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Database: PDB
Entry: 6HVO
LinkDB: 6HVO
Original site: 6HVO 
HEADER    REPLICATION                             11-OCT-18   6HVO              
TITLE     CRYSTAL STRUCTURE OF HUMAN PCNA IN COMPLEX WITH THREE PEPTIDES OF P12 
TITLE    2 SUBUNIT OF HUMAN POLYMERASE DELTA                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROLIFERATING CELL NUCLEAR ANTIGEN;                        
COMPND   3 CHAIN: A, B, C;                                                      
COMPND   4 SYNONYM: PCNA,CYCLIN;                                                
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: DNA POLYMERASE DELTA SUBUNIT 4;                            
COMPND   8 CHAIN: D, F, E;                                                      
COMPND   9 SYNONYM: DNA POLYMERASE DELTA SUBUNIT P12;                           
COMPND  10 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 BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: POLD4, POLDS;                                                  
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 469008                                      
KEYWDS    PCNA, POLD4, P12, REPLICATION, POLYMERASE DELTA, CRYSTAL              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.GONZALEZ-MAGANA,M.ROMANO-MORENO,A.L.ROJAS,F.J.BLANCO,A.DE BIASIO    
REVDAT   3   27-MAR-19 6HVO    1       JRNL                                     
REVDAT   2   30-JAN-19 6HVO    1       JRNL                                     
REVDAT   1   23-JAN-19 6HVO    0                                                
JRNL        AUTH   A.GONZALEZ-MAGANA,A.IBANEZ DE OPAKUA,M.ROMANO-MORENO,        
JRNL        AUTH 2 J.MURCIANO-CALLES,N.MERINO,I.LUQUE,A.L.ROJAS,S.ONESTI,       
JRNL        AUTH 3 F.J.BLANCO,A.DE BIASIO                                       
JRNL        TITL   THE P12 SUBUNIT OF HUMAN POLYMERASE DELTA USES AN ATYPICAL   
JRNL        TITL 2 PIP BOX FOR MOLECULAR RECOGNITION OF PROLIFERATING CELL      
JRNL        TITL 3 NUCLEAR ANTIGEN (PCNA).                                      
JRNL        REF    J.BIOL.CHEM.                  V. 294  3947 2019              
JRNL        REFN                   ESSN 1083-351X                               
JRNL        PMID   30655288                                                     
JRNL        DOI    10.1074/JBC.RA118.006391                                     
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0222                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 73.88                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 52745                          
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 + TEST SET) : 0.198                           
REMARK   3   R VALUE            (WORKING SET) : 0.195                           
REMARK   3   FREE R VALUE                     : 0.244                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2779                            
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) : 2.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.16                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3833                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.0                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3060                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 199                          
REMARK   3   BIN FREE R VALUE                    : 0.3490                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6147                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 35                                      
REMARK   3   SOLVENT ATOMS            : 243                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 48.84                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.38000                                              
REMARK   3    B22 (A**2) : -0.41000                                             
REMARK   3    B33 (A**2) : -0.97000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.206         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.184         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.155         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.148         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.964                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.940                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6381 ; 0.010 ; 0.015       
REMARK   3   BOND LENGTHS OTHERS               (A):  5947 ; 0.001 ; 0.017       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  8658 ; 1.445 ; 1.731       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 13968 ; 0.490 ; 1.701       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   830 ; 6.830 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   183 ;39.579 ;20.273       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1016 ;16.474 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    29 ;18.448 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   873 ; 0.067 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  7050 ; 0.008 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1070 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS U VALUES : REFINED INDIVIDUALLY                           
REMARK   4                                                                      
REMARK   4 6HVO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-OCT-18.                  
REMARK 100 THE DEPOSITION ID IS D_1200012380.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 02-FEB-18                          
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               : ALBA                               
REMARK 200  BEAMLINE                       : XALOC                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97925                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS 0.5.17                     
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 55602                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 154.980                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 12.90                              
REMARK 200  R MERGE                    (I) : 0.16600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.16                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 13.20                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.09600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
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: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.96                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.61                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: BIS TRIS 6.5 , LI2SO4 (0.2M), PEG 3350   
REMARK 280  24%, PH 6.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
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       35.98250            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       77.49100            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       41.94400            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       77.49100            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       35.98250            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       41.94400            
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: 9540 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 35750 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -121.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, F, E                      
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A    -2                                                      
REMARK 465     VAL A   188                                                      
REMARK 465     ASP A   189                                                      
REMARK 465     LYS A   190                                                      
REMARK 465     GLU A   256                                                      
REMARK 465     ASP A   257                                                      
REMARK 465     GLU A   258                                                      
REMARK 465     GLU A   259                                                      
REMARK 465     GLY A   260                                                      
REMARK 465     SER A   261                                                      
REMARK 465     GLY B    -2                                                      
REMARK 465     PRO B    -1                                                      
REMARK 465     HIS B     0                                                      
REMARK 465     VAL B   188                                                      
REMARK 465     ASP B   189                                                      
REMARK 465     LYS B   190                                                      
REMARK 465     GLU B   256                                                      
REMARK 465     ASP B   257                                                      
REMARK 465     GLU B   258                                                      
REMARK 465     GLU B   259                                                      
REMARK 465     GLY B   260                                                      
REMARK 465     SER B   261                                                      
REMARK 465     GLY C    -2                                                      
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     ASP C   257                                                      
REMARK 465     GLU C   258                                                      
REMARK 465     GLU C   259                                                      
REMARK 465     GLY C   260                                                      
REMARK 465     SER C   261                                                      
REMARK 465     MET D     1                                                      
REMARK 465     GLY D     2                                                      
REMARK 465     ARG D     3                                                      
REMARK 465     ARG D    16                                                      
REMARK 465     ARG D    17                                                      
REMARK 465     GLU D    18                                                      
REMARK 465     GLY D    19                                                      
REMARK 465     MET F     1                                                      
REMARK 465     GLY F     2                                                      
REMARK 465     ARG F    16                                                      
REMARK 465     ARG F    17                                                      
REMARK 465     GLU F    18                                                      
REMARK 465     GLY F    19                                                      
REMARK 465     MET E     1                                                      
REMARK 465     GLY E     2                                                      
REMARK 465     LYS E    15                                                      
REMARK 465     ARG E    16                                                      
REMARK 465     ARG E    17                                                      
REMARK 465     GLU E    18                                                      
REMARK 465     GLY E    19                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    HIS A   0       75.52     62.33                                   
REMARK 500    ALA A 242     -120.52     38.44                                   
REMARK 500    ASN B  95       55.83   -119.52                                   
REMARK 500    ASN B 200      -51.66   -126.62                                   
REMARK 500    ALA B 242     -120.10     41.16                                   
REMARK 500    ASN C 107      -11.36     82.39                                   
REMARK 500    ASP C 232       -2.20     72.89                                   
REMARK 500    MET C 244      -46.77   -142.65                                   
REMARK 500    VAL D  14       -7.95   -145.15                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 303                 
DBREF  6HVO A    1   261  UNP    P12004   PCNA_HUMAN       1    261             
DBREF  6HVO B    1   261  UNP    P12004   PCNA_HUMAN       1    261             
DBREF  6HVO C    1   261  UNP    P12004   PCNA_HUMAN       1    261             
DBREF  6HVO D    1    19  UNP    Q9HCU8   DPOD4_HUMAN      1     19             
DBREF  6HVO F    1    19  UNP    Q9HCU8   DPOD4_HUMAN      1     19             
DBREF  6HVO E    1    19  UNP    Q9HCU8   DPOD4_HUMAN      1     19             
SEQADV 6HVO GLY A   -2  UNP  P12004              EXPRESSION TAG                 
SEQADV 6HVO PRO A   -1  UNP  P12004              EXPRESSION TAG                 
SEQADV 6HVO HIS A    0  UNP  P12004              EXPRESSION TAG                 
SEQADV 6HVO GLY B   -2  UNP  P12004              EXPRESSION TAG                 
SEQADV 6HVO PRO B   -1  UNP  P12004              EXPRESSION TAG                 
SEQADV 6HVO HIS B    0  UNP  P12004              EXPRESSION TAG                 
SEQADV 6HVO GLY C   -2  UNP  P12004              EXPRESSION TAG                 
SEQADV 6HVO PRO C   -1  UNP  P12004              EXPRESSION TAG                 
SEQADV 6HVO HIS C    0  UNP  P12004              EXPRESSION TAG                 
SEQRES   1 A  264  GLY PRO HIS 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  264  GLY PRO HIS MET PHE GLU ALA ARG LEU VAL GLN GLY SER          
SEQRES   2 B  264  ILE LEU LYS LYS VAL LEU GLU ALA LEU LYS ASP LEU ILE          
SEQRES   3 B  264  ASN GLU ALA CYS TRP ASP ILE SER SER SER GLY VAL ASN          
SEQRES   4 B  264  LEU GLN SER MET ASP SER SER HIS VAL SER LEU VAL GLN          
SEQRES   5 B  264  LEU THR LEU ARG SER GLU GLY PHE ASP THR TYR ARG CYS          
SEQRES   6 B  264  ASP ARG ASN LEU ALA MET GLY VAL ASN LEU THR SER MET          
SEQRES   7 B  264  SER LYS ILE LEU LYS CYS ALA GLY ASN GLU ASP ILE ILE          
SEQRES   8 B  264  THR LEU ARG ALA GLU ASP ASN ALA ASP THR LEU ALA LEU          
SEQRES   9 B  264  VAL PHE GLU ALA PRO ASN GLN GLU LYS VAL SER ASP TYR          
SEQRES  10 B  264  GLU MET LYS LEU MET ASP LEU ASP VAL GLU GLN LEU GLY          
SEQRES  11 B  264  ILE PRO GLU GLN GLU TYR SER CYS VAL VAL LYS MET PRO          
SEQRES  12 B  264  SER GLY GLU PHE ALA ARG ILE CYS ARG ASP LEU SER HIS          
SEQRES  13 B  264  ILE GLY ASP ALA VAL VAL ILE SER CYS ALA LYS ASP GLY          
SEQRES  14 B  264  VAL LYS PHE SER ALA SER GLY GLU LEU GLY ASN GLY ASN          
SEQRES  15 B  264  ILE LYS LEU SER GLN THR SER ASN VAL ASP LYS GLU GLU          
SEQRES  16 B  264  GLU ALA VAL THR ILE GLU MET ASN GLU PRO VAL GLN LEU          
SEQRES  17 B  264  THR PHE ALA LEU ARG TYR LEU ASN PHE PHE THR LYS ALA          
SEQRES  18 B  264  THR PRO LEU SER SER THR VAL THR LEU SER MET SER ALA          
SEQRES  19 B  264  ASP VAL PRO LEU VAL VAL GLU TYR LYS ILE ALA ASP MET          
SEQRES  20 B  264  GLY HIS LEU LYS TYR TYR LEU ALA PRO LYS ILE GLU ASP          
SEQRES  21 B  264  GLU GLU GLY SER                                              
SEQRES   1 C  264  GLY PRO HIS 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   19  MET GLY ARG LYS ARG LEU ILE THR ASP SER TYR PRO VAL          
SEQRES   2 D   19  VAL LYS ARG ARG GLU GLY                                      
SEQRES   1 F   19  MET GLY ARG LYS ARG LEU ILE THR ASP SER TYR PRO VAL          
SEQRES   2 F   19  VAL LYS ARG ARG GLU GLY                                      
SEQRES   1 E   19  MET GLY ARG LYS ARG LEU ILE THR ASP SER TYR PRO VAL          
SEQRES   2 E   19  VAL LYS ARG ARG GLU GLY                                      
HET    SO4  A 301       5                                                       
HET    SO4  A 302       5                                                       
HET    SO4  B 301       5                                                       
HET    SO4  B 302       5                                                       
HET    SO4  C 301       5                                                       
HET    SO4  C 302       5                                                       
HET    SO4  C 303       5                                                       
HETNAM     SO4 SULFATE ION                                                      
FORMUL   7  SO4    7(O4 S 2-)                                                   
FORMUL  14  HOH   *243(H2 O)                                                    
HELIX    1 AA1 GLN A    8  ALA A   18  1                                  11    
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 GLY B    9  LYS B   20  1                                  12    
HELIX    8 AA8 GLU B   55  PHE B   57  5                                   3    
HELIX    9 AA9 LEU B   72  LYS B   80  1                                   9    
HELIX   10 AB1 SER B  141  SER B  152  1                                  12    
HELIX   11 AB2 LEU B  209  THR B  216  1                                   8    
HELIX   12 AB3 LYS B  217  SER B  222  5                                   6    
HELIX   13 AB4 GLY C    9  ALA C   18  1                                  10    
HELIX   14 AB5 GLU C   55  PHE C   57  5                                   3    
HELIX   15 AB6 LEU C   72  LYS C   80  1                                   9    
HELIX   16 AB7 SER C  141  HIS C  153  1                                  13    
HELIX   17 AB8 LEU C  209  THR C  216  1                                   8    
HELIX   18 AB9 LYS C  217  SER C  222  5                                   6    
HELIX   19 AC1 LEU D    6  SER D   10  5                                   5    
HELIX   20 AC2 LEU F    6  SER F   10  5                                   5    
HELIX   21 AC3 LEU E    6  SER E   10  5                                   5    
SHEET    1 AA1 9 THR A  59  CYS A  62  0                                        
SHEET    2 AA1 9 MET A   1  LEU A   6 -1  N  GLU A   3   O  ARG A  61           
SHEET    3 AA1 9 ILE A  87  GLU A  93 -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 LYS A 110  LYS A 117 -1  O  SER A 112   N  PHE A 103           
SHEET    6 AA1 9 GLY B 176  SER B 183 -1  O  LYS B 181   N  VAL A 111           
SHEET    7 AA1 9 GLY B 166  SER B 172 -1  N  PHE B 169   O  ILE B 180           
SHEET    8 AA1 9 ALA B 157  CYS B 162 -1  N  SER B 161   O  LYS B 168           
SHEET    9 AA1 9 VAL B 203  ALA B 208 -1  O  LEU B 205   N  ILE B 160           
SHEET    1 AA2 9 LEU A  66  ASN A  71  0                                        
SHEET    2 AA2 9 GLU A  25  ILE A  30 -1  N  TRP A  28   O  MET A  68           
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  VAL A  48   N  SER A  39           
SHEET    5 AA2 9 GLY A 245  LEU A 251 -1  O  TYR A 250   N  LEU A  47           
SHEET    6 AA2 9 LEU A 235  ILE A 241 -1  N  VAL A 237   O  TYR A 249           
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  CYS A 135   O  MET A 229           
SHEET    9 AA2 9 THR A 196  MET A 199 -1  O  GLU A 198   N  VAL A 136           
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 GLY A 166  GLY A 173 -1  O  LYS A 168   N  SER A 161           
SHEET    4 AA3 9 GLY A 176  SER A 183 -1  O  LEU A 182   N  VAL A 167           
SHEET    5 AA3 9 LYS C 110  LYS C 117 -1  O  VAL C 111   N  LYS A 181           
SHEET    6 AA3 9 THR C  98  GLU C 104 -1  N  LEU C  99   O  MET C 116           
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 9 THR B  59  CYS B  62  0                                        
SHEET    2 AA4 9 PHE B   2  LEU B   6 -1  N  GLU B   3   O  ARG B  61           
SHEET    3 AA4 9 ILE B  87  ALA B  92 -1  O  LEU B  90   N  ALA B   4           
SHEET    4 AA4 9 THR B  98  GLU B 104 -1  O  ALA B 100   N  ARG B  91           
SHEET    5 AA4 9 LYS B 110  LYS B 117 -1  O  SER B 112   N  PHE B 103           
SHEET    6 AA4 9 GLY C 176  SER C 183 -1  O  LYS C 181   N  VAL B 111           
SHEET    7 AA4 9 GLY C 166  GLY C 173 -1  N  PHE C 169   O  ILE C 180           
SHEET    8 AA4 9 ALA C 157  CYS C 162 -1  N  SER C 161   O  LYS C 168           
SHEET    9 AA4 9 VAL C 203  ALA C 208 -1  O  LEU C 205   N  ILE C 160           
SHEET    1 AA5 9 LEU B  66  ASN B  71  0                                        
SHEET    2 AA5 9 GLU B  25  SER B  31 -1  N  TRP B  28   O  MET B  68           
SHEET    3 AA5 9 GLY B  34  MET B  40 -1  O  GLY B  34   N  SER B  31           
SHEET    4 AA5 9 SER B  46  ARG B  53 -1  O  LEU B  52   N  VAL B  35           
SHEET    5 AA5 9 GLY B 245  LEU B 251 -1  O  TYR B 250   N  LEU B  47           
SHEET    6 AA5 9 LEU B 235  ILE B 241 -1  N  ILE B 241   O  GLY B 245           
SHEET    7 AA5 9 THR B 224  MET B 229 -1  N  SER B 228   O  VAL B 236           
SHEET    8 AA5 9 CYS B 135  PRO B 140 -1  N  MET B 139   O  VAL B 225           
SHEET    9 AA5 9 THR B 196  MET B 199 -1  O  THR B 196   N  LYS B 138           
SHEET    1 AA6 2 GLN B 125  LEU B 126  0                                        
SHEET    2 AA6 2 VAL D  13  LYS D  15 -1  O  VAL D  14   N  GLN B 125           
SHEET    1 AA7 9 LEU C  66  ASN C  71  0                                        
SHEET    2 AA7 9 GLU C  25  SER C  31 -1  N  TRP C  28   O  MET C  68           
SHEET    3 AA7 9 GLY C  34  MET C  40 -1  O  ASN C  36   N  ASP C  29           
SHEET    4 AA7 9 SER C  46  ARG C  53 -1  O  LEU C  50   N  LEU C  37           
SHEET    5 AA7 9 GLY C 245  LEU C 251 -1  O  TYR C 250   N  LEU C  47           
SHEET    6 AA7 9 LEU C 235  ILE C 241 -1  N  VAL C 237   O  TYR C 249           
SHEET    7 AA7 9 THR C 224  MET C 229 -1  N  THR C 226   O  GLU C 238           
SHEET    8 AA7 9 CYS C 135  PRO C 140 -1  N  MET C 139   O  VAL C 225           
SHEET    9 AA7 9 THR C 196  MET C 199 -1  O  GLU C 198   N  VAL C 136           
SHEET    1 AA8 2 GLN C 125  LEU C 126  0                                        
SHEET    2 AA8 2 VAL F  13  LYS F  15 -1  O  VAL F  14   N  GLN C 125           
SSBOND   1 CYS A  135    CYS A  162                          1555   1555  2.91  
SITE     1 AC1  3 ARG A 210  LYS A 254  LYS E   4                               
SITE     1 AC2  2 HIS A 153  LYS C  77                                          
SITE     1 AC3  4 ARG B  53  LYS B 240  HIS B 246  HOH B 411                    
SITE     1 AC4  4 ARG B  64  ASN B  65  ARG C  64  ASN C  65                    
SITE     1 AC5  3 SER C  42  SER C  43  LEU F   6                               
SITE     1 AC6  4 ALA C 208  ARG C 210  LYS C 254  HOH C 404                    
SITE     1 AC7  2 ARG C 146  ARG C 149                                          
CRYST1   71.965   83.888  154.982  90.00  90.00  90.00 P 21 21 21   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      0.013896  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011921  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006452        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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