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Database: PDB
Entry: 6K3A
LinkDB: 6K3A
Original site: 6K3A 
HEADER    REPLICATION                             17-MAY-19   6K3A              
TITLE     CRYSTAL STRUCTURE OF HUMAN PCNA IN COMPLEX WITH DNMT1 PIP BOX MOTIF.  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROLIFERATING CELL NUCLEAR ANTIGEN;                        
COMPND   3 CHAIN: A, C, E;                                                      
COMPND   4 SYNONYM: PCNA,CYCLIN;                                                
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: PEPTIDE FROM DNA (CYTOSINE-5)-METHYLTRANSFERASE 1;         
COMPND   8 CHAIN: B, D, F;                                                      
COMPND   9 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: PCNA;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 SYNTHETIC: YES;                                                      
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606                                                 
KEYWDS    DNMT1, PCNA, DNA METHYLATION, PIP BOX, REPLICATION                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.JIMENJI,S.KORI,K.ARITA                                              
REVDAT   3   24-JUL-19 6K3A    1       JRNL                                     
REVDAT   2   10-JUL-19 6K3A    1       JRNL                                     
REVDAT   1   26-JUN-19 6K3A    0                                                
JRNL        AUTH   T.JIMENJI,R.MATSUMURA,S.KORI,K.ARITA                         
JRNL        TITL   STRUCTURE OF PCNA IN COMPLEX WITH DNMT1 PIP BOX REVEALS THE  
JRNL        TITL 2 BASIS FOR THE MOLECULAR MECHANISM OF THE INTERACTION.        
JRNL        REF    BIOCHEM.BIOPHYS.RES.COMMUN.   V. 516   578 2019              
JRNL        REFN                   ESSN 1090-2104                               
JRNL        PMID   31235252                                                     
JRNL        DOI    10.1016/J.BBRC.2019.06.060                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.15.2_3472: ???)                            
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.84                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 34349                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.220                           
REMARK   3   R VALUE            (WORKING SET) : 0.217                           
REMARK   3   FREE R VALUE                     : 0.264                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.190                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1783                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 40.8505 -  5.4043    0.98     2533   146  0.2069 0.2306        
REMARK   3     2  5.4043 -  4.2911    0.99     2511   142  0.1627 0.2195        
REMARK   3     3  4.2911 -  3.7491    0.99     2520   159  0.1814 0.2274        
REMARK   3     4  3.7491 -  3.4065    0.99     2472   114  0.2099 0.1974        
REMARK   3     5  3.4065 -  3.1624    0.99     2547   100  0.2385 0.3625        
REMARK   3     6  3.1624 -  2.9760    0.99     2509   134  0.2589 0.3265        
REMARK   3     7  2.9760 -  2.8270    1.00     2473   149  0.2797 0.3562        
REMARK   3     8  2.8270 -  2.7040    1.00     2497   158  0.2732 0.3303        
REMARK   3     9  2.7040 -  2.5999    1.00     2498   136  0.2721 0.3112        
REMARK   3    10  2.5999 -  2.5102    1.00     2545   132  0.2790 0.3681        
REMARK   3    11  2.5102 -  2.4317    1.00     2437   150  0.2867 0.3226        
REMARK   3    12  2.4317 -  2.3622    1.00     2459   160  0.3010 0.3576        
REMARK   3    13  2.3622 -  2.3001    1.00     2565   103  0.3192 0.4019        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.310            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.890           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.005           5694                                  
REMARK   3   ANGLE     :  0.852           7689                                  
REMARK   3   CHIRALITY :  0.050            951                                  
REMARK   3   PLANARITY :  0.005            948                                  
REMARK   3   DIHEDRAL  :  6.378           3462                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6K3A COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 27-MAY-19.                  
REMARK 100 THE DEPOSITION ID IS D_1300012212.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-DEC-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : BL-17A                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.98                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 6M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 34458                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.840                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 3.200                              
REMARK 200  R MERGE                    (I) : 0.06200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 0.0000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.38                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.66400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 5MLO                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 41.41                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.6M SODIUM CITRATE, PH 6.5, VAPOR       
REMARK 280  DIFFUSION, TEMPERATURE 293K                                         
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       70.77000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       40.79900            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       70.77000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       40.79900            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8110 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 30950 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -47.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F                      
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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH C 301  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A    -2                                                      
REMARK 465     PRO A    -1                                                      
REMARK 465     GLY A     0                                                      
REMARK 465     ASN A   107                                                      
REMARK 465     GLN A   108                                                      
REMARK 465     ASP A   122                                                      
REMARK 465     VAL A   123                                                      
REMARK 465     GLU A   124                                                      
REMARK 465     ALA A   163                                                      
REMARK 465     LYS A   164                                                      
REMARK 465     ASP A   165                                                      
REMARK 465     THR A   185                                                      
REMARK 465     SER A   186                                                      
REMARK 465     ASN A   187                                                      
REMARK 465     VAL A   188                                                      
REMARK 465     ASP A   189                                                      
REMARK 465     LYS A   190                                                      
REMARK 465     GLU A   191                                                      
REMARK 465     GLU A   192                                                      
REMARK 465     GLU A   258                                                      
REMARK 465     GLU A   259                                                      
REMARK 465     GLY A   260                                                      
REMARK 465     SER A   261                                                      
REMARK 465     SER B   161                                                      
REMARK 465     PRO B   175                                                      
REMARK 465     ALA B   176                                                      
REMARK 465     LYS B   177                                                      
REMARK 465     ARG B   178                                                      
REMARK 465     LYS B   179                                                      
REMARK 465     PRO B   180                                                      
REMARK 465     GLY C    -2                                                      
REMARK 465     PRO C    -1                                                      
REMARK 465     GLY C     0                                                      
REMARK 465     ASN C   107                                                      
REMARK 465     GLN C   108                                                      
REMARK 465     ASP C   122                                                      
REMARK 465     VAL C   123                                                      
REMARK 465     GLU C   124                                                      
REMARK 465     ALA C   163                                                      
REMARK 465     LYS C   164                                                      
REMARK 465     ASP C   165                                                      
REMARK 465     THR C   185                                                      
REMARK 465     SER C   186                                                      
REMARK 465     ASN C   187                                                      
REMARK 465     VAL C   188                                                      
REMARK 465     ASP C   189                                                      
REMARK 465     LYS C   190                                                      
REMARK 465     GLU C   191                                                      
REMARK 465     GLU C   192                                                      
REMARK 465     GLU C   258                                                      
REMARK 465     GLU C   259                                                      
REMARK 465     GLY C   260                                                      
REMARK 465     SER C   261                                                      
REMARK 465     SER D   161                                                      
REMARK 465     PRO D   175                                                      
REMARK 465     ALA D   176                                                      
REMARK 465     LYS D   177                                                      
REMARK 465     ARG D   178                                                      
REMARK 465     LYS D   179                                                      
REMARK 465     PRO D   180                                                      
REMARK 465     GLY E    -2                                                      
REMARK 465     PRO E    -1                                                      
REMARK 465     GLY E     0                                                      
REMARK 465     ASN E   107                                                      
REMARK 465     GLN E   108                                                      
REMARK 465     ASP E   122                                                      
REMARK 465     VAL E   123                                                      
REMARK 465     GLU E   124                                                      
REMARK 465     ALA E   163                                                      
REMARK 465     LYS E   164                                                      
REMARK 465     ASP E   165                                                      
REMARK 465     THR E   185                                                      
REMARK 465     SER E   186                                                      
REMARK 465     ASN E   187                                                      
REMARK 465     VAL E   188                                                      
REMARK 465     ASP E   189                                                      
REMARK 465     LYS E   190                                                      
REMARK 465     GLU E   191                                                      
REMARK 465     GLU E   192                                                      
REMARK 465     GLU E   258                                                      
REMARK 465     GLU E   259                                                      
REMARK 465     GLY E   260                                                      
REMARK 465     SER E   261                                                      
REMARK 465     SER F   161                                                      
REMARK 465     PRO F   175                                                      
REMARK 465     ALA F   176                                                      
REMARK 465     LYS F   177                                                      
REMARK 465     ARG F   178                                                      
REMARK 465     LYS F   179                                                      
REMARK 465     PRO F   180                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A  20    NZ                                                  
REMARK 470     ARG A  53    CZ   NH1  NH2                                       
REMARK 470     ARG A  64    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A  80    CG   CD   CE   NZ                                   
REMARK 470     ARG A  91    CZ   NH1  NH2                                       
REMARK 470     GLU A  93    OE1  OE2                                            
REMARK 470     ASP A  94    OD1  OD2                                            
REMARK 470     GLU A 109    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 113    OD1  OD2                                            
REMARK 470     GLU A 115    CD   OE1  OE2                                       
REMARK 470     LYS A 117    CD   CE   NZ                                        
REMARK 470     LEU A 121    CG   CD1  CD2                                       
REMARK 470     GLN A 125    OE1  NE2                                            
REMARK 470     GLU A 132    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 138    NZ                                                  
REMARK 470     GLU A 143    OE1  OE2                                            
REMARK 470     CYS A 162    SG                                                  
REMARK 470     LYS A 168    CE   NZ                                             
REMARK 470     GLU A 174    CG   CD   OE1  OE2                                  
REMARK 470     ASN A 179    OD1  ND2                                            
REMARK 470     ILE A 180    O                                                   
REMARK 470     LYS A 181    CE   NZ                                             
REMARK 470     GLU A 193    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 198    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 201    CD   OE1  OE2                                       
REMARK 470     ASP A 232    OD1  OD2                                            
REMARK 470     LYS A 240    CD   CE   NZ                                        
REMARK 470     ASP A 243    CG   OD1  OD2                                       
REMARK 470     GLU A 256    OE1  OE2                                            
REMARK 470     LYS B 173    CD   CE   NZ                                        
REMARK 470     LYS C  13    NZ                                                  
REMARK 470     ARG C  53    CZ   NH1  NH2                                       
REMARK 470     ARG C  64    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS C  80    CD   CE   NZ                                        
REMARK 470     ARG C  91    CZ   NH1  NH2                                       
REMARK 470     GLU C  93    OE1  OE2                                            
REMARK 470     ASP C  94    CG   OD1  OD2                                       
REMARK 470     GLU C 109    CG   CD   OE1  OE2                                  
REMARK 470     ASP C 113    OD1  OD2                                            
REMARK 470     GLU C 115    CD   OE1  OE2                                       
REMARK 470     LEU C 121    CG   CD1  CD2                                       
REMARK 470     GLN C 125    CD   OE1  NE2                                       
REMARK 470     GLU C 132    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 138    CE   NZ                                             
REMARK 470     GLU C 143    OE1  OE2                                            
REMARK 470     CYS C 162    SG                                                  
REMARK 470     LYS C 168    CE   NZ                                             
REMARK 470     GLU C 174    CG   CD   OE1  OE2                                  
REMARK 470     ASN C 179    OD1  ND2                                            
REMARK 470     ILE C 180    O                                                   
REMARK 470     LYS C 181    CE   NZ                                             
REMARK 470     GLU C 198    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 201    OE1  OE2                                            
REMARK 470     ASP C 232    OD1  OD2                                            
REMARK 470     LYS C 240    CD   CE   NZ                                        
REMARK 470     ASP C 243    CG   OD1  OD2                                       
REMARK 470     LYS D 173    CD   CE   NZ                                        
REMARK 470     ARG E   5    CZ   NH1  NH2                                       
REMARK 470     GLN E   8    CD   OE1  NE2                                       
REMARK 470     ARG E  53    CZ   NH1  NH2                                       
REMARK 470     ARG E  61    CZ   NH1  NH2                                       
REMARK 470     ARG E  64    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS E  80    CD   CE   NZ                                        
REMARK 470     ARG E  91    CZ   NH1  NH2                                       
REMARK 470     GLU E  93    OE1  OE2                                            
REMARK 470     ASP E  94    OD1  OD2                                            
REMARK 470     GLU E 109    CG   CD   OE1  OE2                                  
REMARK 470     ASP E 113    OD1  OD2                                            
REMARK 470     GLU E 115    CD   OE1  OE2                                       
REMARK 470     LEU E 121    CG   CD1  CD2                                       
REMARK 470     GLN E 125    CD   OE1  NE2                                       
REMARK 470     GLU E 132    CG   CD   OE1  OE2                                  
REMARK 470     LYS E 138    CD   CE   NZ                                        
REMARK 470     GLU E 143    OE1  OE2                                            
REMARK 470     LYS E 168    CE   NZ                                             
REMARK 470     GLU E 174    CG   CD   OE1  OE2                                  
REMARK 470     ASN E 179    OD1  ND2                                            
REMARK 470     ILE E 180    O                                                   
REMARK 470     LYS E 181    CE   NZ                                             
REMARK 470     GLU E 193    CG   CD   OE1  OE2                                  
REMARK 470     GLU E 198    CG   CD   OE1  OE2                                  
REMARK 470     GLU E 201    CD   OE1  OE2                                       
REMARK 470     ASP E 232    OD1  OD2                                            
REMARK 470     LYS E 240    CD   CE   NZ                                        
REMARK 470     ASP E 243    CG   OD1  OD2                                       
REMARK 470     LYS F 173    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    MET A   119     O    HOH A   301              2.02            
REMARK 500   O    SER E    42     O    HOH E   301              2.12            
REMARK 500   NE2  GLN C    38     O    LEU C   126              2.14            
REMARK 500   NE2  GLN E    38     O    LEU E   126              2.15            
REMARK 500   NE2  GLN A    38     O    LEU A   126              2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH C   312     O    HOH C   312     2557     2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ILE A  87   CG1 -  CB  -  CG2 ANGL. DEV. = -14.0 DEGREES          
REMARK 500    LEU E  16   CA  -  CB  -  CG  ANGL. DEV. = -14.2 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLU A 201      144.66   -170.20                                   
REMARK 500    ALA A 242      118.54    -38.84                                   
REMARK 500    ASP A 243      -56.71     81.88                                   
REMARK 500    ALA C 242      119.17    -38.69                                   
REMARK 500    ASP C 243      -56.90     82.19                                   
REMARK 500    LYS D 173      -67.18   -108.11                                   
REMARK 500    GLU E 201      145.44   -171.33                                   
REMARK 500    ALA E 242      118.61    -38.28                                   
REMARK 500    ASP E 243      -56.17     81.24                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  6K3A A    1   261  UNP    P12004   PCNA_HUMAN       1    261             
DBREF  6K3A B  161   180  UNP    K7ERQ1   K7ERQ1_HUMAN    40     59             
DBREF  6K3A C    1   261  UNP    P12004   PCNA_HUMAN       1    261             
DBREF  6K3A D  161   180  UNP    K7ERQ1   K7ERQ1_HUMAN    40     59             
DBREF  6K3A E    1   261  UNP    P12004   PCNA_HUMAN       1    261             
DBREF  6K3A F  161   180  UNP    K7ERQ1   K7ERQ1_HUMAN    40     59             
SEQADV 6K3A GLY A   -2  UNP  P12004              EXPRESSION TAG                 
SEQADV 6K3A PRO A   -1  UNP  P12004              EXPRESSION TAG                 
SEQADV 6K3A GLY A    0  UNP  P12004              EXPRESSION TAG                 
SEQADV 6K3A GLY C   -2  UNP  P12004              EXPRESSION TAG                 
SEQADV 6K3A PRO C   -1  UNP  P12004              EXPRESSION TAG                 
SEQADV 6K3A GLY C    0  UNP  P12004              EXPRESSION TAG                 
SEQADV 6K3A GLY E   -2  UNP  P12004              EXPRESSION TAG                 
SEQADV 6K3A PRO E   -1  UNP  P12004              EXPRESSION TAG                 
SEQADV 6K3A GLY E    0  UNP  P12004              EXPRESSION TAG                 
SEQRES   1 A  264  GLY PRO GLY MET PHE GLU ALA ARG LEU VAL GLN GLY SER          
SEQRES   2 A  264  ILE LEU LYS LYS VAL LEU GLU ALA LEU LYS ASP LEU ILE          
SEQRES   3 A  264  ASN GLU ALA CYS TRP ASP ILE SER SER SER GLY VAL ASN          
SEQRES   4 A  264  LEU GLN SER MET ASP SER SER HIS VAL SER LEU VAL GLN          
SEQRES   5 A  264  LEU THR LEU ARG SER GLU GLY PHE ASP THR TYR ARG CYS          
SEQRES   6 A  264  ASP ARG ASN LEU ALA MET GLY VAL ASN LEU THR SER MET          
SEQRES   7 A  264  SER LYS ILE LEU LYS CYS ALA GLY ASN GLU ASP ILE ILE          
SEQRES   8 A  264  THR LEU ARG ALA GLU ASP ASN ALA ASP THR LEU ALA LEU          
SEQRES   9 A  264  VAL PHE GLU ALA PRO ASN GLN GLU LYS VAL SER ASP TYR          
SEQRES  10 A  264  GLU MET LYS LEU MET ASP LEU ASP VAL GLU GLN LEU GLY          
SEQRES  11 A  264  ILE PRO GLU GLN GLU TYR SER CYS VAL VAL LYS MET PRO          
SEQRES  12 A  264  SER GLY GLU PHE ALA ARG ILE CYS ARG ASP LEU SER HIS          
SEQRES  13 A  264  ILE GLY ASP ALA VAL VAL ILE SER CYS ALA LYS ASP GLY          
SEQRES  14 A  264  VAL LYS PHE SER ALA SER GLY GLU LEU GLY ASN GLY ASN          
SEQRES  15 A  264  ILE LYS LEU SER GLN THR SER ASN VAL ASP LYS GLU GLU          
SEQRES  16 A  264  GLU ALA VAL THR ILE GLU MET ASN GLU PRO VAL GLN LEU          
SEQRES  17 A  264  THR PHE ALA LEU ARG TYR LEU ASN PHE PHE THR LYS ALA          
SEQRES  18 A  264  THR PRO LEU SER SER THR VAL THR LEU SER MET SER ALA          
SEQRES  19 A  264  ASP VAL PRO LEU VAL VAL GLU TYR LYS ILE ALA ASP MET          
SEQRES  20 A  264  GLY HIS LEU LYS TYR TYR LEU ALA PRO LYS ILE GLU ASP          
SEQRES  21 A  264  GLU GLU GLY SER                                              
SEQRES   1 B   20  SER THR ARG GLN THR THR ILE THR SER HIS PHE ALA LYS          
SEQRES   2 B   20  GLY PRO ALA LYS ARG LYS PRO                                  
SEQRES   1 C  264  GLY PRO GLY MET PHE GLU ALA ARG LEU VAL GLN GLY SER          
SEQRES   2 C  264  ILE LEU LYS LYS VAL LEU GLU ALA LEU LYS ASP LEU ILE          
SEQRES   3 C  264  ASN GLU ALA CYS TRP ASP ILE SER SER SER GLY VAL ASN          
SEQRES   4 C  264  LEU GLN SER MET ASP SER SER HIS VAL SER LEU VAL GLN          
SEQRES   5 C  264  LEU THR LEU ARG SER GLU GLY PHE ASP THR TYR ARG CYS          
SEQRES   6 C  264  ASP ARG ASN LEU ALA MET GLY VAL ASN LEU THR SER MET          
SEQRES   7 C  264  SER LYS ILE LEU LYS CYS ALA GLY ASN GLU ASP ILE ILE          
SEQRES   8 C  264  THR LEU ARG ALA GLU ASP ASN ALA ASP THR LEU ALA LEU          
SEQRES   9 C  264  VAL PHE GLU ALA PRO ASN GLN GLU LYS VAL SER ASP TYR          
SEQRES  10 C  264  GLU MET LYS LEU MET ASP LEU ASP VAL GLU GLN LEU GLY          
SEQRES  11 C  264  ILE PRO GLU GLN GLU TYR SER CYS VAL VAL LYS MET PRO          
SEQRES  12 C  264  SER GLY GLU PHE ALA ARG ILE CYS ARG ASP LEU SER HIS          
SEQRES  13 C  264  ILE GLY ASP ALA VAL VAL ILE SER CYS ALA LYS ASP GLY          
SEQRES  14 C  264  VAL LYS PHE SER ALA SER GLY GLU LEU GLY ASN GLY ASN          
SEQRES  15 C  264  ILE LYS LEU SER GLN THR SER ASN VAL ASP LYS GLU GLU          
SEQRES  16 C  264  GLU ALA VAL THR ILE GLU MET ASN GLU PRO VAL GLN LEU          
SEQRES  17 C  264  THR PHE ALA LEU ARG TYR LEU ASN PHE PHE THR LYS ALA          
SEQRES  18 C  264  THR PRO LEU SER SER THR VAL THR LEU SER MET SER ALA          
SEQRES  19 C  264  ASP VAL PRO LEU VAL VAL GLU TYR LYS ILE ALA ASP MET          
SEQRES  20 C  264  GLY HIS LEU LYS TYR TYR LEU ALA PRO LYS ILE GLU ASP          
SEQRES  21 C  264  GLU GLU GLY SER                                              
SEQRES   1 D   20  SER THR ARG GLN THR THR ILE THR SER HIS PHE ALA LYS          
SEQRES   2 D   20  GLY PRO ALA LYS ARG LYS PRO                                  
SEQRES   1 E  264  GLY PRO GLY MET PHE GLU ALA ARG LEU VAL GLN GLY SER          
SEQRES   2 E  264  ILE LEU LYS LYS VAL LEU GLU ALA LEU LYS ASP LEU ILE          
SEQRES   3 E  264  ASN GLU ALA CYS TRP ASP ILE SER SER SER GLY VAL ASN          
SEQRES   4 E  264  LEU GLN SER MET ASP SER SER HIS VAL SER LEU VAL GLN          
SEQRES   5 E  264  LEU THR LEU ARG SER GLU GLY PHE ASP THR TYR ARG CYS          
SEQRES   6 E  264  ASP ARG ASN LEU ALA MET GLY VAL ASN LEU THR SER MET          
SEQRES   7 E  264  SER LYS ILE LEU LYS CYS ALA GLY ASN GLU ASP ILE ILE          
SEQRES   8 E  264  THR LEU ARG ALA GLU ASP ASN ALA ASP THR LEU ALA LEU          
SEQRES   9 E  264  VAL PHE GLU ALA PRO ASN GLN GLU LYS VAL SER ASP TYR          
SEQRES  10 E  264  GLU MET LYS LEU MET ASP LEU ASP VAL GLU GLN LEU GLY          
SEQRES  11 E  264  ILE PRO GLU GLN GLU TYR SER CYS VAL VAL LYS MET PRO          
SEQRES  12 E  264  SER GLY GLU PHE ALA ARG ILE CYS ARG ASP LEU SER HIS          
SEQRES  13 E  264  ILE GLY ASP ALA VAL VAL ILE SER CYS ALA LYS ASP GLY          
SEQRES  14 E  264  VAL LYS PHE SER ALA SER GLY GLU LEU GLY ASN GLY ASN          
SEQRES  15 E  264  ILE LYS LEU SER GLN THR SER ASN VAL ASP LYS GLU GLU          
SEQRES  16 E  264  GLU ALA VAL THR ILE GLU MET ASN GLU PRO VAL GLN LEU          
SEQRES  17 E  264  THR PHE ALA LEU ARG TYR LEU ASN PHE PHE THR LYS ALA          
SEQRES  18 E  264  THR PRO LEU SER SER THR VAL THR LEU SER MET SER ALA          
SEQRES  19 E  264  ASP VAL PRO LEU VAL VAL GLU TYR LYS ILE ALA ASP MET          
SEQRES  20 E  264  GLY HIS LEU LYS TYR TYR LEU ALA PRO LYS ILE GLU ASP          
SEQRES  21 E  264  GLU GLU GLY SER                                              
SEQRES   1 F   20  SER THR ARG GLN THR THR ILE THR SER HIS PHE ALA LYS          
SEQRES   2 F   20  GLY PRO ALA LYS ARG LYS PRO                                  
FORMUL   7  HOH   *46(H2 O)                                                     
HELIX    1 AA1 GLY A    9  LYS A   20  1                                  12    
HELIX    2 AA2 GLU A   55  PHE A   57  5                                   3    
HELIX    3 AA3 LEU A   72  LYS A   80  1                                   9    
HELIX    4 AA4 SER A  141  HIS A  153  1                                  13    
HELIX    5 AA5 LEU A  209  THR A  216  1                                   8    
HELIX    6 AA6 LYS A  217  SER A  222  5                                   6    
HELIX    7 AA7 THR B  166  HIS B  170  5                                   5    
HELIX    8 AA8 GLY C    9  LYS C   20  1                                  12    
HELIX    9 AA9 GLU C   55  PHE C   57  5                                   3    
HELIX   10 AB1 LEU C   72  LYS C   80  1                                   9    
HELIX   11 AB2 SER C  141  HIS C  153  1                                  13    
HELIX   12 AB3 LEU C  209  THR C  216  1                                   8    
HELIX   13 AB4 LYS C  217  SER C  222  5                                   6    
HELIX   14 AB5 THR D  166  HIS D  170  5                                   5    
HELIX   15 AB6 GLY E    9  LYS E   20  1                                  12    
HELIX   16 AB7 GLU E   55  PHE E   57  5                                   3    
HELIX   17 AB8 LEU E   72  LYS E   80  1                                   9    
HELIX   18 AB9 SER E  141  HIS E  153  1                                  13    
HELIX   19 AC1 LEU E  209  THR E  216  1                                   8    
HELIX   20 AC2 LYS E  217  SER E  222  5                                   6    
HELIX   21 AC3 THR F  166  HIS F  170  5                                   5    
SHEET    1 AA1 9 THR A  59  CYS A  62  0                                        
SHEET    2 AA1 9 PHE A   2  LEU A   6 -1  N  GLU A   3   O  ARG A  61           
SHEET    3 AA1 9 ILE A  87  ALA A  92 -1  O  ALA A  92   N  PHE A   2           
SHEET    4 AA1 9 THR A  98  GLU A 104 -1  O  ALA A 100   N  ARG A  91           
SHEET    5 AA1 9 VAL A 111  LYS A 117 -1  O  TYR A 114   N  LEU A 101           
SHEET    6 AA1 9 GLY E 176  ASN E 179 -1  O  ASN E 179   N  ASP A 113           
SHEET    7 AA1 9 LYS E 168  SER E 172 -1  N  ALA E 171   O  GLY E 178           
SHEET    8 AA1 9 ALA E 157  CYS E 162 -1  N  SER E 161   O  LYS E 168           
SHEET    9 AA1 9 VAL E 203  ALA E 208 -1  O  LEU E 205   N  ILE E 160           
SHEET    1 AA2 9 LEU A  66  ASN A  71  0                                        
SHEET    2 AA2 9 GLU A  25  SER A  31 -1  N  ILE A  30   O  LEU A  66           
SHEET    3 AA2 9 GLY A  34  MET A  40 -1  O  ASN A  36   N  ASP A  29           
SHEET    4 AA2 9 SER A  46  ARG A  53 -1  O  LEU A  50   N  LEU A  37           
SHEET    5 AA2 9 GLY A 245  LEU A 251 -1  O  LYS A 248   N  GLN A  49           
SHEET    6 AA2 9 LEU A 235  ILE A 241 -1  N  TYR A 239   O  LEU A 247           
SHEET    7 AA2 9 THR A 224  MET A 229 -1  N  SER A 228   O  VAL A 236           
SHEET    8 AA2 9 CYS A 135  PRO A 140 -1  N  MET A 139   O  VAL A 225           
SHEET    9 AA2 9 THR A 196  MET A 199 -1  O  THR A 196   N  LYS A 138           
SHEET    1 AA3 9 VAL A 203  ALA A 208  0                                        
SHEET    2 AA3 9 ALA A 157  CYS A 162 -1  N  ILE A 160   O  LEU A 205           
SHEET    3 AA3 9 LYS A 168  SER A 172 -1  O  LYS A 168   N  SER A 161           
SHEET    4 AA3 9 GLY A 176  ASN A 179 -1  O  GLY A 178   N  ALA A 171           
SHEET    5 AA3 9 VAL C 111  LYS C 117 -1  O  ASP C 113   N  ASN A 179           
SHEET    6 AA3 9 THR C  98  GLU C 104 -1  N  LEU C 101   O  TYR C 114           
SHEET    7 AA3 9 ILE C  87  ALA C  92 -1  N  ILE C  87   O  GLU C 104           
SHEET    8 AA3 9 PHE C   2  LEU C   6 -1  N  LEU C   6   O  ILE C  88           
SHEET    9 AA3 9 THR C  59  CYS C  62 -1  O  THR C  59   N  ARG C   5           
SHEET    1 AA4 2 LYS A 254  ILE A 255  0                                        
SHEET    2 AA4 2 ARG B 163  GLN B 164 -1  O  ARG B 163   N  ILE A 255           
SHEET    1 AA5 9 LEU C  66  ASN C  71  0                                        
SHEET    2 AA5 9 GLU C  25  SER C  31 -1  N  ILE C  30   O  LEU C  66           
SHEET    3 AA5 9 GLY C  34  MET C  40 -1  O  ASN C  36   N  ASP C  29           
SHEET    4 AA5 9 SER C  46  ARG C  53 -1  O  LEU C  50   N  LEU C  37           
SHEET    5 AA5 9 GLY C 245  LEU C 251 -1  O  LYS C 248   N  GLN C  49           
SHEET    6 AA5 9 LEU C 235  ILE C 241 -1  N  TYR C 239   O  LEU C 247           
SHEET    7 AA5 9 THR C 224  MET C 229 -1  N  SER C 228   O  VAL C 236           
SHEET    8 AA5 9 CYS C 135  PRO C 140 -1  N  CYS C 135   O  MET C 229           
SHEET    9 AA5 9 THR C 196  MET C 199 -1  O  THR C 196   N  LYS C 138           
SHEET    1 AA6 9 VAL C 203  ALA C 208  0                                        
SHEET    2 AA6 9 ALA C 157  CYS C 162 -1  N  ILE C 160   O  LEU C 205           
SHEET    3 AA6 9 LYS C 168  GLY C 173 -1  O  LYS C 168   N  SER C 161           
SHEET    4 AA6 9 GLY C 176  ASN C 179 -1  O  GLY C 176   N  GLY C 173           
SHEET    5 AA6 9 VAL E 111  LYS E 117 -1  O  ASP E 113   N  ASN C 179           
SHEET    6 AA6 9 THR E  98  GLU E 104 -1  N  LEU E 101   O  TYR E 114           
SHEET    7 AA6 9 ILE E  87  ALA E  92 -1  N  ARG E  91   O  ALA E 100           
SHEET    8 AA6 9 PHE E   2  LEU E   6 -1  N  PHE E   2   O  ALA E  92           
SHEET    9 AA6 9 THR E  59  CYS E  62 -1  O  THR E  59   N  ARG E   5           
SHEET    1 AA7 2 LYS C 254  ILE C 255  0                                        
SHEET    2 AA7 2 ARG D 163  GLN D 164 -1  O  ARG D 163   N  ILE C 255           
SHEET    1 AA8 9 LEU E  66  ASN E  71  0                                        
SHEET    2 AA8 9 GLU E  25  SER E  31 -1  N  ILE E  30   O  LEU E  66           
SHEET    3 AA8 9 GLY E  34  MET E  40 -1  O  ASN E  36   N  ASP E  29           
SHEET    4 AA8 9 SER E  46  ARG E  53 -1  O  LEU E  50   N  LEU E  37           
SHEET    5 AA8 9 GLY E 245  LEU E 251 -1  O  LYS E 248   N  GLN E  49           
SHEET    6 AA8 9 LEU E 235  ILE E 241 -1  N  VAL E 237   O  TYR E 249           
SHEET    7 AA8 9 THR E 224  MET E 229 -1  N  SER E 228   O  VAL E 236           
SHEET    8 AA8 9 CYS E 135  PRO E 140 -1  N  CYS E 135   O  MET E 229           
SHEET    9 AA8 9 THR E 196  MET E 199 -1  O  THR E 196   N  LYS E 138           
SHEET    1 AA9 2 LYS E 254  ILE E 255  0                                        
SHEET    2 AA9 2 ARG F 163  GLN F 164 -1  O  ARG F 163   N  ILE E 255           
CRYST1  141.540   81.598   68.105  90.00  90.02  90.00 C 1 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      0.007065  0.000000  0.000003        0.00000                         
SCALE2      0.000000  0.012255  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014683        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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