CNRS Nantes University UFIP UFIP
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***  ssb1ue1  ***

elNémo ID: 210709094723144507

Job options:

ID        	=	 210709094723144507
JOBID     	=	 ssb1ue1
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 ssb1ue1

HEADER    DNA BINDING PROTEIN                     08-MAY-03   1UE1              
TITLE     CRYSTAL STRUCTURE OF THE SINGLE-STRANDED DNA-BINDING                  
TITLE    2 PROTEIN FROM MYCOBACTERIUM TUBERCULOSIS                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SINGLE-STRAND BINDING PROTEIN;                             
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: SINGLE-STRANDED DNA-BINDING PROTEIN;                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;                     
SOURCE   3 ORGANISM_TAXID: 1773;                                                
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   7 EXPRESSION_SYSTEM_PLASMID: PET11D                                    
KEYWDS    OLIGONUCLEOTIDE BINDING FOLD, DNA-BINDING PROTEIN,                    
KEYWDS   2 STRUCTURAL GENOMICS, PSI, PROTEIN STRUCTURE INITIATIVE, TB           
KEYWDS   3 STRUCTURAL GENOMICS CONSORTIUM, TBSGC, DNA BINDING PROTEIN           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.SAIKRISHNAN,J.JEYAKANTHAN,J.VENKATESH,N.ACHARYA,K.SEKAR,            
AUTHOR   2 U.VARSHNEY,M.VIJAYAN,TB STRUCTURAL GENOMICS CONSORTIUM               
AUTHOR   3 (TBSGC)                                                              
REVDAT   3   24-FEB-09 1UE1    1       VERSN                                    
REVDAT   2   01-FEB-05 1UE1    1       AUTHOR KEYWDS REMARK                     
REVDAT   1   10-FEB-04 1UE1    0                                                
JRNL        AUTH   K.SAIKRISHNAN,J.JEYAKANTHAN,J.VENKATESH,N.ACHARYA,           
JRNL        AUTH 2 K.SEKAR,U.VARSHNEY,M.VIJAYAN                                 
JRNL        TITL   STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS                      
JRNL        TITL 2 SINGLE-STRANDED DNA-BINDING PROTEIN. VARIABILITY             
JRNL        TITL 3 IN QUATERNARY STRUCTURE AND ITS IMPLICATIONS                 
JRNL        REF    J.MOL.BIOL.                   V. 331   385 2003              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   12888346                                                     
JRNL        DOI    10.1016/S0022-2836(03)00729-0                                
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   K.SAIKRISHNAN,J.JEYAKANTHAN,J.VENKATESH,N.ACHARYA,           
REMARK   1  AUTH 2 K.PURNAPATRE,K.SEKAR,U.VARSHNEY,M.VIJAYAN                    
REMARK   1  TITL   CRYSTALLIZATION AND PRELIMINARY X-RAY STUDIES OF             
REMARK   1  TITL 2 THE SINGLE-STRANDED DNA-BINDING PROTEIN FROM                 
REMARK   1  TITL 3 MYCOBACTERIUM TUBERCULOSIS.                                  
REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.D      V.  58   327 2002              
REMARK   1  REFN                   ISSN 0907-4449                               
REMARK   1  PMID   11807266                                                     
REMARK   1  DOI    10.1107/S090744490102008X                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 15.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 173687.490                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 92.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 8844                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.228                           
REMARK   3   FREE R VALUE                     : 0.288                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.500                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 931                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.009                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.54                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 96                           
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4490                       
REMARK   3   BIN FREE R VALUE                    : 0.3970                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 11.90                        
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.110                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1725                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 1                                       
REMARK   3   SOLVENT ATOMS            : 212                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 44.10                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 67.00                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -7.66000                                             
REMARK   3    B22 (A**2) : -7.66000                                             
REMARK   3    B33 (A**2) : 15.32000                                             
REMARK   3    B12 (A**2) : -6.35000                                             
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.36                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.37                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 15.00                           
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.50                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.56                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.70                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 26.50                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.92                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 7.210 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 10.140; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 9.820 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 12.320; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.30                                                 
REMARK   3   BSOL        : 65.94                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: A LARGE NUMBER OF THE ISOLATED WATER      
REMARK   3  MOLECULES REPRESENT THE DISCREET AND ISOLATED ELECTRON              
REMARK   3  DENSITIES, WHICH MAY CORRESPOND TO THE UNDEFINED REGIONS OF         
REMARK   3  THE POLYPEPTIDE CHAIN PRIMARILY AT THE C-TERMINUS AND THE LOOPS     
REMARK   4                                                                      
REMARK   4 1UE1 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 14-MAY-03.                  
REMARK 100 THE RCSB ID CODE IS RCSB005717.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 05-APR-02                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.4                                
REMARK 200  NUMBER OF CRYSTALS USED        : 2                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU200                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : OSMIC MIRROR                       
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 9456                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
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     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.08100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.54                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR                          
REMARK 200 SOFTWARE USED: MLPHARE                                               
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.27                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1M SODIUM ACETATE, 500MM SODIUN          
REMARK 280  CHLORIDE, 50MM ZINC SULFATE, 20MM TRIS-HCL, PH 7.4, VAPOR           
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 298K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
REMARK 290       6555   -X,-X+Y,-Z+1/3                                          
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       25.72000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       51.44000            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       51.44000            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       25.72000            
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: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000      136.34704            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       51.44000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     ARG A    42                                                      
REMARK 465     GLN A    43                                                      
REMARK 465     THR A    44                                                      
REMARK 465     GLY A    45                                                      
REMARK 465     GLU A    46                                                      
REMARK 465     SER A   121                                                      
REMARK 465     ARG A   122                                                      
REMARK 465     SER A   123                                                      
REMARK 465     GLY A   124                                                      
REMARK 465     GLY A   125                                                      
REMARK 465     PHE A   126                                                      
REMARK 465     GLY A   127                                                      
REMARK 465     SER A   128                                                      
REMARK 465     GLY A   129                                                      
REMARK 465     SER A   130                                                      
REMARK 465     ARG A   131                                                      
REMARK 465     PRO A   132                                                      
REMARK 465     ALA A   133                                                      
REMARK 465     PRO A   134                                                      
REMARK 465     ALA A   135                                                      
REMARK 465     GLN A   136                                                      
REMARK 465     THR A   137                                                      
REMARK 465     SER A   138                                                      
REMARK 465     SER A   139                                                      
REMARK 465     ALA A   140                                                      
REMARK 465     SER A   141                                                      
REMARK 465     GLY A   142                                                      
REMARK 465     ASP A   143                                                      
REMARK 465     ASP A   144                                                      
REMARK 465     PRO A   145                                                      
REMARK 465     TRP A   146                                                      
REMARK 465     GLY A   147                                                      
REMARK 465     SER A   148                                                      
REMARK 465     ALA A   149                                                      
REMARK 465     PRO A   150                                                      
REMARK 465     ALA A   151                                                      
REMARK 465     SER A   152                                                      
REMARK 465     GLY A   153                                                      
REMARK 465     SER A   154                                                      
REMARK 465     PHE A   155                                                      
REMARK 465     GLY A   156                                                      
REMARK 465     GLY A   157                                                      
REMARK 465     GLY A   158                                                      
REMARK 465     ASP A   159                                                      
REMARK 465     ASP A   160                                                      
REMARK 465     GLU A   161                                                      
REMARK 465     PRO A   162                                                      
REMARK 465     PRO A   163                                                      
REMARK 465     PHE A   164                                                      
REMARK 465     MET B     1                                                      
REMARK 465     GLU B    92                                                      
REMARK 465     GLY B    93                                                      
REMARK 465     GLU B    94                                                      
REMARK 465     GLY B   124                                                      
REMARK 465     GLY B   125                                                      
REMARK 465     PHE B   126                                                      
REMARK 465     GLY B   127                                                      
REMARK 465     SER B   128                                                      
REMARK 465     GLY B   129                                                      
REMARK 465     SER B   130                                                      
REMARK 465     ARG B   131                                                      
REMARK 465     PRO B   132                                                      
REMARK 465     ALA B   133                                                      
REMARK 465     PRO B   134                                                      
REMARK 465     ALA B   135                                                      
REMARK 465     GLN B   136                                                      
REMARK 465     THR B   137                                                      
REMARK 465     SER B   138                                                      
REMARK 465     SER B   139                                                      
REMARK 465     ALA B   140                                                      
REMARK 465     SER B   141                                                      
REMARK 465     GLY B   142                                                      
REMARK 465     ASP B   143                                                      
REMARK 465     ASP B   144                                                      
REMARK 465     PRO B   145                                                      
REMARK 465     TRP B   146                                                      
REMARK 465     GLY B   147                                                      
REMARK 465     SER B   148                                                      
REMARK 465     ALA B   149                                                      
REMARK 465     PRO B   150                                                      
REMARK 465     ALA B   151                                                      
REMARK 465     SER B   152                                                      
REMARK 465     GLY B   153                                                      
REMARK 465     SER B   154                                                      
REMARK 465     PHE B   155                                                      
REMARK 465     GLY B   156                                                      
REMARK 465     GLY B   157                                                      
REMARK 465     GLY B   158                                                      
REMARK 465     ASP B   159                                                      
REMARK 465     ASP B   160                                                      
REMARK 465     GLU B   161                                                      
REMARK 465     PRO B   162                                                      
REMARK 465     PRO B   163                                                      
REMARK 465     PHE B   164                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;            
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ILE A  39    CG1  CG2  CD1                                       
REMARK 470     TYR A  40    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     TRP A  47    CB   CG   CD1  CD2  NE1  CE2  CE3                   
REMARK 470     TRP A  47    CZ2  CZ3  CH2                                       
REMARK 470     GLU A  51    CG   CD   OE1  OE2                                  
REMARK 470     PHE A  88    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLU A  89    CG   CD   OE1  OE2                                  
REMARK 470     GLU A  94    CG   CD   OE1  OE2                                  
REMARK 470     ASN A 118    CG   OD1  ND2                                       
REMARK 470     ILE B  39    CG1  CG2  CD1                                       
REMARK 470     THR B  44    OG1  CG2                                            
REMARK 470     LYS B  48    CB   CG   CD   CE   NZ                              
REMARK 470     GLU B  51    CB   CG   CD   OE1  OE2                             
REMARK 470     LYS B  95    CG   CD   CE   NZ                                   
REMARK 470     ARG B  96    CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 470     THR B  97    OG1  CG2                                            
REMARK 470     LYS B 116    CG   CD   CE   NZ                                   
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     TRP A   60   CZ2                                                 
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    PRO A  37     -167.76    -54.98                                   
REMARK 500    LYS A  48      179.44    -33.88                                   
REMARK 500    ASP A  49      138.23     76.74                                   
REMARK 500    GLU A  51     -121.27     39.60                                   
REMARK 500    ALA A  52      138.08    111.33                                   
REMARK 500    ARG A  61     -149.30     59.63                                   
REMARK 500    GLU A  89     -170.02     12.39                                   
REMARK 500    THR A  90      -25.78    158.60                                   
REMARK 500    ARG A  91       59.55    -95.47                                   
REMARK 500    GLU A  92      -24.39    170.30                                   
REMARK 500    GLU A  94      102.78   -177.02                                   
REMARK 500    LYS A  95      109.11     53.43                                   
REMARK 500    LEU A 110       38.07    -99.58                                   
REMARK 500    ALA A 113     -178.24   -175.66                                   
REMARK 500    LYS A 119     -162.22    -64.18                                   
REMARK 500    ASP B  41       97.55    -69.36                                   
REMARK 500    ARG B  42        1.79    -49.43                                   
REMARK 500    THR B  44      172.90     76.34                                   
REMARK 500    GLU B  46     -136.42   -125.86                                   
REMARK 500    ARG B  61     -136.64     56.14                                   
REMARK 500    THR B  90     -158.58    -36.51                                   
REMARK 500    ARG B  96      107.17    172.64                                   
REMARK 500    ALA B 113      163.82    179.75                                   
REMARK 500    ALA B 115      140.24   -170.49                                   
REMARK 500    ALA B 120     -122.16    -91.34                                   
REMARK 500    SER B 121      112.60   -162.92                                   
REMARK 500    ARG B 122      -85.59   -146.17                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH B 426        DISTANCE =  6.54 ANGSTROMS                       
REMARK 525    HOH B 428        DISTANCE =  5.17 ANGSTROMS                       
REMARK 525    HOH A 194        DISTANCE =  9.32 ANGSTROMS                       
REMARK 525    HOH A 199        DISTANCE =  6.14 ANGSTROMS                       
REMARK 525    HOH B 439        DISTANCE =  7.38 ANGSTROMS                       
REMARK 525    HOH A 204        DISTANCE = 14.60 ANGSTROMS                       
REMARK 525    HOH B 442        DISTANCE =  5.70 ANGSTROMS                       
REMARK 525    HOH A 207        DISTANCE =  6.26 ANGSTROMS                       
REMARK 525    HOH B 443        DISTANCE =  5.70 ANGSTROMS                       
REMARK 525    HOH A 208        DISTANCE =  5.84 ANGSTROMS                       
REMARK 525    HOH B 444        DISTANCE = 11.94 ANGSTROMS                       
REMARK 525    HOH A 209        DISTANCE =  5.87 ANGSTROMS                       
REMARK 525    HOH B 445        DISTANCE = 14.56 ANGSTROMS                       
REMARK 525    HOH B 446        DISTANCE = 13.53 ANGSTROMS                       
REMARK 525    HOH A 211        DISTANCE =  8.15 ANGSTROMS                       
REMARK 525    HOH B 447        DISTANCE = 15.37 ANGSTROMS                       
REMARK 525    HOH A 212        DISTANCE = 10.93 ANGSTROMS                       
REMARK 525    HOH B 448        DISTANCE = 10.25 ANGSTROMS                       
REMARK 525    HOH A 213        DISTANCE = 13.29 ANGSTROMS                       
REMARK 525    HOH B 450        DISTANCE =  8.00 ANGSTROMS                       
REMARK 525    HOH B 451        DISTANCE = 10.60 ANGSTROMS                       
REMARK 525    HOH B 452        DISTANCE =  8.18 ANGSTROMS                       
REMARK 525    HOH B 453        DISTANCE =  9.63 ANGSTROMS                       
REMARK 525    HOH A 220        DISTANCE =  7.93 ANGSTROMS                       
REMARK 525    HOH A 221        DISTANCE =  7.10 ANGSTROMS                       
REMARK 525    HOH B 457        DISTANCE =  6.63 ANGSTROMS                       
REMARK 525    HOH A 222        DISTANCE =  5.89 ANGSTROMS                       
REMARK 525    HOH B 458        DISTANCE = 16.53 ANGSTROMS                       
REMARK 525    HOH A 223        DISTANCE = 18.02 ANGSTROMS                       
REMARK 525    HOH B 459        DISTANCE = 11.66 ANGSTROMS                       
REMARK 525    HOH A 225        DISTANCE = 10.76 ANGSTROMS                       
REMARK 525    HOH A 226        DISTANCE =  7.77 ANGSTROMS                       
REMARK 525    HOH A 227        DISTANCE =  7.95 ANGSTROMS                       
REMARK 525    HOH B 463        DISTANCE =  6.25 ANGSTROMS                       
REMARK 525    HOH A 229        DISTANCE =  8.26 ANGSTROMS                       
REMARK 525    HOH B 466        DISTANCE =  8.41 ANGSTROMS                       
REMARK 525    HOH B 467        DISTANCE =  9.83 ANGSTROMS                       
REMARK 525    HOH A 232        DISTANCE =  8.21 ANGSTROMS                       
REMARK 525    HOH B 468        DISTANCE = 11.49 ANGSTROMS                       
REMARK 525    HOH B 469        DISTANCE =  9.88 ANGSTROMS                       
REMARK 525    HOH A 234        DISTANCE =  7.52 ANGSTROMS                       
REMARK 525    HOH A 235        DISTANCE =  8.25 ANGSTROMS                       
REMARK 525    HOH A 236        DISTANCE = 10.40 ANGSTROMS                       
REMARK 525    HOH A 239        DISTANCE = 11.39 ANGSTROMS                       
REMARK 525    HOH B 477        DISTANCE =  5.14 ANGSTROMS                       
REMARK 525    HOH B 480        DISTANCE =  7.85 ANGSTROMS                       
REMARK 525    HOH B 481        DISTANCE = 12.42 ANGSTROMS                       
REMARK 525    HOH B 482        DISTANCE = 11.00 ANGSTROMS                       
REMARK 525    HOH B 483        DISTANCE = 15.63 ANGSTROMS                       
REMARK 525    HOH B 484        DISTANCE = 13.94 ANGSTROMS                       
REMARK 525    HOH B 485        DISTANCE = 11.97 ANGSTROMS                       
REMARK 525    HOH B 486        DISTANCE = 12.39 ANGSTROMS                       
REMARK 525    HOH B 487        DISTANCE = 11.43 ANGSTROMS                       
REMARK 525    HOH B 489        DISTANCE = 11.71 ANGSTROMS                       
REMARK 525    HOH B 490        DISTANCE = 11.86 ANGSTROMS                       
REMARK 525    HOH B 491        DISTANCE = 11.40 ANGSTROMS                       
REMARK 525    HOH B 497        DISTANCE =  8.88 ANGSTROMS                       
REMARK 525    HOH B 498        DISTANCE = 15.24 ANGSTROMS                       
REMARK 525    HOH B 501        DISTANCE = 11.93 ANGSTROMS                       
REMARK 525    HOH B 504        DISTANCE =  5.31 ANGSTROMS                       
REMARK 525    HOH B 505        DISTANCE = 17.38 ANGSTROMS                       
REMARK 525    HOH B 506        DISTANCE = 21.96 ANGSTROMS                       
REMARK 525    HOH B 507        DISTANCE = 14.80 ANGSTROMS                       
REMARK 525    HOH B 508        DISTANCE = 14.83 ANGSTROMS                       
REMARK 525    HOH B 511        DISTANCE =  5.24 ANGSTROMS                       
REMARK 525    HOH B 512        DISTANCE = 14.25 ANGSTROMS                       
REMARK 525    HOH B 520        DISTANCE =  7.53 ANGSTROMS                       
REMARK 525    HOH B 521        DISTANCE = 11.61 ANGSTROMS                       
REMARK 525    HOH B 522        DISTANCE =  5.33 ANGSTROMS                       
REMARK 525    HOH B 523        DISTANCE = 12.68 ANGSTROMS                       
REMARK 525    HOH B 524        DISTANCE =  9.70 ANGSTROMS                       
REMARK 525    HOH B 525        DISTANCE = 10.31 ANGSTROMS                       
REMARK 525    HOH B 526        DISTANCE =  5.86 ANGSTROMS                       
REMARK 525    HOH B 530        DISTANCE =  5.49 ANGSTROMS                       
REMARK 525    HOH B 533        DISTANCE =  8.33 ANGSTROMS                       
REMARK 525    HOH B 534        DISTANCE = 17.56 ANGSTROMS                       
REMARK 525    HOH B 536        DISTANCE = 18.16 ANGSTROMS                       
REMARK 525    HOH B 537        DISTANCE = 13.55 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620  SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                            
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 400  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B  62   OE2                                                    
REMARK 620 2 GLU B  65   OE2  59.8                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 400                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1UE5   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN WITH CD                                             
REMARK 900 RELATED ID: 1UE6   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN WITHOUT LIGAND AT 2.7                               
REMARK 900 RELATED ID: 1UE7   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN WITHOUT LIGAND AT 3.2                               
REMARK 900 RELATED ID: RV0054   RELATED DB: TARGETDB                            
DBREF  1UE1 A    1   164  UNP    P0A610   SSB_MYCTU        1    164             
DBREF  1UE1 B    1   164  UNP    P0A610   SSB_MYCTU        1    164             
SEQRES   1 A  164  MET ALA GLY ASP THR THR ILE THR ILE VAL GLY ASN LEU          
SEQRES   2 A  164  THR ALA ASP PRO GLU LEU ARG PHE THR PRO SER GLY ALA          
SEQRES   3 A  164  ALA VAL ALA ASN PHE THR VAL ALA SER THR PRO ARG ILE          
SEQRES   4 A  164  TYR ASP ARG GLN THR GLY GLU TRP LYS ASP GLY GLU ALA          
SEQRES   5 A  164  LEU PHE LEU ARG CYS ASN ILE TRP ARG GLU ALA ALA GLU          
SEQRES   6 A  164  ASN VAL ALA GLU SER LEU THR ARG GLY ALA ARG VAL ILE          
SEQRES   7 A  164  VAL SER GLY ARG LEU LYS GLN ARG SER PHE GLU THR ARG          
SEQRES   8 A  164  GLU GLY GLU LYS ARG THR VAL ILE GLU VAL GLU VAL ASP          
SEQRES   9 A  164  GLU ILE GLY PRO SER LEU ARG TYR ALA THR ALA LYS VAL          
SEQRES  10 A  164  ASN LYS ALA SER ARG SER GLY GLY PHE GLY SER GLY SER          
SEQRES  11 A  164  ARG PRO ALA PRO ALA GLN THR SER SER ALA SER GLY ASP          
SEQRES  12 A  164  ASP PRO TRP GLY SER ALA PRO ALA SER GLY SER PHE GLY          
SEQRES  13 A  164  GLY GLY ASP ASP GLU PRO PRO PHE                              
SEQRES   1 B  164  MET ALA GLY ASP THR THR ILE THR ILE VAL GLY ASN LEU          
SEQRES   2 B  164  THR ALA ASP PRO GLU LEU ARG PHE THR PRO SER GLY ALA          
SEQRES   3 B  164  ALA VAL ALA ASN PHE THR VAL ALA SER THR PRO ARG ILE          
SEQRES   4 B  164  TYR ASP ARG GLN THR GLY GLU TRP LYS ASP GLY GLU ALA          
SEQRES   5 B  164  LEU PHE LEU ARG CYS ASN ILE TRP ARG GLU ALA ALA GLU          
SEQRES   6 B  164  ASN VAL ALA GLU SER LEU THR ARG GLY ALA ARG VAL ILE          
SEQRES   7 B  164  VAL SER GLY ARG LEU LYS GLN ARG SER PHE GLU THR ARG          
SEQRES   8 B  164  GLU GLY GLU LYS ARG THR VAL ILE GLU VAL GLU VAL ASP          
SEQRES   9 B  164  GLU ILE GLY PRO SER LEU ARG TYR ALA THR ALA LYS VAL          
SEQRES  10 B  164  ASN LYS ALA SER ARG SER GLY GLY PHE GLY SER GLY SER          
SEQRES  11 B  164  ARG PRO ALA PRO ALA GLN THR SER SER ALA SER GLY ASP          
SEQRES  12 B  164  ASP PRO TRP GLY SER ALA PRO ALA SER GLY SER PHE GLY          
SEQRES  13 B  164  GLY GLY ASP ASP GLU PRO PRO PHE                              
HET     ZN  B 400       1                                                       
HETNAM      ZN ZINC ION                                                         
FORMUL   3   ZN    ZN 2+                                                        
FORMUL   4  HOH   *212(H2 O)                                                    
HELIX    1   1 ARG A   61  LEU A   71  1                                  11    
HELIX    2   2 ARG B   61  LEU B   71  1                                  11    
SHEET    1   A 7 GLU A  18  PHE A  21  0                                        
SHEET    2   A 7 ALA A  27  SER A  35 -1  N  VAL A  28   O  ARG A  20           
SHEET    3   A 7 THR A   6  LEU A  13 -1  O  ASN A  12   N  ALA A  34           
SHEET    4   A 7 ARG A  76  PHE A  88 -1  N  VAL A  77   O  GLY A  11           
SHEET    5   A 7 ARG A  96  PRO A 108 -1  O  ARG A  96   N  PHE A  88           
SHEET    6   A 7 LEU A  53  TRP A  60  1  O  ARG A  56   N  VAL A 101           
SHEET    7   A 7 ALA A  27  SER A  35 -1  N  ALA A  29   O  ILE A  59           
SHEET    1   B 2 ALA A 113  LYS A 116  0                                        
SHEET    2   B 2 LYS B 116  LYS B 119 -1  O  LYS B 116   N  LYS A 116           
SHEET    1   C 7 GLU B  18  PHE B  21  0                                        
SHEET    2   C 7 ALA B  27  SER B  35 -1  O  VAL B  28   N  ARG B  20           
SHEET    3   C 7 THR B   6  LEU B  13 -1  O  ASN B  12   N  ALA B  34           
SHEET    4   C 7 ARG B  76  SER B  87 -1  N  VAL B  77   O  GLY B  11           
SHEET    5   C 7 THR B  97  PRO B 108 -1  O  VAL B  98   N  ARG B  86           
SHEET    6   C 7 LEU B  53  TRP B  60  1  O  ARG B  56   N  VAL B 101           
SHEET    7   C 7 ALA B  27  SER B  35 -1  N  ALA B  29   O  ILE B  59           
SHEET    1   D 2 ARG B  38  TYR B  40  0                                        
SHEET    2   D 2 TRP B  47  ASP B  49 -1  O  LYS B  48   N  ILE B  39           
LINK        ZN    ZN B 400                 OE2 GLU B  62     1555   1555  2.49  
LINK        ZN    ZN B 400                 OE2 GLU B  65     1555   1555  2.32  
SITE     1 AC1  4 ARG A  56  GLU A 100  GLU B  62  GLU B  65                    
CRYST1   78.720   78.720   77.160  90.00  90.00 120.00 P 31 2 1     12          
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      0.012703  0.007334  0.000000        0.00000                         
SCALE2      0.000000  0.014668  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012960        0.00000                         
ATOM      1  N   GLY A   3       6.474  80.373  27.313  1.00 75.84           N  
ATOM      2  CA  GLY A   3       5.095  80.834  27.653  1.00 64.04           C  
ATOM      3  C   GLY A   3       4.029  79.810  27.310  1.00 66.50           C  
ATOM      4  O   GLY A   3       3.254  79.391  28.171  1.00 67.99           O  
ATOM      5  N   ASP A   4       3.980  79.401  26.049  1.00 55.93           N  
ATOM      6  CA  ASP A   4       2.992  78.422  25.627  1.00 56.72           C  
ATOM      7  C   ASP A   4       3.363  77.023  26.083  1.00 62.48           C  
ATOM      8  O   ASP A   4       4.500  76.760  26.469  1.00 54.28           O  
ATOM      9  CB  ASP A   4       2.850  78.408  24.104  1.00 53.32           C  
ATOM     10  CG  ASP A   4       1.941  79.496  23.594  1.00 63.15           C  
ATOM     11  OD1 ASP A   4       0.765  79.531  24.012  1.00 64.08           O  
ATOM     12  OD2 ASP A   4       2.402  80.310  22.769  1.00 71.53           O  
ATOM     13  N   THR A   5       2.379  76.133  26.032  1.00 54.46           N  
ATOM     14  CA  THR A   5       2.567  74.746  26.392  1.00 31.01           C  
ATOM     15  C   THR A   5       2.708  73.959  25.087  1.00 43.32           C  
ATOM     16  O   THR A   5       1.805  73.948  24.247  1.00 31.45           O  
ATOM     17  CB  THR A   5       1.375  74.215  27.151  1.00 34.93           C  
ATOM     18  OG1 THR A   5       1.269  74.899  28.409  1.00 44.39           O  
ATOM     19  CG2 THR A   5       1.528  72.719  27.369  1.00 24.72           C  
ATOM     20  N   THR A   6       3.847  73.305  24.917  1.00 40.48           N  
ATOM     21  CA  THR A   6       4.086  72.548  23.709  1.00 41.64           C  
ATOM     22  C   THR A   6       4.130  71.061  23.981  1.00 43.40           C  
ATOM     23  O   THR A   6       4.328  70.630  25.116  1.00 45.52           O  
ATOM     24  CB  THR A   6       5.413  72.945  23.068  1.00 51.68           C  
ATOM     25  OG1 THR A   6       6.487  72.587  23.947  1.00 50.08           O  
ATOM     26  CG2 THR A   6       5.450  74.440  22.808  1.00 48.09           C  
ATOM     27  N   ILE A   7       3.938  70.282  22.920  1.00 41.71           N  
ATOM     28  CA  ILE A   7       3.974  68.838  23.018  1.00 31.03           C  
ATOM     29  C   ILE A   7       4.439  68.229  21.713  1.00 39.62           C  
ATOM     30  O   ILE A   7       4.469  68.886  20.673  1.00 49.77           O  
ATOM     31  CB  ILE A   7       2.599  68.245  23.316  1.00 43.48           C  
ATOM     32  CG1 ILE A   7       1.644  68.633  22.192  1.00 13.50           C  
ATOM     33  CG2 ILE A   7       2.110  68.677  24.711  1.00 35.71           C  
ATOM     34  CD1 ILE A   7       0.450  67.712  22.125  1.00 46.31           C  
ATOM     35  N   THR A   8       4.793  66.953  21.797  1.00 42.35           N  
ATOM     36  CA  THR A   8       5.242  66.158  20.670  1.00 30.36           C  
ATOM     37  C   THR A   8       4.368  64.930  20.675  1.00 30.51           C  
ATOM     38  O   THR A   8       4.301  64.221  21.671  1.00 41.47           O  
ATOM     39  CB  THR A   8       6.682  65.661  20.838  1.00 26.77           C  
ATOM     40  OG1 THR A   8       7.596  66.746  20.663  1.00 42.94           O  
ATOM     41  CG2 THR A   8       6.979  64.580  19.823  1.00 33.70           C  
ATOM     42  N   ILE A   9       3.681  64.678  19.578  1.00 33.07           N  
ATOM     43  CA  ILE A   9       2.860  63.492  19.530  1.00 35.90           C  
ATOM     44  C   ILE A   9       3.247  62.699  18.296  1.00 40.69           C  
ATOM     45  O   ILE A   9       3.369  63.255  17.200  1.00 33.62           O  
ATOM     46  CB  ILE A   9       1.335  63.830  19.523  1.00 27.30           C  
ATOM     47  CG1 ILE A   9       0.517  62.532  19.396  1.00 50.44           C  
ATOM     48  CG2 ILE A   9       1.006  64.794  18.397  1.00 43.29           C  
ATOM     49  CD1 ILE A   9      -1.002  62.642  19.758  1.00 16.99           C  
ATOM     50  N   VAL A  10       3.503  61.410  18.509  1.00 35.56           N  
ATOM     51  CA  VAL A  10       3.851  60.486  17.444  1.00 30.64           C  
ATOM     52  C   VAL A  10       2.619  59.616  17.296  1.00 36.55           C  
ATOM     53  O   VAL A  10       2.119  59.093  18.274  1.00 27.65           O  
ATOM     54  CB  VAL A  10       5.052  59.602  17.827  1.00 43.72           C  
ATOM     55  CG1 VAL A  10       5.148  58.403  16.891  1.00 32.12           C  
ATOM     56  CG2 VAL A  10       6.328  60.413  17.749  1.00 38.85           C  
ATOM     57  N   GLY A  11       2.118  59.480  16.076  1.00 39.45           N  
ATOM     58  CA  GLY A  11       0.932  58.673  15.866  1.00 39.09           C  
ATOM     59  C   GLY A  11       0.630  58.683  14.388  1.00 48.08           C  
ATOM     60  O   GLY A  11       1.389  59.267  13.617  1.00 45.10           O  
ATOM     61  N   ASN A  12      -0.470  58.060  13.985  1.00 37.46           N  
ATOM     62  CA  ASN A  12      -0.815  58.009  12.574  1.00 44.48           C  
ATOM     63  C   ASN A  12      -2.040  58.837  12.311  1.00 35.56           C  
ATOM     64  O   ASN A  12      -2.921  58.938  13.166  1.00 38.11           O  
ATOM     65  CB  ASN A  12      -1.079  56.569  12.125  1.00 51.88           C  
ATOM     66  CG  ASN A  12      -0.197  55.566  12.836  1.00 53.99           C  
ATOM     67  OD1 ASN A  12      -0.476  55.176  13.968  1.00 49.38           O  
ATOM     68  ND2 ASN A  12       0.881  55.156  12.183  1.00 54.46           N  
ATOM     69  N   LEU A  13      -2.091  59.438  11.128  1.00 37.35           N  
ATOM     70  CA  LEU A  13      -3.234  60.263  10.753  1.00 43.94           C  
ATOM     71  C   LEU A  13      -4.409  59.320  10.623  1.00 38.55           C  
ATOM     72  O   LEU A  13      -4.259  58.240  10.067  1.00 37.57           O  
ATOM     73  CB  LEU A  13      -2.986  60.964   9.416  1.00 27.29           C  
ATOM     74  CG  LEU A  13      -1.704  61.791   9.269  1.00 32.88           C  
ATOM     75  CD1 LEU A  13      -1.739  62.482   7.921  1.00 46.87           C  
ATOM     76  CD2 LEU A  13      -1.587  62.828  10.371  1.00 38.42           C  
ATOM     77  N   THR A  14      -5.565  59.715  11.149  1.00 43.18           N  
ATOM     78  CA  THR A  14      -6.749  58.869  11.080  1.00 42.10           C  
ATOM     79  C   THR A  14      -7.407  58.991   9.722  1.00 45.44           C  
ATOM     80  O   THR A  14      -8.324  58.242   9.402  1.00 54.59           O  
ATOM     81  CB  THR A  14      -7.799  59.254  12.139  1.00 36.62           C  
ATOM     82  OG1 THR A  14      -8.068  60.654  12.043  1.00 44.45           O  
ATOM     83  CG2 THR A  14      -7.316  58.923  13.535  1.00 46.29           C  
ATOM     84  N   ALA A  15      -6.943  59.944   8.924  1.00 49.29           N  
ATOM     85  CA  ALA A  15      -7.510  60.155   7.599  1.00 53.47           C  
ATOM     86  C   ALA A  15      -6.690  61.175   6.826  1.00 54.44           C  
ATOM     87  O   ALA A  15      -5.970  61.968   7.425  1.00 45.38           O  
ATOM     88  CB  ALA A  15      -8.945  60.632   7.729  1.00 44.60           C  
ATOM     89  N   ASP A  16      -6.797  61.157   5.501  1.00 55.11           N  
ATOM     90  CA  ASP A  16      -6.053  62.107   4.682  1.00 58.10           C  
ATOM     91  C   ASP A  16      -6.263  63.533   5.192  1.00 59.39           C  
ATOM     92  O   ASP A  16      -7.328  63.869   5.715  1.00 59.75           O  
ATOM     93  CB  ASP A  16      -6.508  62.050   3.221  1.00 67.26           C  
ATOM     94  CG  ASP A  16      -6.502  60.654   2.659  1.00 63.12           C  
ATOM     95  OD1 ASP A  16      -5.516  59.927   2.899  1.00 69.20           O  
ATOM     96  OD2 ASP A  16      -7.480  60.294   1.965  1.00 66.87           O  
ATOM     97  N   PRO A  17      -5.242  64.390   5.053  1.00 62.77           N  
ATOM     98  CA  PRO A  17      -5.340  65.784   5.501  1.00 64.00           C  
ATOM     99  C   PRO A  17      -6.301  66.619   4.643  1.00 65.08           C  
ATOM    100  O   PRO A  17      -6.143  66.707   3.423  1.00 74.62           O  
ATOM    101  CB  PRO A  17      -3.902  66.281   5.386  1.00 52.49           C  
ATOM    102  CG  PRO A  17      -3.104  65.053   5.623  1.00 49.42           C  
ATOM    103  CD  PRO A  17      -3.836  64.030   4.799  1.00 56.22           C  
ATOM    104  N   GLU A  18      -7.299  67.220   5.285  1.00 63.80           N  
ATOM    105  CA  GLU A  18      -8.265  68.070   4.597  1.00 52.13           C  
ATOM    106  C   GLU A  18      -7.575  69.373   4.228  1.00 54.14           C  
ATOM    107  O   GLU A  18      -7.278  70.173   5.107  1.00 66.67           O  
ATOM    108  CB  GLU A  18      -9.439  68.410   5.519  1.00 57.17           C  
ATOM    109  CG  GLU A  18     -10.611  67.441   5.525  1.00 56.10           C  
ATOM    110  CD  GLU A  18     -11.674  67.845   6.539  1.00 60.30           C  
ATOM    111  OE1 GLU A  18     -12.004  69.048   6.616  1.00 74.88           O  
ATOM    112  OE2 GLU A  18     -12.187  66.963   7.259  1.00 65.40           O  
ATOM    113  N   LEU A  19      -7.305  69.601   2.948  1.00 62.35           N  
ATOM    114  CA  LEU A  19      -6.671  70.860   2.574  1.00 68.48           C  
ATOM    115  C   LEU A  19      -7.679  71.828   1.992  1.00 77.34           C  
ATOM    116  O   LEU A  19      -8.047  71.732   0.820  1.00 82.93           O  
ATOM    117  CB  LEU A  19      -5.549  70.657   1.558  1.00 57.95           C  
ATOM    118  CG  LEU A  19      -5.041  71.992   0.993  1.00 53.37           C  
ATOM    119  CD1 LEU A  19      -4.654  72.936   2.137  1.00 40.14           C  
ATOM    120  CD2 LEU A  19      -3.852  71.752   0.072  1.00 52.98           C  
ATOM    121  N   ARG A  20      -8.122  72.764   2.821  1.00 80.16           N  
ATOM    122  CA  ARG A  20      -9.080  73.772   2.394  1.00 75.83           C  
ATOM    123  C   ARG A  20      -8.407  75.137   2.390  1.00 70.36           C  
ATOM    124  O   ARG A  20      -7.360  75.323   3.014  1.00 72.20           O  
ATOM    125  CB  ARG A  20     -10.299  73.772   3.326  1.00 71.07           C  
ATOM    126  CG  ARG A  20     -11.392  72.778   2.923  1.00 81.60           C  
ATOM    127  CD  ARG A  20     -10.853  71.361   2.742  1.00 81.10           C  
ATOM    128  NE  ARG A  20     -11.895  70.421   2.331  1.00 74.09           N  
ATOM    129  CZ  ARG A  20     -11.681  69.135   2.062  1.00 72.02           C  
ATOM    130  NH1 ARG A  20     -12.688  68.357   1.694  1.00 78.84           N  
ATOM    131  NH2 ARG A  20     -10.461  68.623   2.159  1.00 71.08           N  
ATOM    132  N   PHE A  21      -8.999  76.085   1.671  1.00 67.09           N  
ATOM    133  CA  PHE A  21      -8.445  77.425   1.604  1.00 66.96           C  
ATOM    134  C   PHE A  21      -9.382  78.455   2.198  1.00 78.00           C  
ATOM    135  O   PHE A  21     -10.593  78.249   2.256  1.00 79.30           O  
ATOM    136  CB  PHE A  21      -8.134  77.807   0.163  1.00 50.64           C  
ATOM    137  CG  PHE A  21      -6.998  77.037  -0.431  1.00 64.43           C  
ATOM    138  CD1 PHE A  21      -7.167  75.717  -0.828  1.00 63.77           C  
ATOM    139  CD2 PHE A  21      -5.753  77.634  -0.601  1.00 73.87           C  
ATOM    140  CE1 PHE A  21      -6.113  75.001  -1.387  1.00 73.00           C  
ATOM    141  CE2 PHE A  21      -4.691  76.926  -1.158  1.00 77.68           C  
ATOM    142  CZ  PHE A  21      -4.872  75.609  -1.554  1.00 69.63           C  
ATOM    143  N   THR A  22      -8.800  79.563   2.648  1.00 93.43           N  
ATOM    144  CA  THR A  22      -9.559  80.659   3.229  1.00114.06           C  
ATOM    145  C   THR A  22      -9.808  81.676   2.119  1.00119.38           C  
ATOM    146  O   THR A  22      -9.114  81.673   1.101  1.00112.28           O  
ATOM    147  CB  THR A  22      -8.776  81.337   4.377  1.00122.49           C  
ATOM    148  OG1 THR A  22      -7.548  81.872   3.870  1.00125.20           O  
ATOM    149  CG2 THR A  22      -8.471  80.334   5.479  1.00127.36           C  
ATOM    150  N   PRO A  23     -10.799  82.563   2.301  1.00125.77           N  
ATOM    151  CA  PRO A  23     -11.094  83.565   1.274  1.00126.52           C  
ATOM    152  C   PRO A  23      -9.851  84.339   0.846  1.00121.52           C  
ATOM    153  O   PRO A  23      -9.644  84.597  -0.341  1.00117.02           O  
ATOM    154  CB  PRO A  23     -12.133  84.455   1.953  1.00134.07           C  
ATOM    155  CG  PRO A  23     -11.755  84.362   3.402  1.00136.79           C  
ATOM    156  CD  PRO A  23     -11.505  82.882   3.554  1.00130.57           C  
ATOM    157  N   SER A  24      -9.026  84.697   1.824  1.00116.72           N  
ATOM    158  CA  SER A  24      -7.803  85.440   1.563  1.00112.46           C  
ATOM    159  C   SER A  24      -6.806  84.647   0.714  1.00109.52           C  
ATOM    160  O   SER A  24      -5.830  85.207   0.210  1.00110.68           O  
ATOM    161  CB  SER A  24      -7.161  85.874   2.889  1.00106.86           C  
ATOM    162  OG  SER A  24      -7.095  84.804   3.816  1.00110.90           O  
ATOM    163  N   GLY A  25      -7.050  83.348   0.556  1.00106.00           N  
ATOM    164  CA  GLY A  25      -6.165  82.527  -0.255  1.00107.24           C  
ATOM    165  C   GLY A  25      -5.234  81.573   0.478  1.00105.82           C  
ATOM    166  O   GLY A  25      -4.861  80.531  -0.067  1.00 97.44           O  
ATOM    167  N   ALA A  26      -4.849  81.925   1.703  1.00101.08           N  
ATOM    168  CA  ALA A  26      -3.954  81.090   2.500  1.00 90.06           C  
ATOM    169  C   ALA A  26      -4.539  79.691   2.652  1.00 87.10           C  
ATOM    170  O   ALA A  26      -5.754  79.524   2.748  1.00 94.01           O  
ATOM    171  CB  ALA A  26      -3.729  81.721   3.870  1.00 76.58           C  
ATOM    172  N   ALA A  27      -3.668  78.689   2.671  1.00 86.44           N  
ATOM    173  CA  ALA A  27      -4.103  77.307   2.797  1.00 73.05           C  
ATOM    174  C   ALA A  27      -4.074  76.839   4.241  1.00 76.16           C  
ATOM    175  O   ALA A  27      -3.252  77.289   5.040  1.00 73.98           O  
ATOM    176  CB  ALA A  27      -3.224  76.413   1.949  1.00 78.84           C  
ATOM    177  N   VAL A  28      -4.978  75.925   4.567  1.00 70.35           N  
ATOM    178  CA  VAL A  28      -5.058  75.381   5.912  1.00 65.53           C  
ATOM    179  C   VAL A  28      -5.223  73.877   5.836  1.00 61.80           C  
ATOM    180  O   VAL A  28      -6.108  73.375   5.144  1.00 64.36           O  
ATOM    181  CB  VAL A  28      -6.270  75.921   6.687  1.00 72.89           C  
ATOM    182  CG1 VAL A  28      -6.007  75.835   8.180  1.00 58.82           C  
ATOM    183  CG2 VAL A  28      -6.580  77.331   6.256  1.00 80.91           C  
ATOM    184  N   ALA A  29      -4.370  73.159   6.550  1.00 57.72           N  
ATOM    185  CA  ALA A  29      -4.454  71.714   6.574  1.00 54.37           C  
ATOM    186  C   ALA A  29      -4.915  71.265   7.960  1.00 50.97           C  
ATOM    187  O   ALA A  29      -4.376  71.691   8.988  1.00 48.40           O  
ATOM    188  CB  ALA A  29      -3.107  71.108   6.234  1.00 38.73           C  
ATOM    189  N   ASN A  30      -5.943  70.426   7.971  1.00 50.50           N  
ATOM    190  CA  ASN A  30      -6.502  69.881   9.196  1.00 41.35           C  
ATOM    191  C   ASN A  30      -6.359  68.368   9.179  1.00 47.64           C  
ATOM    192  O   ASN A  30      -6.457  67.735   8.130  1.00 33.92           O  
ATOM    193  CB  ASN A  30      -7.982  70.240   9.324  1.00 40.99           C  
ATOM    194  CG  ASN A  30      -8.203  71.565  10.025  1.00 46.26           C  
ATOM    195  OD1 ASN A  30      -8.268  72.618   9.389  1.00 57.55           O  
ATOM    196  ND2 ASN A  30      -8.303  71.521  11.352  1.00 40.27           N  
ATOM    197  N   PHE A  31      -6.125  67.793  10.348  1.00 42.79           N  
ATOM    198  CA  PHE A  31      -5.969  66.356  10.469  1.00 39.61           C  
ATOM    199  C   PHE A  31      -5.833  66.015  11.938  1.00 39.08           C  
ATOM    200  O   PHE A  31      -5.382  66.835  12.744  1.00 32.83           O  
ATOM    201  CB  PHE A  31      -4.730  65.882   9.694  1.00 28.60           C  
ATOM    202  CG  PHE A  31      -3.447  66.564  10.108  1.00 35.81           C  
ATOM    203  CD1 PHE A  31      -2.851  67.506   9.290  1.00 41.40           C  
ATOM    204  CD2 PHE A  31      -2.831  66.252  11.322  1.00 45.69           C  
ATOM    205  CE1 PHE A  31      -1.656  68.133   9.671  1.00 32.32           C  
ATOM    206  CE2 PHE A  31      -1.643  66.869  11.714  1.00 18.88           C  
ATOM    207  CZ  PHE A  31      -1.055  67.810  10.886  1.00 49.89           C  
ATOM    208  N   THR A  32      -6.254  64.812  12.296  1.00 34.96           N  
ATOM    209  CA  THR A  32      -6.144  64.380  13.672  1.00 24.62           C  
ATOM    210  C   THR A  32      -5.174  63.212  13.753  1.00 32.08           C  
ATOM    211  O   THR A  32      -5.304  62.215  13.035  1.00 30.26           O  
ATOM    212  CB  THR A  32      -7.514  63.969  14.269  1.00 30.38           C  
ATOM    213  OG1 THR A  32      -8.051  62.862  13.551  1.00 54.42           O  
ATOM    214  CG2 THR A  32      -8.488  65.114  14.181  1.00 23.84           C  
ATOM    215  N   VAL A  33      -4.172  63.366  14.612  1.00 35.75           N  
ATOM    216  CA  VAL A  33      -3.175  62.332  14.823  1.00 31.64           C  
ATOM    217  C   VAL A  33      -3.691  61.420  15.936  1.00 43.71           C  
ATOM    218  O   VAL A  33      -4.186  61.891  16.966  1.00 44.05           O  
ATOM    219  CB  VAL A  33      -1.835  62.953  15.243  1.00 35.16           C  
ATOM    220  CG1 VAL A  33      -0.909  61.892  15.774  1.00 19.15           C  
ATOM    221  CG2 VAL A  33      -1.210  63.659  14.064  1.00 40.20           C  
ATOM    222  N   ALA A  34      -3.598  60.114  15.714  1.00 40.71           N  
ATOM    223  CA  ALA A  34      -4.053  59.138  16.695  1.00 27.55           C  
ATOM    224  C   ALA A  34      -2.847  58.389  17.222  1.00 26.18           C  
ATOM    225  O   ALA A  34      -2.282  57.538  16.537  1.00 33.56           O  
ATOM    226  CB  ALA A  34      -5.021  58.172  16.053  1.00 30.37           C  
ATOM    227  N   SER A  35      -2.444  58.695  18.445  1.00 34.44           N  
ATOM    228  CA  SER A  35      -1.277  58.037  19.010  1.00 44.39           C  
ATOM    229  C   SER A  35      -1.635  56.850  19.878  1.00 53.58           C  
ATOM    230  O   SER A  35      -2.365  56.991  20.856  1.00 65.04           O  
ATOM    231  CB  SER A  35      -0.467  59.036  19.825  1.00 38.60           C  
ATOM    232  OG  SER A  35       0.559  58.382  20.542  1.00 61.55           O  
ATOM    233  N   THR A  36      -1.108  55.680  19.525  1.00 70.20           N  
ATOM    234  CA  THR A  36      -1.377  54.462  20.284  1.00 78.85           C  
ATOM    235  C   THR A  36      -0.088  53.714  20.651  1.00 80.20           C  
ATOM    236  O   THR A  36       0.701  53.338  19.783  1.00 85.53           O  
ATOM    237  CB  THR A  36      -2.322  53.530  19.509  1.00 84.83           C  
ATOM    238  OG1 THR A  36      -3.474  54.271  19.091  1.00 87.44           O  
ATOM    239  CG2 THR A  36      -2.783  52.383  20.398  1.00 96.44           C  
ATOM    240  N   PRO A  37       0.127  53.501  21.963  1.00 80.78           N  
ATOM    241  CA  PRO A  37       1.215  52.847  22.708  1.00 88.95           C  
ATOM    242  C   PRO A  37       1.704  51.410  22.462  1.00 98.88           C  
ATOM    243  O   PRO A  37       1.371  50.751  21.474  1.00 94.15           O  
ATOM    244  CB  PRO A  37       0.776  53.032  24.158  1.00 86.79           C  
ATOM    245  CG  PRO A  37       0.086  54.342  24.113  1.00 80.72           C  
ATOM    246  CD  PRO A  37      -0.784  54.171  22.905  1.00 73.95           C  
ATOM    247  N   ARG A  38       2.512  50.957  23.420  1.00110.12           N  
ATOM    248  CA  ARG A  38       3.152  49.644  23.432  1.00115.61           C  
ATOM    249  C   ARG A  38       2.778  48.822  24.681  1.00126.16           C  
ATOM    250  O   ARG A  38       2.030  49.297  25.540  1.00125.33           O  
ATOM    251  CB  ARG A  38       4.669  49.855  23.371  1.00114.76           C  
ATOM    252  CG  ARG A  38       5.182  51.052  24.207  1.00103.67           C  
ATOM    253  CD  ARG A  38       5.163  50.757  25.704  1.00104.42           C  
ATOM    254  NE  ARG A  38       5.655  51.862  26.528  1.00107.20           N  
ATOM    255  CZ  ARG A  38       4.880  52.771  27.116  1.00112.45           C  
ATOM    256  NH1 ARG A  38       5.423  53.736  27.846  1.00115.71           N  
ATOM    257  NH2 ARG A  38       3.561  52.718  26.980  1.00102.25           N  
ATOM    258  N   ILE A  39       3.295  47.594  24.773  1.00134.09           N  
ATOM    259  CA  ILE A  39       3.023  46.719  25.922  1.00134.73           C  
ATOM    260  C   ILE A  39       4.155  45.720  26.204  1.00134.91           C  
ATOM    261  O   ILE A  39       5.274  45.893  25.720  1.00132.95           O  
ATOM    262  CB  ILE A  39       1.709  45.976  25.722  1.00134.87           C  
ATOM    263  N   TYR A  40       3.859  44.677  26.981  1.00135.74           N  
ATOM    264  CA  TYR A  40       4.870  43.680  27.339  1.00136.11           C  
ATOM    265  C   TYR A  40       4.370  42.232  27.453  1.00140.24           C  
ATOM    266  O   TYR A  40       3.167  41.976  27.493  1.00142.58           O  
ATOM    267  CB  TYR A  40       5.545  44.091  28.646  1.00129.32           C  
ATOM    268  N   ASP A  41       5.324  41.300  27.513  1.00144.32           N  
ATOM    269  CA  ASP A  41       5.071  39.858  27.624  1.00144.33           C  
ATOM    270  C   ASP A  41       4.048  39.288  26.645  1.00146.26           C  
ATOM    271  O   ASP A  41       3.081  38.646  27.110  1.00147.69           O  
ATOM    272  CB  ASP A  41       4.659  39.496  29.056  1.00144.37           C  
ATOM    273  CG  ASP A  41       5.837  39.465  30.013  1.00143.16           C  
ATOM    274  OD1 ASP A  41       6.482  40.517  30.204  1.00139.71           O  
ATOM    275  OD2 ASP A  41       6.118  38.385  30.574  1.00147.94           O  
ATOM    276  N   TRP A  47       2.389  40.592  23.284  1.00119.09           N  
ATOM    277  CA  TRP A  47       1.130  40.805  24.061  1.00129.23           C  
ATOM    278  C   TRP A  47       0.586  42.221  23.957  1.00137.04           C  
ATOM    279  O   TRP A  47      -0.515  42.514  24.414  1.00138.26           O  
ATOM    280  N   LYS A  48       1.366  43.076  23.296  1.00140.98           N  
ATOM    281  CA  LYS A  48       1.102  44.506  23.101  1.00146.05           C  
ATOM    282  C   LYS A  48      -0.272  45.165  22.926  1.00148.96           C  
ATOM    283  O   LYS A  48      -1.316  44.508  22.967  1.00150.52           O  
ATOM    284  CB  LYS A  48       2.053  45.015  21.995  1.00145.30           C  
ATOM    285  CG  LYS A  48       3.499  44.676  22.294  1.00141.29           C  
ATOM    286  CD  LYS A  48       4.272  44.383  21.033  1.00129.16           C  
ATOM    287  CE  LYS A  48       5.692  44.017  21.387  1.00125.82           C  
ATOM    288  NZ  LYS A  48       6.494  43.772  20.165  1.00126.87           N  
ATOM    289  N   ASP A  49      -0.219  46.496  22.777  1.00149.01           N  
ATOM    290  CA  ASP A  49      -1.348  47.431  22.585  1.00140.55           C  
ATOM    291  C   ASP A  49      -2.264  47.870  23.740  1.00134.06           C  
ATOM    292  O   ASP A  49      -2.672  47.079  24.602  1.00140.01           O  
ATOM    293  CB  ASP A  49      -2.214  46.993  21.401  1.00139.93           C  
ATOM    294  CG  ASP A  49      -1.540  47.273  20.075  1.00133.27           C  
ATOM    295  OD1 ASP A  49      -0.451  46.708  19.828  1.00128.65           O  
ATOM    296  OD2 ASP A  49      -2.086  48.069  19.286  1.00120.35           O  
ATOM    297  N   GLY A  50      -2.572  49.170  23.724  1.00123.97           N  
ATOM    298  CA  GLY A  50      -3.420  49.796  24.730  1.00116.91           C  
ATOM    299  C   GLY A  50      -3.546  51.313  24.574  1.00119.03           C  
ATOM    300  O   GLY A  50      -3.460  51.841  23.474  1.00122.49           O  
ATOM    301  N   GLU A  51      -3.765  52.004  25.693  1.00114.65           N  
ATOM    302  CA  GLU A  51      -3.917  53.466  25.760  1.00111.18           C  
ATOM    303  C   GLU A  51      -4.710  54.179  24.647  1.00104.91           C  
ATOM    304  O   GLU A  51      -5.895  53.888  24.458  1.00108.47           O  
ATOM    305  CB  GLU A  51      -2.537  54.112  25.910  1.00115.14           C  
ATOM    306  N   ALA A  52      -4.067  55.120  23.943  1.00 88.21           N  
ATOM    307  CA  ALA A  52      -4.680  55.882  22.837  1.00 71.47           C  
ATOM    308  C   ALA A  52      -4.913  57.361  23.123  1.00 64.85           C  
ATOM    309  O   ALA A  52      -5.350  57.747  24.209  1.00 77.25           O  
ATOM    310  CB  ALA A  52      -6.002  55.247  22.394  1.00 64.68           C  
ATOM    311  N   LEU A  53      -4.613  58.178  22.119  1.00 47.99           N  
ATOM    312  CA  LEU A  53      -4.758  59.628  22.189  1.00 48.94           C  
ATOM    313  C   LEU A  53      -5.001  60.203  20.786  1.00 46.18           C  
ATOM    314  O   LEU A  53      -4.208  59.995  19.865  1.00 45.62           O  
ATOM    315  CB  LEU A  53      -3.491  60.254  22.770  1.00 53.58           C  
ATOM    316  CG  LEU A  53      -3.651  61.627  23.414  1.00 43.36           C  
ATOM    317  CD1 LEU A  53      -4.305  61.436  24.773  1.00 50.36           C  
ATOM    318  CD2 LEU A  53      -2.302  62.297  23.571  1.00 41.21           C  
ATOM    319  N   PHE A  54      -6.101  60.925  20.627  1.00 45.36           N  
ATOM    320  CA  PHE A  54      -6.448  61.527  19.345  1.00 29.76           C  
ATOM    321  C   PHE A  54      -6.397  63.051  19.456  1.00 37.07           C  
ATOM    322  O   PHE A  54      -7.247  63.648  20.109  1.00 36.69           O  
ATOM    323  CB  PHE A  54      -7.872  61.132  18.926  1.00 34.05           C  
ATOM    324  CG  PHE A  54      -8.037  59.676  18.561  1.00 45.88           C  
ATOM    325  CD1 PHE A  54      -8.103  58.697  19.547  1.00 46.97           C  
ATOM    326  CD2 PHE A  54      -8.136  59.289  17.220  1.00 35.10           C  
ATOM    327  CE1 PHE A  54      -8.267  57.348  19.206  1.00 49.93           C  
ATOM    328  CE2 PHE A  54      -8.298  57.949  16.864  1.00 37.92           C  
ATOM    329  CZ  PHE A  54      -8.364  56.975  17.858  1.00 53.19           C  
ATOM    330  N   LEU A  55      -5.426  63.688  18.808  1.00 37.82           N  
ATOM    331  CA  LEU A  55      -5.341  65.139  18.861  1.00 28.39           C  
ATOM    332  C   LEU A  55      -5.562  65.861  17.529  1.00 41.70           C  
ATOM    333  O   LEU A  55      -4.817  65.681  16.566  1.00 41.48           O  
ATOM    334  CB  LEU A  55      -3.996  65.535  19.445  1.00 34.61           C  
ATOM    335  CG  LEU A  55      -3.847  65.092  20.895  1.00 33.24           C  
ATOM    336  CD1 LEU A  55      -2.498  65.527  21.427  1.00 24.26           C  
ATOM    337  CD2 LEU A  55      -4.992  65.708  21.713  1.00 28.85           C  
ATOM    338  N   ARG A  56      -6.588  66.697  17.484  1.00 34.06           N  
ATOM    339  CA  ARG A  56      -6.897  67.459  16.278  1.00 24.41           C  
ATOM    340  C   ARG A  56      -5.792  68.475  16.041  1.00 18.64           C  
ATOM    341  O   ARG A  56      -5.464  69.254  16.930  1.00 38.05           O  
ATOM    342  CB  ARG A  56      -8.233  68.192  16.448  1.00 15.81           C  
ATOM    343  CG  ARG A  56      -9.449  67.277  16.595  1.00 39.61           C  
ATOM    344  CD  ARG A  56     -10.635  68.019  17.213  1.00 46.38           C  
ATOM    345  NE  ARG A  56     -10.762  69.369  16.678  1.00 49.21           N  
ATOM    346  CZ  ARG A  56     -10.674  70.479  17.407  1.00 63.05           C  
ATOM    347  NH1 ARG A  56     -10.798  71.661  16.823  1.00 47.85           N  
ATOM    348  NH2 ARG A  56     -10.478  70.414  18.721  1.00 66.95           N  
ATOM    349  N   CYS A  57      -5.231  68.485  14.837  1.00 41.59           N  
ATOM    350  CA  CYS A  57      -4.151  69.421  14.506  1.00 35.23           C  
ATOM    351  C   CYS A  57      -4.475  70.296  13.304  1.00 40.49           C  
ATOM    352  O   CYS A  57      -5.357  69.982  12.505  1.00 35.49           O  
ATOM    353  CB  CYS A  57      -2.859  68.664  14.174  1.00 26.74           C  
ATOM    354  SG  CYS A  57      -2.255  67.504  15.436  1.00 44.88           S  
ATOM    355  N   ASN A  58      -3.752  71.403  13.189  1.00 31.72           N  
ATOM    356  CA  ASN A  58      -3.902  72.284  12.052  1.00 46.11           C  
ATOM    357  C   ASN A  58      -2.607  73.027  11.787  1.00 54.44           C  
ATOM    358  O   ASN A  58      -2.006  73.612  12.684  1.00 51.41           O  
ATOM    359  CB  ASN A  58      -5.057  73.276  12.234  1.00 46.50           C  
ATOM    360  CG  ASN A  58      -5.029  73.977  13.563  1.00 39.87           C  
ATOM    361  OD1 ASN A  58      -5.494  73.443  14.564  1.00 49.12           O  
ATOM    362  ND2 ASN A  58      -4.490  75.187  13.582  1.00 50.80           N  
ATOM    363  N   ILE A  59      -2.166  72.957  10.541  1.00 54.87           N  
ATOM    364  CA  ILE A  59      -0.956  73.629  10.106  1.00 46.97           C  
ATOM    365  C   ILE A  59      -1.510  74.602   9.083  1.00 46.90           C  
ATOM    366  O   ILE A  59      -2.619  74.394   8.594  1.00 37.46           O  
ATOM    367  CB  ILE A  59       0.026  72.636   9.425  1.00 39.06           C  
ATOM    368  CG1 ILE A  59       1.319  73.346   9.031  1.00 50.37           C  
ATOM    369  CG2 ILE A  59      -0.617  72.025   8.208  1.00 39.16           C  
ATOM    370  CD1 ILE A  59       2.107  73.871  10.204  1.00 64.97           C  
ATOM    371  N   TRP A  60      -0.768  75.664   8.781  1.00 50.72           N  
ATOM    372  CA  TRP A  60      -1.221  76.651   7.802  1.00 60.53           C  
ATOM    373  C   TRP A  60      -0.108  76.971   6.824  1.00 50.45           C  
ATOM    374  O   TRP A  60       0.985  76.432   6.920  1.00 59.39           O  
ATOM    375  CB  TRP A  60      -1.649  77.967   8.474  1.00 60.02           C  
ATOM    376  CG  TRP A  60      -2.820  77.891   9.415  1.00 55.34           C  
ATOM    377  CD1 TRP A  60      -2.841  77.325  10.657  1.00 60.16           C  
ATOM    378  CD2 TRP A  60      -4.122  78.451   9.208  1.00 59.40           C  
ATOM    379  NE1 TRP A  60      -4.074  77.505  11.242  1.00 56.43           N  
ATOM    380  CE2 TRP A  60      -4.879  78.194  10.376  1.00 47.75           C  
ATOM    381  CE3 TRP A  60      -4.722  79.151   8.157  1.00 59.13           C  
ATOM    382  CZ2 TRP A  60      -6.206  78.606  10.516  0.00 56.77           C  
ATOM    383  CZ3 TRP A  60      -6.047  79.562   8.299  1.00 64.96           C  
ATOM    384  CH2 TRP A  60      -6.770  79.289   9.472  1.00 54.30           C  
ATOM    385  N   ARG A  61      -0.405  77.863   5.886  1.00 53.40           N  
ATOM    386  CA  ARG A  61       0.558  78.304   4.889  1.00 48.98           C  
ATOM    387  C   ARG A  61       1.083  77.156   4.031  1.00 45.76           C  
ATOM    388  O   ARG A  61       0.377  76.182   3.789  1.00 54.85           O  
ATOM    389  CB  ARG A  61       1.726  79.017   5.578  1.00 64.16           C  
ATOM    390  CG  ARG A  61       1.323  80.107   6.587  1.00 96.57           C  
ATOM    391  CD  ARG A  61       0.452  81.203   5.965  1.00113.46           C  
ATOM    392  NE  ARG A  61       0.265  82.360   6.848  1.00123.63           N  
ATOM    393  CZ  ARG A  61      -0.314  82.321   8.047  1.00124.99           C  
ATOM    394  NH1 ARG A  61      -0.777  81.178   8.536  1.00121.68           N  
ATOM    395  NH2 ARG A  61      -0.432  83.433   8.760  1.00124.76           N  
ATOM    396  N   GLU A  62       2.325  77.273   3.572  1.00 55.62           N  
ATOM    397  CA  GLU A  62       2.931  76.246   2.726  1.00 62.89           C  
ATOM    398  C   GLU A  62       3.094  74.896   3.427  1.00 58.30           C  
ATOM    399  O   GLU A  62       3.008  73.845   2.790  1.00 47.67           O  
ATOM    400  CB  GLU A  62       4.292  76.716   2.193  1.00 67.03           C  
ATOM    401  CG  GLU A  62       4.249  77.572   0.917  1.00 82.00           C  
ATOM    402  CD  GLU A  62       3.858  79.024   1.163  1.00 97.36           C  
ATOM    403  OE1 GLU A  62       4.393  79.633   2.115  1.00 90.73           O  
ATOM    404  OE2 GLU A  62       3.030  79.563   0.393  1.00 98.23           O  
ATOM    405  N   ALA A  63       3.338  74.919   4.733  1.00 53.27           N  
ATOM    406  CA  ALA A  63       3.488  73.673   5.475  1.00 39.78           C  
ATOM    407  C   ALA A  63       2.184  72.891   5.362  1.00 34.98           C  
ATOM    408  O   ALA A  63       2.191  71.664   5.336  1.00 42.53           O  
ATOM    409  CB  ALA A  63       3.806  73.959   6.940  1.00 29.12           C  
ATOM    410  N   ALA A  64       1.068  73.613   5.276  1.00 36.58           N  
ATOM    411  CA  ALA A  64      -0.247  72.989   5.171  1.00 42.97           C  
ATOM    412  C   ALA A  64      -0.427  72.240   3.857  1.00 50.46           C  
ATOM    413  O   ALA A  64      -1.053  71.177   3.830  1.00 55.53           O  
ATOM    414  CB  ALA A  64      -1.351  74.041   5.336  1.00 37.01           C  
ATOM    415  N   GLU A  65       0.119  72.784   2.769  1.00 49.27           N  
ATOM    416  CA  GLU A  65      -0.003  72.127   1.470  1.00 51.67           C  
ATOM    417  C   GLU A  65       0.979  70.976   1.350  1.00 59.17           C  
ATOM    418  O   GLU A  65       0.685  69.952   0.720  1.00 59.65           O  
ATOM    419  CB  GLU A  65       0.227  73.124   0.342  1.00 49.67           C  
ATOM    420  CG  GLU A  65      -0.897  74.123   0.197  1.00 69.29           C  
ATOM    421  CD  GLU A  65      -0.683  75.061  -0.965  1.00 75.97           C  
ATOM    422  OE1 GLU A  65      -0.511  74.566  -2.097  1.00 80.11           O  
ATOM    423  OE2 GLU A  65      -0.689  76.291  -0.744  1.00 83.74           O  
ATOM    424  N   ASN A  66       2.151  71.143   1.955  1.00 51.64           N  
ATOM    425  CA  ASN A  66       3.146  70.086   1.924  1.00 48.12           C  
ATOM    426  C   ASN A  66       2.580  68.918   2.725  1.00 58.81           C  
ATOM    427  O   ASN A  66       2.661  67.767   2.290  1.00 58.56           O  
ATOM    428  CB  ASN A  66       4.458  70.577   2.515  1.00 54.94           C  
ATOM    429  CG  ASN A  66       4.979  71.802   1.806  1.00 55.26           C  
ATOM    430  OD1 ASN A  66       4.923  71.890   0.580  1.00 67.28           O  
ATOM    431  ND2 ASN A  66       5.495  72.754   2.569  1.00 63.11           N  
ATOM    432  N   VAL A  67       2.003  69.216   3.890  1.00 38.47           N  
ATOM    433  CA  VAL A  67       1.378  68.184   4.708  1.00 34.30           C  
ATOM    434  C   VAL A  67       0.329  67.515   3.818  1.00 36.71           C  
ATOM    435  O   VAL A  67       0.288  66.302   3.685  1.00 43.45           O  
ATOM    436  CB  VAL A  67       0.657  68.803   5.939  1.00 46.28           C  
ATOM    437  CG1 VAL A  67      -0.403  67.831   6.484  1.00 14.67           C  
ATOM    438  CG2 VAL A  67       1.682  69.166   7.017  1.00 34.61           C  
ATOM    439  N   ALA A  68      -0.504  68.343   3.201  1.00 42.76           N  
ATOM    440  CA  ALA A  68      -1.577  67.890   2.328  1.00 48.70           C  
ATOM    441  C   ALA A  68      -1.125  66.965   1.213  1.00 41.12           C  
ATOM    442  O   ALA A  68      -1.747  65.936   0.983  1.00 58.17           O  
ATOM    443  CB  ALA A  68      -2.303  69.097   1.730  1.00 44.86           C  
ATOM    444  N   GLU A  69      -0.045  67.322   0.526  1.00 48.51           N  
ATOM    445  CA  GLU A  69       0.449  66.503  -0.583  1.00 58.65           C  
ATOM    446  C   GLU A  69       1.481  65.429  -0.193  1.00 57.70           C  
ATOM    447  O   GLU A  69       1.940  64.669  -1.043  1.00 51.90           O  
ATOM    448  CB  GLU A  69       1.064  67.403  -1.662  1.00 58.14           C  
ATOM    449  CG  GLU A  69       1.225  66.717  -3.019  1.00 92.58           C  
ATOM    450  CD  GLU A  69       2.518  67.087  -3.731  1.00104.21           C  
ATOM    451  OE1 GLU A  69       3.582  66.546  -3.362  1.00115.70           O  
ATOM    452  OE2 GLU A  69       2.474  67.923  -4.658  1.00114.47           O  
ATOM    453  N   SER A  70       1.839  65.353   1.083  1.00 57.59           N  
ATOM    454  CA  SER A  70       2.839  64.386   1.508  1.00 34.87           C  
ATOM    455  C   SER A  70       2.306  63.358   2.492  1.00 42.59           C  
ATOM    456  O   SER A  70       2.986  62.386   2.799  1.00 36.49           O  
ATOM    457  CB  SER A  70       4.021  65.118   2.138  1.00 48.17           C  
ATOM    458  OG  SER A  70       4.358  66.282   1.402  1.00 47.37           O  
ATOM    459  N   LEU A  71       1.095  63.555   2.995  1.00 38.73           N  
ATOM    460  CA  LEU A  71       0.556  62.598   3.956  1.00 40.33           C  
ATOM    461  C   LEU A  71      -0.795  62.029   3.557  1.00 53.15           C  
ATOM    462  O   LEU A  71      -1.606  62.698   2.906  1.00 61.22           O  
ATOM    463  CB  LEU A  71       0.452  63.241   5.347  1.00 34.14           C  
ATOM    464  CG  LEU A  71       1.754  63.743   5.960  1.00 18.20           C  
ATOM    465  CD1 LEU A  71       1.475  64.385   7.285  1.00 40.86           C  
ATOM    466  CD2 LEU A  71       2.707  62.604   6.121  1.00 11.28           C  
ATOM    467  N   THR A  72      -1.020  60.778   3.949  1.00 53.27           N  
ATOM    468  CA  THR A  72      -2.268  60.083   3.668  1.00 50.06           C  
ATOM    469  C   THR A  72      -2.698  59.400   4.957  1.00 47.92           C  
ATOM    470  O   THR A  72      -2.073  59.576   6.001  1.00 52.97           O  
ATOM    471  CB  THR A  72      -2.092  59.018   2.562  1.00 54.07           C  
ATOM    472  OG1 THR A  72      -1.371  57.890   3.077  1.00 58.04           O  
ATOM    473  CG2 THR A  72      -1.316  59.602   1.390  1.00 61.48           C  
ATOM    474  N   ARG A  73      -3.763  58.621   4.882  1.00 42.64           N  
ATOM    475  CA  ARG A  73      -4.268  57.930   6.050  1.00 40.18           C  
ATOM    476  C   ARG A  73      -3.180  57.013   6.596  1.00 37.06           C  
ATOM    477  O   ARG A  73      -2.216  56.702   5.899  1.00 48.00           O  
ATOM    478  CB  ARG A  73      -5.513  57.133   5.661  1.00 52.31           C  
ATOM    479  CG  ARG A  73      -6.461  56.777   6.806  1.00 66.05           C  
ATOM    480  CD  ARG A  73      -7.800  56.319   6.239  1.00 46.74           C  
ATOM    481  NE  ARG A  73      -7.591  55.419   5.111  1.00 63.71           N  
ATOM    482  CZ  ARG A  73      -8.477  55.205   4.145  1.00 76.33           C  
ATOM    483  NH1 ARG A  73      -8.192  54.364   3.157  1.00 70.01           N  
ATOM    484  NH2 ARG A  73      -9.646  55.834   4.161  1.00 69.53           N  
ATOM    485  N   GLY A  74      -3.324  56.612   7.856  1.00 29.96           N  
ATOM    486  CA  GLY A  74      -2.362  55.722   8.487  1.00 23.74           C  
ATOM    487  C   GLY A  74      -0.942  56.230   8.667  1.00 36.06           C  
ATOM    488  O   GLY A  74      -0.186  55.672   9.457  1.00 47.93           O  
ATOM    489  N   ALA A  75      -0.567  57.287   7.959  1.00 26.13           N  
ATOM    490  CA  ALA A  75       0.787  57.811   8.065  1.00 29.34           C  
ATOM    491  C   ALA A  75       1.241  58.099   9.504  1.00 41.08           C  
ATOM    492  O   ALA A  75       0.556  58.784  10.281  1.00 37.86           O  
ATOM    493  CB  ALA A  75       0.918  59.065   7.219  1.00 13.73           C  
ATOM    494  N   ARG A  76       2.415  57.572   9.839  1.00 34.73           N  
ATOM    495  CA  ARG A  76       3.013  57.753  11.151  1.00 26.34           C  
ATOM    496  C   ARG A  76       3.797  59.054  11.130  1.00 39.38           C  
ATOM    497  O   ARG A  76       4.792  59.174  10.415  1.00 51.10           O  
ATOM    498  CB  ARG A  76       3.948  56.599  11.463  1.00 25.38           C  
ATOM    499  CG  ARG A  76       4.402  56.563  12.898  1.00 30.37           C  
ATOM    500  CD  ARG A  76       5.486  55.524  13.103  1.00 25.96           C  
ATOM    501  NE  ARG A  76       5.907  55.459  14.499  1.00 48.30           N  
ATOM    502  CZ  ARG A  76       5.130  55.046  15.498  1.00 40.39           C  
ATOM    503  NH1 ARG A  76       3.881  54.662  15.262  1.00 36.98           N  
ATOM    504  NH2 ARG A  76       5.608  54.998  16.733  1.00 34.16           N  
ATOM    505  N   VAL A  77       3.357  60.021  11.932  1.00 27.87           N  
ATOM    506  CA  VAL A  77       3.981  61.325  11.962  1.00 18.67           C  
ATOM    507  C   VAL A  77       4.552  61.756  13.306  1.00 26.58           C  
ATOM    508  O   VAL A  77       4.262  61.172  14.356  1.00 32.45           O  
ATOM    509  CB  VAL A  77       2.969  62.404  11.534  1.00 32.96           C  
ATOM    510  CG1 VAL A  77       2.615  62.271  10.052  1.00 16.67           C  
ATOM    511  CG2 VAL A  77       1.715  62.267  12.371  1.00 31.86           C  
ATOM    512  N   ILE A  78       5.391  62.780  13.242  1.00 29.86           N  
ATOM    513  CA  ILE A  78       5.974  63.376  14.423  1.00 32.84           C  
ATOM    514  C   ILE A  78       5.429  64.787  14.335  1.00 38.96           C  
ATOM    515  O   ILE A  78       5.532  65.435  13.289  1.00 40.24           O  
ATOM    516  CB  ILE A  78       7.505  63.440  14.383  1.00 43.92           C  
ATOM    517  CG1 ILE A  78       8.084  62.047  14.162  1.00 25.00           C  
ATOM    518  CG2 ILE A  78       8.029  64.001  15.717  1.00 31.86           C  
ATOM    519  CD1 ILE A  78       9.579  62.040  14.076  1.00 45.41           C  
ATOM    520  N   VAL A  79       4.833  65.247  15.427  1.00 46.04           N  
ATOM    521  CA  VAL A  79       4.229  66.564  15.462  1.00 43.02           C  
ATOM    522  C   VAL A  79       4.606  67.349  16.705  1.00 32.42           C  
ATOM    523  O   VAL A  79       4.420  66.886  17.833  1.00 37.78           O  
ATOM    524  CB  VAL A  79       2.675  66.452  15.389  1.00 35.70           C  
ATOM    525  CG1 VAL A  79       2.037  67.791  15.658  1.00 26.10           C  
ATOM    526  CG2 VAL A  79       2.255  65.946  14.021  1.00 20.54           C  
ATOM    527  N   SER A  80       5.152  68.536  16.479  1.00 37.59           N  
ATOM    528  CA  SER A  80       5.526  69.428  17.563  1.00 33.34           C  
ATOM    529  C   SER A  80       4.669  70.669  17.373  1.00 41.50           C  
ATOM    530  O   SER A  80       4.669  71.283  16.302  1.00 35.55           O  
ATOM    531  CB  SER A  80       7.004  69.801  17.485  1.00 35.47           C  
ATOM    532  OG  SER A  80       7.359  70.702  18.521  1.00 45.64           O  
ATOM    533  N   GLY A  81       3.916  71.027  18.405  1.00 32.91           N  
ATOM    534  CA  GLY A  81       3.075  72.196  18.286  1.00 27.00           C  
ATOM    535  C   GLY A  81       2.705  72.761  19.630  1.00 42.40           C  
ATOM    536  O   GLY A  81       3.374  72.503  20.635  1.00 44.60           O  
ATOM    537  N   ARG A  82       1.620  73.519  19.650  1.00 42.97           N  
ATOM    538  CA  ARG A  82       1.171  74.151  20.870  1.00 40.61           C  
ATOM    539  C   ARG A  82      -0.252  73.744  21.167  1.00 40.35           C  
ATOM    540  O   ARG A  82      -1.106  73.782  20.285  1.00 35.82           O  
ATOM    541  CB  ARG A  82       1.262  75.672  20.712  1.00 49.93           C  
ATOM    542  CG  ARG A  82       2.681  76.165  20.426  1.00 83.68           C  
ATOM    543  CD  ARG A  82       2.772  77.672  20.154  1.00 94.54           C  
ATOM    544  NE  ARG A  82       2.600  78.011  18.742  1.00100.77           N  
ATOM    545  CZ  ARG A  82       1.427  78.161  18.135  1.00100.84           C  
ATOM    546  NH1 ARG A  82       0.301  78.006  18.818  1.00102.60           N  
ATOM    547  NH2 ARG A  82       1.382  78.463  16.844  1.00 98.04           N  
ATOM    548  N   LEU A  83      -0.500  73.337  22.408  1.00 41.09           N  
ATOM    549  CA  LEU A  83      -1.842  72.952  22.816  1.00 37.85           C  
ATOM    550  C   LEU A  83      -2.674  74.210  22.939  1.00 40.01           C  
ATOM    551  O   LEU A  83      -2.230  75.207  23.508  1.00 43.08           O  
ATOM    552  CB  LEU A  83      -1.833  72.270  24.174  1.00 29.90           C  
ATOM    553  CG  LEU A  83      -1.424  70.814  24.256  1.00 40.22           C  
ATOM    554  CD1 LEU A  83      -1.570  70.364  25.712  1.00 35.59           C  
ATOM    555  CD2 LEU A  83      -2.299  69.977  23.341  1.00 29.43           C  
ATOM    556  N   LYS A  84      -3.880  74.166  22.400  1.00 33.95           N  
ATOM    557  CA  LYS A  84      -4.783  75.298  22.481  1.00 34.12           C  
ATOM    558  C   LYS A  84      -6.088  74.706  22.952  1.00 29.61           C  
ATOM    559  O   LYS A  84      -6.500  73.659  22.466  1.00 39.31           O  
ATOM    560  CB  LYS A  84      -4.949  75.960  21.109  1.00 38.24           C  
ATOM    561  CG  LYS A  84      -4.424  77.387  21.061  1.00 58.60           C  
ATOM    562  CD  LYS A  84      -3.035  77.508  21.701  1.00 53.87           C  
ATOM    563  CE  LYS A  84      -2.551  78.961  21.755  1.00 69.70           C  
ATOM    564  NZ  LYS A  84      -1.229  79.091  22.440  1.00 54.13           N  
ATOM    565  N   GLN A  85      -6.720  75.341  23.927  1.00 32.32           N  
ATOM    566  CA  GLN A  85      -7.979  74.819  24.413  1.00 47.84           C  
ATOM    567  C   GLN A  85      -9.009  75.929  24.561  1.00 53.53           C  
ATOM    568  O   GLN A  85      -8.681  77.053  24.943  1.00 55.78           O  
ATOM    569  CB  GLN A  85      -7.790  74.136  25.762  1.00 41.59           C  
ATOM    570  CG  GLN A  85      -7.901  75.100  26.905  1.00 34.77           C  
ATOM    571  CD  GLN A  85      -8.170  74.419  28.206  1.00 34.74           C  
ATOM    572  OE1 GLN A  85      -8.524  73.244  28.239  1.00 26.33           O  
ATOM    573  NE2 GLN A  85      -8.019  75.156  29.299  1.00 26.70           N  
ATOM    574  N   ARG A  86     -10.258  75.599  24.254  1.00 64.23           N  
ATOM    575  CA  ARG A  86     -11.359  76.543  24.369  1.00 76.62           C  
ATOM    576  C   ARG A  86     -12.423  75.956  25.301  1.00 82.02           C  
ATOM    577  O   ARG A  86     -12.584  74.736  25.373  1.00 88.30           O  
ATOM    578  CB  ARG A  86     -11.946  76.846  22.978  1.00 80.25           C  
ATOM    579  CG  ARG A  86     -11.392  78.128  22.350  1.00 80.68           C  
ATOM    580  CD  ARG A  86     -11.943  78.401  20.952  1.00 94.25           C  
ATOM    581  NE  ARG A  86     -11.821  79.809  20.568  1.00105.91           N  
ATOM    582  CZ  ARG A  86     -10.694  80.515  20.635  1.00117.54           C  
ATOM    583  NH1 ARG A  86      -9.574  79.952  21.069  1.00127.87           N  
ATOM    584  NH2 ARG A  86     -10.683  81.790  20.276  1.00122.80           N  
ATOM    585  N   SER A  87     -13.128  76.825  26.025  1.00 88.33           N  
ATOM    586  CA  SER A  87     -14.175  76.403  26.958  1.00 83.36           C  
ATOM    587  C   SER A  87     -15.515  76.956  26.499  1.00 78.47           C  
ATOM    588  O   SER A  87     -15.667  78.166  26.347  1.00 81.14           O  
ATOM    589  CB  SER A  87     -13.867  76.930  28.354  1.00 85.65           C  
ATOM    590  OG  SER A  87     -12.564  76.557  28.754  1.00 98.35           O  
ATOM    591  N   PHE A  88     -16.494  76.083  26.301  1.00 76.06           N  
ATOM    592  CA  PHE A  88     -17.792  76.543  25.830  1.00 80.37           C  
ATOM    593  C   PHE A  88     -18.969  76.477  26.801  1.00 86.97           C  
ATOM    594  O   PHE A  88     -18.837  76.152  27.983  1.00 81.26           O  
ATOM    595  CB  PHE A  88     -18.160  75.809  24.532  1.00 53.75           C  
ATOM    596  N   GLU A  89     -20.116  76.828  26.227  1.00100.07           N  
ATOM    597  CA  GLU A  89     -21.455  76.879  26.814  1.00108.67           C  
ATOM    598  C   GLU A  89     -21.782  76.787  28.306  1.00115.42           C  
ATOM    599  O   GLU A  89     -20.925  76.860  29.190  1.00111.05           O  
ATOM    600  CB  GLU A  89     -22.325  75.884  26.070  1.00103.96           C  
ATOM    601  N   THR A  90     -23.093  76.649  28.514  1.00124.08           N  
ATOM    602  CA  THR A  90     -23.808  76.526  29.786  1.00130.90           C  
ATOM    603  C   THR A  90     -25.246  76.945  29.446  1.00140.11           C  
ATOM    604  O   THR A  90     -26.204  76.528  30.099  1.00145.57           O  
ATOM    605  CB  THR A  90     -23.246  77.449  30.897  1.00127.18           C  
ATOM    606  OG1 THR A  90     -22.020  76.904  31.401  1.00121.02           O  
ATOM    607  CG2 THR A  90     -24.241  77.565  32.050  1.00113.80           C  
ATOM    608  N   ARG A  91     -25.370  77.766  28.403  1.00147.56           N  
ATOM    609  CA  ARG A  91     -26.657  78.253  27.903  1.00147.68           C  
ATOM    610  C   ARG A  91     -27.059  77.322  26.763  1.00147.13           C  
ATOM    611  O   ARG A  91     -27.222  77.749  25.625  1.00146.38           O  
ATOM    612  CB  ARG A  91     -26.513  79.693  27.379  1.00149.95           C  
ATOM    613  CG  ARG A  91     -27.748  80.270  26.675  1.00146.61           C  
ATOM    614  CD  ARG A  91     -28.834  80.688  27.653  1.00148.77           C  
ATOM    615  NE  ARG A  91     -28.705  82.083  28.072  1.00150.52           N  
ATOM    616  CZ  ARG A  91     -28.946  83.130  27.285  1.00150.52           C  
ATOM    617  NH1 ARG A  91     -29.330  82.947  26.027  1.00150.52           N  
ATOM    618  NH2 ARG A  91     -28.809  84.364  27.757  1.00150.52           N  
ATOM    619  N   GLU A  92     -27.194  76.040  27.085  1.00148.80           N  
ATOM    620  CA  GLU A  92     -27.563  75.007  26.121  1.00150.31           C  
ATOM    621  C   GLU A  92     -27.374  73.663  26.817  1.00150.52           C  
ATOM    622  O   GLU A  92     -27.998  72.663  26.455  1.00149.99           O  
ATOM    623  CB  GLU A  92     -26.663  75.086  24.879  1.00147.51           C  
ATOM    624  CG  GLU A  92     -25.175  74.960  25.173  1.00149.82           C  
ATOM    625  CD  GLU A  92     -24.741  73.531  25.449  1.00150.52           C  
ATOM    626  OE1 GLU A  92     -23.607  73.333  25.933  1.00150.25           O  
ATOM    627  OE2 GLU A  92     -25.530  72.604  25.172  1.00150.52           O  
ATOM    628  N   GLY A  93     -26.503  73.663  27.823  1.00149.15           N  
ATOM    629  CA  GLY A  93     -26.209  72.463  28.587  1.00142.04           C  
ATOM    630  C   GLY A  93     -25.428  72.798  29.847  1.00134.78           C  
ATOM    631  O   GLY A  93     -25.977  73.406  30.769  1.00139.18           O  
ATOM    632  N   GLU A  94     -24.153  72.406  29.894  1.00123.21           N  
ATOM    633  CA  GLU A  94     -23.306  72.683  31.055  1.00112.05           C  
ATOM    634  C   GLU A  94     -21.838  72.232  30.935  1.00109.81           C  
ATOM    635  O   GLU A  94     -21.520  71.049  31.080  1.00105.15           O  
ATOM    636  CB  GLU A  94     -23.929  72.077  32.309  1.00105.73           C  
ATOM    637  N   LYS A  95     -20.963  73.205  30.679  1.00104.62           N  
ATOM    638  CA  LYS A  95     -19.509  73.036  30.551  1.00 92.81           C  
ATOM    639  C   LYS A  95     -18.914  72.014  29.591  1.00 84.07           C  
ATOM    640  O   LYS A  95     -18.959  70.808  29.825  1.00 85.70           O  
ATOM    641  CB  LYS A  95     -18.880  72.835  31.933  1.00 97.25           C  
ATOM    642  CG  LYS A  95     -18.548  74.144  32.646  1.00106.07           C  
ATOM    643  CD  LYS A  95     -17.876  73.897  33.992  1.00110.75           C  
ATOM    644  CE  LYS A  95     -17.466  75.200  34.672  1.00110.29           C  
ATOM    645  NZ  LYS A  95     -16.826  74.962  36.000  1.00109.85           N  
ATOM    646  N   ARG A  96     -18.314  72.537  28.525  1.00 79.63           N  
ATOM    647  CA  ARG A  96     -17.668  71.731  27.495  1.00 71.70           C  
ATOM    648  C   ARG A  96     -16.246  72.254  27.256  1.00 65.11           C  
ATOM    649  O   ARG A  96     -16.009  73.466  27.268  1.00 52.40           O  
ATOM    650  CB  ARG A  96     -18.455  71.797  26.184  1.00 59.43           C  
ATOM    651  CG  ARG A  96     -17.995  70.769  25.166  1.00 81.35           C  
ATOM    652  CD  ARG A  96     -18.493  71.054  23.761  1.00 62.66           C  
ATOM    653  NE  ARG A  96     -18.080  69.992  22.852  1.00 65.29           N  
ATOM    654  CZ  ARG A  96     -18.189  70.048  21.529  1.00 72.15           C  
ATOM    655  NH1 ARG A  96     -18.700  71.126  20.951  1.00 74.82           N  
ATOM    656  NH2 ARG A  96     -17.787  69.024  20.786  1.00 65.30           N  
ATOM    657  N   THR A  97     -15.313  71.330  27.036  1.00 51.59           N  
ATOM    658  CA  THR A  97     -13.916  71.667  26.803  1.00 39.31           C  
ATOM    659  C   THR A  97     -13.416  70.966  25.555  1.00 47.58           C  
ATOM    660  O   THR A  97     -13.754  69.813  25.306  1.00 54.56           O  
ATOM    661  CB  THR A  97     -13.027  71.199  27.966  1.00 35.05           C  
ATOM    662  OG1 THR A  97     -11.761  71.855  27.900  1.00 37.97           O  
ATOM    663  CG2 THR A  97     -12.767  69.713  27.869  1.00 40.46           C  
ATOM    664  N   VAL A  98     -12.607  71.656  24.766  1.00 47.64           N  
ATOM    665  CA  VAL A  98     -12.053  71.042  23.569  1.00 55.73           C  
ATOM    666  C   VAL A  98     -10.614  71.495  23.432  1.00 57.36           C  
ATOM    667  O   VAL A  98     -10.231  72.541  23.954  1.00 58.39           O  
ATOM    668  CB  VAL A  98     -12.897  71.374  22.314  1.00 56.70           C  
ATOM    669  CG1 VAL A  98     -12.142  71.014  21.040  1.00 53.34           C  
ATOM    670  CG2 VAL A  98     -14.190  70.565  22.368  1.00 42.84           C  
ATOM    671  N   ILE A  99      -9.813  70.696  22.741  1.00 54.42           N  
ATOM    672  CA  ILE A  99      -8.407  70.998  22.605  1.00 40.40           C  
ATOM    673  C   ILE A  99      -7.918  70.767  21.173  1.00 39.94           C  
ATOM    674  O   ILE A  99      -8.472  69.934  20.450  1.00 47.31           O  
ATOM    675  CB  ILE A  99      -7.645  70.138  23.649  1.00 42.26           C  
ATOM    676  CG1 ILE A  99      -6.523  70.951  24.275  1.00 64.07           C  
ATOM    677  CG2 ILE A  99      -7.154  68.845  23.032  1.00 51.40           C  
ATOM    678  CD1 ILE A  99      -6.095  70.411  25.633  1.00 73.34           C  
ATOM    679  N   GLU A 100      -6.903  71.525  20.756  1.00 33.10           N  
ATOM    680  CA  GLU A 100      -6.351  71.403  19.401  1.00 39.61           C  
ATOM    681  C   GLU A 100      -4.871  71.748  19.426  1.00 35.75           C  
ATOM    682  O   GLU A 100      -4.419  72.487  20.291  1.00 41.66           O  
ATOM    683  CB  GLU A 100      -7.090  72.325  18.406  1.00 29.79           C  
ATOM    684  CG  GLU A 100      -6.984  73.825  18.694  1.00 58.83           C  
ATOM    685  CD  GLU A 100      -7.737  74.708  17.681  1.00 74.56           C  
ATOM    686  OE1 GLU A 100      -8.969  74.548  17.512  1.00 59.32           O  
ATOM    687  OE2 GLU A 100      -7.091  75.578  17.056  1.00 74.31           O  
ATOM    688  N   VAL A 101      -4.117  71.204  18.481  1.00 34.98           N  
ATOM    689  CA  VAL A 101      -2.684  71.451  18.416  1.00 32.93           C  
ATOM    690  C   VAL A 101      -2.287  72.318  17.222  1.00 24.39           C  
ATOM    691  O   VAL A 101      -2.497  71.939  16.075  1.00 42.39           O  
ATOM    692  CB  VAL A 101      -1.906  70.103  18.364  1.00 46.17           C  
ATOM    693  CG1 VAL A 101      -0.438  70.336  18.007  1.00 38.65           C  
ATOM    694  CG2 VAL A 101      -2.007  69.401  19.716  1.00 46.89           C  
ATOM    695  N   GLU A 102      -1.746  73.499  17.501  1.00 27.74           N  
ATOM    696  CA  GLU A 102      -1.287  74.394  16.443  1.00 34.57           C  
ATOM    697  C   GLU A 102       0.091  73.834  16.102  1.00 40.19           C  
ATOM    698  O   GLU A 102       1.048  74.005  16.866  1.00 41.49           O  
ATOM    699  CB  GLU A 102      -1.151  75.845  16.945  1.00 23.73           C  
ATOM    700  CG  GLU A 102      -2.461  76.593  17.174  1.00 40.18           C  
ATOM    701  CD  GLU A 102      -2.258  78.102  17.388  1.00 61.91           C  
ATOM    702  OE1 GLU A 102      -2.919  78.668  18.287  1.00 57.56           O  
ATOM    703  OE2 GLU A 102      -1.448  78.721  16.654  1.00 42.58           O  
ATOM    704  N   VAL A 103       0.183  73.155  14.964  1.00 33.90           N  
ATOM    705  CA  VAL A 103       1.425  72.521  14.540  1.00 32.86           C  
ATOM    706  C   VAL A 103       2.547  73.433  14.056  1.00 39.70           C  
ATOM    707  O   VAL A 103       2.387  74.175  13.087  1.00 51.21           O  
ATOM    708  CB  VAL A 103       1.146  71.483  13.428  1.00 37.36           C  
ATOM    709  CG1 VAL A 103       2.411  70.723  13.094  1.00 30.36           C  
ATOM    710  CG2 VAL A 103       0.060  70.525  13.875  1.00 34.72           C  
ATOM    711  N   ASP A 104       3.690  73.353  14.734  1.00 36.41           N  
ATOM    712  CA  ASP A 104       4.868  74.129  14.367  1.00 38.13           C  
ATOM    713  C   ASP A 104       5.637  73.345  13.309  1.00 39.14           C  
ATOM    714  O   ASP A 104       5.944  73.862  12.240  1.00 57.00           O  
ATOM    715  CB  ASP A 104       5.764  74.364  15.590  1.00 37.39           C  
ATOM    716  CG  ASP A 104       5.195  75.404  16.535  1.00 56.54           C  
ATOM    717  OD1 ASP A 104       4.842  76.503  16.050  1.00 57.79           O  
ATOM    718  OD2 ASP A 104       5.104  75.129  17.755  1.00 59.31           O  
ATOM    719  N   GLU A 105       5.948  72.091  13.618  1.00 48.17           N  
ATOM    720  CA  GLU A 105       6.666  71.225  12.691  1.00 46.61           C  
ATOM    721  C   GLU A 105       6.028  69.844  12.723  1.00 38.78           C  
ATOM    722  O   GLU A 105       5.545  69.378  13.764  1.00 36.22           O  
ATOM    723  CB  GLU A 105       8.142  71.091  13.072  1.00 44.78           C  
ATOM    724  CG  GLU A 105       8.934  72.379  13.164  1.00 51.46           C  
ATOM    725  CD  GLU A 105       9.496  72.839  11.830  1.00 67.19           C  
ATOM    726  OE1 GLU A 105       9.911  71.978  11.025  1.00 49.30           O  
ATOM    727  OE2 GLU A 105       9.547  74.069  11.598  1.00 61.88           O  
ATOM    728  N   ILE A 106       6.045  69.201  11.567  1.00 35.01           N  
ATOM    729  CA  ILE A 106       5.487  67.876  11.380  1.00 42.33           C  
ATOM    730  C   ILE A 106       6.202  67.264  10.206  1.00 42.51           C  
ATOM    731  O   ILE A 106       6.578  67.967   9.263  1.00 37.78           O  
ATOM    732  CB  ILE A 106       4.004  67.925  11.008  1.00 45.93           C  
ATOM    733  CG1 ILE A 106       3.501  66.510  10.745  1.00 22.55           C  
ATOM    734  CG2 ILE A 106       3.813  68.774   9.760  1.00 42.26           C  
ATOM    735  CD1 ILE A 106       2.021  66.419  10.497  1.00 19.12           C  
ATOM    736  N   GLY A 107       6.371  65.953  10.258  1.00 47.31           N  
ATOM    737  CA  GLY A 107       7.042  65.256   9.182  1.00 40.25           C  
ATOM    738  C   GLY A 107       6.773  63.781   9.334  1.00 42.73           C  
ATOM    739  O   GLY A 107       6.576  63.306  10.459  1.00 56.41           O  
ATOM    740  N   PRO A 108       6.738  63.026   8.227  1.00 41.19           N  
ATOM    741  CA  PRO A 108       6.479  61.590   8.339  1.00 38.30           C  
ATOM    742  C   PRO A 108       7.614  60.931   9.092  1.00 25.85           C  
ATOM    743  O   PRO A 108       8.769  61.247   8.857  1.00 35.42           O  
ATOM    744  CB  PRO A 108       6.401  61.142   6.882  1.00 41.47           C  
ATOM    745  CG  PRO A 108       7.326  62.104   6.172  1.00 27.74           C  
ATOM    746  CD  PRO A 108       6.953  63.417   6.821  1.00 38.65           C  
ATOM    747  N   SER A 109       7.286  60.034  10.015  1.00 38.95           N  
ATOM    748  CA  SER A 109       8.311  59.347  10.796  1.00 32.69           C  
ATOM    749  C   SER A 109       8.980  58.222  10.009  1.00 38.76           C  
ATOM    750  O   SER A 109       8.312  57.478   9.281  1.00 22.86           O  
ATOM    751  CB  SER A 109       7.696  58.774  12.077  1.00 32.15           C  
ATOM    752  OG  SER A 109       8.567  57.851  12.712  1.00 25.18           O  
ATOM    753  N   LEU A 110      10.297  58.097  10.174  1.00 37.99           N  
ATOM    754  CA  LEU A 110      11.073  57.057   9.500  1.00 37.20           C  
ATOM    755  C   LEU A 110      11.371  55.853  10.400  1.00 41.13           C  
ATOM    756  O   LEU A 110      12.455  55.284  10.336  1.00 39.69           O  
ATOM    757  CB  LEU A 110      12.400  57.630   9.012  1.00 38.06           C  
ATOM    758  CG  LEU A 110      12.382  58.844   8.090  1.00 25.12           C  
ATOM    759  CD1 LEU A 110      13.811  59.193   7.775  1.00 33.64           C  
ATOM    760  CD2 LEU A 110      11.608  58.549   6.807  1.00 28.67           C  
ATOM    761  N   ARG A 111      10.419  55.459  11.237  1.00 45.98           N  
ATOM    762  CA  ARG A 111      10.640  54.321  12.122  1.00 43.33           C  
ATOM    763  C   ARG A 111      10.239  53.027  11.433  1.00 35.03           C  
ATOM    764  O   ARG A 111      10.902  52.010  11.583  1.00 46.16           O  
ATOM    765  CB  ARG A 111       9.848  54.503  13.419  1.00 48.82           C  
ATOM    766  CG  ARG A 111      10.097  53.456  14.485  1.00 39.40           C  
ATOM    767  CD  ARG A 111       9.415  53.887  15.766  1.00 57.21           C  
ATOM    768  NE  ARG A 111       9.392  52.853  16.794  1.00 70.99           N  
ATOM    769  CZ  ARG A 111       9.052  53.074  18.062  1.00 79.72           C  
ATOM    770  NH1 ARG A 111       8.714  54.297  18.462  1.00 71.25           N  
ATOM    771  NH2 ARG A 111       9.034  52.071  18.930  1.00 74.06           N  
ATOM    772  N   TYR A 112       9.147  53.067  10.682  1.00 34.33           N  
ATOM    773  CA  TYR A 112       8.693  51.887   9.963  1.00 33.53           C  
ATOM    774  C   TYR A 112       8.495  52.242   8.487  1.00 35.03           C  
ATOM    775  O   TYR A 112       7.558  51.775   7.849  1.00 42.21           O  
ATOM    776  CB  TYR A 112       7.370  51.394  10.538  1.00 28.70           C  
ATOM    777  CG  TYR A 112       7.403  51.096  12.011  1.00 41.72           C  
ATOM    778  CD1 TYR A 112       6.472  51.664  12.869  1.00 35.34           C  
ATOM    779  CD2 TYR A 112       8.334  50.219  12.543  1.00 39.04           C  
ATOM    780  CE1 TYR A 112       6.455  51.354  14.222  1.00 53.34           C  
ATOM    781  CE2 TYR A 112       8.327  49.900  13.899  1.00 55.99           C  
ATOM    782  CZ  TYR A 112       7.384  50.471  14.735  1.00 53.29           C  
ATOM    783  OH  TYR A 112       7.336  50.125  16.073  1.00 40.76           O  
ATOM    784  N   ALA A 113       9.365  53.076   7.936  1.00 29.38           N  
ATOM    785  CA  ALA A 113       9.193  53.448   6.537  1.00 39.83           C  
ATOM    786  C   ALA A 113      10.305  54.319   6.001  1.00 38.46           C  
ATOM    787  O   ALA A 113      11.273  54.631   6.701  1.00 45.12           O  
ATOM    788  CB  ALA A 113       7.857  54.166   6.355  1.00 42.68           C  
ATOM    789  N   THR A 114      10.154  54.702   4.740  1.00 28.34           N  
ATOM    790  CA  THR A 114      11.122  55.571   4.090  1.00 40.68           C  
ATOM    791  C   THR A 114      10.342  56.637   3.369  1.00 38.04           C  
ATOM    792  O   THR A 114       9.116  56.607   3.335  1.00 43.56           O  
ATOM    793  CB  THR A 114      12.013  54.828   3.056  1.00 43.12           C  
ATOM    794  OG1 THR A 114      11.191  54.138   2.100  1.00 43.64           O  
ATOM    795  CG2 THR A 114      12.939  53.854   3.764  1.00 33.35           C  
ATOM    796  N   ALA A 115      11.057  57.589   2.802  1.00 45.02           N  
ATOM    797  CA  ALA A 115      10.412  58.649   2.072  1.00 47.62           C  
ATOM    798  C   ALA A 115      11.461  59.329   1.246  1.00 54.33           C  
ATOM    799  O   ALA A 115      12.624  59.385   1.639  1.00 47.78           O  
ATOM    800  CB  ALA A 115       9.786  59.639   3.034  1.00 59.94           C  
ATOM    801  N   LYS A 116      11.061  59.822   0.085  1.00 60.25           N  
ATOM    802  CA  LYS A 116      11.991  60.546  -0.753  1.00 69.33           C  
ATOM    803  C   LYS A 116      11.679  62.009  -0.508  1.00 70.22           C  
ATOM    804  O   LYS A 116      10.584  62.489  -0.809  1.00 70.55           O  
ATOM    805  CB  LYS A 116      11.814  60.156  -2.220  1.00 79.52           C  
ATOM    806  CG  LYS A 116      12.303  58.734  -2.482  1.00 99.94           C  
ATOM    807  CD  LYS A 116      12.379  58.380  -3.956  1.00 99.36           C  
ATOM    808  CE  LYS A 116      12.960  56.984  -4.132  1.00 99.61           C  
ATOM    809  NZ  LYS A 116      13.043  56.570  -5.558  1.00110.87           N  
ATOM    810  N   VAL A 117      12.644  62.697   0.090  1.00 64.62           N  
ATOM    811  CA  VAL A 117      12.501  64.104   0.424  1.00 66.59           C  
ATOM    812  C   VAL A 117      13.006  65.004  -0.698  1.00 70.60           C  
ATOM    813  O   VAL A 117      14.204  65.064  -0.961  1.00 70.33           O  
ATOM    814  CB  VAL A 117      13.274  64.426   1.726  1.00 67.89           C  
ATOM    815  CG1 VAL A 117      13.215  65.914   2.024  1.00 66.67           C  
ATOM    816  CG2 VAL A 117      12.691  63.623   2.882  1.00 66.29           C  
ATOM    817  N   ASN A 118      12.084  65.705  -1.352  1.00 75.36           N  
ATOM    818  CA  ASN A 118      12.434  66.602  -2.448  1.00 87.25           C  
ATOM    819  C   ASN A 118      12.484  68.061  -1.988  1.00 95.50           C  
ATOM    820  O   ASN A 118      11.459  68.629  -1.607  1.00104.12           O  
ATOM    821  CB  ASN A 118      11.427  66.447  -3.582  1.00 61.71           C  
ATOM    822  N   LYS A 119      13.675  68.660  -2.024  1.00104.98           N  
ATOM    823  CA  LYS A 119      13.858  70.053  -1.613  1.00103.72           C  
ATOM    824  C   LYS A 119      13.107  71.029  -2.507  1.00107.63           C  
ATOM    825  O   LYS A 119      12.203  70.656  -3.254  1.00104.33           O  
ATOM    826  CB  LYS A 119      15.336  70.454  -1.653  1.00105.54           C  
ATOM    827  CG  LYS A 119      16.168  70.156  -0.419  1.00108.51           C  
ATOM    828  CD  LYS A 119      17.374  71.100  -0.393  1.00108.68           C  
ATOM    829  CE  LYS A 119      18.689  70.380  -0.138  1.00112.60           C  
ATOM    830  NZ  LYS A 119      19.858  71.287  -0.354  1.00111.14           N  
ATOM    831  N   ALA A 120      13.520  72.290  -2.422  1.00112.32           N  
ATOM    832  CA  ALA A 120      12.943  73.374  -3.207  1.00119.59           C  
ATOM    833  C   ALA A 120      13.869  74.592  -3.151  1.00124.41           C  
ATOM    834  O   ALA A 120      14.327  75.038  -4.227  1.00124.93           O  
ATOM    835  CB  ALA A 120      11.561  73.733  -2.669  1.00121.32           C  
TER     836      ALA A 120                                                      
ATOM    837  N   ALA B   2      12.904  55.948  36.281  1.00 99.84           N  
ATOM    838  CA  ALA B   2      11.964  55.132  35.466  1.00103.03           C  
ATOM    839  C   ALA B   2      12.146  55.497  34.001  1.00103.65           C  
ATOM    840  O   ALA B   2      12.216  54.628  33.126  1.00 99.82           O  
ATOM    841  CB  ALA B   2      10.528  55.410  35.901  1.00107.63           C  
ATOM    842  N   GLY B   3      12.238  56.798  33.751  1.00 99.79           N  
ATOM    843  CA  GLY B   3      12.398  57.276  32.398  1.00 85.69           C  
ATOM    844  C   GLY B   3      13.560  58.222  32.171  1.00 79.51           C  
ATOM    845  O   GLY B   3      14.019  58.942  33.054  1.00 62.49           O  
ATOM    846  N   ASP B   4      14.028  58.204  30.936  1.00 73.59           N  
ATOM    847  CA  ASP B   4      15.127  59.030  30.502  1.00 70.89           C  
ATOM    848  C   ASP B   4      14.635  60.460  30.289  1.00 70.01           C  
ATOM    849  O   ASP B   4      13.445  60.754  30.426  1.00 71.43           O  
ATOM    850  CB  ASP B   4      15.670  58.460  29.195  1.00 75.11           C  
ATOM    851  CG  ASP B   4      15.867  56.956  29.260  1.00 77.79           C  
ATOM    852  OD1 ASP B   4      14.925  56.245  29.677  1.00 68.41           O  
ATOM    853  OD2 ASP B   4      16.961  56.485  28.895  1.00 68.41           O  
ATOM    854  N   THR B   5      15.571  61.346  29.970  1.00 61.52           N  
ATOM    855  CA  THR B   5      15.273  62.743  29.708  1.00 30.61           C  
ATOM    856  C   THR B   5      15.074  62.812  28.202  1.00 41.01           C  
ATOM    857  O   THR B   5      15.939  62.391  27.442  1.00 42.65           O  
ATOM    858  CB  THR B   5      16.454  63.607  30.114  1.00 36.63           C  
ATOM    859  OG1 THR B   5      16.553  63.619  31.543  1.00 37.54           O  
ATOM    860  CG2 THR B   5      16.298  65.016  29.578  1.00 40.05           C  
ATOM    861  N   THR B   6      13.939  63.341  27.764  1.00 42.47           N  
ATOM    862  CA  THR B   6      13.654  63.393  26.340  1.00 38.30           C  
ATOM    863  C   THR B   6      13.578  64.786  25.728  1.00 46.05           C  
ATOM    864  O   THR B   6      13.271  65.766  26.408  1.00 60.38           O  
ATOM    865  CB  THR B   6      12.346  62.689  26.053  1.00 42.69           C  
ATOM    866  OG1 THR B   6      11.283  63.397  26.702  1.00 63.36           O  
ATOM    867  CG2 THR B   6      12.390  61.275  26.581  1.00 46.31           C  
ATOM    868  N   ILE B   7      13.853  64.860  24.429  1.00 42.90           N  
ATOM    869  CA  ILE B   7      13.807  66.122  23.719  1.00 37.49           C  
ATOM    870  C   ILE B   7      13.373  65.998  22.271  1.00 39.10           C  
ATOM    871  O   ILE B   7      13.601  64.980  21.609  1.00 34.05           O  
ATOM    872  CB  ILE B   7      15.176  66.847  23.706  1.00 43.66           C  
ATOM    873  CG1 ILE B   7      16.040  66.319  22.566  1.00 34.85           C  
ATOM    874  CG2 ILE B   7      15.888  66.662  25.040  1.00 55.16           C  
ATOM    875  CD1 ILE B   7      17.294  67.140  22.353  1.00 47.40           C  
ATOM    876  N   THR B   8      12.746  67.070  21.799  1.00 34.95           N  
ATOM    877  CA  THR B   8      12.283  67.192  20.434  1.00 32.96           C  
ATOM    878  C   THR B   8      13.091  68.351  19.872  1.00 41.14           C  
ATOM    879  O   THR B   8      12.901  69.491  20.283  1.00 47.27           O  
ATOM    880  CB  THR B   8      10.810  67.579  20.370  1.00 37.55           C  
ATOM    881  OG1 THR B   8      10.034  66.627  21.107  1.00 46.45           O  
ATOM    882  CG2 THR B   8      10.345  67.622  18.917  1.00 34.70           C  
ATOM    883  N   ILE B   9      14.002  68.055  18.955  1.00 35.24           N  
ATOM    884  CA  ILE B   9      14.837  69.075  18.346  1.00 36.52           C  
ATOM    885  C   ILE B   9      14.639  69.121  16.845  1.00 37.63           C  
ATOM    886  O   ILE B   9      14.692  68.097  16.181  1.00 28.95           O  
ATOM    887  CB  ILE B   9      16.320  68.808  18.598  1.00 44.35           C  
ATOM    888  CG1 ILE B   9      17.173  69.727  17.727  1.00 47.75           C  
ATOM    889  CG2 ILE B   9      16.646  67.372  18.285  1.00 42.33           C  
ATOM    890  CD1 ILE B   9      18.662  69.510  17.902  1.00 54.77           C  
ATOM    891  N   VAL B  10      14.404  70.321  16.324  1.00 44.95           N  
ATOM    892  CA  VAL B  10      14.225  70.516  14.897  1.00 39.37           C  
ATOM    893  C   VAL B  10      15.480  71.200  14.381  1.00 47.67           C  
ATOM    894  O   VAL B  10      16.050  72.059  15.061  1.00 36.74           O  
ATOM    895  CB  VAL B  10      13.002  71.394  14.581  1.00 38.14           C  
ATOM    896  CG1 VAL B  10      12.898  71.581  13.083  1.00 32.71           C  
ATOM    897  CG2 VAL B  10      11.711  70.728  15.109  1.00 29.82           C  
ATOM    898  N   GLY B  11      15.918  70.805  13.188  1.00 46.07           N  
ATOM    899  CA  GLY B  11      17.115  71.388  12.615  1.00 38.50           C  
ATOM    900  C   GLY B  11      17.496  70.732  11.309  1.00 41.47           C  
ATOM    901  O   GLY B  11      16.699  69.991  10.727  1.00 35.65           O  
ATOM    902  N   ASN B  12      18.713  71.005  10.846  1.00 47.91           N  
ATOM    903  CA  ASN B  12      19.198  70.426   9.591  1.00 56.12           C  
ATOM    904  C   ASN B  12      20.355  69.466   9.813  1.00 51.63           C  
ATOM    905  O   ASN B  12      21.127  69.624  10.758  1.00 60.91           O  
ATOM    906  CB  ASN B  12      19.648  71.524   8.622  1.00 42.70           C  
ATOM    907  CG  ASN B  12      18.511  72.428   8.193  1.00 56.37           C  
ATOM    908  OD1 ASN B  12      18.518  73.629   8.470  1.00 50.88           O  
ATOM    909  ND2 ASN B  12      17.524  71.855   7.512  1.00 47.86           N  
ATOM    910  N   LEU B  13      20.466  68.472   8.934  1.00 52.62           N  
ATOM    911  CA  LEU B  13      21.539  67.485   9.011  1.00 51.27           C  
ATOM    912  C   LEU B  13      22.826  68.111   8.506  1.00 49.07           C  
ATOM    913  O   LEU B  13      22.902  68.542   7.353  1.00 59.71           O  
ATOM    914  CB  LEU B  13      21.200  66.261   8.160  1.00 46.13           C  
ATOM    915  CG  LEU B  13      20.158  65.326   8.771  1.00 61.12           C  
ATOM    916  CD1 LEU B  13      19.793  64.249   7.773  1.00 68.88           C  
ATOM    917  CD2 LEU B  13      20.713  64.708  10.049  1.00 58.66           C  
ATOM    918  N   THR B  14      23.830  68.162   9.374  1.00 42.35           N  
ATOM    919  CA  THR B  14      25.120  68.745   9.027  1.00 45.94           C  
ATOM    920  C   THR B  14      25.682  68.069   7.802  1.00 44.46           C  
ATOM    921  O   THR B  14      26.369  68.688   6.996  1.00 62.77           O  
ATOM    922  CB  THR B  14      26.134  68.563  10.159  1.00 46.83           C  
ATOM    923  OG1 THR B  14      26.090  67.206  10.619  1.00 55.25           O  
ATOM    924  CG2 THR B  14      25.829  69.502  11.302  1.00 58.40           C  
ATOM    925  N   ALA B  15      25.380  66.787   7.674  1.00 47.69           N  
ATOM    926  CA  ALA B  15      25.869  65.996   6.562  1.00 49.93           C  
ATOM    927  C   ALA B  15      25.019  64.746   6.448  1.00 56.95           C  
ATOM    928  O   ALA B  15      24.235  64.439   7.344  1.00 74.49           O  
ATOM    929  CB  ALA B  15      27.304  65.616   6.814  1.00 36.29           C  
ATOM    930  N   ASP B  16      25.171  64.022   5.349  1.00 66.83           N  
ATOM    931  CA  ASP B  16      24.409  62.799   5.154  1.00 64.21           C  
ATOM    932  C   ASP B  16      24.641  61.869   6.331  1.00 63.64           C  
ATOM    933  O   ASP B  16      25.683  61.934   6.990  1.00 57.45           O  
ATOM    934  CB  ASP B  16      24.845  62.111   3.866  1.00 73.57           C  
ATOM    935  CG  ASP B  16      24.605  62.967   2.654  1.00 81.88           C  
ATOM    936  OD1 ASP B  16      23.433  63.123   2.253  1.00 86.73           O  
ATOM    937  OD2 ASP B  16      25.590  63.498   2.107  1.00102.04           O  
ATOM    938  N   PRO B  17      23.665  60.995   6.615  1.00 60.40           N  
ATOM    939  CA  PRO B  17      23.753  60.037   7.720  1.00 49.27           C  
ATOM    940  C   PRO B  17      24.844  58.988   7.463  1.00 56.81           C  
ATOM    941  O   PRO B  17      24.873  58.343   6.416  1.00 61.97           O  
ATOM    942  CB  PRO B  17      22.358  59.420   7.750  1.00 49.88           C  
ATOM    943  CG  PRO B  17      21.490  60.469   7.097  1.00 50.49           C  
ATOM    944  CD  PRO B  17      22.343  60.928   5.972  1.00 53.90           C  
ATOM    945  N   GLU B  18      25.736  58.825   8.433  1.00 68.10           N  
ATOM    946  CA  GLU B  18      26.831  57.869   8.334  1.00 68.51           C  
ATOM    947  C   GLU B  18      26.351  56.513   8.833  1.00 72.11           C  
ATOM    948  O   GLU B  18      26.264  56.283  10.043  1.00 75.00           O  
ATOM    949  CB  GLU B  18      27.997  58.362   9.185  1.00 80.27           C  
ATOM    950  CG  GLU B  18      29.349  57.822   8.800  1.00 95.18           C  
ATOM    951  CD  GLU B  18      30.467  58.675   9.365  1.00113.24           C  
ATOM    952  OE1 GLU B  18      30.494  58.880  10.599  1.00113.33           O  
ATOM    953  OE2 GLU B  18      31.314  59.148   8.576  1.00121.11           O  
ATOM    954  N   LEU B  19      26.034  55.616   7.905  1.00 63.28           N  
ATOM    955  CA  LEU B  19      25.550  54.298   8.286  1.00 53.92           C  
ATOM    956  C   LEU B  19      26.641  53.256   8.406  1.00 51.49           C  
ATOM    957  O   LEU B  19      27.344  52.968   7.445  1.00 60.36           O  
ATOM    958  CB  LEU B  19      24.506  53.798   7.292  1.00 51.29           C  
ATOM    959  CG  LEU B  19      23.974  52.404   7.618  1.00 34.71           C  
ATOM    960  CD1 LEU B  19      23.387  52.410   9.015  1.00 40.07           C  
ATOM    961  CD2 LEU B  19      22.935  51.996   6.609  1.00 34.58           C  
ATOM    962  N   ARG B  20      26.774  52.694   9.601  1.00 56.13           N  
ATOM    963  CA  ARG B  20      27.755  51.653   9.861  1.00 55.49           C  
ATOM    964  C   ARG B  20      27.049  50.487  10.543  1.00 54.55           C  
ATOM    965  O   ARG B  20      25.848  50.548  10.794  1.00 60.56           O  
ATOM    966  CB  ARG B  20      28.888  52.183  10.741  1.00 69.74           C  
ATOM    967  CG  ARG B  20      29.952  52.982   9.981  1.00 85.63           C  
ATOM    968  CD  ARG B  20      29.481  54.379   9.587  1.00104.15           C  
ATOM    969  NE  ARG B  20      30.499  55.121   8.839  1.00105.35           N  
ATOM    970  CZ  ARG B  20      30.751  54.963   7.542  1.00105.01           C  
ATOM    971  NH1 ARG B  20      30.058  54.089   6.826  1.00115.18           N  
ATOM    972  NH2 ARG B  20      31.702  55.676   6.958  1.00104.70           N  
ATOM    973  N   PHE B  21      27.781  49.415  10.825  1.00 56.42           N  
ATOM    974  CA  PHE B  21      27.177  48.255  11.472  1.00 50.41           C  
ATOM    975  C   PHE B  21      28.056  47.734  12.585  1.00 35.69           C  
ATOM    976  O   PHE B  21      29.260  47.622  12.422  1.00 47.26           O  
ATOM    977  CB  PHE B  21      26.946  47.119  10.468  1.00 42.35           C  
ATOM    978  CG  PHE B  21      26.085  47.500   9.301  1.00 54.41           C  
ATOM    979  CD1 PHE B  21      26.574  48.331   8.298  1.00 39.15           C  
ATOM    980  CD2 PHE B  21      24.779  47.036   9.205  1.00 51.47           C  
ATOM    981  CE1 PHE B  21      25.783  48.684   7.226  1.00 34.92           C  
ATOM    982  CE2 PHE B  21      23.982  47.392   8.125  1.00 49.18           C  
ATOM    983  CZ  PHE B  21      24.484  48.215   7.139  1.00 32.30           C  
ATOM    984  N   THR B  22      27.440  47.404  13.711  1.00 45.01           N  
ATOM    985  CA  THR B  22      28.162  46.877  14.856  1.00 44.83           C  
ATOM    986  C   THR B  22      28.730  45.520  14.475  1.00 59.29           C  
ATOM    987  O   THR B  22      28.464  45.011  13.387  1.00 63.08           O  
ATOM    988  CB  THR B  22      27.227  46.711  16.057  1.00 46.81           C  
ATOM    989  OG1 THR B  22      26.253  45.699  15.776  1.00 49.06           O  
ATOM    990  CG2 THR B  22      26.513  48.024  16.340  1.00 46.48           C  
ATOM    991  N   PRO B  23      29.525  44.908  15.362  1.00 68.61           N  
ATOM    992  CA  PRO B  23      30.071  43.602  14.994  1.00 62.48           C  
ATOM    993  C   PRO B  23      28.994  42.536  14.761  1.00 63.87           C  
ATOM    994  O   PRO B  23      29.075  41.755  13.813  1.00 73.85           O  
ATOM    995  CB  PRO B  23      30.995  43.278  16.172  1.00 60.69           C  
ATOM    996  CG  PRO B  23      30.373  44.018  17.317  1.00 58.76           C  
ATOM    997  CD  PRO B  23      30.010  45.328  16.690  1.00 65.43           C  
ATOM    998  N   SER B  24      27.981  42.523  15.620  1.00 57.12           N  
ATOM    999  CA  SER B  24      26.898  41.556  15.527  1.00 44.15           C  
ATOM   1000  C   SER B  24      26.031  41.720  14.268  1.00 47.69           C  
ATOM   1001  O   SER B  24      25.318  40.794  13.874  1.00 50.37           O  
ATOM   1002  CB  SER B  24      26.009  41.669  16.765  1.00 48.58           C  
ATOM   1003  OG  SER B  24      25.400  42.954  16.830  1.00 51.35           O  
ATOM   1004  N   GLY B  25      26.071  42.899  13.659  1.00 26.71           N  
ATOM   1005  CA  GLY B  25      25.279  43.142  12.467  1.00 30.19           C  
ATOM   1006  C   GLY B  25      24.280  44.279  12.598  1.00 47.15           C  
ATOM   1007  O   GLY B  25      23.814  44.806  11.590  1.00 39.72           O  
ATOM   1008  N   ALA B  26      23.955  44.669  13.830  1.00 46.72           N  
ATOM   1009  CA  ALA B  26      22.988  45.741  14.054  1.00 49.18           C  
ATOM   1010  C   ALA B  26      23.451  47.047  13.426  1.00 51.15           C  
ATOM   1011  O   ALA B  26      24.561  47.506  13.690  1.00 54.83           O  
ATOM   1012  CB  ALA B  26      22.750  45.931  15.544  1.00 32.04           C  
ATOM   1013  N   ALA B  27      22.592  47.633  12.594  1.00 42.14           N  
ATOM   1014  CA  ALA B  27      22.882  48.893  11.907  1.00 39.94           C  
ATOM   1015  C   ALA B  27      22.902  50.056  12.890  1.00 47.82           C  
ATOM   1016  O   ALA B  27      22.277  49.994  13.948  1.00 49.21           O  
ATOM   1017  CB  ALA B  27      21.837  49.148  10.828  1.00 27.52           C  
ATOM   1018  N   VAL B  28      23.619  51.117  12.530  1.00 55.05           N  
ATOM   1019  CA  VAL B  28      23.738  52.315  13.363  1.00 51.45           C  
ATOM   1020  C   VAL B  28      24.042  53.529  12.483  1.00 53.12           C  
ATOM   1021  O   VAL B  28      25.020  53.543  11.738  1.00 60.11           O  
ATOM   1022  CB  VAL B  28      24.880  52.184  14.407  1.00 50.48           C  
ATOM   1023  CG1 VAL B  28      24.915  53.417  15.291  1.00 59.09           C  
ATOM   1024  CG2 VAL B  28      24.678  50.958  15.261  1.00 57.25           C  
ATOM   1025  N   ALA B  29      23.200  54.548  12.570  1.00 55.99           N  
ATOM   1026  CA  ALA B  29      23.391  55.752  11.778  1.00 42.26           C  
ATOM   1027  C   ALA B  29      23.703  56.926  12.684  1.00 45.30           C  
ATOM   1028  O   ALA B  29      23.081  57.088  13.731  1.00 44.04           O  
ATOM   1029  CB  ALA B  29      22.149  56.040  10.976  1.00 26.33           C  
ATOM   1030  N   ASN B  30      24.679  57.731  12.276  1.00 55.73           N  
ATOM   1031  CA  ASN B  30      25.094  58.909  13.027  1.00 47.03           C  
ATOM   1032  C   ASN B  30      24.901  60.144  12.182  1.00 55.99           C  
ATOM   1033  O   ASN B  30      24.942  60.090  10.948  1.00 45.95           O  
ATOM   1034  CB  ASN B  30      26.568  58.824  13.431  1.00 36.92           C  
ATOM   1035  CG  ASN B  30      26.788  58.009  14.695  1.00 63.36           C  
ATOM   1036  OD1 ASN B  30      26.745  56.777  14.678  1.00 74.40           O  
ATOM   1037  ND2 ASN B  30      27.020  58.701  15.807  1.00 77.39           N  
ATOM   1038  N   PHE B  31      24.689  61.261  12.866  1.00 58.32           N  
ATOM   1039  CA  PHE B  31      24.496  62.555  12.225  1.00 56.29           C  
ATOM   1040  C   PHE B  31      24.294  63.573  13.334  1.00 51.26           C  
ATOM   1041  O   PHE B  31      24.114  63.203  14.496  1.00 45.69           O  
ATOM   1042  CB  PHE B  31      23.269  62.534  11.304  1.00 44.54           C  
ATOM   1043  CG  PHE B  31      22.028  62.005  11.960  1.00 43.25           C  
ATOM   1044  CD1 PHE B  31      21.661  60.675  11.811  1.00 53.41           C  
ATOM   1045  CD2 PHE B  31      21.236  62.832  12.743  1.00 55.56           C  
ATOM   1046  CE1 PHE B  31      20.525  60.177  12.438  1.00 54.10           C  
ATOM   1047  CE2 PHE B  31      20.102  62.344  13.373  1.00 56.31           C  
ATOM   1048  CZ  PHE B  31      19.746  61.013  13.219  1.00 51.23           C  
ATOM   1049  N   THR B  32      24.345  64.854  12.991  1.00 43.95           N  
ATOM   1050  CA  THR B  32      24.139  65.878  13.997  1.00 39.90           C  
ATOM   1051  C   THR B  32      23.172  66.907  13.442  1.00 42.94           C  
ATOM   1052  O   THR B  32      23.283  67.330  12.292  1.00 47.92           O  
ATOM   1053  CB  THR B  32      25.458  66.577  14.412  1.00 26.90           C  
ATOM   1054  OG1 THR B  32      25.702  67.691  13.552  1.00 49.95           O  
ATOM   1055  CG2 THR B  32      26.625  65.624  14.321  1.00 17.17           C  
ATOM   1056  N   VAL B  33      22.207  67.290  14.268  1.00 41.76           N  
ATOM   1057  CA  VAL B  33      21.209  68.263  13.871  1.00 41.60           C  
ATOM   1058  C   VAL B  33      21.695  69.669  14.206  1.00 46.68           C  
ATOM   1059  O   VAL B  33      22.182  69.924  15.307  1.00 31.20           O  
ATOM   1060  CB  VAL B  33      19.870  68.011  14.596  1.00 44.53           C  
ATOM   1061  CG1 VAL B  33      18.899  69.127  14.282  1.00 34.18           C  
ATOM   1062  CG2 VAL B  33      19.287  66.662  14.176  1.00 35.36           C  
ATOM   1063  N   ALA B  34      21.572  70.568  13.237  1.00 44.15           N  
ATOM   1064  CA  ALA B  34      21.973  71.951  13.415  1.00 45.42           C  
ATOM   1065  C   ALA B  34      20.684  72.728  13.588  1.00 51.10           C  
ATOM   1066  O   ALA B  34      20.018  73.081  12.613  1.00 56.24           O  
ATOM   1067  CB  ALA B  34      22.726  72.442  12.195  1.00 46.31           C  
ATOM   1068  N   SER B  35      20.335  72.969  14.844  1.00 52.22           N  
ATOM   1069  CA  SER B  35      19.124  73.685  15.213  1.00 45.30           C  
ATOM   1070  C   SER B  35      19.468  75.153  15.385  1.00 46.62           C  
ATOM   1071  O   SER B  35      20.205  75.510  16.307  1.00 52.77           O  
ATOM   1072  CB  SER B  35      18.575  73.092  16.521  1.00 46.79           C  
ATOM   1073  OG  SER B  35      17.592  73.913  17.127  1.00 51.11           O  
ATOM   1074  N   THR B  36      18.949  75.997  14.491  1.00 50.23           N  
ATOM   1075  CA  THR B  36      19.209  77.441  14.535  1.00 53.68           C  
ATOM   1076  C   THR B  36      17.988  78.236  15.005  1.00 55.22           C  
ATOM   1077  O   THR B  36      16.963  78.264  14.331  1.00 45.87           O  
ATOM   1078  CB  THR B  36      19.636  77.989  13.137  1.00 53.25           C  
ATOM   1079  OG1 THR B  36      18.631  77.679  12.165  1.00 57.86           O  
ATOM   1080  CG2 THR B  36      20.945  77.372  12.690  1.00 45.51           C  
ATOM   1081  N   PRO B  37      18.084  78.887  16.178  1.00 64.54           N  
ATOM   1082  CA  PRO B  37      16.992  79.686  16.744  1.00 74.02           C  
ATOM   1083  C   PRO B  37      17.037  81.119  16.220  1.00 82.29           C  
ATOM   1084  O   PRO B  37      18.113  81.631  15.918  1.00 89.83           O  
ATOM   1085  CB  PRO B  37      17.269  79.613  18.236  1.00 71.92           C  
ATOM   1086  CG  PRO B  37      18.758  79.696  18.265  1.00 72.13           C  
ATOM   1087  CD  PRO B  37      19.173  78.737  17.161  1.00 67.67           C  
ATOM   1088  N   ARG B  38      15.878  81.766  16.121  1.00 87.03           N  
ATOM   1089  CA  ARG B  38      15.806  83.142  15.625  1.00 92.95           C  
ATOM   1090  C   ARG B  38      15.912  84.208  16.717  1.00 97.49           C  
ATOM   1091  O   ARG B  38      15.443  84.015  17.839  1.00 97.83           O  
ATOM   1092  CB  ARG B  38      14.505  83.355  14.847  1.00 91.09           C  
ATOM   1093  CG  ARG B  38      14.513  82.802  13.436  1.00 82.54           C  
ATOM   1094  CD  ARG B  38      15.501  83.556  12.563  1.00 86.63           C  
ATOM   1095  NE  ARG B  38      15.498  83.063  11.191  1.00 87.76           N  
ATOM   1096  CZ  ARG B  38      14.445  83.110  10.381  1.00 97.61           C  
ATOM   1097  NH1 ARG B  38      13.303  83.634  10.807  1.00 99.65           N  
ATOM   1098  NH2 ARG B  38      14.529  82.629   9.146  1.00101.38           N  
ATOM   1099  N   ILE B  39      16.526  85.336  16.369  1.00 99.95           N  
ATOM   1100  CA  ILE B  39      16.698  86.454  17.290  1.00101.44           C  
ATOM   1101  C   ILE B  39      16.202  87.734  16.619  1.00108.50           C  
ATOM   1102  O   ILE B  39      16.469  87.961  15.441  1.00112.59           O  
ATOM   1103  CB  ILE B  39      18.167  86.594  17.668  1.00 96.38           C  
ATOM   1104  N   TYR B  40      15.484  88.567  17.370  1.00119.08           N  
ATOM   1105  CA  TYR B  40      14.942  89.818  16.836  1.00132.64           C  
ATOM   1106  C   TYR B  40      15.627  91.058  17.397  1.00138.42           C  
ATOM   1107  O   TYR B  40      15.522  91.343  18.593  1.00141.70           O  
ATOM   1108  CB  TYR B  40      13.434  89.916  17.134  1.00138.22           C  
ATOM   1109  CG  TYR B  40      12.726  91.172  16.620  1.00144.31           C  
ATOM   1110  CD1 TYR B  40      11.457  91.517  17.092  1.00147.41           C  
ATOM   1111  CD2 TYR B  40      13.321  92.015  15.674  1.00150.16           C  
ATOM   1112  CE1 TYR B  40      10.784  92.648  16.614  1.00150.14           C  
ATOM   1113  CE2 TYR B  40      12.655  93.150  15.189  1.00150.45           C  
ATOM   1114  CZ  TYR B  40      11.396  93.468  15.678  1.00150.51           C  
ATOM   1115  OH  TYR B  40      10.742  94.586  15.209  1.00150.33           O  
ATOM   1116  N   ASP B  41      16.330  91.789  16.536  1.00143.16           N  
ATOM   1117  CA  ASP B  41      16.971  93.027  16.964  1.00146.64           C  
ATOM   1118  C   ASP B  41      15.775  93.934  17.207  1.00148.65           C  
ATOM   1119  O   ASP B  41      15.246  94.505  16.254  1.00149.55           O  
ATOM   1120  CB  ASP B  41      17.806  93.655  15.841  1.00147.46           C  
ATOM   1121  CG  ASP B  41      18.843  92.715  15.273  1.00150.48           C  
ATOM   1122  OD1 ASP B  41      19.749  92.291  16.021  1.00150.52           O  
ATOM   1123  OD2 ASP B  41      18.754  92.410  14.065  1.00150.51           O  
ATOM   1124  N   ARG B  42      15.330  94.064  18.455  1.00149.80           N  
ATOM   1125  CA  ARG B  42      14.175  94.914  18.743  1.00145.26           C  
ATOM   1126  C   ARG B  42      14.286  96.309  18.115  1.00148.06           C  
ATOM   1127  O   ARG B  42      13.401  97.141  18.305  1.00150.16           O  
ATOM   1128  CB  ARG B  42      13.954  95.037  20.261  1.00135.98           C  
ATOM   1129  CG  ARG B  42      13.125  93.904  20.874  1.00124.94           C  
ATOM   1130  CD  ARG B  42      11.723  93.857  20.266  1.00116.05           C  
ATOM   1131  NE  ARG B  42      10.943  92.689  20.677  1.00117.03           N  
ATOM   1132  CZ  ARG B  42       9.695  92.448  20.282  1.00116.72           C  
ATOM   1133  NH1 ARG B  42       9.084  93.292  19.467  1.00121.62           N  
ATOM   1134  NH2 ARG B  42       9.058  91.360  20.697  1.00114.41           N  
ATOM   1135  N   GLN B  43      15.367  96.565  17.373  1.00147.85           N  
ATOM   1136  CA  GLN B  43      15.564  97.858  16.705  1.00147.32           C  
ATOM   1137  C   GLN B  43      16.075  97.719  15.275  1.00149.66           C  
ATOM   1138  O   GLN B  43      17.290  97.756  15.039  1.00149.95           O  
ATOM   1139  CB  GLN B  43      16.546  98.738  17.472  1.00143.99           C  
ATOM   1140  CG  GLN B  43      16.236 100.231  17.340  1.00142.25           C  
ATOM   1141  CD  GLN B  43      15.679 100.624  15.973  1.00137.77           C  
ATOM   1142  OE1 GLN B  43      16.394 100.632  14.972  1.00137.02           O  
ATOM   1143  NE2 GLN B  43      14.390 100.948  15.933  1.00133.32           N  
ATOM   1144  N   THR B  44      15.140  97.606  14.331  1.00150.52           N  
ATOM   1145  CA  THR B  44      15.444  97.451  12.898  1.00150.52           C  
ATOM   1146  C   THR B  44      15.903  96.048  12.535  1.00150.52           C  
ATOM   1147  O   THR B  44      16.150  95.188  13.376  1.00150.52           O  
ATOM   1148  CB  THR B  44      16.498  98.412  12.447  1.00150.52           C  
ATOM   1149  N   GLY B  45      16.034  95.863  11.222  1.00150.52           N  
ATOM   1150  CA  GLY B  45      16.404  94.587  10.649  1.00149.77           C  
ATOM   1151  C   GLY B  45      15.176  93.778  10.958  1.00150.52           C  
ATOM   1152  O   GLY B  45      14.199  94.342  11.440  1.00150.52           O  
ATOM   1153  N   GLU B  46      15.188  92.482  10.699  1.00149.71           N  
ATOM   1154  CA  GLU B  46      14.015  91.688  11.026  1.00147.24           C  
ATOM   1155  C   GLU B  46      14.468  90.532  11.902  1.00143.34           C  
ATOM   1156  O   GLU B  46      15.255  90.742  12.825  1.00137.35           O  
ATOM   1157  CB  GLU B  46      13.308  91.226   9.739  1.00150.28           C  
ATOM   1158  CG  GLU B  46      12.661  92.404   8.980  1.00150.52           C  
ATOM   1159  CD  GLU B  46      11.644  91.990   7.921  1.00150.52           C  
ATOM   1160  OE1 GLU B  46      10.708  91.230   8.252  1.00148.14           O  
ATOM   1161  OE2 GLU B  46      11.771  92.441   6.761  1.00147.98           O  
ATOM   1162  N   TRP B  47      13.980  89.325  11.652  1.00139.10           N  
ATOM   1163  CA  TRP B  47      14.423  88.203  12.466  1.00132.91           C  
ATOM   1164  C   TRP B  47      15.864  87.868  12.091  1.00124.35           C  
ATOM   1165  O   TRP B  47      16.312  88.164  10.984  1.00128.91           O  
ATOM   1166  CB  TRP B  47      13.527  86.981  12.253  1.00137.22           C  
ATOM   1167  CG  TRP B  47      12.279  86.972  13.094  1.00134.03           C  
ATOM   1168  CD1 TRP B  47      10.992  87.085  12.652  1.00133.25           C  
ATOM   1169  CD2 TRP B  47      12.197  86.759  14.512  1.00133.87           C  
ATOM   1170  NE1 TRP B  47      10.115  86.951  13.702  1.00137.71           N  
ATOM   1171  CE2 TRP B  47      10.829  86.756  14.856  1.00135.96           C  
ATOM   1172  CE3 TRP B  47      13.151  86.582  15.526  1.00132.40           C  
ATOM   1173  CZ2 TRP B  47      10.385  86.560  16.171  1.00135.12           C  
ATOM   1174  CZ3 TRP B  47      12.707  86.390  16.836  1.00131.69           C  
ATOM   1175  CH2 TRP B  47      11.336  86.388  17.144  1.00133.13           C  
ATOM   1176  N   LYS B  48      16.590  87.258  13.018  1.00115.23           N  
ATOM   1177  CA  LYS B  48      17.968  86.908  12.748  1.00 98.34           C  
ATOM   1178  C   LYS B  48      18.291  85.498  13.188  1.00 96.95           C  
ATOM   1179  O   LYS B  48      17.673  84.966  14.109  1.00 81.20           O  
ATOM   1180  N   ASP B  49      19.263  84.890  12.517  1.00 94.20           N  
ATOM   1181  CA  ASP B  49      19.694  83.534  12.831  1.00 97.15           C  
ATOM   1182  C   ASP B  49      20.620  83.544  14.044  1.00102.73           C  
ATOM   1183  O   ASP B  49      21.830  83.712  13.903  1.00115.13           O  
ATOM   1184  CB  ASP B  49      20.433  82.930  11.635  1.00 99.14           C  
ATOM   1185  CG  ASP B  49      19.510  82.617  10.474  1.00105.14           C  
ATOM   1186  OD1 ASP B  49      18.589  83.419  10.209  1.00113.20           O  
ATOM   1187  OD2 ASP B  49      19.715  81.573   9.817  1.00101.91           O  
ATOM   1188  N   GLY B  50      20.051  83.363  15.232  1.00101.71           N  
ATOM   1189  CA  GLY B  50      20.850  83.356  16.447  1.00 86.35           C  
ATOM   1190  C   GLY B  50      21.825  82.194  16.518  1.00 83.39           C  
ATOM   1191  O   GLY B  50      22.030  81.482  15.532  1.00 80.16           O  
ATOM   1192  N   GLU B  51      22.422  81.997  17.691  1.00 76.75           N  
ATOM   1193  CA  GLU B  51      23.383  80.918  17.875  1.00 86.30           C  
ATOM   1194  C   GLU B  51      22.839  79.498  17.760  1.00 82.05           C  
ATOM   1195  O   GLU B  51      21.996  79.074  18.558  1.00 84.56           O  
ATOM   1196  N   ALA B  52      23.348  78.753  16.780  1.00 69.52           N  
ATOM   1197  CA  ALA B  52      22.918  77.378  16.531  1.00 61.39           C  
ATOM   1198  C   ALA B  52      23.431  76.338  17.527  1.00 62.91           C  
ATOM   1199  O   ALA B  52      24.504  76.483  18.118  1.00 53.93           O  
ATOM   1200  CB  ALA B  52      23.310  76.963  15.124  1.00 49.38           C  
ATOM   1201  N   LEU B  53      22.640  75.277  17.686  1.00 61.49           N  
ATOM   1202  CA  LEU B  53      22.948  74.167  18.581  1.00 47.89           C  
ATOM   1203  C   LEU B  53      23.295  72.935  17.734  1.00 46.44           C  
ATOM   1204  O   LEU B  53      22.599  72.621  16.770  1.00 45.39           O  
ATOM   1205  CB  LEU B  53      21.730  73.874  19.465  1.00 41.27           C  
ATOM   1206  CG  LEU B  53      21.830  72.768  20.520  1.00 52.58           C  
ATOM   1207  CD1 LEU B  53      22.965  73.059  21.484  1.00 58.38           C  
ATOM   1208  CD2 LEU B  53      20.518  72.671  21.270  1.00 45.87           C  
ATOM   1209  N   PHE B  54      24.379  72.248  18.073  1.00 41.75           N  
ATOM   1210  CA  PHE B  54      24.764  71.061  17.319  1.00 41.33           C  
ATOM   1211  C   PHE B  54      24.617  69.829  18.186  1.00 46.98           C  
ATOM   1212  O   PHE B  54      25.301  69.694  19.202  1.00 52.31           O  
ATOM   1213  CB  PHE B  54      26.207  71.166  16.819  1.00 43.72           C  
ATOM   1214  CG  PHE B  54      26.384  72.120  15.672  1.00 59.06           C  
ATOM   1215  CD1 PHE B  54      26.523  73.485  15.896  1.00 66.96           C  
ATOM   1216  CD2 PHE B  54      26.387  71.655  14.360  1.00 58.87           C  
ATOM   1217  CE1 PHE B  54      26.663  74.375  14.829  1.00 58.49           C  
ATOM   1218  CE2 PHE B  54      26.526  72.538  13.285  1.00 67.60           C  
ATOM   1219  CZ  PHE B  54      26.663  73.901  13.522  1.00 56.47           C  
ATOM   1220  N   LEU B  55      23.716  68.934  17.793  1.00 44.69           N  
ATOM   1221  CA  LEU B  55      23.498  67.717  18.557  1.00 44.74           C  
ATOM   1222  C   LEU B  55      23.728  66.482  17.710  1.00 51.31           C  
ATOM   1223  O   LEU B  55      23.093  66.315  16.667  1.00 51.68           O  
ATOM   1224  CB  LEU B  55      22.082  67.696  19.125  1.00 42.85           C  
ATOM   1225  CG  LEU B  55      21.875  68.556  20.365  1.00 42.88           C  
ATOM   1226  CD1 LEU B  55      20.396  68.692  20.676  1.00 45.78           C  
ATOM   1227  CD2 LEU B  55      22.617  67.929  21.520  1.00 38.34           C  
ATOM   1228  N   ARG B  56      24.648  65.626  18.149  1.00 50.76           N  
ATOM   1229  CA  ARG B  56      24.919  64.403  17.416  1.00 45.89           C  
ATOM   1230  C   ARG B  56      23.847  63.407  17.829  1.00 58.60           C  
ATOM   1231  O   ARG B  56      23.465  63.329  19.006  1.00 51.85           O  
ATOM   1232  CB  ARG B  56      26.302  63.839  17.747  1.00 40.29           C  
ATOM   1233  CG  ARG B  56      26.662  62.603  16.898  1.00 67.28           C  
ATOM   1234  CD  ARG B  56      27.785  62.879  15.886  1.00 72.90           C  
ATOM   1235  NE  ARG B  56      27.418  62.539  14.507  1.00 79.03           N  
ATOM   1236  CZ  ARG B  56      28.207  62.726  13.449  1.00 85.45           C  
ATOM   1237  NH1 ARG B  56      29.417  63.251  13.602  1.00 85.73           N  
ATOM   1238  NH2 ARG B  56      27.791  62.393  12.233  1.00 89.85           N  
ATOM   1239  N   CYS B  57      23.360  62.652  16.854  1.00 49.33           N  
ATOM   1240  CA  CYS B  57      22.324  61.671  17.104  1.00 50.93           C  
ATOM   1241  C   CYS B  57      22.653  60.328  16.469  1.00 56.13           C  
ATOM   1242  O   CYS B  57      23.154  60.274  15.347  1.00 68.51           O  
ATOM   1243  CB  CYS B  57      20.996  62.153  16.521  1.00 45.35           C  
ATOM   1244  SG  CYS B  57      20.494  63.797  16.981  1.00 56.23           S  
ATOM   1245  N   ASN B  58      22.369  59.248  17.189  1.00 52.36           N  
ATOM   1246  CA  ASN B  58      22.567  57.911  16.656  1.00 53.32           C  
ATOM   1247  C   ASN B  58      21.231  57.186  16.742  1.00 54.59           C  
ATOM   1248  O   ASN B  58      20.600  57.138  17.796  1.00 54.67           O  
ATOM   1249  CB  ASN B  58      23.642  57.131  17.422  1.00 60.80           C  
ATOM   1250  CG  ASN B  58      23.917  57.692  18.797  1.00 57.37           C  
ATOM   1251  OD1 ASN B  58      24.691  58.636  18.950  1.00 55.67           O  
ATOM   1252  ND2 ASN B  58      23.289  57.111  19.810  1.00 68.12           N  
ATOM   1253  N   ILE B  59      20.794  56.649  15.610  1.00 57.66           N  
ATOM   1254  CA  ILE B  59      19.532  55.924  15.522  1.00 46.98           C  
ATOM   1255  C   ILE B  59      19.902  54.476  15.233  1.00 49.55           C  
ATOM   1256  O   ILE B  59      20.902  54.207  14.569  1.00 36.99           O  
ATOM   1257  CB  ILE B  59      18.636  56.524  14.397  1.00 45.08           C  
ATOM   1258  CG1 ILE B  59      17.231  55.934  14.463  1.00 53.56           C  
ATOM   1259  CG2 ILE B  59      19.272  56.308  13.045  1.00 47.95           C  
ATOM   1260  CD1 ILE B  59      16.230  56.661  13.578  1.00 48.70           C  
ATOM   1261  N   TRP B  60      19.096  53.546  15.729  1.00 56.59           N  
ATOM   1262  CA  TRP B  60      19.388  52.129  15.578  1.00 52.10           C  
ATOM   1263  C   TRP B  60      18.488  51.256  14.718  1.00 52.36           C  
ATOM   1264  O   TRP B  60      17.351  51.605  14.404  1.00 52.34           O  
ATOM   1265  CB  TRP B  60      19.463  51.509  16.964  1.00 49.23           C  
ATOM   1266  CG  TRP B  60      20.829  51.202  17.407  1.00 57.23           C  
ATOM   1267  CD1 TRP B  60      21.590  50.127  17.045  1.00 63.06           C  
ATOM   1268  CD2 TRP B  60      21.618  51.961  18.319  1.00 61.94           C  
ATOM   1269  NE1 TRP B  60      22.803  50.166  17.684  1.00 68.63           N  
ATOM   1270  CE2 TRP B  60      22.843  51.282  18.473  1.00 79.40           C  
ATOM   1271  CE3 TRP B  60      21.396  53.148  19.026  1.00 71.96           C  
ATOM   1272  CZ2 TRP B  60      23.859  51.761  19.305  1.00 90.47           C  
ATOM   1273  CZ3 TRP B  60      22.407  53.623  19.854  1.00 82.35           C  
ATOM   1274  CH2 TRP B  60      23.622  52.927  19.990  1.00 92.45           C  
ATOM   1275  N   ARG B  61      19.033  50.092  14.371  1.00 58.05           N  
ATOM   1276  CA  ARG B  61      18.350  49.071  13.585  1.00 46.37           C  
ATOM   1277  C   ARG B  61      17.822  49.531  12.238  1.00 44.76           C  
ATOM   1278  O   ARG B  61      18.484  50.253  11.493  1.00 48.59           O  
ATOM   1279  CB  ARG B  61      17.189  48.470  14.383  1.00 51.78           C  
ATOM   1280  CG  ARG B  61      17.517  48.039  15.806  1.00 51.54           C  
ATOM   1281  CD  ARG B  61      18.677  47.066  15.870  1.00 47.37           C  
ATOM   1282  NE  ARG B  61      18.857  46.501  17.210  1.00 66.53           N  
ATOM   1283  CZ  ARG B  61      18.898  47.207  18.340  1.00 67.20           C  
ATOM   1284  NH1 ARG B  61      18.764  48.526  18.321  1.00 76.11           N  
ATOM   1285  NH2 ARG B  61      19.090  46.592  19.498  1.00 83.64           N  
ATOM   1286  N   GLU B  62      16.603  49.106  11.941  1.00 36.45           N  
ATOM   1287  CA  GLU B  62      15.976  49.426  10.675  1.00 46.31           C  
ATOM   1288  C   GLU B  62      15.660  50.905  10.549  1.00 48.95           C  
ATOM   1289  O   GLU B  62      15.612  51.445   9.447  1.00 50.06           O  
ATOM   1290  CB  GLU B  62      14.728  48.554  10.501  1.00 43.14           C  
ATOM   1291  CG  GLU B  62      15.061  47.040  10.501  1.00 48.19           C  
ATOM   1292  CD  GLU B  62      16.132  46.648   9.468  1.00 56.00           C  
ATOM   1293  OE1 GLU B  62      15.826  46.731   8.254  1.00 61.54           O  
ATOM   1294  OE2 GLU B  62      17.277  46.267   9.861  1.00 21.95           O  
ATOM   1295  N   ALA B  63      15.471  51.565  11.685  1.00 52.81           N  
ATOM   1296  CA  ALA B  63      15.187  52.987  11.683  1.00 37.92           C  
ATOM   1297  C   ALA B  63      16.391  53.668  11.050  1.00 49.20           C  
ATOM   1298  O   ALA B  63      16.241  54.525  10.173  1.00 42.71           O  
ATOM   1299  CB  ALA B  63      14.985  53.485  13.097  1.00 42.86           C  
ATOM   1300  N   ALA B  64      17.581  53.271  11.505  1.00 37.91           N  
ATOM   1301  CA  ALA B  64      18.837  53.809  10.987  1.00 36.27           C  
ATOM   1302  C   ALA B  64      18.925  53.591   9.479  1.00 37.95           C  
ATOM   1303  O   ALA B  64      19.222  54.516   8.727  1.00 42.34           O  
ATOM   1304  CB  ALA B  64      20.019  53.137  11.675  1.00 21.68           C  
ATOM   1305  N   GLU B  65      18.669  52.359   9.050  1.00 35.57           N  
ATOM   1306  CA  GLU B  65      18.707  52.008   7.638  1.00 41.52           C  
ATOM   1307  C   GLU B  65      17.703  52.903   6.922  1.00 44.08           C  
ATOM   1308  O   GLU B  65      17.959  53.401   5.832  1.00 42.04           O  
ATOM   1309  CB  GLU B  65      18.347  50.520   7.454  1.00 44.18           C  
ATOM   1310  CG  GLU B  65      19.435  49.524   7.929  1.00 60.18           C  
ATOM   1311  CD  GLU B  65      18.972  48.061   7.934  1.00 61.48           C  
ATOM   1312  OE1 GLU B  65      18.370  47.620   6.936  1.00 87.71           O  
ATOM   1313  OE2 GLU B  65      19.211  47.343   8.929  1.00 56.73           O  
ATOM   1314  N   ASN B  66      16.562  53.121   7.560  1.00 43.18           N  
ATOM   1315  CA  ASN B  66      15.530  53.971   6.988  1.00 42.97           C  
ATOM   1316  C   ASN B  66      16.037  55.399   6.864  1.00 45.99           C  
ATOM   1317  O   ASN B  66      15.675  56.117   5.938  1.00 51.10           O  
ATOM   1318  CB  ASN B  66      14.285  53.937   7.867  1.00 54.46           C  
ATOM   1319  CG  ASN B  66      13.607  52.594   7.847  1.00 54.07           C  
ATOM   1320  OD1 ASN B  66      13.270  52.085   6.784  1.00 50.88           O  
ATOM   1321  ND2 ASN B  66      13.399  52.010   9.021  1.00 60.73           N  
ATOM   1322  N   VAL B  67      16.872  55.808   7.813  1.00 52.23           N  
ATOM   1323  CA  VAL B  67      17.453  57.138   7.799  1.00 49.87           C  
ATOM   1324  C   VAL B  67      18.410  57.226   6.613  1.00 53.14           C  
ATOM   1325  O   VAL B  67      18.238  58.055   5.720  1.00 53.39           O  
ATOM   1326  CB  VAL B  67      18.247  57.419   9.100  1.00 56.39           C  
ATOM   1327  CG1 VAL B  67      18.986  58.736   8.979  1.00 53.06           C  
ATOM   1328  CG2 VAL B  67      17.302  57.459  10.298  1.00 52.83           C  
ATOM   1329  N   ALA B  68      19.412  56.353   6.609  1.00 48.95           N  
ATOM   1330  CA  ALA B  68      20.414  56.316   5.550  1.00 46.26           C  
ATOM   1331  C   ALA B  68      19.821  56.374   4.148  1.00 49.65           C  
ATOM   1332  O   ALA B  68      20.374  57.020   3.265  1.00 57.35           O  
ATOM   1333  CB  ALA B  68      21.271  55.063   5.692  1.00 36.41           C  
ATOM   1334  N   GLU B  69      18.690  55.706   3.954  1.00 57.29           N  
ATOM   1335  CA  GLU B  69      18.032  55.648   2.653  1.00 50.49           C  
ATOM   1336  C   GLU B  69      17.035  56.768   2.407  1.00 49.38           C  
ATOM   1337  O   GLU B  69      16.524  56.913   1.302  1.00 56.30           O  
ATOM   1338  CB  GLU B  69      17.316  54.298   2.509  1.00 57.91           C  
ATOM   1339  CG  GLU B  69      16.611  54.084   1.174  1.00 64.71           C  
ATOM   1340  CD  GLU B  69      15.928  52.727   1.073  1.00 67.79           C  
ATOM   1341  OE1 GLU B  69      15.325  52.441   0.013  1.00 67.94           O  
ATOM   1342  OE2 GLU B  69      15.992  51.951   2.051  1.00 46.77           O  
ATOM   1343  N   SER B  70      16.763  57.579   3.419  1.00 56.03           N  
ATOM   1344  CA  SER B  70      15.775  58.636   3.243  1.00 48.37           C  
ATOM   1345  C   SER B  70      16.269  60.071   3.400  1.00 51.69           C  
ATOM   1346  O   SER B  70      15.779  60.973   2.722  1.00 59.33           O  
ATOM   1347  CB  SER B  70      14.606  58.401   4.213  1.00 46.37           C  
ATOM   1348  OG  SER B  70      14.188  57.039   4.217  1.00 37.98           O  
ATOM   1349  N   LEU B  71      17.244  60.282   4.278  1.00 51.35           N  
ATOM   1350  CA  LEU B  71      17.736  61.625   4.548  1.00 46.92           C  
ATOM   1351  C   LEU B  71      19.139  61.970   4.050  1.00 55.27           C  
ATOM   1352  O   LEU B  71      20.056  61.148   4.084  1.00 56.47           O  
ATOM   1353  CB  LEU B  71      17.665  61.878   6.056  1.00 50.76           C  
ATOM   1354  CG  LEU B  71      16.343  61.546   6.748  1.00 43.50           C  
ATOM   1355  CD1 LEU B  71      16.495  61.821   8.242  1.00 63.93           C  
ATOM   1356  CD2 LEU B  71      15.208  62.384   6.159  1.00 26.77           C  
ATOM   1357  N   THR B  72      19.301  63.216   3.619  1.00 56.81           N  
ATOM   1358  CA  THR B  72      20.582  63.694   3.119  1.00 64.68           C  
ATOM   1359  C   THR B  72      21.001  65.049   3.684  1.00 67.73           C  
ATOM   1360  O   THR B  72      20.343  65.595   4.568  1.00 77.30           O  
ATOM   1361  CB  THR B  72      20.585  63.747   1.581  1.00 49.33           C  
ATOM   1362  OG1 THR B  72      19.292  64.143   1.106  1.00 52.20           O  
ATOM   1363  CG2 THR B  72      20.934  62.381   1.018  1.00 38.17           C  
ATOM   1364  N   ARG B  73      22.103  65.582   3.165  1.00 70.47           N  
ATOM   1365  CA  ARG B  73      22.659  66.849   3.630  1.00 59.16           C  
ATOM   1366  C   ARG B  73      21.694  68.020   3.689  1.00 63.11           C  
ATOM   1367  O   ARG B  73      20.908  68.261   2.760  1.00 55.25           O  
ATOM   1368  CB  ARG B  73      23.854  67.253   2.763  1.00 72.51           C  
ATOM   1369  CG  ARG B  73      24.639  68.441   3.306  1.00 71.14           C  
ATOM   1370  CD  ARG B  73      25.439  69.127   2.213  1.00 71.01           C  
ATOM   1371  NE  ARG B  73      26.273  68.191   1.461  1.00 92.32           N  
ATOM   1372  CZ  ARG B  73      26.291  68.101   0.132  1.00 95.54           C  
ATOM   1373  NH1 ARG B  73      25.519  68.890  -0.606  1.00 89.04           N  
ATOM   1374  NH2 ARG B  73      27.085  67.223  -0.466  1.00 95.73           N  
ATOM   1375  N   GLY B  74      21.776  68.753   4.796  1.00 57.31           N  
ATOM   1376  CA  GLY B  74      20.945  69.926   4.984  1.00 57.05           C  
ATOM   1377  C   GLY B  74      19.450  69.704   5.036  1.00 56.14           C  
ATOM   1378  O   GLY B  74      18.684  70.666   4.969  1.00 58.85           O  
ATOM   1379  N   ALA B  75      19.024  68.451   5.156  1.00 50.49           N  
ATOM   1380  CA  ALA B  75      17.601  68.149   5.232  1.00 45.87           C  
ATOM   1381  C   ALA B  75      17.064  68.620   6.581  1.00 53.51           C  
ATOM   1382  O   ALA B  75      17.732  68.475   7.607  1.00 63.92           O  
ATOM   1383  CB  ALA B  75      17.378  66.651   5.079  1.00 33.10           C  
ATOM   1384  N   ARG B  76      15.867  69.195   6.585  1.00 49.22           N  
ATOM   1385  CA  ARG B  76      15.273  69.661   7.829  1.00 31.10           C  
ATOM   1386  C   ARG B  76      14.578  68.451   8.414  1.00 43.79           C  
ATOM   1387  O   ARG B  76      13.858  67.747   7.707  1.00 36.18           O  
ATOM   1388  CB  ARG B  76      14.256  70.771   7.563  1.00 45.23           C  
ATOM   1389  CG  ARG B  76      13.801  71.533   8.808  1.00 31.46           C  
ATOM   1390  CD  ARG B  76      13.165  72.855   8.407  1.00 28.69           C  
ATOM   1391  NE  ARG B  76      13.548  73.925   9.321  1.00 47.89           N  
ATOM   1392  CZ  ARG B  76      12.965  74.148  10.494  1.00 42.33           C  
ATOM   1393  NH1 ARG B  76      13.377  75.140  11.271  1.00 55.28           N  
ATOM   1394  NH2 ARG B  76      11.953  73.388  10.883  1.00 55.95           N  
ATOM   1395  N   VAL B  77      14.795  68.194   9.699  1.00 26.58           N  
ATOM   1396  CA  VAL B  77      14.169  67.038  10.306  1.00 34.46           C  
ATOM   1397  C   VAL B  77      13.643  67.279  11.720  1.00 46.01           C  
ATOM   1398  O   VAL B  77      14.045  68.221  12.409  1.00 48.83           O  
ATOM   1399  CB  VAL B  77      15.163  65.854  10.324  1.00 43.36           C  
ATOM   1400  CG1 VAL B  77      15.556  65.483   8.907  1.00 34.92           C  
ATOM   1401  CG2 VAL B  77      16.405  66.222  11.114  1.00 34.70           C  
ATOM   1402  N   ILE B  78      12.720  66.425  12.137  1.00 43.83           N  
ATOM   1403  CA  ILE B  78      12.159  66.506  13.475  1.00 48.53           C  
ATOM   1404  C   ILE B  78      12.725  65.292  14.203  1.00 47.60           C  
ATOM   1405  O   ILE B  78      12.663  64.171  13.697  1.00 46.58           O  
ATOM   1406  CB  ILE B  78      10.608  66.428  13.455  1.00 38.58           C  
ATOM   1407  CG1 ILE B  78      10.070  67.349  12.361  1.00 37.16           C  
ATOM   1408  CG2 ILE B  78      10.037  66.846  14.833  1.00 21.63           C  
ATOM   1409  CD1 ILE B  78       8.582  67.678  12.481  1.00 46.11           C  
ATOM   1410  N   VAL B  79      13.292  65.507  15.381  1.00 40.51           N  
ATOM   1411  CA  VAL B  79      13.863  64.395  16.124  1.00 39.93           C  
ATOM   1412  C   VAL B  79      13.338  64.308  17.538  1.00 42.73           C  
ATOM   1413  O   VAL B  79      13.453  65.255  18.317  1.00 47.89           O  
ATOM   1414  CB  VAL B  79      15.412  64.500  16.190  1.00 42.21           C  
ATOM   1415  CG1 VAL B  79      15.976  63.481  17.171  1.00 19.38           C  
ATOM   1416  CG2 VAL B  79      16.010  64.287  14.803  1.00 28.96           C  
ATOM   1417  N   SER B  80      12.746  63.168  17.861  1.00 38.63           N  
ATOM   1418  CA  SER B  80      12.260  62.930  19.211  1.00 43.43           C  
ATOM   1419  C   SER B  80      13.229  61.885  19.754  1.00 39.46           C  
ATOM   1420  O   SER B  80      13.419  60.848  19.136  1.00 36.40           O  
ATOM   1421  CB  SER B  80      10.837  62.368  19.187  1.00 50.47           C  
ATOM   1422  OG  SER B  80      10.307  62.257  20.497  1.00 54.33           O  
ATOM   1423  N   GLY B  81      13.860  62.154  20.889  1.00 34.53           N  
ATOM   1424  CA  GLY B  81      14.801  61.186  21.415  1.00 33.43           C  
ATOM   1425  C   GLY B  81      15.144  61.329  22.884  1.00 32.46           C  
ATOM   1426  O   GLY B  81      14.524  62.101  23.609  1.00 39.43           O  
ATOM   1427  N   ARG B  82      16.143  60.573  23.320  1.00 27.66           N  
ATOM   1428  CA  ARG B  82      16.572  60.585  24.709  1.00 46.87           C  
ATOM   1429  C   ARG B  82      18.023  60.996  24.820  1.00 48.26           C  
ATOM   1430  O   ARG B  82      18.877  60.508  24.080  1.00 45.59           O  
ATOM   1431  CB  ARG B  82      16.377  59.194  25.327  1.00 48.60           C  
ATOM   1432  CG  ARG B  82      14.915  58.781  25.441  1.00 49.59           C  
ATOM   1433  CD  ARG B  82      14.742  57.290  25.649  1.00 59.93           C  
ATOM   1434  NE  ARG B  82      14.989  56.500  24.436  1.00 66.56           N  
ATOM   1435  CZ  ARG B  82      16.131  55.874  24.152  1.00 58.35           C  
ATOM   1436  NH1 ARG B  82      17.162  55.930  24.984  1.00 60.60           N  
ATOM   1437  NH2 ARG B  82      16.240  55.175  23.033  1.00 53.29           N  
ATOM   1438  N   LEU B  83      18.294  61.904  25.750  1.00 52.82           N  
ATOM   1439  CA  LEU B  83      19.642  62.384  25.970  1.00 51.04           C  
ATOM   1440  C   LEU B  83      20.457  61.310  26.662  1.00 48.83           C  
ATOM   1441  O   LEU B  83      20.016  60.707  27.642  1.00 46.82           O  
ATOM   1442  CB  LEU B  83      19.630  63.654  26.826  1.00 42.09           C  
ATOM   1443  CG  LEU B  83      18.934  64.866  26.214  1.00 44.39           C  
ATOM   1444  CD1 LEU B  83      19.173  66.085  27.104  1.00 31.07           C  
ATOM   1445  CD2 LEU B  83      19.466  65.110  24.793  1.00 40.51           C  
ATOM   1446  N   LYS B  84      21.649  61.077  26.126  1.00 57.97           N  
ATOM   1447  CA  LYS B  84      22.580  60.092  26.659  1.00 62.90           C  
ATOM   1448  C   LYS B  84      23.942  60.764  26.775  1.00 60.84           C  
ATOM   1449  O   LYS B  84      24.389  61.447  25.852  1.00 58.35           O  
ATOM   1450  CB  LYS B  84      22.681  58.891  25.719  1.00 61.16           C  
ATOM   1451  CG  LYS B  84      22.219  57.594  26.334  1.00 77.86           C  
ATOM   1452  CD  LYS B  84      20.749  57.649  26.701  1.00 77.11           C  
ATOM   1453  CE  LYS B  84      20.295  56.320  27.279  1.00 75.01           C  
ATOM   1454  NZ  LYS B  84      18.835  56.303  27.520  1.00 50.86           N  
ATOM   1455  N   GLN B  85      24.598  60.569  27.909  1.00 63.74           N  
ATOM   1456  CA  GLN B  85      25.901  61.172  28.136  1.00 66.68           C  
ATOM   1457  C   GLN B  85      27.014  60.132  28.042  1.00 70.14           C  
ATOM   1458  O   GLN B  85      27.178  59.309  28.945  1.00 73.36           O  
ATOM   1459  CB  GLN B  85      25.908  61.826  29.516  1.00 68.77           C  
ATOM   1460  CG  GLN B  85      27.118  62.687  29.832  1.00 64.50           C  
ATOM   1461  CD  GLN B  85      26.910  63.497  31.099  1.00 57.07           C  
ATOM   1462  OE1 GLN B  85      25.989  64.310  31.179  1.00 45.71           O  
ATOM   1463  NE2 GLN B  85      27.756  63.273  32.098  1.00 61.27           N  
ATOM   1464  N   ARG B  86      27.770  60.156  26.947  1.00 66.53           N  
ATOM   1465  CA  ARG B  86      28.875  59.217  26.785  1.00 78.06           C  
ATOM   1466  C   ARG B  86      30.064  59.648  27.630  1.00 84.07           C  
ATOM   1467  O   ARG B  86      29.996  60.634  28.363  1.00 95.10           O  
ATOM   1468  CB  ARG B  86      29.355  59.156  25.340  1.00 81.56           C  
ATOM   1469  CG  ARG B  86      28.489  58.413  24.360  1.00 96.76           C  
ATOM   1470  CD  ARG B  86      29.357  58.035  23.166  1.00105.28           C  
ATOM   1471  NE  ARG B  86      30.161  59.166  22.703  1.00113.38           N  
ATOM   1472  CZ  ARG B  86      31.216  59.057  21.900  1.00126.43           C  
ATOM   1473  NH1 ARG B  86      31.603  57.863  21.467  1.00133.95           N  
ATOM   1474  NH2 ARG B  86      31.882  60.141  21.524  1.00131.78           N  
ATOM   1475  N   SER B  87      31.162  58.909  27.497  1.00 86.95           N  
ATOM   1476  CA  SER B  87      32.394  59.202  28.223  1.00 90.58           C  
ATOM   1477  C   SER B  87      33.608  58.782  27.405  1.00 98.33           C  
ATOM   1478  O   SER B  87      33.869  57.590  27.246  1.00 97.44           O  
ATOM   1479  CB  SER B  87      32.428  58.461  29.562  1.00 75.40           C  
ATOM   1480  OG  SER B  87      31.344  58.838  30.389  1.00 85.10           O  
ATOM   1481  N   PHE B  88      34.341  59.758  26.877  1.00109.08           N  
ATOM   1482  CA  PHE B  88      35.542  59.463  26.106  1.00120.65           C  
ATOM   1483  C   PHE B  88      36.713  60.152  26.804  1.00125.25           C  
ATOM   1484  O   PHE B  88      36.565  61.255  27.337  1.00132.51           O  
ATOM   1485  CB  PHE B  88      35.380  59.916  24.639  1.00125.22           C  
ATOM   1486  CG  PHE B  88      35.627  61.387  24.396  1.00133.06           C  
ATOM   1487  CD1 PHE B  88      35.143  62.357  25.271  1.00137.46           C  
ATOM   1488  CD2 PHE B  88      36.312  61.801  23.255  1.00135.75           C  
ATOM   1489  CE1 PHE B  88      35.343  63.714  25.017  1.00138.98           C  
ATOM   1490  CE2 PHE B  88      36.516  63.155  22.991  1.00139.41           C  
ATOM   1491  CZ  PHE B  88      36.029  64.114  23.873  1.00138.24           C  
ATOM   1492  N   GLU B  89      37.870  59.498  26.825  1.00127.00           N  
ATOM   1493  CA  GLU B  89      39.017  60.071  27.511  1.00118.33           C  
ATOM   1494  C   GLU B  89      40.094  60.695  26.623  1.00116.93           C  
ATOM   1495  O   GLU B  89      40.501  60.148  25.594  1.00106.30           O  
ATOM   1496  CB  GLU B  89      39.610  59.029  28.472  1.00116.59           C  
ATOM   1497  CG  GLU B  89      38.577  58.535  29.502  1.00108.84           C  
ATOM   1498  CD  GLU B  89      39.136  57.555  30.520  1.00102.09           C  
ATOM   1499  OE1 GLU B  89      39.678  56.504  30.121  1.00104.18           O  
ATOM   1500  OE2 GLU B  89      39.020  57.835  31.729  1.00 99.40           O  
ATOM   1501  N   THR B  90      40.505  61.877  27.073  1.00119.49           N  
ATOM   1502  CA  THR B  90      41.498  62.769  26.477  1.00129.06           C  
ATOM   1503  C   THR B  90      42.729  62.186  25.787  1.00139.36           C  
ATOM   1504  O   THR B  90      42.743  61.036  25.349  1.00145.05           O  
ATOM   1505  CB  THR B  90      41.994  63.740  27.559  1.00124.75           C  
ATOM   1506  OG1 THR B  90      42.730  63.007  28.547  1.00118.89           O  
ATOM   1507  CG2 THR B  90      40.816  64.405  28.246  1.00119.57           C  
ATOM   1508  N   ARG B  91      43.756  63.030  25.684  1.00147.08           N  
ATOM   1509  CA  ARG B  91      45.044  62.679  25.092  1.00148.63           C  
ATOM   1510  C   ARG B  91      44.948  62.204  23.650  1.00150.52           C  
ATOM   1511  O   ARG B  91      45.457  61.102  23.357  1.00150.47           O  
ATOM   1512  CB  ARG B  91      45.711  61.609  25.955  1.00149.48           C  
ATOM   1513  CG  ARG B  91      45.801  62.013  27.413  1.00147.78           C  
ATOM   1514  CD  ARG B  91      45.512  60.847  28.331  1.00148.25           C  
ATOM   1515  NE  ARG B  91      45.273  61.297  29.699  1.00149.28           N  
ATOM   1516  CZ  ARG B  91      44.993  60.485  30.712  1.00150.52           C  
ATOM   1517  NH1 ARG B  91      44.918  59.175  30.510  1.00150.52           N  
ATOM   1518  NH2 ARG B  91      44.785  60.981  31.925  1.00150.52           N  
ATOM   1519  N   LYS B  95      39.309  61.876  31.588  1.00 89.42           N  
ATOM   1520  CA  LYS B  95      37.869  62.095  31.654  1.00 91.39           C  
ATOM   1521  C   LYS B  95      37.406  62.935  30.468  1.00 98.13           C  
ATOM   1522  O   LYS B  95      38.308  63.490  29.731  1.00 98.96           O  
ATOM   1523  CB  LYS B  95      37.538  62.744  33.051  1.00 79.14           C  
ATOM   1524  N   ARG B  96      36.099  62.971  30.180  1.00103.74           N  
ATOM   1525  CA  ARG B  96      35.578  63.737  29.071  1.00106.62           C  
ATOM   1526  C   ARG B  96      34.111  63.388  28.953  1.00104.53           C  
ATOM   1527  O   ARG B  96      33.821  62.223  28.656  1.00111.21           O  
ATOM   1528  N   THR B  97      33.119  64.190  29.292  1.00 94.14           N  
ATOM   1529  CA  THR B  97      31.876  63.523  28.891  1.00 76.57           C  
ATOM   1530  C   THR B  97      31.246  64.349  27.777  1.00 69.17           C  
ATOM   1531  O   THR B  97      31.562  65.534  27.652  1.00 78.02           O  
ATOM   1532  CB  THR B  97      30.893  63.261  29.978  1.00 59.16           C  
ATOM   1533  N   VAL B  98      30.390  63.744  26.946  1.00 66.06           N  
ATOM   1534  CA  VAL B  98      29.707  64.455  25.862  1.00 56.39           C  
ATOM   1535  C   VAL B  98      28.227  64.051  25.823  1.00 52.16           C  
ATOM   1536  O   VAL B  98      27.873  62.924  26.158  1.00 61.28           O  
ATOM   1537  CB  VAL B  98      30.378  64.182  24.508  1.00 65.77           C  
ATOM   1538  CG1 VAL B  98      29.553  64.770  23.370  1.00 78.56           C  
ATOM   1539  CG2 VAL B  98      31.762  64.806  24.512  1.00 77.71           C  
ATOM   1540  N   ILE B  99      27.366  64.983  25.422  1.00 56.15           N  
ATOM   1541  CA  ILE B  99      25.925  64.744  25.373  1.00 60.07           C  
ATOM   1542  C   ILE B  99      25.360  64.590  23.965  1.00 60.17           C  
ATOM   1543  O   ILE B  99      25.382  65.526  23.165  1.00 47.90           O  
ATOM   1544  CB  ILE B  99      25.170  65.885  26.088  1.00 66.40           C  
ATOM   1545  CG1 ILE B  99      25.502  65.852  27.581  1.00 74.82           C  
ATOM   1546  CG2 ILE B  99      23.669  65.757  25.856  1.00 59.91           C  
ATOM   1547  CD1 ILE B  99      25.163  67.125  28.316  1.00 82.66           C  
ATOM   1548  N   GLU B 100      24.841  63.403  23.677  1.00 49.32           N  
ATOM   1549  CA  GLU B 100      24.265  63.128  22.375  1.00 61.27           C  
ATOM   1550  C   GLU B 100      22.856  62.584  22.499  1.00 64.29           C  
ATOM   1551  O   GLU B 100      22.406  62.237  23.591  1.00 63.52           O  
ATOM   1552  CB  GLU B 100      25.146  62.152  21.590  1.00 73.77           C  
ATOM   1553  CG  GLU B 100      25.897  61.142  22.435  1.00 85.59           C  
ATOM   1554  CD  GLU B 100      26.800  60.253  21.596  1.00 98.64           C  
ATOM   1555  OE1 GLU B 100      27.565  60.793  20.766  1.00 97.41           O  
ATOM   1556  OE2 GLU B 100      26.749  59.016  21.770  1.00112.12           O  
ATOM   1557  N   VAL B 101      22.164  62.507  21.368  1.00 60.15           N  
ATOM   1558  CA  VAL B 101      20.787  62.040  21.344  1.00 49.81           C  
ATOM   1559  C   VAL B 101      20.627  60.648  20.753  1.00 45.88           C  
ATOM   1560  O   VAL B 101      21.273  60.303  19.765  1.00 59.15           O  
ATOM   1561  CB  VAL B 101      19.895  63.021  20.534  1.00 41.08           C  
ATOM   1562  CG1 VAL B 101      18.479  62.497  20.437  1.00 39.35           C  
ATOM   1563  CG2 VAL B 101      19.898  64.372  21.190  1.00 46.12           C  
ATOM   1564  N   GLU B 102      19.766  59.851  21.374  1.00 41.05           N  
ATOM   1565  CA  GLU B 102      19.468  58.513  20.885  1.00 30.98           C  
ATOM   1566  C   GLU B 102      18.050  58.668  20.351  1.00 31.22           C  
ATOM   1567  O   GLU B 102      17.115  58.830  21.118  1.00 28.89           O  
ATOM   1568  CB  GLU B 102      19.491  57.497  22.020  1.00 35.65           C  
ATOM   1569  CG  GLU B 102      19.774  56.080  21.555  1.00 60.88           C  
ATOM   1570  CD  GLU B 102      19.256  55.030  22.516  1.00 69.40           C  
ATOM   1571  OE1 GLU B 102      19.655  55.045  23.701  1.00 74.83           O  
ATOM   1572  OE2 GLU B 102      18.443  54.188  22.080  1.00 72.99           O  
ATOM   1573  N   VAL B 103      17.907  58.634  19.032  1.00 35.30           N  
ATOM   1574  CA  VAL B 103      16.623  58.807  18.372  1.00 24.50           C  
ATOM   1575  C   VAL B 103      15.614  57.681  18.567  1.00 29.32           C  
ATOM   1576  O   VAL B 103      15.953  56.503  18.533  1.00 47.46           O  
ATOM   1577  CB  VAL B 103      16.840  59.013  16.866  1.00 39.45           C  
ATOM   1578  CG1 VAL B 103      15.528  59.363  16.179  1.00 39.91           C  
ATOM   1579  CG2 VAL B 103      17.874  60.093  16.653  1.00 31.73           C  
ATOM   1580  N   ASP B 104      14.361  58.068  18.767  1.00 36.98           N  
ATOM   1581  CA  ASP B 104      13.255  57.135  18.944  1.00 34.56           C  
ATOM   1582  C   ASP B 104      12.342  57.280  17.742  1.00 35.54           C  
ATOM   1583  O   ASP B 104      11.663  56.347  17.344  1.00 50.32           O  
ATOM   1584  CB  ASP B 104      12.467  57.458  20.219  1.00 24.25           C  
ATOM   1585  CG  ASP B 104      13.243  57.131  21.473  1.00 32.20           C  
ATOM   1586  OD1 ASP B 104      14.158  56.278  21.391  1.00 34.84           O  
ATOM   1587  OD2 ASP B 104      12.937  57.706  22.540  1.00 47.25           O  
ATOM   1588  N   GLU B 105      12.336  58.474  17.172  1.00 28.41           N  
ATOM   1589  CA  GLU B 105      11.525  58.772  16.009  1.00 33.39           C  
ATOM   1590  C   GLU B 105      12.149  59.992  15.366  1.00 36.74           C  
ATOM   1591  O   GLU B 105      12.583  60.923  16.052  1.00 30.44           O  
ATOM   1592  CB  GLU B 105      10.083  59.077  16.414  1.00 41.79           C  
ATOM   1593  CG  GLU B 105       9.427  57.970  17.195  1.00 40.05           C  
ATOM   1594  CD  GLU B 105       8.464  57.180  16.370  1.00 41.63           C  
ATOM   1595  OE1 GLU B 105       8.651  57.114  15.141  1.00 49.80           O  
ATOM   1596  OE2 GLU B 105       7.518  56.615  16.954  1.00 63.44           O  
ATOM   1597  N   ILE B 106      12.198  59.970  14.041  1.00 29.36           N  
ATOM   1598  CA  ILE B 106      12.773  61.055  13.279  1.00 25.29           C  
ATOM   1599  C   ILE B 106      12.115  61.050  11.927  1.00 24.88           C  
ATOM   1600  O   ILE B 106      11.856  59.994  11.359  1.00 44.75           O  
ATOM   1601  CB  ILE B 106      14.272  60.872  13.090  1.00 32.69           C  
ATOM   1602  CG1 ILE B 106      14.824  62.032  12.259  1.00 31.17           C  
ATOM   1603  CG2 ILE B 106      14.550  59.528  12.434  1.00 27.93           C  
ATOM   1604  CD1 ILE B 106      16.320  62.020  12.090  1.00 26.77           C  
ATOM   1605  N   GLY B 107      11.825  62.237  11.419  1.00 41.18           N  
ATOM   1606  CA  GLY B 107      11.181  62.331  10.129  1.00 37.98           C  
ATOM   1607  C   GLY B 107      11.483  63.647   9.457  1.00 38.37           C  
ATOM   1608  O   GLY B 107      11.849  64.614  10.127  1.00 42.89           O  
ATOM   1609  N   PRO B 108      11.374  63.707   8.122  1.00 34.86           N  
ATOM   1610  CA  PRO B 108      11.641  64.946   7.399  1.00 35.15           C  
ATOM   1611  C   PRO B 108      10.522  65.937   7.659  1.00 31.78           C  
ATOM   1612  O   PRO B 108       9.354  65.603   7.527  1.00 45.63           O  
ATOM   1613  CB  PRO B 108      11.668  64.490   5.950  1.00 29.67           C  
ATOM   1614  CG  PRO B 108      10.715  63.350   5.955  1.00 29.57           C  
ATOM   1615  CD  PRO B 108      11.159  62.607   7.173  1.00 28.48           C  
ATOM   1616  N   SER B 109      10.880  67.155   8.038  1.00 34.10           N  
ATOM   1617  CA  SER B 109       9.869  68.168   8.293  1.00 34.17           C  
ATOM   1618  C   SER B 109       9.284  68.662   6.978  1.00 29.44           C  
ATOM   1619  O   SER B 109      10.013  69.054   6.067  1.00 35.04           O  
ATOM   1620  CB  SER B 109      10.477  69.342   9.056  1.00 19.48           C  
ATOM   1621  OG  SER B 109       9.660  70.485   8.931  1.00 33.01           O  
ATOM   1622  N   LEU B 110       7.961  68.635   6.893  1.00 38.32           N  
ATOM   1623  CA  LEU B 110       7.247  69.091   5.715  1.00 35.66           C  
ATOM   1624  C   LEU B 110       7.075  70.600   5.741  1.00 46.17           C  
ATOM   1625  O   LEU B 110       6.105  71.123   5.199  1.00 41.15           O  
ATOM   1626  CB  LEU B 110       5.878  68.436   5.650  1.00 38.02           C  
ATOM   1627  CG  LEU B 110       5.924  66.931   5.463  1.00 39.61           C  
ATOM   1628  CD1 LEU B 110       4.525  66.386   5.468  1.00 43.39           C  
ATOM   1629  CD2 LEU B 110       6.628  66.611   4.153  1.00 45.13           C  
ATOM   1630  N   ARG B 111       8.023  71.287   6.377  1.00 49.87           N  
ATOM   1631  CA  ARG B 111       8.012  72.745   6.490  1.00 47.27           C  
ATOM   1632  C   ARG B 111       8.291  73.392   5.131  1.00 52.73           C  
ATOM   1633  O   ARG B 111       7.423  74.046   4.548  1.00 48.18           O  
ATOM   1634  CB  ARG B 111       9.078  73.187   7.492  1.00 37.86           C  
ATOM   1635  CG  ARG B 111       9.180  74.691   7.704  1.00 50.21           C  
ATOM   1636  CD  ARG B 111       8.588  75.076   9.048  1.00 62.37           C  
ATOM   1637  NE  ARG B 111       8.886  76.451   9.427  1.00 54.17           N  
ATOM   1638  CZ  ARG B 111       8.691  76.941  10.646  1.00 69.72           C  
ATOM   1639  NH1 ARG B 111       8.199  76.167  11.605  1.00 71.35           N  
ATOM   1640  NH2 ARG B 111       8.989  78.204  10.912  1.00 73.59           N  
ATOM   1641  N   TYR B 112       9.518  73.221   4.645  1.00 50.17           N  
ATOM   1642  CA  TYR B 112       9.916  73.764   3.353  1.00 46.58           C  
ATOM   1643  C   TYR B 112      10.114  72.623   2.367  1.00 49.87           C  
ATOM   1644  O   TYR B 112      11.073  72.632   1.601  1.00 65.32           O  
ATOM   1645  CB  TYR B 112      11.240  74.525   3.443  1.00 35.16           C  
ATOM   1646  CG  TYR B 112      11.324  75.619   4.467  1.00 42.62           C  
ATOM   1647  CD1 TYR B 112      12.006  75.421   5.662  1.00 55.09           C  
ATOM   1648  CD2 TYR B 112      10.733  76.858   4.242  1.00 43.30           C  
ATOM   1649  CE1 TYR B 112      12.122  76.440   6.600  1.00 72.85           C  
ATOM   1650  CE2 TYR B 112      10.837  77.883   5.173  1.00 61.32           C  
ATOM   1651  CZ  TYR B 112      11.526  77.665   6.356  1.00 70.03           C  
ATOM   1652  OH  TYR B 112      11.638  78.671   7.288  1.00 83.77           O  
ATOM   1653  N   ALA B 113       9.233  71.629   2.390  1.00 62.26           N  
ATOM   1654  CA  ALA B 113       9.372  70.509   1.465  1.00 58.27           C  
ATOM   1655  C   ALA B 113       8.294  69.449   1.615  1.00 58.80           C  
ATOM   1656  O   ALA B 113       7.585  69.381   2.627  1.00 61.54           O  
ATOM   1657  CB  ALA B 113      10.740  69.863   1.631  1.00 59.86           C  
ATOM   1658  N   THR B 114       8.198  68.612   0.590  1.00 53.63           N  
ATOM   1659  CA  THR B 114       7.243  67.518   0.544  1.00 53.15           C  
ATOM   1660  C   THR B 114       8.002  66.223   0.814  1.00 49.20           C  
ATOM   1661  O   THR B 114       9.188  66.248   1.133  1.00 45.44           O  
ATOM   1662  CB  THR B 114       6.582  67.425  -0.854  1.00 54.21           C  
ATOM   1663  OG1 THR B 114       7.598  67.406  -1.864  1.00 32.81           O  
ATOM   1664  CG2 THR B 114       5.670  68.609  -1.089  1.00 57.55           C  
ATOM   1665  N   ALA B 115       7.314  65.096   0.682  1.00 50.93           N  
ATOM   1666  CA  ALA B 115       7.929  63.796   0.884  1.00 52.67           C  
ATOM   1667  C   ALA B 115       6.975  62.693   0.440  1.00 58.97           C  
ATOM   1668  O   ALA B 115       5.764  62.789   0.654  1.00 55.64           O  
ATOM   1669  CB  ALA B 115       8.295  63.617   2.348  1.00 57.83           C  
ATOM   1670  N   LYS B 116       7.529  61.665  -0.203  1.00 60.47           N  
ATOM   1671  CA  LYS B 116       6.756  60.509  -0.667  1.00 59.08           C  
ATOM   1672  C   LYS B 116       7.081  59.407   0.327  1.00 46.90           C  
ATOM   1673  O   LYS B 116       8.190  58.885   0.333  1.00 43.54           O  
ATOM   1674  CB  LYS B 116       7.194  60.094  -2.065  1.00 49.40           C  
ATOM   1675  N   VAL B 117       6.112  59.060   1.162  1.00 41.25           N  
ATOM   1676  CA  VAL B 117       6.319  58.058   2.191  1.00 39.98           C  
ATOM   1677  C   VAL B 117       5.850  56.665   1.811  1.00 54.14           C  
ATOM   1678  O   VAL B 117       4.669  56.468   1.534  1.00 69.68           O  
ATOM   1679  CB  VAL B 117       5.594  58.477   3.497  1.00 52.79           C  
ATOM   1680  CG1 VAL B 117       6.007  57.568   4.645  1.00 33.37           C  
ATOM   1681  CG2 VAL B 117       5.902  59.933   3.823  1.00 38.84           C  
ATOM   1682  N   ASN B 118       6.775  55.702   1.803  1.00 66.90           N  
ATOM   1683  CA  ASN B 118       6.459  54.297   1.491  1.00 75.62           C  
ATOM   1684  C   ASN B 118       6.378  53.511   2.793  1.00 78.27           C  
ATOM   1685  O   ASN B 118       7.401  53.301   3.443  1.00 80.03           O  
ATOM   1686  CB  ASN B 118       7.560  53.621   0.651  1.00 72.77           C  
ATOM   1687  CG  ASN B 118       7.569  54.061  -0.794  1.00 89.74           C  
ATOM   1688  OD1 ASN B 118       6.557  53.980  -1.492  1.00 98.98           O  
ATOM   1689  ND2 ASN B 118       8.731  54.507  -1.264  1.00 93.98           N  
ATOM   1690  N   LYS B 119       5.187  53.077   3.189  1.00 83.71           N  
ATOM   1691  CA  LYS B 119       5.086  52.274   4.406  1.00 84.36           C  
ATOM   1692  C   LYS B 119       5.925  51.026   4.126  1.00 85.23           C  
ATOM   1693  O   LYS B 119       6.197  50.711   2.967  1.00 89.64           O  
ATOM   1694  CB  LYS B 119       3.643  51.816   4.664  1.00 88.67           C  
ATOM   1695  CG  LYS B 119       2.728  52.730   5.476  1.00 77.81           C  
ATOM   1696  CD  LYS B 119       1.717  51.846   6.234  1.00 86.88           C  
ATOM   1697  CE  LYS B 119       0.454  52.576   6.669  1.00 84.30           C  
ATOM   1698  NZ  LYS B 119      -0.457  52.836   5.520  1.00 83.82           N  
ATOM   1699  N   ALA B 120       6.347  50.323   5.172  1.00 87.71           N  
ATOM   1700  CA  ALA B 120       7.099  49.090   4.978  1.00 85.10           C  
ATOM   1701  C   ALA B 120       6.002  48.033   4.961  1.00 99.17           C  
ATOM   1702  O   ALA B 120       5.083  48.100   4.141  1.00 95.98           O  
ATOM   1703  CB  ALA B 120       8.054  48.855   6.135  1.00 66.80           C  
ATOM   1704  N   SER B 121       6.081  47.060   5.859  1.00113.91           N  
ATOM   1705  CA  SER B 121       5.036  46.052   5.923  1.00126.86           C  
ATOM   1706  C   SER B 121       5.061  45.285   7.233  1.00138.16           C  
ATOM   1707  O   SER B 121       6.003  44.550   7.532  1.00145.14           O  
ATOM   1708  CB  SER B 121       5.126  45.075   4.745  1.00122.18           C  
ATOM   1709  OG  SER B 121       6.040  44.027   5.004  1.00112.68           O  
ATOM   1710  N   ARG B 122       4.016  45.499   8.021  1.00146.28           N  
ATOM   1711  CA  ARG B 122       3.846  44.828   9.295  1.00145.94           C  
ATOM   1712  C   ARG B 122       2.342  44.613   9.488  1.00149.08           C  
ATOM   1713  O   ARG B 122       1.805  43.566   9.118  1.00150.52           O  
ATOM   1714  CB  ARG B 122       4.458  45.657  10.448  1.00141.07           C  
ATOM   1715  CG  ARG B 122       3.901  47.072  10.663  1.00129.31           C  
ATOM   1716  CD  ARG B 122       4.147  47.513  12.110  1.00119.82           C  
ATOM   1717  NE  ARG B 122       3.318  48.642  12.537  1.00118.19           N  
ATOM   1718  CZ  ARG B 122       3.125  48.979  13.813  1.00121.32           C  
ATOM   1719  NH1 ARG B 122       3.699  48.274  14.780  1.00116.93           N  
ATOM   1720  NH2 ARG B 122       2.354  50.014  14.129  1.00119.36           N  
ATOM   1721  N   SER B 123       1.665  45.622  10.025  1.00150.50           N  
ATOM   1722  CA  SER B 123       0.230  45.561  10.273  1.00150.20           C  
ATOM   1723  C   SER B 123      -0.530  46.495   9.332  1.00150.52           C  
ATOM   1724  O   SER B 123      -1.131  47.472   9.830  1.00150.52           O  
ATOM   1725  CB  SER B 123      -0.054  45.943  11.727  1.00148.14           C  
ATOM   1726  OG  SER B 123       0.479  47.222  12.021  1.00146.23           O  
TER    1727      SER B 123                                                      
HETATM 1728 ZN    ZN B 400      19.574  45.996  10.784  1.00 95.77          ZN  
HETATM 1729  O   HOH A 165       3.069  75.842  30.057  1.00 34.22           O  
HETATM 1730  O   HOH A 166      -6.721  63.103  10.852  1.00 36.79           O  
HETATM 1731  O   HOH A 167      -4.056  80.638  18.033  1.00 56.44           O  
HETATM 1732  O   HOH A 168       5.626  58.562   8.260  1.00 50.07           O  
HETATM 1733  O   HOH A 169       8.502  56.559  19.911  1.00 53.73           O  
HETATM 1734  O   HOH A 170       6.930  70.877   9.852  1.00 50.19           O  
HETATM 1735  O   HOH A 171      -7.841  67.440  19.745  1.00 48.11           O  
HETATM 1736  O   HOH A 172      -7.937  69.565  12.811  1.00 44.18           O  
HETATM 1737  O   HOH A 173       7.865  73.353  18.964  1.00 60.39           O  
HETATM 1738  O   HOH A 174     -11.505  71.499   5.671  1.00 59.48           O  
HETATM 1739  O   HOH A 175      -2.207  81.790  10.794  1.00 50.46           O  
HETATM 1740  O   HOH A 176      -5.376  76.944  16.026  1.00 58.40           O  
HETATM 1741  O   HOH A 177      16.547  67.257  -1.815  1.00 77.83           O  
HETATM 1742  O   HOH A 178      11.948  56.792  13.237  1.00 57.29           O  
HETATM 1743  O   HOH A 179      -8.554  67.499   0.771  1.00 82.62           O  
HETATM 1744  O   HOH A 180      -1.958  79.144  25.156  1.00 79.17           O  
HETATM 1745  O   HOH A 181      -2.830  79.868  13.611  1.00 48.50           O  
HETATM 1746  O   HOH A 182       2.031  77.620  -2.095  1.00 66.03           O  
HETATM 1747  O   HOH A 183       6.771  40.265  24.624  1.00 52.83           O  
HETATM 1748  O   HOH A 184       1.209  80.843  10.911  1.00 76.70           O  
HETATM 1749  O   HOH A 185      -4.556  49.071  19.892  1.00 73.04           O  
HETATM 1750  O   HOH A 186       6.524  63.290  23.831  1.00 55.35           O  
HETATM 1751  O   HOH A 187      -9.374  66.006  23.647  1.00 52.28           O  
HETATM 1752  O   HOH A 188     -10.518  67.225  21.828  1.00 73.54           O  
HETATM 1753  O   HOH A 189     -12.070  76.679  -0.295  1.00 62.75           O  
HETATM 1754  O   HOH A 190       5.167  77.597  13.072  1.00 57.79           O  
HETATM 1755  O   HOH A 191     -14.828  73.720  33.712  1.00 72.75           O  
HETATM 1756  O   HOH A 192       9.357  74.545  21.879  1.00 40.36           O  
HETATM 1757  O   HOH A 193       2.704  55.251  18.820  1.00 59.45           O  
HETATM 1758  O   HOH A 194       0.160  84.380  35.410  1.00 54.35           O  
HETATM 1759  O   HOH A 195       2.563  52.965  13.589  1.00 42.87           O  
HETATM 1760  O   HOH A 196      -1.731  85.326  10.475  1.00 67.97           O  
HETATM 1761  O   HOH A 197       4.177  48.172  27.978  1.00 83.01           O  
HETATM 1762  O   HOH A 198      -8.770  70.977  -2.092  1.00 48.29           O  
HETATM 1763  O   HOH A 199     -12.399  71.947  -3.600  1.00 79.02           O  
HETATM 1764  O   HOH A 200       2.273  73.183  -3.346  1.00 63.98           O  
HETATM 1765  O   HOH A 201       0.010  69.833  -5.332  1.00 87.35           O  
HETATM 1766  O   HOH A 202      -6.785  51.156  20.994  1.00 51.96           O  
HETATM 1767  O   HOH A 203       3.490  85.534   8.351  1.00 56.20           O  
HETATM 1768  O   HOH A 204       5.034  82.294  42.364  1.00 44.24           O  
HETATM 1769  O   HOH A 205       5.488  69.713  27.259  1.00 58.16           O  
HETATM 1770  O   HOH A 206      -5.295  83.935   6.557  1.00 62.69           O  
HETATM 1771  O   HOH A 207      -5.066  63.889  -3.914  1.00 64.12           O  
HETATM 1772  O   HOH A 208       0.033  60.361  -4.493  1.00 65.53           O  
HETATM 1773  O   HOH A 209       2.617  61.724  -6.571  1.00 82.97           O  
HETATM 1774  O   HOH A 210      13.161  77.332  -0.650  1.00 58.48           O  
HETATM 1775  O   HOH A 211      -9.913  70.342  -6.993  1.00 64.36           O  
HETATM 1776  O   HOH A 212     -11.782  68.355  -9.202  1.00 64.83           O  
HETATM 1777  O   HOH A 213     -12.321  74.224 -11.515  1.00 47.55           O  
HETATM 1778  O   HOH A 214       4.634  68.020  -8.498  1.00 81.05           O  
HETATM 1779  O   HOH A 215       0.294  45.862  16.937  1.00 63.83           O  
HETATM 1780  O   HOH A 216     -13.374  66.569  19.804  1.00 56.63           O  
HETATM 1781  O   HOH A 217       4.035  70.090  -3.907  1.00 53.28           O  
HETATM 1782  O   HOH A 218       1.033  67.134  -6.441  1.00 69.68           O  
HETATM 1783  O   HOH A 219      -8.652  62.299  -0.562  1.00 84.41           O  
HETATM 1784  O   HOH A 220      -1.336  61.041  -7.291  1.00 62.60           O  
HETATM 1785  O   HOH A 221       7.549  76.459  -5.784  1.00 63.05           O  
HETATM 1786  O   HOH A 222      10.331  77.429  -7.838  1.00 66.34           O  
HETATM 1787  O   HOH A 223     -15.897  72.837 -15.465  1.00 60.91           O  
HETATM 1788  O   HOH A 224       0.818  78.304   0.538  1.00 71.70           O  
HETATM 1789  O   HOH A 225     -11.985  71.922  -9.197  1.00 68.56           O  
HETATM 1790  O   HOH A 226       3.022  90.247   7.332  1.00 82.92           O  
HETATM 1791  O   HOH A 227      16.687  81.181   0.239  1.00 75.10           O  
HETATM 1792  O   HOH A 228      -6.615  59.737  -0.518  1.00 68.77           O  
HETATM 1793  O   HOH A 229       5.297  76.718  -7.562  1.00 74.11           O  
HETATM 1794  O   HOH A 230       1.318  58.900   4.146  1.00 60.74           O  
HETATM 1795  O   HOH A 231       2.999  60.052   0.943  1.00 47.23           O  
HETATM 1796  O   HOH A 232       0.903  85.638  32.951  1.00 67.83           O  
HETATM 1797  O   HOH A 233     -15.036  66.886  22.436  1.00 57.06           O  
HETATM 1798  O   HOH A 234       8.099  86.161   2.596  1.00 54.82           O  
HETATM 1799  O   HOH A 235     -14.127  62.041  -3.412  1.00 58.05           O  
HETATM 1800  O   HOH A 236     -12.793  58.542  -6.804  1.00 79.75           O  
HETATM 1801  O   HOH A 237     -15.107  72.373   4.193  1.00 62.15           O  
HETATM 1802  O   HOH A 238      -6.921  54.770  27.425  1.00 68.66           O  
HETATM 1803  O   HOH A 239     -15.724  73.102  -8.205  1.00 69.45           O  
HETATM 1804  O   HOH B 401      11.052  67.025  27.875  1.00 54.77           O  
HETATM 1805  O   HOH B 402      12.568  51.546  -0.418  1.00 46.69           O  
HETATM 1806  O   HOH B 403      12.556  67.559   5.146  1.00 45.69           O  
HETATM 1807  O   HOH B 404      21.442  59.109   2.482  1.00 68.68           O  
HETATM 1808  O   HOH B 405      12.243  64.605  29.182  1.00 44.55           O  
HETATM 1809  O   HOH B 406      26.693  62.159   9.171  1.00 75.05           O  
HETATM 1810  O   HOH B 407      17.247  54.053  18.179  1.00 59.21           O  
HETATM 1811  O   HOH B 408      15.282  79.896  12.772  1.00 50.12           O  
HETATM 1812  O   HOH B 409      25.616  66.153  20.633  1.00 47.62           O  
HETATM 1813  O   HOH B 410       8.004  96.338  19.065  1.00 44.61           O  
HETATM 1814  O   HOH B 411      29.169  43.975  11.222  1.00 54.83           O  
HETATM 1815  O   HOH B 412      10.989  81.796  10.309  1.00 72.23           O  
HETATM 1816  O   HOH B 413      11.290  72.515  19.639  1.00 57.50           O  
HETATM 1817  O   HOH B 414      15.093  49.600  -0.564  1.00 41.03           O  
HETATM 1818  O   HOH B 415      -0.367  44.163   6.219  1.00 62.79           O  
HETATM 1819  O   HOH B 416      38.208  58.099  34.202  1.00 61.09           O  
HETATM 1820  O   HOH B 417      23.315  77.775  20.913  1.00 60.43           O  
HETATM 1821  O   HOH B 418      22.948  70.065   1.014  1.00 49.62           O  
HETATM 1822  O   HOH B 419       2.458  56.129   5.161  1.00 56.74           O  
HETATM 1823  O   HOH B 420      37.100  66.001  26.788  1.00 63.35           O  
HETATM 1824  O   HOH B 421      19.379  98.932  12.843  1.00 82.51           O  
HETATM 1825  O   HOH B 422       1.813  54.874   2.462  1.00 49.89           O  
HETATM 1826  O   HOH B 423       4.363  51.634  -0.005  1.00 45.74           O  
HETATM 1827  O   HOH B 424       6.872  50.931  -2.186  1.00 52.44           O  
HETATM 1828  O   HOH B 425      11.286  55.918  24.985  1.00 60.72           O  
HETATM 1829  O   HOH B 426      23.358  82.097  24.195  1.00 84.89           O  
HETATM 1830  O   HOH B 427       9.755  59.151  33.394  1.00 40.48           O  
HETATM 1831  O   HOH B 428       8.030  58.320  36.341  1.00 70.39           O  
HETATM 1832  O   HOH B 429      14.487  53.087  16.146  1.00 53.62           O  
HETATM 1833  O   HOH B 430      29.680  66.422  17.061  1.00 75.78           O  
HETATM 1834  O   HOH B 431      28.001  67.926  27.157  1.00 52.17           O  
HETATM 1835  O   HOH B 432      27.832  68.557  30.145  1.00 57.81           O  
HETATM 1836  O   HOH B 433       8.443  96.994  15.821  1.00 79.08           O  
HETATM 1837  O   HOH B 434       9.953  81.505   7.059  1.00 57.13           O  
HETATM 1838  O   HOH B 435      12.651  78.062  12.978  1.00 64.00           O  
HETATM 1839  O   HOH B 436      20.243  49.465  22.520  1.00 72.84           O  
HETATM 1840  O   HOH B 437      26.873  72.190   6.678  1.00 52.72           O  
HETATM 1841  O   HOH B 438      42.682  59.338  31.729  1.00 56.48           O  
HETATM 1842  O   HOH B 439      25.708  75.438   4.087  1.00 61.27           O  
HETATM 1843  O   HOH B 440      -1.291  51.278  10.519  1.00 73.60           O  
HETATM 1844  O   HOH B 441      11.585  97.884  17.165  1.00 59.59           O  
HETATM 1845  O   HOH B 442      28.553  41.620   8.142  1.00 59.87           O  
HETATM 1846  O   HOH B 443      33.790  41.523  10.613  1.00 75.93           O  
HETATM 1847  O   HOH B 444      38.301  36.575   8.280  1.00 74.86           O  
HETATM 1848  O   HOH B 445      39.531  33.286   8.242  1.00 78.04           O  
HETATM 1849  O   HOH B 446      41.119  36.680  10.313  1.00 83.65           O  
HETATM 1850  O   HOH B 447      44.147  40.365  11.148  1.00 44.22           O  
HETATM 1851  O   HOH B 448      38.709  38.342  13.051  1.00 75.30           O  
HETATM 1852  O   HOH B 449       1.408  47.615   4.929  1.00 55.30           O  
HETATM 1853  O   HOH B 450       3.437  36.239   6.348  1.00 70.54           O  
HETATM 1854  O   HOH B 451       4.113  33.629   4.330  1.00 62.99           O  
HETATM 1855  O   HOH B 452      26.700  55.767  36.386  1.00 50.13           O  
HETATM 1856  O   HOH B 453      26.666  57.297  39.576  1.00 72.59           O  
HETATM 1857  O   HOH B 454      27.964  67.240  -3.432  1.00 57.21           O  
HETATM 1858  O   HOH B 455      25.511  67.528  -5.669  1.00 49.05           O  
HETATM 1859  O   HOH B 456       7.435  57.834  32.010  1.00 65.75           O  
HETATM 1860  O   HOH B 457       1.766  49.898  -3.578  1.00 66.54           O  
HETATM 1861  O   HOH B 458      40.000  31.084   7.498  1.00 76.10           O  
HETATM 1862  O   HOH B 459       2.899  59.642  40.999  1.00 69.52           O  
HETATM 1863  O   HOH B 460      15.057  48.612  16.993  1.00 41.90           O  
HETATM 1864  O   HOH B 461      29.100  63.687  19.033  1.00 66.26           O  
HETATM 1865  O   HOH B 462      32.438  62.260  15.822  1.00 76.24           O  
HETATM 1866  O   HOH B 463       5.961  94.776  11.184  1.00 57.77           O  
HETATM 1867  O   HOH B 464       6.035  91.671  12.837  1.00 76.62           O  
HETATM 1868  O   HOH B 465      42.368  62.489  33.312  1.00 76.45           O  
HETATM 1869  O   HOH B 466      36.584  65.160   5.968  1.00 63.79           O  
HETATM 1870  O   HOH B 467      36.893  65.137   3.133  1.00 58.55           O  
HETATM 1871  O   HOH B 468      37.377  61.680  -1.024  1.00 64.86           O  
HETATM 1872  O   HOH B 469      26.800  78.257   2.278  1.00 84.62           O  
HETATM 1873  O   HOH B 470       9.311  50.842   2.773  1.00 63.70           O  
HETATM 1874  O   HOH B 471       8.145  66.316  27.818  1.00 65.98           O  
HETATM 1875  O   HOH B 472      10.051  83.358  13.323  1.00 79.34           O  
HETATM 1876  O   HOH B 473      17.186  98.952   4.714  1.00 75.06           O  
HETATM 1877  O   HOH B 474      24.870  71.048   4.727  1.00 65.05           O  
HETATM 1878  O   HOH B 475       0.256  55.772  -0.250  1.00 73.07           O  
HETATM 1879  O   HOH B 476       8.042  48.909  -1.192  1.00 47.21           O  
HETATM 1880  O   HOH B 477      11.768  80.836   2.627  1.00 57.07           O  
HETATM 1881  O   HOH B 478      10.709  77.956   0.844  1.00 67.25           O  
HETATM 1882  O   HOH B 479       9.385  75.927  -0.967  1.00 63.59           O  
HETATM 1883  O   HOH B 480      25.171  76.865   5.836  1.00 57.99           O  
HETATM 1884  O   HOH B 481      39.175  39.269   7.025  1.00 76.17           O  
HETATM 1885  O   HOH B 482      39.248  40.082   9.969  1.00 87.92           O  
HETATM 1886  O   HOH B 483      43.523  39.484   8.313  1.00 75.49           O  
HETATM 1887  O   HOH B 484      41.747  36.026  14.736  1.00 73.20           O  
HETATM 1888  O   HOH B 485      40.556  39.124  15.945  1.00 72.19           O  
HETATM 1889  O   HOH B 486      39.912  39.250  19.276  1.00 68.57           O  
HETATM 1890  O   HOH B 487      36.554  41.772  23.814  1.00 58.23           O  
HETATM 1891  O   HOH B 488       7.301  66.525  -6.684  1.00 74.32           O  
HETATM 1892  O   HOH B 489      30.859  79.149   4.264  1.00 70.47           O  
HETATM 1893  O   HOH B 490      36.694  42.525   4.713  1.00 72.67           O  
HETATM 1894  O   HOH B 491      36.027  33.238  10.780  1.00 80.73           O  
HETATM 1895  O   HOH B 492      16.959  98.339   7.774  1.00 65.87           O  
HETATM 1896  O   HOH B 493      25.642  64.900  -0.112  1.00 70.84           O  
HETATM 1897  O   HOH B 494      12.875  50.943  -2.847  1.00 69.80           O  
HETATM 1898  O   HOH B 495      16.444 101.025   9.686  1.00 67.47           O  
HETATM 1899  O   HOH B 496       7.779  55.553  -4.533  1.00 66.99           O  
HETATM 1900  O   HOH B 497      22.194  82.628  26.691  1.00 50.00           O  
HETATM 1901  O   HOH B 498      40.526  32.011  11.339  1.00 62.65           O  
HETATM 1902  O   HOH B 499      18.573  48.872  21.105  1.00 72.80           O  
HETATM 1903  O   HOH B 500      14.009  77.184   1.849  1.00 57.95           O  
HETATM 1904  O   HOH B 501      40.739  42.637  18.747  1.00 57.09           O  
HETATM 1905  O   HOH B 502      13.660  83.843   5.861  1.00 62.00           O  
HETATM 1906  O   HOH B 503      38.318  55.983  36.265  1.00 52.65           O  
HETATM 1907  O   HOH B 504      24.794  73.379   9.250  1.00 72.12           O  
HETATM 1908  O   HOH B 505      43.581  34.168   7.988  1.00 75.78           O  
HETATM 1909  O   HOH B 506      48.034  31.147  10.607  1.00 65.15           O  
HETATM 1910  O   HOH B 507      44.044  43.048  13.209  1.00 56.32           O  
HETATM 1911  O   HOH B 508      29.957  50.549  42.602  1.00 57.81           O  
HETATM 1912  O   HOH B 509       8.517  88.412  16.144  1.00 98.35           O  
HETATM 1913  O   HOH B 510       9.248  88.962  18.358  1.00 79.73           O  
HETATM 1914  O   HOH B 511      32.978  62.008   4.508  1.00 74.69           O  
HETATM 1915  O   HOH B 512      40.866  39.222  21.862  1.00 64.12           O  
HETATM 1916  O   HOH B 513      16.457  64.521   2.682  1.00 57.64           O  
HETATM 1917  O   HOH B 514      12.839  53.568  19.530  1.00 72.00           O  
HETATM 1918  O   HOH B 515      32.079  40.133  13.618  1.00 58.49           O  
HETATM 1919  O   HOH B 516      17.785 100.589  12.634  1.00 63.40           O  
HETATM 1920  O   HOH B 517      10.578  65.227  24.652  1.00 62.32           O  
HETATM 1921  O   HOH B 518       1.739  54.960  -4.752  1.00 82.35           O  
HETATM 1922  O   HOH B 519       6.562  93.606  14.794  1.00 73.47           O  
HETATM 1923  O   HOH B 520      35.670  38.236  14.712  1.00 64.58           O  
HETATM 1924  O   HOH B 521      38.280  64.343   0.566  1.00 49.10           O  
HETATM 1925  O   HOH B 522      17.450  75.433   2.917  1.00 75.82           O  
HETATM 1926  O   HOH B 523      35.299  40.946  25.938  1.00 79.07           O  
HETATM 1927  O   HOH B 524      36.926  43.423  21.450  1.00 79.23           O  
HETATM 1928  O   HOH B 525      36.834  34.965  13.743  1.00 86.17           O  
HETATM 1929  O   HOH B 526      12.051  88.020   2.932  1.00 56.27           O  
HETATM 1930  O   HOH B 527      39.705  57.738  37.278  1.00 78.52           O  
HETATM 1931  O   HOH B 528      38.177  56.580  39.582  1.00 86.90           O  
HETATM 1932  O   HOH B 529      11.708  88.096  21.776  1.00 82.41           O  
HETATM 1933  O   HOH B 530      36.616  60.559   8.588  1.00 90.77           O  
HETATM 1934  O   HOH B 531       3.778  54.232  -2.524  1.00 76.51           O  
HETATM 1935  O   HOH B 532      28.545  68.402  32.577  1.00 45.72           O  
HETATM 1936  O   HOH B 533      33.994  40.527   7.209  1.00 78.62           O  
HETATM 1937  O   HOH B 534      45.885  37.430  11.173  1.00 80.39           O  
HETATM 1938  O   HOH B 535      29.857  59.445  16.486  1.00 77.87           O  
HETATM 1939  O   HOH B 536      46.700  41.828   9.447  1.00 46.64           O  
HETATM 1940  O   HOH B 537      42.991  46.379  15.399  1.00 65.38           O  
CONECT 1294 1728                                                                
CONECT 1313 1728                                                                
CONECT 1728 1294 1313                                                           
MASTER      533    0    1    2   18    0    1    6 1938    2    3   26          
END                                                                             



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