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Database: PDB
Entry: 1AXC
LinkDB: 1AXC
Original site: 1AXC 
HEADER    COMPLEX (DNA-BINDING PROTEIN/DNA)       14-OCT-97   1AXC              
TITLE     HUMAN PCNA                                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PCNA;                                                      
COMPND   3 CHAIN: A, C, E;                                                      
COMPND   4 SYNONYM: PROLIFERATING CELL NUCLEAR ANTIGEN;                         
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: P21/WAF1;                                                  
COMPND   7 CHAIN: B, D, F;                                                      
COMPND   8 FRAGMENT: 22 C TERMINAL RESIDUES (139 - 160)                         
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 MOL_ID: 2;                                                           
SOURCE   6 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   7 ORGANISM_COMMON: HUMAN;                                              
SOURCE   8 ORGANISM_TAXID: 9606                                                 
KEYWDS    DNA, REPLICATION, PROCESSIVITY, ONCOGENE, WAF1, CIP1,                 
KEYWDS   2 COMPLEX (DNA-BINDING PROTEIN/DNA)                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.M.GULBIS,J.KURIYAN                                                  
REVDAT   3   24-FEB-09 1AXC    1       VERSN                                    
REVDAT   2   30-SEP-03 1AXC    1       JRNL   DBREF                             
REVDAT   1   28-JAN-98 1AXC    0                                                
JRNL        AUTH   J.M.GULBIS,Z.KELMAN,J.HURWITZ,M.O'DONNELL,J.KURIYAN          
JRNL        TITL   STRUCTURE OF THE C-TERMINAL REGION OF                        
JRNL        TITL 2 P21(WAF1/CIP1) COMPLEXED WITH HUMAN PCNA.                    
JRNL        REF    CELL(CAMBRIDGE,MASS.)         V.  87   297 1996              
JRNL        REFN                   ISSN 0092-8674                               
JRNL        PMID   8861913                                                      
JRNL        DOI    10.1016/S0092-8674(00)81347-1                                
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.8                                           
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 15.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 10000000.000                   
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 22893                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.192                           
REMARK   3   FREE R VALUE                     : 0.289                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7509                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 295                                     
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) : 9.95000                                              
REMARK   3    B22 (A**2) : 9.95000                                              
REMARK   3    B33 (A**2) : -19.91000                                            
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 COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.008                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.40                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : 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  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PARHCDX.PRO                                    
REMARK   3  PARAMETER FILE  2  : PARAM19.SOL                                    
REMARK   3  PARAMETER FILE  3  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : TOPHCSDX.PRO                                   
REMARK   3  TOPOLOGY FILE  2   : TOPH19.SOL                                     
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1AXC COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : OCT-96                             
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X25                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
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 : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 33552                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 15.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.0                               
REMARK 200  DATA REDUNDANCY                : 3.900                              
REMARK 200  R MERGE                    (I) : 0.07300                            
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: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: X-PLOR 3.8                                            
REMARK 200 STARTING MODEL: YEAST PCNA                                           
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.49                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.48                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+1/3                                           
REMARK 290       6555   -X,-X+Y,-Z+2/3                                          
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      155.93333            
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       77.96667            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       77.96667            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      155.93333            
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: 10640 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 33290 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -40.0 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 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     ASN A   107                                                      
REMARK 465     GLN A   108                                                      
REMARK 465     ASN A   187                                                      
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   139                                                      
REMARK 465     ARG B   140                                                      
REMARK 465     LYS B   141                                                      
REMARK 465     ARG B   142                                                      
REMARK 465     ASN C   107                                                      
REMARK 465     GLN C   108                                                      
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   256                                                      
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     GLY D   139                                                      
REMARK 465     ARG D   140                                                      
REMARK 465     LYS D   141                                                      
REMARK 465     ARG D   142                                                      
REMARK 465     ASP E   189                                                      
REMARK 465     LYS E   190                                                      
REMARK 465     GLU E   256                                                      
REMARK 465     ASP E   257                                                      
REMARK 465     GLU E   258                                                      
REMARK 465     GLU E   259                                                      
REMARK 465     GLY E   260                                                      
REMARK 465     SER E   261                                                      
REMARK 465     GLY F   139                                                      
REMARK 465     ARG F   140                                                      
REMARK 465     LYS F   141                                                      
REMARK 465     ARG F   142                                                      
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     GLU A 109    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 191    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 198    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 232    CG   OD1  OD2                                       
REMARK 470     ILE A 255    CG1  CG2  CD1                                       
REMARK 470     ARG B 143    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU C 109    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 191    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 198    CG   CD   OE1  OE2                                  
REMARK 470     ARG C 210    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP C 232    CG   OD1  OD2                                       
REMARK 470     ILE C 255    CG1  CG2  CD1                                       
REMARK 470     ARG D 143    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN E 107    CG   OD1  ND2                                       
REMARK 470     GLN E 108    CG   CD   OE1  NE2                                  
REMARK 470     GLU E 109    CG   CD   OE1  OE2                                  
REMARK 470     ASP E 165    CG   OD1  OD2                                       
REMARK 470     SER E 186    OG                                                  
REMARK 470     ASN E 187    CG   OD1  ND2                                       
REMARK 470     GLU E 191    CG   CD   OE1  OE2                                  
REMARK 470     GLU E 198    CG   CD   OE1  OE2                                  
REMARK 470     ASP E 232    CG   OD1  OD2                                       
REMARK 470     ILE E 255    CG1  CG2  CD1                                       
REMARK 470     ARG F 143    CG   CD   NE   CZ   NH1  NH2                        
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    LYS A  20      -36.57    -36.14                                   
REMARK 500    GLU A 198       75.88   -100.27                                   
REMARK 500    MET A 244      -59.35   -128.14                                   
REMARK 500    THR C 216      -17.58    -49.97                                   
REMARK 500    LYS C 217        2.66    -68.10                                   
REMARK 500    ALA C 242      107.31    -43.65                                   
REMARK 500    PRO E 106      -51.92    -28.42                                   
REMARK 500    ASP E 122       78.63   -105.33                                   
REMARK 500    ASN E 187       84.90     39.71                                   
REMARK 500    GLU E 201      139.46   -172.48                                   
REMARK 500    THR E 216       -3.88    -57.71                                   
REMARK 500    ALA E 242      123.02    -29.73                                   
REMARK 500    ASP E 243      -16.22     67.96                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  1AXC A    1   261  UNP    P12004   PCNA_HUMAN       1    261             
DBREF  1AXC B  139   160  UNP    P38936   CDN1A_HUMAN    139    160             
DBREF  1AXC C    1   261  UNP    P12004   PCNA_HUMAN       1    261             
DBREF  1AXC D  139   160  UNP    P38936   CDN1A_HUMAN    139    160             
DBREF  1AXC E    1   261  UNP    P12004   PCNA_HUMAN       1    261             
DBREF  1AXC F  139   160  UNP    P38936   CDN1A_HUMAN    139    160             
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   22  GLY ARG LYS ARG ARG GLN THR SER MET THR ASP PHE TYR          
SEQRES   2 B   22  HIS SER LYS ARG ARG LEU ILE PHE SER                          
SEQRES   1 C  261  MET PHE GLU ALA ARG LEU VAL GLN GLY SER ILE LEU LYS          
SEQRES   2 C  261  LYS VAL LEU GLU ALA LEU LYS ASP LEU ILE ASN GLU ALA          
SEQRES   3 C  261  CYS TRP ASP ILE SER SER SER GLY VAL ASN LEU GLN SER          
SEQRES   4 C  261  MET ASP SER SER HIS VAL SER LEU VAL GLN LEU THR LEU          
SEQRES   5 C  261  ARG SER GLU GLY PHE ASP THR TYR ARG CYS ASP ARG ASN          
SEQRES   6 C  261  LEU ALA MET GLY VAL ASN LEU THR SER MET SER LYS ILE          
SEQRES   7 C  261  LEU LYS CYS ALA GLY ASN GLU ASP ILE ILE THR LEU ARG          
SEQRES   8 C  261  ALA GLU ASP ASN ALA ASP THR LEU ALA LEU VAL PHE GLU          
SEQRES   9 C  261  ALA PRO ASN GLN GLU LYS VAL SER ASP TYR GLU MET LYS          
SEQRES  10 C  261  LEU MET ASP LEU ASP VAL GLU GLN LEU GLY ILE PRO GLU          
SEQRES  11 C  261  GLN GLU TYR SER CYS VAL VAL LYS MET PRO SER GLY GLU          
SEQRES  12 C  261  PHE ALA ARG ILE CYS ARG ASP LEU SER HIS ILE GLY ASP          
SEQRES  13 C  261  ALA VAL VAL ILE SER CYS ALA LYS ASP GLY VAL LYS PHE          
SEQRES  14 C  261  SER ALA SER GLY GLU LEU GLY ASN GLY ASN ILE LYS LEU          
SEQRES  15 C  261  SER GLN THR SER ASN VAL ASP LYS GLU GLU GLU ALA VAL          
SEQRES  16 C  261  THR ILE GLU MET ASN GLU PRO VAL GLN LEU THR PHE ALA          
SEQRES  17 C  261  LEU ARG TYR LEU ASN PHE PHE THR LYS ALA THR PRO LEU          
SEQRES  18 C  261  SER SER THR VAL THR LEU SER MET SER ALA ASP VAL PRO          
SEQRES  19 C  261  LEU VAL VAL GLU TYR LYS ILE ALA ASP MET GLY HIS LEU          
SEQRES  20 C  261  LYS TYR TYR LEU ALA PRO LYS ILE GLU ASP GLU GLU GLY          
SEQRES  21 C  261  SER                                                          
SEQRES   1 D   22  GLY ARG LYS ARG ARG GLN THR SER MET THR ASP PHE TYR          
SEQRES   2 D   22  HIS SER LYS ARG ARG LEU ILE PHE SER                          
SEQRES   1 E  261  MET PHE GLU ALA ARG LEU VAL GLN GLY SER ILE LEU LYS          
SEQRES   2 E  261  LYS VAL LEU GLU ALA LEU LYS ASP LEU ILE ASN GLU ALA          
SEQRES   3 E  261  CYS TRP ASP ILE SER SER SER GLY VAL ASN LEU GLN SER          
SEQRES   4 E  261  MET ASP SER SER HIS VAL SER LEU VAL GLN LEU THR LEU          
SEQRES   5 E  261  ARG SER GLU GLY PHE ASP THR TYR ARG CYS ASP ARG ASN          
SEQRES   6 E  261  LEU ALA MET GLY VAL ASN LEU THR SER MET SER LYS ILE          
SEQRES   7 E  261  LEU LYS CYS ALA GLY ASN GLU ASP ILE ILE THR LEU ARG          
SEQRES   8 E  261  ALA GLU ASP ASN ALA ASP THR LEU ALA LEU VAL PHE GLU          
SEQRES   9 E  261  ALA PRO ASN GLN GLU LYS VAL SER ASP TYR GLU MET LYS          
SEQRES  10 E  261  LEU MET ASP LEU ASP VAL GLU GLN LEU GLY ILE PRO GLU          
SEQRES  11 E  261  GLN GLU TYR SER CYS VAL VAL LYS MET PRO SER GLY GLU          
SEQRES  12 E  261  PHE ALA ARG ILE CYS ARG ASP LEU SER HIS ILE GLY ASP          
SEQRES  13 E  261  ALA VAL VAL ILE SER CYS ALA LYS ASP GLY VAL LYS PHE          
SEQRES  14 E  261  SER ALA SER GLY GLU LEU GLY ASN GLY ASN ILE LYS LEU          
SEQRES  15 E  261  SER GLN THR SER ASN VAL ASP LYS GLU GLU GLU ALA VAL          
SEQRES  16 E  261  THR ILE GLU MET ASN GLU PRO VAL GLN LEU THR PHE ALA          
SEQRES  17 E  261  LEU ARG TYR LEU ASN PHE PHE THR LYS ALA THR PRO LEU          
SEQRES  18 E  261  SER SER THR VAL THR LEU SER MET SER ALA ASP VAL PRO          
SEQRES  19 E  261  LEU VAL VAL GLU TYR LYS ILE ALA ASP MET GLY HIS LEU          
SEQRES  20 E  261  LYS TYR TYR LEU ALA PRO LYS ILE GLU ASP GLU GLU GLY          
SEQRES  21 E  261  SER                                                          
SEQRES   1 F   22  GLY ARG LYS ARG ARG GLN THR SER MET THR ASP PHE TYR          
SEQRES   2 F   22  HIS SER LYS ARG ARG LEU ILE PHE SER                          
FORMUL   7  HOH   *295(H2 O)                                                    
HELIX    1   1 GLY A    9  LEU A   19  1                                  11    
HELIX    2   2 SER A   54  GLY A   56  5                                   3    
HELIX    3   3 LEU A   72  CYS A   81  1                                  10    
HELIX    4   4 SER A  141  HIS A  153  1                                  13    
HELIX    5   5 LEU A  209  LEU A  221  1                                  13    
HELIX    6   6 MET B  147  ASP B  149  5                                   3    
HELIX    7   7 GLY C    9  ALA C   18  1                                  10    
HELIX    8   8 SER C   54  GLY C   56  5                                   3    
HELIX    9   9 LEU C   72  CYS C   81  1                                  10    
HELIX   10  10 SER C  141  ILE C  154  1                                  14    
HELIX   11  11 LEU C  209  LEU C  221  1                                  13    
HELIX   12  12 MET D  147  ASP D  149  5                                   3    
HELIX   13  13 GLY E    9  GLU E   17  1                                   9    
HELIX   14  14 SER E   54  GLY E   56  5                                   3    
HELIX   15  15 LEU E   72  CYS E   81  1                                  10    
HELIX   16  16 SER E  141  ILE E  154  1                                  14    
HELIX   17  17 LEU E  209  LEU E  221  1                                  13    
HELIX   18  18 MET F  147  ASP F  149  5                                   3    
SHEET    1   A 5 THR A  59  CYS A  62  0                                        
SHEET    2   A 5 PHE A   2  LEU A   6 -1  N  ARG A   5   O  THR A  59           
SHEET    3   A 5 ILE A  87  ALA A  92 -1  N  ALA A  92   O  PHE A   2           
SHEET    4   A 5 THR A  98  GLU A 104 -1  N  GLU A 104   O  ILE A  87           
SHEET    5   A 5 VAL A 111  LYS A 117 -1  N  MET A 116   O  LEU A  99           
SHEET    1   B 8 LEU A  66  ASN A  71  0                                        
SHEET    2   B 8 GLU A  25  SER A  31 -1  N  ILE A  30   O  LEU A  66           
SHEET    3   B 8 GLY A  34  MET A  40 -1  N  ASN A  36   O  ASP A  29           
SHEET    4   B 8 SER A  46  ARG A  53 -1  N  LEU A  52   O  VAL A  35           
SHEET    5   B 8 GLY A 245  LEU A 251 -1  N  TYR A 250   O  LEU A  47           
SHEET    6   B 8 LEU A 235  TYR A 239 -1  N  TYR A 239   O  LEU A 247           
SHEET    7   B 8 THR A 224  MET A 229 -1  N  SER A 228   O  VAL A 236           
SHEET    8   B 8 CYS A 135  PRO A 140 -1  N  MET A 139   O  VAL A 225           
SHEET    1   C 2 ALA A 157  CYS A 162  0                                        
SHEET    2   C 2 VAL A 203  ALA A 208 -1  N  PHE A 207   O  VAL A 158           
SHEET    1   D 2 GLY A 166  GLY A 173  0                                        
SHEET    2   D 2 GLY A 176  SER A 183 -1  N  LEU A 182   O  VAL A 167           
SHEET    1   E 5 THR C  59  CYS C  62  0                                        
SHEET    2   E 5 PHE C   2  LEU C   6 -1  N  ARG C   5   O  THR C  59           
SHEET    3   E 5 ILE C  87  ALA C  92 -1  N  ALA C  92   O  PHE C   2           
SHEET    4   E 5 THR C  98  GLU C 104 -1  N  GLU C 104   O  ILE C  87           
SHEET    5   E 5 VAL C 111  LYS C 117 -1  N  MET C 116   O  LEU C  99           
SHEET    1   F 9 LEU C  66  ASN C  71  0                                        
SHEET    2   F 9 GLU C  25  SER C  31 -1  N  ILE C  30   O  LEU C  66           
SHEET    3   F 9 GLY C  34  MET C  40 -1  N  ASN C  36   O  ASP C  29           
SHEET    4   F 9 SER C  46  ARG C  53 -1  N  LEU C  52   O  VAL C  35           
SHEET    5   F 9 GLY C 245  LEU C 251 -1  N  TYR C 250   O  LEU C  47           
SHEET    6   F 9 LEU C 235  TYR C 239 -1  N  TYR C 239   O  LEU C 247           
SHEET    7   F 9 THR C 224  MET C 229 -1  N  SER C 228   O  VAL C 236           
SHEET    8   F 9 CYS C 135  PRO C 140 -1  N  MET C 139   O  VAL C 225           
SHEET    9   F 9 THR C 196  MET C 199 -1  N  GLU C 198   O  VAL C 136           
SHEET    1   G 4 VAL C 203  ALA C 208  0                                        
SHEET    2   G 4 ALA C 157  ALA C 163 -1  N  CYS C 162   O  VAL C 203           
SHEET    3   G 4 GLY C 166  GLY C 173 -1  N  SER C 170   O  VAL C 159           
SHEET    4   G 4 GLY C 176  SER C 183 -1  N  LEU C 182   O  VAL C 167           
SHEET    1   H 5 THR E  59  CYS E  62  0                                        
SHEET    2   H 5 PHE E   2  LEU E   6 -1  N  ARG E   5   O  THR E  59           
SHEET    3   H 5 ILE E  87  ALA E  92 -1  N  ALA E  92   O  PHE E   2           
SHEET    4   H 5 THR E  98  GLU E 104 -1  N  GLU E 104   O  ILE E  87           
SHEET    5   H 5 VAL E 111  LYS E 117 -1  N  MET E 116   O  LEU E  99           
SHEET    1   I 2 GLU E  25  ILE E  30  0                                        
SHEET    2   I 2 LEU E  66  ASN E  71 -1  N  VAL E  70   O  ALA E  26           
SHEET    1   J 7 GLY E  34  MET E  40  0                                        
SHEET    2   J 7 SER E  46  ARG E  53 -1  N  LEU E  52   O  VAL E  35           
SHEET    3   J 7 GLY E 245  LEU E 251 -1  N  TYR E 250   O  LEU E  47           
SHEET    4   J 7 LEU E 235  TYR E 239 -1  N  TYR E 239   O  LEU E 247           
SHEET    5   J 7 THR E 224  MET E 229 -1  N  SER E 228   O  VAL E 236           
SHEET    6   J 7 CYS E 135  PRO E 140 -1  N  MET E 139   O  VAL E 225           
SHEET    7   J 7 THR E 196  MET E 199 -1  N  GLU E 198   O  VAL E 136           
SHEET    1   K 4 VAL E 203  ALA E 208  0                                        
SHEET    2   K 4 ALA E 157  ALA E 163 -1  N  CYS E 162   O  VAL E 203           
SHEET    3   K 4 GLY E 166  SER E 172 -1  N  SER E 170   O  VAL E 159           
SHEET    4   K 4 ASN E 177  SER E 183 -1  N  LEU E 182   O  VAL E 167           
CRYST1   83.500   83.500  233.900  90.00  90.00 120.00 P 32 2 1     18          
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      0.011976  0.006914  0.000000        0.00000                         
SCALE2      0.000000  0.013829  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004275        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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