865       C  
ATOM   1175  C   ASN A 291      19.877  -7.134   9.153  1.00 21.81           C  
ANISOU 1175  C   ASN A 291     2242   3559   2485    316    603   -792       C  
ATOM   1176  O   ASN A 291      19.751  -7.745   8.090  1.00 26.44           O  
ANISOU 1176  O   ASN A 291     2867   4166   3012    380    635   -874       O  
ATOM   1177  CB  ASN A 291      22.129  -7.971   9.804  1.00 24.38           C  
ANISOU 1177  CB  ASN A 291     2214   4128   2922    485    555   -992       C  
ATOM   1178  CG  ASN A 291      21.749  -8.727  11.067  1.00 19.78           C  
ANISOU 1178  CG  ASN A 291     1654   3398   2465    662    385   -955       C  
ATOM   1179  OD1 ASN A 291      21.716  -8.157  12.164  1.00 24.00           O  
ANISOU 1179  OD1 ASN A 291     2149   3941   3030    616    346   -889       O  
ATOM   1180  ND2 ASN A 291      21.452 -10.009  10.926  1.00 20.64           N  
ANISOU 1180  ND2 ASN A 291     1839   3359   2643    848    275   -985       N  
ATOM   1181  H   ASN A 291      21.387  -6.406  11.538  1.00 27.41           H  
ATOM   1182  HA  ASN A 291      21.672  -6.183   8.899  1.00 24.59           H  
ATOM   1183  HB2 ASN A 291      22.006  -8.565   9.047  1.00 29.30           H  
ATOM   1184  HB3 ASN A 291      23.061  -7.712   9.875  1.00 29.30           H  
ATOM   1185 HD21 ASN A 291      21.231 -10.477  11.612  1.00 24.80           H  
ATOM   1186 HD22 ASN A 291      21.479 -10.373  10.147  1.00 24.80           H  
ATOM   1187  N   LEU A 292      18.840  -6.789   9.915  1.00 18.58           N  
ANISOU 1187  N   LEU A 292     1981   2955   2123    273    513   -636       N  
ATOM   1188  CA  LEU A 292      17.494  -7.251   9.638  1.00 18.91           C  
ANISOU 1188  CA  LEU A 292     2216   2797   2173    317    434   -558       C  
ATOM   1189  C   LEU A 292      16.657  -6.229   8.889  1.00 19.67           C  
ANISOU 1189  C   LEU A 292     2459   2848   2166    156    495   -451       C  
ATOM   1190  O   LEU A 292      15.703  -6.609   8.202  1.00 22.16           O  
ANISOU 1190  O   LEU A 292     2905   3066   2447    186    455   -428       O  
ATOM   1191  CB  LEU A 292      16.787  -7.604  10.951  1.00 18.52           C  
ANISOU 1191  CB  LEU A 292     2223   2580   2232    377    296   -460       C  
ATOM   1192  CG  LEU A 292      17.486  -8.653  11.813  1.00 20.93           C  
ANISOU 1192  CG  LEU A 292     2424   2890   2638    547    196   -520       C  
ATOM   1193  CD1 LEU A 292      16.728  -8.840  13.113  1.00 22.59           C  
ANISOU 1193  CD1 LEU A 292     2712   2957   2912    558     77   -388       C  
ATOM   1194  CD2 LEU A 292      17.636  -9.969  11.046  1.00 28.85           C  
ANISOU 1194  CD2 LEU A 292     3433   3850   3677    719    156   -643       C  
ATOM   1195  H   LEU A 292      18.897  -6.281  10.607  1.00 22.33           H  
ATOM   1196  HA  LEU A 292      17.540  -8.052   9.094  1.00 22.73           H  
ATOM   1197  HB2 LEU A 292      16.711  -6.796  11.483  1.00 22.25           H  
ATOM   1198  HB3 LEU A 292      15.904  -7.946  10.739  1.00 22.25           H  
ATOM   1199  HG  LEU A 292      18.381  -8.352  12.035  1.00 25.15           H  
ATOM   1200 HD11 LEU A 292      17.182  -9.507  13.650  1.00 27.14           H  
ATOM   1201 HD12 LEU A 292      16.701  -7.995  13.588  1.00 27.14           H  
ATOM   1202 HD13 LEU A 292      15.826  -9.135  12.913  1.00 27.14           H  
ATOM   1203 HD21 LEU A 292      18.062 -10.623  11.621  1.00 34.65           H  
ATOM   1204 HD22 LEU A 292      16.757 -10.283  10.782  1.00 34.65           H  
ATOM   1205 HD23 LEU A 292      18.182  -9.815  10.259  1.00 34.65           H  
ATOM   1206  N   ALA A 293      16.980  -4.952   9.002  1.00 16.05           N  
ANISOU 1206  N   ALA A 293     1988   2447   1664    -12    574   -385       N  
ATOM   1207  CA  ALA A 293      16.181  -3.892   8.411  1.00 18.03           C  
ANISOU 1207  CA  ALA A 293     2398   2616   1836   -152    605   -260       C  
ATOM   1208  C   ALA A 293      17.003  -2.629   8.504  1.00 17.05           C  
ANISOU 1208  C   ALA A 293     2224   2577   1677   -340    709   -227       C  
ATOM   1209  O   ALA A 293      18.011  -2.574   9.214  1.00 19.61           O  
ANISOU 1209  O   ALA A 293     2384   3012   2053   -360    739   -301       O  
ATOM   1210  CB  ALA A 293      14.843  -3.709   9.128  1.00 17.33           C  
ANISOU 1210  CB  ALA A 293     2436   2325   1825   -121    488   -153       C  
ATOM   1211  H   ALA A 293      17.672  -4.667   9.425  1.00 19.30           H  
ATOM   1212  HA  ALA A 293      15.996  -4.101   7.482  1.00 21.67           H  
ATOM   1213  HB1 ALA A 293      14.346  -2.999   8.692  1.00 20.83           H  
ATOM   1214  HB2 ALA A 293      14.344  -4.539   9.081  1.00 20.83           H  
ATOM   1215  HB3 ALA A 293      15.011  -3.475  10.054  1.00 20.83           H  
ATOM   1216  N   LYS A 294      16.550  -1.594   7.804  1.00 17.39           N  
ANISOU 1216  N   LYS A 294     2415   2557   1636   -482    751   -111       N  
ATOM   1217  CA  LYS A 294      17.170  -0.288   8.020  1.00 18.05           C  
ANISOU 1217  CA  LYS A 294     2492   2652   1714   -686    830    -55       C  
ATOM   1218  C   LYS A 294      16.908   0.168   9.450  1.00 15.73           C  
ANISOU 1218  C   LYS A 294     2181   2232   1565   -674    745    -44       C  
ATOM   1219  O   LYS A 294      17.824   0.575  10.173  1.00 18.75           O  
ANISOU 1219  O   LYS A 294     2432   2695   1996   -762    783   -103       O  
ATOM   1220  CB  LYS A 294      16.652   0.747   7.014  1.00 18.61           C  
ANISOU 1220  CB  LYS A 294     2743   2616   1713   -787    817     90       C  
ATOM   1221  CG  LYS A 294      17.304   2.104   7.142  1.00 27.61           C  
ANISOU 1221  CG  LYS A 294     3884   3719   2889   -954    841    144       C  
ATOM   1222  CD  LYS A 294      16.812   3.075   6.068  1.00 30.72           C  
ANISOU 1222  CD  LYS A 294     4453   4007   3213  -1024    816    289       C  
ATOM   1223  H   LYS A 294      15.914  -1.617   7.226  1.00 20.91           H  
ATOM   1224  HA  LYS A 294      18.126  -0.362   7.872  1.00 21.69           H  
ATOM   1225  HB2 LYS A 294      16.821   0.422   6.116  1.00 22.37           H  
ATOM   1226  HB3 LYS A 294      15.699   0.864   7.150  1.00 22.37           H  
ATOM   1227  HG2 LYS A 294      17.093   2.480   8.011  1.00 33.17           H  
ATOM   1228  HG3 LYS A 294      18.265   2.008   7.047  1.00 33.17           H  
ATOM   1229  N   HIS A 295      15.651   0.060   9.893  1.00 14.27           N  
ANISOU 1229  N   HIS A 295     2459   1224   1740   -375    941     79       N  
ATOM   1230  CA  HIS A 295      15.224   0.479  11.220  1.00 14.82           C  
ANISOU 1230  CA  HIS A 295     2444   1344   1846   -419    797     82       C  
ATOM   1231  C   HIS A 295      14.454  -0.638  11.905  1.00 13.64           C  
ANISOU 1231  C   HIS A 295     2242   1239   1703   -335    738     74       C  
ATOM   1232  O   HIS A 295      13.790  -1.465  11.259  1.00 13.08           O  
ANISOU 1232  O   HIS A 295     2281   1129   1560   -260    765     34       O  
ATOM   1233  CB  HIS A 295      14.331   1.696  11.144  1.00 15.30           C  
ANISOU 1233  CB  HIS A 295     2694   1323   1796   -436    692     45       C  
ATOM   1234  CG  HIS A 295      14.937   2.852  10.434  1.00 20.52           C  
ANISOU 1234  CG  HIS A 295     3444   1906   2444   -505    767     63       C  
ATOM   1235  ND1 HIS A 295      15.923   3.629  10.995  1.00 23.10           N  
ANISOU 1235  ND1 HIS A 295     3665   2236   2874   -652    798     63       N  
ATOM   1236  CD2 HIS A 295      14.708   3.363   9.202  1.00 29.45           C  
ANISOU 1236  CD2 HIS A 295     4764   2959   3466   -467    822     89       C  
ATOM   1237  CE1 HIS A 295      16.264   4.582  10.145  1.00 27.37           C  
ANISOU 1237  CE1 HIS A 295     4335   2678   3386   -694    885     84       C  
ATOM   1238  NE2 HIS A 295      15.546   4.440   9.046  1.00 33.92           N  
ANISOU 1238  NE2 HIS A 295     5344   3458   4086   -572    903    112       N  
ATOM   1239  H   HIS A 295      15.009  -0.265   9.422  1.00 17.16           H  
ATOM   1240  HA  HIS A 295      16.010   0.682  11.751  1.00 17.83           H  
ATOM   1241  HB2 HIS A 295      13.518   1.455  10.673  1.00 18.39           H  
ATOM   1242  HB3 HIS A 295      14.120   1.982  12.046  1.00 18.39           H  
ATOM   1243  HD2 HIS A 295      14.096   3.045   8.577  1.00 35.37           H  
ATOM   1244  HE1 HIS A 295      16.901   5.242  10.295  1.00 32.88           H  
ATOM   1245  N   CYS A 296      14.515  -0.661  13.242  1.00 11.56           N  
ANISOU 1245  N   CYS A 296     1802   1082   1509   -358    634     94       N  
ATOM   1246  CA  CYS A 296      13.620  -1.492  14.037  1.00 13.41           C  
ANISOU 1246  CA  CYS A 296     1987   1380   1728   -262    523     80       C  
ATOM   1247  C   CYS A 296      12.713  -0.552  14.818  1.00  9.80           C  
ANISOU 1247  C   CYS A 296     1588    946   1188   -291    350      5       C  
ATOM   1248  O   CYS A 296      13.199   0.306  15.572  1.00 11.19           O  
ANISOU 1248  O   CYS A 296     1700   1175   1375   -394    295    -18       O  
ATOM   1249  CB  CYS A 296      14.360  -2.413  15.001  1.00 11.30           C  
ANISOU 1249  CB  CYS A 296     1460   1253   1582   -212    535    188       C  
ATOM   1250  SG  CYS A 296      13.213  -3.415  15.996  1.00 12.33           S  
ANISOU 1250  SG  CYS A 296     1566   1434   1683   -109    433    194       S  
ATOM   1251  H   CYS A 296      15.071  -0.200  13.708  1.00 13.91           H  
ATOM   1252  HA  CYS A 296      13.104  -2.059  13.442  1.00 16.13           H  
ATOM   1253  HB2 CYS A 296      14.929  -3.014  14.494  1.00 13.60           H  
ATOM   1254  HB3 CYS A 296      14.899  -1.877  15.604  1.00 13.60           H  
ATOM   1255  HG  CYS A 296      13.847  -4.121  16.730  1.00 14.83           H  
ATOM   1256  N   LEU A 297      11.409  -0.726  14.642  1.00  8.24           N  
ANISOU 1256  N   LEU A 297     1506    716    910   -213    283    -42       N  
ATOM   1257  CA  LEU A 297      10.405  -0.024  15.427  1.00 11.62           C  
ANISOU 1257  CA  LEU A 297     1965   1167   1283   -185    159   -101       C  
ATOM   1258  C   LEU A 297      10.034  -0.935  16.584  1.00  9.04           C  
ANISOU 1258  C   LEU A 297     1489    973    973   -150    101    -93       C  
ATOM   1259  O   LEU A 297       9.350  -1.943  16.387  1.00  8.84           O  
ANISOU 1259  O   LEU A 297     1452    959    946    -95    110    -80       O  
ATOM   1260  CB  LEU A 297       9.195   0.314  14.560  1.00 11.11           C  
ANISOU 1260  CB  LEU A 297     2052   1039   1131   -102    119   -115       C  
ATOM   1261  CG  LEU A 297       8.087   1.031  15.315  1.00 10.67           C  
ANISOU 1261  CG  LEU A 297     2004    999   1050    -22     33   -154       C  
ATOM   1262  CD1 LEU A 297       8.469   2.461  15.652  1.00 10.75           C  
ANISOU 1262  CD1 LEU A 297     2123    883   1079    -54     73   -189       C  
ATOM   1263  CD2 LEU A 297       6.774   0.974  14.522  1.00  9.26           C  
ANISOU 1263  CD2 LEU A 297     1868    852    797     88    -35   -122       C  
ATOM   1264  H   LEU A 297      11.072  -1.261  14.059  1.00  9.93           H  
ATOM   1265  HA  LEU A 297      10.755   0.810  15.776  1.00 13.98           H  
ATOM   1266  HB2 LEU A 297       9.482   0.891  13.835  1.00 13.37           H  
ATOM   1267  HB3 LEU A 297       8.827  -0.510  14.204  1.00 13.37           H  
ATOM   1268  HG  LEU A 297       7.946   0.576  16.160  1.00 12.84           H  
ATOM   1269 HD11 LEU A 297       7.736   2.880  16.129  1.00 12.94           H  
ATOM   1270 HD12 LEU A 297       9.264   2.453  16.208  1.00 12.94           H  
ATOM   1271 HD13 LEU A 297       8.646   2.943  14.829  1.00 12.94           H  
ATOM   1272 HD21 LEU A 297       6.087   1.450  15.014  1.00 11.14           H  
ATOM   1273 HD22 LEU A 297       6.910   1.390  13.656  1.00 11.14           H  
ATOM   1274 HD23 LEU A 297       6.515   0.046  14.406  1.00 11.14           H  
ATOM   1275  N   HIS A 298      10.458  -0.564  17.797  1.00  8.45           N  
ANISOU 1275  N   HIS A 298     1315   1002    892   -208     47   -104       N  
ATOM   1276  CA  HIS A 298      10.158  -1.328  19.003  1.00  8.16           C  
ANISOU 1276  CA  HIS A 298     1151   1116    833   -180     -6    -70       C  
ATOM   1277  C   HIS A 298       8.835  -0.790  19.536  1.00  8.80           C  
ANISOU 1277  C   HIS A 298     1313   1193    836   -136    -54   -166       C  
ATOM   1278  O   HIS A 298       8.761   0.406  19.858  1.00 10.77           O  
ANISOU 1278  O   HIS A 298     1655   1400   1039   -181    -64   -263       O  
ATOM   1279  CB  HIS A 298      11.230  -1.154  20.058  1.00  9.32           C  
ANISOU 1279  CB  HIS A 298     1150   1436    955   -281    -62    -29       C  
ATOM   1280  CG  HIS A 298      12.579  -1.657  19.635  1.00  9.22           C  
ANISOU 1280  CG  HIS A 298      985   1474   1046   -298     -9    100       C  
ATOM   1281  ND1 HIS A 298      12.984  -2.958  19.861  1.00  9.94           N  
ANISOU 1281  ND1 HIS A 298      918   1645   1213   -189     36    274       N  
ATOM   1282  CD2 HIS A 298      13.614  -1.039  18.999  1.00 11.60           C  
ANISOU 1282  CD2 HIS A 298     1257   1747   1404   -398     39    100       C  
ATOM   1283  CE1 HIS A 298      14.225  -3.100  19.420  1.00 10.79           C  
ANISOU 1283  CE1 HIS A 298      881   1791   1427   -196    104    378       C  
ATOM   1284  NE2 HIS A 298      14.623  -1.962  18.872  1.00 14.69           N  
ANISOU 1284  NE2 HIS A 298     1442   2232   1908   -336    106    269       N  
ATOM   1285  H   HIS A 298      10.929   0.140  17.945  1.00 10.17           H  
ATOM   1286  HA  HIS A 298      10.103  -2.273  18.795  1.00  9.83           H  
ATOM   1287  HB2 HIS A 298      11.317  -0.210  20.262  1.00 11.22           H  
ATOM   1288  HB3 HIS A 298      10.968  -1.643  20.854  1.00 11.22           H  
ATOM   1289  HD2 HIS A 298      13.634  -0.157  18.706  1.00 13.95           H  
ATOM   1290  HE1 HIS A 298      14.734  -3.875  19.484  1.00 12.77           H  
ATOM   1291  N   VAL A 299       7.812  -1.649  19.632  1.00  8.00           N  
ANISOU 1291  N   VAL A 299     1180   1124    736    -58    -52   -143       N  
ATOM   1292  CA  VAL A 299       6.456  -1.255  20.010  1.00  8.26           C  
ANISOU 1292  CA  VAL A 299     1240   1175    723      8    -71   -210       C  
ATOM   1293  C   VAL A 299       6.031  -2.079  21.212  1.00  9.34           C  
ANISOU 1293  C   VAL A 299     1272   1452    823     10    -65   -174       C  
ATOM   1294  O   VAL A 299       6.174  -3.307  21.191  1.00 10.01           O  
ANISOU 1294  O   VAL A 299     1290   1560    956      5    -34    -78       O  
ATOM   1295  CB  VAL A 299       5.460  -1.451  18.862  1.00  9.10           C  
ANISOU 1295  CB  VAL A 299     1377   1229    853     72    -80   -209       C  
ATOM   1296  CG1 VAL A 299       4.056  -0.986  19.300  1.00 12.99           C  
ANISOU 1296  CG1 VAL A 299     1830   1783   1324    167    -96   -247       C  
ATOM   1297  CG2 VAL A 299       5.868  -0.669  17.619  1.00  8.96           C  
ANISOU 1297  CG2 VAL A 299     1484   1088    833     79    -82   -208       C  
ATOM   1298  H   VAL A 299       7.886  -2.492  19.476  1.00  9.64           H  
ATOM   1299  HA  VAL A 299       6.464  -0.318  20.259  1.00  9.95           H  
ATOM   1300  HB  VAL A 299       5.448  -2.395  18.638  1.00 10.96           H  
ATOM   1301 HG11 VAL A 299       3.439  -1.104  18.560  1.00 15.63           H  
ATOM   1302 HG12 VAL A 299       3.769  -1.519  20.058  1.00 15.63           H  
ATOM   1303 HG13 VAL A 299       4.097  -0.050  19.550  1.00 15.63           H  
ATOM   1304 HG21 VAL A 299       5.212  -0.820  16.921  1.00 10.79           H  
ATOM   1305 HG22 VAL A 299       5.907   0.275  17.839  1.00 10.79           H  
ATOM   1306 HG23 VAL A 299       6.740  -0.976  17.325  1.00 10.79           H  
ATOM   1307  N   VAL A 300       5.505  -1.408  22.247  1.00  8.86           N  
ANISOU 1307  N   VAL A 300     1227   1461    678     19    -61   -248       N  
ATOM   1308  CA  VAL A 300       5.045  -2.073  23.464  1.00 10.66           C  
ANISOU 1308  CA  VAL A 300     1378   1839    832     15    -35   -211       C  
ATOM   1309  C   VAL A 300       3.522  -2.169  23.442  1.00  9.86           C  
ANISOU 1309  C   VAL A 300     1238   1747    760     98     20   -244       C  
ATOM   1310  O   VAL A 300       2.814  -1.154  23.568  1.00 11.56           O  
ANISOU 1310  O   VAL A 300     1498   1934    959    172     58   -341       O  
ATOM   1311  CB  VAL A 300       5.500  -1.339  24.720  1.00 10.02           C  
ANISOU 1311  CB  VAL A 300     1343   1856    609    -60    -45   -278       C  
ATOM   1312  CG1 VAL A 300       5.033  -2.118  25.918  1.00 10.67           C  
ANISOU 1312  CG1 VAL A 300     1359   2088    606    -60    -11   -204       C  
ATOM   1313  CG2 VAL A 300       6.988  -1.192  24.720  1.00 10.22           C  
ANISOU 1313  CG2 VAL A 300     1348   1914    621   -167   -122   -237       C  
ATOM   1314  H   VAL A 300       5.404  -0.554  22.262  1.00 10.67           H  
ATOM   1315  HA  VAL A 300       5.410  -2.972  23.460  1.00 12.82           H  
ATOM   1316  HB  VAL A 300       5.122  -0.446  24.752  1.00 12.06           H  
ATOM   1317 HG11 VAL A 300       5.349  -1.679  26.723  1.00 12.84           H  
ATOM   1318 HG12 VAL A 300       4.063  -2.148  25.917  1.00 12.84           H  
ATOM   1319 HG13 VAL A 300       5.391  -3.018  25.869  1.00 12.84           H  
ATOM   1320 HG21 VAL A 300       7.259  -0.726  25.526  1.00 12.30           H  
ATOM   1321 HG22 VAL A 300       7.392  -2.073  24.696  1.00 12.30           H  
ATOM   1322 HG23 VAL A 300       7.255  -0.684  23.938  1.00 12.30           H  
ATOM   1323  N   GLY A 301       3.005  -3.352  23.224  1.00  9.49           N  
ANISOU 1323  N   GLY A 301     1104   1728    775     87     45   -161       N  
ATOM   1324  CA  GLY A 301       1.585  -3.608  23.434  1.00  8.74           C  
ANISOU 1324  CA  GLY A 301      913   1707    702    119    101   -176       C  
ATOM   1325  C   GLY A 301       1.293  -3.867  24.893  1.00  9.78           C  
ANISOU 1325  C   GLY A 301     1014   1967    735    106    189   -150       C  
ATOM   1326  O   GLY A 301       2.164  -4.141  25.685  1.00 11.87           O  
ANISOU 1326  O   GLY A 301     1321   2285    904     61    184    -86       O  
ATOM   1327  H   GLY A 301       3.451  -4.035  22.950  1.00 11.43           H  
ATOM   1328  HA2 GLY A 301       1.068  -2.840  23.145  1.00 10.31           H  
ATOM   1329  HA3 GLY A 301       1.314  -4.384  22.920  1.00 10.31           H  
ATOM   1330  N   PRO A 302       0.011  -3.825  25.249  1.00 11.41           N  
ANISOU 1330  N   PRO A 302     1123   2257    954    146    274   -178       N  
ATOM   1331  CA  PRO A 302      -0.356  -4.094  26.645  1.00 12.19           C  
ANISOU 1331  CA  PRO A 302     1206   2488    937    128    394   -152       C  
ATOM   1332  C   PRO A 302      -0.113  -5.551  26.987  1.00 12.32           C  
ANISOU 1332  C   PRO A 302     1195   2523    961     29    432      9       C  
ATOM   1333  O   PRO A 302      -0.342  -6.452  26.173  1.00 13.46           O  
ANISOU 1333  O   PRO A 302     1284   2588   1242    -33    434     61       O  
ATOM   1334  CB  PRO A 302      -1.852  -3.760  26.710  1.00 13.55           C  
ANISOU 1334  CB  PRO A 302     1250   2711   1186    201    490   -201       C  
ATOM   1335  CG  PRO A 302      -2.324  -3.960  25.310  1.00 12.97           C  
ANISOU 1335  CG  PRO A 302     1050   2619   1259    207    404   -194       C  
ATOM   1336  CD  PRO A 302      -1.188  -3.499  24.433  1.00 12.49           C  
ANISOU 1336  CD  PRO A 302     1134   2411   1199    217    269   -217       C  
ATOM   1337  HA  PRO A 302       0.133  -3.511  27.247  1.00 14.45           H  
ATOM   1338  HB2 PRO A 302      -2.302  -4.363  27.322  1.00 16.08           H  
ATOM   1339  HB3 PRO A 302      -1.978  -2.842  26.996  1.00 16.08           H  
ATOM   1340  HG2 PRO A 302      -2.517  -4.899  25.159  1.00 15.39           H  
ATOM   1341  HG3 PRO A 302      -3.119  -3.428  25.152  1.00 15.39           H  
ATOM   1342  HD2 PRO A 302      -1.179  -3.984  23.593  1.00 15.02           H  
ATOM   1343  HD3 PRO A 302      -1.244  -2.545  24.265  1.00 15.02           H  
ATOM   1344  N   ASN A 303       0.320  -5.776  28.219  1.00 15.58           N  
ANISOU 1344  N   ASN A 303     1680   2988   1252      7    453     85       N  
ATOM   1345  CA  ASN A 303       0.399  -7.119  28.775  1.00 14.22           C  
ANISOU 1345  CA  ASN A 303     1505   2805   1093    -46    519    266       C  
ATOM   1346  C   ASN A 303      -0.910  -7.326  29.517  1.00 16.46           C  
ANISOU 1346  C   ASN A 303     1744   3136   1376    -70    662    249       C  
ATOM   1347  O   ASN A 303      -1.066  -6.947  30.686  1.00 17.36           O  
ANISOU 1347  O   ASN A 303     1916   3338   1342    -58    711    235       O  
ATOM   1348  CB  ASN A 303       1.612  -7.283  29.683  1.00 16.40           C  
ANISOU 1348  CB  ASN A 303     1854   3144   1232    -39    444    388       C  
ATOM   1349  CG  ASN A 303       1.749  -8.698  30.205  1.00 16.32           C  
ANISOU 1349  CG  ASN A 303     1852   3092   1257    -47    520    606       C  
ATOM   1350  OD1 ASN A 303       0.835  -9.498  30.094  1.00 19.13           O  
ANISOU 1350  OD1 ASN A 303     2193   3358   1716    -93    656    635       O  
ATOM   1351  ND2 ASN A 303       2.902  -9.004  30.786  1.00 23.60           N  
ANISOU 1351  ND2 ASN A 303     2786   4077   2104     -7    435    758       N  
ATOM   1352  H   ASN A 303       0.576  -5.159  28.761  1.00 18.73           H  
ATOM   1353  HA  ASN A 303       0.493  -7.778  28.069  1.00 17.10           H  
ATOM   1354  HB2 ASN A 303       2.414  -7.066  29.183  1.00 19.71           H  
ATOM   1355  HB3 ASN A 303       1.523  -6.687  30.443  1.00 19.71           H  
ATOM   1356 HD21 ASN A 303       3.030  -9.794  31.099  1.00 28.35           H  
ATOM   1357 HD22 ASN A 303       3.522  -8.411  30.849  1.00 28.35           H  
ATOM   1358  N   VAL A 304      -1.897  -7.868  28.804  1.00 19.05           N  
ANISOU 1358  N   VAL A 304     1961   3413   1866   -122    732    234       N  
ATOM   1359  CA  VAL A 304      -3.203  -8.030  29.411  1.00 20.89           C  
ANISOU 1359  CA  VAL A 304     2109   3700   2129   -152    873    218       C  
ATOM   1360  C   VAL A 304      -3.154  -9.081  30.508  1.00 27.16           C  
ANISOU 1360  C   VAL A 304     2986   4474   2861   -218   1000    364       C  
ATOM   1361  O   VAL A 304      -3.976  -9.040  31.431  1.00 26.09           O  
ANISOU 1361  O   VAL A 304     2833   4408   2671   -228   1135    361       O  
ATOM   1362  CB  VAL A 304      -4.264  -8.384  28.347  1.00 29.22           C  
ANISOU 1362  CB  VAL A 304     2987   4739   3375   -226    884    170       C  
ATOM   1363  CG1 VAL A 304      -4.356  -7.276  27.318  1.00 30.91           C  
ANISOU 1363  CG1 VAL A 304     3120   5002   3624   -136    747     48       C  
ATOM   1364  CG2 VAL A 304      -3.954  -9.701  27.684  1.00 28.65           C  
ANISOU 1364  CG2 VAL A 304     2947   4524   3414   -369    905    249       C  
ATOM   1365  H   VAL A 304      -1.832  -8.139  27.990  1.00 22.90           H  
ATOM   1366  HA  VAL A 304      -3.470  -7.186  29.807  1.00 25.11           H  
ATOM   1367  HB  VAL A 304      -5.125  -8.475  28.785  1.00 35.10           H  
ATOM   1368 HG11 VAL A 304      -5.026  -7.513  26.657  1.00 37.13           H  
ATOM   1369 HG12 VAL A 304      -4.609  -6.452  27.763  1.00 37.13           H  
ATOM   1370 HG13 VAL A 304      -3.492  -7.169  26.890  1.00 37.13           H  
ATOM   1371 HG21 VAL A 304      -4.640  -9.893  27.026  1.00 34.41           H  
ATOM   1372 HG22 VAL A 304      -3.088  -9.640  27.251  1.00 34.41           H  
ATOM   1373 HG23 VAL A 304      -3.938 -10.398  28.358  1.00 34.41           H  
ATOM   1374  N   ASN A 305      -2.192 -10.014  30.451  1.00 20.48           N  
ANISOU 1374  N   ASN A 305     2236   3528   2018   -250    974    504       N  
ATOM   1375  CA  ASN A 305      -2.081 -11.001  31.532  1.00 22.05           C  
ANISOU 1375  CA  ASN A 305     2528   3711   2140   -291   1082    670       C  
ATOM   1376  C   ASN A 305      -1.670 -10.357  32.844  1.00 28.83           C  
ANISOU 1376  C   ASN A 305     3464   4736   2756   -220   1045    705       C  
ATOM   1377  O   ASN A 305      -1.921 -10.940  33.910  1.00 29.98           O  
ANISOU 1377  O   ASN A 305     3673   4921   2796   -255   1156    819       O  
ATOM   1378  CB  ASN A 305      -1.085 -12.090  31.147  1.00 25.08           C  
ANISOU 1378  CB  ASN A 305     2989   3940   2600   -294   1054    832       C  
ATOM   1379  CG  ASN A 305      -1.701 -13.173  30.257  1.00 25.61           C  
ANISOU 1379  CG  ASN A 305     3040   3832   2859   -448   1164    812       C  
ATOM   1380  OD1 ASN A 305      -2.919 -13.217  30.079  1.00 33.62           O  
ANISOU 1380  OD1 ASN A 305     3960   4886   3928   -589   1258    696       O  
ATOM   1381  ND2 ASN A 305      -0.866 -14.026  29.701  1.00 43.43           N  
ANISOU 1381  ND2 ASN A 305     5372   5910   5219   -423   1150    920       N  
ATOM   1382  H   ASN A 305      -1.612 -10.093  29.820  1.00 24.62           H  
ATOM   1383  HA  ASN A 305      -2.944 -11.424  31.663  1.00 26.50           H  
ATOM   1384  HB2 ASN A 305      -0.349 -11.687  30.661  1.00 30.13           H  
ATOM   1385  HB3 ASN A 305      -0.757 -12.517  31.953  1.00 30.13           H  
ATOM   1386 HD21 ASN A 305      -1.165 -14.652  29.193  1.00 52.15           H  
ATOM   1387 HD22 ASN A 305      -0.021 -13.958  29.847  1.00 52.15           H  
ATOM   1388  N   LYS A 306      -1.053  -9.174  32.798  1.00 23.83           N  
ANISOU 1388  N   LYS A 306     2843   4196   2016   -150    901    597       N  
ATOM   1389  CA  LYS A 306      -0.739  -8.411  33.996  1.00 23.76           C  
ANISOU 1389  CA  LYS A 306     2925   4341   1760   -133    871    562       C  
ATOM   1390  C   LYS A 306      -1.685  -7.230  34.196  1.00 24.22           C  
ANISOU 1390  C   LYS A 306     2987   4439   1779   -115    964    347       C  
ATOM   1391  O   LYS A 306      -1.345  -6.280  34.907  1.00 32.32           O  
ANISOU 1391  O   LYS A 306     4122   5542   2618   -108    936    241       O  
ATOM   1392  CB  LYS A 306       0.709  -7.939  33.948  1.00 27.04           C  
ANISOU 1392  CB  LYS A 306     3372   4820   2080   -108    663    578       C  
ATOM   1393  CG  LYS A 306       1.704  -9.086  33.860  1.00 27.65           C  
ANISOU 1393  CG  LYS A 306     3423   4870   2214    -77    591    822       C  
ATOM   1394  CD  LYS A 306       3.124  -8.617  34.116  1.00 42.55           C  
ANISOU 1394  CD  LYS A 306     5292   6889   3987    -62    394    858       C  
ATOM   1395  CE  LYS A 306       4.109  -9.781  34.055  1.00 46.08           C  
ANISOU 1395  CE  LYS A 306     5671   7317   4522     19    350   1130       C  
ATOM   1396  NZ  LYS A 306       3.644 -10.935  34.874  1.00 48.77           N  
ANISOU 1396  NZ  LYS A 306     6061   7637   4833     43    482   1334       N  
ATOM   1397  H   LYS A 306      -0.804  -8.791  32.070  1.00 28.63           H  
ATOM   1398  HA  LYS A 306      -0.835  -8.990  34.768  1.00 28.54           H  
ATOM   1399  HB2 LYS A 306       0.832  -7.376  33.168  1.00 32.48           H  
ATOM   1400  HB3 LYS A 306       0.903  -7.436  34.755  1.00 32.48           H  
ATOM   1401  HG2 LYS A 306       1.480  -9.756  34.526  1.00 33.22           H  
ATOM   1402  HG3 LYS A 306       1.667  -9.475  32.973  1.00 33.22           H  
ATOM   1403  HD2 LYS A 306       3.376  -7.968  33.440  1.00 51.10           H  
ATOM   1404  HD3 LYS A 306       3.178  -8.216  34.997  1.00 51.10           H  
ATOM   1405  HE2 LYS A 306       4.199 -10.077  33.136  1.00 55.34           H  
ATOM   1406  HE3 LYS A 306       4.969  -9.492  34.397  1.00 55.34           H  
ATOM   1407  HZ1 LYS A 306       4.323 -11.489  35.033  1.00 58.56           H  
ATOM   1408  HZ2 LYS A 306       3.320 -10.646  35.651  1.00 58.56           H  
ATOM   1409  HZ3 LYS A 306       3.005 -11.378  34.442  1.00 58.56           H  
ATOM   1410  N   GLY A 307      -2.851  -7.269  33.572  1.00 23.97           N  
ANISOU 1410  N   GLY A 307     2832   4345   1929   -107   1081    281       N  
ATOM   1411  CA  GLY A 307      -3.903  -6.307  33.845  1.00 25.39           C  
ANISOU 1411  CA  GLY A 307     2982   4554   2112    -52   1219    126       C  
ATOM   1412  C   GLY A 307      -3.834  -5.010  33.068  1.00 31.04           C  
ANISOU 1412  C   GLY A 307     3685   5223   2887     42   1145    -45       C  
ATOM   1413  O   GLY A 307      -4.598  -4.084  33.375  1.00 31.78           O  
ANISOU 1413  O   GLY A 307     3785   5306   2981    121   1285   -167       O  
ATOM   1414  H   GLY A 307      -3.061  -7.853  32.977  1.00 28.80           H  
ATOM   1415  HA2 GLY A 307      -4.757  -6.721  33.643  1.00 30.51           H  
ATOM   1416  HA3 GLY A 307      -3.876  -6.082  34.788  1.00 30.51           H  
ATOM   1417  N   GLU A 308      -2.954  -4.903  32.075  1.00 23.66           N  
ANISOU 1417  N   GLU A 308     2745   4236   2010     46    961    -50       N  
ATOM   1418  CA  GLU A 308      -2.859  -3.677  31.297  1.00 21.11           C  
ANISOU 1418  CA  GLU A 308     2434   3842   1746    135    904   -198       C  
ATOM   1419  C   GLU A 308      -4.013  -3.628  30.304  1.00 23.55           C  
ANISOU 1419  C   GLU A 308     2540   4134   2274    214    944   -213       C  
ATOM   1420  O   GLU A 308      -4.467  -4.658  29.810  1.00 25.49           O  
ANISOU 1420  O   GLU A 308     2639   4409   2635    147    928   -117       O  
ATOM   1421  CB  GLU A 308      -1.498  -3.584  30.604  1.00 24.33           C  
ANISOU 1421  CB  GLU A 308     2908   4203   2133    102    709   -191       C  
ATOM   1422  CG  GLU A 308      -0.365  -3.523  31.641  1.00 25.74           C  
ANISOU 1422  CG  GLU A 308     3238   4440   2102     19    638   -167       C  
ATOM   1423  CD  GLU A 308       1.028  -3.441  31.040  1.00 26.94           C  
ANISOU 1423  CD  GLU A 308     3414   4566   2258    -24    452   -141       C  
ATOM   1424  OE1 GLU A 308       1.985  -3.164  31.813  1.00 29.10           O  
ANISOU 1424  OE1 GLU A 308     3772   4906   2380    -98    368   -142       O  
ATOM   1425  OE2 GLU A 308       1.185  -3.662  29.836  1.00 19.27           O  
ANISOU 1425  OE2 GLU A 308     2367   3523   1431      6    392   -118       O  
ATOM   1426  H   GLU A 308      -2.408  -5.522  31.835  1.00 28.43           H  
ATOM   1427  HA  GLU A 308      -2.924  -2.895  31.869  1.00 25.37           H  
ATOM   1428  HB2 GLU A 308      -1.364  -4.366  30.046  1.00 29.23           H  
ATOM   1429  HB3 GLU A 308      -1.464  -2.780  30.062  1.00 29.23           H  
ATOM   1430  HG2 GLU A 308      -0.492  -2.736  32.194  1.00 30.92           H  
ATOM   1431  HG3 GLU A 308      -0.402  -4.323  32.188  1.00 30.92           H  
ATOM   1432  N   ASP A 309      -4.517  -2.423  30.049  1.00 22.86           N  
ANISOU 1432  N   ASP A 309     2447   3991   2249    347   1003   -326       N  
ATOM   1433  CA  ASP A 309      -5.786  -2.282  29.354  1.00 21.47           C  
ANISOU 1433  CA  ASP A 309     2041   3844   2272    448   1049   -310       C  
ATOM   1434  C   ASP A 309      -5.619  -2.654  27.891  1.00 19.76           C  
ANISOU 1434  C   ASP A 309     1699   3638   2170    436    853   -255       C  
ATOM   1435  O   ASP A 309      -4.745  -2.126  27.206  1.00 17.95           O  
ANISOU 1435  O   ASP A 309     1575   3329   1915    478    735   -294       O  
ATOM   1436  CB  ASP A 309      -6.309  -0.845  29.481  1.00 23.25           C  
ANISOU 1436  CB  ASP A 309     2301   3980   2554    626   1184   -420       C  
ATOM   1437  CG  ASP A 309      -7.764  -0.710  29.076  1.00 34.83           C  
ANISOU 1437  CG  ASP A 309     3490   5518   4226    747   1256   -373       C  
ATOM   1438  OD1 ASP A 309      -8.519  -0.050  29.815  1.00 46.86           O  
ANISOU 1438  OD1 ASP A 309     4993   7026   5787    839   1466   -449       O  
ATOM   1439  OD2 ASP A 309      -8.175  -1.272  28.043  1.00 35.78           O  
ANISOU 1439  OD2 ASP A 309     3402   5730   4464    730   1103   -272       O  
ATOM   1440  H   ASP A 309      -4.145  -1.679  30.267  1.00 27.47           H  
ATOM   1441  HA  ASP A 309      -6.441  -2.877  29.753  1.00 25.80           H  
ATOM   1442  HB2 ASP A 309      -6.228  -0.560  30.404  1.00 27.73           H  
ATOM   1443  HB3 ASP A 309      -5.783  -0.266  28.907  1.00 27.73           H  
ATOM   1444  N   ILE A 310      -6.507  -3.524  27.405  1.00 20.78           N  
ANISOU 1444  N   ILE A 310     2130   3892   1875     94    924   -428       N  
ATOM   1445  CA  ILE A 310      -6.480  -3.919  26.004  1.00 19.37           C  
ANISOU 1445  CA  ILE A 310     1761   3658   1942     54    688   -335       C  
ATOM   1446  C   ILE A 310      -6.659  -2.736  25.069  1.00 18.30           C  
ANISOU 1446  C   ILE A 310     1548   3422   1985    278    661   -411       C  
ATOM   1447  O   ILE A 310      -6.275  -2.811  23.903  1.00 17.31           O  
ANISOU 1447  O   ILE A 310     1403   3190   1985    245    442   -378       O  
ATOM   1448  CB  ILE A 310      -7.560  -4.985  25.729  1.00 23.04           C  
ANISOU 1448  CB  ILE A 310     1931   4304   2518   -104    703   -138       C  
ATOM   1449  CG1 ILE A 310      -7.393  -5.565  24.321  1.00 22.42           C  
ANISOU 1449  CG1 ILE A 310     1803   4122   2594   -232    421    -63       C  
ATOM   1450  CG2 ILE A 310      -8.942  -4.389  25.900  1.00 32.46           C  
ANISOU 1450  CG2 ILE A 310     2849   5625   3858     59    917    -73       C  
ATOM   1451  CD1 ILE A 310      -6.245  -6.471  24.182  1.00 24.82           C  
ANISOU 1451  CD1 ILE A 310     2377   4241   2813   -378    267    -59       C  
ATOM   1452  H   ILE A 310      -7.131  -3.896  27.866  1.00 24.93           H  
ATOM   1453  HA  ILE A 310      -5.608  -4.306  25.826  1.00 23.28           H  
ATOM   1454  HB  ILE A 310      -7.451  -5.705  26.370  1.00 27.68           H  
ATOM   1455 HG12 ILE A 310      -8.193  -6.065  24.093  1.00 26.94           H  
ATOM   1456 HG13 ILE A 310      -7.269  -4.834  23.696  1.00 26.94           H  
ATOM   1457 HG21 ILE A 310      -9.605  -5.078  25.738  1.00 38.98           H  
ATOM   1458 HG22 ILE A 310      -9.030  -4.050  26.804  1.00 38.98           H  
ATOM   1459 HG23 ILE A 310      -9.054  -3.666  25.263  1.00 38.98           H  
ATOM   1460 HD11 ILE A 310      -6.205  -6.792  23.268  1.00 29.82           H  
ATOM   1461 HD12 ILE A 310      -5.433  -5.987  24.399  1.00 29.82           H  
ATOM   1462 HD13 ILE A 310      -6.357  -7.218  24.791  1.00 29.82           H  
ATOM   1463  N   GLN A 311      -7.257  -1.644  25.544  1.00 22.34           N  
ANISOU 1463  N   GLN A 311     2066   3918   2506    513    897   -491       N  
ATOM   1464  CA  GLN A 311      -7.419  -0.463  24.694  1.00 25.44           C  
ANISOU 1464  CA  GLN A 311     2444   4138   3086    734    864   -521       C  
ATOM   1465  C   GLN A 311      -6.085   0.064  24.192  1.00 26.40           C  
ANISOU 1465  C   GLN A 311     2834   4052   3144    710    669   -662       C  
ATOM   1466  O   GLN A 311      -6.005   0.634  23.094  1.00 22.92           O  
ANISOU 1466  O   GLN A 311     2356   3492   2859    802    538   -634       O  
ATOM   1467  CB  GLN A 311      -8.155   0.629  25.477  1.00 35.20           C  
ANISOU 1467  CB  GLN A 311     3765   5253   4355    941   1174   -591       C  
ATOM   1468  CG  GLN A 311      -8.700   1.761  24.620  1.00 57.78           C  
ANISOU 1468  CG  GLN A 311     6512   7974   7469   1168   1160   -571       C  
ATOM   1469  CD  GLN A 311      -9.831   1.315  23.706  1.00 51.19           C  
ANISOU 1469  CD  GLN A 311     5222   7333   6896   1197   1046   -331       C  
ATOM   1470  OE1 GLN A 311     -10.979   1.209  24.127  1.00 46.31           O  
ANISOU 1470  OE1 GLN A 311     4340   6873   6384   1263   1210   -244       O  
ATOM   1471  NE2 GLN A 311      -9.499   1.051  22.441  1.00 57.73           N  
ANISOU 1471  NE2 GLN A 311     5974   8160   7800   1116    740   -223       N  
ATOM   1472  H   GLN A 311      -7.572  -1.560  26.339  1.00 26.85           H  
ATOM   1473  HA  GLN A 311      -7.950  -0.704  23.919  1.00 30.57           H  
ATOM   1474  HB2 GLN A 311      -8.906   0.225  25.941  1.00 42.27           H  
ATOM   1475  HB3 GLN A 311      -7.540   1.018  26.119  1.00 42.27           H  
ATOM   1476  HG2 GLN A 311      -9.041   2.460  25.199  1.00 69.37           H  
ATOM   1477  HG3 GLN A 311      -7.985   2.108  24.064  1.00 69.37           H  
ATOM   1478 HE21 GLN A 311      -8.683   1.136  22.184  1.00 69.31           H  
ATOM   1479 HE22 GLN A 311     -10.102   0.795  21.883  1.00 69.31           H  
ATOM   1480  N   LEU A 312      -5.015  -0.130  24.960  1.00 19.41           N  
ANISOU 1480  N   LEU A 312     2226   3103   2045    542    614   -761       N  
ATOM   1481  CA  LEU A 312      -3.703   0.324  24.537  1.00 17.01           C  
ANISOU 1481  CA  LEU A 312     2133   2603   1728    450    406   -822       C  
ATOM   1482  C   LEU A 312      -3.156  -0.435  23.344  1.00 15.33           C  
ANISOU 1482  C   LEU A 312     1786   2378   1662    347    193   -688       C  
ATOM   1483  O   LEU A 312      -2.119  -0.035  22.809  1.00 15.83           O  
ANISOU 1483  O   LEU A 312     1958   2295   1762    298     64   -700       O  
ATOM   1484  CB  LEU A 312      -2.727   0.217  25.711  1.00 16.50           C  
ANISOU 1484  CB  LEU A 312     2333   2525   1411    255    350   -891       C  
ATOM   1485  CG  LEU A 312      -3.013   1.184  26.864  1.00 19.68           C  
ANISOU 1485  CG  LEU A 312     3056   2812   1607    304    537  -1024       C  
ATOM   1486  CD1 LEU A 312      -2.321   0.729  28.141  1.00 22.60           C  
ANISOU 1486  CD1 LEU A 312     3630   3262   1693     98    424  -1019       C  
ATOM   1487  CD2 LEU A 312      -2.582   2.601  26.482  1.00 22.05           C  
ANISOU 1487  CD2 LEU A 312     3491   2884   2002    318    495  -1156       C  
ATOM   1488  H   LEU A 312      -5.027  -0.521  25.726  1.00 23.33           H  
ATOM   1489  HA  LEU A 312      -3.769   1.255  24.274  1.00 20.45           H  
ATOM   1490  HB2 LEU A 312      -2.770  -0.684  26.066  1.00 19.84           H  
ATOM   1491  HB3 LEU A 312      -1.833   0.404  25.386  1.00 19.84           H  
ATOM   1492  HG  LEU A 312      -3.967   1.194  27.040  1.00 23.43           H  
ATOM   1493 HD11 LEU A 312      -2.522   1.359  28.851  1.00 27.15           H  
ATOM   1494 HD12 LEU A 312      -2.646  -0.153  28.380  1.00 27.15           H  
ATOM   1495 HD13 LEU A 312      -1.364   0.698  27.988  1.00 27.15           H  
ATOM   1496 HD21 LEU A 312      -2.768   3.198  27.223  1.00 26.49           H  
ATOM   1497 HD22 LEU A 312      -1.631   2.600  26.288  1.00 26.49           H  
ATOM   1498 HD23 LEU A 312      -3.079   2.882  25.697  1.00 26.49           H  
ATOM   1499  N   LEU A 313      -3.802  -1.527  22.941  1.00 14.71           N  
ANISOU 1499  N   LEU A 313     1508   2434   1648    290    173   -561       N  
ATOM   1500  CA  LEU A 313      -3.375  -2.204  21.727  1.00 12.37           C  
ANISOU 1500  CA  LEU A 313     1186   2070   1443    203     16   -469       C  
ATOM   1501  C   LEU A 313      -3.607  -1.314  20.517  1.00 14.02           C  
ANISOU 1501  C   LEU A 313     1380   2178   1769    321    -47   -470       C  
ATOM   1502  O   LEU A 313      -2.808  -1.318  19.577  1.00 12.51           O  
ANISOU 1502  O   LEU A 313     1298   1855   1602    281   -138   -450       O  
ATOM   1503  CB  LEU A 313      -4.106  -3.538  21.599  1.00 13.42           C  
ANISOU 1503  CB  LEU A 313     1198   2322   1578     63     -3   -351       C  
ATOM   1504  CG  LEU A 313      -3.575  -4.505  20.573  1.00 15.03           C  
ANISOU 1504  CG  LEU A 313     1510   2402   1798    -61   -117   -284       C  
ATOM   1505  CD1 LEU A 313      -2.080  -4.799  20.738  1.00 12.25           C  
ANISOU 1505  CD1 LEU A 313     1318   1910   1425    -57   -114   -282       C  
ATOM   1506  CD2 LEU A 313      -4.378  -5.801  20.626  1.00 16.08           C  
ANISOU 1506  CD2 LEU A 313     1597   2612   1901   -254   -137   -183       C  
ATOM   1507  H   LEU A 313      -4.473  -1.885  23.344  1.00 17.69           H  
ATOM   1508  HA  LEU A 313      -2.427  -2.407  21.766  1.00 14.88           H  
ATOM   1509  HB2 LEU A 313      -4.065  -3.985  22.459  1.00 16.14           H  
ATOM   1510  HB3 LEU A 313      -5.028  -3.353  21.365  1.00 16.14           H  
ATOM   1511  HG  LEU A 313      -3.673  -4.092  19.701  1.00 18.07           H  
ATOM   1512 HD11 LEU A 313      -1.809  -5.444  20.065  1.00 14.73           H  
ATOM   1513 HD12 LEU A 313      -1.582  -3.975  20.626  1.00 14.73           H  
ATOM   1514 HD13 LEU A 313      -1.925  -5.161  21.624  1.00 14.73           H  
ATOM   1515 HD21 LEU A 313      -4.024  -6.419  19.968  1.00 19.33           H  
ATOM   1516 HD22 LEU A 313      -4.302  -6.183  21.514  1.00 19.33           H  
ATOM   1517 HD23 LEU A 313      -5.307  -5.604  20.429  1.00 19.33           H  
ATOM   1518  N   LYS A 314      -4.653  -0.498  20.540  1.00 14.84           N  
ANISOU 1518  N   LYS A 314     1357   2335   1947    491     25   -471       N  
ATOM   1519  CA  LYS A 314      -4.839   0.482  19.473  1.00 15.83           C  
ANISOU 1519  CA  LYS A 314     1492   2342   2181    631    -52   -439       C  
ATOM   1520  C   LYS A 314      -3.687   1.481  19.456  1.00 12.63           C  
ANISOU 1520  C   LYS A 314     1351   1702   1745    663    -46   -550       C  
ATOM   1521  O   LYS A 314      -3.099   1.749  18.404  1.00 13.83           O  
ANISOU 1521  O   LYS A 314     1604   1724   1925    627   -152   -507       O  
ATOM   1522  CB  LYS A 314      -6.168   1.196  19.658  1.00 16.48           C  
ANISOU 1522  CB  LYS A 314     1352   2517   2391    872     57   -377       C  
ATOM   1523  CG  LYS A 314      -6.432   2.281  18.632  1.00 21.22           C  
ANISOU 1523  CG  LYS A 314     1971   2976   3118   1046    -29   -291       C  
ATOM   1524  CD  LYS A 314      -7.827   2.876  18.769  1.00 29.55           C  
ANISOU 1524  CD  LYS A 314     2776   4091   4362   1234     84   -138       C  
ATOM   1525  CE  LYS A 314      -8.056   3.978  17.747  1.00 44.18           C  
ANISOU 1525  CE  LYS A 314     4662   5771   6355   1388    -23    -22       C  
ATOM   1526  NZ  LYS A 314      -9.361   4.693  17.955  1.00 54.56           N  
ANISOU 1526  NZ  LYS A 314     5732   7110   7886   1615     65     57       N  
ATOM   1527  H   LYS A 314      -5.260  -0.489  21.149  1.00 17.84           H  
ATOM   1528  HA  LYS A 314      -4.860   0.026  18.617  1.00 19.03           H  
ATOM   1529  HB2 LYS A 314      -6.883   0.544  19.589  1.00 19.81           H  
ATOM   1530  HB3 LYS A 314      -6.179   1.610  20.535  1.00 19.81           H  
ATOM   1531  HG2 LYS A 314      -5.786   2.995  18.751  1.00 25.50           H  
ATOM   1532  HG3 LYS A 314      -6.350   1.905  17.742  1.00 25.50           H  
ATOM   1533  HD2 LYS A 314      -8.489   2.182  18.624  1.00 35.50           H  
ATOM   1534  HD3 LYS A 314      -7.931   3.254  19.656  1.00 35.50           H  
ATOM   1535  HE2 LYS A 314      -7.341   4.630  17.819  1.00 53.06           H  
ATOM   1536  HE3 LYS A 314      -8.063   3.590  16.858  1.00 53.06           H  
ATOM   1537  HZ1 LYS A 314      -9.461   5.329  17.341  1.00 65.50           H  
ATOM   1538  HZ2 LYS A 314     -10.037   4.118  17.887  1.00 65.50           H  
ATOM   1539  HZ3 LYS A 314      -9.379   5.065  18.763  1.00 65.50           H  
ATOM   1540  N   SER A 315      -3.340   2.031  20.624  1.00 14.11           N  
ANISOU 1540  N   SER A 315     1684   1831   1848    688     76   -686       N  
ATOM   1541  CA  SER A 315      -2.211   2.955  20.700  1.00 13.45           C  
ANISOU 1541  CA  SER A 315     1860   1530   1722    609     39   -759       C  
ATOM   1542  C   SER A 315      -0.942   2.323  20.171  1.00 13.43           C  
ANISOU 1542  C   SER A 315     1863   1519   1721    417   -101   -702       C  
ATOM   1543  O   SER A 315      -0.161   2.966  19.445  1.00 15.54           O  
ANISOU 1543  O   SER A 315     2232   1631   2042    371   -159   -675       O  
ATOM   1544  CB  SER A 315      -1.998   3.408  22.146  1.00 15.73           C  
ANISOU 1544  CB  SER A 315     2348   1776   1852    541    148   -882       C  
ATOM   1545  OG  SER A 315      -3.173   4.011  22.658  1.00 25.40           O  
ANISOU 1545  OG  SER A 315     3579   2977   3094    731    367   -920       O  
ATOM   1546  H   SER A 315      -3.736   1.888  21.373  1.00 16.97           H  
ATOM   1547  HA  SER A 315      -2.418   3.732  20.158  1.00 15.97           H  
ATOM   1548  HB2 SER A 315      -1.774   2.637  22.690  1.00 18.91           H  
ATOM   1549  HB3 SER A 315      -1.274   4.053  22.172  1.00 18.91           H  
ATOM   1550  HG  SER A 315      -2.984   4.495  23.318  1.00 30.51           H  
ATOM   1551  N   ALA A 316      -0.719   1.059  20.510  1.00 11.54           N  
ANISOU 1551  N   ALA A 316     1510   1436   1439    307   -123   -641       N  
ATOM   1552  CA  ALA A 316       0.479   0.369  20.032  1.00  9.95           C  
ANISOU 1552  CA  ALA A 316     1285   1221   1277    182   -191   -536       C  
ATOM   1553  C   ALA A 316       0.529   0.305  18.511  1.00  9.72           C  
ANISOU 1553  C   ALA A 316     1267   1102   1325    223   -191   -462       C  
ATOM   1554  O   ALA A 316       1.548   0.639  17.898  1.00 10.51           O  
ANISOU 1554  O   ALA A 316     1416   1101   1478    178   -186   -406       O  
ATOM   1555  CB  ALA A 316       0.530  -1.051  20.622  1.00 11.70           C  
ANISOU 1555  CB  ALA A 316     1414   1580   1453    115   -186   -461       C  
ATOM   1556  H   ALA A 316      -1.235   0.583  21.007  1.00 13.88           H  
ATOM   1557  HA  ALA A 316       1.256   0.866  20.334  1.00 11.98           H  
ATOM   1558  HB1 ALA A 316       1.331  -1.496  20.305  1.00 14.08           H  
ATOM   1559  HB2 ALA A 316       0.546  -0.990  21.590  1.00 14.08           H  
ATOM   1560  HB3 ALA A 316      -0.257  -1.540  20.334  1.00 14.08           H  
ATOM   1561  N   TYR A 317      -0.574  -0.115  17.891  1.00  9.27           N  
ANISOU 1561  N   TYR A 317     1171   1094   1256    278   -202   -442       N  
ATOM   1562  CA  TYR A 317      -0.611  -0.219  16.440  1.00 10.02           C  
ANISOU 1562  CA  TYR A 317     1357   1106   1346    271   -236   -374       C  
ATOM   1563  C   TYR A 317      -0.532   1.155  15.780  1.00 10.56           C  
ANISOU 1563  C   TYR A 317     1522   1038   1451    348   -264   -367       C  
ATOM   1564  O   TYR A 317      -0.049   1.260  14.651  1.00 10.96           O  
ANISOU 1564  O   TYR A 317     1709    985   1470    313   -259   -302       O  
ATOM   1565  CB  TYR A 317      -1.872  -0.965  15.992  1.00 12.88           C  
ANISOU 1565  CB  TYR A 317     1662   1571   1659    235   -321   -329       C  
ATOM   1566  CG  TYR A 317      -1.727  -2.488  16.044  1.00  9.63           C  
ANISOU 1566  CG  TYR A 317     1300   1182   1178     99   -292   -310       C  
ATOM   1567  CD1 TYR A 317      -0.806  -3.137  15.257  1.00 11.14           C  
ANISOU 1567  CD1 TYR A 317     1700   1223   1312     54   -211   -291       C  
ATOM   1568  CD2 TYR A 317      -2.523  -3.264  16.882  1.00 11.83           C  
ANISOU 1568  CD2 TYR A 317     1444   1603   1449     29   -307   -298       C  
ATOM   1569  CE1 TYR A 317      -0.666  -4.514  15.294  1.00 10.27           C  
ANISOU 1569  CE1 TYR A 317     1703   1057   1143    -31   -148   -276       C  
ATOM   1570  CE2 TYR A 317      -2.399  -4.644  16.924  1.00 11.90           C  
ANISOU 1570  CE2 TYR A 317     1554   1573   1393   -106   -282   -269       C  
ATOM   1571  CZ  TYR A 317      -1.458  -5.268  16.108  1.00 12.11           C  
ANISOU 1571  CZ  TYR A 317     1833   1400   1366   -124   -203   -265       C  
ATOM   1572  OH  TYR A 317      -1.346  -6.652  16.131  1.00  9.86           O  
ANISOU 1572  OH  TYR A 317     1720   1006   1021   -225   -143   -240       O  
ATOM   1573  H   TYR A 317      -1.304  -0.343  18.286  1.00 11.16           H  
ATOM   1574  HA  TYR A 317       0.153  -0.737  16.143  1.00 12.06           H  
ATOM   1575  HB2 TYR A 317      -2.606  -0.715  16.574  1.00 15.49           H  
ATOM   1576  HB3 TYR A 317      -2.074  -0.716  15.077  1.00 15.49           H  
ATOM   1577  HD1 TYR A 317      -0.265  -2.640  14.686  1.00 13.41           H  
ATOM   1578  HD2 TYR A 317      -3.152  -2.847  17.425  1.00 14.24           H  
ATOM   1579  HE1 TYR A 317      -0.026  -4.928  14.760  1.00 12.36           H  
ATOM   1580  HE2 TYR A 317      -2.937  -5.147  17.491  1.00 14.31           H  
ATOM   1581  HH  TYR A 317      -1.769  -6.964  16.786  1.00 11.79           H  
ATOM   1582  N   GLU A 318      -0.994   2.209  16.452  1.00 11.84           N  
ANISOU 1582  N   GLU A 318     1666   1169   1664    458   -262   -429       N  
ATOM   1583  CA  GLU A 318      -0.917   3.542  15.849  1.00 11.94           C  
ANISOU 1583  CA  GLU A 318     1823    992   1724    542   -281   -408       C  
ATOM   1584  C   GLU A 318       0.525   3.941  15.530  1.00 12.52           C  
ANISOU 1584  C   GLU A 318     2031    929   1798    393   -246   -384       C  
ATOM   1585  O   GLU A 318       0.756   4.732  14.611  1.00 14.47           O  
ANISOU 1585  O   GLU A 318     2406   1039   2053    387   -251   -305       O  
ATOM   1586  CB  GLU A 318      -1.564   4.583  16.761  1.00 13.72           C  
ANISOU 1586  CB  GLU A 318     2059   1167   1986    671   -206   -473       C  
ATOM   1587  CG  GLU A 318      -3.078   4.531  16.713  1.00 14.58           C  
ANISOU 1587  CG  GLU A 318     1988   1387   2166    886   -210   -416       C  
ATOM   1588  CD  GLU A 318      -3.741   5.583  17.582  1.00 24.78           C  
ANISOU 1588  CD  GLU A 318     3304   2596   3514   1044    -37   -455       C  
ATOM   1589  OE1 GLU A 318      -3.073   6.093  18.506  1.00 28.70           O  
ANISOU 1589  OE1 GLU A 318     3987   2976   3942    952     67   -588       O  
ATOM   1590  OE2 GLU A 318      -4.927   5.880  17.351  1.00 29.46           O  
ANISOU 1590  OE2 GLU A 318     3723   3237   4233   1246     -9   -340       O  
ATOM   1591  H   GLU A 318      -1.347   2.183  17.235  1.00 14.25           H  
ATOM   1592  HA  GLU A 318      -1.415   3.526  15.016  1.00 14.37           H  
ATOM   1593  HB2 GLU A 318      -1.286   4.420  17.675  1.00 16.50           H  
ATOM   1594  HB3 GLU A 318      -1.284   5.468  16.481  1.00 16.50           H  
ATOM   1595  HG2 GLU A 318      -3.368   4.673  15.798  1.00 17.32           H  
ATOM   1596  HG3 GLU A 318      -3.372   3.660  17.022  1.00 17.32           H  
ATOM   1597  N   ASN A 319       1.496   3.382  16.243  1.00 10.50           N  
ANISOU 1597  N   ASN A 319     1708    736   1544    260   -215   -408       N  
ATOM   1598  CA  ASN A 319       2.893   3.676  15.964  1.00 12.37           C  
ANISOU 1598  CA  ASN A 319     1968    898   1834    108   -185   -327       C  
ATOM   1599  C   ASN A 319       3.280   3.234  14.564  1.00 11.72           C  
ANISOU 1599  C   ASN A 319     1924    787   1743    112    -89   -202       C  
ATOM   1600  O   ASN A 319       4.185   3.824  13.963  1.00 11.93           O  
ANISOU 1600  O   ASN A 319     2003    714   1814     22    -23   -105       O  
ATOM   1601  CB  ASN A 319       3.801   2.992  16.985  1.00 11.61           C  
ANISOU 1601  CB  ASN A 319     1707    938   1767    -19   -202   -302       C  
ATOM   1602  CG  ASN A 319       3.625   3.543  18.388  1.00 12.43           C  
ANISOU 1602  CG  ASN A 319     1870   1047   1804    -94   -303   -429       C  
ATOM   1603  OD1 ASN A 319       4.090   4.637  18.696  1.00 15.95           O  
ANISOU 1603  OD1 ASN A 319     2461   1354   2245   -231   -369   -468       O  
ATOM   1604  ND2 ASN A 319       2.958   2.770  19.243  1.00 12.38           N  
ANISOU 1604  ND2 ASN A 319     1805   1182   1716    -34   -303   -494       N  
ATOM   1605  H   ASN A 319       1.373   2.831  16.892  1.00 12.42           H  
ATOM   1606  HA  ASN A 319       3.024   4.634  16.039  1.00 14.88           H  
ATOM   1607  HB2 ASN A 319       3.595   2.045  17.007  1.00 13.97           H  
ATOM   1608  HB3 ASN A 319       4.726   3.125  16.725  1.00 13.97           H  
ATOM   1609 HD21 ASN A 319       2.830   3.035  20.052  1.00 14.89           H  
ATOM   1610 HD22 ASN A 319       2.655   2.007  18.988  1.00 14.89           H  
ATOM   1611  N   PHE A 320       2.633   2.183  14.047  1.00 10.98           N  
ANISOU 1611  N   PHE A 320     1839    769   1566    182    -66   -199       N  
ATOM   1612  CA  PHE A 320       2.949   1.678  12.711  1.00 10.65           C  
ANISOU 1612  CA  PHE A 320     1947    666   1435    172     52   -115       C  
ATOM   1613  C   PHE A 320       2.719   2.765  11.656  1.00 11.86           C  
ANISOU 1613  C   PHE A 320     2303    683   1522    171     12    -54       C  
ATOM   1614  O   PHE A 320       3.350   2.753  10.594  1.00 12.98           O  
ANISOU 1614  O   PHE A 320     2609    741   1580    126    154     36       O  
ATOM   1615  CB  PHE A 320       2.080   0.470  12.334  1.00 10.47           C  
ANISOU 1615  CB  PHE A 320     2005    698   1274    186     23   -150       C  
ATOM   1616  CG  PHE A 320       2.382  -0.844  13.065  1.00  9.52           C  
ANISOU 1616  CG  PHE A 320     1781    650   1188    186    110   -172       C  
ATOM   1617  CD1 PHE A 320       2.963  -0.887  14.340  1.00  9.83           C  
ANISOU 1617  CD1 PHE A 320     1590    778   1368    193    111   -167       C  
ATOM   1618  CD2 PHE A 320       2.038  -2.052  12.464  1.00 10.02           C  
ANISOU 1618  CD2 PHE A 320     2031    667   1110    154    164   -188       C  
ATOM   1619  CE1 PHE A 320       3.197  -2.108  14.936  1.00  8.71           C  
ANISOU 1619  CE1 PHE A 320     1377    683   1249    209    173   -142       C  
ATOM   1620  CE2 PHE A 320       2.253  -3.268  13.065  1.00  9.86           C  
ANISOU 1620  CE2 PHE A 320     1976    652   1118    166    251   -192       C  
ATOM   1621  CZ  PHE A 320       2.834  -3.314  14.314  1.00  9.13           C  
ANISOU 1621  CZ  PHE A 320     1618    657   1193    214    259   -152       C  
ATOM   1622  H   PHE A 320       2.010   1.747  14.449  1.00 13.22           H  
ATOM   1623  HA  PHE A 320       3.877   1.392  12.722  1.00 12.82           H  
ATOM   1624  HB2 PHE A 320       1.155   0.693  12.523  1.00 12.60           H  
ATOM   1625  HB3 PHE A 320       2.193   0.300  11.386  1.00 12.60           H  
ATOM   1626  HD1 PHE A 320       3.189  -0.099  14.780  1.00 11.83           H  
ATOM   1627  HD2 PHE A 320       1.645  -2.035  11.621  1.00 11.85           H  
ATOM   1628  HE1 PHE A 320       3.606  -2.134  15.771  1.00 10.27           H  
ATOM   1629  HE2 PHE A 320       2.009  -4.055  12.632  1.00 11.82           H  
ATOM   1630  HZ  PHE A 320       2.983  -4.128  14.738  1.00 10.78           H  
ATOM   1631  N   ASN A 321       1.778   3.678  11.913  1.00 12.22           N  
ANISOU 1631  N   ASN A 321     2357    693   1594    245   -154    -83       N  
ATOM   1632  CA  ASN A 321       1.419   4.670  10.899  1.00 13.90           C  
ANISOU 1632  CA  ASN A 321     2772    761   1748    278   -227     18       C  
ATOM   1633  C   ASN A 321       2.481   5.718  10.651  1.00 15.10           C  
ANISOU 1633  C   ASN A 321     3000    779   1959    181   -123     85       C  
ATOM   1634  O   ASN A 321       2.339   6.497   9.702  1.00 16.80           O  
ANISOU 1634  O   ASN A 321     3379    897   2106    179   -151    191       O  
ATOM   1635  CB  ASN A 321       0.095   5.314  11.285  1.00 15.14           C  
ANISOU 1635  CB  ASN A 321     2860    925   1970    446   -399      9       C  
ATOM   1636  CG  ASN A 321      -1.053   4.346  11.102  1.00 18.40           C  
ANISOU 1636  CG  ASN A 321     3154   1527   2311    479   -536     30       C  
ATOM   1637  OD1 ASN A 321      -1.014   3.526  10.215  1.00 16.22           O  
ANISOU 1637  OD1 ASN A 321     3001   1296   1866    356   -565     76       O  
ATOM   1638  ND2 ASN A 321      -2.051   4.427  11.962  1.00 14.79           N  
ANISOU 1638  ND2 ASN A 321     2474   1176   1970    620   -598     -3       N  
ATOM   1639  H   ASN A 321       1.342   3.742  12.652  1.00 14.49           H  
ATOM   1640  HA  ASN A 321       1.301   4.217  10.049  1.00 16.50           H  
ATOM   1641  HB2 ASN A 321       0.126   5.581  12.217  1.00 18.21           H  
ATOM   1642  HB3 ASN A 321      -0.063   6.089  10.723  1.00 18.21           H  
ATOM   1643 HD21 ASN A 321      -2.723   3.895  11.892  1.00 17.57           H  
ATOM   1644 HD22 ASN A 321      -2.029   5.013  12.592  1.00 17.57           H  
ATOM   1645  N   GLN A 322       3.549   5.751  11.449  1.00 14.75           N  
ANISOU 1645  N   GLN A 322     2851    718   2036     72    -31     56       N  
ATOM   1646  CA  GLN A 322       4.663   6.637  11.157  1.00 17.28           C  
ANISOU 1646  CA  GLN A 322     3232    908   2424    -91     56    163       C  
ATOM   1647  C   GLN A 322       5.582   6.088  10.076  1.00 17.31           C  
ANISOU 1647  C   GLN A 322     3276    929   2371   -167    290    315       C  
ATOM   1648  O   GLN A 322       6.546   6.779   9.710  1.00 19.23           O  
ANISOU 1648  O   GLN A 322     3520   1106   2679   -319    397    448       O  
ATOM   1649  CB  GLN A 322       5.480   6.895  12.432  1.00 22.00           C  
ANISOU 1649  CB  GLN A 322     3674   1516   3170   -253     19    116       C  
ATOM   1650  CG  GLN A 322       4.645   7.259  13.644  1.00 22.96           C  
ANISOU 1650  CG  GLN A 322     3812   1621   3290   -175   -132    -69       C  
ATOM   1651  CD  GLN A 322       3.648   8.363  13.381  1.00 27.42           C  
ANISOU 1651  CD  GLN A 322     4511   2084   3821    -23   -166   -102       C  
ATOM   1652  OE1 GLN A 322       3.831   9.171  12.476  1.00 22.67           O  
ANISOU 1652  OE1 GLN A 322     4042   1353   3219    -52   -146      7       O  
ATOM   1653  NE2 GLN A 322       2.568   8.387  14.158  1.00 39.57           N  
ANISOU 1653  NE2 GLN A 322     6014   3676   5344    144   -196   -222       N  
ATOM   1654  H   GLN A 322       3.646   5.272  12.157  1.00 17.53           H  
ATOM   1655  HA  GLN A 322       4.309   7.486  10.850  1.00 20.77           H  
ATOM   1656  HB2 GLN A 322       5.978   6.091  12.649  1.00 26.44           H  
ATOM   1657  HB3 GLN A 322       6.092   7.629  12.265  1.00 26.44           H  
ATOM   1658  HG2 GLN A 322       4.151   6.475  13.930  1.00 27.58           H  
ATOM   1659  HG3 GLN A 322       5.236   7.556  14.353  1.00 27.58           H  
ATOM   1660 HE21 GLN A 322       2.466   7.793  14.772  1.00 47.52           H  
ATOM   1661 HE22 GLN A 322       1.971   8.997  14.047  1.00 47.52           H  
ATOM   1662  N   HIS A 323       5.287   4.896   9.539  1.00 14.27           N  
ANISOU 1662  N   HIS A 323     2773   1008   1642    -86    201    345       N  
ATOM   1663  CA  HIS A 323       6.143   4.240   8.564  1.00 15.07           C  
ANISOU 1663  CA  HIS A 323     2870   1267   1589   -163    216    375       C  
ATOM   1664  C   HIS A 323       5.324   3.710   7.402  1.00 13.57           C  
ANISOU 1664  C   HIS A 323     2708   1139   1310    -60    112    476       C  
ATOM   1665  O   HIS A 323       4.292   3.078   7.607  1.00 15.97           O  
ANISOU 1665  O   HIS A 323     2940   1472   1655     66     20    450       O  
ATOM   1666  CB  HIS A 323       6.932   3.128   9.268  1.00 12.70           C  
ANISOU 1666  CB  HIS A 323     2416   1146   1265   -202    243    233       C  
ATOM   1667  CG  HIS A 323       7.722   3.647  10.415  1.00 13.85           C  
ANISOU 1667  CG  HIS A 323     2516   1278   1469   -309    325    132       C  
ATOM   1668  ND1 HIS A 323       8.962   4.222  10.254  1.00 17.30           N  
ANISOU 1668  ND1 HIS A 323     2969   1745   1859   -476    427    109       N  
ATOM   1669  CD2 HIS A 323       7.423   3.744  11.732  1.00 17.18           C  
ANISOU 1669  CD2 HIS A 323     2873   1675   1980   -292    324     40       C  
ATOM   1670  CE1 HIS A 323       9.401   4.623  11.436  1.00 17.53           C  
ANISOU 1670  CE1 HIS A 323     2937   1776   1948   -555    476     -3       C  
ATOM   1671  NE2 HIS A 323       8.484   4.354  12.343  1.00 17.09           N  
ANISOU 1671  NE2 HIS A 323     2838   1689   1967   -445    414    -44       N  
ATOM   1672  H   HIS A 323       4.581   4.445   9.733  1.00 17.16           H  
ATOM   1673  HA  HIS A 323       6.763   4.872   8.169  1.00 18.12           H  
ATOM   1674  HB2 HIS A 323       6.313   2.461   9.603  1.00 15.28           H  
ATOM   1675  HB3 HIS A 323       7.546   2.723   8.635  1.00 15.28           H  
ATOM   1676  HD2 HIS A 323       6.643   3.450  12.143  1.00 20.65           H  
ATOM   1677  HE1 HIS A 323      10.222   5.027  11.600  1.00 21.07           H  
ATOM   1678  N   GLU A 324       5.782   3.994   6.175  1.00 16.99           N  
ANISOU 1678  N   GLU A 324     3235   1613   1608   -132    131    583       N  
ATOM   1679  CA  GLU A 324       4.978   3.682   4.996  1.00 16.15           C  
ANISOU 1679  CA  GLU A 324     3124   1599   1411    -49     24    670       C  
ATOM   1680  C   GLU A 324       4.825   2.179   4.780  1.00 17.39           C  
ANISOU 1680  C   GLU A 324     3201   1935   1473    -15    -21    573       C  
ATOM   1681  O   GLU A 324       3.775   1.724   4.304  1.00 15.88           O  
ANISOU 1681  O   GLU A 324     2968   1806   1261     83   -131    589       O  
ATOM   1682  CB  GLU A 324       5.585   4.337   3.752  1.00 18.42           C  
ANISOU 1682  CB  GLU A 324     3484   1933   1582   -147     64    785       C  
ATOM   1683  CG  GLU A 324       5.070   5.722   3.505  1.00 30.26           C  
ANISOU 1683  CG  GLU A 324     5062   3266   3168   -106     40    941       C  
ATOM   1684  CD  GLU A 324       3.588   5.729   3.201  1.00 28.45           C  
ANISOU 1684  CD  GLU A 324     4792   3034   2983     67   -105   1025       C  
ATOM   1685  OE1 GLU A 324       3.157   5.004   2.252  1.00 33.04           O  
ANISOU 1685  OE1 GLU A 324     5335   3798   3422    100   -184   1056       O  
ATOM   1686  OE2 GLU A 324       2.855   6.441   3.914  1.00 40.76           O  
ANISOU 1686  OE2 GLU A 324     6340   4428   4720    164   -134   1042       O  
ATOM   1687  H   GLU A 324       6.541   4.361   6.005  1.00 20.43           H  
ATOM   1688  HA  GLU A 324       4.091   4.048   5.136  1.00 19.41           H  
ATOM   1689  HB2 GLU A 324       6.547   4.391   3.863  1.00 22.14           H  
ATOM   1690  HB3 GLU A 324       5.371   3.796   2.976  1.00 22.14           H  
ATOM   1691  HG2 GLU A 324       5.221   6.264   4.295  1.00 36.34           H  
ATOM   1692  HG3 GLU A 324       5.537   6.106   2.746  1.00 36.34           H  
ATOM   1693  N   VAL A 325       5.864   1.408   5.084  1.00 15.18           N  
ANISOU 1693  N   VAL A 325     2836   1757   1173    -96     65    442       N  
ATOM   1694  CA  VAL A 325       5.896  -0.038   4.901  1.00 13.91           C  
ANISOU 1694  CA  VAL A 325     2564   1745    976    -67     49    315       C  
ATOM   1695  C   VAL A 325       6.574  -0.644   6.118  1.00 12.80           C  
ANISOU 1695  C   VAL A 325     2306   1606    950    -69    106    189       C  
ATOM   1696  O   VAL A 325       7.657  -0.187   6.518  1.00 13.93           O  
ANISOU 1696  O   VAL A 325     2437   1753   1102   -158    195    167       O  
ATOM   1697  CB  VAL A 325       6.651  -0.432   3.621  1.00 15.39           C  
ANISOU 1697  CB  VAL A 325     2774   2092    982   -161    104    297       C  
ATOM   1698  CG1 VAL A 325       6.626  -1.959   3.439  1.00 17.72           C  
ANISOU 1698  CG1 VAL A 325     2957   2507   1270   -122     98    139       C  
ATOM   1699  CG2 VAL A 325       6.045   0.261   2.402  1.00 17.23           C  
ANISOU 1699  CG2 VAL A 325     3093   2351   1100   -165     40    441       C  
ATOM   1700  H   VAL A 325       6.597   1.714   5.414  1.00 18.25           H  
ATOM   1701  HA  VAL A 325       4.991  -0.381   4.840  1.00 16.73           H  
ATOM   1702  HB  VAL A 325       7.575  -0.146   3.701  1.00 18.50           H  
ATOM   1703 HG11 VAL A 325       7.094  -2.188   2.621  1.00 21.30           H  
ATOM   1704 HG12 VAL A 325       7.063  -2.375   4.198  1.00 21.30           H  
ATOM   1705 HG13 VAL A 325       5.703  -2.255   3.386  1.00 21.30           H  
ATOM   1706 HG21 VAL A 325       6.540  -0.003   1.610  1.00 20.71           H  
ATOM   1707 HG22 VAL A 325       5.116  -0.006   2.316  1.00 20.71           H  
ATOM   1708 HG23 VAL A 325       6.103   1.221   2.523  1.00 20.71           H  
ATOM   1709  N   LEU A 326       5.960  -1.691   6.673  1.00 10.51           N  
ANISOU 1709  N   LEU A 326     1930   1328    737     19     55    112       N  
ATOM   1710  CA  LEU A 326       6.526  -2.398   7.802  1.00  9.12           C  
ANISOU 1710  CA  LEU A 326     1648   1162    654     35     90     24       C  
ATOM   1711  C   LEU A 326       6.360  -3.909   7.674  1.00 10.87           C  
ANISOU 1711  C   LEU A 326     1797   1436    899     94     73    -63       C  
ATOM   1712  O   LEU A 326       5.318  -4.408   7.223  1.00 11.56           O  
ANISOU 1712  O   LEU A 326     1897   1516    981    136     12    -74       O  
ATOM   1713  CB  LEU A 326       5.886  -1.969   9.147  1.00 11.60           C  
ANISOU 1713  CB  LEU A 326     1945   1380   1083     75     59     38       C  
ATOM   1714  CG  LEU A 326       5.557  -0.529   9.407  1.00 11.93           C  
ANISOU 1714  CG  LEU A 326     2066   1312   1154     50     63    104       C  
ATOM   1715  CD1 LEU A 326       4.174  -0.196   8.873  1.00 12.16           C  
ANISOU 1715  CD1 LEU A 326     2149   1274   1198    134    -21    172       C  
ATOM   1716  CD2 LEU A 326       5.676  -0.262  10.905  1.00 11.72           C  
ANISOU 1716  CD2 LEU A 326     1984   1252   1216     36     91     50       C  
ATOM   1717  H   LEU A 326       5.207  -2.007   6.404  1.00 12.65           H  
ATOM   1718  HA  LEU A 326       7.474  -2.194   7.802  1.00 10.76           H  
ATOM   1719  HB2 LEU A 326       5.051  -2.454   9.233  1.00 13.96           H  
ATOM   1720  HB3 LEU A 326       6.498  -2.235   9.851  1.00 13.96           H  
ATOM   1721  HG  LEU A 326       6.177   0.057   8.945  1.00 14.35           H  
ATOM   1722 HD11 LEU A 326       3.982   0.738   9.053  1.00 14.63           H  
ATOM   1723 HD12 LEU A 326       4.158  -0.358   7.916  1.00 14.63           H  
ATOM   1724 HD13 LEU A 326       3.520  -0.760   9.314  1.00 14.63           H  
ATOM   1725 HD21 LEU A 326       5.455   0.666  11.079  1.00 14.09           H  
ATOM   1726 HD22 LEU A 326       5.062  -0.843  11.379  1.00 14.09           H  
ATOM   1727 HD23 LEU A 326       6.587  -0.443  11.186  1.00 14.09           H  
ATOM   1728  N   LEU A 327       7.393  -4.638   8.134  1.00 10.13           N  
ANISOU 1728  N   LEU A 327     1618   1388    844     99    128   -131       N  
ATOM   1729  CA  LEU A 327       7.315  -6.065   8.420  1.00  8.73           C  
ANISOU 1729  CA  LEU A 327     1372   1201    746    174    121   -200       C  
ATOM   1730  C   LEU A 327       7.069  -6.186   9.921  1.00  9.58           C  
ANISOU 1730  C   LEU A 327     1439   1250    950    216     90   -161       C  
ATOM   1731  O   LEU A 327       7.844  -5.612  10.713  1.00 10.07           O  
ANISOU 1731  O   LEU A 327     1461   1348   1014    190    110   -138       O  
ATOM   1732  CB  LEU A 327       8.616  -6.757   8.061  1.00 11.63           C  
ANISOU 1732  CB  LEU A 327     1662   1645   1110    182    195   -282       C  
ATOM   1733  CG  LEU A 327       8.788  -8.196   8.518  1.00 12.52           C  
ANISOU 1733  CG  LEU A 327     1703   1711   1342    281    200   -340       C  
ATOM   1734  CD1 LEU A 327       7.735  -9.077   7.833  1.00 13.96           C  
ANISOU 1734  CD1 LEU A 327     1936   1826   1543    296    182   -401       C  
ATOM   1735  CD2 LEU A 327      10.179  -8.713   8.269  1.00 13.31           C  
ANISOU 1735  CD2 LEU A 327     1703   1890   1465    316    274   -419       C  
ATOM   1736  H   LEU A 327       8.172  -4.308   8.291  1.00 12.19           H  
ATOM   1737  HA  LEU A 327       6.605  -6.491   7.915  1.00 10.52           H  
ATOM   1738  HB2 LEU A 327       8.695  -6.757   7.094  1.00 13.99           H  
ATOM   1739  HB3 LEU A 327       9.342  -6.247   8.454  1.00 13.99           H  
ATOM   1740  HG  LEU A 327       8.659  -8.237   9.479  1.00 15.06           H  
ATOM   1741 HD11 LEU A 327       7.863  -9.998   8.112  1.00 16.79           H  
ATOM   1742 HD12 LEU A 327       6.851  -8.773   8.092  1.00 16.79           H  
ATOM   1743 HD13 LEU A 327       7.841  -9.006   6.871  1.00 16.79           H  
ATOM   1744 HD21 LEU A 327      10.231  -9.635   8.567  1.00 16.01           H  
ATOM   1745 HD22 LEU A 327      10.369  -8.662   7.319  1.00 16.01           H  
ATOM   1746 HD23 LEU A 327      10.811  -8.169   8.763  1.00 16.01           H  
ATOM   1747  N   ALA A 328       6.015  -6.905  10.317  1.00  8.55           N  
ANISOU 1747  N   ALA A 328     1314   1050    886    261     47   -160       N  
ATOM   1748  CA  ALA A 328       5.636  -6.850  11.724  1.00  8.23           C  
ANISOU 1748  CA  ALA A 328     1250    974    904    275     23   -112       C  
ATOM   1749  C   ALA A 328       5.085  -8.186  12.204  1.00  9.48           C  
ANISOU 1749  C   ALA A 328     1390   1068   1144    320     12   -117       C  
ATOM   1750  O   ALA A 328       4.554  -8.969  11.412  1.00  9.70           O  
ANISOU 1750  O   ALA A 328     1438   1053   1195    328     13   -171       O  
ATOM   1751  CB  ALA A 328       4.572  -5.773  11.980  1.00  8.21           C  
ANISOU 1751  CB  ALA A 328     1289    939    892    248     -9    -82       C  
ATOM   1752  H   ALA A 328       5.531  -7.405   9.812  1.00 10.30           H  
ATOM   1753  HA  ALA A 328       6.445  -6.664  12.227  1.00  9.91           H  
ATOM   1754  HB1 ALA A 328       4.359  -5.758  12.926  1.00  9.89           H  
ATOM   1755  HB2 ALA A 328       4.923  -4.911  11.705  1.00  9.89           H  
ATOM   1756  HB3 ALA A 328       3.778  -5.986  11.465  1.00  9.89           H  
ATOM   1757  N   PRO A 329       5.144  -8.440  13.500  1.00  8.42           N  
ANISOU 1757  N   PRO A 329     1227    927   1044    334      6    -60       N  
ATOM   1758  CA  PRO A 329       4.350  -9.492  14.132  1.00  8.75           C  
ANISOU 1758  CA  PRO A 329     1278    891   1154    346      0    -33       C  
ATOM   1759  C   PRO A 329       3.042  -8.937  14.669  1.00  9.51           C  
ANISOU 1759  C   PRO A 329     1386    985   1242    293    -15    -30       C  
ATOM   1760  O   PRO A 329       2.871  -7.732  14.803  1.00 10.13           O  
ANISOU 1760  O   PRO A 329     1463   1110   1276    267    -24    -37       O  
ATOM   1761  CB  PRO A 329       5.262  -9.904  15.291  1.00 10.10           C  
ANISOU 1761  CB  PRO A 329     1410   1095   1334    386     -3     52       C  
ATOM   1762  CG  PRO A 329       5.779  -8.520  15.763  1.00  9.93           C  
ANISOU 1762  CG  PRO A 329     1356   1193   1224    339    -11     54       C  
ATOM   1763  CD  PRO A 329       5.977  -7.729  14.489  1.00  8.80           C  
ANISOU 1763  CD  PRO A 329     1234   1059   1051    316      6    -17       C  
ATOM   1764  HA  PRO A 329       4.179 -10.236  13.534  1.00 10.53           H  
ATOM   1765  HB2 PRO A 329       4.757 -10.358  15.984  1.00 12.16           H  
ATOM   1766  HB3 PRO A 329       5.983 -10.473  14.979  1.00 12.16           H  
ATOM   1767  HG2 PRO A 329       5.119  -8.097  16.335  1.00 11.95           H  
ATOM   1768  HG3 PRO A 329       6.616  -8.624  16.241  1.00 11.95           H  
ATOM   1769  HD2 PRO A 329       5.671  -6.815  14.601  1.00 10.60           H  
ATOM   1770  HD3 PRO A 329       6.909  -7.737  14.221  1.00 10.60           H  
ATOM   1771  N   LEU A 330       2.149  -9.848  15.039  1.00 11.51           N  
ANISOU 1771  N   LEU A 330     1648   1176   1550    273     -7    -23       N  
ATOM   1772  CA  LEU A 330       0.975  -9.431  15.797  1.00 11.46           C  
ANISOU 1772  CA  LEU A 330     1626   1190   1538    218     -5    -26       C  
ATOM   1773  C   LEU A 330       1.381  -9.007  17.203  1.00 10.19           C  
ANISOU 1773  C   LEU A 330     1448   1098   1326    197      7     41       C  
ATOM   1774  O   LEU A 330       2.213  -9.651  17.853  1.00 16.07           O  
ANISOU 1774  O   LEU A 330     2196   1850   2058    217      8    124       O  
ATOM   1775  CB  LEU A 330      -0.042 -10.562  15.905  1.00 11.88           C  
ANISOU 1775  CB  LEU A 330     1685   1173   1657    170     18    -40       C  
ATOM   1776  CG  LEU A 330      -0.797 -10.877  14.612  1.00 13.85           C  
ANISOU 1776  CG  LEU A 330     1928   1394   1939    155      2   -143       C  
ATOM   1777  CD1 LEU A 330      -1.581 -12.156  14.867  1.00 17.97           C  
ANISOU 1777  CD1 LEU A 330     2460   1830   2537     82     45   -162       C  
ATOM   1778  CD2 LEU A 330      -1.689  -9.764  14.187  1.00 13.93           C  
ANISOU 1778  CD2 LEU A 330     1891   1486   1916    154    -41   -197       C  
ATOM   1779  H   LEU A 330       2.198 -10.689  14.869  1.00 13.85           H  
ATOM   1780  HA  LEU A 330       0.558  -8.687  15.334  1.00 13.79           H  
ATOM   1781  HB2 LEU A 330       0.424 -11.369  16.174  1.00 14.30           H  
ATOM   1782  HB3 LEU A 330      -0.700 -10.319  16.575  1.00 14.30           H  
ATOM   1783  HG  LEU A 330      -0.179 -10.992  13.874  1.00 16.65           H  
ATOM   1784 HD11 LEU A 330      -2.083 -12.383  14.069  1.00 21.60           H  
ATOM   1785 HD12 LEU A 330      -0.960 -12.870  15.082  1.00 21.60           H  
ATOM   1786 HD13 LEU A 330      -2.188 -12.012  15.610  1.00 21.60           H  
ATOM   1787 HD21 LEU A 330      -2.143 -10.019  13.369  1.00 16.75           H  
ATOM   1788 HD22 LEU A 330      -2.338  -9.595  14.888  1.00 16.75           H  
ATOM   1789 HD23 LEU A 330      -1.152  -8.970  14.035  1.00 16.75           H  
ATOM   1790  N   LEU A 331       0.823  -7.903  17.657  1.00  8.35           N  
ANISOU 1790  N   LEU A 331     1190    921   1061    162     14      1       N  
ATOM   1791  CA  LEU A 331       1.200  -7.370  18.952  1.00 10.08           C  
ANISOU 1791  CA  LEU A 331     1388   1230   1210    121     34     26       C  
ATOM   1792  C   LEU A 331       0.388  -7.975  20.090  1.00  9.60           C  
ANISOU 1792  C   LEU A 331     1316   1202   1128     54     69     58       C  
ATOM   1793  O   LEU A 331      -0.805  -8.279  19.947  1.00  9.44           O  
ANISOU 1793  O   LEU A 331     1283   1146   1158     22     93     16       O  
ATOM   1794  CB  LEU A 331       1.054  -5.851  18.969  1.00 11.10           C  
ANISOU 1794  CB  LEU A 331     1503   1388   1326    106     46    -56       C  
ATOM   1795  CG  LEU A 331       1.879  -5.062  17.944  1.00 11.81           C  
ANISOU 1795  CG  LEU A 331     1621   1446   1420    141     27    -73       C  
ATOM   1796  CD1 LEU A 331       1.551  -3.566  18.003  1.00 10.94           C  
ANISOU 1796  CD1 LEU A 331     1519   1312   1326    125     51   -143       C  
ATOM   1797  CD2 LEU A 331       3.354  -5.254  18.138  1.00 13.28           C  
ANISOU 1797  CD2 LEU A 331     1796   1697   1551    136     21    -30       C  
ATOM   1798  H   LEU A 331       0.227  -7.446  17.237  1.00 10.06           H  
ATOM   1799  HA  LEU A 331       2.128  -7.602  19.113  1.00 12.13           H  
ATOM   1800  HB2 LEU A 331       0.122  -5.639  18.805  1.00 13.35           H  
ATOM   1801  HB3 LEU A 331       1.317  -5.535  19.847  1.00 13.35           H  
ATOM   1802  HG  LEU A 331       1.643  -5.403  17.068  1.00 14.21           H  
ATOM   1803 HD11 LEU A 331       2.093  -3.098  17.348  1.00 13.16           H  
ATOM   1804 HD12 LEU A 331       0.610  -3.441  17.804  1.00 13.16           H  
ATOM   1805 HD13 LEU A 331       1.749  -3.234  18.893  1.00 13.16           H  
ATOM   1806 HD21 LEU A 331       3.830  -4.734  17.472  1.00 15.97           H  
ATOM   1807 HD22 LEU A 331       3.597  -4.954  19.028  1.00 15.97           H  
ATOM   1808 HD23 LEU A 331       3.566  -6.195  18.036  1.00 15.97           H  
ATOM   1809  N   SER A 332       1.058  -8.118  21.229  1.00 11.93           N  
ANISOU 1809  N   SER A 332     1608   1592   1334     21     73    133       N  
ATOM   1810  CA  SER A 332       0.529  -8.593  22.496  1.00 12.89           C  
ANISOU 1810  CA  SER A 332     1728   1786   1383    -62    110    190       C  
ATOM   1811  C   SER A 332       0.070 -10.033  22.436  1.00 14.49           C  
ANISOU 1811  C   SER A 332     1979   1885   1642    -71    123    290       C  
ATOM   1812  O   SER A 332      -0.580 -10.487  23.374  1.00 20.61           O  
ANISOU 1812  O   SER A 332     2766   2703   2364   -162    171    343       O  
ATOM   1813  CB  SER A 332      -0.601  -7.703  22.991  1.00 14.47           C  
ANISOU 1813  CB  SER A 332     1882   2050   1566   -139    172     65       C  
ATOM   1814  OG  SER A 332      -0.098  -6.422  23.384  1.00 15.35           O  
ANISOU 1814  OG  SER A 332     1963   2251   1618   -154    180    -22       O  
ATOM   1815  H   SER A 332       1.894  -7.928  21.294  1.00 14.35           H  
ATOM   1816  HA  SER A 332       1.241  -8.558  23.154  1.00 15.50           H  
ATOM   1817  HB2 SER A 332      -1.247  -7.585  22.277  1.00 17.40           H  
ATOM   1818  HB3 SER A 332      -1.025  -8.125  23.755  1.00 17.40           H  
ATOM   1819  HG  SER A 332      -0.094  -6.359  24.222  1.00 18.45           H  
ATOM   1820  N   ALA A 333       0.443 -10.770  21.389  1.00 17.61           N  
ANISOU 1820  N   ALA A 333     2409   2145   2139      8     94    312       N  
ATOM   1821  CA  ALA A 333      -0.042 -12.130  21.170  1.00 21.35           C  
ANISOU 1821  CA  ALA A 333     2938   2474   2699     -9    122    372       C  
ATOM   1822  C   ALA A 333       0.883 -13.194  21.722  1.00 32.79           C  
ANISOU 1822  C   ALA A 333     4445   3865   4149     46    102    551       C  
ATOM   1823  O   ALA A 333       0.545 -14.383  21.651  1.00 34.59           O  
ANISOU 1823  O   ALA A 333     4741   3936   4464     30    137    620       O  
ATOM   1824  CB  ALA A 333      -0.244 -12.377  19.669  1.00 24.95           C  
ANISOU 1824  CB  ALA A 333     3398   2811   3271     38    113    264       C  
ATOM   1825  H   ALA A 333       0.986 -10.497  20.781  1.00 21.17           H  
ATOM   1826  HA  ALA A 333      -0.898 -12.221  21.616  1.00 25.66           H  
ATOM   1827  HB1 ALA A 333      -0.566 -13.283  19.538  1.00 29.98           H  
ATOM   1828  HB2 ALA A 333      -0.895 -11.743  19.329  1.00 29.98           H  
ATOM   1829  HB3 ALA A 333       0.603 -12.259  19.212  1.00 29.98           H  
ATOM   1830  N   GLY A 334       2.042 -12.808  22.246  1.00 21.70           N  
ANISOU 1830  N   GLY A 334     3011   2575   2659    112     46    627       N  
ATOM   1831  CA  GLY A 334       2.958 -13.793  22.790  1.00 26.65           C  
ANISOU 1831  CA  GLY A 334     3674   3165   3288    196      5    816       C  
ATOM   1832  C   GLY A 334       2.698 -14.012  24.266  1.00 28.54           C  
ANISOU 1832  C   GLY A 334     3942   3515   3387    110      9    974       C  
ATOM   1833  O   GLY A 334       1.587 -14.382  24.670  1.00 27.78           O  
ANISOU 1833  O   GLY A 334     3898   3374   3282    -12     80    991       O  
ATOM   1834  H   GLY A 334       2.314 -11.994  22.296  1.00 26.08           H  
ATOM   1835  HA2 GLY A 334       2.845 -14.637  22.325  1.00 32.02           H  
ATOM   1836  HA3 GLY A 334       3.872 -13.489  22.675  1.00 32.02           H  
ATOM   1837  N   ILE A 335       3.718 -13.764  25.088  1.00 20.40           N  
ANISOU 1837  N   ILE A 335     2867   2650   2234    152    -65   1047       N  
ATOM   1838  CA  ILE A 335       3.540 -13.860  26.519  1.00 19.51           C  
ANISOU 1838  CA  ILE A 335     2776   2675   1960     60    -67   1134       C  
ATOM   1839  C   ILE A 335       2.583 -12.794  27.056  1.00 22.80           C  
ANISOU 1839  C   ILE A 335     3157   3262   2245   -102      2   1026       C  
ATOM   1840  O   ILE A 335       2.105 -12.914  28.198  1.00 21.07           O  
ANISOU 1840  O   ILE A 335     2961   3140   1904   -207     37   1065       O  
ATOM   1841  CB  ILE A 335       4.891 -13.768  27.255  1.00 27.28           C  
ANISOU 1841  CB  ILE A 335     3698   3815   2851    135   -168   1191       C  
ATOM   1842  CG1 ILE A 335       5.627 -12.494  26.867  1.00 32.44           C  
ANISOU 1842  CG1 ILE A 335     4232   4630   3466    149   -200   1048       C  
ATOM   1843  CG2 ILE A 335       5.729 -15.013  26.976  1.00 28.70           C  
ANISOU 1843  CG2 ILE A 335     3918   3831   3156    287   -229   1309       C  
ATOM   1844  CD1 ILE A 335       6.798 -12.172  27.768  1.00 39.87           C  
ANISOU 1844  CD1 ILE A 335     5084   5779   4286    165   -280   1072       C  
ATOM   1845  H   ILE A 335       4.510 -13.542  24.838  1.00 24.51           H  
ATOM   1846  HA  ILE A 335       3.154 -14.733  26.696  1.00 23.44           H  
ATOM   1847  HB  ILE A 335       4.724 -13.726  28.210  1.00 32.77           H  
ATOM   1848 HG12 ILE A 335       5.966 -12.592  25.964  1.00 38.97           H  
ATOM   1849 HG13 ILE A 335       5.007 -11.749  26.910  1.00 38.97           H  
ATOM   1850 HG21 ILE A 335       6.570 -14.941  27.454  1.00 34.48           H  
ATOM   1851 HG22 ILE A 335       5.243 -15.796  27.279  1.00 34.48           H  
ATOM   1852 HG23 ILE A 335       5.895 -15.075  26.023  1.00 34.48           H  
ATOM   1853 HD11 ILE A 335       7.220 -11.355  27.457  1.00 47.88           H  
ATOM   1854 HD12 ILE A 335       6.476 -12.053  28.675  1.00 47.88           H  
ATOM   1855 HD13 ILE A 335       7.433 -12.905  27.735  1.00 47.88           H  
ATOM   1856  N   PHE A 336       2.296 -11.751  26.278  1.00 17.63           N  
ANISOU 1856  N   PHE A 336     2443   2629   1628   -119     30    850       N  
ATOM   1857  CA  PHE A 336       1.427 -10.688  26.770  1.00 16.63           C  
ANISOU 1857  CA  PHE A 336     2271   2633   1413   -252    101    688       C  
ATOM   1858  C   PHE A 336      -0.040 -11.082  26.760  1.00 22.23           C  
ANISOU 1858  C   PHE A 336     3010   3256   2179   -352    199    644       C  
ATOM   1859  O   PHE A 336      -0.856 -10.347  27.317  1.00 18.16           O  
ANISOU 1859  O   PHE A 336     2447   2860   1592   -462    272    517       O  
ATOM   1860  CB  PHE A 336       1.653  -9.414  25.941  1.00 14.82           C  
ANISOU 1860  CB  PHE A 336     1979   2405   1249   -212     96    486       C  
ATOM   1861  CG  PHE A 336       2.813  -8.566  26.449  1.00 14.64           C  
ANISOU 1861  CG  PHE A 336     1896   2564   1102   -213     45    458       C  
ATOM   1862  CD1 PHE A 336       3.031  -7.296  25.960  1.00 15.26           C  
ANISOU 1862  CD1 PHE A 336     1930   2654   1213   -218     60    280       C  
ATOM   1863  CD2 PHE A 336       3.689  -9.054  27.419  1.00 15.89           C  
ANISOU 1863  CD2 PHE A 336     2041   2860   1137   -208    -21    597       C  
ATOM   1864  CE1 PHE A 336       4.072  -6.526  26.424  1.00 17.30           C  
ANISOU 1864  CE1 PHE A 336     2130   3077   1364   -251     27    232       C  
ATOM   1865  CE2 PHE A 336       4.734  -8.277  27.897  1.00 24.60           C  
ANISOU 1865  CE2 PHE A 336     3064   4116   2167   -220    -67    526       C  
ATOM   1866  CZ  PHE A 336       4.924  -7.010  27.394  1.00 21.24           C  
ANISOU 1866  CZ  PHE A 336     2594   3718   1759   -255    -38    343       C  
ATOM   1867  H   PHE A 336       2.587 -11.639  25.477  1.00 21.20           H  
ATOM   1868  HA  PHE A 336       1.657 -10.479  27.689  1.00 19.99           H  
ATOM   1869  HB2 PHE A 336       1.846  -9.666  25.025  1.00 17.83           H  
ATOM   1870  HB3 PHE A 336       0.850  -8.872  25.974  1.00 17.83           H  
ATOM   1871  HD1 PHE A 336       2.466  -6.954  25.306  1.00 18.34           H  
ATOM   1872  HD2 PHE A 336       3.570  -9.915  27.751  1.00 19.11           H  
ATOM   1873  HE1 PHE A 336       4.202  -5.671  26.081  1.00 20.79           H  
ATOM   1874  HE2 PHE A 336       5.303  -8.611  28.552  1.00 29.55           H  
ATOM   1875  HZ  PHE A 336       5.624  -6.483  27.707  1.00 25.53           H  
ATOM   1876  N   GLY A 337      -0.383 -12.191  26.121  1.00 20.05           N  
ANISOU 1876  N   GLY A 337     2799   2780   2038   -322    210    721       N  
ATOM   1877  CA  GLY A 337      -1.641 -12.864  26.382  1.00 19.19           C  
ANISOU 1877  CA  GLY A 337     2726   2612   1955   -450    304    731       C  
ATOM   1878  C   GLY A 337      -2.880 -12.350  25.686  1.00 24.43           C  
ANISOU 1878  C   GLY A 337     3317   3246   2719   -503    368    516       C  
ATOM   1879  O   GLY A 337      -3.979 -12.843  25.981  1.00 25.29           O  
ANISOU 1879  O   GLY A 337     3425   3344   2839   -633    457    500       O  
ATOM   1880  H   GLY A 337       0.102 -12.577  25.525  1.00 24.09           H  
ATOM   1881  HA2 GLY A 337      -1.540 -13.794  26.126  1.00 23.07           H  
ATOM   1882  HA3 GLY A 337      -1.812 -12.815  27.335  1.00 23.07           H  
ATOM   1883  N   ALA A 338      -2.764 -11.374  24.794  1.00 18.15           N  
ANISOU 1883  N   ALA A 338     2455   2447   1993   -412    327    360       N  
ATOM   1884  CA  ALA A 338      -3.928 -10.943  24.036  1.00 18.69           C  
ANISOU 1884  CA  ALA A 338     2449   2487   2166   -431    362    182       C  
ATOM   1885  C   ALA A 338      -4.345 -12.021  23.045  1.00 17.25           C  
ANISOU 1885  C   ALA A 338     2302   2134   2118   -429    360    190       C  
ATOM   1886  O   ALA A 338      -3.516 -12.778  22.536  1.00 19.90           O  
ANISOU 1886  O   ALA A 338     2716   2340   2506   -357    316    286       O  
ATOM   1887  CB  ALA A 338      -3.622  -9.650  23.282  1.00 18.36           C  
ANISOU 1887  CB  ALA A 338     2351   2463   2162   -321    307     52       C  
ATOM   1888  H   ALA A 338      -2.036 -10.954  24.612  1.00 21.81           H  
ATOM   1889  HA  ALA A 338      -4.665 -10.777  24.645  1.00 22.46           H  
ATOM   1890  HB1 ALA A 338      -4.413  -9.377  22.791  1.00 22.07           H  
ATOM   1891  HB2 ALA A 338      -3.375  -8.963  23.921  1.00 22.07           H  
ATOM   1892  HB3 ALA A 338      -2.889  -9.809  22.667  1.00 22.07           H  
ATOM   1893  N   ASP A 339      -5.645 -12.084  22.762  1.00 14.54           N  
ANISOU 1893  N   ASP A 339     1887   1802   1838   -512    413     67       N  
ATOM   1894  CA  ASP A 339      -6.113 -12.999  21.728  1.00 15.16           C  
ANISOU 1894  CA  ASP A 339     1978   1742   2039   -531    411     27       C  
ATOM   1895  C   ASP A 339      -5.551 -12.574  20.385  1.00 13.75           C  
ANISOU 1895  C   ASP A 339     1792   1509   1921   -388    315    -39       C  
ATOM   1896  O   ASP A 339      -5.736 -11.418  19.989  1.00 13.80           O  
ANISOU 1896  O   ASP A 339     1721   1603   1918   -317    271   -136       O  
ATOM   1897  CB  ASP A 339      -7.623 -13.051  21.649  1.00 19.13           C  
ANISOU 1897  CB  ASP A 339     2368   2312   2588   -654    475   -116       C  
ATOM   1898  CG  ASP A 339      -8.112 -14.081  20.652  1.00 37.02           C  
ANISOU 1898  CG  ASP A 339     4645   4454   4968   -712    479   -174       C  
ATOM   1899  OD1 ASP A 339      -8.308 -15.251  21.046  1.00 47.39           O  
ANISOU 1899  OD1 ASP A 339     6037   5659   6311   -844    560   -100       O  
ATOM   1900  OD2 ASP A 339      -8.261 -13.741  19.466  1.00 26.23           O  
ANISOU 1900  OD2 ASP A 339     3219   3093   3656   -633    404   -290       O  
ATOM   1901  H   ASP A 339      -6.259 -11.619  23.144  1.00 17.49           H  
ATOM   1902  HA  ASP A 339      -5.805 -13.891  21.954  1.00 18.22           H  
ATOM   1903  HB2 ASP A 339      -7.979 -13.281  22.521  1.00 22.99           H  
ATOM   1904  HB3 ASP A 339      -7.956 -12.182  21.373  1.00 22.99           H  
ATOM   1905  N   PRO A 340      -4.841 -13.448  19.663  1.00 13.75           N  
ANISOU 1905  N   PRO A 340     1877   1363   1984   -341    289     11       N  
ATOM   1906  CA  PRO A 340      -4.201 -12.998  18.415  1.00 12.37           C  
ANISOU 1906  CA  PRO A 340     1698   1168   1835   -217    210    -52       C  
ATOM   1907  C   PRO A 340      -5.185 -12.628  17.320  1.00 10.61           C  
ANISOU 1907  C   PRO A 340     1388    995   1648   -228    176   -209       C  
ATOM   1908  O   PRO A 340      -4.864 -11.762  16.505  1.00  9.80           O  
ANISOU 1908  O   PRO A 340     1262    940   1521   -132    106   -250       O  
ATOM   1909  CB  PRO A 340      -3.342 -14.197  18.014  1.00 12.98           C  
ANISOU 1909  CB  PRO A 340     1874   1078   1981   -184    218     16       C  
ATOM   1910  CG  PRO A 340      -4.029 -15.360  18.612  1.00 18.47           C  
ANISOU 1910  CG  PRO A 340     2616   1669   2732   -312    300     62       C  
ATOM   1911  CD  PRO A 340      -4.534 -14.850  19.954  1.00 16.73           C  
ANISOU 1911  CD  PRO A 340     2362   1579   2414   -391    337    128       C  
ATOM   1912  HA  PRO A 340      -3.630 -12.235  18.597  1.00 14.88           H  
ATOM   1913  HB2 PRO A 340      -3.306 -14.271  17.047  1.00 15.61           H  
ATOM   1914  HB3 PRO A 340      -2.446 -14.098  18.372  1.00 15.61           H  
ATOM   1915  HG2 PRO A 340      -4.766 -15.640  18.046  1.00 22.20           H  
ATOM   1916  HG3 PRO A 340      -3.404 -16.092  18.730  1.00 22.20           H  
ATOM   1917  HD2 PRO A 340      -5.330 -15.331  20.233  1.00 20.11           H  
ATOM   1918  HD3 PRO A 340      -3.848 -14.923  20.635  1.00 20.11           H  
ATOM   1919  N   ILE A 341      -6.370 -13.234  17.283  1.00 13.26           N  
ANISOU 1919  N   ILE A 341     1669   1336   2032   -348    220   -290       N  
ATOM   1920  CA  ILE A 341      -7.339 -12.840  16.259  1.00 11.91           C  
ANISOU 1920  CA  ILE A 341     1384   1259   1881   -350    167   -440       C  
ATOM   1921  C   ILE A 341      -7.852 -11.432  16.560  1.00 11.54           C  
ANISOU 1921  C   ILE A 341     1230   1356   1797   -280    129   -473       C  
ATOM   1922  O   ILE A 341      -8.000 -10.586  15.663  1.00 12.44           O  
ANISOU 1922  O   ILE A 341     1289   1534   1902   -180     41   -523       O  
ATOM   1923  CB  ILE A 341      -8.490 -13.857  16.167  1.00 15.87           C  
ANISOU 1923  CB  ILE A 341     1830   1753   2447   -516    226   -541       C  
ATOM   1924  CG1 ILE A 341      -7.940 -15.283  16.117  1.00 17.68           C  
ANISOU 1924  CG1 ILE A 341     2194   1784   2741   -592    294   -495       C  
ATOM   1925  CG2 ILE A 341      -9.265 -13.560  14.908  1.00 19.06           C  
ANISOU 1925  CG2 ILE A 341     2116   2272   2855   -503    142   -694       C  
ATOM   1926  CD1 ILE A 341      -8.994 -16.364  16.015  1.00 25.10           C  
ANISOU 1926  CD1 ILE A 341     3103   2678   3757   -787    373   -602       C  
ATOM   1927  H   ILE A 341      -6.631 -13.854  17.819  1.00 15.94           H  
ATOM   1928  HA  ILE A 341      -6.896 -12.835  15.396  1.00 14.11           H  
ATOM   1929  HB  ILE A 341      -9.060 -13.783  16.947  1.00 19.08           H  
ATOM   1930 HG12 ILE A 341      -7.363 -15.363  15.342  1.00 21.26           H  
ATOM   1931 HG13 ILE A 341      -7.433 -15.445  16.928  1.00 21.26           H  
ATOM   1932 HG21 ILE A 341     -10.011 -14.177  14.844  1.00 22.91           H  
ATOM   1933 HG22 ILE A 341      -9.593 -12.648  14.947  1.00 22.91           H  
ATOM   1934 HG23 ILE A 341      -8.679 -13.669  14.143  1.00 22.91           H  
ATOM   1935 HD11 ILE A 341      -8.557 -17.230  16.014  1.00 30.16           H  
ATOM   1936 HD12 ILE A 341      -9.592 -16.295  16.775  1.00 30.16           H  
ATOM   1937 HD13 ILE A 341      -9.491 -16.243  15.190  1.00 30.16           H  
ATOM   1938  N   HIS A 342      -8.091 -11.143  17.840  1.00 11.66           N  
ANISOU 1938  N   HIS A 342     1223   1418   1790   -327    200   -440       N  
ATOM   1939  CA  HIS A 342      -8.456  -9.787  18.222  1.00 11.43           C  
ANISOU 1939  CA  HIS A 342     1102   1496   1745   -250    185   -488       C  
ATOM   1940  C   HIS A 342      -7.356  -8.806  17.843  1.00 11.00           C  
ANISOU 1940  C   HIS A 342     1119   1403   1657   -110    117   -429       C  
ATOM   1941  O   HIS A 342      -7.630  -7.714  17.326  1.00 12.09           O  
ANISOU 1941  O   HIS A 342     1200   1576   1816     -6     59   -477       O  
ATOM   1942  CB  HIS A 342      -8.731  -9.721  19.727  1.00 12.04           C  
ANISOU 1942  CB  HIS A 342     1159   1638   1779   -345    293   -476       C  
ATOM   1943  CG  HIS A 342      -9.016  -8.342  20.219  1.00 13.34           C  
ANISOU 1943  CG  HIS A 342     1238   1893   1939   -271    302   -551       C  
ATOM   1944  ND1 HIS A 342     -10.128  -7.635  19.832  1.00 18.72           N  
ANISOU 1944  ND1 HIS A 342     1765   2653   2697   -212    281   -683       N  
ATOM   1945  CD2 HIS A 342      -8.318  -7.526  21.036  1.00 13.45           C  
ANISOU 1945  CD2 HIS A 342     1294   1923   1891   -240    330   -525       C  
ATOM   1946  CE1 HIS A 342     -10.113  -6.447  20.415  1.00 15.45           C  
ANISOU 1946  CE1 HIS A 342     1312   2272   2288   -140    308   -736       C  
ATOM   1947  NE2 HIS A 342      -9.025  -6.358  21.153  1.00 21.26           N  
ANISOU 1947  NE2 HIS A 342     2169   2973   2935   -170    343   -652       N  
ATOM   1948  H   HIS A 342      -8.050 -11.705  18.491  1.00 13.82           H  
ATOM   1949  HA  HIS A 342      -9.268  -9.535  17.755  1.00 13.54           H  
ATOM   1950  HB2 HIS A 342      -9.503 -10.273  19.929  1.00 14.27           H  
ATOM   1951  HB3 HIS A 342      -7.953 -10.051  20.202  1.00 14.27           H  
ATOM   1952  HD2 HIS A 342      -7.506  -7.722  21.446  1.00 16.17           H  
ATOM   1953  HE1 HIS A 342     -10.761  -5.787  20.321  1.00 18.58           H  
ATOM   1954  N   SER A 343      -6.095  -9.176  18.087  1.00  9.99           N  
ANISOU 1954  N   SER A 343     1111   1201   1482   -104    124   -321       N  
ATOM   1955  CA  SER A 343      -4.991  -8.280  17.767  1.00 10.53           C  
ANISOU 1955  CA  SER A 343     1237   1248   1515     -1     76   -276       C  
ATOM   1956  C   SER A 343      -4.960  -7.980  16.287  1.00  9.03           C  
ANISOU 1956  C   SER A 343     1050   1036   1344     80     -7   -304       C  
ATOM   1957  O   SER A 343      -4.741  -6.836  15.898  1.00  9.99           O  
ANISOU 1957  O   SER A 343     1174   1164   1457    162    -48   -304       O  
ATOM   1958  CB  SER A 343      -3.690  -8.902  18.235  1.00 10.00           C  
ANISOU 1958  CB  SER A 343     1266   1134   1401    -11     92   -165       C  
ATOM   1959  OG  SER A 343      -2.650  -8.006  18.000  1.00 10.32           O  
ANISOU 1959  OG  SER A 343     1339   1178   1403     62     58   -141       O  
ATOM   1960  H   SER A 343      -5.859  -9.928  18.432  1.00 12.02           H  
ATOM   1961  HA  SER A 343      -5.100  -7.437  18.234  1.00 12.67           H  
ATOM   1962  HB2 SER A 343      -3.746  -9.092  19.184  1.00 12.04           H  
ATOM   1963  HB3 SER A 343      -3.529  -9.722  17.741  1.00 12.04           H  
ATOM   1964  HG  SER A 343      -2.062  -8.087  18.595  1.00 12.42           H  
ATOM   1965  N   LEU A 344      -5.211  -8.987  15.448  1.00  9.40           N  
ANISOU 1965  N   LEU A 344     1102   1058   1413     46    -27   -333       N  
ATOM   1966  CA  LEU A 344      -5.277  -8.749  13.998  1.00 10.79           C  
ANISOU 1966  CA  LEU A 344     1271   1255   1572    104   -109   -370       C  
ATOM   1967  C   LEU A 344      -6.389  -7.769  13.663  1.00 10.89           C  
ANISOU 1967  C   LEU A 344     1180   1357   1602    161   -172   -421       C  
ATOM   1968  O   LEU A 344      -6.238  -6.901  12.791  1.00 10.95           O  
ANISOU 1968  O   LEU A 344     1201   1383   1576    252   -248   -393       O  
ATOM   1969  CB  LEU A 344      -5.460 -10.050  13.243  1.00  9.38           C  
ANISOU 1969  CB  LEU A 344     1103   1050   1409     32   -106   -430       C  
ATOM   1970  CG  LEU A 344      -5.575  -9.925  11.718  1.00 11.02           C  
ANISOU 1970  CG  LEU A 344     1299   1322   1565     64   -189   -488       C  
ATOM   1971  CD1 LEU A 344      -4.394  -9.196  11.150  1.00 14.33           C  
ANISOU 1971  CD1 LEU A 344     1801   1729   1914    147   -217   -414       C  
ATOM   1972  CD2 LEU A 344      -5.737 -11.280  11.056  1.00 15.67           C  
ANISOU 1972  CD2 LEU A 344     1898   1884   2174    -33   -165   -587       C  
ATOM   1973  H   LEU A 344      -5.345  -9.803  15.684  1.00 11.32           H  
ATOM   1974  HA  LEU A 344      -4.434  -8.368  13.707  1.00 12.98           H  
ATOM   1975  HB2 LEU A 344      -4.696 -10.619  13.429  1.00 11.29           H  
ATOM   1976  HB3 LEU A 344      -6.273 -10.473  13.560  1.00 11.29           H  
ATOM   1977  HG  LEU A 344      -6.372  -9.410  11.520  1.00 13.26           H  
ATOM   1978 HD11 LEU A 344      -4.484  -9.153  10.185  1.00 17.23           H  
ATOM   1979 HD12 LEU A 344      -4.368  -8.300  11.520  1.00 17.23           H  
ATOM   1980 HD13 LEU A 344      -3.584  -9.675  11.385  1.00 17.23           H  
ATOM   1981 HD21 LEU A 344      -5.823 -11.154  10.098  1.00 18.85           H  
ATOM   1982 HD22 LEU A 344      -4.956 -11.822  11.250  1.00 18.85           H  
ATOM   1983 HD23 LEU A 344      -6.532 -11.710  11.406  1.00 18.85           H  
ATOM   1984  N   ARG A 345      -7.529  -7.897  14.329  1.00 10.49           N  
ANISOU 1984  N   ARG A 345     1018   1363   1602    112   -140   -490       N  
ATOM   1985  CA  ARG A 345      -8.631  -6.987  14.058  1.00 11.24           C  
ANISOU 1985  CA  ARG A 345      983   1550   1736    192   -201   -548       C  
ATOM   1986  C   ARG A 345      -8.264  -5.559  14.422  1.00 12.17           C  
ANISOU 1986  C   ARG A 345     1128   1623   1871    310   -206   -498       C  
ATOM   1987  O   ARG A 345      -8.551  -4.627  13.664  1.00 13.12           O  
ANISOU 1987  O   ARG A 345     1223   1754   2007    432   -293   -477       O  
ATOM   1988  CB  ARG A 345      -9.880  -7.432  14.830  1.00 14.64           C  
ANISOU 1988  CB  ARG A 345     1270   2067   2227    103   -141   -652       C  
ATOM   1989  CG  ARG A 345     -10.377  -8.793  14.478  1.00 24.29           C  
ANISOU 1989  CG  ARG A 345     2458   3320   3450    -38   -123   -719       C  
ATOM   1990  CD  ARG A 345     -11.772  -8.762  13.884  1.00 35.74           C  
ANISOU 1990  CD  ARG A 345     3715   4928   4936    -43   -189   -843       C  
ATOM   1991  NE  ARG A 345     -12.199 -10.099  13.503  1.00 23.06           N  
ANISOU 1991  NE  ARG A 345     2083   3346   3332   -211   -161   -931       N  
ATOM   1992  CZ  ARG A 345     -12.414 -10.476  12.238  1.00 27.76           C  
ANISOU 1992  CZ  ARG A 345     2646   4014   3888   -224   -256   -994       C  
ATOM   1993  NH1 ARG A 345     -12.259  -9.620  11.238  1.00 21.02           N  
ANISOU 1993  NH1 ARG A 345     1782   3229   2974    -74   -392   -952       N  
ATOM   1994  NH2 ARG A 345     -12.816 -11.720  11.979  1.00 35.79           N  
ANISOU 1994  NH2 ARG A 345     3642   5037   4920   -404   -208  -1104       N  
ATOM   1995  H   ARG A 345      -7.688  -8.490  14.931  1.00 12.62           H  
ATOM   1996  HA  ARG A 345      -8.835  -7.014  13.110  1.00 13.52           H  
ATOM   1997  HB2 ARG A 345      -9.673  -7.433  15.777  1.00 17.61           H  
ATOM   1998  HB3 ARG A 345     -10.596  -6.803  14.647  1.00 17.61           H  
ATOM   1999  HG2 ARG A 345      -9.781  -9.190  13.825  1.00 29.18           H  
ATOM   2000  HG3 ARG A 345     -10.403  -9.339  15.279  1.00 29.18           H  
ATOM   2001  HD2 ARG A 345     -12.396  -8.414  14.540  1.00 42.92           H  
ATOM   2002  HD3 ARG A 345     -11.775  -8.200  13.093  1.00 42.92           H  
ATOM   2003  HE  ARG A 345     -12.321 -10.679  14.126  1.00 27.70           H  
ATOM   2004 HH11 ARG A 345     -12.018  -8.810  11.399  1.00 25.25           H  
ATOM   2005 HH12 ARG A 345     -12.400  -9.874  10.429  1.00 25.25           H  
ATOM   2006 HH21 ARG A 345     -12.936 -12.276  12.624  1.00 42.99           H  
ATOM   2007 HH22 ARG A 345     -12.955 -11.967  11.167  1.00 42.99           H  
ATOM   2008  N   VAL A 346      -7.584  -5.360  15.559  1.00 10.88           N  
ANISOU 2008  N   VAL A 346     1027   1406   1701    272   -115   -474       N  
ATOM   2009  CA  VAL A 346      -7.164  -4.006  15.923  1.00 12.85           C  
ANISOU 2009  CA  VAL A 346     1312   1599   1972    357   -102   -455       C  
ATOM   2010  C   VAL A 346      -6.162  -3.482  14.902  1.00 11.62           C  
ANISOU 2010  C   VAL A 346     1274   1368   1772    423   -168   -360       C  
ATOM   2011  O   VAL A 346      -6.211  -2.315  14.493  1.00 12.48           O  
ANISOU 2011  O   VAL A 346     1401   1421   1919    526   -206   -332       O  
ATOM   2012  CB  VAL A 346      -6.577  -3.985  17.347  1.00 13.28           C  
ANISOU 2012  CB  VAL A 346     1403   1648   1996    272      6   -466       C  
ATOM   2013  CG1 VAL A 346      -6.133  -2.574  17.743  1.00 12.03           C  
ANISOU 2013  CG1 VAL A 346     1280   1427   1865    334     35   -484       C  
ATOM   2014  CG2 VAL A 346      -7.620  -4.472  18.351  1.00 13.85           C  
ANISOU 2014  CG2 VAL A 346     1361   1812   2088    188     85   -556       C  
ATOM   2015  H   VAL A 346      -7.361  -5.974  16.118  1.00 13.09           H  
ATOM   2016  HA  VAL A 346      -7.943  -3.428  15.916  1.00 15.46           H  
ATOM   2017  HB  VAL A 346      -5.804  -4.570  17.361  1.00 15.97           H  
ATOM   2018 HG11 VAL A 346      -5.789  -2.595  18.650  1.00 14.47           H  
ATOM   2019 HG12 VAL A 346      -5.440  -2.278  17.133  1.00 14.47           H  
ATOM   2020 HG13 VAL A 346      -6.896  -1.977  17.692  1.00 14.47           H  
ATOM   2021 HG21 VAL A 346      -7.241  -4.434  19.243  1.00 16.65           H  
ATOM   2022 HG22 VAL A 346      -8.401  -3.899  18.299  1.00 16.65           H  
ATOM   2023 HG23 VAL A 346      -7.865  -5.385  18.134  1.00 16.65           H  
ATOM   2024  N   CYS A 347      -5.260  -4.351  14.447  1.00  9.66           N  
ANISOU 2024  N   CYS A 347     1108   1112   1451    365   -173   -308       N  
ATOM   2025  CA  CYS A 347      -4.319  -3.971  13.399  1.00 12.06           C  
ANISOU 2025  CA  CYS A 347     1510   1376   1696    404   -220   -232       C  
ATOM   2026  C   CYS A 347      -5.056  -3.478  12.163  1.00 11.09           C  
ANISOU 2026  C   CYS A 347     1361   1285   1567    491   -324   -210       C  
ATOM   2027  O   CYS A 347      -4.803  -2.379  11.642  1.00 12.51           O  
ANISOU 2027  O   CYS A 347     1600   1412   1740    566   -361   -137       O  
ATOM   2028  CB  CYS A 347      -3.455  -5.165  13.025  1.00 12.58           C  
ANISOU 2028  CB  CYS A 347     1630   1449   1701    337   -205   -217       C  
ATOM   2029  SG  CYS A 347      -2.173  -4.758  11.821  1.00 12.35           S  
ANISOU 2029  SG  CYS A 347     1707   1402   1582    358   -230   -147       S  
ATOM   2030  H   CYS A 347      -5.172  -5.159  14.727  1.00 11.63           H  
ATOM   2031  HA  CYS A 347      -3.752  -3.259  13.735  1.00 14.51           H  
ATOM   2032  HB2 CYS A 347      -3.019  -5.501  13.824  1.00 15.13           H  
ATOM   2033  HB3 CYS A 347      -4.019  -5.854  12.641  1.00 15.13           H  
ATOM   2034  HG  CYS A 347      -1.444  -5.703  11.693  1.00 14.85           H  
ATOM   2035  N   VAL A 348      -6.003  -4.282  11.690  1.00 11.55           N  
ANISOU 2035  N   VAL A 348     1329   1436   1623    474   -375   -268       N  
ATOM   2036  CA  VAL A 348      -6.751  -3.921  10.488  1.00 11.21           C  
ANISOU 2036  CA  VAL A 348     1239   1474   1547    553   -497   -247       C  
ATOM   2037  C   VAL A 348      -7.500  -2.602  10.666  1.00 12.32           C  
ANISOU 2037  C   VAL A 348     1322   1585   1774    693   -544   -212       C  
ATOM   2038  O   VAL A 348      -7.606  -1.801   9.725  1.00 16.04           O  
ANISOU 2038  O   VAL A 348     1832   2056   2208    774   -623   -112       O  
ATOM   2039  CB  VAL A 348      -7.724  -5.071  10.119  1.00 13.48           C  
ANISOU 2039  CB  VAL A 348     1407   1890   1824    484   -534   -353       C  
ATOM   2040  CG1 VAL A 348      -8.843  -4.611   9.225  1.00 19.24           C  
ANISOU 2040  CG1 VAL A 348     2021   2752   2538    576   -672   -355       C  
ATOM   2041  CG2 VAL A 348      -6.948  -6.220   9.452  1.00 15.65           C  
ANISOU 2041  CG2 VAL A 348     1761   2173   2010    377   -511   -381       C  
ATOM   2042  H   VAL A 348      -6.230  -5.034  12.041  1.00 13.89           H  
ATOM   2043  HA  VAL A 348      -6.116  -3.794   9.766  1.00 13.28           H  
ATOM   2044  HB  VAL A 348      -8.131  -5.389  10.940  1.00 16.21           H  
ATOM   2045 HG11 VAL A 348      -9.391  -5.375   8.986  1.00 23.13           H  
ATOM   2046 HG12 VAL A 348      -9.377  -3.956   9.700  1.00 23.13           H  
ATOM   2047 HG13 VAL A 348      -8.465  -4.212   8.425  1.00 23.13           H  
ATOM   2048 HG21 VAL A 348      -7.570  -6.925   9.215  1.00 18.81           H  
ATOM   2049 HG22 VAL A 348      -6.510  -5.883   8.654  1.00 18.81           H  
ATOM   2050 HG23 VAL A 348      -6.286  -6.558  10.075  1.00 18.81           H  
ATOM   2051  N   ASP A 349      -8.033  -2.352  11.871  1.00 12.68           N  
ANISOU 2051  N   ASP A 349     1286   1602   1931    701   -470   -289       N  
ATOM   2052  CA  ASP A 349      -8.844  -1.170  12.104  1.00 16.75           C  
ANISOU 2052  CA  ASP A 349     1748   2082   2534    794   -467   -274       C  
ATOM   2053  C   ASP A 349      -8.005   0.073  12.356  1.00 15.33           C  
ANISOU 2053  C   ASP A 349     1701   1744   2380    822   -405   -189       C  
ATOM   2054  O   ASP A 349      -8.534   1.198  12.227  1.00 17.74           O  
ANISOU 2054  O   ASP A 349     1993   1987   2759    917   -410   -140       O  
ATOM   2055  CB  ASP A 349      -9.752  -1.388  13.312  1.00 16.13           C  
ANISOU 2055  CB  ASP A 349     1529   2054   2547    763   -388   -410       C  
ATOM   2056  CG  ASP A 349     -10.926  -2.291  13.019  1.00 31.82           C  
ANISOU 2056  CG  ASP A 349     3348   4205   4539    735   -441   -501       C  
ATOM   2057  OD1 ASP A 349     -11.485  -2.880  13.984  1.00 29.40           O  
ANISOU 2057  OD1 ASP A 349     2932   3961   4276    650   -357   -622       O  
ATOM   2058  OD2 ASP A 349     -11.276  -2.434  11.828  1.00 30.43           O  
ANISOU 2058  OD2 ASP A 349     3149   4107   4307    773   -557   -453       O  
ATOM   2059  H   ASP A 349      -7.935  -2.856  12.561  1.00 15.25           H  
ATOM   2060  HA  ASP A 349      -9.395  -1.020  11.319  1.00 20.14           H  
ATOM   2061  HB2 ASP A 349      -9.235  -1.794  14.025  1.00 19.39           H  
ATOM   2062  HB3 ASP A 349     -10.101  -0.530  13.602  1.00 19.39           H  
ATOM   2063  N   THR A 350      -6.729  -0.092  12.697  1.00 14.24           N  
ANISOU 2063  N   THR A 350     1680   1539   2191    744   -342   -174       N  
ATOM   2064  CA  THR A 350      -5.896   1.010  13.177  1.00 14.67           C  
ANISOU 2064  CA  THR A 350     1838   1459   2278    731   -259   -138       C  
ATOM   2065  C   THR A 350      -4.772   1.390  12.230  1.00 13.38           C  
ANISOU 2065  C   THR A 350     1815   1230   2038    713   -282    -18       C  
ATOM   2066  O   THR A 350      -4.518   2.584  12.047  1.00 15.66           O  
ANISOU 2066  O   THR A 350     2172   1401   2377    743   -254     49       O  
ATOM   2067  CB  THR A 350      -5.277   0.630  14.538  1.00 13.85           C  
ANISOU 2067  CB  THR A 350     1737   1354   2171    632   -153   -237       C  
ATOM   2068  OG1 THR A 350      -6.339   0.261  15.413  1.00 16.06           O  
ANISOU 2068  OG1 THR A 350     1885   1712   2506    628   -120   -349       O  
ATOM   2069  CG2 THR A 350      -4.502   1.786  15.111  1.00 15.63           C  
ANISOU 2069  CG2 THR A 350     2050   1461   2428    606    -66   -240       C  
ATOM   2070  H   THR A 350      -6.316  -0.845  12.658  1.00 17.12           H  
ATOM   2071  HA  THR A 350      -6.458   1.792  13.293  1.00 17.64           H  
ATOM   2072  HB  THR A 350      -4.656  -0.109  14.443  1.00 16.65           H  
ATOM   2073  HG1 THR A 350      -6.531  -0.549  15.306  1.00 19.31           H  
ATOM   2074 HG21 THR A 350      -4.125   1.539  15.970  1.00 18.79           H  
ATOM   2075 HG22 THR A 350      -3.781   2.031  14.510  1.00 18.79           H  
ATOM   2076 HG23 THR A 350      -5.086   2.551  15.230  1.00 18.79           H  
ATOM   2077  N   VAL A 351      -4.101   0.412  11.619  1.00 13.72           N  
ANISOU 2077  N   VAL A 351     1903   1342   1968    662   -321      4       N  
ATOM   2078  CA  VAL A 351      -2.956   0.691  10.756  1.00 13.36           C  
ANISOU 2078  CA  VAL A 351     1989   1259   1828    625   -325    102       C  
ATOM   2079  C   VAL A 351      -3.473   1.100   9.389  1.00 15.35           C  
ANISOU 2079  C   VAL A 351     2260   1544   2028    689   -422    214       C  
ATOM   2080  O   VAL A 351      -4.354   0.441   8.822  1.00 15.44           O  
ANISOU 2080  O   VAL A 351     2190   1674   2004    729   -511    198       O  
ATOM   2081  CB  VAL A 351      -2.027  -0.528  10.666  1.00 14.53           C  
ANISOU 2081  CB  VAL A 351     2160   1488   1875    535   -302     68       C  
ATOM   2082  CG1 VAL A 351      -0.860  -0.243   9.756  1.00 17.85           C  
ANISOU 2082  CG1 VAL A 351     2694   1899   2188    482   -286    150       C  
ATOM   2083  CG2 VAL A 351      -1.537  -0.934  12.086  1.00 13.53           C  
ANISOU 2083  CG2 VAL A 351     1995   1356   1789    461   -207    -18       C  
ATOM   2084  H   VAL A 351      -4.292  -0.424  11.689  1.00 16.50           H  
ATOM   2085  HA  VAL A 351      -2.443   1.427  11.125  1.00 16.07           H  
ATOM   2086  HB  VAL A 351      -2.519  -1.274  10.289  1.00 17.48           H  
ATOM   2087 HG11 VAL A 351      -0.281  -1.021   9.731  1.00 21.46           H  
ATOM   2088 HG12 VAL A 351      -1.193  -0.049   8.866  1.00 21.46           H  
ATOM   2089 HG13 VAL A 351      -0.371   0.522  10.100  1.00 21.46           H  
ATOM   2090 HG21 VAL A 351      -0.941  -1.695  12.009  1.00 16.27           H  
ATOM   2091 HG22 VAL A 351      -1.066  -0.185  12.484  1.00 16.27           H  
ATOM   2092 HG23 VAL A 351      -2.305  -1.168  12.631  1.00 16.27           H  
ATOM   2093  N   ARG A 352      -2.963   2.215   8.881  1.00 13.50           N  
ANISOU 2093  N   ARG A 352     2126   1213   1792    689   -404    326       N  
ATOM   2094  CA  ARG A 352      -3.336   2.704   7.574  1.00 15.25           C  
ANISOU 2094  CA  ARG A 352     2377   1467   1951    738   -491    466       C  
ATOM   2095  C   ARG A 352      -2.209   2.627   6.572  1.00 16.29           C  
ANISOU 2095  C   ARG A 352     2636   1635   1921    650   -483    553       C  
ATOM   2096  O   ARG A 352      -2.477   2.659   5.362  1.00 17.30           O  
ANISOU 2096  O   ARG A 352     2778   1858   1939    662   -562    656       O  
ATOM   2097  CB  ARG A 352      -3.834   4.152   7.688  1.00 19.20           C  
ANISOU 2097  CB  ARG A 352     2885   1817   2595    821   -479    554       C  
ATOM   2098  CG  ARG A 352      -5.172   4.262   8.408  1.00 18.86           C  
ANISOU 2098  CG  ARG A 352     2696   1775   2696    930   -494    479       C  
ATOM   2099  CD  ARG A 352      -5.668   5.712   8.466  1.00 27.29           C  
ANISOU 2099  CD  ARG A 352     3768   2675   3924   1035   -473    570       C  
ATOM   2100  NE  ARG A 352      -4.779   6.548   9.257  1.00 46.53           N  
ANISOU 2100  NE  ARG A 352     6296   4924   6460    970   -348    534       N  
ATOM   2101  CZ  ARG A 352      -4.795   6.609  10.586  1.00 54.78           C  
ANISOU 2101  CZ  ARG A 352     7297   5914   7605    946   -238    377       C  
ATOM   2102  NH1 ARG A 352      -3.938   7.395  11.222  1.00 37.51           N  
ANISOU 2102  NH1 ARG A 352     5184   3564   5503    864   -143    329       N  
ATOM   2103  NH2 ARG A 352      -5.661   5.879  11.282  1.00 51.81           N  
ANISOU 2103  NH2 ARG A 352     6800   5655   7231    984   -234    255       N  
ATOM   2104  H   ARG A 352      -2.390   2.711   9.287  1.00 16.03           H  
ATOM   2105  HA  ARG A 352      -4.069   2.176   7.221  1.00 18.13           H  
ATOM   2106  HB2 ARG A 352      -3.182   4.671   8.185  1.00 23.08           H  
ATOM   2107  HB3 ARG A 352      -3.941   4.520   6.797  1.00 23.08           H  
ATOM   2108  HG2 ARG A 352      -5.834   3.733   7.937  1.00 22.67           H  
ATOM   2109  HG3 ARG A 352      -5.074   3.938   9.317  1.00 22.67           H  
ATOM   2110  HD2 ARG A 352      -5.708   6.074   7.567  1.00 32.78           H  
ATOM   2111  HD3 ARG A 352      -6.549   5.734   8.872  1.00 32.78           H  
ATOM   2112  HE  ARG A 352      -4.205   7.034   8.838  1.00 55.87           H  
ATOM   2113 HH11 ARG A 352      -3.373   7.865  10.776  1.00 45.05           H  
ATOM   2114 HH12 ARG A 352      -3.948   7.436  12.081  1.00 45.05           H  
ATOM   2115 HH21 ARG A 352      -6.215   5.363  10.874  1.00 62.21           H  
ATOM   2116 HH22 ARG A 352      -5.668   5.923  12.141  1.00 62.21           H  
ATOM   2117  N   THR A 353      -0.973   2.505   7.036  1.00 15.34           N  
ANISOU 2117  N   THR A 353     2594   1464   1770    553   -386    510       N  
ATOM   2118  CA  THR A 353       0.147   2.265   6.147  1.00 14.42           C  
ANISOU 2118  CA  THR A 353     2578   1412   1489    451   -355    562       C  
ATOM   2119  C   THR A 353       0.200   0.776   5.802  1.00 16.76           C  
ANISOU 2119  C   THR A 353     2826   1876   1666    427   -390    471       C  
ATOM   2120  O   THR A 353      -0.630  -0.036   6.226  1.00 16.54           O  
ANISOU 2120  O   THR A 353     2692   1901   1690    480   -440    378       O  
ATOM   2121  CB  THR A 353       1.440   2.744   6.806  1.00 13.62           C  
ANISOU 2121  CB  THR A 353     2563   1204   1409    349   -229    542       C  
ATOM   2122  OG1 THR A 353       1.542   2.162   8.115  1.00 16.33           O  
ANISOU 2122  OG1 THR A 353     2829   1537   1840    344   -183    404       O  
ATOM   2123  CG2 THR A 353       1.434   4.274   6.926  1.00 19.61           C  
ANISOU 2123  CG2 THR A 353     3383   1790   2277    350   -190    627       C  
ATOM   2124  H   THR A 353      -0.758   2.557   7.867  1.00 18.44           H  
ATOM   2125  HA  THR A 353       0.033   2.766   5.324  1.00 17.34           H  
ATOM   2126  HB  THR A 353       2.206   2.480   6.273  1.00 16.31           H  
ATOM   2127  HG1 THR A 353       2.327   2.241   8.405  1.00 19.64           H  
ATOM   2128 HG21 THR A 353       2.253   4.577   7.348  1.00 23.57           H  
ATOM   2129 HG22 THR A 353       1.366   4.676   6.045  1.00 23.57           H  
ATOM   2130 HG23 THR A 353       0.678   4.562   7.462  1.00 23.57           H  
ATOM   2131  N   ASN A 354       1.226   0.387   5.065  1.00 15.14           N  
ANISOU 2131  N   ASN A 354     2680   1758   1313    326   -341    472       N  
ATOM   2132  CA  ASN A 354       1.268  -0.938   4.452  1.00 16.12           C  
ANISOU 2132  CA  ASN A 354     2739   2052   1336    285   -354    365       C  
ATOM   2133  C   ASN A 354       2.037  -1.869   5.366  1.00 13.49           C  
ANISOU 2133  C   ASN A 354     2332   1710   1084    238   -256    222       C  
ATOM   2134  O   ASN A 354       3.248  -1.707   5.535  1.00 12.23           O  
ANISOU 2134  O   ASN A 354     2198   1539    909    165   -160    211       O  
ATOM   2135  CB  ASN A 354       1.892  -0.818   3.077  1.00 14.73           C  
ANISOU 2135  CB  ASN A 354     2642   1993    960    201   -341    428       C  
ATOM   2136  CG  ASN A 354       1.174   0.205   2.225  1.00 23.78           C  
ANISOU 2136  CG  ASN A 354     3812   3150   2073    238   -422    593       C  
ATOM   2137  OD1 ASN A 354       0.042  -0.013   1.832  1.00 24.44           O  
ANISOU 2137  OD1 ASN A 354     3825   3316   2146    304   -533    605       O  
ATOM   2138  ND2 ASN A 354       1.807   1.360   1.998  1.00 28.83           N  
ANISOU 2138  ND2 ASN A 354     4543   3703   2708    196   -363    725       N  
ATOM   2139  H   ASN A 354       1.916   0.872   4.901  1.00 18.20           H  
ATOM   2140  HA  ASN A 354       0.379  -1.312   4.355  1.00 19.38           H  
ATOM   2141  HB2 ASN A 354       2.817  -0.542   3.168  1.00 17.71           H  
ATOM   2142  HB3 ASN A 354       1.844  -1.676   2.627  1.00 17.71           H  
ATOM   2143 HD21 ASN A 354       1.433   1.968   1.518  1.00 34.63           H  
ATOM   2144 HD22 ASN A 354       2.588   1.495   2.331  1.00 34.63           H  
ATOM   2145  N   VAL A 355       1.345  -2.861   5.924  1.00 12.81           N  
ANISOU 2145  N   VAL A 355     2149   1639   1081    275   -284    120       N  
ATOM   2146  CA  VAL A 355       1.908  -3.735   6.941  1.00  9.23           C  
ANISOU 2146  CA  VAL A 355     1631   1153    721    255   -209     22       C  
ATOM   2147  C   VAL A 355       1.867  -5.186   6.466  1.00 10.63           C  
ANISOU 2147  C   VAL A 355     1759   1402    876    234   -201    -95       C  
ATOM   2148  O   VAL A 355       0.827  -5.684   6.027  1.00 12.12           O  
ANISOU 2148  O   VAL A 355     1914   1639   1052    244   -267   -139       O  
ATOM   2149  CB  VAL A 355       1.207  -3.558   8.312  1.00 12.43           C  
ANISOU 2149  CB  VAL A 355     1984   1473   1266    302   -218     15       C  
ATOM   2150  CG1 VAL A 355      -0.265  -3.828   8.213  1.00 17.34           C  
ANISOU 2150  CG1 VAL A 355     2548   2118   1923    354   -301     -8       C  
ATOM   2151  CG2 VAL A 355       1.841  -4.446   9.348  1.00 12.29           C  
ANISOU 2151  CG2 VAL A 355     1916   1439   1315    279   -152    -49       C  
ATOM   2152  H   VAL A 355       0.530  -3.049   5.721  1.00 15.41           H  
ATOM   2153  HA  VAL A 355       2.844  -3.507   7.051  1.00 11.02           H  
ATOM   2154  HB  VAL A 355       1.317  -2.636   8.591  1.00 14.95           H  
ATOM   2155 HG11 VAL A 355      -0.668  -3.703   9.087  1.00 20.85           H  
ATOM   2156 HG12 VAL A 355      -0.657  -3.210   7.577  1.00 20.85           H  
ATOM   2157 HG13 VAL A 355      -0.399  -4.741   7.914  1.00 20.85           H  
ATOM   2158 HG21 VAL A 355       1.402  -4.299  10.201  1.00 14.79           H  
ATOM   2159 HG22 VAL A 355       1.737  -5.371   9.077  1.00 14.79           H  
ATOM   2160 HG23 VAL A 355       2.783  -4.226   9.419  1.00 14.79           H  
ATOM   2161  N   TYR A 356       3.006  -5.845   6.565  1.00 10.21           N  
ANISOU 2161  N   TYR A 356     1693   1356    832    204   -117   -156       N  
ATOM   2162  CA  TYR A 356       3.221  -7.229   6.184  1.00 11.49           C  
ANISOU 2162  CA  TYR A 356     1817   1542   1007    192    -79   -280       C  
ATOM   2163  C   TYR A 356       3.428  -8.004   7.474  1.00  8.54           C  
ANISOU 2163  C   TYR A 356     1393   1070    782    230    -43   -300       C  
ATOM   2164  O   TYR A 356       4.468  -7.856   8.134  1.00  9.76           O  
ANISOU 2164  O   TYR A 356     1529   1209    971    246      5   -270       O  
ATOM   2165  CB  TYR A 356       4.423  -7.343   5.262  1.00 11.76           C  
ANISOU 2165  CB  TYR A 356     1865   1659    942    148     -4   -332       C  
ATOM   2166  CG  TYR A 356       4.135  -6.720   3.902  1.00 15.42           C  
ANISOU 2166  CG  TYR A 356     2391   2244   1223     91    -40   -303       C  
ATOM   2167  CD1 TYR A 356       4.234  -5.351   3.706  1.00 14.96           C  
ANISOU 2167  CD1 TYR A 356     2404   2197   1082     71    -65   -159       C  
ATOM   2168  CD2 TYR A 356       3.745  -7.511   2.848  1.00 13.37           C  
ANISOU 2168  CD2 TYR A 356     2125   2084    872     52    -50   -418       C  
ATOM   2169  CE1 TYR A 356       3.960  -4.783   2.462  1.00 16.87           C  
ANISOU 2169  CE1 TYR A 356     2718   2550   1142     24   -108    -94       C  
ATOM   2170  CE2 TYR A 356       3.467  -6.959   1.613  1.00 16.00           C  
ANISOU 2170  CE2 TYR A 356     2513   2564   1003     -6    -97   -378       C  
ATOM   2171  CZ  TYR A 356       3.575  -5.590   1.445  1.00 15.32           C  
ANISOU 2171  CZ  TYR A 356     2505   2487    830    -12   -131   -198       C  
ATOM   2172  OH  TYR A 356       3.299  -5.060   0.194  1.00 19.83           O  
ANISOU 2172  OH  TYR A 356     3135   3181   1220    -49   -182   -122       O  
ATOM   2173  H   TYR A 356       3.724  -5.485   6.873  1.00 12.29           H  
ATOM   2174  HA  TYR A 356       2.451  -7.588   5.716  1.00 13.82           H  
ATOM   2175  HB2 TYR A 356       5.177  -6.880   5.658  1.00 14.14           H  
ATOM   2176  HB3 TYR A 356       4.640  -8.279   5.131  1.00 14.14           H  
ATOM   2177  HD1 TYR A 356       4.487  -4.804   4.414  1.00 17.98           H  
ATOM   2178  HD2 TYR A 356       3.667  -8.430   2.968  1.00 16.08           H  
ATOM   2179  HE1 TYR A 356       4.040  -3.866   2.334  1.00 20.28           H  
ATOM   2180  HE2 TYR A 356       3.211  -7.502   0.902  1.00 19.24           H  
ATOM   2181  HH  TYR A 356       2.468  -5.009   0.081  1.00 23.84           H  
ATOM   2182  N   LEU A 357       2.438  -8.824   7.823  1.00 10.27           N  
ANISOU 2182  N   LEU A 357     1587   1236   1079    236    -69   -343       N  
ATOM   2183  CA  LEU A 357       2.434  -9.553   9.092  1.00  9.42           C  
ANISOU 2183  CA  LEU A 357     1450   1029   1098    262    -41   -328       C  
ATOM   2184  C   LEU A 357       2.974 -10.960   8.895  1.00 11.96           C  
ANISOU 2184  C   LEU A 357     1766   1284   1496    276     20   -413       C  
ATOM   2185  O   LEU A 357       2.492 -11.704   8.026  1.00 12.64           O  
ANISOU 2185  O   LEU A 357     1858   1365   1579    238     30   -526       O  
ATOM   2186  CB  LEU A 357       1.022  -9.641   9.641  1.00  9.55           C  
ANISOU 2186  CB  LEU A 357     1446   1017   1164    242    -84   -323       C  
ATOM   2187  CG  LEU A 357       0.392  -8.314  10.057  1.00 11.71           C  
ANISOU 2187  CG  LEU A 357     1710   1328   1410    255   -135   -251       C  
ATOM   2188  CD1 LEU A 357      -1.067  -8.510  10.248  1.00 12.36           C  
ANISOU 2188  CD1 LEU A 357     1741   1419   1534    236   -174   -288       C  
ATOM   2189  CD2 LEU A 357       1.023  -7.807  11.321  1.00 12.13           C  
ANISOU 2189  CD2 LEU A 357     1762   1350   1496    271   -101   -180       C  
ATOM   2190  H   LEU A 357       1.747  -8.976   7.335  1.00 12.36           H  
ATOM   2191  HA  LEU A 357       3.005  -9.089   9.724  1.00 11.33           H  
ATOM   2192  HB2 LEU A 357       0.453 -10.030   8.958  1.00 11.49           H  
ATOM   2193  HB3 LEU A 357       1.035 -10.213  10.425  1.00 11.49           H  
ATOM   2194  HG  LEU A 357       0.537  -7.648   9.367  1.00 14.09           H  
ATOM   2195 HD11 LEU A 357      -1.465  -7.669  10.522  1.00 14.86           H  
ATOM   2196 HD12 LEU A 357      -1.458  -8.804   9.411  1.00 14.86           H  
ATOM   2197 HD13 LEU A 357      -1.208  -9.182  10.933  1.00 14.86           H  
ATOM   2198 HD21 LEU A 357       0.601  -6.971  11.571  1.00 14.59           H  
ATOM   2199 HD22 LEU A 357       0.896  -8.465  12.023  1.00 14.59           H  
ATOM   2200 HD23 LEU A 357       1.970  -7.667  11.167  1.00 14.59           H  
ATOM   2201  N   ALA A 358       3.976 -11.314   9.687  1.00 10.07           N  
ANISOU 2201  N   ALA A 358     1508    994   1326    332     60   -366       N  
ATOM   2202  CA  ALA A 358       4.576 -12.637   9.666  1.00  9.74           C  
ANISOU 2202  CA  ALA A 358     1456    851   1392    383    119   -423       C  
ATOM   2203  C   ALA A 358       4.055 -13.404  10.869  1.00 11.48           C  
ANISOU 2203  C   ALA A 358     1692    942   1727    399    115   -343       C  
ATOM   2204  O   ALA A 358       4.270 -12.986  12.014  1.00 13.87           O  
ANISOU 2204  O   ALA A 358     1979   1265   2025    423     89   -219       O  
ATOM   2205  CB  ALA A 358       6.103 -12.540   9.678  1.00 12.77           C  
ANISOU 2205  CB  ALA A 358     1790   1283   1778    456    156   -413       C  
ATOM   2206  H   ALA A 358       4.336 -10.788  10.264  1.00 12.12           H  
ATOM   2207  HA  ALA A 358       4.323 -13.115   8.861  1.00 11.51           H  
ATOM   2208  HB1 ALA A 358       6.477 -13.435   9.668  1.00 15.35           H  
ATOM   2209  HB2 ALA A 358       6.394 -12.050   8.893  1.00 15.35           H  
ATOM   2210  HB3 ALA A 358       6.383 -12.073  10.481  1.00 15.35           H  
ATOM   2211  N   VAL A 359       3.360 -14.509  10.614  1.00 10.99           N  
ANISOU 2211  N   VAL A 359     1665    769   1742    362    145   -408       N  
ATOM   2212  CA  VAL A 359       2.780 -15.357  11.652  1.00 13.18           C  
ANISOU 2212  CA  VAL A 359     1973    924   2112    344    148   -326       C  
ATOM   2213  C   VAL A 359       3.492 -16.705  11.606  1.00 15.22           C  
ANISOU 2213  C   VAL A 359     2255   1066   2462    401    180   -328       C  
ATOM   2214  O   VAL A 359       3.315 -17.483  10.663  1.00 15.33           O  
ANISOU 2214  O   VAL A 359     2291   1031   2505    368    219   -450       O  
ATOM   2215  CB  VAL A 359       1.260 -15.504  11.470  1.00 12.79           C  
ANISOU 2215  CB  VAL A 359     1936    853   2070    223    149   -398       C  
ATOM   2216  CG1 VAL A 359       0.673 -16.410  12.522  1.00 16.15           C  
ANISOU 2216  CG1 VAL A 359     2399   1148   2589    177    179   -316       C  
ATOM   2217  CG2 VAL A 359       0.588 -14.138  11.464  1.00 16.63           C  
ANISOU 2217  CG2 VAL A 359     2380   1491   2448    188     88   -390       C  
ATOM   2218  H   VAL A 359       3.205 -14.799   9.819  1.00 13.23           H  
ATOM   2219  HA  VAL A 359       2.949 -14.968  12.525  1.00 15.85           H  
ATOM   2220  HB  VAL A 359       1.087 -15.918  10.611  1.00 15.38           H  
ATOM   2221 HG11 VAL A 359      -0.287 -16.467  12.389  1.00 19.41           H  
ATOM   2222 HG12 VAL A 359       1.071 -17.290  12.439  1.00 19.41           H  
ATOM   2223 HG13 VAL A 359       0.863 -16.041  13.398  1.00 19.41           H  
ATOM   2224 HG21 VAL A 359      -0.370 -14.258  11.364  1.00 19.99           H  
ATOM   2225 HG22 VAL A 359       0.779 -13.688  12.302  1.00 19.99           H  
ATOM   2226 HG23 VAL A 359       0.935 -13.619  10.723  1.00 19.99           H  
ATOM   2227  N   PHE A 360       4.313 -16.964  12.627  1.00 16.86           N  
ANISOU 2227  N   PHE A 360     2453   1239   2715    489    158   -195       N  
ATOM   2228  CA  PHE A 360       5.146 -18.159  12.671  1.00 19.35           C  
ANISOU 2228  CA  PHE A 360     2783   1442   3127    579    174   -182       C  
ATOM   2229  C   PHE A 360       4.325 -19.448  12.720  1.00 16.86           C  
ANISOU 2229  C   PHE A 360     2549    945   2912    519    215   -198       C  
ATOM   2230  O   PHE A 360       4.631 -20.410  12.002  1.00 19.98           O  
ANISOU 2230  O   PHE A 360     2968   1240   3382    548    259   -294       O  
ATOM   2231  CB  PHE A 360       6.076 -18.064  13.890  1.00 21.21           C  
ANISOU 2231  CB  PHE A 360     2980   1705   3374    678    119    -17       C  
ATOM   2232  CG  PHE A 360       7.054 -19.193  13.998  1.00 27.70           C  
ANISOU 2232  CG  PHE A 360     3805   2424   4298    804    116      8       C  
ATOM   2233  CD1 PHE A 360       8.277 -19.116  13.363  1.00 25.01           C  
ANISOU 2233  CD1 PHE A 360     3386   2153   3965    915    122    -72       C  
ATOM   2234  CD2 PHE A 360       6.746 -20.319  14.729  1.00 35.24           C  
ANISOU 2234  CD2 PHE A 360     4840   3208   5342    815    115    111       C  
ATOM   2235  CE1 PHE A 360       9.195 -20.150  13.460  1.00 37.54           C  
ANISOU 2235  CE1 PHE A 360     4964   3644   5656   1055    119    -58       C  
ATOM   2236  CE2 PHE A 360       7.660 -21.365  14.831  1.00 35.62           C  
ANISOU 2236  CE2 PHE A 360     4896   3140   5497    952    107    140       C  
ATOM   2237  CZ  PHE A 360       8.881 -21.273  14.188  1.00 35.42           C  
ANISOU 2237  CZ  PHE A 360     4783   3189   5487   1080    106     50       C  
ATOM   2238  H   PHE A 360       4.406 -16.456  13.314  1.00 20.27           H  
ATOM   2239  HA  PHE A 360       5.677 -18.201  11.860  1.00 23.26           H  
ATOM   2240  HB2 PHE A 360       6.582 -17.239  13.831  1.00 25.49           H  
ATOM   2241  HB3 PHE A 360       5.534 -18.064  14.695  1.00 25.49           H  
ATOM   2242  HD1 PHE A 360       8.488 -18.360  12.864  1.00 30.05           H  
ATOM   2243  HD2 PHE A 360       5.923 -20.382  15.157  1.00 42.32           H  
ATOM   2244  HE1 PHE A 360      10.019 -20.085  13.034  1.00 45.08           H  
ATOM   2245  HE2 PHE A 360       7.451 -22.122  15.329  1.00 42.77           H  
ATOM   2246  HZ  PHE A 360       9.491 -21.972  14.248  1.00 42.54           H  
ATOM   2247  N   ASP A 361       3.283 -19.481  13.551  1.00 16.55           N  
ANISOU 2247  N   ASP A 361     2549    860   2878    425    213   -114       N  
ATOM   2248  CA  ASP A 361       2.536 -20.709  13.830  1.00 18.35           C  
ANISOU 2248  CA  ASP A 361     2856    907   3208    352    259    -99       C  
ATOM   2249  C   ASP A 361       1.484 -20.922  12.749  1.00 18.52           C  
ANISOU 2249  C   ASP A 361     2880    923   3236    221    308   -285       C  
ATOM   2250  O   ASP A 361       0.561 -20.110  12.621  1.00 17.20           O  
ANISOU 2250  O   ASP A 361     2676    865   2995    123    298   -333       O  
ATOM   2251  CB  ASP A 361       1.872 -20.588  15.200  1.00 19.08           C  
ANISOU 2251  CB  ASP A 361     2982    983   3283    287    250     72       C  
ATOM   2252  CG  ASP A 361       1.000 -21.776  15.560  1.00 20.20           C  
ANISOU 2252  CG  ASP A 361     3210    947   3520    181    307     99       C  
ATOM   2253  OD1 ASP A 361       0.932 -22.765  14.803  1.00 24.65           O  
ANISOU 2253  OD1 ASP A 361     3811   1377   4178    165    351    -12       O  
ATOM   2254  OD2 ASP A 361       0.380 -21.707  16.636  1.00 37.46           O  
ANISOU 2254  OD2 ASP A 361     5427   3129   5676    102    315    233       O  
ATOM   2255  H   ASP A 361       2.983 -18.794  13.973  1.00 19.68           H  
ATOM   2256  HA  ASP A 361       3.134 -21.473  13.828  1.00 21.84           H  
ATOM   2257  HB2 ASP A 361       2.563 -20.512  15.877  1.00 22.93           H  
ATOM   2258  HB3 ASP A 361       1.312 -19.796  15.207  1.00 22.93           H  
ATOM   2259  N   LYS A 362       1.611 -22.010  11.981  1.00 14.89           N  
ANISOU 2259  N   LYS A 362     2607   1085   1966    611    -42   -333       N  
ATOM   2260  CA  LYS A 362       0.654 -22.268  10.912  1.00 15.64           C  
ANISOU 2260  CA  LYS A 362     2718   1121   2103    556   -128   -466       C  
ATOM   2261  C   LYS A 362      -0.752 -22.470  11.455  1.00 19.02           C  
ANISOU 2261  C   LYS A 362     3133   1390   2704    357   -163   -413       C  
ATOM   2262  O   LYS A 362      -1.733 -22.119  10.784  1.00 15.73           O  
ANISOU 2262  O   LYS A 362     2705    980   2292    276   -216   -469       O  
ATOM   2263  CB  LYS A 362       1.079 -23.490  10.092  1.00 19.33           C  
ANISOU 2263  CB  LYS A 362     3254   1530   2562    696   -195   -612       C  
ATOM   2264  CG  LYS A 362       0.054 -23.857   9.025  1.00 21.66           C  
ANISOU 2264  CG  LYS A 362     3602   1749   2879    621   -293   -750       C  
ATOM   2265  CD  LYS A 362       0.687 -24.561   7.848  1.00 34.70           C  
ANISOU 2265  CD  LYS A 362     5310   3461   4415    802   -343   -949       C  
ATOM   2266  CE  LYS A 362      -0.356 -24.898   6.795  1.00 46.37           C  
ANISOU 2266  CE  LYS A 362     6853   4870   5896    704   -447  -1092       C  
ATOM   2267  NZ  LYS A 362      -1.357 -25.869   7.321  1.00 51.57           N  
ANISOU 2267  NZ  LYS A 362     7611   5227   6755    543   -535  -1054       N  
ATOM   2268  H   LYS A 362       2.232 -22.600  12.060  1.00 17.90           H  
ATOM   2269  HA  LYS A 362       0.647 -21.500  10.319  1.00 18.80           H  
ATOM   2270  HB2 LYS A 362       1.920 -23.298   9.650  1.00 23.23           H  
ATOM   2271  HB3 LYS A 362       1.182 -24.250  10.686  1.00 23.23           H  
ATOM   2272  HG2 LYS A 362      -0.609 -24.450   9.411  1.00 26.03           H  
ATOM   2273  HG3 LYS A 362      -0.372 -23.048   8.701  1.00 26.03           H  
ATOM   2274  HD2 LYS A 362       1.354 -23.983   7.445  1.00 41.68           H  
ATOM   2275  HD3 LYS A 362       1.100 -25.385   8.147  1.00 41.68           H  
ATOM   2276  HE2 LYS A 362      -0.823 -24.089   6.533  1.00 55.68           H  
ATOM   2277  HE3 LYS A 362       0.080 -25.295   6.025  1.00 55.68           H  
ATOM   2278  HZ1 LYS A 362      -1.667 -26.376   6.658  1.00 61.91           H  
ATOM   2279  HZ2 LYS A 362      -0.980 -26.393   7.933  1.00 61.91           H  
ATOM   2280  HZ3 LYS A 362      -2.038 -25.433   7.693  1.00 61.91           H  
ATOM   2281  N   ASN A 363      -0.878 -23.037  12.660  1.00 15.20           N  
ANISOU 2281  N   ASN A 363     2650    785   2339    276   -152   -291       N  
ATOM   2282  CA  ASN A 363      -2.203 -23.236  13.234  1.00 15.55           C  
ANISOU 2282  CA  ASN A 363     2676    734   2496     74   -202   -221       C  
ATOM   2283  C   ASN A 363      -2.896 -21.912  13.479  1.00 15.67           C  
ANISOU 2283  C   ASN A 363     2600    865   2489      2   -154   -204       C  
ATOM   2284  O   ASN A 363      -4.108 -21.785  13.250  1.00 16.83           O  
ANISOU 2284  O   ASN A 363     2694   1002   2698   -115   -227   -222       O  
ATOM   2285  CB  ASN A 363      -2.105 -24.001  14.555  1.00 16.41           C  
ANISOU 2285  CB  ASN A 363     2793    743   2698    -31   -215    -48       C  
ATOM   2286  CG  ASN A 363      -1.489 -25.355  14.384  1.00 18.63           C  
ANISOU 2286  CG  ASN A 363     3184    857   3039     59   -295    -59       C  
ATOM   2287  OD1 ASN A 363      -0.356 -25.592  14.793  1.00 22.34           O  
ANISOU 2287  OD1 ASN A 363     3667   1319   3502    196   -255     -5       O  
ATOM   2288  ND2 ASN A 363      -2.237 -26.255  13.794  1.00 20.77           N  
ANISOU 2288  ND2 ASN A 363     3539    981   3373    -17   -429   -124       N  
ATOM   2289  H   ASN A 363      -0.226 -23.308  13.151  1.00 18.27           H  
ATOM   2290  HA  ASN A 363      -2.726 -23.760  12.608  1.00 18.48           H  
ATOM   2291  HB2 ASN A 363      -1.555 -23.495  15.175  1.00 19.62           H  
ATOM   2292  HB3 ASN A 363      -2.995 -24.118  14.921  1.00 19.62           H  
ATOM   2293 HD21 ASN A 363      -1.935 -27.051  13.669  1.00 24.75           H  
ATOM   2294 HD22 ASN A 363      -3.030 -26.050  13.531  1.00 24.75           H  
ATOM   2295  N   LEU A 364      -2.150 -20.925  13.974  1.00 14.48           N  
ANISOU 2295  N   LEU A 364     2413    842   2248     69    -42   -164       N  
ATOM   2296  CA  LEU A 364      -2.713 -19.595  14.154  1.00 12.62           C  
ANISOU 2296  CA  LEU A 364     2066    753   1974     42     22   -172       C  
ATOM   2297  C   LEU A 364      -2.956 -18.919  12.814  1.00 14.06           C  
ANISOU 2297  C   LEU A 364     2270    952   2119    115    -51   -267       C  
ATOM   2298  O   LEU A 364      -4.009 -18.301  12.604  1.00 15.54           O  
ANISOU 2298  O   LEU A 364     2372   1176   2358     89    -84   -289       O  
ATOM   2299  CB  LEU A 364      -1.787 -18.762  15.020  1.00 15.83           C  
ANISOU 2299  CB  LEU A 364     2457   1279   2279     59    138   -108       C  
ATOM   2300  CG  LEU A 364      -2.226 -17.300  15.185  1.00 13.27           C  
ANISOU 2300  CG  LEU A 364     2084   1033   1927     69    168   -156       C  
ATOM   2301  CD1 LEU A 364      -3.599 -17.186  15.729  1.00 17.22           C  
ANISOU 2301  CD1 LEU A 364     2446   1585   2513     28    184   -198       C  
ATOM   2302  CD2 LEU A 364      -1.227 -16.618  16.097  1.00 15.14           C  
ANISOU 2302  CD2 LEU A 364     2347   1358   2048     40    256   -102       C  
ATOM   2303  H   LEU A 364      -1.326 -21.001  14.209  1.00 17.41           H  
ATOM   2304  HA  LEU A 364      -3.566 -19.666  14.609  1.00 15.17           H  
ATOM   2305  HB2 LEU A 364      -1.748 -19.160  15.904  1.00 19.03           H  
ATOM   2306  HB3 LEU A 364      -0.904 -18.762  14.618  1.00 19.03           H  
ATOM   2307  HG  LEU A 364      -2.248 -16.863  14.319  1.00 15.96           H  
ATOM   2308 HD11 LEU A 364      -3.825 -16.247  15.822  1.00 20.70           H  
ATOM   2309 HD12 LEU A 364      -4.217 -17.616  15.118  1.00 20.70           H  
ATOM   2310 HD13 LEU A 364      -3.632 -17.622  16.595  1.00 20.70           H  
ATOM   2311 HD21 LEU A 364      -1.490 -15.693  16.218  1.00 18.20           H  
ATOM   2312 HD22 LEU A 364      -1.220 -17.074  16.953  1.00 18.20           H  
ATOM   2313 HD23 LEU A 364      -0.348 -16.662  15.691  1.00 18.20           H  
ATOM   2314  N   TYR A 365      -1.999 -19.013  11.898  1.00 13.97           N  
ANISOU 2314  N   TYR A 365     2344    963   2001    212    -81   -309       N  
ATOM   2315  CA  TYR A 365      -2.177 -18.409  10.578  1.00 14.33           C  
ANISOU 2315  CA  TYR A 365     2388   1085   1973    242   -166   -366       C  
ATOM   2316  C   TYR A 365      -3.479 -18.880   9.948  1.00 15.76           C  
ANISOU 2316  C   TYR A 365     2543   1196   2251    175   -268   -434       C  
ATOM   2317  O   TYR A 365      -4.263 -18.068   9.438  1.00 14.49           O  
ANISOU 2317  O   TYR A 365     2303   1095   2106    148   -326   -415       O  
ATOM   2318  CB  TYR A 365      -0.987 -18.753   9.682  1.00 12.14           C  
ANISOU 2318  CB  TYR A 365     2166    925   1520    347   -181   -418       C  
ATOM   2319  CG  TYR A 365      -1.145 -18.305   8.255  1.00 12.72           C  
ANISOU 2319  CG  TYR A 365     2214   1146   1472    343   -280   -466       C  
ATOM   2320  CD1 TYR A 365      -0.782 -17.019   7.864  1.00 14.24           C  
ANISOU 2320  CD1 TYR A 365     2356   1508   1548    292   -313   -341       C  
ATOM   2321  CD2 TYR A 365      -1.687 -19.150   7.316  1.00 14.12           C  
ANISOU 2321  CD2 TYR A 365     2426   1292   1646    354   -367   -618       C  
ATOM   2322  CE1 TYR A 365      -0.936 -16.605   6.573  1.00 13.95           C  
ANISOU 2322  CE1 TYR A 365     2273   1641   1387    250   -425   -335       C  
ATOM   2323  CE2 TYR A 365      -1.855 -18.737   6.010  1.00 15.00           C  
ANISOU 2323  CE2 TYR A 365     2489   1595   1615    322   -460   -651       C  
ATOM   2324  CZ  TYR A 365      -1.474 -17.449   5.656  1.00 15.99           C  
ANISOU 2324  CZ  TYR A 365     2534   1923   1621    267   -486   -489       C  
ATOM   2325  OH  TYR A 365      -1.660 -17.067   4.331  1.00 18.84           O  
ANISOU 2325  OH  TYR A 365     2826   2508   1825    199   -602   -479       O  
ATOM   2326  H   TYR A 365      -1.247 -19.415  12.011  1.00 16.80           H  
ATOM   2327  HA  TYR A 365      -2.210 -17.444  10.668  1.00 17.24           H  
ATOM   2328  HB2 TYR A 365      -0.195 -18.323  10.040  1.00 14.60           H  
ATOM   2329  HB3 TYR A 365      -0.870 -19.715   9.677  1.00 14.60           H  
ATOM   2330  HD1 TYR A 365      -0.429 -16.432   8.493  1.00 17.13           H  
ATOM   2331  HD2 TYR A 365      -1.944 -20.010   7.563  1.00 16.76           H  
ATOM   2332  HE1 TYR A 365      -0.673 -15.749   6.322  1.00 16.78           H  
ATOM   2333  HE2 TYR A 365      -2.218 -19.312   5.377  1.00 17.82           H  
ATOM   2334  HH  TYR A 365      -2.009 -17.695   3.896  1.00 22.64           H  
ATOM   2335  N   ASP A 366      -3.743 -20.200  10.000  1.00 16.43           N  
ANISOU 2335  N   ASP A 366     2681   1162   2399    129   -306   -484       N  
ATOM   2336  CA  ASP A 366      -4.968 -20.728   9.403  1.00 15.41           C  
ANISOU 2336  CA  ASP A 366     2550    961   2344     11   -439   -541       C  
ATOM   2337  C   ASP A 366      -6.212 -20.172  10.088  1.00 18.11           C  
ANISOU 2337  C   ASP A 366     2720   1382   2781   -101   -424   -433       C  
ATOM   2338  O   ASP A 366      -7.222 -19.898   9.419  1.00 21.13           O  
ANISOU 2338  O   ASP A 366     3007   1849   3173   -164   -506   -433       O  
ATOM   2339  CB  ASP A 366      -4.963 -22.265   9.460  1.00 19.08           C  
ANISOU 2339  CB  ASP A 366     3110   1291   2848    -49   -481   -566       C  
ATOM   2340  CG  ASP A 366      -4.010 -22.905   8.460  1.00 27.57           C  
ANISOU 2340  CG  ASP A 366     4288   2375   3814     91   -492   -705       C  
ATOM   2341  OD1 ASP A 366      -3.737 -24.139   8.600  1.00 26.37           O  
ANISOU 2341  OD1 ASP A 366     4231   2075   3713    106   -524   -739       O  
ATOM   2342  OD2 ASP A 366      -3.546 -22.222   7.525  1.00 21.52           O  
ANISOU 2342  OD2 ASP A 366     3509   1762   2908    189   -494   -788       O  
ATOM   2343  H   ASP A 366      -3.237 -20.791  10.367  1.00 19.75           H  
ATOM   2344  HA  ASP A 366      -4.998 -20.458   8.472  1.00 18.53           H  
ATOM   2345  HB2 ASP A 366      -4.694 -22.545  10.349  1.00 22.93           H  
ATOM   2346  HB3 ASP A 366      -5.857 -22.589   9.267  1.00 22.93           H  
ATOM   2347  N   LYS A 367      -6.177 -20.026  11.419  1.00 17.99           N  
ANISOU 2347  N   LYS A 367     2633   1392   2812   -121   -317   -343       N  
ATOM   2348  CA  LYS A 367      -7.326 -19.455  12.116  1.00 19.27           C  
ANISOU 2348  CA  LYS A 367     2588   1715   3020   -179   -279   -277       C  
ATOM   2349  C   LYS A 367      -7.532 -17.993  11.729  1.00 19.64           C  
ANISOU 2349  C   LYS A 367     2556   1856   3050    -25   -259   -310       C  
ATOM   2350  O   LYS A 367      -8.671 -17.540  11.560  1.00 21.19           O  
ANISOU 2350  O   LYS A 367     2586   2179   3288    -14   -298   -297       O  
ATOM   2351  CB  LYS A 367      -7.164 -19.569  13.633  1.00 21.01           C  
ANISOU 2351  CB  LYS A 367     2733   2007   3244   -230   -161   -198       C  
ATOM   2352  CG  LYS A 367      -7.370 -20.978  14.166  1.00 26.73           C  
ANISOU 2352  CG  LYS A 367     3479   2663   4014   -442   -230    -89       C  
ATOM   2353  CD  LYS A 367      -7.459 -20.984  15.681  1.00 36.65           C  
ANISOU 2353  CD  LYS A 367     4583   4102   5239   -542   -123     32       C  
ATOM   2354  H   LYS A 367      -5.516 -20.244  11.924  1.00 21.63           H  
ATOM   2355  HA  LYS A 367      -8.112 -19.965  11.863  1.00 23.16           H  
ATOM   2356  HB2 LYS A 367      -6.267 -19.290  13.872  1.00 25.25           H  
ATOM   2357  HB3 LYS A 367      -7.816 -18.992  14.061  1.00 25.25           H  
ATOM   2358  HG2 LYS A 367      -8.196 -21.340  13.809  1.00 32.11           H  
ATOM   2359  HG3 LYS A 367      -6.622 -21.535  13.901  1.00 32.11           H  
ATOM   2360  N   LEU A 368      -6.435 -17.243  11.603  1.00 14.38           N  
ANISOU 2360  N   LEU A 368     2002   1134   2326     88   -220   -329       N  
ATOM   2361  CA  LEU A 368      -6.526 -15.843  11.223  1.00 14.61           C  
ANISOU 2361  CA  LEU A 368     2011   1180   2360    205   -257   -328       C  
ATOM   2362  C   LEU A 368      -7.139 -15.698   9.835  1.00 17.43           C  
ANISOU 2362  C   LEU A 368     2333   1569   2722    197   -403   -312       C  
ATOM   2363  O   LEU A 368      -8.049 -14.888   9.615  1.00 18.19           O  
ANISOU 2363  O   LEU A 368     2312   1709   2892    271   -468   -286       O  
ATOM   2364  CB  LEU A 368      -5.129 -15.219  11.266  1.00 12.69           C  
ANISOU 2364  CB  LEU A 368     1914    883   2023    241   -231   -303       C  
ATOM   2365  CG  LEU A 368      -4.524 -15.052  12.645  1.00 14.66           C  
ANISOU 2365  CG  LEU A 368     2190   1130   2249    241   -101   -306       C  
ATOM   2366  CD1 LEU A 368      -3.058 -14.677  12.582  1.00 17.52           C  
ANISOU 2366  CD1 LEU A 368     2685   1490   2482    220    -92   -245       C  
ATOM   2367  CD2 LEU A 368      -5.263 -14.044  13.483  1.00 16.64           C  
ANISOU 2367  CD2 LEU A 368     2365   1388   2570    328    -69   -368       C  
ATOM   2368  H   LEU A 368      -5.632 -17.524  11.732  1.00 17.29           H  
ATOM   2369  HA  LEU A 368      -7.094 -15.372  11.852  1.00 17.57           H  
ATOM   2370  HB2 LEU A 368      -4.529 -15.783  10.754  1.00 15.26           H  
ATOM   2371  HB3 LEU A 368      -5.179 -14.337  10.865  1.00 15.26           H  
ATOM   2372  HG  LEU A 368      -4.602 -15.917  13.079  1.00 17.62           H  
ATOM   2373 HD11 LEU A 368      -2.716 -14.585  13.486  1.00 21.06           H  
ATOM   2374 HD12 LEU A 368      -2.573 -15.375  12.115  1.00 21.06           H  
ATOM   2375 HD13 LEU A 368      -2.967 -13.836  12.107  1.00 21.06           H  
ATOM   2376 HD21 LEU A 368      -4.831 -13.974  14.348  1.00 20.01           H  
ATOM   2377 HD22 LEU A 368      -5.244 -13.185  13.033  1.00 20.01           H  
ATOM   2378 HD23 LEU A 368      -6.181 -14.338  13.595  1.00 20.01           H  
ATOM   2379  N   VAL A 369      -6.640 -16.475   8.875  1.00 15.85           N  
ANISOU 2379  N   VAL A 369     2224   1366   2431    125   -462   -336       N  
ATOM   2380  CA  VAL A 369      -7.144 -16.370   7.514  1.00 18.98           C  
ANISOU 2380  CA  VAL A 369     2582   1846   2785     83   -603   -323       C  
ATOM   2381  C   VAL A 369      -8.615 -16.768   7.478  1.00 19.57           C  
ANISOU 2381  C   VAL A 369     2504   1984   2948      4   -660   -310       C  
ATOM   2382  O   VAL A 369      -9.437 -16.103   6.835  1.00 22.46           O  
ANISOU 2382  O   VAL A 369     2743   2450   3341     21   -760   -240       O  
ATOM   2383  CB  VAL A 369      -6.284 -17.215   6.555  1.00 23.91           C  
ANISOU 2383  CB  VAL A 369     3329   2504   3252     38   -641   -411       C  
ATOM   2384  CG1 VAL A 369      -6.981 -17.390   5.209  1.00 29.45           C  
ANISOU 2384  CG1 VAL A 369     3978   3330   3883    -54   -786   -431       C  
ATOM   2385  CG2 VAL A 369      -4.911 -16.574   6.370  1.00 23.81           C  
ANISOU 2385  CG2 VAL A 369     3386   2561   3100    106   -608   -372       C  
ATOM   2386  H   VAL A 369      -6.019 -17.059   8.986  1.00 19.05           H  
ATOM   2387  HA  VAL A 369      -7.077 -15.448   7.220  1.00 22.82           H  
ATOM   2388  HB  VAL A 369      -6.161 -18.096   6.943  1.00 28.73           H  
ATOM   2389 HG11 VAL A 369      -6.402 -17.894   4.617  1.00 35.38           H  
ATOM   2390 HG12 VAL A 369      -7.813 -17.869   5.344  1.00 35.38           H  
ATOM   2391 HG13 VAL A 369      -7.160 -16.515   4.830  1.00 35.38           H  
ATOM   2392 HG21 VAL A 369      -4.387 -17.121   5.764  1.00 28.61           H  
ATOM   2393 HG22 VAL A 369      -5.025 -15.685   5.999  1.00 28.61           H  
ATOM   2394 HG23 VAL A 369      -4.469 -16.519   7.231  1.00 28.61           H  
ATOM   2395  N   SER A 370      -8.978 -17.836   8.198  1.00 20.81           N  
ANISOU 2395  N   SER A 370     2654   2109   3146   -100   -617   -339       N  
ATOM   2396  CA  SER A 370     -10.369 -18.274   8.240  1.00 26.85           C  
ANISOU 2396  CA  SER A 370     3247   2997   3959   -234   -683   -286       C  
ATOM   2397  C   SER A 370     -11.270 -17.237   8.902  1.00 25.96           C  
ANISOU 2397  C   SER A 370     2894   3052   3918   -105   -631   -216       C  
ATOM   2398  O   SER A 370     -12.390 -16.974   8.423  1.00 24.30           O  
ANISOU 2398  O   SER A 370     2489   3021   3724   -119   -717   -149       O  
ATOM   2399  CB  SER A 370     -10.459 -19.611   8.972  1.00 31.58           C  
ANISOU 2399  CB  SER A 370     3903   3517   4578   -419   -679   -283       C  
ATOM   2400  OG  SER A 370     -11.809 -19.981   9.178  1.00 45.92           O  
ANISOU 2400  OG  SER A 370     5517   5516   6413   -599   -747   -181       O  
ATOM   2401  H   SER A 370      -8.441 -18.318   8.665  1.00 25.01           H  
ATOM   2402  HA  SER A 370     -10.686 -18.397   7.332  1.00 32.26           H  
ATOM   2403  HB2 SER A 370     -10.022 -20.293   8.439  1.00 37.93           H  
ATOM   2404  HB3 SER A 370     -10.019 -19.530   9.833  1.00 37.93           H  
ATOM   2405  HG  SER A 370     -11.846 -20.716   9.584  1.00 55.14           H  
ATOM   2406  N   SER A 371     -10.805 -16.642  10.003  1.00 22.14           N  
ANISOU 2406  N   SER A 371     2411   2535   3465     37   -497   -245       N  
ATOM   2407  CA  SER A 371     -11.581 -15.604  10.663  1.00 27.50           C  
ANISOU 2407  CA  SER A 371     2885   3360   4203    227   -446   -250       C  
ATOM   2408  C   SER A 371     -11.720 -14.369   9.798  1.00 25.50           C  
ANISOU 2408  C   SER A 371     2631   3047   4011    416   -555   -232       C  
ATOM   2409  O   SER A 371     -12.742 -13.680   9.871  1.00 29.16           O  
ANISOU 2409  O   SER A 371     2885   3652   4544    582   -587   -220       O  
ATOM   2410  CB  SER A 371     -10.935 -15.211  11.994  1.00 28.27           C  
ANISOU 2410  CB  SER A 371     3027   3420   4294    330   -290   -327       C  
ATOM   2411  OG  SER A 371     -10.863 -16.313  12.868  1.00 40.21           O  
ANISOU 2411  OG  SER A 371     4509   5017   5752    140   -208   -295       O  
ATOM   2412  H   SER A 371     -10.052 -16.821  10.379  1.00 26.60           H  
ATOM   2413  HA  SER A 371     -12.464 -15.963  10.843  1.00 33.04           H  
ATOM   2414  HB2 SER A 371     -10.038 -14.884  11.824  1.00 33.96           H  
ATOM   2415  HB3 SER A 371     -11.469 -14.515  12.409  1.00 33.96           H  
ATOM   2416  HG  SER A 371     -10.278 -16.854  12.600  1.00 48.29           H  
ATOM   2417  N  APHE A 372     -10.715 -14.084   8.975  0.53 26.11           N  
ANISOU 2417  N  APHE A 372     2919   2946   4056    396   -628   -212       N  
ATOM   2418  N  BPHE A 372     -10.722 -14.055   8.973  0.47 26.02           N  
ANISOU 2418  N  BPHE A 372     2907   2934   4046    400   -630   -212       N  
ATOM   2419  CA APHE A 372     -10.766 -12.913   8.127  0.53 27.76           C  
ANISOU 2419  CA APHE A 372     3142   3086   4317    518   -776   -136       C  
ATOM   2420  CA BPHE A 372     -10.834 -12.877   8.132  0.47 27.84           C  
ANISOU 2420  CA BPHE A 372     3142   3102   4335    527   -779   -134       C  
ATOM   2421  C  APHE A 372     -11.394 -13.189   6.769  0.53 33.67           C  
ANISOU 2421  C  APHE A 372     3796   3969   5026    401   -931    -30       C  
ATOM   2422  C  BPHE A 372     -11.370 -13.177   6.739  0.47 33.68           C  
ANISOU 2422  C  BPHE A 372     3802   3968   5026    400   -934    -28       C  
ATOM   2423  O  APHE A 372     -11.876 -12.250   6.127  0.53 47.48           O  
ANISOU 2423  O  APHE A 372     5467   5725   6847    506  -1077     80       O  
ATOM   2424  O  BPHE A 372     -11.792 -12.243   6.050  0.47 47.53           O  
ANISOU 2424  O  BPHE A 372     5489   5725   6846    496  -1084     85       O  
ATOM   2425  CB APHE A 372      -9.371 -12.325   7.924  0.53 26.11           C  
ANISOU 2425  CB APHE A 372     3172   2694   4055    508   -804   -112       C  
ATOM   2426  CB BPHE A 372      -9.480 -12.162   8.045  0.47 24.69           C  
ANISOU 2426  CB BPHE A 372     2980   2503   3899    542   -805   -116       C  
ATOM   2427  CG APHE A 372      -9.396 -10.849   7.802  0.53 24.94           C  
ANISOU 2427  CG APHE A 372     3071   2389   4017    670   -942    -42       C  
ATOM   2428  CG BPHE A 372      -9.285 -11.163   9.131  0.47 22.83           C  
ANISOU 2428  CG BPHE A 372     2806   2112   3755    727   -757   -188       C  
ATOM   2429  CD1APHE A 372      -9.319 -10.061   8.940  0.53 26.69           C  
ANISOU 2429  CD1APHE A 372     3352   2455   4334    851   -884   -145       C  
ATOM   2430  CD1BPHE A 372      -9.343  -9.804   8.877  0.47 26.38           C  
ANISOU 2430  CD1BPHE A 372     3326   2379   4318    880   -919   -132       C  
ATOM   2431  CD2APHE A 372      -9.584 -10.239   6.579  0.53 25.72           C  
ANISOU 2431  CD2APHE A 372     3155   2486   4130    643  -1153    125       C  
ATOM   2432  CD2BPHE A 372      -9.124 -11.587  10.440  0.47 27.54           C  
ANISOU 2432  CD2BPHE A 372     3393   2743   4328    743   -570   -316       C  
ATOM   2433  CE1APHE A 372      -9.393  -8.703   8.842  0.53 30.55           C  
ANISOU 2433  CE1APHE A 372     3926   2800   4883    947   -985   -100       C  
ATOM   2434  CE1BPHE A 372      -9.201  -8.893   9.890  0.47 32.92           C  
ANISOU 2434  CE1BPHE A 372     4244   3113   5151    978   -830   -231       C  
ATOM   2435  CE2APHE A 372      -9.652  -8.876   6.475  0.53 23.01           C  
ANISOU 2435  CE2APHE A 372     2880   1955   3906    770  -1306    215       C  
ATOM   2436  CE2BPHE A 372      -8.987 -10.664  11.468  0.47 25.97           C  
ANISOU 2436  CE2BPHE A 372     3252   2431   4184    912   -524   -426       C  
ATOM   2437  CZ APHE A 372      -9.552  -8.103   7.614  0.53 30.54           C  
ANISOU 2437  CZ APHE A 372     3930   2762   4911    903  -1192     82       C  
ATOM   2438  CZ BPHE A 372      -9.024  -9.323  11.186  0.47 26.18           C  
ANISOU 2438  CZ BPHE A 372     3377   2324   4246    996   -632   -383       C  
ATOM   2439  H  APHE A 372      -9.999 -14.554   8.894  0.53 31.37           H  
ATOM   2440  H  BPHE A 372      -9.991 -14.500   8.887  0.47 31.26           H  
ATOM   2441  HA APHE A 372     -11.302 -12.240   8.575  0.53 33.34           H  
ATOM   2442  HA BPHE A 372     -11.458 -12.257   8.541  0.47 33.45           H  
ATOM   2443  HB2APHE A 372      -8.815 -12.556   8.685  0.53 31.37           H  
ATOM   2444  HB2BPHE A 372      -8.770 -12.820   8.113  0.47 29.67           H  
ATOM   2445  HB3APHE A 372      -8.988 -12.689   7.111  0.53 31.37           H  
ATOM   2446  HB3BPHE A 372      -9.422 -11.698   7.196  0.47 29.67           H  
ATOM   2447  HD1APHE A 372      -9.216 -10.460   9.774  0.53 32.07           H  
ATOM   2448  HD1BPHE A 372      -9.479  -9.506   8.006  0.47 31.69           H  
ATOM   2449  HD2APHE A 372      -9.665 -10.762   5.814  0.53 30.90           H  
ATOM   2450  HD2BPHE A 372      -9.108 -12.497  10.632  0.47 33.08           H  
ATOM   2451  HE1APHE A 372      -9.337  -8.180   9.609  0.53 36.70           H  
ATOM   2452  HE1BPHE A 372      -9.225  -7.982   9.702  0.47 39.54           H  
ATOM   2453  HE2APHE A 372      -9.765  -8.474   5.644  0.53 27.43           H  
ATOM   2454  HE2BPHE A 372      -8.871 -10.954  12.344  0.47 31.20           H  
ATOM   2455  HZ APHE A 372      -9.592  -7.176   7.551  0.53 36.68           H  
ATOM   2456  HZ BPHE A 372      -8.929  -8.702  11.872  0.47 31.45           H  
ATOM   2457  N   LEU A 373     -11.407 -14.441   6.326  1.00 38.59           N  
ANISOU 2457  N   LEU A 373     4438   4683   5542    184   -925    -60       N  
ATOM   2458  CA  LEU A 373     -12.055 -14.817   5.063  1.00 46.50           C  
ANISOU 2458  CA  LEU A 373     5352   5845   6470     31  -1074     11       C  
ATOM   2459  C   LEU A 373     -11.463 -14.036   3.897  1.00 50.63           C  
ANISOU 2459  C   LEU A 373     5946   6369   6922     31  -1212    107       C  
ATOM   2460  O   LEU A 373     -10.244 -13.884   3.802  1.00 40.85           O  
ANISOU 2460  O   LEU A 373     4882   5038   5599     28  -1183     77       O  
ATOM   2461  CB  LEU A 373     -13.564 -14.584   5.144  1.00 46.49           C  
ANISOU 2461  CB  LEU A 373     5065   6047   6552     74  -1130    107       C  
ATOM   2462  H  ALEU A 373     -11.045 -15.102   6.740  0.53 46.35           H  
ATOM   2463  H  BLEU A 373     -11.065 -15.102   6.757  0.47 46.35           H  
ATOM   2464  HA  LEU A 373     -11.908 -15.761   4.899  1.00 55.83           H  
TER    2465      LEU A 373                                                      
HETATM 2466  P   CMP A 401       4.410 -10.016  22.800  0.72 13.78           P  
HETATM 2467  O1P CMP A 401       3.632  -9.756  21.587  0.72 15.13           O  
HETATM 2468  O2P CMP A 401       3.899 -11.011  23.772  0.72 18.23           O  
HETATM 2469  O5' CMP A 401       4.668  -8.689  23.665  0.72 13.04           O  
HETATM 2470  C5' CMP A 401       5.715  -8.625  24.631  0.72 13.52           C  
HETATM 2471  C4' CMP A 401       6.946  -9.051  23.912  0.72 14.28           C  
HETATM 2472  O4' CMP A 401       8.105  -9.135  24.721  0.72 16.94           O  
HETATM 2473  C3' CMP A 401       6.849 -10.439  23.359  0.72 16.58           C  
HETATM 2474  O3' CMP A 401       5.888 -10.466  22.330  0.72 13.26           O  
HETATM 2475  C2' CMP A 401       8.306 -10.737  22.960  0.72 12.02           C  
HETATM 2476  O2' CMP A 401       8.585 -10.213  21.697  0.72 12.56           O  
HETATM 2477  C1' CMP A 401       9.070  -9.894  23.996  0.72 14.30           C  
HETATM 2478  N9  CMP A 401       9.870 -10.677  24.955  0.72 14.23           N  
HETATM 2479  C8  CMP A 401      10.961 -10.188  25.632  0.72 16.00           C  
HETATM 2480  N7  CMP A 401      11.492 -11.057  26.448  0.72 16.99           N  
HETATM 2481  C5  CMP A 401      10.688 -12.181  26.326  0.72 18.58           C  
HETATM 2482  C6  CMP A 401      10.726 -13.438  26.956  0.72 23.92           C  
HETATM 2483  N6  CMP A 401      11.654 -13.787  27.845  0.72 28.73           N  
HETATM 2484  N1  CMP A 401       9.773 -14.338  26.615  0.72 21.19           N  
HETATM 2485  C2  CMP A 401       8.844 -13.981  25.720  0.72 23.63           C  
HETATM 2486  N3  CMP A 401       8.706 -12.827  25.073  0.72 22.09           N  
HETATM 2487  C4  CMP A 401       9.667 -11.955  25.424  0.72 19.13           C  
HETATM 2488  O   HOH A 501      20.914   3.628  17.338  1.00 35.53           O  
HETATM 2489  O   HOH A 502       3.834 -11.022  19.074  1.00 34.65           O  
HETATM 2490  O   HOH A 503      16.801   5.487  31.892  1.00 29.07           O  
HETATM 2491  O   HOH A 504      13.518 -16.797  26.857  1.00 32.59           O  
HETATM 2492  O   HOH A 505      -2.043 -14.794  23.147  1.00 36.46           O  
HETATM 2493  O   HOH A 506     -11.563  -7.226  10.604  1.00 27.15           O  
HETATM 2494  O   HOH A 507      -3.749  -1.639  -1.775  1.00 23.39           O  
HETATM 2495  O   HOH A 508      -0.691 -15.979  20.023  1.00 37.55           O  
HETATM 2496  O   HOH A 509      17.431  -2.193  28.596  1.00 28.26           O  
HETATM 2497  O   HOH A 510       8.807 -12.524   1.682  1.00 19.84           O  
HETATM 2498  O   HOH A 511      10.545 -16.631   5.286  1.00 31.71           O  
HETATM 2499  O   HOH A 512      19.908   0.871  30.203  1.00 30.76           O  
HETATM 2500  O   HOH A 513      12.359 -20.447  11.267  1.00 32.99           O  
HETATM 2501  O   HOH A 514      22.160   7.330  23.674  1.00 38.91           O  
HETATM 2502  O   HOH A 515      -6.888   0.700   4.541  1.00 39.53           O  
HETATM 2503  O   HOH A 516      11.170   7.458  29.456  1.00 28.94           O  
HETATM 2504  O   HOH A 517      18.358  -9.897  26.137  1.00 23.87           O  
HETATM 2505  O   HOH A 518      -4.814   3.128   4.174  1.00 22.64           O  
HETATM 2506  O   HOH A 519      -0.075  -1.603  -0.303  1.00 32.34           O  
HETATM 2507  O   HOH A 520      -6.371  -5.960  31.148  1.00 35.73           O  
HETATM 2508  O   HOH A 521     -10.780  -6.877   3.019  1.00 40.60           O  
HETATM 2509  O   HOH A 522      -5.801 -23.861  13.084  1.00 25.35           O  
HETATM 2510  O   HOH A 523      24.269  -4.340  26.903  1.00 34.08           O  
HETATM 2511  O   HOH A 524      24.632  -0.291  25.859  1.00 31.31           O  
HETATM 2512  O   HOH A 525      -0.798   7.320  19.264  1.00 33.40           O  
HETATM 2513  O   HOH A 526       6.936   2.561  31.495  1.00 33.85           O  
HETATM 2514  O   HOH A 527       3.391  -3.905  28.296  1.00 19.03           O  
HETATM 2515  O   HOH A 528      -6.921  -2.232   7.032  1.00 15.11           O  
HETATM 2516  O   HOH A 529      -4.248 -10.838  35.298  1.00 35.42           O  
HETATM 2517  O   HOH A 530       0.718   5.528  19.645  1.00 29.25           O  
HETATM 2518  O   HOH A 531      15.269   6.674  18.829  1.00 37.78           O  
HETATM 2519  O   HOH A 532      21.416  -6.508  28.630  1.00 38.39           O  
HETATM 2520  O   HOH A 533       0.285 -16.354   2.562  1.00 23.58           O  
HETATM 2521  O   HOH A 534       6.005   5.356  15.295  1.00 32.79           O  
HETATM 2522  O   HOH A 535      20.924 -10.781  25.704  1.00 30.33           O  
HETATM 2523  O   HOH A 536      -6.496   5.204  15.212  1.00 36.06           O  
HETATM 2524  O   HOH A 537       8.802   2.203   5.822  1.00 16.59           O  
HETATM 2525  O   HOH A 538       3.786   7.466   7.584  1.00 26.89           O  
HETATM 2526  O   HOH A 539      20.439  -1.312   9.422  1.00 29.05           O  
HETATM 2527  O   HOH A 540       8.072   5.823  14.627  1.00 20.47           O  
HETATM 2528  O   HOH A 541      -6.414 -10.213  31.904  1.00 38.81           O  
HETATM 2529  O   HOH A 542       4.816  -5.588  22.700  1.00 12.13           O  
HETATM 2530  O   HOH A 543       3.211   6.217  20.781  1.00 37.82           O  
HETATM 2531  O   HOH A 544      17.283  -2.126  17.499  1.00 16.81           O  
HETATM 2532  O   HOH A 545       0.854   4.112  28.631  1.00 23.77           O  
HETATM 2533  O   HOH A 546       7.383 -19.647   5.521  1.00 42.48           O  
HETATM 2534  O   HOH A 547     -10.725  -2.729  16.648  1.00 33.26           O  
HETATM 2535  O   HOH A 548       6.548 -12.806  20.986  1.00 21.57           O  
HETATM 2536  O   HOH A 549      -7.101   0.854   8.977  1.00 19.06           O  
HETATM 2537  O   HOH A 550      11.099 -17.329  24.016  1.00 36.64           O  
HETATM 2538  O   HOH A 551      11.717   6.014  26.174  1.00 22.95           O  
HETATM 2539  O   HOH A 552      21.404   3.594  21.474  1.00 29.19           O  
HETATM 2540  O   HOH A 553      19.590  11.453  29.578  1.00 27.09           O  
HETATM 2541  O   HOH A 554      12.595 -16.564  20.574  1.00 28.43           O  
HETATM 2542  O   HOH A 555       9.601  -1.962   5.594  1.00 18.25           O  
HETATM 2543  O   HOH A 556      -7.482 -10.156  23.597  1.00 33.85           O  
HETATM 2544  O   HOH A 557       8.886   5.527  17.390  1.00 19.05           O  
HETATM 2545  O   HOH A 558      18.122 -12.929  22.147  1.00 25.81           O  
HETATM 2546  O   HOH A 559      -7.685 -20.887   6.844  1.00 37.15           O  
HETATM 2547  O   HOH A 560      18.546 -11.945  24.790  1.00 43.37           O  
HETATM 2548  O   HOH A 561      16.937 -15.739  15.801  1.00 24.53           O  
HETATM 2549  O   HOH A 562     -13.131 -15.958  14.495  1.00 44.26           O  
HETATM 2550  O   HOH A 563      -1.607   2.079   2.742  1.00 23.73           O  
HETATM 2551  O   HOH A 564       0.328 -24.381  17.538  1.00 36.44           O  
HETATM 2552  O   HOH A 565      21.600 -11.253   8.380  1.00 32.14           O  
HETATM 2553  O   HOH A 566       2.765 -12.575  14.480  1.00 20.97           O  
HETATM 2554  O   HOH A 567      16.982   5.559  15.158  1.00 38.83           O  
HETATM 2555  O   HOH A 568       4.709  -2.420  31.390  1.00 26.86           O  
HETATM 2556  O   HOH A 569       3.048  -6.890  -1.985  1.00 38.60           O  
HETATM 2557  O   HOH A 570       0.789   5.023  24.712  1.00 39.78           O  
HETATM 2558  O   HOH A 571       2.903  -2.245  -0.237  1.00 29.18           O  
HETATM 2559  O   HOH A 572      -7.947  -3.532  21.676  1.00 27.84           O  
HETATM 2560  O   HOH A 573       1.778 -18.086   3.958  1.00 19.16           O  
HETATM 2561  O   HOH A 574      12.445   6.936  18.366  1.00 27.68           O  
HETATM 2562  O   HOH A 575       6.439 -13.747  23.550  1.00 25.21           O  
HETATM 2563  O   HOH A 576       6.244 -11.030  -4.602  1.00 33.56           O  
HETATM 2564  O   HOH A 577       9.816   4.178   7.485  1.00 20.21           O  
HETATM 2565  O   HOH A 578       3.115 -11.346  -1.711  1.00 31.28           O  
HETATM 2566  O   HOH A 579       9.822 -18.365   7.371  1.00 22.03           O  
HETATM 2567  O   HOH A 580      11.660  -6.503  24.454  1.00 14.94           O  
HETATM 2568  O   HOH A 581      -7.142 -16.059  23.601  1.00 44.99           O  
HETATM 2569  O   HOH A 582      19.226   7.731  22.547  1.00 42.92           O  
HETATM 2570  O   HOH A 583       5.598   6.350  21.338  1.00 32.40           O  
HETATM 2571  O   HOH A 584      24.782   3.961  27.990  1.00 33.13           O  
HETATM 2572  O   HOH A 585       2.780 -17.390  15.556  1.00 22.96           O  
HETATM 2573  O   HOH A 586       3.260 -11.871  31.340  1.00 35.64           O  
HETATM 2574  O   HOH A 587      -9.448  -2.449   2.706  1.00 31.89           O  
HETATM 2575  O   HOH A 588      26.092 -14.644  19.005  1.00 35.26           O  
HETATM 2576  O   HOH A 589       5.169 -23.313   8.131  1.00 34.22           O  
HETATM 2577  O   HOH A 590       3.390   2.758  30.653  1.00 25.09           O  
HETATM 2578  O   HOH A 591       6.989   5.724  25.003  1.00 24.74           O  
HETATM 2579  O   HOH A 592       8.292  -9.191  27.673  1.00 27.08           O  
HETATM 2580  O   HOH A 593       8.239   5.595   5.766  1.00 24.21           O  
HETATM 2581  O   HOH A 594      -3.323  -0.088  31.451  1.00 34.94           O  
HETATM 2582  O   HOH A 595       5.374 -14.485  14.345  1.00 27.67           O  
HETATM 2583  O   HOH A 596      -8.011  -5.171  29.390  1.00 34.32           O  
HETATM 2584  O   HOH A 597       1.113  -4.204  -2.906  1.00 44.91           O  
HETATM 2585  O   HOH A 598      23.124  -8.105  26.943  1.00 39.28           O  
HETATM 2586  O   HOH A 599      -0.704  -4.073  -3.704  1.00 30.47           O  
HETATM 2587  O   HOH A 600      22.154 -14.218  12.642  1.00 41.05           O  
HETATM 2588  O   HOH A 601      16.105 -15.680   4.952  1.00 39.74           O  
HETATM 2589  O   HOH A 602       6.161  -3.768  29.095  1.00 20.29           O  
HETATM 2590  O   HOH A 603     -12.993 -10.269   8.363  1.00 22.59           O  
HETATM 2591  O   HOH A 604     -11.003  -0.947   9.135  1.00 42.50           O  
HETATM 2592  O   HOH A 605      20.177  -3.957   6.711  1.00 35.40           O  
HETATM 2593  O   HOH A 606       8.282   0.135  -0.743  1.00 41.44           O  
HETATM 2594  O   HOH A 607      14.429  -2.406  -0.240  1.00 40.79           O  
HETATM 2595  O   HOH A 608      -5.059 -15.647  24.953  1.00 42.16           O  
HETATM 2596  O   HOH A 609       2.056   6.901  17.318  1.00 29.33           O  
HETATM 2597  O   HOH A 610      -9.138  -1.321  20.095  1.00 35.90           O  
HETATM 2598  O   HOH A 611      -8.806   6.932  15.511  1.00 40.86           O  
HETATM 2599  O   HOH A 612       9.422   2.212   3.175  1.00 31.94           O  
HETATM 2600  O   HOH A 613      18.206  -1.401  30.956  1.00 37.78           O  
HETATM 2601  O   HOH A 614      23.992   1.322  28.438  1.00 35.71           O  
HETATM 2602  O   HOH A 615      14.822 -17.159  14.815  1.00 40.45           O  
HETATM 2603  O   HOH A 616      14.851  -4.479  -1.931  1.00 38.53           O  
HETATM 2604  O   HOH A 617     -11.711  -2.229  27.112  1.00 46.64           O  
HETATM 2605  O   HOH A 618      -9.348  -0.671  17.518  1.00 32.58           O  
HETATM 2606  O   HOH A 619       8.275   1.757  33.551  1.00 38.73           O  
HETATM 2607  O   HOH A 620       9.467   7.827  18.382  1.00 35.27           O  
HETATM 2608  O   HOH A 621      22.668  -0.130  30.543  1.00 39.23           O  
HETATM 2609  O   HOH A 622      -9.483  -1.917   6.187  1.00 29.82           O  
HETATM 2610  O   HOH A 623      14.929 -18.515  25.266  1.00 44.23           O  
HETATM 2611  O   HOH A 624       9.221   7.163  25.321  1.00 43.22           O  
HETATM 2612  O   HOH A 625       6.694 -16.371  23.550  1.00 42.66           O  
HETATM 2613  O   HOH A 626       6.241  -2.075  -0.706  1.00 36.94           O  
HETATM 2614  O   HOH A 627      -8.211 -14.375  25.336  1.00 36.46           O  
HETATM 2615  O   HOH A 628       4.753 -13.510  18.948  1.00 32.69           O  
HETATM 2616  O   HOH A 629       8.779   8.400  14.281  1.00 35.88           O  
HETATM 2617  O   HOH A 630       8.216 -11.873  -5.737  1.00 39.29           O  
HETATM 2618  O   HOH A 631       1.869 -14.786  15.726  1.00 26.19           O  
HETATM 2619  O   HOH A 632       7.536  -0.721  34.574  1.00 44.74           O  
HETATM 2620  O   HOH A 633       4.939   0.399  32.347  1.00 33.31           O  
HETATM 2621  O   HOH A 634      11.724 -19.985   7.922  1.00 39.34           O  
HETATM 2622  O   HOH A 635       4.526 -13.869  16.611  1.00 42.67           O  
CONECT 2466 2467 2468 2469 2474                                                 
CONECT 2467 2466                                                                
CONECT 2468 2466                                                                
CONECT 2469 2466 2470                                                           
CONECT 2470 2469 2471                                                           
CONECT 2471 2470 2472 2473                                                      
CONECT 2472 2471 2477                                                           
CONECT 2473 2471 2474 2475                                                      
CONECT 2474 2466 2473                                                           
CONECT 2475 2473 2476 2477                                                      
CONECT 2476 2475                                                                
CONECT 2477 2472 2475 2478                                                      
CONECT 2478 2477 2479 2487                                                      
CONECT 2479 2478 2480                                                           
CONECT 2480 2479 2481                                                           
CONECT 2481 2480 2482 2487                                                      
CONECT 2482 2481 2483 2484                                                      
CONECT 2483 2482                                                                
CONECT 2484 2482 2485                                                           
CONECT 2485 2484 2486                                                           
CONECT 2486 2485 2487                                                           
CONECT 2487 2478 2481 2486                                                      
MASTER      356    0    1    8    7    0    4    6 1395    1   22   14          
END                                                                             



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

elNémo is maintained by Yves-Henri Sanejouand.
It was developed by Karsten Suhre.
Between 2003 and 2014, it was hosted by IGS (Marseille).
Last modification: October 18th, 2018.