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Database: PDB
Entry: 1W60
LinkDB: 1W60
Original site: 1W60 
HEADER    DNA-BINDING PROTEIN                     11-AUG-04   1W60              
TITLE     NATIVE HUMAN PCNA                                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROLIFERATING CELL NUCLEAR ANTIGEN;                        
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: PCNA, CYCLIN;                                               
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)                                  
KEYWDS    DNA, REPLICATION, PROCESSIVITY, ONCOGENE, DNA-BINDING                 
KEYWDS   2 PROTEIN, DNA REPLICATION, DNA-BINDING SYSTEMIC LUPUS                 
KEYWDS   3 ERYTHEMATOSUS                                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.KONTOPIDIS,S.WU,D.ZHELEVA,P.TAYLOR,C.MCINNES,D.LANE,                
AUTHOR   2 P.FISCHER,M.WALKINSHAW                                               
REVDAT   3   24-FEB-09 1W60    1       VERSN                                    
REVDAT   2   16-FEB-05 1W60    1       JRNL                                     
REVDAT   1   13-JAN-05 1W60    0                                                
JRNL        AUTH   G.KONTOPIDIS,S.WU,D.ZHELEVA,P.TAYLOR,C.MCINNES,              
JRNL        AUTH 2 D.LANE,P.FISCHER,M.WALKINSHAW                                
JRNL        TITL   STRUCTURAL AND BIOCHEMICAL STUDIES OF HUMAN                  
JRNL        TITL 2 PROLIFERATING CELL NUCLEAR ANTIGEN COMPLEXES                 
JRNL        TITL 3 PROVIDE A RATIONALE FOR CYCLIN ASSOCIATION AND               
JRNL        TITL 4 INHIBITOR DESIGN                                             
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 102  1871 2005              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   15681588                                                     
JRNL        DOI    10.1073/PNAS.0406540102                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.15 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.15                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 11.0                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0                              
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 8605                           
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) : 0.19695                         
REMARK   3   R VALUE            (WORKING SET) : 0.193                           
REMARK   3   FREE R VALUE                     : 0.278                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.8                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 430                             
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3926                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 58                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 50.8                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.33                                                
REMARK   3    B22 (A**2) : -0.33                                                
REMARK   3    B33 (A**2) : 0.49                                                 
REMARK   3    B12 (A**2) : -0.16                                                
REMARK   3    B13 (A**2) : 0.0                                                  
REMARK   3    B23 (A**2) : 0.0                                                  
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.612         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.456         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 26.46         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : NULL  ; NULL                
REMARK   3    ANGLE DISTANCE                  (A) : NULL  ; NULL                
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : NULL  ; NULL                
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : NULL  ; NULL                
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : NULL  ; NULL                
REMARK   3    MULTIPLE TORSION                (A) : NULL  ; NULL                
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL                
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : NULL  ; NULL                
REMARK   3    STAGGERED                 (DEGREES) : NULL  ; NULL                
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1W60 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-AUG-04.                  
REMARK 100 THE PDBE ID CODE IS EBI-15157.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-FEB-00                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 4.60                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SRS                                
REMARK 200  BEAMLINE                       : PX14.1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.3                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL                               
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS  (%): 49.2                                       
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.4                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 35% PEGMME 2K,                           
REMARK 280  0.1M NA ACETATE (PH4.6), 0.2M AS.                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 3                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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 GENERATING THE BIOMOLECULE                                           
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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -0.500000 -0.866025  0.000000       82.89200            
REMARK 350   BIOMT2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3 -0.500000  0.866025  0.000000       41.44600            
REMARK 350   BIOMT2   3 -0.866025 -0.500000  0.000000       71.78658            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 350 BIOMOLECULE:  2                                                      
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -0.500000 -0.866025  0.000000      124.33800            
REMARK 350   BIOMT2   2  0.866025 -0.500000  0.000000       71.78658            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   3 -0.866025 -0.500000  0.000000      143.57316            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400  FUNCTION: THIS PROTEIN IS AN AUXILIARY PROTEIN OF DNA POLYMERASE    
REMARK 400  DELTA AND IS INVOLVED IN THE CONTROL OF EUKARYOTIC DNA REPLICATION  
REMARK 400  BY INCREASING THE POLYMERASE'S PROCESSIBILITY DURING ELONGATION OF  
REMARK 400  THE LEADING STRAND.                                                 
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     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     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 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   ND2  ASN A   187  -  OD2  ASP A   189              2.16            
REMARK 500   O    ASP B   189  -  N    GLU B   191              2.03            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    TRP B  28   NE1   TRP B  28   CE2     0.112                       
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 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    ALA A 163     -148.45   -147.87                                   
REMARK 500    ASN A 187     -161.74   -116.16                                   
REMARK 500    ASP A 189     -146.57   -147.31                                   
REMARK 500    LYS A 190     -144.67   -116.40                                   
REMARK 500    GLU A 193      174.82     44.94                                   
REMARK 500    ALA A 194      -94.32   -144.84                                   
REMARK 500    VAL A 195       72.95   -175.06                                   
REMARK 500    GLU A 198       59.25   -110.09                                   
REMARK 500    ASN B  24       -6.79   -140.95                                   
REMARK 500    SER B  31      122.69    178.81                                   
REMARK 500    SER B  32      -91.74     25.50                                   
REMARK 500    ASP B  86      116.34    -29.54                                   
REMARK 500    ASN B  95       53.48   -107.38                                   
REMARK 500    GLN B 108      168.04    -38.86                                   
REMARK 500    GLU B 109      124.71     95.18                                   
REMARK 500    LYS B 110       50.30     75.76                                   
REMARK 500    ALA B 163     -143.98   -147.69                                   
REMARK 500    LEU B 182      -83.69    -79.95                                   
REMARK 500    SER B 183      165.37     71.48                                   
REMARK 500    ASN B 187     -106.68    -65.67                                   
REMARK 500    VAL B 188       32.18    154.93                                   
REMARK 500    LYS B 190       15.52    -47.73                                   
REMARK 500    GLU B 191      131.27    -18.09                                   
REMARK 500    ALA B 194     -151.52    177.61                                   
REMARK 500    VAL B 195      -69.04   -158.21                                   
REMARK 500    THR B 196      129.98     44.64                                   
REMARK 500    SER B 230       48.01   -150.82                                   
REMARK 500    ALA B 231      135.73     25.52                                   
REMARK 500    ASP B 232      -13.23     83.89                                   
REMARK 500    LYS B 254     -148.62    -80.03                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1AXC   RELATED DB: PDB                                   
REMARK 900  HUMAN PCNA                                                          
REMARK 900 RELATED ID: 1U76   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HPCNA BOUND TO RESIDUES                        
REMARK 900   452-466 OF THEDNA POLYMERASE-DELTA-P66                             
REMARK 900  SUBUNIT                                                             
REMARK 900 RELATED ID: 1U7B   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HPCNA BOUND TO RESIDUES                        
REMARK 900   331-350 OF THEFLAP ENDONUCLEASE-1 (FEN1)                           
REMARK 900 RELATED ID: 1VYJ   RELATED DB: PDB                                   
REMARK 900  STRUCTURAL AND BIOCHEMICAL STUDIES OF HUMAN                         
REMARK 900  PCNA COMPLEXES PROVIDE THE BASIS FOR                                
REMARK 900  ASSOCIATION WITH CDK/CYCLIN AND RATIONAL FOR                        
REMARK 900   INHIBITOR DESIGN                                                   
REMARK 900 RELATED ID: 1VYM   RELATED DB: PDB                                   
REMARK 900  NATIVE HUMAN PCNA                                                   
DBREF  1W60 A    1   261  UNP    P12004   PCNA_HUMAN       1    261             
DBREF  1W60 B    1   261  UNP    P12004   PCNA_HUMAN       1    261             
SEQRES   1 A  261  MET PHE GLU ALA ARG LEU VAL GLN GLY SER ILE LEU LYS          
SEQRES   2 A  261  LYS VAL LEU GLU ALA LEU LYS ASP LEU ILE ASN GLU ALA          
SEQRES   3 A  261  CYS TRP ASP ILE SER SER SER GLY VAL ASN LEU GLN SER          
SEQRES   4 A  261  MET ASP SER SER HIS VAL SER LEU VAL GLN LEU THR LEU          
SEQRES   5 A  261  ARG SER GLU GLY PHE ASP THR TYR ARG CYS ASP ARG ASN          
SEQRES   6 A  261  LEU ALA MET GLY VAL ASN LEU THR SER MET SER LYS ILE          
SEQRES   7 A  261  LEU LYS CYS ALA GLY ASN GLU ASP ILE ILE THR LEU ARG          
SEQRES   8 A  261  ALA GLU ASP ASN ALA ASP THR LEU ALA LEU VAL PHE GLU          
SEQRES   9 A  261  ALA PRO ASN GLN GLU LYS VAL SER ASP TYR GLU MET LYS          
SEQRES  10 A  261  LEU MET ASP LEU ASP VAL GLU GLN LEU GLY ILE PRO GLU          
SEQRES  11 A  261  GLN GLU TYR SER CYS VAL VAL LYS MET PRO SER GLY GLU          
SEQRES  12 A  261  PHE ALA ARG ILE CYS ARG ASP LEU SER HIS ILE GLY ASP          
SEQRES  13 A  261  ALA VAL VAL ILE SER CYS ALA LYS ASP GLY VAL LYS PHE          
SEQRES  14 A  261  SER ALA SER GLY GLU LEU GLY ASN GLY ASN ILE LYS LEU          
SEQRES  15 A  261  SER GLN THR SER ASN VAL ASP LYS GLU GLU GLU ALA VAL          
SEQRES  16 A  261  THR ILE GLU MET ASN GLU PRO VAL GLN LEU THR PHE ALA          
SEQRES  17 A  261  LEU ARG TYR LEU ASN PHE PHE THR LYS ALA THR PRO LEU          
SEQRES  18 A  261  SER SER THR VAL THR LEU SER MET SER ALA ASP VAL PRO          
SEQRES  19 A  261  LEU VAL VAL GLU TYR LYS ILE ALA ASP MET GLY HIS LEU          
SEQRES  20 A  261  LYS TYR TYR LEU ALA PRO LYS ILE GLU ASP GLU GLU GLY          
SEQRES  21 A  261  SER                                                          
SEQRES   1 B  261  MET PHE GLU ALA ARG LEU VAL GLN GLY SER ILE LEU LYS          
SEQRES   2 B  261  LYS VAL LEU GLU ALA LEU LYS ASP LEU ILE ASN GLU ALA          
SEQRES   3 B  261  CYS TRP ASP ILE SER SER SER GLY VAL ASN LEU GLN SER          
SEQRES   4 B  261  MET ASP SER SER HIS VAL SER LEU VAL GLN LEU THR LEU          
SEQRES   5 B  261  ARG SER GLU GLY PHE ASP THR TYR ARG CYS ASP ARG ASN          
SEQRES   6 B  261  LEU ALA MET GLY VAL ASN LEU THR SER MET SER LYS ILE          
SEQRES   7 B  261  LEU LYS CYS ALA GLY ASN GLU ASP ILE ILE THR LEU ARG          
SEQRES   8 B  261  ALA GLU ASP ASN ALA ASP THR LEU ALA LEU VAL PHE GLU          
SEQRES   9 B  261  ALA PRO ASN GLN GLU LYS VAL SER ASP TYR GLU MET LYS          
SEQRES  10 B  261  LEU MET ASP LEU ASP VAL GLU GLN LEU GLY ILE PRO GLU          
SEQRES  11 B  261  GLN GLU TYR SER CYS VAL VAL LYS MET PRO SER GLY GLU          
SEQRES  12 B  261  PHE ALA ARG ILE CYS ARG ASP LEU SER HIS ILE GLY ASP          
SEQRES  13 B  261  ALA VAL VAL ILE SER CYS ALA LYS ASP GLY VAL LYS PHE          
SEQRES  14 B  261  SER ALA SER GLY GLU LEU GLY ASN GLY ASN ILE LYS LEU          
SEQRES  15 B  261  SER GLN THR SER ASN VAL ASP LYS GLU GLU GLU ALA VAL          
SEQRES  16 B  261  THR ILE GLU MET ASN GLU PRO VAL GLN LEU THR PHE ALA          
SEQRES  17 B  261  LEU ARG TYR LEU ASN PHE PHE THR LYS ALA THR PRO LEU          
SEQRES  18 B  261  SER SER THR VAL THR LEU SER MET SER ALA ASP VAL PRO          
SEQRES  19 B  261  LEU VAL VAL GLU TYR LYS ILE ALA ASP MET GLY HIS LEU          
SEQRES  20 B  261  LYS TYR TYR LEU ALA PRO LYS ILE GLU ASP GLU GLU GLY          
SEQRES  21 B  261  SER                                                          
FORMUL   3  HOH   *58(H2 O1)                                                    
HELIX    1   1 GLN A    8  GLU A   17  1                                  10    
HELIX    2   2 LEU A   72  LEU A   79  1                                   8    
HELIX    3   3 SER A  141  HIS A  153  1                                  13    
HELIX    4   4 LEU A  209  THR A  216  1                                   8    
HELIX    5   5 LYS A  217  THR A  219  5                                   3    
HELIX    6   6 GLN B    8  LYS B   20  1                                  13    
HELIX    7   7 LEU B   72  LEU B   79  1                                   8    
HELIX    8   8 SER B  141  SER B  152  1                                  12    
HELIX    9   9 LEU B  209  THR B  216  1                                   8    
HELIX   10  10 LYS B  217  THR B  219  5                                   3    
SHEET    1  AA 5 THR A  59  CYS A  62  0                                        
SHEET    2  AA 5 PHE A   2  LEU A   6 -1  O  GLU A   3   N  ARG A  61           
SHEET    3  AA 5 ILE A  87  ALA A  92 -1  O  ILE A  88   N  LEU A   6           
SHEET    4  AA 5 THR A  98  GLU A 104 -1  O  ALA A 100   N  ARG A  91           
SHEET    5  AA 5 VAL A 111  LYS A 117 -1  O  SER A 112   N  PHE A 103           
SHEET    1  AB 8 LEU A  66  ASN A  71  0                                        
SHEET    2  AB 8 GLU A  25  ILE A  30 -1  O  ALA A  26   N  VAL A  70           
SHEET    3  AB 8 GLY A  34  MET A  40 -1  O  ASN A  36   N  ASP A  29           
SHEET    4  AB 8 SER A  46  ARG A  53 -1  O  VAL A  48   N  SER A  39           
SHEET    5  AB 8 GLY A 245  LEU A 251 -1  O  HIS A 246   N  THR A  51           
SHEET    6  AB 8 VAL A 233  TYR A 239 -1  O  LEU A 235   N  LEU A 251           
SHEET    7  AB 8 THR A 224  SER A 230 -1  O  THR A 226   N  GLU A 238           
SHEET    8  AB 8 CYS A 135  PRO A 140 -1  O  CYS A 135   N  MET A 229           
SHEET    1  AC 4 ASN A 177  LEU A 182  0                                        
SHEET    2  AC 4 VAL A 167  SER A 172 -1  O  VAL A 167   N  LEU A 182           
SHEET    3  AC 4 ALA A 157  CYS A 162 -1  O  VAL A 159   N  SER A 170           
SHEET    4  AC 4 GLN A 204  ALA A 208 -1  O  LEU A 205   N  ILE A 160           
SHEET    1  BA 5 THR B  59  CYS B  62  0                                        
SHEET    2  BA 5 PHE B   2  LEU B   6 -1  O  GLU B   3   N  ARG B  61           
SHEET    3  BA 5 ILE B  87  ALA B  92 -1  O  ILE B  88   N  LEU B   6           
SHEET    4  BA 5 THR B  98  GLU B 104 -1  O  ALA B 100   N  ARG B  91           
SHEET    5  BA 5 SER B 112  LYS B 117 -1  O  SER B 112   N  PHE B 103           
SHEET    1  BB 8 LEU B  66  ASN B  71  0                                        
SHEET    2  BB 8 GLU B  25  SER B  31 -1  O  ALA B  26   N  VAL B  70           
SHEET    3  BB 8 GLY B  34  MET B  40 -1  O  GLY B  34   N  SER B  31           
SHEET    4  BB 8 SER B  46  ARG B  53 -1  O  VAL B  48   N  SER B  39           
SHEET    5  BB 8 GLY B 245  LEU B 251 -1  O  HIS B 246   N  THR B  51           
SHEET    6  BB 8 LEU B 235  TYR B 239 -1  O  LEU B 235   N  LEU B 251           
SHEET    7  BB 8 THR B 224  MET B 229 -1  O  THR B 226   N  GLU B 238           
SHEET    8  BB 8 CYS B 135  PRO B 140 -1  O  CYS B 135   N  MET B 229           
SHEET    1  BC 4 ASN B 177  LYS B 181  0                                        
SHEET    2  BC 4 VAL B 167  SER B 172 -1  O  PHE B 169   N  ILE B 180           
SHEET    3  BC 4 ALA B 157  CYS B 162 -1  O  VAL B 159   N  SER B 170           
SHEET    4  BC 4 VAL B 203  ALA B 208 -1  O  VAL B 203   N  CYS B 162           
CRYST1   82.892   82.892   70.859  90.00  90.00 120.00 P 3           6          
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      0.012064  0.006965  0.000000        0.00000                         
SCALE2      0.000000  0.013930  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014113        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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