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Database: PDB
Entry: 5IY4
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Original site: 5IY4 
HEADER    DNA BINDING PROTEIN                     24-MAR-16   5IY4              
TITLE     CRYSTAL STRUCTURE OF HUMAN PCNA IN COMPLEX WITH THE PIP BOX OF DVC1   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROLIFERATING CELL NUCLEAR ANTIGEN;                        
COMPND   3 CHAIN: A, C, E;                                                      
COMPND   4 SYNONYM: PCNA,CYCLIN;                                                
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: DVC1 PIP BOX;                                              
COMPND   8 CHAIN: B, D, F;                                                      
COMPND   9 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: PCNA;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 SYNTHETIC: YES;                                                      
SOURCE  10 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;                            
SOURCE  11 ORGANISM_TAXID:  32630                                               
KEYWDS    PCNA, PIP BOX, DVC1, DNA BINDING PROTEIN                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.JIANG,M.XU,Y.WANG                                                   
REVDAT   2   27-SEP-17 5IY4    1       REMARK                                   
REVDAT   1   08-JUN-16 5IY4    0                                                
JRNL        AUTH   Y.WANG,M.XU,T.JIANG                                          
JRNL        TITL   CRYSTAL STRUCTURE OF HUMAN PCNA IN COMPLEX WITH THE PIP BOX  
JRNL        TITL 2 OF DVC1                                                      
JRNL        REF    BIOCHEM.BIOPHYS.RES.COMMUN.   V. 474   264 2016              
JRNL        REFN                   ESSN 1090-2104                               
JRNL        PMID   27084448                                                     
JRNL        DOI    10.1016/J.BBRC.2016.04.053                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.95 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.9_1692                                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.95                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.33                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 17810                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.210                           
REMARK   3   R VALUE            (WORKING SET) : 0.207                           
REMARK   3   FREE R VALUE                     : 0.270                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.160                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 919                             
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 48.3353 -  5.6318    0.99     2757   129  0.2029 0.2730        
REMARK   3     2  5.6318 -  4.4712    1.00     2566   142  0.1806 0.2369        
REMARK   3     3  4.4712 -  3.9063    1.00     2551   126  0.2030 0.2479        
REMARK   3     4  3.9063 -  3.5492    1.00     2498   137  0.2146 0.2819        
REMARK   3     5  3.5492 -  3.2949    0.99     2455   152  0.2222 0.2905        
REMARK   3     6  3.2949 -  3.1007    0.93     2302   124  0.2446 0.3111        
REMARK   3     7  3.1007 -  2.9454    0.71     1762   109  0.2305 0.3110        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.290            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.620           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.013           6185                                  
REMARK   3   ANGLE     :  1.463           8350                                  
REMARK   3   CHIRALITY :  0.060            984                                  
REMARK   3   PLANARITY :  0.007           1069                                  
REMARK   3   DIHEDRAL  : 15.014           2301                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: ALL                                                    
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.2113 -38.4560 -38.7756              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2134 T22:   0.1672                                     
REMARK   3      T33:   0.3144 T12:   0.1281                                     
REMARK   3      T13:  -0.0108 T23:  -0.0310                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1258 L22:   1.0254                                     
REMARK   3      L33:   2.1801 L12:   0.5756                                     
REMARK   3      L13:   0.2398 L23:   0.0802                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0473 S12:   0.1067 S13:   0.0395                       
REMARK   3      S21:   0.0565 S22:  -0.0274 S23:   0.0172                       
REMARK   3      S31:  -0.0206 S32:   0.2540 S33:  -0.0221                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: SF FILE CONTAINS FRIEDEL PAIRS UNDER      
REMARK   3  I/F_MINUS AND I/F_PLUS COLUMNS.                                     
REMARK   4                                                                      
REMARK   4 5IY4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 13-APR-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000219584.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-NOV-15                          
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               : SSRF                               
REMARK 200  BEAMLINE                       : BL18U1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9776                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : PSI PILATUS 6M                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 18902                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.945                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.330                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 10.40                              
REMARK 200  R MERGE                    (I) : 0.16000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.3400                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.95                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 10.80                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.77000                            
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: 1U7B                                                 
REMARK 200                                                                      
REMARK 200 REMARK: THE ENTRY CONTAINS FRIEDEL PAIRS IN F_PLUS/MINUS COLUMNS.    
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.14                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.97                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM CITRATE TRIBASIC            
REMARK 280  DEHYDRATES (PH 5.0), 30% V/V JEFFAMINE ED-2001 (PH 7.0), VAPOR      
REMARK 280  DIFFUSION, TEMPERATURE 289K                                         
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+3/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+3/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      161.10400            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       35.82350            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       35.82350            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      241.65600            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       35.82350            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       35.82350            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       80.55200            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       35.82350            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       35.82350            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      241.65600            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       35.82350            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       35.82350            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       80.55200            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000      161.10400            
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: 8590 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 34960 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -43.0 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   187                                                      
REMARK 465     VAL A   188                                                      
REMARK 465     ASP A   189                                                      
REMARK 465     LYS A   190                                                      
REMARK 465     GLU A   191                                                      
REMARK 465     GLU A   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     LEU A   262                                                      
REMARK 465     GLU A   263                                                      
REMARK 465     HIS A   264                                                      
REMARK 465     HIS A   265                                                      
REMARK 465     HIS A   266                                                      
REMARK 465     HIS A   267                                                      
REMARK 465     HIS A   268                                                      
REMARK 465     HIS A   269                                                      
REMARK 465     HIS A   270                                                      
REMARK 465     SER B   321                                                      
REMARK 465     ASN B   322                                                      
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     LEU C   262                                                      
REMARK 465     GLU C   263                                                      
REMARK 465     HIS C   264                                                      
REMARK 465     HIS C   265                                                      
REMARK 465     HIS C   266                                                      
REMARK 465     HIS C   267                                                      
REMARK 465     HIS C   268                                                      
REMARK 465     HIS C   269                                                      
REMARK 465     HIS C   270                                                      
REMARK 465     SER D   321                                                      
REMARK 465     ASN D   322                                                      
REMARK 465     ASN E   187                                                      
REMARK 465     VAL E   188                                                      
REMARK 465     ASP E   189                                                      
REMARK 465     LYS E   190                                                      
REMARK 465     GLU E   191                                                      
REMARK 465     GLU E   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     LEU E   262                                                      
REMARK 465     GLU E   263                                                      
REMARK 465     HIS E   264                                                      
REMARK 465     HIS E   265                                                      
REMARK 465     HIS E   266                                                      
REMARK 465     HIS E   267                                                      
REMARK 465     HIS E   268                                                      
REMARK 465     HIS E   269                                                      
REMARK 465     HIS E   270                                                      
REMARK 465     SER F   321                                                      
REMARK 465     ASN F   322                                                      
REMARK 465     ARG F   334                                                      
REMARK 465     VAL F   335                                                      
REMARK 465     SER F   336                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HIS E    44     CG1  VAL F   327              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   NH1  ARG A     5     ND2  ASN C    95     5454     2.15            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLN A 108       10.42     52.27                                   
REMARK 500    ASP A 243       -3.49     81.45                                   
REMARK 500    GLU C  93     -167.34   -104.93                                   
REMARK 500    GLN C 108       -6.34     85.96                                   
REMARK 500    ALA C 163     -166.63   -121.30                                   
REMARK 500    PRO C 220        1.81    -68.65                                   
REMARK 500    ASP C 243       -6.38     83.65                                   
REMARK 500    GLU E  93     -165.38   -110.95                                   
REMARK 500    GLN E 108        4.60     86.59                                   
REMARK 500    ASP E 243       -1.46     77.00                                   
REMARK 500    HIS F 324      178.61    179.29                                   
REMARK 500    GLN F 325      153.93    177.70                                   
REMARK 500    ASN F 326     -150.71   -122.76                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  5IY4 A    1   261  UNP    P12004   PCNA_HUMAN       1    261             
DBREF  5IY4 B  321   336  PDB    5IY4     5IY4           321    336             
DBREF  5IY4 C    1   261  UNP    P12004   PCNA_HUMAN       1    261             
DBREF  5IY4 D  321   336  PDB    5IY4     5IY4           321    336             
DBREF  5IY4 E    1   261  UNP    P12004   PCNA_HUMAN       1    261             
DBREF  5IY4 F  321   336  PDB    5IY4     5IY4           321    336             
SEQADV 5IY4 LEU A  262  UNP  P12004              EXPRESSION TAG                 
SEQADV 5IY4 GLU A  263  UNP  P12004              EXPRESSION TAG                 
SEQADV 5IY4 HIS A  264  UNP  P12004              EXPRESSION TAG                 
SEQADV 5IY4 HIS A  265  UNP  P12004              EXPRESSION TAG                 
SEQADV 5IY4 HIS A  266  UNP  P12004              EXPRESSION TAG                 
SEQADV 5IY4 HIS A  267  UNP  P12004              EXPRESSION TAG                 
SEQADV 5IY4 HIS A  268  UNP  P12004              EXPRESSION TAG                 
SEQADV 5IY4 HIS A  269  UNP  P12004              EXPRESSION TAG                 
SEQADV 5IY4 HIS A  270  UNP  P12004              EXPRESSION TAG                 
SEQADV 5IY4 LEU C  262  UNP  P12004              EXPRESSION TAG                 
SEQADV 5IY4 GLU C  263  UNP  P12004              EXPRESSION TAG                 
SEQADV 5IY4 HIS C  264  UNP  P12004              EXPRESSION TAG                 
SEQADV 5IY4 HIS C  265  UNP  P12004              EXPRESSION TAG                 
SEQADV 5IY4 HIS C  266  UNP  P12004              EXPRESSION TAG                 
SEQADV 5IY4 HIS C  267  UNP  P12004              EXPRESSION TAG                 
SEQADV 5IY4 HIS C  268  UNP  P12004              EXPRESSION TAG                 
SEQADV 5IY4 HIS C  269  UNP  P12004              EXPRESSION TAG                 
SEQADV 5IY4 HIS C  270  UNP  P12004              EXPRESSION TAG                 
SEQADV 5IY4 LEU E  262  UNP  P12004              EXPRESSION TAG                 
SEQADV 5IY4 GLU E  263  UNP  P12004              EXPRESSION TAG                 
SEQADV 5IY4 HIS E  264  UNP  P12004              EXPRESSION TAG                 
SEQADV 5IY4 HIS E  265  UNP  P12004              EXPRESSION TAG                 
SEQADV 5IY4 HIS E  266  UNP  P12004              EXPRESSION TAG                 
SEQADV 5IY4 HIS E  267  UNP  P12004              EXPRESSION TAG                 
SEQADV 5IY4 HIS E  268  UNP  P12004              EXPRESSION TAG                 
SEQADV 5IY4 HIS E  269  UNP  P12004              EXPRESSION TAG                 
SEQADV 5IY4 HIS E  270  UNP  P12004              EXPRESSION TAG                 
SEQRES   1 A  270  MET PHE GLU ALA ARG LEU VAL GLN GLY SER ILE LEU LYS          
SEQRES   2 A  270  LYS VAL LEU GLU ALA LEU LYS ASP LEU ILE ASN GLU ALA          
SEQRES   3 A  270  CYS TRP ASP ILE SER SER SER GLY VAL ASN LEU GLN SER          
SEQRES   4 A  270  MET ASP SER SER HIS VAL SER LEU VAL GLN LEU THR LEU          
SEQRES   5 A  270  ARG SER GLU GLY PHE ASP THR TYR ARG CYS ASP ARG ASN          
SEQRES   6 A  270  LEU ALA MET GLY VAL ASN LEU THR SER MET SER LYS ILE          
SEQRES   7 A  270  LEU LYS CYS ALA GLY ASN GLU ASP ILE ILE THR LEU ARG          
SEQRES   8 A  270  ALA GLU ASP ASN ALA ASP THR LEU ALA LEU VAL PHE GLU          
SEQRES   9 A  270  ALA PRO ASN GLN GLU LYS VAL SER ASP TYR GLU MET LYS          
SEQRES  10 A  270  LEU MET ASP LEU ASP VAL GLU GLN LEU GLY ILE PRO GLU          
SEQRES  11 A  270  GLN GLU TYR SER CYS VAL VAL LYS MET PRO SER GLY GLU          
SEQRES  12 A  270  PHE ALA ARG ILE CYS ARG ASP LEU SER HIS ILE GLY ASP          
SEQRES  13 A  270  ALA VAL VAL ILE SER CYS ALA LYS ASP GLY VAL LYS PHE          
SEQRES  14 A  270  SER ALA SER GLY GLU LEU GLY ASN GLY ASN ILE LYS LEU          
SEQRES  15 A  270  SER GLN THR SER ASN VAL ASP LYS GLU GLU GLU ALA VAL          
SEQRES  16 A  270  THR ILE GLU MET ASN GLU PRO VAL GLN LEU THR PHE ALA          
SEQRES  17 A  270  LEU ARG TYR LEU ASN PHE PHE THR LYS ALA THR PRO LEU          
SEQRES  18 A  270  SER SER THR VAL THR LEU SER MET SER ALA ASP VAL PRO          
SEQRES  19 A  270  LEU VAL VAL GLU TYR LYS ILE ALA ASP MET GLY HIS LEU          
SEQRES  20 A  270  LYS TYR TYR LEU ALA PRO LYS ILE GLU ASP GLU GLU GLY          
SEQRES  21 A  270  SER LEU GLU HIS HIS HIS HIS HIS HIS HIS                      
SEQRES   1 B   16  SER ASN SER HIS GLN ASN VAL LEU SER ASN TYR PHE PRO          
SEQRES   2 B   16  ARG VAL SER                                                  
SEQRES   1 C  270  MET PHE GLU ALA ARG LEU VAL GLN GLY SER ILE LEU LYS          
SEQRES   2 C  270  LYS VAL LEU GLU ALA LEU LYS ASP LEU ILE ASN GLU ALA          
SEQRES   3 C  270  CYS TRP ASP ILE SER SER SER GLY VAL ASN LEU GLN SER          
SEQRES   4 C  270  MET ASP SER SER HIS VAL SER LEU VAL GLN LEU THR LEU          
SEQRES   5 C  270  ARG SER GLU GLY PHE ASP THR TYR ARG CYS ASP ARG ASN          
SEQRES   6 C  270  LEU ALA MET GLY VAL ASN LEU THR SER MET SER LYS ILE          
SEQRES   7 C  270  LEU LYS CYS ALA GLY ASN GLU ASP ILE ILE THR LEU ARG          
SEQRES   8 C  270  ALA GLU ASP ASN ALA ASP THR LEU ALA LEU VAL PHE GLU          
SEQRES   9 C  270  ALA PRO ASN GLN GLU LYS VAL SER ASP TYR GLU MET LYS          
SEQRES  10 C  270  LEU MET ASP LEU ASP VAL GLU GLN LEU GLY ILE PRO GLU          
SEQRES  11 C  270  GLN GLU TYR SER CYS VAL VAL LYS MET PRO SER GLY GLU          
SEQRES  12 C  270  PHE ALA ARG ILE CYS ARG ASP LEU SER HIS ILE GLY ASP          
SEQRES  13 C  270  ALA VAL VAL ILE SER CYS ALA LYS ASP GLY VAL LYS PHE          
SEQRES  14 C  270  SER ALA SER GLY GLU LEU GLY ASN GLY ASN ILE LYS LEU          
SEQRES  15 C  270  SER GLN THR SER ASN VAL ASP LYS GLU GLU GLU ALA VAL          
SEQRES  16 C  270  THR ILE GLU MET ASN GLU PRO VAL GLN LEU THR PHE ALA          
SEQRES  17 C  270  LEU ARG TYR LEU ASN PHE PHE THR LYS ALA THR PRO LEU          
SEQRES  18 C  270  SER SER THR VAL THR LEU SER MET SER ALA ASP VAL PRO          
SEQRES  19 C  270  LEU VAL VAL GLU TYR LYS ILE ALA ASP MET GLY HIS LEU          
SEQRES  20 C  270  LYS TYR TYR LEU ALA PRO LYS ILE GLU ASP GLU GLU GLY          
SEQRES  21 C  270  SER LEU GLU HIS HIS HIS HIS HIS HIS HIS                      
SEQRES   1 D   16  SER ASN SER HIS GLN ASN VAL LEU SER ASN TYR PHE PRO          
SEQRES   2 D   16  ARG VAL SER                                                  
SEQRES   1 E  270  MET PHE GLU ALA ARG LEU VAL GLN GLY SER ILE LEU LYS          
SEQRES   2 E  270  LYS VAL LEU GLU ALA LEU LYS ASP LEU ILE ASN GLU ALA          
SEQRES   3 E  270  CYS TRP ASP ILE SER SER SER GLY VAL ASN LEU GLN SER          
SEQRES   4 E  270  MET ASP SER SER HIS VAL SER LEU VAL GLN LEU THR LEU          
SEQRES   5 E  270  ARG SER GLU GLY PHE ASP THR TYR ARG CYS ASP ARG ASN          
SEQRES   6 E  270  LEU ALA MET GLY VAL ASN LEU THR SER MET SER LYS ILE          
SEQRES   7 E  270  LEU LYS CYS ALA GLY ASN GLU ASP ILE ILE THR LEU ARG          
SEQRES   8 E  270  ALA GLU ASP ASN ALA ASP THR LEU ALA LEU VAL PHE GLU          
SEQRES   9 E  270  ALA PRO ASN GLN GLU LYS VAL SER ASP TYR GLU MET LYS          
SEQRES  10 E  270  LEU MET ASP LEU ASP VAL GLU GLN LEU GLY ILE PRO GLU          
SEQRES  11 E  270  GLN GLU TYR SER CYS VAL VAL LYS MET PRO SER GLY GLU          
SEQRES  12 E  270  PHE ALA ARG ILE CYS ARG ASP LEU SER HIS ILE GLY ASP          
SEQRES  13 E  270  ALA VAL VAL ILE SER CYS ALA LYS ASP GLY VAL LYS PHE          
SEQRES  14 E  270  SER ALA SER GLY GLU LEU GLY ASN GLY ASN ILE LYS LEU          
SEQRES  15 E  270  SER GLN THR SER ASN VAL ASP LYS GLU GLU GLU ALA VAL          
SEQRES  16 E  270  THR ILE GLU MET ASN GLU PRO VAL GLN LEU THR PHE ALA          
SEQRES  17 E  270  LEU ARG TYR LEU ASN PHE PHE THR LYS ALA THR PRO LEU          
SEQRES  18 E  270  SER SER THR VAL THR LEU SER MET SER ALA ASP VAL PRO          
SEQRES  19 E  270  LEU VAL VAL GLU TYR LYS ILE ALA ASP MET GLY HIS LEU          
SEQRES  20 E  270  LYS TYR TYR LEU ALA PRO LYS ILE GLU ASP GLU GLU GLY          
SEQRES  21 E  270  SER LEU GLU HIS HIS HIS HIS HIS HIS HIS                      
SEQRES   1 F   16  SER ASN SER HIS GLN ASN VAL LEU SER ASN TYR PHE PRO          
SEQRES   2 F   16  ARG VAL SER                                                  
HELIX    1 AA1 GLY A    9  LYS A   20  1                                  12    
HELIX    2 AA2 GLU A   55  PHE A   57  5                                   3    
HELIX    3 AA3 LEU A   72  LYS A   80  1                                   9    
HELIX    4 AA4 SER A  141  LEU A  151  1                                  11    
HELIX    5 AA5 SER A  152  ILE A  154  5                                   3    
HELIX    6 AA6 LEU A  209  THR A  216  1                                   8    
HELIX    7 AA7 LYS A  217  SER A  222  5                                   6    
HELIX    8 AA8 VAL B  327  TYR B  331  5                                   5    
HELIX    9 AA9 GLY C    9  ALA C   18  1                                  10    
HELIX   10 AB1 GLU C   55  PHE C   57  5                                   3    
HELIX   11 AB2 LEU C   72  LYS C   80  1                                   9    
HELIX   12 AB3 SER C  141  LEU C  151  1                                  11    
HELIX   13 AB4 SER C  152  ILE C  154  5                                   3    
HELIX   14 AB5 LEU C  209  THR C  216  1                                   8    
HELIX   15 AB6 LYS C  217  SER C  222  5                                   6    
HELIX   16 AB7 VAL D  327  TYR D  331  5                                   5    
HELIX   17 AB8 GLY E    9  ALA E   18  1                                  10    
HELIX   18 AB9 GLU E   55  PHE E   57  5                                   3    
HELIX   19 AC1 LEU E   72  CYS E   81  1                                  10    
HELIX   20 AC2 SER E  141  LEU E  151  1                                  11    
HELIX   21 AC3 SER E  152  ILE E  154  5                                   3    
HELIX   22 AC4 LEU E  209  THR E  216  1                                   8    
HELIX   23 AC5 LYS E  217  SER E  222  5                                   6    
SHEET    1 AA1 9 THR A  59  CYS A  62  0                                        
SHEET    2 AA1 9 PHE A   2  LEU A   6 -1  N  GLU A   3   O  ARG A  61           
SHEET    3 AA1 9 ILE A  87  ALA A  92 -1  O  LEU A  90   N  ALA A   4           
SHEET    4 AA1 9 THR A  98  GLU A 104 -1  O  GLU A 104   N  ILE A  87           
SHEET    5 AA1 9 LYS A 110  LYS A 117 -1  O  TYR A 114   N  LEU A 101           
SHEET    6 AA1 9 GLY E 176  LEU E 182 -1  O  ASN E 179   N  ASP A 113           
SHEET    7 AA1 9 GLY E 166  SER E 172 -1  N  VAL E 167   O  LEU E 182           
SHEET    8 AA1 9 ALA E 157  ALA E 163 -1  N  VAL E 159   O  SER E 170           
SHEET    9 AA1 9 VAL E 203  ALA E 208 -1  O  VAL E 203   N  CYS E 162           
SHEET    1 AA2 9 LEU A  66  ASN A  71  0                                        
SHEET    2 AA2 9 GLU A  25  SER A  31 -1  N  ILE A  30   O  LEU A  66           
SHEET    3 AA2 9 GLY A  34  MET A  40 -1  O  ASN A  36   N  ASP A  29           
SHEET    4 AA2 9 SER A  46  ARG A  53 -1  O  LEU A  50   N  LEU A  37           
SHEET    5 AA2 9 GLY A 245  LEU A 251 -1  O  LYS A 248   N  GLN A  49           
SHEET    6 AA2 9 LEU A 235  ILE A 241 -1  N  LEU A 235   O  LEU A 251           
SHEET    7 AA2 9 THR A 224  MET A 229 -1  N  THR A 226   O  GLU A 238           
SHEET    8 AA2 9 CYS A 135  PRO A 140 -1  N  VAL A 137   O  LEU A 227           
SHEET    9 AA2 9 THR A 196  MET A 199 -1  O  THR A 196   N  LYS A 138           
SHEET    1 AA3 9 VAL A 203  ALA A 208  0                                        
SHEET    2 AA3 9 ALA A 157  ALA A 163 -1  N  ILE A 160   O  LEU A 205           
SHEET    3 AA3 9 GLY A 166  SER A 172 -1  O  SER A 170   N  VAL A 159           
SHEET    4 AA3 9 GLY A 176  SER A 183 -1  O  ILE A 180   N  PHE A 169           
SHEET    5 AA3 9 LYS C 110  LYS C 117 -1  O  ASP C 113   N  ASN A 179           
SHEET    6 AA3 9 THR C  98  GLU C 104 -1  N  LEU C 101   O  TYR C 114           
SHEET    7 AA3 9 ILE C  87  ALA C  92 -1  N  ARG C  91   O  ALA C 100           
SHEET    8 AA3 9 PHE C   2  LEU C   6 -1  N  PHE C   2   O  ALA C  92           
SHEET    9 AA3 9 THR C  59  CYS C  62 -1  O  THR C  59   N  ARG C   5           
SHEET    1 AA4 9 LEU C  66  ASN C  71  0                                        
SHEET    2 AA4 9 GLU C  25  SER C  31 -1  N  ILE C  30   O  LEU C  66           
SHEET    3 AA4 9 GLY C  34  MET C  40 -1  O  ASN C  36   N  ASP C  29           
SHEET    4 AA4 9 SER C  46  ARG C  53 -1  O  LEU C  50   N  LEU C  37           
SHEET    5 AA4 9 GLY C 245  LEU C 251 -1  O  HIS C 246   N  THR C  51           
SHEET    6 AA4 9 LEU C 235  ILE C 241 -1  N  VAL C 237   O  TYR C 249           
SHEET    7 AA4 9 THR C 224  MET C 229 -1  N  THR C 226   O  GLU C 238           
SHEET    8 AA4 9 CYS C 135  PRO C 140 -1  N  MET C 139   O  VAL C 225           
SHEET    9 AA4 9 THR C 196  MET C 199 -1  O  GLU C 198   N  VAL C 136           
SHEET    1 AA5 9 VAL C 203  ALA C 208  0                                        
SHEET    2 AA5 9 ALA C 157  ALA C 163 -1  N  CYS C 162   O  VAL C 203           
SHEET    3 AA5 9 GLY C 166  SER C 172 -1  O  SER C 170   N  VAL C 159           
SHEET    4 AA5 9 GLY C 176  LEU C 182 -1  O  ILE C 180   N  PHE C 169           
SHEET    5 AA5 9 LYS E 110  LYS E 117 -1  O  ASP E 113   N  ASN C 179           
SHEET    6 AA5 9 THR E  98  GLU E 104 -1  N  LEU E 101   O  TYR E 114           
SHEET    7 AA5 9 ILE E  87  ALA E  92 -1  N  THR E  89   O  VAL E 102           
SHEET    8 AA5 9 PHE E   2  LEU E   6 -1  N  ALA E   4   O  LEU E  90           
SHEET    9 AA5 9 THR E  59  CYS E  62 -1  O  ARG E  61   N  GLU E   3           
SHEET    1 AA6 9 LEU E  66  ASN E  71  0                                        
SHEET    2 AA6 9 GLU E  25  SER E  31 -1  N  TRP E  28   O  MET E  68           
SHEET    3 AA6 9 GLY E  34  MET E  40 -1  O  ASN E  36   N  ASP E  29           
SHEET    4 AA6 9 SER E  46  ARG E  53 -1  O  LEU E  50   N  LEU E  37           
SHEET    5 AA6 9 GLY E 245  LEU E 251 -1  O  TYR E 250   N  LEU E  47           
SHEET    6 AA6 9 LEU E 235  ILE E 241 -1  N  VAL E 237   O  TYR E 249           
SHEET    7 AA6 9 THR E 224  MET E 229 -1  N  THR E 226   O  GLU E 238           
SHEET    8 AA6 9 CYS E 135  PRO E 140 -1  N  VAL E 137   O  LEU E 227           
SHEET    9 AA6 9 THR E 196  MET E 199 -1  O  THR E 196   N  LYS E 138           
SSBOND   1 CYS A  135    CYS A  162                          1555   1555  2.04  
SSBOND   2 CYS C  135    CYS C  162                          1555   1555  2.03  
LINK         CG2 THR A 185                 OE2 GLU C 109     1555   1555  1.53  
CRYST1   71.647   71.647  322.208  90.00  90.00  90.00 P 43 21 2    24          
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      0.013957  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013957  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003104        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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