CNRS Nantes University US2B US2B
home |  start a new run |  job status |  references&downloads |  examples |  help  

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


***  OXIDOREDUCTASE 11-JUN-10 3AJO  ***

elNémo ID: 2412111102262379029

Job options:

ID        	=	 2412111102262379029
JOBID     	=	 OXIDOREDUCTASE 11-JUN-10 3AJO
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


HEADER    OXIDOREDUCTASE                          11-JUN-10   3AJO              
TITLE     CRYSTAL STRUCTURE OF WILD-TYPE HUMAN FERRITIN H CHAIN                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: FERRITIN HEAVY CHAIN;                                      
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: FERRITIN H SUBUNIT, CELL PROLIFERATION-INDUCING GENE 15     
COMPND   5 PROTEIN;                                                             
COMPND   6 EC: 1.16.3.1;                                                        
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: FTH1, FTH, FTHL6, OK/SW-CL.84, PIG15;                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET21D                                    
KEYWDS    4-HELIX BUNDLE, OXIDOREDUCTASE                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.MASUDA,B.MIKAMI                                                     
REVDAT   3   01-NOV-23 3AJO    1       REMARK LINK                              
REVDAT   2   25-MAY-11 3AJO    1       JRNL                                     
REVDAT   1   25-AUG-10 3AJO    0                                                
JRNL        AUTH   T.MASUDA,F.GOTO,T.YOSHIHARA,B.MIKAMI                         
JRNL        TITL   THE UNIVERSAL MECHANISM FOR IRON TRANSLOCATION TO THE        
JRNL        TITL 2 FERROXIDASE SITE IN FERRITIN, WHICH IS MEDIATED BY THE WELL  
JRNL        TITL 3 CONSERVED TRANSIT SITE                                       
JRNL        REF    BIOCHEM.BIOPHYS.RES.COMMUN.   V. 400    94 2010              
JRNL        REFN                   ISSN 0006-291X                               
JRNL        PMID   20705053                                                     
JRNL        DOI    10.1016/J.BBRC.2010.08.017                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.52 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.6_289)                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.52                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.94                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.080                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 39430                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.171                           
REMARK   3   R VALUE            (WORKING SET) : 0.171                           
REMARK   3   FREE R VALUE                     : 0.183                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.030                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1982                            
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 19.9384 -  3.6563    1.00     3007   150  0.1801 0.1623        
REMARK   3     2  3.6563 -  2.9050    1.00     2852   140  0.1663 0.1768        
REMARK   3     3  2.9050 -  2.5386    0.99     2762   145  0.1781 0.1726        
REMARK   3     4  2.5386 -  2.3069    0.99     2711   159  0.1685 0.1804        
REMARK   3     5  2.3069 -  2.1417    0.98     2739   136  0.1581 0.1928        
REMARK   3     6  2.1417 -  2.0156    0.98     2663   147  0.1556 0.1709        
REMARK   3     7  2.0156 -  1.9147    0.97     2645   148  0.1615 0.1760        
REMARK   3     8  1.9147 -  1.8314    0.97     2627   139  0.1642 0.2049        
REMARK   3     9  1.8314 -  1.7610    0.98     2643   151  0.1603 0.1783        
REMARK   3    10  1.7610 -  1.7002    0.97     2606   151  0.1594 0.2144        
REMARK   3    11  1.7002 -  1.6471    0.96     2620   128  0.1541 0.1756        
REMARK   3    12  1.6471 -  1.6001    0.96     2587   127  0.1525 0.1717        
REMARK   3    13  1.6001 -  1.5579    0.94     2553   146  0.1646 0.2153        
REMARK   3    14  1.5579 -  1.5199    0.90     2433   115  0.1829 0.2125        
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              : 0.38                                          
REMARK   3   B_SOL              : 38.58                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.150            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL             
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 11.25                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 13.53                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : 0.00000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
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      :  0.006           1513                                  
REMARK   3   ANGLE     :  0.978           2051                                  
REMARK   3   CHIRALITY :  0.066            215                                  
REMARK   3   PLANARITY :  0.004            272                                  
REMARK   3   DIHEDRAL  : 17.562            581                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
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 3AJO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 15-JUN-10.                  
REMARK 100 THE DEPOSITION ID IS D_1000029334.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-FEB-10                          
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : 9.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL26B1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9                                
REMARK 200  MONOCHROMATOR                  : SI DOUBLE-CRYSTAL MONOCHROMATOR    
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS V                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 40578                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.520                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 30.60                              
REMARK 200  R MERGE                    (I) : 0.04900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 9.6000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.52                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.57                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 10.90                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.35200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 2.710                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: PDB ENTRY 2FHA                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 59.11                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.01                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.0M MAGNESIUM CHLORIDE, 0.1M BICINE     
REMARK 280  (PH 9.0), VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: F 4 3 2                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X,Y,-Z                                                 
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   Z,X,Y                                                   
REMARK 290       6555   Z,-X,-Y                                                 
REMARK 290       7555   -Z,-X,Y                                                 
REMARK 290       8555   -Z,X,-Y                                                 
REMARK 290       9555   Y,Z,X                                                   
REMARK 290      10555   -Y,Z,-X                                                 
REMARK 290      11555   Y,-Z,-X                                                 
REMARK 290      12555   -Y,-Z,X                                                 
REMARK 290      13555   Y,X,-Z                                                  
REMARK 290      14555   -Y,-X,-Z                                                
REMARK 290      15555   Y,-X,Z                                                  
REMARK 290      16555   -Y,X,Z                                                  
REMARK 290      17555   X,Z,-Y                                                  
REMARK 290      18555   -X,Z,Y                                                  
REMARK 290      19555   -X,-Z,-Y                                                
REMARK 290      20555   X,-Z,Y                                                  
REMARK 290      21555   Z,Y,-X                                                  
REMARK 290      22555   Z,-Y,X                                                  
REMARK 290      23555   -Z,Y,X                                                  
REMARK 290      24555   -Z,-Y,-X                                                
REMARK 290      25555   X,Y+1/2,Z+1/2                                           
REMARK 290      26555   -X,-Y+1/2,Z+1/2                                         
REMARK 290      27555   -X,Y+1/2,-Z+1/2                                         
REMARK 290      28555   X,-Y+1/2,-Z+1/2                                         
REMARK 290      29555   Z,X+1/2,Y+1/2                                           
REMARK 290      30555   Z,-X+1/2,-Y+1/2                                         
REMARK 290      31555   -Z,-X+1/2,Y+1/2                                         
REMARK 290      32555   -Z,X+1/2,-Y+1/2                                         
REMARK 290      33555   Y,Z+1/2,X+1/2                                           
REMARK 290      34555   -Y,Z+1/2,-X+1/2                                         
REMARK 290      35555   Y,-Z+1/2,-X+1/2                                         
REMARK 290      36555   -Y,-Z+1/2,X+1/2                                         
REMARK 290      37555   Y,X+1/2,-Z+1/2                                          
REMARK 290      38555   -Y,-X+1/2,-Z+1/2                                        
REMARK 290      39555   Y,-X+1/2,Z+1/2                                          
REMARK 290      40555   -Y,X+1/2,Z+1/2                                          
REMARK 290      41555   X,Z+1/2,-Y+1/2                                          
REMARK 290      42555   -X,Z+1/2,Y+1/2                                          
REMARK 290      43555   -X,-Z+1/2,-Y+1/2                                        
REMARK 290      44555   X,-Z+1/2,Y+1/2                                          
REMARK 290      45555   Z,Y+1/2,-X+1/2                                          
REMARK 290      46555   Z,-Y+1/2,X+1/2                                          
REMARK 290      47555   -Z,Y+1/2,X+1/2                                          
REMARK 290      48555   -Z,-Y+1/2,-X+1/2                                        
REMARK 290      49555   X+1/2,Y,Z+1/2                                           
REMARK 290      50555   -X+1/2,-Y,Z+1/2                                         
REMARK 290      51555   -X+1/2,Y,-Z+1/2                                         
REMARK 290      52555   X+1/2,-Y,-Z+1/2                                         
REMARK 290      53555   Z+1/2,X,Y+1/2                                           
REMARK 290      54555   Z+1/2,-X,-Y+1/2                                         
REMARK 290      55555   -Z+1/2,-X,Y+1/2                                         
REMARK 290      56555   -Z+1/2,X,-Y+1/2                                         
REMARK 290      57555   Y+1/2,Z,X+1/2                                           
REMARK 290      58555   -Y+1/2,Z,-X+1/2                                         
REMARK 290      59555   Y+1/2,-Z,-X+1/2                                         
REMARK 290      60555   -Y+1/2,-Z,X+1/2                                         
REMARK 290      61555   Y+1/2,X,-Z+1/2                                          
REMARK 290      62555   -Y+1/2,-X,-Z+1/2                                        
REMARK 290      63555   Y+1/2,-X,Z+1/2                                          
REMARK 290      64555   -Y+1/2,X,Z+1/2                                          
REMARK 290      65555   X+1/2,Z,-Y+1/2                                          
REMARK 290      66555   -X+1/2,Z,Y+1/2                                          
REMARK 290      67555   -X+1/2,-Z,-Y+1/2                                        
REMARK 290      68555   X+1/2,-Z,Y+1/2                                          
REMARK 290      69555   Z+1/2,Y,-X+1/2                                          
REMARK 290      70555   Z+1/2,-Y,X+1/2                                          
REMARK 290      71555   -Z+1/2,Y,X+1/2                                          
REMARK 290      72555   -Z+1/2,-Y,-X+1/2                                        
REMARK 290      73555   X+1/2,Y+1/2,Z                                           
REMARK 290      74555   -X+1/2,-Y+1/2,Z                                         
REMARK 290      75555   -X+1/2,Y+1/2,-Z                                         
REMARK 290      76555   X+1/2,-Y+1/2,-Z                                         
REMARK 290      77555   Z+1/2,X+1/2,Y                                           
REMARK 290      78555   Z+1/2,-X+1/2,-Y                                         
REMARK 290      79555   -Z+1/2,-X+1/2,Y                                         
REMARK 290      80555   -Z+1/2,X+1/2,-Y                                         
REMARK 290      81555   Y+1/2,Z+1/2,X                                           
REMARK 290      82555   -Y+1/2,Z+1/2,-X                                         
REMARK 290      83555   Y+1/2,-Z+1/2,-X                                         
REMARK 290      84555   -Y+1/2,-Z+1/2,X                                         
REMARK 290      85555   Y+1/2,X+1/2,-Z                                          
REMARK 290      86555   -Y+1/2,-X+1/2,-Z                                        
REMARK 290      87555   Y+1/2,-X+1/2,Z                                          
REMARK 290      88555   -Y+1/2,X+1/2,Z                                          
REMARK 290      89555   X+1/2,Z+1/2,-Y                                          
REMARK 290      90555   -X+1/2,Z+1/2,Y                                          
REMARK 290      91555   -X+1/2,-Z+1/2,-Y                                        
REMARK 290      92555   X+1/2,-Z+1/2,Y                                          
REMARK 290      93555   Z+1/2,Y+1/2,-X                                          
REMARK 290      94555   Z+1/2,-Y+1/2,X                                          
REMARK 290      95555   -Z+1/2,Y+1/2,X                                          
REMARK 290      96555   -Z+1/2,-Y+1/2,-X                                        
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY2   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   6  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY2   6 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY2   7 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY2   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   9  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   9  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY3   9  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  10  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  10  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY3  10 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY3  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  12  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY3  12  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  13  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  13  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3  13  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1  14  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  14 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3  14  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1  15  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  15 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3  15  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1  16  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  16  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3  16  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1  17  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  17  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY3  17  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY1  18 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  18  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY3  18  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY1  19 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  19  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY3  19  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY1  20  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  20  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY3  20  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY1  21  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY2  21  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  21 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  22  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY2  22  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  22  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  23  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY2  23  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  23  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  24  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY2  24  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  24 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  25  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  25  0.000000  1.000000  0.000000       91.36150            
REMARK 290   SMTRY3  25  0.000000  0.000000  1.000000       91.36150            
REMARK 290   SMTRY1  26 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  26  0.000000 -1.000000  0.000000       91.36150            
REMARK 290   SMTRY3  26  0.000000  0.000000  1.000000       91.36150            
REMARK 290   SMTRY1  27 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  27  0.000000  1.000000  0.000000       91.36150            
REMARK 290   SMTRY3  27  0.000000  0.000000 -1.000000       91.36150            
REMARK 290   SMTRY1  28  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  28  0.000000 -1.000000  0.000000       91.36150            
REMARK 290   SMTRY3  28  0.000000  0.000000 -1.000000       91.36150            
REMARK 290   SMTRY1  29  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY2  29  1.000000  0.000000  0.000000       91.36150            
REMARK 290   SMTRY3  29  0.000000  1.000000  0.000000       91.36150            
REMARK 290   SMTRY1  30  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY2  30 -1.000000  0.000000  0.000000       91.36150            
REMARK 290   SMTRY3  30  0.000000 -1.000000  0.000000       91.36150            
REMARK 290   SMTRY1  31  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY2  31 -1.000000  0.000000  0.000000       91.36150            
REMARK 290   SMTRY3  31  0.000000  1.000000  0.000000       91.36150            
REMARK 290   SMTRY1  32  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY2  32  1.000000  0.000000  0.000000       91.36150            
REMARK 290   SMTRY3  32  0.000000 -1.000000  0.000000       91.36150            
REMARK 290   SMTRY1  33  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  33  0.000000  0.000000  1.000000       91.36150            
REMARK 290   SMTRY3  33  1.000000  0.000000  0.000000       91.36150            
REMARK 290   SMTRY1  34  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  34  0.000000  0.000000  1.000000       91.36150            
REMARK 290   SMTRY3  34 -1.000000  0.000000  0.000000       91.36150            
REMARK 290   SMTRY1  35  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  35  0.000000  0.000000 -1.000000       91.36150            
REMARK 290   SMTRY3  35 -1.000000  0.000000  0.000000       91.36150            
REMARK 290   SMTRY1  36  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  36  0.000000  0.000000 -1.000000       91.36150            
REMARK 290   SMTRY3  36  1.000000  0.000000  0.000000       91.36150            
REMARK 290   SMTRY1  37  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  37  1.000000  0.000000  0.000000       91.36150            
REMARK 290   SMTRY3  37  0.000000  0.000000 -1.000000       91.36150            
REMARK 290   SMTRY1  38  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  38 -1.000000  0.000000  0.000000       91.36150            
REMARK 290   SMTRY3  38  0.000000  0.000000 -1.000000       91.36150            
REMARK 290   SMTRY1  39  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  39 -1.000000  0.000000  0.000000       91.36150            
REMARK 290   SMTRY3  39  0.000000  0.000000  1.000000       91.36150            
REMARK 290   SMTRY1  40  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  40  1.000000  0.000000  0.000000       91.36150            
REMARK 290   SMTRY3  40  0.000000  0.000000  1.000000       91.36150            
REMARK 290   SMTRY1  41  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  41  0.000000  0.000000  1.000000       91.36150            
REMARK 290   SMTRY3  41  0.000000 -1.000000  0.000000       91.36150            
REMARK 290   SMTRY1  42 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  42  0.000000  0.000000  1.000000       91.36150            
REMARK 290   SMTRY3  42  0.000000  1.000000  0.000000       91.36150            
REMARK 290   SMTRY1  43 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  43  0.000000  0.000000 -1.000000       91.36150            
REMARK 290   SMTRY3  43  0.000000 -1.000000  0.000000       91.36150            
REMARK 290   SMTRY1  44  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  44  0.000000  0.000000 -1.000000       91.36150            
REMARK 290   SMTRY3  44  0.000000  1.000000  0.000000       91.36150            
REMARK 290   SMTRY1  45  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY2  45  0.000000  1.000000  0.000000       91.36150            
REMARK 290   SMTRY3  45 -1.000000  0.000000  0.000000       91.36150            
REMARK 290   SMTRY1  46  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY2  46  0.000000 -1.000000  0.000000       91.36150            
REMARK 290   SMTRY3  46  1.000000  0.000000  0.000000       91.36150            
REMARK 290   SMTRY1  47  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY2  47  0.000000  1.000000  0.000000       91.36150            
REMARK 290   SMTRY3  47  1.000000  0.000000  0.000000       91.36150            
REMARK 290   SMTRY1  48  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY2  48  0.000000 -1.000000  0.000000       91.36150            
REMARK 290   SMTRY3  48 -1.000000  0.000000  0.000000       91.36150            
REMARK 290   SMTRY1  49  1.000000  0.000000  0.000000       91.36150            
REMARK 290   SMTRY2  49  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  49  0.000000  0.000000  1.000000       91.36150            
REMARK 290   SMTRY1  50 -1.000000  0.000000  0.000000       91.36150            
REMARK 290   SMTRY2  50  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  50  0.000000  0.000000  1.000000       91.36150            
REMARK 290   SMTRY1  51 -1.000000  0.000000  0.000000       91.36150            
REMARK 290   SMTRY2  51  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  51  0.000000  0.000000 -1.000000       91.36150            
REMARK 290   SMTRY1  52  1.000000  0.000000  0.000000       91.36150            
REMARK 290   SMTRY2  52  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  52  0.000000  0.000000 -1.000000       91.36150            
REMARK 290   SMTRY1  53  0.000000  0.000000  1.000000       91.36150            
REMARK 290   SMTRY2  53  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3  53  0.000000  1.000000  0.000000       91.36150            
REMARK 290   SMTRY1  54  0.000000  0.000000  1.000000       91.36150            
REMARK 290   SMTRY2  54 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3  54  0.000000 -1.000000  0.000000       91.36150            
REMARK 290   SMTRY1  55  0.000000  0.000000 -1.000000       91.36150            
REMARK 290   SMTRY2  55 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3  55  0.000000  1.000000  0.000000       91.36150            
REMARK 290   SMTRY1  56  0.000000  0.000000 -1.000000       91.36150            
REMARK 290   SMTRY2  56  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3  56  0.000000 -1.000000  0.000000       91.36150            
REMARK 290   SMTRY1  57  0.000000  1.000000  0.000000       91.36150            
REMARK 290   SMTRY2  57  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY3  57  1.000000  0.000000  0.000000       91.36150            
REMARK 290   SMTRY1  58  0.000000 -1.000000  0.000000       91.36150            
REMARK 290   SMTRY2  58  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY3  58 -1.000000  0.000000  0.000000       91.36150            
REMARK 290   SMTRY1  59  0.000000  1.000000  0.000000       91.36150            
REMARK 290   SMTRY2  59  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY3  59 -1.000000  0.000000  0.000000       91.36150            
REMARK 290   SMTRY1  60  0.000000 -1.000000  0.000000       91.36150            
REMARK 290   SMTRY2  60  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY3  60  1.000000  0.000000  0.000000       91.36150            
REMARK 290   SMTRY1  61  0.000000  1.000000  0.000000       91.36150            
REMARK 290   SMTRY2  61  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3  61  0.000000  0.000000 -1.000000       91.36150            
REMARK 290   SMTRY1  62  0.000000 -1.000000  0.000000       91.36150            
REMARK 290   SMTRY2  62 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3  62  0.000000  0.000000 -1.000000       91.36150            
REMARK 290   SMTRY1  63  0.000000  1.000000  0.000000       91.36150            
REMARK 290   SMTRY2  63 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3  63  0.000000  0.000000  1.000000       91.36150            
REMARK 290   SMTRY1  64  0.000000 -1.000000  0.000000       91.36150            
REMARK 290   SMTRY2  64  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3  64  0.000000  0.000000  1.000000       91.36150            
REMARK 290   SMTRY1  65  1.000000  0.000000  0.000000       91.36150            
REMARK 290   SMTRY2  65  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY3  65  0.000000 -1.000000  0.000000       91.36150            
REMARK 290   SMTRY1  66 -1.000000  0.000000  0.000000       91.36150            
REMARK 290   SMTRY2  66  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY3  66  0.000000  1.000000  0.000000       91.36150            
REMARK 290   SMTRY1  67 -1.000000  0.000000  0.000000       91.36150            
REMARK 290   SMTRY2  67  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY3  67  0.000000 -1.000000  0.000000       91.36150            
REMARK 290   SMTRY1  68  1.000000  0.000000  0.000000       91.36150            
REMARK 290   SMTRY2  68  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY3  68  0.000000  1.000000  0.000000       91.36150            
REMARK 290   SMTRY1  69  0.000000  0.000000  1.000000       91.36150            
REMARK 290   SMTRY2  69  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  69 -1.000000  0.000000  0.000000       91.36150            
REMARK 290   SMTRY1  70  0.000000  0.000000  1.000000       91.36150            
REMARK 290   SMTRY2  70  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  70  1.000000  0.000000  0.000000       91.36150            
REMARK 290   SMTRY1  71  0.000000  0.000000 -1.000000       91.36150            
REMARK 290   SMTRY2  71  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  71  1.000000  0.000000  0.000000       91.36150            
REMARK 290   SMTRY1  72  0.000000  0.000000 -1.000000       91.36150            
REMARK 290   SMTRY2  72  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  72 -1.000000  0.000000  0.000000       91.36150            
REMARK 290   SMTRY1  73  1.000000  0.000000  0.000000       91.36150            
REMARK 290   SMTRY2  73  0.000000  1.000000  0.000000       91.36150            
REMARK 290   SMTRY3  73  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1  74 -1.000000  0.000000  0.000000       91.36150            
REMARK 290   SMTRY2  74  0.000000 -1.000000  0.000000       91.36150            
REMARK 290   SMTRY3  74  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1  75 -1.000000  0.000000  0.000000       91.36150            
REMARK 290   SMTRY2  75  0.000000  1.000000  0.000000       91.36150            
REMARK 290   SMTRY3  75  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1  76  1.000000  0.000000  0.000000       91.36150            
REMARK 290   SMTRY2  76  0.000000 -1.000000  0.000000       91.36150            
REMARK 290   SMTRY3  76  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1  77  0.000000  0.000000  1.000000       91.36150            
REMARK 290   SMTRY2  77  1.000000  0.000000  0.000000       91.36150            
REMARK 290   SMTRY3  77  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY1  78  0.000000  0.000000  1.000000       91.36150            
REMARK 290   SMTRY2  78 -1.000000  0.000000  0.000000       91.36150            
REMARK 290   SMTRY3  78  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY1  79  0.000000  0.000000 -1.000000       91.36150            
REMARK 290   SMTRY2  79 -1.000000  0.000000  0.000000       91.36150            
REMARK 290   SMTRY3  79  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY1  80  0.000000  0.000000 -1.000000       91.36150            
REMARK 290   SMTRY2  80  1.000000  0.000000  0.000000       91.36150            
REMARK 290   SMTRY3  80  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY1  81  0.000000  1.000000  0.000000       91.36150            
REMARK 290   SMTRY2  81  0.000000  0.000000  1.000000       91.36150            
REMARK 290   SMTRY3  81  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  82  0.000000 -1.000000  0.000000       91.36150            
REMARK 290   SMTRY2  82  0.000000  0.000000  1.000000       91.36150            
REMARK 290   SMTRY3  82 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  83  0.000000  1.000000  0.000000       91.36150            
REMARK 290   SMTRY2  83  0.000000  0.000000 -1.000000       91.36150            
REMARK 290   SMTRY3  83 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  84  0.000000 -1.000000  0.000000       91.36150            
REMARK 290   SMTRY2  84  0.000000  0.000000 -1.000000       91.36150            
REMARK 290   SMTRY3  84  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  85  0.000000  1.000000  0.000000       91.36150            
REMARK 290   SMTRY2  85  1.000000  0.000000  0.000000       91.36150            
REMARK 290   SMTRY3  85  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1  86  0.000000 -1.000000  0.000000       91.36150            
REMARK 290   SMTRY2  86 -1.000000  0.000000  0.000000       91.36150            
REMARK 290   SMTRY3  86  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1  87  0.000000  1.000000  0.000000       91.36150            
REMARK 290   SMTRY2  87 -1.000000  0.000000  0.000000       91.36150            
REMARK 290   SMTRY3  87  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1  88  0.000000 -1.000000  0.000000       91.36150            
REMARK 290   SMTRY2  88  1.000000  0.000000  0.000000       91.36150            
REMARK 290   SMTRY3  88  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1  89  1.000000  0.000000  0.000000       91.36150            
REMARK 290   SMTRY2  89  0.000000  0.000000  1.000000       91.36150            
REMARK 290   SMTRY3  89  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY1  90 -1.000000  0.000000  0.000000       91.36150            
REMARK 290   SMTRY2  90  0.000000  0.000000  1.000000       91.36150            
REMARK 290   SMTRY3  90  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY1  91 -1.000000  0.000000  0.000000       91.36150            
REMARK 290   SMTRY2  91  0.000000  0.000000 -1.000000       91.36150            
REMARK 290   SMTRY3  91  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY1  92  1.000000  0.000000  0.000000       91.36150            
REMARK 290   SMTRY2  92  0.000000  0.000000 -1.000000       91.36150            
REMARK 290   SMTRY3  92  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY1  93  0.000000  0.000000  1.000000       91.36150            
REMARK 290   SMTRY2  93  0.000000  1.000000  0.000000       91.36150            
REMARK 290   SMTRY3  93 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  94  0.000000  0.000000  1.000000       91.36150            
REMARK 290   SMTRY2  94  0.000000 -1.000000  0.000000       91.36150            
REMARK 290   SMTRY3  94  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  95  0.000000  0.000000 -1.000000       91.36150            
REMARK 290   SMTRY2  95  0.000000  1.000000  0.000000       91.36150            
REMARK 290   SMTRY3  95  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  96  0.000000  0.000000 -1.000000       91.36150            
REMARK 290   SMTRY2  96  0.000000 -1.000000  0.000000       91.36150            
REMARK 290   SMTRY3  96 -1.000000  0.000000  0.000000        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: 24-MERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: 24-MERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 89820 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 141150 ANGSTROM**2                      
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -316.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 350   BIOMT1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 350   BIOMT1   5  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT2   5  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   5  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT1   6  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT2   6 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT1   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 350   BIOMT2   7 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   7  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT1   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 350   BIOMT2   8  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT1   9  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   9  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT3   9  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT1  10  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT2  10  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT3  10 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT1  11  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT2  11  0.000000  0.000000 -1.000000        0.00000            
REMARK 350   BIOMT3  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT1  12  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT2  12  0.000000  0.000000 -1.000000        0.00000            
REMARK 350   BIOMT3  12  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT1  13  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT2  13  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3  13  0.000000  0.000000 -1.000000        0.00000            
REMARK 350   BIOMT1  14  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT2  14 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3  14  0.000000  0.000000 -1.000000        0.00000            
REMARK 350   BIOMT1  15  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT2  15 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3  15  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1  16  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT2  16  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3  16  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1  17  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2  17  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT3  17  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT1  18 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2  18  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT3  18  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT1  19 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2  19  0.000000  0.000000 -1.000000        0.00000            
REMARK 350   BIOMT3  19  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT1  20  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2  20  0.000000  0.000000 -1.000000        0.00000            
REMARK 350   BIOMT3  20  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT1  21  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT2  21  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3  21 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT1  22  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT2  22  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3  22  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT1  23  0.000000  0.000000 -1.000000        0.00000            
REMARK 350   BIOMT2  23  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3  23  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT1  24  0.000000  0.000000 -1.000000        0.00000            
REMARK 350   BIOMT2  24  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3  24 -1.000000  0.000000  0.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375 MG    MG A 186  LIES ON A SPECIAL POSITION.                          
REMARK 375 MG    MG A 188  LIES ON A SPECIAL POSITION.                          
REMARK 375 MG    MG A 189  LIES ON A SPECIAL POSITION.                          
REMARK 375 MG    MG A 190  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 230  LIES ON A SPECIAL POSITION.                          
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     THR A     1                                                      
REMARK 465     THR A     2                                                      
REMARK 465     ALA A     3                                                      
REMARK 465     SER A     4                                                      
REMARK 465     ASP A   177                                                      
REMARK 465     SER A   178                                                      
REMARK 465     ASP A   179                                                      
REMARK 465     ASN A   180                                                      
REMARK 465     GLU A   181                                                      
REMARK 465     SER A   182                                                      
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    VAL A  46      -62.36   -125.54                                   
REMARK 500    GLU A  94      -48.75     76.08                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 183  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A  27   OE2                                                    
REMARK 620 2 GLU A  62   OE2  89.5                                              
REMARK 620 3 HOH A 236   O    88.3 170.4                                        
REMARK 620 4 HOH A 278   O   157.5  88.8  89.6                                  
REMARK 620 5 HOH A 279   O    84.4  72.8  97.7  73.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 184  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN A  58   OE1                                                    
REMARK 620 2 GLU A  61   OE1  93.4                                              
REMARK 620 3 HOH A 280   O    82.2  96.8                                        
REMARK 620 4 HOH A 281   O    73.9 116.0 139.9                                  
REMARK 620 5 HOH A 282   O    95.8 166.0  74.0  76.9                            
REMARK 620 6 HOH A 399   O   172.5  91.2 103.1  98.8  80.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 185  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 302   O                                                      
REMARK 620 2 HOH A 303   O    93.9                                              
REMARK 620 3 HOH A 305   O    87.3 104.8                                        
REMARK 620 4 HOH A 306   O    90.1  89.5 165.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 186  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 255   O                                                      
REMARK 620 2 HOH A 262   O    89.8                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 187  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 321   O                                                      
REMARK 620 2 HOH A 322   O    86.4                                              
REMARK 620 3 HOH A 323   O   178.8  92.4                                        
REMARK 620 4 HOH A 324   O    90.6  90.3  89.9                                  
REMARK 620 5 HOH A 325   O    85.8  83.6  93.6 173.1                            
REMARK 620 6 HOH A 326   O    91.4 176.4  89.7  92.6  93.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 183                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 184                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 185                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 186                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 187                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 188                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 189                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 190                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 191                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 192                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 193                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 194                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3AJP   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN H FERRITIN E140A MUTANT                   
REMARK 900 RELATED ID: 3AJQ   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN H FERRITIN E140Q MUTANT                   
DBREF  3AJO A    1   182  UNP    P02794   FRIH_HUMAN       2    183             
SEQRES   1 A  182  THR THR ALA SER THR SER GLN VAL ARG GLN ASN TYR HIS          
SEQRES   2 A  182  GLN ASP SER GLU ALA ALA ILE ASN ARG GLN ILE ASN LEU          
SEQRES   3 A  182  GLU LEU TYR ALA SER TYR VAL TYR LEU SER MET SER TYR          
SEQRES   4 A  182  TYR PHE ASP ARG ASP ASP VAL ALA LEU LYS ASN PHE ALA          
SEQRES   5 A  182  LYS TYR PHE LEU HIS GLN SER HIS GLU GLU ARG GLU HIS          
SEQRES   6 A  182  ALA GLU LYS LEU MET LYS LEU GLN ASN GLN ARG GLY GLY          
SEQRES   7 A  182  ARG ILE PHE LEU GLN ASP ILE LYS LYS PRO ASP CYS ASP          
SEQRES   8 A  182  ASP TRP GLU SER GLY LEU ASN ALA MET GLU CYS ALA LEU          
SEQRES   9 A  182  HIS LEU GLU LYS ASN VAL ASN GLN SER LEU LEU GLU LEU          
SEQRES  10 A  182  HIS LYS LEU ALA THR ASP LYS ASN ASP PRO HIS LEU CYS          
SEQRES  11 A  182  ASP PHE ILE GLU THR HIS TYR LEU ASN GLU GLN VAL LYS          
SEQRES  12 A  182  ALA ILE LYS GLU LEU GLY ASP HIS VAL THR ASN LEU ARG          
SEQRES  13 A  182  LYS MET GLY ALA PRO GLU SER GLY LEU ALA GLU TYR LEU          
SEQRES  14 A  182  PHE ASP LYS HIS THR LEU GLY ASP SER ASP ASN GLU SER          
HET     MG  A 183       1                                                       
HET     MG  A 184       1                                                       
HET     MG  A 185       1                                                       
HET     MG  A 186       1                                                       
HET     MG  A 187       1                                                       
HET     MG  A 188       1                                                       
HET     MG  A 189       1                                                       
HET     MG  A 190       1                                                       
HET     MG  A 191       1                                                       
HET     MG  A 192       1                                                       
HET     MG  A 193       1                                                       
HET     MG  A 194       1                                                       
HETNAM      MG MAGNESIUM ION                                                    
FORMUL   2   MG    12(MG 2+)                                                    
FORMUL  14  HOH   *229(H2 O)                                                    
HELIX    1   1 HIS A   13  PHE A   41  1                                  29
HELIX    2   2 LEU A   48  GLY A   77  1                                  30
HELIX    3   3 SER A   95  LYS A  124  1                                  30
HELIX    4   4 ASP A  126  GLY A  159  1                                  34
HELIX    5   5 SER A  163  THR A  174  1                                  12
LINK         OE2 GLU A  27                MG    MG A 183     1555   1555  2.08  
LINK         OE1 GLN A  58                MG    MG A 184     1555   1555  2.25  
LINK         OE1 GLU A  61                MG    MG A 184     1555   1555  2.25  
LINK         OE2 GLU A  62                MG    MG A 183     1555   1555  2.10  
LINK         OE1AGLN A  83                MG    MG A 191     1555   1555  2.71  
LINK        MG    MG A 183                 O   HOH A 236     1555   1555  2.11  
LINK        MG    MG A 183                 O   HOH A 278     1555   1555  2.18  
LINK        MG    MG A 183                 O   HOH A 279     1555   1555  2.46  
LINK        MG    MG A 184                 O   HOH A 280     1555   1555  2.38  
LINK        MG    MG A 184                 O   HOH A 281     1555   1555  2.40  
LINK        MG    MG A 184                 O   HOH A 282     1555   1555  2.29  
LINK        MG    MG A 184                 O   HOH A 399     1555   1555  2.57  
LINK        MG    MG A 185                 O   HOH A 302     1555   1555  2.19  
LINK        MG    MG A 185                 O   HOH A 303     1555   1555  2.14  
LINK        MG    MG A 185                 O   HOH A 305     1555   1555  2.44  
LINK        MG    MG A 185                 O   HOH A 306     1555   1555  2.29  
LINK        MG    MG A 186                 O   HOH A 255     1555   1555  2.23  
LINK        MG    MG A 186                 O   HOH A 262     1555   1555  2.23  
LINK        MG    MG A 187                 O   HOH A 321     1555   1555  2.24  
LINK        MG    MG A 187                 O   HOH A 322     1555   1555  2.21  
LINK        MG    MG A 187                 O   HOH A 323     1555   1555  2.24  
LINK        MG    MG A 187                 O   HOH A 324     1555   1555  2.20  
LINK        MG    MG A 187                 O   HOH A 325     1555   1555  2.33  
LINK        MG    MG A 187                 O   HOH A 326     1555   1555  2.17  
LINK        MG    MG A 188                 O   HOH A 377     1555   1555  2.64  
CISPEP   1 ALA A  160    PRO A  161          0         1.67                     
SITE     1 AC1  6 GLU A  27  GLU A  62  HIS A  65  HOH A 236                    
SITE     2 AC1  6 HOH A 278  HOH A 279                                          
SITE     1 AC2  6 GLN A  58  GLU A  61  HOH A 280  HOH A 281                    
SITE     2 AC2  6 HOH A 282  HOH A 399                                          
SITE     1 AC3  4 HOH A 302  HOH A 303  HOH A 305  HOH A 306                    
SITE     1 AC4  2 HOH A 255  HOH A 262                                          
SITE     1 AC5  6 HOH A 321  HOH A 322  HOH A 323  HOH A 324                    
SITE     2 AC5  6 HOH A 325  HOH A 326                                          
SITE     1 AC6  2 ASP A 131  HOH A 377                                          
SITE     1 AC7  1 HIS A 173                                                     
SITE     1 AC8  1 HIS A 173                                                     
SITE     1 AC9  2 ASN A  25  GLN A  83                                          
SITE     1 BC1  3 ARG A   9  ASN A  11  TYR A  12                               
SITE     1 BC2  3 GLN A  75  HOH A 301  HOH A 327                               
SITE     1 BC3  2 TRP A  93  CYS A 102                                          
CRYST1  182.723  182.723  182.723  90.00  90.00  90.00 F 4 3 2      96          
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      0.005473  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005473  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005473        0.00000                         
ATOM      1  N   THR A   5      22.955 -18.749  56.114  1.00 36.93           N
ATOM      2  CA  THR A   5      23.228 -19.191  54.753  1.00 30.81           C
ATOM      3  C   THR A   5      22.077 -18.773  53.837  1.00 24.11           C
ATOM      4  O   THR A   5      20.917 -18.759  54.252  1.00 34.80           O
ATOM      5  CB  THR A   5      23.443 -20.728  54.680  1.00 42.25           C
ATOM      6  OG1 THR A   5      23.872 -21.112  53.362  1.00 30.99           O
ATOM      7  CG2 THR A   5      22.160 -21.468  55.039  1.00 41.36           C
ATOM      8  N   SER A   6      22.414 -18.414  52.602  1.00 18.95           N
ATOM      9  CA  SER A   6      21.424 -18.023  51.606  1.00 14.81           C
ATOM     10  C   SER A   6      20.409 -19.131  51.352  1.00 13.69           C
ATOM     11  O   SER A   6      20.780 -20.290  51.195  1.00 14.92           O
ATOM     12  CB  SER A   6      22.126 -17.688  50.288  1.00 16.47           C
ATOM     13  OG  SER A   6      21.180 -17.553  49.237  1.00 16.53           O
ATOM     14  N   GLN A   7      19.131 -18.763  51.274  1.00  9.12           N
ATOM     15  CA  GLN A   7      18.060 -19.725  51.029  1.00  8.08           C
ATOM     16  C   GLN A   7      18.162 -20.397  49.667  1.00  9.29           C
ATOM     17  O   GLN A   7      17.521 -21.414  49.440  1.00 11.42           O
ATOM     18  CB  GLN A   7      16.682 -19.050  51.134  1.00  7.62           C
ATOM     19  CG  GLN A   7      16.409 -18.072  49.983  1.00  9.42           C
ATOM     20  CD  GLN A   7      15.227 -17.160  50.237  1.00 10.59           C
ATOM     21  OE1 GLN A   7      14.237 -17.555  50.857  1.00 11.70           O
ATOM     22  NE2 GLN A   7      15.322 -15.928  49.749  1.00  9.69           N
ATOM     23  N   VAL A   8      18.944 -19.825  48.756  1.00  8.88           N
ATOM     24  CA  VAL A   8      19.042 -20.404  47.421  1.00  8.56           C
ATOM     25  C   VAL A   8      20.270 -21.287  47.255  1.00  9.27           C
ATOM     26  O   VAL A   8      20.356 -22.061  46.309  1.00 10.19           O
ATOM     27  CB  VAL A   8      19.024 -19.333  46.279  1.00  9.49           C
ATOM     28  CG1 VAL A   8      17.797 -18.419  46.387  1.00  9.07           C
ATOM     29  CG2 VAL A   8      20.309 -18.516  46.260  1.00 11.74           C
ATOM     30  N   ARG A   9      21.218 -21.177  48.178  1.00  9.06           N
ATOM     31  CA  ARG A   9      22.507 -21.828  47.983  1.00  7.47           C
ATOM     32  C   ARG A   9      22.417 -23.343  48.001  1.00  9.80           C
ATOM     33  O   ARG A   9      21.813 -23.927  48.909  1.00 12.08           O
ATOM     34  CB  ARG A   9      23.512 -21.353  49.029  1.00  8.96           C
ATOM     35  CG  ARG A   9      24.931 -21.695  48.669  1.00  9.21           C
ATOM     36  CD  ARG A   9      25.885 -21.308  49.786  1.00 11.80           C
ATOM     37  NE  ARG A   9      27.273 -21.422  49.345  1.00  9.75           N
ATOM     38  CZ  ARG A   9      28.170 -20.444  49.425  1.00  9.94           C
ATOM     39  NH1 ARG A   9      27.849 -19.268  49.956  1.00 10.80           N
ATOM     40  NH2 ARG A   9      29.396 -20.643  48.977  1.00 11.31           N
ATOM     41  N   GLN A  10      23.045 -23.979  47.015  1.00  8.59           N
ATOM     42  CA  GLN A  10      23.005 -25.431  46.912  1.00  7.16           C
ATOM     43  C   GLN A  10      24.173 -25.897  46.061  1.00  9.48           C
ATOM     44  O   GLN A  10      24.340 -25.445  44.919  1.00  8.67           O
ATOM     45  CB  GLN A  10      21.678 -25.863  46.293  1.00 11.06           C
ATOM     46  CG  GLN A  10      21.471 -27.359  46.232  1.00 11.82           C
ATOM     47  CD  GLN A  10      20.044 -27.715  45.854  1.00 12.60           C
ATOM     48  OE1 GLN A  10      19.400 -27.015  45.064  1.00 12.86           O
ATOM     49  NE2 GLN A  10      19.537 -28.798  46.430  1.00 15.90           N
ATOM     50  N   ASN A  11      24.984 -26.796  46.619  1.00  9.43           N
ATOM     51  CA  ASN A  11      26.154 -27.342  45.925  1.00  8.18           C
ATOM     52  C   ASN A  11      27.148 -26.278  45.443  1.00  7.71           C
ATOM     53  O   ASN A  11      27.788 -26.448  44.408  1.00  8.99           O
ATOM     54  CB  ASN A  11      25.728 -28.218  44.744  1.00  7.70           C
ATOM     55  CG  ASN A  11      26.849 -29.115  44.266  1.00  8.87           C
ATOM     56  OD1 ASN A  11      27.609 -29.648  45.085  1.00 10.79           O
ATOM     57  ND2 ASN A  11      26.970 -29.285  42.954  1.00  8.33           N
ATOM     58  N   TYR A  12      27.287 -25.198  46.204  1.00  8.58           N
ATOM     59  CA  TYR A  12      28.157 -24.097  45.813  1.00  7.27           C
ATOM     60  C   TYR A  12      29.226 -23.880  46.867  1.00  8.80           C
ATOM     61  O   TYR A  12      28.967 -23.321  47.929  1.00 10.42           O
ATOM     62  CB  TYR A  12      27.313 -22.839  45.629  1.00  9.15           C
ATOM     63  CG  TYR A  12      28.003 -21.677  44.945  1.00  7.62           C
ATOM     64  CD1 TYR A  12      28.599 -21.827  43.693  1.00  8.43           C
ATOM     65  CD2 TYR A  12      28.019 -20.421  45.534  1.00  6.92           C
ATOM     66  CE1 TYR A  12      29.208 -20.752  43.051  1.00  8.29           C
ATOM     67  CE2 TYR A  12      28.634 -19.335  44.901  1.00  7.99           C
ATOM     68  CZ  TYR A  12      29.225 -19.517  43.662  1.00  7.60           C
ATOM     69  OH  TYR A  12      29.830 -18.471  43.001  1.00  9.65           O
ATOM     70  N   HIS A  13      30.436 -24.327  46.566  1.00  8.89           N
ATOM     71  CA  HIS A  13      31.490 -24.354  47.576  1.00  8.95           C
ATOM     72  C   HIS A  13      32.009 -22.956  47.879  1.00 10.80           C
ATOM     73  O   HIS A  13      32.044 -22.108  46.996  1.00  9.07           O
ATOM     74  CB  HIS A  13      32.635 -25.234  47.092  1.00 11.02           C
ATOM     75  CG  HIS A  13      33.557 -25.660  48.186  1.00  9.04           C
ATOM     76  ND1 HIS A  13      34.550 -24.844  48.679  1.00 11.03           N
ATOM     77  CD2 HIS A  13      33.634 -26.818  48.883  1.00 14.06           C
ATOM     78  CE1 HIS A  13      35.197 -25.478  49.642  1.00 11.73           C
ATOM     79  NE2 HIS A  13      34.661 -26.678  49.784  1.00 13.90           N
ATOM     80  N   GLN A  14      32.421 -22.704  49.117  1.00  9.70           N
ATOM     81  CA AGLN A  14      32.968 -21.398  49.460  0.55 10.12           C
ATOM     82  CA BGLN A  14      32.987 -21.408  49.484  0.45 10.19           C
ATOM     83  C   GLN A  14      34.192 -21.046  48.615  1.00  8.14           C
ATOM     84  O   GLN A  14      34.434 -19.872  48.331  1.00 10.09           O
ATOM     85  CB AGLN A  14      33.300 -21.322  50.953  0.55 12.91           C
ATOM     86  CB BGLN A  14      33.385 -21.394  50.966  0.45 12.93           C
ATOM     87  CG AGLN A  14      32.073 -21.299  51.849  0.55 16.96           C
ATOM     88  CG BGLN A  14      34.422 -22.442  51.339  0.45 17.69           C
ATOM     89  CD AGLN A  14      32.402 -20.877  53.268  0.55 24.71           C
ATOM     90  CD BGLN A  14      34.895 -22.327  52.781  0.45 24.97           C
ATOM     91  OE1AGLN A  14      33.390 -21.329  53.848  0.55 36.57           O
ATOM     92  OE1BGLN A  14      34.362 -21.542  53.562  0.45 28.11           O
ATOM     93  NE2AGLN A  14      31.574 -20.007  53.835  0.55 31.44           N
ATOM     94  NE2BGLN A  14      35.905 -23.114  53.137  0.45 27.12           N
ATOM     95  N   ASP A  15      34.958 -22.055  48.197  1.00  9.29           N
ATOM     96  CA  ASP A  15      36.135 -21.811  47.370  1.00 10.65           C
ATOM     97  C   ASP A  15      35.710 -21.311  45.993  1.00  8.94           C
ATOM     98  O   ASP A  15      36.379 -20.457  45.403  1.00 10.11           O
ATOM     99  CB  ASP A  15      36.990 -23.079  47.197  1.00 12.12           C
ATOM    100  CG  ASP A  15      37.661 -23.534  48.488  1.00 14.20           C
ATOM    101  OD1 ASP A  15      38.333 -24.587  48.432  1.00 17.84           O
ATOM    102  OD2 ASP A  15      37.527 -22.867  49.536  1.00 15.55           O
ATOM    103  N   SER A  16      34.612 -21.863  45.483  1.00  9.39           N
ATOM    104  CA  SER A  16      34.102 -21.465  44.174  1.00  8.74           C
ATOM    105  C   SER A  16      33.604 -20.027  44.236  1.00  9.58           C
ATOM    106  O   SER A  16      33.896 -19.218  43.350  1.00  8.76           O
ATOM    107  CB  SER A  16      32.980 -22.399  43.730  1.00  8.05           C
ATOM    108  OG  SER A  16      33.462 -23.736  43.652  1.00 10.63           O
ATOM    109  N   GLU A  17      32.871 -19.718  45.302  1.00  8.42           N
ATOM    110  CA  GLU A  17      32.405 -18.360  45.571  1.00  7.38           C
ATOM    111  C   GLU A  17      33.562 -17.354  45.548  1.00  8.71           C
ATOM    112  O   GLU A  17      33.492 -16.311  44.884  1.00  8.08           O
ATOM    113  CB  GLU A  17      31.660 -18.335  46.908  1.00  8.89           C
ATOM    114  CG  GLU A  17      31.133 -16.984  47.319  1.00  7.80           C
ATOM    115  CD  GLU A  17      30.441 -17.028  48.666  1.00 11.12           C
ATOM    116  OE1 GLU A  17      29.868 -16.004  49.080  1.00 11.08           O
ATOM    117  OE2 GLU A  17      30.491 -18.085  49.336  1.00 14.08           O
ATOM    118  N   ALA A  18      34.645 -17.675  46.247  1.00  8.36           N
ATOM    119  CA  ALA A  18      35.806 -16.799  46.274  1.00  9.14           C
ATOM    120  C   ALA A  18      36.451 -16.663  44.893  1.00  7.77           C
ATOM    121  O   ALA A  18      36.830 -15.561  44.477  1.00  8.31           O
ATOM    122  CB  ALA A  18      36.823 -17.316  47.291  1.00  8.99           C
ATOM    123  N   ALA A  19      36.578 -17.781  44.184  1.00  7.75           N
ATOM    124  CA  ALA A  19      37.174 -17.784  42.853  1.00  7.85           C
ATOM    125  C   ALA A  19      36.344 -16.947  41.875  1.00  7.80           C
ATOM    126  O   ALA A  19      36.901 -16.269  41.008  1.00  8.72           O
ATOM    127  CB  ALA A  19      37.343 -19.209  42.343  1.00 10.40           C
ATOM    128  N   ILE A  20      35.023 -16.977  42.026  1.00  7.82           N
ATOM    129  CA  ILE A  20      34.171 -16.147  41.187  1.00  7.35           C
ATOM    130  C   ILE A  20      34.405 -14.654  41.466  1.00  7.85           C
ATOM    131  O   ILE A  20      34.466 -13.839  40.533  1.00  7.57           O
ATOM    132  CB  ILE A  20      32.680 -16.534  41.351  1.00  6.17           C
ATOM    133  CG1 ILE A  20      32.395 -17.881  40.670  1.00  8.02           C
ATOM    134  CG2 ILE A  20      31.741 -15.424  40.821  1.00  7.89           C
ATOM    135  CD1 ILE A  20      32.440 -17.852  39.143  1.00  9.28           C
ATOM    136  N   ASN A  21      34.539 -14.286  42.738  1.00  7.11           N
ATOM    137  CA  ASN A  21      34.906 -12.913  43.076  1.00  6.77           C
ATOM    138  C   ASN A  21      36.245 -12.505  42.452  1.00  7.96           C
ATOM    139  O   ASN A  21      36.373 -11.401  41.920  1.00  7.66           O
ATOM    140  CB  ASN A  21      34.881 -12.683  44.597  1.00  6.55           C
ATOM    141  CG  ASN A  21      33.461 -12.552  45.128  1.00 10.77           C
ATOM    142  OD1 ASN A  21      32.573 -12.073  44.422  1.00  8.94           O
ATOM    143  ND2 ASN A  21      33.230 -12.984  46.359  1.00  8.96           N
ATOM    144  N   ARG A  22      37.239 -13.386  42.481  1.00  7.62           N
ATOM    145  CA AARG A  22      38.519 -13.059  41.855  0.64  8.56           C
ATOM    146  CA BARG A  22      38.520 -13.077  41.849  0.36  8.62           C
ATOM    147  C   ARG A  22      38.357 -12.888  40.346  1.00  7.19           C
ATOM    148  O   ARG A  22      38.986 -12.008  39.740  1.00  8.72           O
ATOM    149  CB AARG A  22      39.580 -14.112  42.179  0.64 11.09           C
ATOM    150  CB BARG A  22      39.553 -14.167  42.134  0.36 11.15           C
ATOM    151  CG AARG A  22      39.885 -14.197  43.671  0.64 13.31           C
ATOM    152  CG BARG A  22      40.077 -14.150  43.554  0.36 13.57           C
ATOM    153  CD AARG A  22      41.108 -15.063  43.951  0.64 17.14           C
ATOM    154  CD BARG A  22      41.265 -15.086  43.711  0.36 16.82           C
ATOM    155  NE AARG A  22      40.942 -16.449  43.506  0.64 20.34           N
ATOM    156  NE BARG A  22      40.885 -16.495  43.622  0.36 19.95           N
ATOM    157  CZ AARG A  22      40.488 -17.441  44.274  0.64 12.57           C
ATOM    158  CZ BARG A  22      41.068 -17.262  42.550  0.36 19.31           C
ATOM    159  NH1AARG A  22      40.140 -17.207  45.526  0.64 11.38           N
ATOM    160  NH1BARG A  22      41.634 -16.764  41.461  0.36 22.79           N
ATOM    161  NH2AARG A  22      40.375 -18.666  43.782  0.64 18.95           N
ATOM    162  NH2BARG A  22      40.693 -18.532  42.571  0.36 18.05           N
ATOM    163  N   GLN A  23      37.503 -13.712  39.744  1.00  8.22           N
ATOM    164  CA  GLN A  23      37.301 -13.607  38.306  1.00  6.31           C
ATOM    165  C   GLN A  23      36.592 -12.301  37.948  1.00  8.66           C
ATOM    166  O   GLN A  23      36.918 -11.684  36.942  1.00  7.29           O
ATOM    167  CB  GLN A  23      36.530 -14.813  37.769  1.00  7.75           C
ATOM    168  CG  GLN A  23      36.460 -14.865  36.237  1.00  7.98           C
ATOM    169  CD  GLN A  23      37.806 -15.200  35.618  1.00 10.05           C
ATOM    170  OE1 GLN A  23      38.583 -15.961  36.200  1.00  9.87           O
ATOM    171  NE2 GLN A  23      38.096 -14.629  34.443  1.00  8.73           N
ATOM    172  N   ILE A  24      35.630 -11.881  38.772  1.00  6.85           N
ATOM    173  CA  ILE A  24      34.978 -10.596  38.551  1.00  6.56           C
ATOM    174  C   ILE A  24      36.007  -9.470  38.483  1.00  8.12           C
ATOM    175  O   ILE A  24      35.969  -8.631  37.581  1.00  7.40           O
ATOM    176  CB  ILE A  24      33.938 -10.292  39.640  1.00  6.40           C
ATOM    177  CG1 ILE A  24      32.721 -11.204  39.458  1.00  8.13           C
ATOM    178  CG2 ILE A  24      33.517  -8.831  39.572  1.00  7.90           C
ATOM    179  CD1 ILE A  24      31.878 -11.350  40.709  1.00  8.25           C
ATOM    180  N   ASN A  25      36.951  -9.464  39.419  1.00  6.91           N
ATOM    181  CA  ASN A  25      37.985  -8.442  39.408  1.00  7.93           C
ATOM    182  C   ASN A  25      38.825  -8.486  38.144  1.00  6.94           C
ATOM    183  O   ASN A  25      39.142  -7.444  37.580  1.00  7.53           O
ATOM    184  CB  ASN A  25      38.877  -8.555  40.641  1.00  6.57           C
ATOM    185  CG  ASN A  25      39.849  -7.405  40.754  1.00  7.57           C
ATOM    186  OD1 ASN A  25      41.009  -7.514  40.350  1.00  8.59           O
ATOM    187  ND2 ASN A  25      39.374  -6.286  41.290  1.00  7.26           N
ATOM    188  N   LEU A  26      39.171  -9.693  37.706  1.00  7.30           N
ATOM    189  CA  LEU A  26      39.987  -9.860  36.508  1.00  6.93           C
ATOM    190  C   LEU A  26      39.269  -9.349  35.258  1.00  7.15           C
ATOM    191  O   LEU A  26      39.894  -8.715  34.404  1.00  7.08           O
ATOM    192  CB  LEU A  26      40.426 -11.319  36.348  1.00  7.37           C
ATOM    193  CG  LEU A  26      41.406 -11.604  35.206  1.00  7.36           C
ATOM    194  CD1 LEU A  26      42.667 -10.744  35.298  1.00 11.01           C
ATOM    195  CD2 LEU A  26      41.750 -13.095  35.194  1.00  8.96           C
ATOM    196  N   GLU A  27      37.967  -9.613  35.161  1.00  7.25           N
ATOM    197  CA  GLU A  27      37.185  -9.135  34.019  1.00  6.94           C
ATOM    198  C   GLU A  27      37.139  -7.612  34.010  1.00  7.86           C
ATOM    199  O   GLU A  27      37.275  -6.985  32.951  1.00  8.59           O
ATOM    200  CB  GLU A  27      35.768  -9.708  34.045  1.00  7.41           C
ATOM    201  CG  GLU A  27      35.715 -11.239  34.033  1.00  9.69           C
ATOM    202  CD  GLU A  27      36.175 -11.847  32.731  1.00 10.67           C
ATOM    203  OE1 GLU A  27      36.493 -13.057  32.692  1.00 10.11           O
ATOM    204  OE2 GLU A  27      36.223 -11.116  31.726  1.00 10.09           O
ATOM    205  N   LEU A  28      36.969  -7.015  35.189  1.00  7.29           N
ATOM    206  CA  LEU A  28      36.961  -5.558  35.294  1.00  5.51           C
ATOM    207  C   LEU A  28      38.334  -4.980  34.940  1.00  7.60           C
ATOM    208  O   LEU A  28      38.438  -3.954  34.273  1.00  7.75           O
ATOM    209  CB  LEU A  28      36.541  -5.127  36.705  1.00  6.29           C
ATOM    210  CG  LEU A  28      35.081  -5.438  37.044  1.00  7.39           C
ATOM    211  CD1 LEU A  28      34.825  -5.267  38.532  1.00  9.91           C
ATOM    212  CD2 LEU A  28      34.127  -4.563  36.210  1.00 10.92           C
ATOM    213  N   TYR A  29      39.389  -5.647  35.393  1.00  7.14           N
ATOM    214  CA  TYR A  29      40.734  -5.261  35.010  1.00  6.57           C
ATOM    215  C   TYR A  29      40.918  -5.296  33.487  1.00  7.84           C
ATOM    216  O   TYR A  29      41.454  -4.354  32.902  1.00  7.36           O
ATOM    217  CB  TYR A  29      41.757  -6.162  35.705  1.00  7.26           C
ATOM    218  CG  TYR A  29      43.162  -5.928  35.226  1.00  7.45           C
ATOM    219  CD1 TYR A  29      43.757  -6.799  34.312  1.00  8.46           C
ATOM    220  CD2 TYR A  29      43.889  -4.815  35.655  1.00  9.27           C
ATOM    221  CE1 TYR A  29      45.051  -6.583  33.851  1.00  8.72           C
ATOM    222  CE2 TYR A  29      45.187  -4.595  35.205  1.00  9.45           C
ATOM    223  CZ  TYR A  29      45.756  -5.480  34.302  1.00  9.11           C
ATOM    224  OH  TYR A  29      47.040  -5.259  33.840  1.00 13.21           O
ATOM    225  N   ALA A  30      40.462  -6.372  32.847  1.00  6.34           N
ATOM    226  CA  ALA A  30      40.565  -6.464  31.395  1.00  6.45           C
ATOM    227  C   ALA A  30      39.797  -5.333  30.723  1.00  7.48           C
ATOM    228  O   ALA A  30      40.261  -4.763  29.728  1.00  7.77           O
ATOM    229  CB  ALA A  30      40.070  -7.816  30.910  1.00  7.96           C
ATOM    230  N   SER A  31      38.634  -4.989  31.268  1.00  6.62           N
ATOM    231  CA  SER A  31      37.878  -3.871  30.713  1.00  5.60           C
ATOM    232  C   SER A  31      38.716  -2.591  30.753  1.00  7.51           C
ATOM    233  O   SER A  31      38.707  -1.789  29.816  1.00  8.15           O
ATOM    234  CB  SER A  31      36.575  -3.673  31.479  1.00  8.08           C
ATOM    235  OG  SER A  31      35.806  -2.647  30.864  1.00 11.20           O
ATOM    236  N   TYR A  32      39.442  -2.405  31.851  1.00  7.52           N
ATOM    237  CA  TYR A  32      40.230  -1.188  32.055  1.00  7.37           C
ATOM    238  C   TYR A  32      41.440  -1.149  31.118  1.00  7.28           C
ATOM    239  O   TYR A  32      41.765  -0.096  30.561  1.00  7.67           O
ATOM    240  CB  TYR A  32      40.671  -1.130  33.524  1.00  7.74           C
ATOM    241  CG  TYR A  32      41.020   0.236  34.087  1.00  6.73           C
ATOM    242  CD1 TYR A  32      40.684   1.416  33.435  1.00  6.84           C
ATOM    243  CD2 TYR A  32      41.665   0.337  35.316  1.00  6.11           C
ATOM    244  CE1 TYR A  32      41.004   2.654  33.984  1.00  8.03           C
ATOM    245  CE2 TYR A  32      41.971   1.557  35.871  1.00  6.36           C
ATOM    246  CZ  TYR A  32      41.638   2.712  35.206  1.00  7.00           C
ATOM    247  OH  TYR A  32      41.945   3.933  35.769  1.00  8.60           O
ATOM    248  N   VAL A  33      42.097  -2.291  30.931  1.00  7.86           N
ATOM    249  CA  VAL A  33      43.218  -2.382  29.991  1.00  7.75           C
ATOM    250  C   VAL A  33      42.764  -1.964  28.600  1.00  7.34           C
ATOM    251  O   VAL A  33      43.392  -1.126  27.945  1.00  8.71           O
ATOM    252  CB  VAL A  33      43.796  -3.815  29.946  1.00  8.10           C
ATOM    253  CG1 VAL A  33      44.830  -3.953  28.817  1.00  9.87           C
ATOM    254  CG2 VAL A  33      44.414  -4.185  31.298  1.00  8.55           C
ATOM    255  N   TYR A  34      41.647  -2.524  28.156  1.00  7.72           N
ATOM    256  CA  TYR A  34      41.168  -2.198  26.825  1.00  6.70           C
ATOM    257  C   TYR A  34      40.722  -0.739  26.704  1.00  8.69           C
ATOM    258  O   TYR A  34      40.878  -0.136  25.640  1.00  8.64           O
ATOM    259  CB  TYR A  34      40.036  -3.134  26.444  1.00  7.31           C
ATOM    260  CG  TYR A  34      40.459  -4.474  25.884  1.00  7.01           C
ATOM    261  CD1 TYR A  34      41.280  -4.551  24.764  1.00  8.69           C
ATOM    262  CD2 TYR A  34      39.973  -5.654  26.419  1.00  8.79           C
ATOM    263  CE1 TYR A  34      41.621  -5.773  24.209  1.00 12.40           C
ATOM    264  CE2 TYR A  34      40.310  -6.883  25.871  1.00  8.43           C
ATOM    265  CZ  TYR A  34      41.135  -6.932  24.766  1.00 10.79           C
ATOM    266  OH  TYR A  34      41.483  -8.145  24.185  1.00 15.68           O
ATOM    267  N   LEU A  35      40.157  -0.177  27.776  1.00  7.15           N
ATOM    268  CA  LEU A  35      39.796   1.239  27.780  1.00  8.17           C
ATOM    269  C   LEU A  35      41.037   2.117  27.573  1.00  8.88           C
ATOM    270  O   LEU A  35      41.023   3.064  26.768  1.00  8.21           O
ATOM    271  CB  LEU A  35      39.110   1.605  29.098  1.00  7.82           C
ATOM    272  CG  LEU A  35      38.797   3.091  29.304  1.00  8.46           C
ATOM    273  CD1 LEU A  35      37.851   3.594  28.230  1.00 10.85           C
ATOM    274  CD2 LEU A  35      38.212   3.336  30.685  1.00  8.32           C
ATOM    275  N   SER A  36      42.104   1.804  28.305  1.00  8.10           N
ATOM    276  CA  SER A  36      43.366   2.522  28.173  1.00  7.70           C
ATOM    277  C   SER A  36      43.932   2.392  26.762  1.00  7.86           C
ATOM    278  O   SER A  36      44.335   3.391  26.145  1.00  8.21           O
ATOM    279  CB  SER A  36      44.380   1.988  29.187  1.00 10.57           C
ATOM    280  OG  SER A  36      45.633   2.638  29.025  1.00 11.96           O
ATOM    281  N   MET A  37      43.964   1.166  26.240  1.00  7.89           N
ATOM    282  CA  MET A  37      44.457   0.951  24.879  1.00  8.73           C
ATOM    283  C   MET A  37      43.657   1.771  23.880  1.00  8.42           C
ATOM    284  O   MET A  37      44.224   2.392  22.977  1.00  8.67           O
ATOM    285  CB  MET A  37      44.345  -0.517  24.481  1.00 12.61           C
ATOM    286  CG  MET A  37      45.338  -1.421  25.121  1.00 12.92           C
ATOM    287  SD  MET A  37      45.026  -3.085  24.470  1.00 17.18           S
ATOM    288  CE  MET A  37      46.215  -4.018  25.417  1.00 17.03           C
ATOM    289  N   SER A  38      42.335   1.775  24.035  1.00  7.68           N
ATOM    290  CA  SER A  38      41.482   2.478  23.086  1.00  7.13           C
ATOM    291  C   SER A  38      41.892   3.938  22.957  1.00  8.57           C
ATOM    292  O   SER A  38      42.114   4.434  21.850  1.00  8.07           O
ATOM    293  CB  SER A  38      40.016   2.390  23.502  1.00  8.98           C
ATOM    294  OG  SER A  38      39.208   3.185  22.651  1.00  9.40           O
ATOM    295  N   TYR A  39      42.018   4.625  24.090  1.00  8.12           N
ATOM    296  CA  TYR A  39      42.286   6.056  24.042  1.00  7.52           C
ATOM    297  C   TYR A  39      43.721   6.398  23.652  1.00  8.23           C
ATOM    298  O   TYR A  39      43.988   7.503  23.178  1.00  8.94           O
ATOM    299  CB  TYR A  39      41.796   6.770  25.311  1.00  8.31           C
ATOM    300  CG  TYR A  39      40.298   6.933  25.244  1.00  6.59           C
ATOM    301  CD1 TYR A  39      39.448   5.945  25.734  1.00  8.36           C
ATOM    302  CD2 TYR A  39      39.719   8.036  24.601  1.00  8.03           C
ATOM    303  CE1 TYR A  39      38.066   6.063  25.623  1.00  6.96           C
ATOM    304  CE2 TYR A  39      38.331   8.159  24.495  1.00  8.27           C
ATOM    305  CZ  TYR A  39      37.518   7.162  25.002  1.00  8.97           C
ATOM    306  OH  TYR A  39      36.141   7.266  24.897  1.00 12.74           O
ATOM    307  N   TYR A  40      44.637   5.440  23.795  1.00  6.90           N
ATOM    308  CA  TYR A  40      45.964   5.627  23.243  1.00  8.95           C
ATOM    309  C   TYR A  40      45.871   5.877  21.736  1.00  7.77           C
ATOM    310  O   TYR A  40      46.554   6.755  21.189  1.00  7.62           O
ATOM    311  CB  TYR A  40      46.847   4.413  23.528  1.00  8.86           C
ATOM    312  CG  TYR A  40      48.168   4.461  22.808  1.00  9.38           C
ATOM    313  CD1 TYR A  40      49.216   5.243  23.282  1.00 10.56           C
ATOM    314  CD2 TYR A  40      48.371   3.726  21.643  1.00 10.07           C
ATOM    315  CE1 TYR A  40      50.433   5.290  22.600  1.00 11.07           C
ATOM    316  CE2 TYR A  40      49.584   3.768  20.963  1.00 10.87           C
ATOM    317  CZ  TYR A  40      50.605   4.550  21.445  1.00 11.40           C
ATOM    318  OH  TYR A  40      51.812   4.587  20.763  1.00 15.19           O
ATOM    319  N   PHE A  41      45.010   5.120  21.057  1.00  7.59           N
ATOM    320  CA  PHE A  41      44.905   5.259  19.602  1.00  7.80           C
ATOM    321  C   PHE A  41      44.122   6.487  19.160  1.00  9.34           C
ATOM    322  O   PHE A  41      44.129   6.845  17.979  1.00  9.08           O
ATOM    323  CB  PHE A  41      44.391   3.954  18.975  1.00  8.26           C
ATOM    324  CG  PHE A  41      45.380   2.854  19.101  1.00  6.88           C
ATOM    325  CD1 PHE A  41      46.468   2.793  18.237  1.00  7.31           C
ATOM    326  CD2 PHE A  41      45.299   1.945  20.151  1.00  9.51           C
ATOM    327  CE1 PHE A  41      47.441   1.815  18.390  1.00  8.62           C
ATOM    328  CE2 PHE A  41      46.274   0.964  20.310  1.00 10.07           C
ATOM    329  CZ  PHE A  41      47.339   0.896  19.428  1.00  9.41           C
ATOM    330  N   ASP A  42      43.491   7.139  20.131  1.00  7.66           N
ATOM    331  CA  ASP A  42      42.781   8.401  19.952  1.00  7.40           C
ATOM    332  C   ASP A  42      43.698   9.614  20.154  1.00  7.75           C
ATOM    333  O   ASP A  42      43.285  10.739  19.911  1.00  8.71           O
ATOM    334  CB  ASP A  42      41.574   8.424  20.913  1.00  9.06           C
ATOM    335  CG  ASP A  42      40.741   9.691  20.806  1.00  9.88           C
ATOM    336  OD1 ASP A  42      40.653  10.426  21.818  1.00  8.86           O
ATOM    337  OD2 ASP A  42      40.166   9.958  19.728  1.00 11.79           O
ATOM    338  N   ARG A  43      44.940   9.388  20.583  1.00  7.07           N
ATOM    339  CA  ARG A  43      45.892  10.495  20.714  1.00  7.51           C
ATOM    340  C   ARG A  43      46.180  11.117  19.355  1.00  8.66           C
ATOM    341  O   ARG A  43      46.258  10.417  18.343  1.00  9.15           O
ATOM    342  CB  ARG A  43      47.213   9.994  21.309  1.00  7.87           C
ATOM    343  CG  ARG A  43      47.128   9.578  22.774  1.00  7.87           C
ATOM    344  CD  ARG A  43      48.377   8.830  23.214  1.00  9.38           C
ATOM    345  NE  ARG A  43      49.620   9.530  22.893  1.00 11.27           N
ATOM    346  CZ  ARG A  43      50.770   9.345  23.541  1.00 17.06           C
ATOM    347  NH1 ARG A  43      50.826   8.510  24.571  1.00 16.73           N
ATOM    348  NH2 ARG A  43      51.859  10.012  23.176  1.00 16.41           N
ATOM    349  N   ASP A  44      46.392  12.428  19.329  1.00  8.49           N
ATOM    350  CA  ASP A  44      46.659  13.105  18.060  1.00  7.61           C
ATOM    351  C   ASP A  44      47.966  12.641  17.406  1.00  8.27           C
ATOM    352  O   ASP A  44      48.135  12.794  16.193  1.00  9.50           O
ATOM    353  CB  ASP A  44      46.678  14.631  18.240  1.00  9.22           C
ATOM    354  CG  ASP A  44      47.966  15.127  18.874  1.00  9.62           C
ATOM    355  OD1 ASP A  44      48.036  15.222  20.123  1.00  9.16           O
ATOM    356  OD2 ASP A  44      48.916  15.409  18.124  1.00 10.75           O
ATOM    357  N   ASP A  45      48.871  12.068  18.202  1.00  8.48           N
ATOM    358  CA  ASP A  45      50.161  11.597  17.704  1.00  8.11           C
ATOM    359  C   ASP A  45      50.196  10.095  17.442  1.00  8.82           C
ATOM    360  O   ASP A  45      51.259   9.517  17.199  1.00 10.69           O
ATOM    361  CB  ASP A  45      51.306  12.009  18.642  1.00  8.52           C
ATOM    362  CG  ASP A  45      51.147  11.476  20.051  1.00 14.63           C
ATOM    363  OD1 ASP A  45      52.034  11.777  20.884  1.00 19.40           O
ATOM    364  OD2 ASP A  45      50.157  10.776  20.345  1.00 11.95           O
ATOM    365  N   VAL A  46      49.017   9.480  17.476  1.00  8.60           N
ATOM    366  CA  VAL A  46      48.858   8.064  17.152  1.00  8.57           C
ATOM    367  C   VAL A  46      47.800   7.957  16.061  1.00  8.57           C
ATOM    368  O   VAL A  46      48.093   7.515  14.944  1.00 11.21           O
ATOM    369  CB  VAL A  46      48.466   7.239  18.387  1.00  7.82           C
ATOM    370  CG1 VAL A  46      48.287   5.769  18.012  1.00 10.67           C
ATOM    371  CG2 VAL A  46      49.530   7.401  19.486  1.00  9.92           C
ATOM    372  N   ALA A  47      46.585   8.385  16.393  1.00  8.76           N
ATOM    373  CA  ALA A  47      45.544   8.705  15.414  1.00  9.08           C
ATOM    374  C   ALA A  47      45.140   7.539  14.525  1.00 10.06           C
ATOM    375  O   ALA A  47      45.066   7.673  13.303  1.00 11.77           O
ATOM    376  CB  ALA A  47      45.955   9.908  14.572  1.00  9.70           C
ATOM    377  N   LEU A  48      44.843   6.409  15.155  1.00  8.69           N
ATOM    378  CA  LEU A  48      44.309   5.249  14.435  1.00  7.93           C
ATOM    379  C   LEU A  48      42.904   4.958  14.969  1.00  7.45           C
ATOM    380  O   LEU A  48      42.732   4.228  15.953  1.00  8.16           O
ATOM    381  CB  LEU A  48      45.233   4.042  14.604  1.00  7.50           C
ATOM    382  CG  LEU A  48      46.598   4.185  13.923  1.00  9.34           C
ATOM    383  CD1 LEU A  48      47.593   3.182  14.457  1.00 10.27           C
ATOM    384  CD2 LEU A  48      46.455   4.065  12.399  1.00 10.28           C
ATOM    385  N   LYS A  49      41.892   5.538  14.321  1.00  8.52           N
ATOM    386  CA ALYS A  49      40.550   5.567  14.897  0.53 10.16           C
ATOM    387  CA BLYS A  49      40.535   5.570  14.869  0.47 10.17           C
ATOM    388  C   LYS A  49      39.884   4.198  14.983  1.00  9.82           C
ATOM    389  O   LYS A  49      39.037   3.974  15.853  1.00  9.33           O
ATOM    390  CB ALYS A  49      39.647   6.557  14.154  0.53 13.61           C
ATOM    391  CB BLYS A  49      39.628   6.508  14.057  0.47 13.61           C
ATOM    392  CG ALYS A  49      39.251   6.118  12.762  0.53 11.97           C
ATOM    393  CG BLYS A  49      39.906   7.992  14.266  0.47 22.02           C
ATOM    394  CD ALYS A  49      38.648   7.280  11.977  0.53 18.74           C
ATOM    395  CD BLYS A  49      38.891   8.861  13.524  0.47 24.02           C
ATOM    396  CE ALYS A  49      37.630   8.040  12.809  0.53 22.82           C
ATOM    397  CE BLYS A  49      39.087  10.346  13.825  0.47 10.93           C
ATOM    398  NZ ALYS A  49      36.494   7.179  13.233  0.53 31.78           N
ATOM    399  NZ BLYS A  49      38.064  11.168  13.134  0.47 34.77           N
ATOM    400  N   ASN A  50      40.260   3.286  14.094  1.00  7.84           N
ATOM    401  CA  ASN A  50      39.629   1.966  14.133  1.00  6.75           C
ATOM    402  C   ASN A  50      40.267   1.045  15.165  1.00  6.97           C
ATOM    403  O   ASN A  50      39.584   0.206  15.751  1.00  9.03           O
ATOM    404  CB  ASN A  50      39.540   1.336  12.742  1.00  8.25           C
ATOM    405  CG  ASN A  50      38.615   2.108  11.830  1.00 12.91           C
ATOM    406  OD1 ASN A  50      37.458   2.368  12.166  1.00 12.31           O
ATOM    407  ND2 ASN A  50      39.126   2.498  10.679  1.00 17.14           N
ATOM    408  N   PHE A  51      41.560   1.218  15.421  1.00  7.96           N
ATOM    409  CA  PHE A  51      42.160   0.596  16.597  1.00  6.21           C
ATOM    410  C   PHE A  51      41.437   1.101  17.842  1.00  8.36           C
ATOM    411  O   PHE A  51      41.088   0.324  18.720  1.00  7.85           O
ATOM    412  CB  PHE A  51      43.649   0.947  16.710  1.00  8.10           C
ATOM    413  CG  PHE A  51      44.575   0.040  15.925  1.00  6.96           C
ATOM    414  CD1 PHE A  51      44.877   0.305  14.591  1.00  9.75           C
ATOM    415  CD2 PHE A  51      45.178  -1.056  16.534  1.00  8.44           C
ATOM    416  CE1 PHE A  51      45.759  -0.522  13.883  1.00  7.87           C
ATOM    417  CE2 PHE A  51      46.057  -1.875  15.836  1.00  9.58           C
ATOM    418  CZ  PHE A  51      46.349  -1.612  14.515  1.00  8.29           C
ATOM    419  N   ALA A  52      41.212   2.408  17.923  1.00  7.15           N
ATOM    420  CA  ALA A  52      40.519   2.946  19.091  1.00  5.90           C
ATOM    421  C   ALA A  52      39.122   2.344  19.231  1.00  8.07           C
ATOM    422  O   ALA A  52      38.737   1.916  20.317  1.00  7.67           O
ATOM    423  CB  ALA A  52      40.460   4.474  19.027  1.00  7.83           C
ATOM    424  N   LYS A  53      38.373   2.285  18.129  1.00  8.00           N
ATOM    425  CA ALYS A  53      37.030   1.718  18.173  0.58  7.90           C
ATOM    426  CA BLYS A  53      37.032   1.701  18.129  0.42  7.96           C
ATOM    427  C   LYS A  53      37.058   0.236  18.562  1.00  7.84           C
ATOM    428  O   LYS A  53      36.264  -0.195  19.400  1.00  9.19           O
ATOM    429  CB ALYS A  53      36.305   1.935  16.840  0.58 10.11           C
ATOM    430  CB BLYS A  53      36.405   1.823  16.733  0.42 10.02           C
ATOM    431  CG ALYS A  53      35.952   3.396  16.575  0.58  9.77           C
ATOM    432  CG BLYS A  53      35.117   1.030  16.541  0.42 12.01           C
ATOM    433  CD ALYS A  53      35.414   3.587  15.160  0.58 15.47           C
ATOM    434  CD BLYS A  53      34.414   1.424  15.244  0.42 17.66           C
ATOM    435  CE ALYS A  53      35.036   5.043  14.900  0.58 19.61           C
ATOM    436  CE BLYS A  53      35.335   1.321  14.040  0.42 20.36           C
ATOM    437  NZ ALYS A  53      34.463   5.243  13.541  0.58 32.24           N
ATOM    438  NZ BLYS A  53      35.657  -0.082  13.674  0.42 20.02           N
ATOM    439  N   TYR A  54      37.979  -0.523  17.981  1.00  8.05           N
ATOM    440  CA  TYR A  54      38.090  -1.955  18.269  1.00  7.23           C
ATOM    441  C   TYR A  54      38.328  -2.195  19.754  1.00  7.73           C
ATOM    442  O   TYR A  54      37.644  -3.003  20.379  1.00  9.44           O
ATOM    443  CB  TYR A  54      39.222  -2.562  17.445  1.00  8.98           C
ATOM    444  CG  TYR A  54      39.525  -4.023  17.723  1.00  7.71           C
ATOM    445  CD1 TYR A  54      38.729  -5.026  17.197  1.00  9.68           C
ATOM    446  CD2 TYR A  54      40.622  -4.387  18.487  1.00  9.90           C
ATOM    447  CE1 TYR A  54      39.008  -6.360  17.433  1.00  9.99           C
ATOM    448  CE2 TYR A  54      40.915  -5.726  18.734  1.00 13.13           C
ATOM    449  CZ  TYR A  54      40.102  -6.704  18.198  1.00 10.47           C
ATOM    450  OH  TYR A  54      40.379  -8.035  18.437  1.00 13.99           O
ATOM    451  N   PHE A  55      39.293  -1.490  20.328  1.00  6.58           N
ATOM    452  CA  PHE A  55      39.588  -1.719  21.735  1.00  6.95           C
ATOM    453  C   PHE A  55      38.482  -1.206  22.654  1.00  8.23           C
ATOM    454  O   PHE A  55      38.242  -1.786  23.713  1.00  7.18           O
ATOM    455  CB  PHE A  55      40.959  -1.149  22.114  1.00  6.74           C
ATOM    456  CG  PHE A  55      42.109  -1.887  21.493  1.00  7.31           C
ATOM    457  CD1 PHE A  55      43.104  -1.199  20.813  1.00  7.53           C
ATOM    458  CD2 PHE A  55      42.196  -3.274  21.595  1.00  9.03           C
ATOM    459  CE1 PHE A  55      44.181  -1.881  20.247  1.00 10.39           C
ATOM    460  CE2 PHE A  55      43.259  -3.961  21.035  1.00 10.06           C
ATOM    461  CZ  PHE A  55      44.253  -3.265  20.354  1.00 10.60           C
ATOM    462  N   LEU A  56      37.801  -0.126  22.274  1.00  8.00           N
ATOM    463  CA  LEU A  56      36.697   0.348  23.108  1.00  6.91           C
ATOM    464  C   LEU A  56      35.584  -0.701  23.146  1.00  8.11           C
ATOM    465  O   LEU A  56      34.988  -0.947  24.202  1.00  8.52           O
ATOM    466  CB  LEU A  56      36.169   1.708  22.640  1.00  8.74           C
ATOM    467  CG  LEU A  56      35.261   2.401  23.660  1.00 11.88           C
ATOM    468  CD1 LEU A  56      35.989   2.660  24.979  1.00 12.77           C
ATOM    469  CD2 LEU A  56      34.744   3.713  23.078  1.00 14.35           C
ATOM    470  N   HIS A  57      35.315  -1.331  22.007  1.00  8.92           N
ATOM    471  CA  HIS A  57      34.315  -2.397  21.982  1.00  8.39           C
ATOM    472  C   HIS A  57      34.728  -3.562  22.879  1.00 11.01           C
ATOM    473  O   HIS A  57      33.907  -4.111  23.620  1.00 11.57           O
ATOM    474  CB  HIS A  57      34.061  -2.883  20.548  1.00 11.65           C
ATOM    475  CG  HIS A  57      33.050  -3.986  20.462  1.00 21.10           C
ATOM    476  ND1 HIS A  57      31.694  -3.759  20.562  1.00 31.10           N
ATOM    477  CD2 HIS A  57      33.197  -5.325  20.317  1.00 27.27           C
ATOM    478  CE1 HIS A  57      31.048  -4.909  20.467  1.00 29.32           C
ATOM    479  NE2 HIS A  57      31.937  -5.874  20.317  1.00 26.65           N
ATOM    480  N   GLN A  58      35.997  -3.943  22.808  1.00  8.62           N
ATOM    481  CA  GLN A  58      36.515  -5.012  23.653  1.00  8.80           C
ATOM    482  C   GLN A  58      36.358  -4.648  25.123  1.00 10.01           C
ATOM    483  O   GLN A  58      36.029  -5.504  25.947  1.00 10.15           O
ATOM    484  CB  GLN A  58      37.990  -5.275  23.336  1.00  9.88           C
ATOM    485  CG  GLN A  58      38.226  -5.762  21.910  1.00 10.57           C
ATOM    486  CD  GLN A  58      37.502  -7.050  21.632  1.00 25.89           C
ATOM    487  OE1 GLN A  58      37.544  -7.964  22.442  1.00 23.01           O
ATOM    488  NE2 GLN A  58      36.829  -7.132  20.491  1.00 27.19           N
ATOM    489  N   SER A  59      36.586  -3.381  25.454  1.00  8.23           N
ATOM    490  CA  SER A  59      36.437  -2.924  26.830  1.00  8.38           C
ATOM    491  C   SER A  59      35.002  -3.129  27.304  1.00  8.25           C
ATOM    492  O   SER A  59      34.754  -3.641  28.403  1.00  9.14           O
ATOM    493  CB  SER A  59      36.818  -1.445  26.945  1.00  7.37           C
ATOM    494  OG  SER A  59      36.584  -0.957  28.263  1.00  8.48           O
ATOM    495  N   HIS A  60      34.044  -2.735  26.474  1.00  9.33           N
ATOM    496  CA  HIS A  60      32.647  -2.885  26.852  1.00 10.31           C
ATOM    497  C   HIS A  60      32.248  -4.355  26.990  1.00 10.43           C
ATOM    498  O   HIS A  60      31.487  -4.702  27.898  1.00 10.83           O
ATOM    499  CB  HIS A  60      31.740  -2.105  25.890  1.00 11.32           C
ATOM    500  CG  HIS A  60      31.975  -0.625  25.941  1.00 15.24           C
ATOM    501  ND1 HIS A  60      31.824   0.200  24.848  1.00 21.27           N
ATOM    502  CD2 HIS A  60      32.397   0.169  26.954  1.00 20.02           C
ATOM    503  CE1 HIS A  60      32.110   1.444  25.194  1.00 21.86           C
ATOM    504  NE2 HIS A  60      32.466   1.451  26.466  1.00 18.91           N
ATOM    505  N   GLU A  61      32.789  -5.219  26.132  1.00  8.86           N
ATOM    506  CA  GLU A  61      32.524  -6.654  26.253  1.00  9.65           C
ATOM    507  C   GLU A  61      33.007  -7.202  27.599  1.00 11.88           C
ATOM    508  O   GLU A  61      32.331  -8.033  28.213  1.00  9.47           O
ATOM    509  CB  GLU A  61      33.182  -7.435  25.113  1.00 10.87           C
ATOM    510  CG  GLU A  61      32.501  -7.264  23.766  1.00 16.16           C
ATOM    511  CD  GLU A  61      33.176  -8.078  22.684  1.00 28.16           C
ATOM    512  OE1 GLU A  61      34.337  -8.476  22.895  1.00 25.62           O
ATOM    513  OE2 GLU A  61      32.559  -8.318  21.622  1.00 28.61           O
ATOM    514  N   GLU A  62      34.177  -6.757  28.054  1.00  9.56           N
ATOM    515  CA  GLU A  62      34.694  -7.215  29.346  1.00  8.32           C
ATOM    516  C   GLU A  62      33.809  -6.773  30.508  1.00  9.84           C
ATOM    517  O   GLU A  62      33.626  -7.534  31.464  1.00  8.33           O
ATOM    518  CB  GLU A  62      36.129  -6.740  29.574  1.00  7.95           C
ATOM    519  CG  GLU A  62      37.126  -7.196  28.525  1.00 10.73           C
ATOM    520  CD  GLU A  62      37.320  -8.689  28.513  1.00 17.14           C
ATOM    521  OE1 GLU A  62      37.944  -9.209  27.567  1.00 19.50           O
ATOM    522  OE2 GLU A  62      36.857  -9.355  29.456  1.00 14.71           O
ATOM    523  N   ARG A  63      33.256  -5.563  30.443  1.00  9.09           N
ATOM    524  CA  ARG A  63      32.305  -5.139  31.472  1.00  7.55           C
ATOM    525  C   ARG A  63      31.092  -6.067  31.490  1.00  8.92           C
ATOM    526  O   ARG A  63      30.620  -6.448  32.562  1.00 10.12           O
ATOM    527  CB  ARG A  63      31.887  -3.674  31.296  1.00 11.42           C
ATOM    528  CG  ARG A  63      30.679  -3.243  32.151  1.00 15.83           C
ATOM    529  CD  ARG A  63      30.899  -3.413  33.660  1.00 24.77           C
ATOM    530  NE  ARG A  63      31.385  -2.194  34.308  1.00 29.71           N
ATOM    531  CZ  ARG A  63      30.608  -1.253  34.854  1.00 26.64           C
ATOM    532  NH1 ARG A  63      29.281  -1.367  34.843  1.00 17.55           N
ATOM    533  NH2 ARG A  63      31.168  -0.190  35.419  1.00 27.02           N
ATOM    534  N   GLU A  64      30.604  -6.459  30.314  1.00  9.06           N
ATOM    535  CA  GLU A  64      29.518  -7.432  30.256  1.00  9.06           C
ATOM    536  C   GLU A  64      29.914  -8.769  30.875  1.00  8.95           C
ATOM    537  O   GLU A  64      29.114  -9.393  31.580  1.00  9.72           O
ATOM    538  CB  GLU A  64      29.049  -7.644  28.814  1.00 11.20           C
ATOM    539  CG  GLU A  64      28.459  -6.400  28.186  1.00 16.95           C
ATOM    540  CD  GLU A  64      28.084  -6.594  26.725  1.00 38.26           C
ATOM    541  OE1 GLU A  64      28.596  -7.544  26.091  1.00 41.86           O
ATOM    542  OE2 GLU A  64      27.276  -5.789  26.211  1.00 47.66           O
ATOM    543  N   HIS A  65      31.142  -9.204  30.621  1.00  7.70           N
ATOM    544  CA  HIS A  65      31.635 -10.446  31.233  1.00  7.49           C
ATOM    545  C   HIS A  65      31.614 -10.351  32.751  1.00  8.06           C
ATOM    546  O   HIS A  65      31.242 -11.310  33.432  1.00  9.01           O
ATOM    547  CB  HIS A  65      33.073 -10.743  30.825  1.00  7.55           C
ATOM    548  CG  HIS A  65      33.250 -11.030  29.371  1.00 13.55           C
ATOM    549  ND1 HIS A  65      34.492 -11.167  28.789  1.00 15.43           N
ATOM    550  CD2 HIS A  65      32.349 -11.181  28.371  1.00 17.18           C
ATOM    551  CE1 HIS A  65      34.350 -11.394  27.496  1.00 21.96           C
ATOM    552  NE2 HIS A  65      33.059 -11.410  27.217  1.00 23.30           N
ATOM    553  N   ALA A  66      32.046  -9.211  33.286  1.00  6.91           N
ATOM    554  CA  ALA A  66      32.050  -9.006  34.736  1.00  8.05           C
ATOM    555  C   ALA A  66      30.630  -9.030  35.301  1.00  8.95           C
ATOM    556  O   ALA A  66      30.356  -9.673  36.321  1.00  8.51           O
ATOM    557  CB  ALA A  66      32.743  -7.686  35.086  1.00  7.62           C
ATOM    558  N   GLU A  67      29.725  -8.320  34.638  1.00  7.77           N
ATOM    559  CA  GLU A  67      28.337  -8.259  35.089  1.00  8.48           C
ATOM    560  C   GLU A  67      27.678  -9.632  35.134  1.00  6.81           C
ATOM    561  O   GLU A  67      26.934  -9.934  36.069  1.00  7.09           O
ATOM    562  CB  GLU A  67      27.534  -7.297  34.211  1.00  9.65           C
ATOM    563  CG  GLU A  67      27.925  -5.851  34.473  1.00 10.61           C
ATOM    564  CD  GLU A  67      27.293  -4.849  33.533  1.00 14.92           C
ATOM    565  OE1 GLU A  67      27.613  -3.657  33.682  1.00 15.58           O
ATOM    566  OE2 GLU A  67      26.487  -5.232  32.664  1.00 19.11           O
ATOM    567  N   LYS A  68      27.965 -10.467  34.138  1.00  6.78           N
ATOM    568  CA  LYS A  68      27.387 -11.810  34.110  1.00  7.10           C
ATOM    569  C   LYS A  68      27.890 -12.670  35.269  1.00  7.79           C
ATOM    570  O   LYS A  68      27.155 -13.507  35.806  1.00  6.90           O
ATOM    571  CB  LYS A  68      27.664 -12.492  32.772  1.00  7.21           C
ATOM    572  CG  LYS A  68      26.993 -13.852  32.657  1.00 10.90           C
ATOM    573  CD  LYS A  68      27.233 -14.477  31.291  1.00 13.20           C
ATOM    574  CE  LYS A  68      26.346 -13.815  30.246  1.00 20.48           C
ATOM    575  NZ  LYS A  68      26.663 -14.270  28.863  1.00 33.16           N
ATOM    576  N   LEU A  69      29.148 -12.471  35.652  1.00  6.94           N
ATOM    577  CA  LEU A  69      29.696 -13.183  36.809  1.00  7.37           C
ATOM    578  C   LEU A  69      29.099 -12.693  38.124  1.00  6.75           C
ATOM    579  O   LEU A  69      28.886 -13.480  39.050  1.00  7.65           O
ATOM    580  CB  LEU A  69      31.218 -13.050  36.841  1.00  6.72           C
ATOM    581  CG  LEU A  69      31.953 -13.978  35.876  1.00  7.44           C
ATOM    582  CD1 LEU A  69      33.290 -13.373  35.494  1.00  8.43           C
ATOM    583  CD2 LEU A  69      32.129 -15.373  36.476  1.00 11.06           C
ATOM    584  N   MET A  70      28.828 -11.394  38.205  1.00  6.64           N
ATOM    585  CA  MET A  70      28.138 -10.850  39.364  1.00  6.33           C
ATOM    586  C   MET A  70      26.721 -11.414  39.470  1.00  6.32           C
ATOM    587  O   MET A  70      26.269 -11.787  40.559  1.00  7.56           O
ATOM    588  CB  MET A  70      28.137  -9.322  39.315  1.00  7.20           C
ATOM    589  CG  MET A  70      29.550  -8.764  39.454  1.00  8.00           C
ATOM    590  SD  MET A  70      29.676  -6.988  39.209  1.00  9.47           S
ATOM    591  CE  MET A  70      29.008  -6.387  40.768  1.00 10.82           C
ATOM    592  N   LYS A  71      26.042 -11.519  38.331  1.00  6.67           N
ATOM    593  CA  LYS A  71      24.732 -12.153  38.281  1.00  6.56           C
ATOM    594  C   LYS A  71      24.812 -13.607  38.752  1.00  6.97           C
ATOM    595  O   LYS A  71      23.967 -14.055  39.533  1.00  7.30           O
ATOM    596  CB  LYS A  71      24.170 -12.063  36.855  1.00  7.24           C
ATOM    597  CG  LYS A  71      22.807 -12.727  36.678  1.00  7.47           C
ATOM    598  CD  LYS A  71      22.314 -12.607  35.248  1.00 16.79           C
ATOM    599  CE  LYS A  71      20.986 -13.339  35.079  1.00 19.25           C
ATOM    600  NZ  LYS A  71      20.502 -13.323  33.669  1.00 30.21           N
ATOM    601  N   LEU A  72      25.830 -14.331  38.284  1.00  7.41           N
ATOM    602  CA  LEU A  72      26.012 -15.741  38.646  1.00  7.72           C
ATOM    603  C   LEU A  72      26.208 -15.889  40.154  1.00  7.03           C
ATOM    604  O   LEU A  72      25.601 -16.760  40.798  1.00  7.73           O
ATOM    605  CB  LEU A  72      27.207 -16.321  37.886  1.00  7.94           C
ATOM    606  CG  LEU A  72      27.632 -17.786  38.095  1.00  8.17           C
ATOM    607  CD1 LEU A  72      28.339 -18.011  39.435  1.00  9.26           C
ATOM    608  CD2 LEU A  72      26.458 -18.743  37.958  1.00  7.91           C
ATOM    609  N   GLN A  73      27.059 -15.038  40.723  1.00  5.92           N
ATOM    610  CA  GLN A  73      27.316 -15.066  42.162  1.00  6.16           C
ATOM    611  C   GLN A  73      26.001 -14.998  42.933  1.00  7.24           C
ATOM    612  O   GLN A  73      25.725 -15.824  43.807  1.00  8.40           O
ATOM    613  CB  GLN A  73      28.239 -13.896  42.554  1.00  6.83           C
ATOM    614  CG  GLN A  73      28.723 -13.926  44.009  1.00  7.20           C
ATOM    615  CD  GLN A  73      29.752 -15.014  44.263  1.00  8.25           C
ATOM    616  OE1 GLN A  73      29.404 -16.188  44.385  1.00  8.92           O
ATOM    617  NE2 GLN A  73      31.019 -14.629  44.351  1.00  7.34           N
ATOM    618  N   ASN A  74      25.166 -14.026  42.589  1.00  7.02           N
ATOM    619  CA  ASN A  74      23.860 -13.907  43.237  1.00  6.41           C
ATOM    620  C   ASN A  74      22.925 -15.077  42.925  1.00  6.53           C
ATOM    621  O   ASN A  74      22.175 -15.524  43.790  1.00  7.39           O
ATOM    622  CB  ASN A  74      23.199 -12.582  42.856  1.00  6.63           C
ATOM    623  CG  ASN A  74      23.788 -11.399  43.603  1.00  9.34           C
ATOM    624  OD1 ASN A  74      24.396 -11.555  44.663  1.00  9.92           O
ATOM    625  ND2 ASN A  74      23.603 -10.206  43.057  1.00  8.43           N
ATOM    626  N   GLN A  75      22.953 -15.572  41.691  1.00  6.91           N
ATOM    627  CA  GLN A  75      22.091 -16.697  41.328  1.00  6.33           C
ATOM    628  C   GLN A  75      22.363 -17.890  42.225  1.00  7.14           C
ATOM    629  O   GLN A  75      21.450 -18.596  42.607  1.00  8.01           O
ATOM    630  CB  GLN A  75      22.330 -17.114  39.882  1.00  7.00           C
ATOM    631  CG  GLN A  75      21.663 -16.212  38.854  1.00  8.77           C
ATOM    632  CD  GLN A  75      21.998 -16.602  37.447  1.00  9.53           C
ATOM    633  OE1 GLN A  75      23.168 -16.753  37.089  1.00  9.75           O
ATOM    634  NE2 GLN A  75      20.966 -16.760  36.619  1.00 10.89           N
ATOM    635  N   ARG A  76      23.636 -18.110  42.542  1.00  7.35           N
ATOM    636  CA  ARG A  76      24.022 -19.291  43.318  1.00  8.05           C
ATOM    637  C   ARG A  76      23.994 -19.046  44.832  1.00  7.21           C
ATOM    638  O   ARG A  76      24.211 -19.975  45.623  1.00  8.59           O
ATOM    639  CB  ARG A  76      25.408 -19.782  42.874  1.00  7.49           C
ATOM    640  CG  ARG A  76      25.453 -20.310  41.430  1.00  8.57           C
ATOM    641  CD  ARG A  76      24.596 -21.570  41.232  1.00  7.67           C
ATOM    642  NE  ARG A  76      25.021 -22.660  42.108  1.00  7.93           N
ATOM    643  CZ  ARG A  76      25.960 -23.550  41.801  1.00  7.73           C
ATOM    644  NH1 ARG A  76      26.592 -23.505  40.628  1.00  7.39           N
ATOM    645  NH2 ARG A  76      26.276 -24.490  42.691  1.00  8.97           N
ATOM    646  N   GLY A  77      23.719 -17.813  45.247  1.00  8.36           N
ATOM    647  CA  GLY A  77      23.622 -17.509  46.665  1.00  7.72           C
ATOM    648  C   GLY A  77      24.944 -17.132  47.311  1.00  8.72           C
ATOM    649  O   GLY A  77      25.045 -17.056  48.540  1.00 10.80           O
ATOM    650  N   GLY A  78      25.962 -16.890  46.491  1.00  8.12           N
ATOM    651  CA  GLY A  78      27.215 -16.353  46.989  1.00  8.50           C
ATOM    652  C   GLY A  78      27.096 -14.854  47.192  1.00 10.24           C
ATOM    653  O   GLY A  78      26.086 -14.239  46.845  1.00 11.01           O
ATOM    654  N   ARG A  79      28.127 -14.254  47.769  1.00  8.52           N
ATOM    655  CA  ARG A  79      28.091 -12.825  48.014  1.00  9.69           C
ATOM    656  C   ARG A  79      29.254 -12.154  47.324  1.00 10.05           C
ATOM    657  O   ARG A  79      30.409 -12.582  47.448  1.00 10.20           O
ATOM    658  CB  ARG A  79      28.048 -12.527  49.514  1.00 11.45           C
ATOM    659  CG  ARG A  79      26.729 -12.967  50.146  1.00 11.74           C
ATOM    660  CD  ARG A  79      25.551 -12.087  49.704  1.00 12.88           C
ATOM    661  NE  ARG A  79      24.253 -12.675  50.061  1.00 16.79           N
ATOM    662  CZ  ARG A  79      23.389 -13.179  49.181  1.00 14.29           C
ATOM    663  NH1 ARG A  79      23.656 -13.162  47.871  1.00 12.82           N
ATOM    664  NH2 ARG A  79      22.238 -13.681  49.609  1.00 14.37           N
ATOM    665  N   ILE A  80      28.929 -11.130  46.542  1.00  7.61           N
ATOM    666  CA  ILE A  80      29.929 -10.395  45.786  1.00  7.75           C
ATOM    667  C   ILE A  80      30.837  -9.600  46.718  1.00  8.05           C
ATOM    668  O   ILE A  80      30.364  -8.871  47.601  1.00 11.96           O
ATOM    669  CB  ILE A  80      29.255  -9.424  44.801  1.00  9.07           C
ATOM    670  CG1 ILE A  80      28.467 -10.207  43.742  1.00  7.64           C
ATOM    671  CG2 ILE A  80      30.303  -8.507  44.159  1.00  9.10           C
ATOM    672  CD1 ILE A  80      27.389  -9.379  43.046  1.00  9.08           C
ATOM    673  N   PHE A  81      32.140  -9.780  46.517  1.00  9.18           N
ATOM    674  CA APHE A  81      33.158  -9.018  47.233  0.57  9.30           C
ATOM    675  CA BPHE A  81      33.160  -9.021  47.233  0.43  9.36           C
ATOM    676  C   PHE A  81      34.071  -8.382  46.197  1.00  8.74           C
ATOM    677  O   PHE A  81      34.744  -9.080  45.443  1.00 11.34           O
ATOM    678  CB APHE A  81      33.956  -9.942  48.160  0.57 13.55           C
ATOM    679  CB BPHE A  81      33.988  -9.932  48.148  0.43 13.56           C
ATOM    680  CG APHE A  81      35.064  -9.254  48.915  0.57 15.87           C
ATOM    681  CG BPHE A  81      33.246 -10.434  49.361  0.43 19.79           C
ATOM    682  CD1APHE A  81      36.381  -9.383  48.504  0.57 20.14           C
ATOM    683  CD1BPHE A  81      33.859 -11.308  50.245  0.43 23.17           C
ATOM    684  CD2APHE A  81      34.791  -8.496  50.043  0.57 21.15           C
ATOM    685  CD2BPHE A  81      31.946 -10.038  49.622  0.43 23.08           C
ATOM    686  CE1APHE A  81      37.404  -8.759  49.200  0.57 21.72           C
ATOM    687  CE1BPHE A  81      33.187 -11.773  51.362  0.43 20.07           C
ATOM    688  CE2APHE A  81      35.814  -7.869  50.744  0.57 18.34           C
ATOM    689  CE2BPHE A  81      31.272 -10.505  50.736  0.43 18.56           C
ATOM    690  CZ APHE A  81      37.115  -8.000  50.319  0.57 20.29           C
ATOM    691  CZ BPHE A  81      31.894 -11.370  51.603  0.43 20.46           C
ATOM    692  N   LEU A  82      34.074  -7.058  46.160  1.00 10.24           N
ATOM    693  CA  LEU A  82      34.825  -6.321  45.152  1.00  9.42           C
ATOM    694  C   LEU A  82      36.156  -5.854  45.703  1.00 12.53           C
ATOM    695  O   LEU A  82      36.298  -5.621  46.908  1.00 12.20           O
ATOM    696  CB  LEU A  82      34.022  -5.118  44.670  1.00  9.48           C
ATOM    697  CG  LEU A  82      32.674  -5.438  44.020  1.00 10.29           C
ATOM    698  CD1 LEU A  82      31.855  -4.166  43.776  1.00 12.16           C
ATOM    699  CD2 LEU A  82      32.871  -6.202  42.719  1.00  9.11           C
ATOM    700  N  AGLN A  83      37.134  -5.732  44.813  0.46  9.13           N
ATOM    701  N  BGLN A  83      37.135  -5.722  44.817  0.54  9.12           N
ATOM    702  CA AGLN A  83      38.440  -5.187  45.158  0.46  8.78           C
ATOM    703  CA BGLN A  83      38.430  -5.167  45.182  0.54  8.76           C
ATOM    704  C  AGLN A  83      38.782  -4.055  44.202  0.46  6.78           C
ATOM    705  C  BGLN A  83      38.819  -4.094  44.178  0.54  6.78           C
ATOM    706  O  AGLN A  83      38.096  -3.855  43.196  0.46  8.89           O
ATOM    707  O  BGLN A  83      38.205  -3.977  43.111  0.54  8.81           O
ATOM    708  CB AGLN A  83      39.518  -6.272  45.082  0.46 12.90           C
ATOM    709  CB BGLN A  83      39.499  -6.260  45.224  0.54 13.08           C
ATOM    710  CG AGLN A  83      39.363  -7.366  46.126  0.46 13.40           C
ATOM    711  CG BGLN A  83      39.192  -7.382  46.205  0.54 13.27           C
ATOM    712  CD AGLN A  83      40.616  -8.208  46.282  0.46 22.60           C
ATOM    713  CD BGLN A  83      39.084  -6.905  47.648  0.54 16.66           C
ATOM    714  OE1AGLN A  83      41.464  -8.256  45.390  0.46 32.65           O
ATOM    715  OE1BGLN A  83      39.636  -5.872  48.022  0.54 23.82           O
ATOM    716  NE2AGLN A  83      40.738  -8.880  47.422  0.46 33.34           N
ATOM    717  NE2BGLN A  83      38.371  -7.668  48.467  0.54 21.07           N
ATOM    718  N   ASP A  84      39.844  -3.315  44.507  1.00  8.23           N
ATOM    719  CA  ASP A  84      40.314  -2.263  43.609  1.00  7.19           C
ATOM    720  C   ASP A  84      40.538  -2.834  42.209  1.00  5.72           C
ATOM    721  O   ASP A  84      41.001  -3.962  42.056  1.00  8.20           O
ATOM    722  CB  ASP A  84      41.660  -1.698  44.087  1.00  8.85           C
ATOM    723  CG  ASP A  84      41.570  -0.958  45.407  1.00  9.31           C
ATOM    724  OD1 ASP A  84      42.663  -0.652  45.938  1.00 12.00           O
ATOM    725  OD2 ASP A  84      40.459  -0.690  45.921  1.00  8.58           O
ATOM    726  N   ILE A  85      40.244  -2.036  41.188  1.00  7.02           N
ATOM    727  CA  ILE A  85      40.603  -2.408  39.825  1.00  7.65           C
ATOM    728  C   ILE A  85      41.961  -1.780  39.521  1.00  7.38           C
ATOM    729  O   ILE A  85      42.092  -0.555  39.439  1.00  8.42           O
ATOM    730  CB  ILE A  85      39.558  -1.942  38.798  1.00  8.03           C
ATOM    731  CG1 ILE A  85      38.165  -2.412  39.211  1.00  8.13           C
ATOM    732  CG2 ILE A  85      39.909  -2.488  37.408  1.00  9.02           C
ATOM    733  CD1 ILE A  85      37.038  -1.730  38.433  1.00 11.13           C
ATOM    734  N   LYS A  86      42.981  -2.617  39.382  1.00  7.76           N
ATOM    735  CA  LYS A  86      44.334  -2.109  39.158  1.00  7.54           C
ATOM    736  C   LYS A  86      44.450  -1.401  37.818  1.00  7.59           C
ATOM    737  O   LYS A  86      43.846  -1.821  36.826  1.00  8.79           O
ATOM    738  CB  LYS A  86      45.354  -3.246  39.216  1.00  8.44           C
ATOM    739  CG  LYS A  86      45.491  -3.898  40.577  1.00 10.32           C
ATOM    740  CD  LYS A  86      46.062  -2.939  41.601  1.00 15.89           C
ATOM    741  CE  LYS A  86      46.417  -3.685  42.878  1.00 16.23           C
ATOM    742  NZ  LYS A  86      46.864  -2.749  43.940  1.00 23.14           N
ATOM    743  N   LYS A  87      45.236  -0.333  37.774  1.00  7.75           N
ATOM    744  CA  LYS A  87      45.480   0.327  36.498  1.00  7.04           C
ATOM    745  C   LYS A  87      46.245  -0.617  35.575  1.00  7.56           C
ATOM    746  O   LYS A  87      46.938  -1.544  36.028  1.00 10.27           O
ATOM    747  CB  LYS A  87      46.243   1.643  36.702  1.00 11.69           C
ATOM    748  CG  LYS A  87      47.689   1.460  37.106  1.00 12.86           C
ATOM    749  CD  LYS A  87      48.375   2.801  37.338  1.00 14.45           C
ATOM    750  CE  LYS A  87      49.844   2.603  37.674  1.00 25.28           C
ATOM    751  NZ  LYS A  87      50.567   3.896  37.826  1.00 41.36           N
ATOM    752  N   PRO A  88      46.118  -0.411  34.265  1.00  8.75           N
ATOM    753  CA  PRO A  88      46.845  -1.275  33.328  1.00 11.22           C
ATOM    754  C   PRO A  88      48.368  -1.179  33.484  1.00 13.27           C
ATOM    755  O   PRO A  88      48.891  -0.159  33.922  1.00 14.56           O
ATOM    756  CB  PRO A  88      46.407  -0.740  31.957  1.00 12.13           C
ATOM    757  CG  PRO A  88      45.082  -0.092  32.207  1.00 11.81           C
ATOM    758  CD  PRO A  88      45.225   0.536  33.578  1.00 10.74           C
ATOM    759  N   ASP A  89      49.074  -2.242  33.118  1.00 25.68           N
ATOM    760  CA  ASP A  89      50.539  -2.253  33.198  1.00 31.76           C
ATOM    761  C   ASP A  89      51.262  -1.117  32.453  1.00 44.28           C
ATOM    762  O   ASP A  89      52.365  -0.715  32.841  1.00 38.79           O
ATOM    763  CB  ASP A  89      51.077  -3.596  32.707  1.00 28.37           C
ATOM    764  CG  ASP A  89      50.868  -4.701  33.716  1.00 54.10           C
ATOM    765  OD1 ASP A  89      51.046  -5.885  33.354  1.00 61.66           O
ATOM    766  OD2 ASP A  89      50.521  -4.379  34.874  1.00 35.11           O
ATOM    767  N   CYS A  90      50.648  -0.603  31.391  1.00 38.70           N
ATOM    768  CA ACYS A  90      51.299   0.398  30.551  0.56 35.58           C
ATOM    769  CA BCYS A  90      51.295   0.389  30.539  0.44 35.56           C
ATOM    770  C   CYS A  90      50.446   1.650  30.374  1.00 40.07           C
ATOM    771  O   CYS A  90      49.219   1.591  30.438  1.00 34.82           O
ATOM    772  CB ACYS A  90      51.634  -0.198  29.179  0.56 36.77           C
ATOM    773  CB BCYS A  90      51.576  -0.223  29.165  0.44 36.71           C
ATOM    774  SG ACYS A  90      52.670  -1.685  29.236  0.56 44.76           S
ATOM    775  SG BCYS A  90      52.951   0.524  28.272  0.44 43.94           S
ATOM    776  N   ASP A  91      51.108   2.785  30.155  1.00 35.41           N
ATOM    777  CA  ASP A  91      50.423   4.041  29.861  1.00 28.61           C
ATOM    778  C   ASP A  91      50.498   4.303  28.360  1.00 36.89           C
ATOM    779  O   ASP A  91      49.517   4.723  27.738  1.00 32.11           O
ATOM    780  CB  ASP A  91      51.070   5.212  30.613  1.00 27.78           C
ATOM    781  CG  ASP A  91      50.827   5.158  32.113  1.00 42.15           C
ATOM    782  OD1 ASP A  91      49.647   5.150  32.539  1.00 43.56           O
ATOM    783  OD2 ASP A  91      51.822   5.143  32.870  1.00 43.37           O
ATOM    784  N   ASP A  92      51.679   4.046  27.799  1.00 30.65           N
ATOM    785  CA  ASP A  92      51.971   4.223  26.374  1.00 27.81           C
ATOM    786  C   ASP A  92      52.149   2.844  25.725  1.00 31.84           C
ATOM    787  O   ASP A  92      53.087   2.106  26.035  1.00 30.52           O
ATOM    788  CB  ASP A  92      53.245   5.065  26.213  1.00 32.49           C
ATOM    789  CG  ASP A  92      53.610   5.336  24.754  1.00 32.39           C
ATOM    790  OD1 ASP A  92      53.957   6.493  24.437  1.00 45.67           O
ATOM    791  OD2 ASP A  92      53.567   4.401  23.929  1.00 29.75           O
ATOM    792  N   TRP A  93      51.249   2.502  24.814  1.00 31.37           N
ATOM    793  CA  TRP A  93      51.228   1.161  24.251  1.00 22.59           C
ATOM    794  C   TRP A  93      52.102   1.007  23.005  1.00 23.90           C
ATOM    795  O   TRP A  93      52.104  -0.051  22.368  1.00 19.35           O
ATOM    796  CB  TRP A  93      49.784   0.751  23.984  1.00 24.61           C
ATOM    797  CG  TRP A  93      48.954   0.770  25.234  1.00 18.01           C
ATOM    798  CD1 TRP A  93      48.183   1.799  25.696  1.00 22.99           C
ATOM    799  CD2 TRP A  93      48.825  -0.287  26.184  1.00 20.33           C
ATOM    800  NE1 TRP A  93      47.572   1.440  26.876  1.00 19.03           N
ATOM    801  CE2 TRP A  93      47.947   0.164  27.197  1.00 18.37           C
ATOM    802  CE3 TRP A  93      49.358  -1.575  26.276  1.00 21.82           C
ATOM    803  CZ2 TRP A  93      47.601  -0.628  28.290  1.00 28.68           C
ATOM    804  CZ3 TRP A  93      49.015  -2.357  27.365  1.00 33.13           C
ATOM    805  CH2 TRP A  93      48.141  -1.883  28.356  1.00 29.49           C
ATOM    806  N   GLU A  94      52.821   2.075  22.661  1.00 15.16           N
ATOM    807  CA  GLU A  94      53.905   2.034  21.672  1.00 16.31           C
ATOM    808  C   GLU A  94      53.505   1.967  20.182  1.00 17.57           C
ATOM    809  O   GLU A  94      54.029   2.722  19.347  1.00 16.39           O
ATOM    810  CB  GLU A  94      54.861   0.888  22.018  1.00 23.38           C
ATOM    811  CG  GLU A  94      56.254   1.044  21.453  1.00 38.53           C
ATOM    812  CD  GLU A  94      57.268   0.161  22.165  1.00 53.24           C
ATOM    813  OE1 GLU A  94      58.314   0.692  22.602  1.00 58.61           O
ATOM    814  OE2 GLU A  94      57.016  -1.058  22.297  1.00 42.90           O
ATOM    815  N   SER A  95      52.596   1.057  19.843  1.00 12.67           N
ATOM    816  CA  SER A  95      52.227   0.838  18.447  1.00 11.05           C
ATOM    817  C   SER A  95      50.981  -0.028  18.395  1.00 10.34           C
ATOM    818  O   SER A  95      50.614  -0.651  19.386  1.00 10.02           O
ATOM    819  CB  SER A  95      53.355   0.127  17.691  1.00 12.76           C
ATOM    820  OG  SER A  95      53.523  -1.221  18.135  1.00 12.27           O
ATOM    821  N   GLY A  96      50.337  -0.076  17.236  1.00  8.65           N
ATOM    822  CA  GLY A  96      49.217  -0.988  17.043  1.00 10.07           C
ATOM    823  C   GLY A  96      49.599  -2.435  17.321  1.00  9.11           C
ATOM    824  O   GLY A  96      48.862  -3.154  18.004  1.00 11.13           O
ATOM    825  N   LEU A  97      50.745  -2.863  16.790  1.00  8.15           N
ATOM    826  CA  LEU A  97      51.232  -4.226  17.003  1.00  8.64           C
ATOM    827  C   LEU A  97      51.456  -4.523  18.481  1.00 11.74           C
ATOM    828  O   LEU A  97      51.037  -5.571  18.981  1.00 10.42           O
ATOM    829  CB  LEU A  97      52.529  -4.473  16.214  1.00  9.89           C
ATOM    830  CG  LEU A  97      53.205  -5.821  16.483  1.00 11.35           C
ATOM    831  CD1 LEU A  97      52.282  -6.997  16.189  1.00 12.34           C
ATOM    832  CD2 LEU A  97      54.495  -5.946  15.673  1.00 16.52           C
ATOM    833  N   ASN A  98      52.118  -3.611  19.184  1.00  9.81           N
ATOM    834  CA  ASN A  98      52.392  -3.864  20.585  1.00  9.46           C
ATOM    835  C   ASN A  98      51.097  -3.952  21.391  1.00 10.71           C
ATOM    836  O   ASN A  98      50.974  -4.791  22.287  1.00 11.21           O
ATOM    837  CB  ASN A  98      53.334  -2.817  21.169  1.00 11.02           C
ATOM    838  CG  ASN A  98      53.739  -3.151  22.587  1.00 19.33           C
ATOM    839  OD1 ASN A  98      54.413  -4.154  22.832  1.00 20.71           O
ATOM    840  ND2 ASN A  98      53.314  -2.330  23.530  1.00 18.66           N
ATOM    841  N   ALA A  99      50.120  -3.111  21.064  1.00  9.53           N
ATOM    842  CA  ALA A  99      48.841  -3.173  21.767  1.00  9.18           C
ATOM    843  C   ALA A  99      48.151  -4.517  21.524  1.00  8.59           C
ATOM    844  O   ALA A  99      47.622  -5.130  22.455  1.00  9.08           O
ATOM    845  CB  ALA A  99      47.944  -2.018  21.349  1.00  9.15           C
ATOM    846  N   MET A 100      48.150  -4.973  20.274  1.00  8.15           N
ATOM    847  CA  MET A 100      47.590  -6.286  19.954  1.00  8.08           C
ATOM    848  C   MET A 100      48.295  -7.405  20.705  1.00 10.38           C
ATOM    849  O   MET A 100      47.648  -8.331  21.183  1.00  9.17           O
ATOM    850  CB  MET A 100      47.629  -6.555  18.445  1.00  9.47           C
ATOM    851  CG  MET A 100      46.624  -5.741  17.641  1.00 11.37           C
ATOM    852  SD  MET A 100      44.911  -6.157  18.004  1.00  8.91           S
ATOM    853  CE  MET A 100      44.067  -4.964  16.965  1.00 10.15           C
ATOM    854  N   GLU A 101      49.622  -7.316  20.807  1.00  9.36           N
ATOM    855  CA  GLU A 101      50.382  -8.321  21.546  1.00  9.66           C
ATOM    856  C   GLU A 101      50.024  -8.303  23.033  1.00  9.04           C
ATOM    857  O   GLU A 101      49.895  -9.358  23.663  1.00 10.41           O
ATOM    858  CB  GLU A 101      51.892  -8.126  21.341  1.00 11.05           C
ATOM    859  CG  GLU A 101      52.376  -8.513  19.951  1.00 10.02           C
ATOM    860  CD  GLU A 101      53.842  -8.173  19.719  1.00 22.60           C
ATOM    861  OE1 GLU A 101      54.497  -8.880  18.926  1.00 37.40           O
ATOM    862  OE2 GLU A 101      54.336  -7.197  20.321  1.00 32.68           O
ATOM    863  N   CYS A 102      49.838  -7.115  23.592  1.00  8.64           N
ATOM    864  CA ACYS A 102      49.427  -7.015  24.981  0.58 10.15           C
ATOM    865  CA BCYS A 102      49.410  -6.981  24.981  0.42 10.16           C
ATOM    866  C   CYS A 102      48.036  -7.592  25.192  1.00 11.63           C
ATOM    867  O   CYS A 102      47.788  -8.268  26.192  1.00 10.91           O
ATOM    868  CB ACYS A 102      49.495  -5.568  25.460  0.58  9.99           C
ATOM    869  CB BCYS A 102      49.368  -5.511  25.401  0.42  9.89           C
ATOM    870  SG ACYS A 102      51.195  -4.976  25.624  0.58 15.07           S
ATOM    871  SG BCYS A 102      48.594  -5.237  27.022  0.42 20.21           S
ATOM    872  N   ALA A 103      47.133  -7.328  24.251  1.00  9.77           N
ATOM    873  CA  ALA A 103      45.781  -7.865  24.344  1.00  9.78           C
ATOM    874  C   ALA A 103      45.812  -9.389  24.276  1.00 10.51           C
ATOM    875  O   ALA A 103      45.105 -10.062  25.026  1.00  9.23           O
ATOM    876  CB  ALA A 103      44.904  -7.297  23.236  1.00 10.36           C
ATOM    877  N   LEU A 104      46.620  -9.931  23.369  1.00  9.94           N
ATOM    878  CA  LEU A 104      46.772 -11.384  23.269  1.00  9.81           C
ATOM    879  C   LEU A 104      47.237 -11.986  24.597  1.00  9.72           C
ATOM    880  O   LEU A 104      46.698 -12.993  25.067  1.00  9.69           O
ATOM    881  CB  LEU A 104      47.752 -11.741  22.148  1.00  8.59           C
ATOM    882  CG  LEU A 104      48.059 -13.225  21.959  1.00  8.25           C
ATOM    883  CD1 LEU A 104      46.789 -14.015  21.637  1.00 10.40           C
ATOM    884  CD2 LEU A 104      49.091 -13.405  20.853  1.00 11.36           C
ATOM    885  N   HIS A 105      48.238 -11.360  25.205  1.00 10.00           N
ATOM    886  CA  HIS A 105      48.768 -11.825  26.476  1.00 11.00           C
ATOM    887  C   HIS A 105      47.680 -11.751  27.549  1.00 11.65           C
ATOM    888  O   HIS A 105      47.507 -12.692  28.334  1.00 10.44           O
ATOM    889  CB  HIS A 105      49.976 -10.968  26.858  1.00 12.20           C
ATOM    890  CG  HIS A 105      50.614 -11.350  28.156  1.00 21.18           C
ATOM    891  ND1 HIS A 105      51.601 -12.309  28.247  1.00 32.94           N
ATOM    892  CD2 HIS A 105      50.425 -10.883  29.413  1.00 24.51           C
ATOM    893  CE1 HIS A 105      51.985 -12.424  29.506  1.00 25.08           C
ATOM    894  NE2 HIS A 105      51.289 -11.568  30.234  1.00 28.21           N
ATOM    895  N   LEU A 106      46.939 -10.642  27.568  1.00  9.72           N
ATOM    896  CA  LEU A 106      45.836 -10.459  28.512  1.00  9.23           C
ATOM    897  C   LEU A 106      44.786 -11.556  28.370  1.00 11.99           C
ATOM    898  O   LEU A 106      44.378 -12.173  29.354  1.00 10.62           O
ATOM    899  CB  LEU A 106      45.176  -9.092  28.302  1.00 10.87           C
ATOM    900  CG  LEU A 106      43.865  -8.814  29.045  1.00  9.89           C
ATOM    901  CD1 LEU A 106      44.106  -8.724  30.553  1.00 13.87           C
ATOM    902  CD2 LEU A 106      43.271  -7.525  28.536  1.00 10.10           C
ATOM    903  N   GLU A 107      44.356 -11.814  27.142  1.00 11.49           N
ATOM    904  CA  GLU A 107      43.294 -12.795  26.951  1.00 11.90           C
ATOM    905  C   GLU A 107      43.758 -14.201  27.312  1.00  9.81           C
ATOM    906  O   GLU A 107      42.963 -15.007  27.803  1.00 10.63           O
ATOM    907  CB  GLU A 107      42.759 -12.746  25.522  1.00 11.13           C
ATOM    908  CG  GLU A 107      42.187 -11.397  25.142  1.00 13.32           C
ATOM    909  CD  GLU A 107      40.798 -11.160  25.672  1.00 23.51           C
ATOM    910  OE1 GLU A 107      40.337 -11.935  26.539  1.00 22.53           O
ATOM    911  OE2 GLU A 107      40.165 -10.189  25.209  1.00 25.86           O
ATOM    912  N   LYS A 108      45.027 -14.508  27.063  1.00  9.79           N
ATOM    913  CA  LYS A 108      45.566 -15.795  27.481  1.00 12.37           C
ATOM    914  C   LYS A 108      45.637 -15.884  29.012  1.00 11.21           C
ATOM    915  O   LYS A 108      45.343 -16.933  29.593  1.00 11.00           O
ATOM    916  CB  LYS A 108      46.911 -16.090  26.797  1.00 10.81           C
ATOM    917  CG  LYS A 108      46.754 -16.272  25.275  1.00 10.31           C
ATOM    918  CD  LYS A 108      48.066 -16.630  24.582  1.00 14.70           C
ATOM    919  CE  LYS A 108      48.416 -18.080  24.827  1.00 25.80           C
ATOM    920  NZ  LYS A 108      49.633 -18.471  24.075  1.00 35.41           N
ATOM    921  N   ASN A 109      45.989 -14.785  29.677  1.00  9.78           N
ATOM    922  CA  ASN A 109      45.971 -14.801  31.137  1.00 11.97           C
ATOM    923  C   ASN A 109      44.560 -15.019  31.675  1.00 12.11           C
ATOM    924  O   ASN A 109      44.358 -15.781  32.622  1.00 13.11           O
ATOM    925  CB  ASN A 109      46.554 -13.507  31.708  1.00 10.97           C
ATOM    926  CG  ASN A 109      48.068 -13.530  31.768  1.00 22.88           C
ATOM    927  OD1 ASN A 109      48.685 -14.597  31.787  1.00 31.41           O
ATOM    928  ND2 ASN A 109      48.675 -12.352  31.802  1.00 24.02           N
ATOM    929  N   VAL A 110      43.584 -14.349  31.071  1.00 11.15           N
ATOM    930  CA  VAL A 110      42.202 -14.483  31.506  1.00  8.02           C
ATOM    931  C   VAL A 110      41.723 -15.918  31.282  1.00  8.99           C
ATOM    932  O   VAL A 110      41.053 -16.508  32.133  1.00  9.38           O
ATOM    933  CB  VAL A 110      41.295 -13.493  30.772  1.00  8.92           C
ATOM    934  CG1 VAL A 110      39.829 -13.785  31.072  1.00 13.52           C
ATOM    935  CG2 VAL A 110      41.667 -12.052  31.160  1.00 11.29           C
ATOM    936  N   ASN A 111      42.083 -16.480  30.133  1.00 10.18           N
ATOM    937  CA  ASN A 111      41.760 -17.867  29.835  1.00  9.44           C
ATOM    938  C   ASN A 111      42.337 -18.823  30.879  1.00  8.14           C
ATOM    939  O   ASN A 111      41.652 -19.741  31.338  1.00  9.11           O
ATOM    940  CB  ASN A 111      42.263 -18.231  28.436  1.00  8.58           C
ATOM    941  CG  ASN A 111      41.609 -19.476  27.887  1.00  8.31           C
ATOM    942  OD1 ASN A 111      40.444 -19.744  28.152  1.00  8.86           O
ATOM    943  ND2 ASN A 111      42.358 -20.239  27.107  1.00 11.48           N
ATOM    944  N   GLN A 112      43.595 -18.618  31.252  1.00  9.66           N
ATOM    945  CA  GLN A 112      44.209 -19.468  32.261  1.00 10.24           C
ATOM    946  C   GLN A 112      43.423 -19.387  33.570  1.00  8.85           C
ATOM    947  O   GLN A 112      43.170 -20.405  34.218  1.00  9.14           O
ATOM    948  CB  GLN A 112      45.675 -19.088  32.483  1.00 12.41           C
ATOM    949  CG  GLN A 112      46.360 -19.898  33.565  1.00 14.67           C
ATOM    950  CD  GLN A 112      46.339 -21.394  33.288  1.00 32.38           C
ATOM    951  OE1 GLN A 112      46.214 -22.208  34.207  1.00 37.85           O
ATOM    952  NE2 GLN A 112      46.457 -21.763  32.018  1.00 30.88           N
ATOM    953  N   SER A 113      43.012 -18.180  33.951  1.00  7.74           N
ATOM    954  CA  SER A 113      42.220 -18.018  35.164  1.00  7.00           C
ATOM    955  C   SER A 113      40.898 -18.780  35.071  1.00  8.24           C
ATOM    956  O   SER A 113      40.466 -19.423  36.029  1.00  9.39           O
ATOM    957  CB  SER A 113      41.962 -16.536  35.446  1.00  8.65           C
ATOM    958  OG  SER A 113      41.158 -16.384  36.605  1.00 10.60           O
ATOM    959  N   LEU A 114      40.257 -18.709  33.909  1.00  7.88           N
ATOM    960  CA  LEU A 114      39.002 -19.423  33.692  1.00  7.77           C
ATOM    961  C   LEU A 114      39.179 -20.938  33.736  1.00  9.06           C
ATOM    962  O   LEU A 114      38.318 -21.654  34.241  1.00  8.50           O
ATOM    963  CB  LEU A 114      38.364 -18.989  32.366  1.00  8.40           C
ATOM    964  CG  LEU A 114      37.776 -17.574  32.403  1.00  7.83           C
ATOM    965  CD1 LEU A 114      37.602 -17.039  30.985  1.00  9.54           C
ATOM    966  CD2 LEU A 114      36.457 -17.533  33.154  1.00  9.12           C
ATOM    967  N   LEU A 115      40.290 -21.425  33.189  1.00  9.13           N
ATOM    968  CA  LEU A 115      40.588 -22.855  33.240  1.00  8.97           C
ATOM    969  C   LEU A 115      40.851 -23.308  34.673  1.00 10.21           C
ATOM    970  O   LEU A 115      40.405 -24.389  35.068  1.00  9.40           O
ATOM    971  CB  LEU A 115      41.771 -23.194  32.337  1.00  9.39           C
ATOM    972  CG  LEU A 115      41.478 -23.003  30.845  1.00  9.98           C
ATOM    973  CD1 LEU A 115      42.746 -23.136  30.018  1.00 11.67           C
ATOM    974  CD2 LEU A 115      40.396 -23.982  30.373  1.00  9.62           C
ATOM    975  N   GLU A 116      41.555 -22.490  35.455  1.00  9.66           N
ATOM    976  CA  GLU A 116      41.736 -22.800  36.880  1.00  9.43           C
ATOM    977  C   GLU A 116      40.386 -22.814  37.606  1.00 10.49           C
ATOM    978  O   GLU A 116      40.131 -23.678  38.456  1.00 10.86           O
ATOM    979  CB  GLU A 116      42.719 -21.827  37.536  1.00 11.16           C
ATOM    980  CG  GLU A 116      44.137 -22.011  37.030  1.00 11.99           C
ATOM    981  CD  GLU A 116      45.070 -20.892  37.442  1.00 24.64           C
ATOM    982  OE1 GLU A 116      46.224 -20.889  36.968  1.00 24.19           O
ATOM    983  OE2 GLU A 116      44.654 -20.021  38.235  1.00 30.13           O
ATOM    984  N   LEU A 117      39.508 -21.874  37.253  1.00  9.03           N
ATOM    985  CA  LEU A 117      38.175 -21.825  37.841  1.00  8.83           C
ATOM    986  C   LEU A 117      37.394 -23.095  37.501  1.00  9.33           C
ATOM    987  O   LEU A 117      36.696 -23.664  38.345  1.00  9.25           O
ATOM    988  CB  LEU A 117      37.422 -20.586  37.337  1.00 10.41           C
ATOM    989  CG  LEU A 117      36.525 -19.782  38.282  1.00 18.08           C
ATOM    990  CD1 LEU A 117      35.606 -18.899  37.444  1.00 21.65           C
ATOM    991  CD2 LEU A 117      35.717 -20.626  39.237  1.00 18.85           C
ATOM    992  N   HIS A 118      37.504 -23.542  36.253  1.00  8.39           N
ATOM    993  CA  HIS A 118      36.794 -24.735  35.824  1.00  7.98           C
ATOM    994  C   HIS A 118      37.344 -25.965  36.545  1.00  9.59           C
ATOM    995  O   HIS A 118      36.587 -26.853  36.931  1.00  9.94           O
ATOM    996  CB  HIS A 118      36.890 -24.905  34.306  1.00  8.41           C
ATOM    997  CG  HIS A 118      35.950 -25.934  33.763  1.00  6.57           C
ATOM    998  ND1 HIS A 118      36.164 -27.290  33.909  1.00 10.01           N
ATOM    999  CD2 HIS A 118      34.784 -25.807  33.088  1.00  9.06           C
ATOM   1000  CE1 HIS A 118      35.174 -27.950  33.337  1.00  8.34           C
ATOM   1001  NE2 HIS A 118      34.320 -27.074  32.838  1.00  9.68           N
ATOM   1002  N   LYS A 119      38.661 -26.007  36.727  1.00  9.93           N
ATOM   1003  CA  LYS A 119      39.280 -27.108  37.455  1.00 11.70           C
ATOM   1004  C   LYS A 119      38.746 -27.164  38.887  1.00  9.51           C
ATOM   1005  O   LYS A 119      38.427 -28.235  39.401  1.00  9.59           O
ATOM   1006  CB  LYS A 119      40.806 -26.961  37.439  1.00 11.44           C
ATOM   1007  CG  LYS A 119      41.552 -27.931  38.343  1.00 16.36           C
ATOM   1008  CD  LYS A 119      43.033 -27.548  38.427  1.00 27.98           C
ATOM   1009  CE  LYS A 119      43.717 -28.141  39.659  1.00 39.19           C
ATOM   1010  NZ  LYS A 119      43.645 -29.627  39.694  1.00 45.50           N
ATOM   1011  N   LEU A 120      38.637 -26.006  39.528  1.00 11.14           N
ATOM   1012  CA  LEU A 120      38.058 -25.939  40.865  1.00  9.85           C
ATOM   1013  C   LEU A 120      36.606 -26.419  40.869  1.00 11.06           C
ATOM   1014  O   LEU A 120      36.195 -27.207  41.723  1.00  9.54           O
ATOM   1015  CB  LEU A 120      38.136 -24.511  41.399  1.00  9.61           C
ATOM   1016  CG  LEU A 120      37.454 -24.237  42.740  1.00  9.73           C
ATOM   1017  CD1 LEU A 120      38.048 -25.128  43.817  1.00 13.76           C
ATOM   1018  CD2 LEU A 120      37.598 -22.770  43.129  1.00 12.36           C
ATOM   1019  N   ALA A 121      35.817 -25.934  39.919  1.00  9.37           N
ATOM   1020  CA  ALA A 121      34.425 -26.329  39.849  1.00  8.32           C
ATOM   1021  C   ALA A 121      34.286 -27.838  39.657  1.00  9.34           C
ATOM   1022  O   ALA A 121      33.409 -28.473  40.237  1.00 10.42           O
ATOM   1023  CB  ALA A 121      33.735 -25.582  38.712  1.00  8.93           C
ATOM   1024  N   THR A 122      35.167 -28.403  38.842  1.00  9.28           N
ATOM   1025  CA  THR A 122      35.222 -29.837  38.607  1.00  8.24           C
ATOM   1026  C   THR A 122      35.602 -30.579  39.896  1.00 10.61           C
ATOM   1027  O   THR A 122      34.981 -31.578  40.262  1.00 10.71           O
ATOM   1028  CB  THR A 122      36.245 -30.138  37.492  1.00 10.21           C
ATOM   1029  OG1 THR A 122      35.764 -29.612  36.244  1.00 10.19           O
ATOM   1030  CG2 THR A 122      36.460 -31.629  37.337  1.00 12.08           C
ATOM   1031  N   ASP A 123      36.614 -30.077  40.591  1.00 10.50           N
ATOM   1032  CA  ASP A 123      37.045 -30.707  41.837  1.00 11.72           C
ATOM   1033  C   ASP A 123      35.936 -30.712  42.889  1.00 10.24           C
ATOM   1034  O   ASP A 123      35.843 -31.654  43.681  1.00 12.55           O
ATOM   1035  CB  ASP A 123      38.287 -30.012  42.393  1.00 11.45           C
ATOM   1036  CG  ASP A 123      39.538 -30.314  41.585  1.00 22.20           C
ATOM   1037  OD1 ASP A 123      40.537 -29.573  41.725  1.00 25.92           O
ATOM   1038  OD2 ASP A 123      39.524 -31.294  40.812  1.00 24.76           O
ATOM   1039  N   LYS A 124      35.105 -29.669  42.896  1.00  8.77           N
ATOM   1040  CA  LYS A 124      34.005 -29.547  43.854  1.00  9.09           C
ATOM   1041  C   LYS A 124      32.690 -30.111  43.303  1.00  9.66           C
ATOM   1042  O   LYS A 124      31.631 -29.923  43.895  1.00  9.97           O
ATOM   1043  CB  LYS A 124      33.817 -28.085  44.283  1.00 10.17           C
ATOM   1044  CG  LYS A 124      35.062 -27.453  44.911  1.00 10.12           C
ATOM   1045  CD  LYS A 124      35.568 -28.296  46.077  1.00 12.39           C
ATOM   1046  CE  LYS A 124      36.603 -27.548  46.888  1.00 14.42           C
ATOM   1047  NZ  LYS A 124      37.156 -28.437  47.960  1.00 20.81           N
ATOM   1048  N   ASN A 125      32.768 -30.794  42.163  1.00  8.84           N
ATOM   1049  CA  ASN A 125      31.606 -31.448  41.563  1.00  8.74           C
ATOM   1050  C   ASN A 125      30.434 -30.480  41.434  1.00 10.18           C
ATOM   1051  O   ASN A 125      29.324 -30.743  41.914  1.00  9.92           O
ATOM   1052  CB  ASN A 125      31.212 -32.697  42.367  1.00  9.90           C
ATOM   1053  CG  ASN A 125      32.375 -33.668  42.544  1.00 18.71           C
ATOM   1054  OD1 ASN A 125      32.872 -34.232  41.576  1.00 25.12           O
ATOM   1055  ND2 ASN A 125      32.814 -33.849  43.783  1.00 26.45           N
ATOM   1056  N   ASP A 126      30.705 -29.350  40.779  1.00  9.36           N
ATOM   1057  CA  ASP A 126      29.698 -28.317  40.540  1.00  8.16           C
ATOM   1058  C   ASP A 126      29.435 -28.251  39.039  1.00  8.39           C
ATOM   1059  O   ASP A 126      30.028 -27.439  38.327  1.00  8.58           O
ATOM   1060  CB  ASP A 126      30.213 -26.971  41.059  1.00  7.53           C
ATOM   1061  CG  ASP A 126      29.138 -25.882  41.089  1.00  7.37           C
ATOM   1062  OD1 ASP A 126      28.156 -25.970  40.310  1.00  9.03           O
ATOM   1063  OD2 ASP A 126      29.289 -24.930  41.889  1.00  9.40           O
ATOM   1064  N   PRO A 127      28.538 -29.108  38.540  1.00  7.61           N
ATOM   1065  CA  PRO A 127      28.344 -29.138  37.085  1.00  8.10           C
ATOM   1066  C   PRO A 127      27.633 -27.894  36.570  1.00  7.52           C
ATOM   1067  O   PRO A 127      27.836 -27.520  35.409  1.00  8.54           O
ATOM   1068  CB  PRO A 127      27.476 -30.385  36.876  1.00  7.59           C
ATOM   1069  CG  PRO A 127      26.750 -30.564  38.192  1.00  8.27           C
ATOM   1070  CD  PRO A 127      27.770 -30.165  39.226  1.00  8.15           C
ATOM   1071  N   HIS A 128      26.819 -27.252  37.402  1.00  7.10           N
ATOM   1072  CA  HIS A 128      26.190 -26.022  36.940  1.00  6.81           C
ATOM   1073  C   HIS A 128      27.253 -24.963  36.652  1.00  7.68           C
ATOM   1074  O   HIS A 128      27.196 -24.249  35.638  1.00  8.22           O
ATOM   1075  CB  HIS A 128      25.181 -25.473  37.945  1.00  6.35           C
ATOM   1076  CG  HIS A 128      24.647 -24.132  37.543  1.00  6.24           C
ATOM   1077  ND1 HIS A 128      25.198 -22.951  37.979  1.00  7.95           N
ATOM   1078  CD2 HIS A 128      23.659 -23.795  36.678  1.00  7.71           C
ATOM   1079  CE1 HIS A 128      24.552 -21.935  37.432  1.00  6.85           C
ATOM   1080  NE2 HIS A 128      23.618 -22.423  36.626  1.00  7.44           N
ATOM   1081  N   LEU A 129      28.235 -24.855  37.543  1.00  7.76           N
ATOM   1082  CA  LEU A 129      29.279 -23.855  37.375  1.00  6.52           C
ATOM   1083  C   LEU A 129      30.188 -24.198  36.194  1.00  7.94           C
ATOM   1084  O   LEU A 129      30.603 -23.323  35.431  1.00  7.89           O
ATOM   1085  CB  LEU A 129      30.105 -23.713  38.663  1.00  6.90           C
ATOM   1086  CG  LEU A 129      31.216 -22.665  38.643  1.00  7.65           C
ATOM   1087  CD1 LEU A 129      30.682 -21.288  38.242  1.00 11.54           C
ATOM   1088  CD2 LEU A 129      31.854 -22.609  40.030  1.00 10.65           C
ATOM   1089  N   CYS A 130      30.493 -25.484  36.036  1.00  7.18           N
ATOM   1090  CA  CYS A 130      31.257 -25.941  34.879  1.00  7.47           C
ATOM   1091  C   CYS A 130      30.578 -25.525  33.579  1.00  9.28           C
ATOM   1092  O   CYS A 130      31.211 -24.944  32.699  1.00  9.56           O
ATOM   1093  CB  CYS A 130      31.422 -27.456  34.907  1.00  8.91           C
ATOM   1094  SG  CYS A 130      32.654 -28.018  36.101  1.00 10.70           S
ATOM   1095  N   ASP A 131      29.288 -25.824  33.472  1.00  8.07           N
ATOM   1096  CA  ASP A 131      28.511 -25.484  32.286  1.00  8.89           C
ATOM   1097  C   ASP A 131      28.463 -23.967  32.074  1.00  9.45           C
ATOM   1098  O   ASP A 131      28.552 -23.484  30.950  1.00  9.76           O
ATOM   1099  CB  ASP A 131      27.096 -26.072  32.398  1.00  9.45           C
ATOM   1100  CG  ASP A 131      26.156 -25.560  31.317  1.00 14.41           C
ATOM   1101  OD1 ASP A 131      26.272 -26.009  30.164  1.00 16.12           O
ATOM   1102  OD2 ASP A 131      25.303 -24.711  31.632  1.00 24.13           O
ATOM   1103  N   PHE A 132      28.328 -23.211  33.154  1.00  8.13           N
ATOM   1104  CA  PHE A 132      28.321 -21.753  33.043  1.00  7.34           C
ATOM   1105  C   PHE A 132      29.617 -21.240  32.417  1.00  8.93           C
ATOM   1106  O   PHE A 132      29.604 -20.403  31.519  1.00  8.81           O
ATOM   1107  CB  PHE A 132      28.113 -21.140  34.432  1.00  8.57           C
ATOM   1108  CG  PHE A 132      28.281 -19.642  34.479  1.00  7.60           C
ATOM   1109  CD1 PHE A 132      29.509 -19.080  34.784  1.00  8.31           C
ATOM   1110  CD2 PHE A 132      27.207 -18.803  34.239  1.00 10.76           C
ATOM   1111  CE1 PHE A 132      29.667 -17.693  34.835  1.00 10.16           C
ATOM   1112  CE2 PHE A 132      27.357 -17.425  34.291  1.00 10.95           C
ATOM   1113  CZ  PHE A 132      28.588 -16.876  34.584  1.00 10.75           C
ATOM   1114  N   ILE A 133      30.747 -21.745  32.891  1.00  7.18           N
ATOM   1115  CA AILE A 133      32.044 -21.306  32.391  0.24  7.27           C
ATOM   1116  CA BILE A 133      32.053 -21.322  32.399  0.76  7.23           C
ATOM   1117  C   ILE A 133      32.245 -21.733  30.939  1.00  6.75           C
ATOM   1118  O   ILE A 133      32.704 -20.938  30.104  1.00  8.40           O
ATOM   1119  CB AILE A 133      33.193 -21.844  33.265  0.24  7.22           C
ATOM   1120  CB BILE A 133      33.172 -21.935  33.270  0.76  7.13           C
ATOM   1121  CG1AILE A 133      33.067 -21.311  34.693  0.24  9.42           C
ATOM   1122  CG1BILE A 133      33.111 -21.371  34.693  0.76  9.53           C
ATOM   1123  CG2AILE A 133      34.540 -21.450  32.678  0.24  9.49           C
ATOM   1124  CG2BILE A 133      34.546 -21.685  32.650  0.76  9.76           C
ATOM   1125  CD1AILE A 133      33.329 -19.829  34.819  0.24 10.13           C
ATOM   1126  CD1BILE A 133      33.882 -22.219  35.719  0.76  6.87           C
ATOM   1127  N   GLU A 134      31.888 -22.973  30.632  1.00  7.61           N
ATOM   1128  CA  GLU A 134      31.992 -23.479  29.264  1.00  7.76           C
ATOM   1129  C   GLU A 134      31.132 -22.674  28.303  1.00 10.28           C
ATOM   1130  O   GLU A 134      31.602 -22.240  27.246  1.00 13.17           O
ATOM   1131  CB  GLU A 134      31.594 -24.949  29.216  1.00  8.57           C
ATOM   1132  CG  GLU A 134      32.618 -25.853  29.868  1.00 10.11           C
ATOM   1133  CD  GLU A 134      32.103 -27.247  30.134  1.00 15.61           C
ATOM   1134  OE1 GLU A 134      31.549 -27.887  29.216  1.00 18.53           O
ATOM   1135  OE2 GLU A 134      32.266 -27.716  31.267  1.00 11.57           O
ATOM   1136  N   THR A 135      29.880 -22.456  28.682  1.00  9.26           N
ATOM   1137  CA  THR A 135      28.911 -21.810  27.810  1.00  8.13           C
ATOM   1138  C   THR A 135      29.253 -20.356  27.518  1.00 11.48           C
ATOM   1139  O   THR A 135      29.237 -19.914  26.357  1.00 12.82           O
ATOM   1140  CB  THR A 135      27.511 -21.850  28.455  1.00 12.10           C
ATOM   1141  OG1 THR A 135      27.089 -23.210  28.575  1.00 15.06           O
ATOM   1142  CG2 THR A 135      26.501 -21.062  27.614  1.00 12.53           C
ATOM   1143  N   HIS A 136      29.575 -19.610  28.567  1.00  8.66           N
ATOM   1144  CA  HIS A 136      29.662 -18.169  28.445  1.00  6.96           C
ATOM   1145  C   HIS A 136      31.074 -17.633  28.336  1.00  9.09           C
ATOM   1146  O   HIS A 136      31.249 -16.486  27.929  1.00 10.92           O
ATOM   1147  CB  HIS A 136      28.934 -17.495  29.607  1.00  9.28           C
ATOM   1148  CG  HIS A 136      27.475 -17.816  29.649  1.00 10.29           C
ATOM   1149  ND1 HIS A 136      26.597 -17.383  28.678  1.00 16.03           N
ATOM   1150  CD2 HIS A 136      26.745 -18.551  30.520  1.00 12.93           C
ATOM   1151  CE1 HIS A 136      25.385 -17.830  28.956  1.00 17.45           C
ATOM   1152  NE2 HIS A 136      25.448 -18.543  30.066  1.00 14.94           N
ATOM   1153  N   TYR A 137      32.082 -18.442  28.671  1.00  8.45           N
ATOM   1154  CA  TYR A 137      33.449 -17.922  28.728  1.00  7.65           C
ATOM   1155  C   TYR A 137      34.487 -18.661  27.887  1.00  8.85           C
ATOM   1156  O   TYR A 137      35.292 -18.020  27.218  1.00 10.60           O
ATOM   1157  CB  TYR A 137      33.926 -17.786  30.194  1.00  7.92           C
ATOM   1158  CG  TYR A 137      33.098 -16.760  30.920  1.00  7.11           C
ATOM   1159  CD1 TYR A 137      31.854 -17.089  31.440  1.00  8.37           C
ATOM   1160  CD2 TYR A 137      33.524 -15.440  31.021  1.00 11.50           C
ATOM   1161  CE1 TYR A 137      31.073 -16.138  32.058  1.00  7.16           C
ATOM   1162  CE2 TYR A 137      32.748 -14.487  31.644  1.00 10.87           C
ATOM   1163  CZ  TYR A 137      31.520 -14.842  32.152  1.00  8.81           C
ATOM   1164  OH  TYR A 137      30.729 -13.897  32.751  1.00  8.80           O
ATOM   1165  N   LEU A 138      34.498 -19.991  27.926  1.00  8.98           N
ATOM   1166  CA  LEU A 138      35.645 -20.701  27.361  1.00  7.80           C
ATOM   1167  C   LEU A 138      35.773 -20.538  25.855  1.00  8.13           C
ATOM   1168  O   LEU A 138      36.873 -20.315  25.363  1.00  8.44           O
ATOM   1169  CB  LEU A 138      35.648 -22.188  27.733  1.00  7.89           C
ATOM   1170  CG  LEU A 138      35.800 -22.456  29.230  1.00  8.08           C
ATOM   1171  CD1 LEU A 138      36.027 -23.944  29.401  1.00  7.97           C
ATOM   1172  CD2 LEU A 138      36.940 -21.663  29.852  1.00  8.81           C
ATOM   1173  N   ASN A 139      34.674 -20.657  25.114  1.00  8.25           N
ATOM   1174  CA  ASN A 139      34.796 -20.490  23.669  1.00  8.03           C
ATOM   1175  C   ASN A 139      34.965 -19.023  23.299  1.00  8.84           C
ATOM   1176  O   ASN A 139      35.618 -18.705  22.309  1.00  8.80           O
ATOM   1177  CB  ASN A 139      33.650 -21.136  22.890  1.00  9.22           C
ATOM   1178  CG  ASN A 139      33.949 -21.223  21.406  1.00  9.42           C
ATOM   1179  OD1 ASN A 139      34.969 -21.789  20.994  1.00  8.94           O
ATOM   1180  ND2 ASN A 139      33.075 -20.644  20.591  1.00 10.12           N
ATOM   1181  N   GLU A 140      34.398 -18.117  24.090  1.00  8.84           N
ATOM   1182  CA AGLU A 140      34.632 -16.706  23.831  0.53 10.13           C
ATOM   1183  CA BGLU A 140      34.631 -16.699  23.859  0.47 10.15           C
ATOM   1184  C   GLU A 140      36.124 -16.399  23.934  1.00  8.78           C
ATOM   1185  O   GLU A 140      36.655 -15.645  23.124  1.00  9.80           O
ATOM   1186  CB AGLU A 140      33.787 -15.812  24.749  0.53 11.52           C
ATOM   1187  CB BGLU A 140      33.875 -15.838  24.871  0.47 11.65           C
ATOM   1188  CG AGLU A 140      32.298 -16.031  24.543  0.53 11.33           C
ATOM   1189  CG BGLU A 140      33.727 -14.398  24.427  0.47 18.30           C
ATOM   1190  CD AGLU A 140      31.426 -14.892  25.035  0.53 20.79           C
ATOM   1191  CD BGLU A 140      32.852 -14.271  23.184  0.47 17.02           C
ATOM   1192  OE1AGLU A 140      31.949 -13.790  25.304  0.53 23.28           O
ATOM   1193  OE1BGLU A 140      31.955 -15.124  22.992  0.47 24.04           O
ATOM   1194  OE2AGLU A 140      30.199 -15.103  25.136  0.53 28.03           O
ATOM   1195  OE2BGLU A 140      33.049 -13.318  22.409  0.47 25.52           O
ATOM   1196  N   GLN A 141      36.809 -17.005  24.905  1.00  8.32           N
ATOM   1197  CA  GLN A 141      38.246 -16.799  25.050  1.00  9.63           C
ATOM   1198  C   GLN A 141      39.016 -17.391  23.878  1.00  8.09           C
ATOM   1199  O   GLN A 141      39.929 -16.770  23.356  1.00  8.73           O
ATOM   1200  CB  GLN A 141      38.781 -17.395  26.356  1.00 10.14           C
ATOM   1201  CG  GLN A 141      38.482 -16.563  27.589  1.00 14.09           C
ATOM   1202  CD  GLN A 141      38.727 -15.092  27.352  1.00 12.80           C
ATOM   1203  OE1 GLN A 141      37.788 -14.328  27.166  1.00 17.73           O
ATOM   1204  NE2 GLN A 141      39.996 -14.695  27.308  1.00 12.68           N
ATOM   1205  N   VAL A 142      38.654 -18.601  23.472  1.00  7.88           N
ATOM   1206  CA  VAL A 142      39.322 -19.220  22.335  1.00  8.22           C
ATOM   1207  C   VAL A 142      39.156 -18.367  21.075  1.00  8.15           C
ATOM   1208  O   VAL A 142      40.126 -18.137  20.350  1.00  7.95           O
ATOM   1209  CB  VAL A 142      38.843 -20.671  22.127  1.00  6.54           C
ATOM   1210  CG1 VAL A 142      39.185 -21.160  20.729  1.00  7.86           C
ATOM   1211  CG2 VAL A 142      39.484 -21.570  23.190  1.00  8.68           C
ATOM   1212  N   LYS A 143      37.947 -17.860  20.835  1.00  8.13           N
ATOM   1213  CA  LYS A 143      37.728 -16.988  19.684  1.00  8.42           C
ATOM   1214  C   LYS A 143      38.528 -15.686  19.787  1.00  9.49           C
ATOM   1215  O   LYS A 143      39.104 -15.224  18.798  1.00  9.33           O
ATOM   1216  CB  LYS A 143      36.239 -16.686  19.504  1.00  8.67           C
ATOM   1217  CG  LYS A 143      35.433 -17.892  19.044  1.00  9.42           C
ATOM   1218  CD  LYS A 143      33.957 -17.537  18.817  1.00 12.09           C
ATOM   1219  CE  LYS A 143      33.300 -17.038  20.087  1.00 16.17           C
ATOM   1220  NZ  LYS A 143      31.857 -16.676  19.864  1.00 22.13           N
ATOM   1221  N   ALA A 144      38.578 -15.097  20.981  1.00  9.03           N
ATOM   1222  CA  ALA A 144      39.289 -13.832  21.161  1.00  9.35           C
ATOM   1223  C   ALA A 144      40.786 -14.004  20.940  1.00  8.56           C
ATOM   1224  O   ALA A 144      41.452 -13.170  20.298  1.00  9.15           O
ATOM   1225  CB  ALA A 144      39.022 -13.259  22.548  1.00 10.44           C
ATOM   1226  N   ILE A 145      41.329 -15.085  21.485  1.00  7.63           N
ATOM   1227  CA  ILE A 145      42.751 -15.362  21.362  1.00  7.72           C
ATOM   1228  C   ILE A 145      43.116 -15.618  19.901  1.00  7.57           C
ATOM   1229  O   ILE A 145      44.128 -15.118  19.409  1.00  7.88           O
ATOM   1230  CB  ILE A 145      43.158 -16.541  22.280  1.00  6.90           C
ATOM   1231  CG1 ILE A 145      43.079 -16.097  23.745  1.00  9.34           C
ATOM   1232  CG2 ILE A 145      44.569 -17.044  21.950  1.00  8.45           C
ATOM   1233  CD1 ILE A 145      43.012 -17.258  24.724  1.00 10.33           C
ATOM   1234  N   LYS A 146      42.280 -16.377  19.201  1.00  7.73           N
ATOM   1235  CA  LYS A 146      42.513 -16.645  17.791  1.00  8.71           C
ATOM   1236  C   LYS A 146      42.481 -15.360  16.959  1.00  7.49           C
ATOM   1237  O   LYS A 146      43.344 -15.148  16.112  1.00  8.68           O
ATOM   1238  CB  LYS A 146      41.498 -17.676  17.272  1.00  7.68           C
ATOM   1239  CG  LYS A 146      41.564 -17.950  15.757  1.00  7.10           C
ATOM   1240  CD  LYS A 146      42.919 -18.525  15.324  1.00  7.10           C
ATOM   1241  CE  LYS A 146      42.848 -19.203  13.949  1.00  7.75           C
ATOM   1242  NZ  LYS A 146      42.570 -18.233  12.844  1.00  8.60           N
ATOM   1243  N   GLU A 147      41.496 -14.505  17.217  1.00  6.51           N
ATOM   1244  CA  GLU A 147      41.389 -13.235  16.503  1.00  7.03           C
ATOM   1245  C   GLU A 147      42.606 -12.344  16.732  1.00  7.71           C
ATOM   1246  O   GLU A 147      43.157 -11.771  15.786  1.00  8.83           O
ATOM   1247  CB  GLU A 147      40.113 -12.516  16.908  1.00  7.61           C
ATOM   1248  CG  GLU A 147      39.968 -11.123  16.327  1.00 10.88           C
ATOM   1249  CD  GLU A 147      38.616 -10.553  16.659  1.00 15.86           C
ATOM   1250  OE1 GLU A 147      38.534  -9.690  17.561  1.00 15.40           O
ATOM   1251  OE2 GLU A 147      37.619 -11.012  16.053  1.00 19.22           O
ATOM   1252  N   LEU A 148      43.043 -12.235  17.986  1.00  7.43           N
ATOM   1253  CA  LEU A 148      44.210 -11.420  18.291  1.00  7.17           C
ATOM   1254  C   LEU A 148      45.469 -12.008  17.673  1.00  7.34           C
ATOM   1255  O   LEU A 148      46.331 -11.266  17.188  1.00  8.09           O
ATOM   1256  CB  LEU A 148      44.366 -11.255  19.797  1.00  8.03           C
ATOM   1257  CG  LEU A 148      43.293 -10.348  20.395  1.00  8.98           C
ATOM   1258  CD1 LEU A 148      43.201 -10.533  21.907  1.00 10.49           C
ATOM   1259  CD2 LEU A 148      43.565  -8.882  20.030  1.00 11.03           C
ATOM   1260  N   GLY A 149      45.572 -13.337  17.658  1.00  7.68           N
ATOM   1261  CA  GLY A 149      46.688 -13.982  16.982  1.00  7.94           C
ATOM   1262  C   GLY A 149      46.701 -13.632  15.504  1.00  8.20           C
ATOM   1263  O   GLY A 149      47.735 -13.291  14.938  1.00  7.84           O
ATOM   1264  N   ASP A 150      45.533 -13.719  14.879  1.00  7.97           N
ATOM   1265  CA  ASP A 150      45.409 -13.373  13.471  1.00  7.80           C
ATOM   1266  C   ASP A 150      45.856 -11.928  13.244  1.00  8.06           C
ATOM   1267  O   ASP A 150      46.591 -11.636  12.295  1.00  8.02           O
ATOM   1268  CB  ASP A 150      43.951 -13.499  13.011  1.00  7.56           C
ATOM   1269  CG  ASP A 150      43.446 -14.941  12.934  1.00 10.23           C
ATOM   1270  OD1 ASP A 150      44.221 -15.917  13.044  1.00  9.16           O
ATOM   1271  OD2 ASP A 150      42.214 -15.088  12.754  1.00 11.57           O
ATOM   1272  N   HIS A 151      45.422 -11.025  14.123  1.00  7.08           N
ATOM   1273  CA  HIS A 151      45.762  -9.610  13.984  1.00  7.03           C
ATOM   1274  C   HIS A 151      47.266  -9.386  14.111  1.00  9.08           C
ATOM   1275  O   HIS A 151      47.872  -8.671  13.303  1.00  8.47           O
ATOM   1276  CB  HIS A 151      45.009  -8.765  15.018  1.00  7.10           C
ATOM   1277  CG  HIS A 151      43.539  -8.645  14.757  1.00  6.39           C
ATOM   1278  ND1 HIS A 151      42.944  -9.090  13.597  1.00  8.94           N
ATOM   1279  CD2 HIS A 151      42.547  -8.113  15.512  1.00  9.02           C
ATOM   1280  CE1 HIS A 151      41.648  -8.837  13.648  1.00  9.10           C
ATOM   1281  NE2 HIS A 151      41.381  -8.242  14.799  1.00  9.62           N
ATOM   1282  N   VAL A 152      47.872  -9.996  15.127  1.00  7.55           N
ATOM   1283  CA  VAL A 152      49.309  -9.868  15.331  1.00  7.76           C
ATOM   1284  C   VAL A 152      50.061 -10.369  14.097  1.00  9.70           C
ATOM   1285  O   VAL A 152      50.982  -9.714  13.599  1.00  8.64           O
ATOM   1286  CB  VAL A 152      49.743 -10.642  16.583  1.00  7.14           C
ATOM   1287  CG1 VAL A 152      51.257 -10.776  16.625  1.00 10.98           C
ATOM   1288  CG2 VAL A 152      49.228  -9.940  17.826  1.00  8.39           C
ATOM   1289  N   THR A 153      49.653 -11.527  13.587  1.00  7.85           N
ATOM   1290  CA  THR A 153      50.283 -12.083  12.397  1.00  7.70           C
ATOM   1291  C   THR A 153      50.227 -11.126  11.217  1.00  8.70           C
ATOM   1292  O   THR A 153      51.238 -10.875  10.560  1.00 10.26           O
ATOM   1293  CB  THR A 153      49.630 -13.402  12.019  1.00  8.79           C
ATOM   1294  OG1 THR A 153      49.970 -14.369  13.021  1.00  9.27           O
ATOM   1295  CG2 THR A 153      50.134 -13.884  10.680  1.00  8.23           C
ATOM   1296  N   ASN A 154      49.045 -10.602  10.936  1.00  8.67           N
ATOM   1297  CA  ASN A 154      48.913  -9.672   9.821  1.00  8.27           C
ATOM   1298  C   ASN A 154      49.770  -8.424   9.998  1.00 10.13           C
ATOM   1299  O   ASN A 154      50.457  -8.004   9.069  1.00 10.15           O
ATOM   1300  CB  ASN A 154      47.446  -9.319   9.586  1.00  8.63           C
ATOM   1301  CG  ASN A 154      46.739 -10.376   8.758  1.00 11.15           C
ATOM   1302  OD1 ASN A 154      46.971 -10.479   7.558  1.00 10.97           O
ATOM   1303  ND2 ASN A 154      45.919 -11.195   9.402  1.00 12.40           N
ATOM   1304  N   LEU A 155      49.763  -7.847  11.196  1.00  8.80           N
ATOM   1305  CA  LEU A 155      50.581  -6.663  11.425  1.00  7.61           C
ATOM   1306  C   LEU A 155      52.072  -6.957  11.220  1.00  9.89           C
ATOM   1307  O   LEU A 155      52.778  -6.170  10.580  1.00 10.38           O
ATOM   1308  CB  LEU A 155      50.303  -6.076  12.811  1.00  7.62           C
ATOM   1309  CG  LEU A 155      48.969  -5.323  12.859  1.00  8.24           C
ATOM   1310  CD1 LEU A 155      48.452  -5.178  14.290  1.00 10.74           C
ATOM   1311  CD2 LEU A 155      49.094  -3.943  12.199  1.00  9.65           C
ATOM   1312  N   ARG A 156      52.548  -8.090  11.737  1.00  9.63           N
ATOM   1313  CA  ARG A 156      53.947  -8.473  11.529  1.00 10.00           C
ATOM   1314  C   ARG A 156      54.264  -8.645  10.050  1.00 12.89           C
ATOM   1315  O   ARG A 156      55.273  -8.126   9.551  1.00 13.78           O
ATOM   1316  CB  ARG A 156      54.263  -9.773  12.272  1.00 12.78           C
ATOM   1317  CG  ARG A 156      54.303  -9.635  13.785  1.00 13.22           C
ATOM   1318  CD  ARG A 156      54.618 -10.969  14.446  1.00 17.05           C
ATOM   1319  NE  ARG A 156      54.753 -10.828  15.893  1.00 21.40           N
ATOM   1320  CZ  ARG A 156      54.379 -11.749  16.774  1.00 31.09           C
ATOM   1321  NH1 ARG A 156      53.827 -12.889  16.363  1.00 36.94           N
ATOM   1322  NH2 ARG A 156      54.547 -11.520  18.069  1.00 27.29           N
ATOM   1323  N   LYS A 157      53.413  -9.388   9.346  1.00 10.57           N
ATOM   1324  CA  LYS A 157      53.658  -9.645   7.930  1.00 11.88           C
ATOM   1325  C   LYS A 157      53.647  -8.368   7.103  1.00 14.03           C
ATOM   1326  O   LYS A 157      54.391  -8.251   6.126  1.00 18.25           O
ATOM   1327  CB  LYS A 157      52.673 -10.673   7.383  1.00 13.43           C
ATOM   1328  CG  LYS A 157      52.994 -12.075   7.878  1.00 18.60           C
ATOM   1329  CD  LYS A 157      52.198 -13.144   7.169  1.00 28.07           C
ATOM   1330  CE  LYS A 157      52.686 -14.524   7.582  1.00 26.10           C
ATOM   1331  NZ  LYS A 157      53.988 -14.910   6.942  1.00 25.16           N
ATOM   1332  N   MET A 158      52.826  -7.404   7.507  1.00 11.38           N
ATOM   1333  CA  MET A 158      52.711  -6.145   6.777  1.00 12.03           C
ATOM   1334  C   MET A 158      53.898  -5.218   7.017  1.00 13.03           C
ATOM   1335  O   MET A 158      54.080  -4.245   6.282  1.00 14.48           O
ATOM   1336  CB  MET A 158      51.416  -5.415   7.147  1.00 10.60           C
ATOM   1337  CG  MET A 158      50.156  -6.129   6.688  1.00 12.12           C
ATOM   1338  SD  MET A 158      48.674  -5.384   7.388  1.00 12.23           S
ATOM   1339  CE  MET A 158      48.567  -3.868   6.440  1.00 12.53           C
ATOM   1340  N   GLY A 159      54.688  -5.503   8.048  1.00 13.20           N
ATOM   1341  CA  GLY A 159      55.868  -4.705   8.357  1.00 15.00           C
ATOM   1342  C   GLY A 159      55.810  -3.840   9.609  1.00 16.90           C
ATOM   1343  O   GLY A 159      56.705  -3.017   9.844  1.00 16.98           O
ATOM   1344  N   ALA A 160      54.771  -4.008  10.420  1.00 12.14           N
ATOM   1345  CA  ALA A 160      54.670  -3.290  11.693  1.00 12.34           C
ATOM   1346  C   ALA A 160      55.724  -3.803  12.676  1.00 16.81           C
ATOM   1347  O   ALA A 160      56.174  -4.943  12.560  1.00 17.21           O
ATOM   1348  CB  ALA A 160      53.275  -3.453  12.284  1.00 15.13           C
ATOM   1349  N   PRO A 161      56.108  -2.973  13.662  1.00 19.54           N
ATOM   1350  CA  PRO A 161      55.614  -1.621  13.945  1.00 23.01           C
ATOM   1351  C   PRO A 161      56.358  -0.529  13.180  1.00 26.19           C
ATOM   1352  O   PRO A 161      55.929   0.629  13.217  1.00 22.91           O
ATOM   1353  CB  PRO A 161      55.906  -1.467  15.436  1.00 28.72           C
ATOM   1354  CG  PRO A 161      57.166  -2.256  15.631  1.00 25.74           C
ATOM   1355  CD  PRO A 161      57.080  -3.424  14.677  1.00 20.36           C
ATOM   1356  N   GLU A 162      57.452  -0.887  12.511  1.00 20.27           N
ATOM   1357  CA  GLU A 162      58.282   0.099  11.832  1.00 24.02           C
ATOM   1358  C   GLU A 162      57.504   0.819  10.746  1.00 29.71           C
ATOM   1359  O   GLU A 162      57.618   2.037  10.596  1.00 29.45           O
ATOM   1360  CB  GLU A 162      59.534  -0.547  11.228  1.00 21.40           C
ATOM   1361  CG  GLU A 162      60.549  -1.038  12.256  1.00 30.98           C
ATOM   1362  CD  GLU A 162      60.257  -2.442  12.754  1.00 35.48           C
ATOM   1363  OE1 GLU A 162      61.031  -2.946  13.596  1.00 39.60           O
ATOM   1364  OE2 GLU A 162      59.261  -3.045  12.303  1.00 26.63           O
ATOM   1365  N   SER A 163      56.714   0.061   9.992  1.00 20.30           N
ATOM   1366  CA  SER A 163      55.901   0.628   8.919  1.00 21.58           C
ATOM   1367  C   SER A 163      54.636   1.285   9.474  1.00 24.14           C
ATOM   1368  O   SER A 163      53.686   0.605   9.886  1.00 20.81           O
ATOM   1369  CB  SER A 163      55.542  -0.459   7.901  1.00 20.38           C
ATOM   1370  OG  SER A 163      54.746   0.057   6.846  1.00 21.14           O
ATOM   1371  N   GLY A 164      54.633   2.612   9.498  1.00 20.39           N
ATOM   1372  CA  GLY A 164      53.443   3.359   9.858  1.00 20.93           C
ATOM   1373  C   GLY A 164      52.351   3.137   8.830  1.00 19.91           C
ATOM   1374  O   GLY A 164      51.167   3.142   9.172  1.00 16.65           O
ATOM   1375  N   LEU A 165      52.753   2.950   7.571  1.00 17.09           N
ATOM   1376  CA  LEU A 165      51.822   2.559   6.505  1.00 18.59           C
ATOM   1377  C   LEU A 165      51.090   1.232   6.782  1.00 14.92           C
ATOM   1378  O   LEU A 165      49.888   1.126   6.534  1.00 13.02           O
ATOM   1379  CB  LEU A 165      52.548   2.492   5.158  1.00 21.24           C
ATOM   1380  CG  LEU A 165      51.685   2.260   3.913  1.00 16.78           C
ATOM   1381  CD1 LEU A 165      50.681   3.390   3.760  1.00 15.85           C
ATOM   1382  CD2 LEU A 165      52.540   2.160   2.669  1.00 16.71           C
ATOM   1383  N   ALA A 166      51.803   0.225   7.290  1.00 11.87           N
ATOM   1384  CA  ALA A 166      51.169  -1.045   7.655  1.00 14.43           C
ATOM   1385  C   ALA A 166      50.050  -0.859   8.680  1.00 11.80           C
ATOM   1386  O   ALA A 166      48.932  -1.346   8.488  1.00 10.21           O
ATOM   1387  CB  ALA A 166      52.206  -2.043   8.176  1.00 13.04           C
ATOM   1388  N   GLU A 167      50.337  -0.167   9.781  1.00  9.09           N
ATOM   1389  CA  GLU A 167      49.317   0.008  10.800  1.00  9.42           C
ATOM   1390  C   GLU A 167      48.148   0.845  10.261  1.00  7.38           C
ATOM   1391  O   GLU A 167      46.986   0.574  10.561  1.00  8.79           O
ATOM   1392  CB  GLU A 167      49.931   0.590  12.084  1.00 12.65           C
ATOM   1393  CG  GLU A 167      51.138  -0.251  12.565  1.00 15.66           C
ATOM   1394  CD  GLU A 167      51.362  -0.198  14.060  1.00 17.93           C
ATOM   1395  OE1 GLU A 167      51.827  -1.218  14.626  1.00 13.11           O
ATOM   1396  OE2 GLU A 167      51.074   0.854  14.673  1.00 15.64           O
ATOM   1397  N   TYR A 168      48.457   1.836   9.430  1.00  8.54           N
ATOM   1398  CA  TYR A 168      47.422   2.650   8.827  1.00  8.22           C
ATOM   1399  C   TYR A 168      46.481   1.800   7.976  1.00  8.13           C
ATOM   1400  O   TYR A 168      45.253   1.920   8.067  1.00  7.51           O
ATOM   1401  CB  TYR A 168      48.049   3.765   7.975  1.00  8.59           C
ATOM   1402  CG  TYR A 168      47.038   4.593   7.224  1.00  7.93           C
ATOM   1403  CD1 TYR A 168      46.633   4.237   5.939  1.00  9.47           C
ATOM   1404  CD2 TYR A 168      46.480   5.731   7.801  1.00  8.74           C
ATOM   1405  CE1 TYR A 168      45.697   5.006   5.248  1.00  9.37           C
ATOM   1406  CE2 TYR A 168      45.551   6.502   7.120  1.00  8.67           C
ATOM   1407  CZ  TYR A 168      45.166   6.135   5.846  1.00  8.72           C
ATOM   1408  OH  TYR A 168      44.244   6.882   5.144  1.00 10.56           O
ATOM   1409  N   LEU A 169      47.054   0.953   7.130  1.00  7.88           N
ATOM   1410  CA  LEU A 169      46.233   0.166   6.227  1.00  7.98           C
ATOM   1411  C   LEU A 169      45.481  -0.942   6.955  1.00  8.38           C
ATOM   1412  O   LEU A 169      44.349  -1.261   6.596  1.00  7.85           O
ATOM   1413  CB  LEU A 169      47.074  -0.395   5.079  1.00  9.50           C
ATOM   1414  CG  LEU A 169      47.625   0.656   4.114  1.00  7.99           C
ATOM   1415  CD1 LEU A 169      48.572  -0.021   3.126  1.00  9.67           C
ATOM   1416  CD2 LEU A 169      46.500   1.369   3.369  1.00 10.38           C
ATOM   1417  N   PHE A 170      46.101  -1.524   7.978  1.00  8.05           N
ATOM   1418  CA  PHE A 170      45.420  -2.517   8.800  1.00  6.99           C
ATOM   1419  C   PHE A 170      44.215  -1.894   9.502  1.00  7.45           C
ATOM   1420  O   PHE A 170      43.135  -2.483   9.571  1.00  8.31           O
ATOM   1421  CB  PHE A 170      46.400  -3.077   9.839  1.00  7.70           C
ATOM   1422  CG  PHE A 170      45.823  -4.167  10.696  1.00  7.86           C
ATOM   1423  CD1 PHE A 170      45.865  -5.490  10.280  1.00 10.10           C
ATOM   1424  CD2 PHE A 170      45.240  -3.869  11.922  1.00  8.47           C
ATOM   1425  CE1 PHE A 170      45.323  -6.503  11.076  1.00 11.72           C
ATOM   1426  CE2 PHE A 170      44.702  -4.869  12.723  1.00 11.48           C
ATOM   1427  CZ  PHE A 170      44.745  -6.193  12.298  1.00 10.46           C
ATOM   1428  N   ASP A 171      44.415  -0.694  10.038  1.00  7.56           N
ATOM   1429  CA  ASP A 171      43.334   0.072  10.639  1.00  9.16           C
ATOM   1430  C   ASP A 171      42.132   0.195   9.685  1.00  7.81           C
ATOM   1431  O   ASP A 171      40.982   0.043  10.099  1.00 10.47           O
ATOM   1432  CB  ASP A 171      43.870   1.449  11.058  1.00  7.96           C
ATOM   1433  CG  ASP A 171      42.797   2.351  11.626  1.00  9.93           C
ATOM   1434  OD1 ASP A 171      42.645   2.389  12.868  1.00  9.82           O
ATOM   1435  OD2 ASP A 171      42.108   3.028  10.832  1.00  9.73           O
ATOM   1436  N   LYS A 172      42.394   0.452   8.404  1.00  8.56           N
ATOM   1437  CA  LYS A 172      41.304   0.629   7.436  1.00  7.84           C
ATOM   1438  C   LYS A 172      40.676  -0.689   6.988  1.00  8.29           C
ATOM   1439  O   LYS A 172      39.453  -0.819   6.922  1.00 14.04           O
ATOM   1440  CB  LYS A 172      41.794   1.381   6.195  1.00  8.21           C
ATOM   1441  CG  LYS A 172      42.522   2.681   6.492  1.00  9.24           C
ATOM   1442  CD  LYS A 172      41.644   3.697   7.207  1.00 11.43           C
ATOM   1443  CE  LYS A 172      42.503   4.837   7.789  1.00 11.73           C
ATOM   1444  NZ  LYS A 172      43.503   4.331   8.826  1.00 10.30           N
ATOM   1445  N   HIS A 173      41.516  -1.664   6.661  1.00  8.38           N
ATOM   1446  CA  HIS A 173      41.023  -2.892   6.032  1.00  8.80           C
ATOM   1447  C   HIS A 173      40.532  -3.978   6.978  1.00 11.19           C
ATOM   1448  O   HIS A 173      39.546  -4.657   6.682  1.00 16.72           O
ATOM   1449  CB  HIS A 173      42.102  -3.494   5.138  1.00  8.06           C
ATOM   1450  CG  HIS A 173      42.330  -2.738   3.868  1.00  9.31           C
ATOM   1451  ND1 HIS A 173      41.407  -2.709   2.843  1.00 16.50           N
ATOM   1452  CD2 HIS A 173      43.387  -2.003   3.446  1.00 10.65           C
ATOM   1453  CE1 HIS A 173      41.884  -1.980   1.847  1.00 12.94           C
ATOM   1454  NE2 HIS A 173      43.084  -1.542   2.187  1.00 13.19           N
ATOM   1455  N   THR A 174      41.241  -4.185   8.079  1.00  8.97           N
ATOM   1456  CA  THR A 174      40.842  -5.216   9.033  1.00  8.94           C
ATOM   1457  C   THR A 174      39.908  -4.676  10.110  1.00 10.05           C
ATOM   1458  O   THR A 174      38.908  -5.312  10.440  1.00 11.69           O
ATOM   1459  CB  THR A 174      42.062  -5.889   9.669  1.00  9.89           C
ATOM   1460  OG1 THR A 174      42.810  -6.568   8.649  1.00 12.76           O
ATOM   1461  CG2 THR A 174      41.621  -6.904  10.711  1.00  9.56           C
ATOM   1462  N   LEU A 175      40.212  -3.494  10.644  1.00  9.18           N
ATOM   1463  CA  LEU A 175      39.415  -2.970  11.751  1.00  9.28           C
ATOM   1464  C   LEU A 175      38.327  -1.994  11.324  1.00 12.15           C
ATOM   1465  O   LEU A 175      37.497  -1.588  12.141  1.00 14.75           O
ATOM   1466  CB  LEU A 175      40.313  -2.300  12.792  1.00  7.92           C
ATOM   1467  CG  LEU A 175      41.408  -3.192  13.379  1.00  7.72           C
ATOM   1468  CD1 LEU A 175      42.227  -2.425  14.423  1.00  9.20           C
ATOM   1469  CD2 LEU A 175      40.818  -4.462  13.988  1.00  9.55           C
ATOM   1470  N   GLY A 176      38.326  -1.621  10.050  1.00 13.28           N
ATOM   1471  CA  GLY A 176      37.382  -0.632   9.557  1.00 15.47           C
ATOM   1472  C   GLY A 176      36.057  -1.243   9.144  1.00 32.64           C
ATOM   1473  O   GLY A 176      35.954  -2.458   8.971  1.00 33.43           O
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: April 25th, 2023.