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Database: PDB
Entry: 3TBL
LinkDB: 3TBL
Original site: 3TBL 
HEADER    REPLICATION                             07-AUG-11   3TBL              
TITLE     STRUCTURE OF MONO-UBIQUITINATED PCNA: IMPLICATIONS FOR DNA POLYMERASE 
TITLE    2 SWITCHING AND OKAZAKI FRAGMENT MATURATION                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROLIFERATING CELL NUCLEAR ANTIGEN;                        
COMPND   3 CHAIN: A, B, C;                                                      
COMPND   4 SYNONYM: PCNA, CYCLIN;                                               
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: UBIQUITIN;                                                 
COMPND   8 CHAIN: D, E;                                                         
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: 668369;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: DH5A;                                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PTACTAC;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PLASMID;                                  
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 GENE: RPS27A;                                                        
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    PCNA, UBIQUITIN, TRANSLESION SYNTHESIS, REPLICATION                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Z.ZHANG,M.LEE,E.LEE,S.ZHANG                                           
REVDAT   4   29-JAN-20 3TBL    1       REMARK                                   
REVDAT   3   25-SEP-13 3TBL    1       REMARK                                   
REVDAT   2   27-JUN-12 3TBL    1       JRNL                                     
REVDAT   1   23-MAY-12 3TBL    0                                                
JRNL        AUTH   Z.ZHANG,S.ZHANG,S.H.LIN,X.WANG,L.WU,E.Y.LEE,M.Y.LEE          
JRNL        TITL   STRUCTURE OF MONOUBIQUITINATED PCNA: IMPLICATIONS FOR DNA    
JRNL        TITL 2 POLYMERASE SWITCHING AND OKAZAKI FRAGMENT MATURATION.        
JRNL        REF    CELL CYCLE                    V.  11  2128 2012              
JRNL        REFN                   ISSN 1538-4101                               
JRNL        PMID   22592530                                                     
JRNL        DOI    10.4161/CC.20595                                             
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.7_650                                       
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 : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.60                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 28695                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.225                           
REMARK   3   R VALUE            (WORKING SET) : 0.222                           
REMARK   3   FREE R VALUE                     : 0.293                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.080                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1458                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 0.60                                          
REMARK   3   SHRINKAGE RADIUS   : 0.27                                          
REMARK   3   K_SOL              : 0.31                                          
REMARK   3   B_SOL              : 103.8                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.310            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 34.450           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 127.0                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -27.94020                                            
REMARK   3    B22 (A**2) : -27.94020                                            
REMARK   3    B33 (A**2) : 55.88050                                             
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  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      :   NULL           NULL                                  
REMARK   3   ANGLE     :   NULL           NULL                                  
REMARK   3   CHIRALITY :   NULL           NULL                                  
REMARK   3   PLANARITY :   NULL           NULL                                  
REMARK   3   DIHEDRAL  :   NULL           NULL                                  
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):  13.5591 -38.7692  31.6755              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6070 T22:   0.5946                                     
REMARK   3      T33:   0.6219 T12:   0.0076                                     
REMARK   3      T13:   0.0752 T23:  -0.1572                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5447 L22:   0.8247                                     
REMARK   3      L33:   0.3412 L12:   0.2267                                     
REMARK   3      L13:   0.2586 L23:   0.3609                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0894 S12:  -0.0876 S13:  -0.0783                       
REMARK   3      S21:   0.3793 S22:  -0.2256 S23:   0.4238                       
REMARK   3      S31:   0.1604 S32:  -0.1749 S33:   0.0241                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3TBL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-AUG-11.                  
REMARK 100 THE DEPOSITION ID IS D_1000067279.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-NOV-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9793                             
REMARK 200  MONOCHROMATOR                  : ROSENBAUM-ROCK HIGH-RESOLUTION     
REMARK 200                                   DOUBLE-CRYSTAL MONOCHROMATOR.      
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 28695                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 114.000                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
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: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 59.65                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.05                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.9 TO 1.3 M SODIUM CITRATE, PH 6.5,     
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 288K                     
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       48.67850            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       80.52750            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       80.52750            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       73.01775            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       80.52750            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       80.52750            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       24.33925            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       80.52750            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       80.52750            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       73.01775            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       80.52750            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       80.52750            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       24.33925            
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       48.67850            
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: PENTAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E                         
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ASN A   187                                                      
REMARK 465     VAL A   188                                                      
REMARK 465     ASP A   189                                                      
REMARK 465     LYS A   190                                                      
REMARK 465     GLU A   191                                                      
REMARK 465     GLU A   192                                                      
REMARK 465     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     ASN B   187                                                      
REMARK 465     VAL B   188                                                      
REMARK 465     ASP B   189                                                      
REMARK 465     LYS B   190                                                      
REMARK 465     GLU B   191                                                      
REMARK 465     ASP B   257                                                      
REMARK 465     GLU B   258                                                      
REMARK 465     GLU B   259                                                      
REMARK 465     GLY B   260                                                      
REMARK 465     SER B   261                                                      
REMARK 465     SER C   186                                                      
REMARK 465     ASN C   187                                                      
REMARK 465     VAL C   188                                                      
REMARK 465     ASP C   189                                                      
REMARK 465     LYS C   190                                                      
REMARK 465     GLU C   191                                                      
REMARK 465     GLU C   259                                                      
REMARK 465     GLY C   260                                                      
REMARK 465     SER C   261                                                      
REMARK 465     MET D     1                                                      
REMARK 465     GLN D     2                                                      
REMARK 465     GLY D    75                                                      
REMARK 465     GLY D    76                                                      
REMARK 465     MET E     1                                                      
REMARK 465     GLN E     2                                                      
REMARK 465     GLY E    75                                                      
REMARK 465     GLY E    76                                                      
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    LEU D    56     O    TYR D    59              2.18            
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    LEU A  22      -59.26   -123.55                                   
REMARK 500    ASN A  24      -74.09   -101.11                                   
REMARK 500    ASP A  41     -179.61    -69.93                                   
REMARK 500    VAL A  45      -70.39    -97.70                                   
REMARK 500    ASP A  94      -78.26    -50.57                                   
REMARK 500    ASN A 107       -5.76     79.26                                   
REMARK 500    GLU A 109      -63.23   -120.34                                   
REMARK 500    VAL A 123      -61.52    -98.70                                   
REMARK 500    GLU A 124      -10.92     74.21                                   
REMARK 500    GLN A 125     -108.52     57.83                                   
REMARK 500    LEU A 126       71.22     67.22                                   
REMARK 500    GLU A 130      159.51    172.65                                   
REMARK 500    GLN A 131     -179.41   -173.44                                   
REMARK 500    SER A 183       83.86     70.05                                   
REMARK 500    ALA A 194       75.27     57.43                                   
REMARK 500    GLU A 201      139.41   -176.83                                   
REMARK 500    VAL A 233      139.64   -175.85                                   
REMARK 500    MET A 244      -58.97   -131.43                                   
REMARK 500    VAL B  45      -60.35   -120.74                                   
REMARK 500    ASP B  63      -76.13    -86.18                                   
REMARK 500    ASP B  94     -117.45     47.18                                   
REMARK 500    ALA B  96       70.18     53.86                                   
REMARK 500    GLN B 108     -109.41     67.81                                   
REMARK 500    GLU B 109      151.91    -49.64                                   
REMARK 500    LYS B 110       74.79     73.36                                   
REMARK 500    GLU B 130       70.43     58.18                                   
REMARK 500    GLU B 193     -144.16     48.18                                   
REMARK 500    ALA B 194       70.76     43.85                                   
REMARK 500    MET B 244      -63.17   -132.78                                   
REMARK 500    PRO B 253     -179.38    -66.74                                   
REMARK 500    LEU C  19      -55.23   -124.83                                   
REMARK 500    ASN C  24      -73.23    -89.38                                   
REMARK 500    ASP C  63      -72.77    -83.39                                   
REMARK 500    ASP C  94     -114.41     55.28                                   
REMARK 500    ALA C  96       71.37     60.60                                   
REMARK 500    ASN C 107       -3.46     58.49                                   
REMARK 500    GLN C 108     -136.78     59.78                                   
REMARK 500    GLU C 109      -16.42     75.80                                   
REMARK 500    ASP C 122      -76.66   -112.17                                   
REMARK 500    GLU C 124      -62.19   -131.72                                   
REMARK 500    GLN C 125     -116.11     60.05                                   
REMARK 500    LEU C 126       68.65     63.76                                   
REMARK 500    ILE C 128       77.54     51.12                                   
REMARK 500    GLU C 130     -144.76     55.64                                   
REMARK 500    GLN C 131      176.95    173.04                                   
REMARK 500    ILE C 154      -74.18   -105.88                                   
REMARK 500    LEU C 182      -61.86   -132.47                                   
REMARK 500    SER C 183       42.82     71.51                                   
REMARK 500    GLN C 184     -135.22     63.57                                   
REMARK 500    GLU C 193     -160.92   -160.13                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      61 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 VAL E   17     GLU E   18                 -149.09                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  3TBL A    1   261  UNP    P12004   PCNA_HUMAN       1    261             
DBREF  3TBL B    1   261  UNP    P12004   PCNA_HUMAN       1    261             
DBREF  3TBL C    1   261  UNP    P12004   PCNA_HUMAN       1    261             
DBREF  3TBL D    1    76  UNP    P62979   RS27A_HUMAN      1     76             
DBREF  3TBL E    1    76  UNP    P62979   RS27A_HUMAN      1     76             
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                                                          
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   76  MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE          
SEQRES   2 D   76  THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL          
SEQRES   3 D   76  LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP          
SEQRES   4 D   76  GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP          
SEQRES   5 D   76  GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER          
SEQRES   6 D   76  THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY                  
SEQRES   1 E   76  MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE          
SEQRES   2 E   76  THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL          
SEQRES   3 E   76  LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP          
SEQRES   4 E   76  GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP          
SEQRES   5 E   76  GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER          
SEQRES   6 E   76  THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY                  
HELIX    1   1 GLY A    9  ASP A   21  1                                  13    
HELIX    2   2 GLU A   55  PHE A   57  5                                   3    
HELIX    3   3 LEU A   72  LYS A   80  1                                   9    
HELIX    4   4 SER A  141  GLY A  155  1                                  15    
HELIX    5   5 LEU A  209  THR A  216  1                                   8    
HELIX    6   6 LYS A  217  SER A  222  5                                   6    
HELIX    7   7 GLY B    9  ASP B   21  1                                  13    
HELIX    8   8 LEU B   72  LYS B   80  1                                   9    
HELIX    9   9 SER B  141  GLY B  155  1                                  15    
HELIX   10  10 LEU B  209  THR B  216  1                                   8    
HELIX   11  11 LYS B  217  SER B  222  5                                   6    
HELIX   12  12 GLN C    8  ALA C   18  1                                  11    
HELIX   13  13 LEU C   72  LYS C   80  1                                   9    
HELIX   14  14 SER C  141  SER C  152  1                                  12    
HELIX   15  15 LEU C  209  THR C  216  1                                   8    
HELIX   16  16 LYS C  217  THR C  219  5                                   3    
HELIX   17  17 THR D   22  GLY D   35  1                                  14    
HELIX   18  18 THR D   55  TYR D   59  5                                   5    
HELIX   19  19 THR E   22  GLY E   35  1                                  14    
SHEET    1   A 9 THR A  59  ARG A  61  0                                        
SHEET    2   A 9 PHE A   2  LEU A   6 -1  N  GLU A   3   O  ARG A  61           
SHEET    3   A 9 ILE A  87  ALA A  92 -1  O  ALA A  92   N  PHE A   2           
SHEET    4   A 9 THR A  98  GLU A 104 -1  O  GLU A 104   N  ILE A  87           
SHEET    5   A 9 VAL A 111  LYS A 117 -1  O  TYR A 114   N  LEU A 101           
SHEET    6   A 9 GLY B 176  LYS B 181 -1  O  ASN B 179   N  ASP A 113           
SHEET    7   A 9 VAL B 167  SER B 172 -1  N  PHE B 169   O  ILE B 180           
SHEET    8   A 9 ALA B 157  CYS B 162 -1  N  SER B 161   O  LYS B 168           
SHEET    9   A 9 VAL B 203  ALA B 208 -1  O  LEU B 205   N  ILE B 160           
SHEET    1   B 9 LEU A  66  ASN A  71  0                                        
SHEET    2   B 9 GLU A  25  SER A  31 -1  N  ILE A  30   O  LEU A  66           
SHEET    3   B 9 GLY A  34  MET A  40 -1  O  ASN A  36   N  ASP A  29           
SHEET    4   B 9 LEU A  47  ARG A  53 -1  O  LEU A  50   N  LEU A  37           
SHEET    5   B 9 GLY A 245  LEU A 251 -1  O  LYS A 248   N  GLN A  49           
SHEET    6   B 9 LEU A 235  ILE A 241 -1  N  TYR A 239   O  LEU A 247           
SHEET    7   B 9 THR A 224  MET A 229 -1  N  SER A 228   O  VAL A 236           
SHEET    8   B 9 CYS A 135  PRO A 140 -1  N  MET A 139   O  VAL A 225           
SHEET    9   B 9 THR A 196  MET A 199 -1  O  THR A 196   N  LYS A 138           
SHEET    1   C 9 VAL A 203  ALA A 208  0                                        
SHEET    2   C 9 ALA A 157  ALA A 163 -1  N  CYS A 162   O  VAL A 203           
SHEET    3   C 9 GLY A 166  GLY A 173 -1  O  LYS A 168   N  SER A 161           
SHEET    4   C 9 GLY A 176  LYS A 181 -1  O  GLY A 176   N  GLY A 173           
SHEET    5   C 9 VAL C 111  LYS C 117 -1  O  ASP C 113   N  ASN A 179           
SHEET    6   C 9 THR C  98  GLU C 104 -1  N  PHE C 103   O  SER C 112           
SHEET    7   C 9 ILE C  87  ALA C  92 -1  N  ILE C  87   O  GLU C 104           
SHEET    8   C 9 PHE C   2  LEU C   6 -1  N  PHE C   2   O  ALA C  92           
SHEET    9   C 9 THR C  59  CYS C  62 -1  O  ARG C  61   N  GLU C   3           
SHEET    1   D 9 THR B  59  CYS B  62  0                                        
SHEET    2   D 9 PHE B   2  LEU B   6 -1  N  GLU B   3   O  ARG B  61           
SHEET    3   D 9 ILE B  87  ALA B  92 -1  O  ALA B  92   N  PHE B   2           
SHEET    4   D 9 THR B  98  ALA B 105 -1  O  GLU B 104   N  ILE B  87           
SHEET    5   D 9 GLN B 108  LYS B 117 -1  O  MET B 116   N  LEU B  99           
SHEET    6   D 9 GLY C 176  ILE C 180 -1  O  ASN C 177   N  GLU B 115           
SHEET    7   D 9 GLY C 166  GLY C 173 -1  N  PHE C 169   O  ILE C 180           
SHEET    8   D 9 ALA C 157  ALA C 163 -1  N  VAL C 159   O  SER C 170           
SHEET    9   D 9 VAL C 203  ALA C 208 -1  O  PHE C 207   N  VAL C 158           
SHEET    1   E 9 LEU B  66  ASN B  71  0                                        
SHEET    2   E 9 GLU B  25  ILE B  30 -1  N  ILE B  30   O  LEU B  66           
SHEET    3   E 9 GLY B  34  MET B  40 -1  O  ASN B  36   N  ASP B  29           
SHEET    4   E 9 LEU B  47  ARG B  53 -1  O  LEU B  50   N  LEU B  37           
SHEET    5   E 9 GLY B 245  LEU B 251 -1  O  HIS B 246   N  THR B  51           
SHEET    6   E 9 LEU B 235  TYR B 239 -1  N  LEU B 235   O  LEU B 251           
SHEET    7   E 9 THR B 224  MET B 229 -1  N  THR B 226   O  GLU B 238           
SHEET    8   E 9 CYS B 135  PRO B 140 -1  N  CYS B 135   O  MET B 229           
SHEET    9   E 9 THR B 196  MET B 199 -1  O  THR B 196   N  LYS B 138           
SHEET    1   F 9 LEU C  66  ASN C  71  0                                        
SHEET    2   F 9 GLU C  25  ILE C  30 -1  N  ALA C  26   O  VAL C  70           
SHEET    3   F 9 GLY C  34  MET C  40 -1  O  ASN C  36   N  ASP C  29           
SHEET    4   F 9 LEU C  47  ARG C  53 -1  O  LEU C  50   N  LEU C  37           
SHEET    5   F 9 GLY C 245  LEU C 251 -1  O  TYR C 250   N  LEU C  47           
SHEET    6   F 9 VAL C 233  ILE C 241 -1  N  TYR C 239   O  LEU C 247           
SHEET    7   F 9 THR C 224  SER C 230 -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  O  GLU C 198   N  VAL C 136           
SHEET    1   G 4 PHE D   4  THR D   7  0                                        
SHEET    2   G 4 THR D  66  LEU D  71  1  O  LEU D  67   N  LYS D   6           
SHEET    3   G 4 GLN D  41  PHE D  45 -1  N  ILE D  44   O  HIS D  68           
SHEET    4   G 4 LYS D  48  GLN D  49 -1  O  LYS D  48   N  PHE D  45           
SHEET    1   H 5 THR E  12  THR E  14  0                                        
SHEET    2   H 5 PHE E   4  LYS E   6 -1  N  VAL E   5   O  ILE E  13           
SHEET    3   H 5 THR E  66  LEU E  71  1  O  LEU E  67   N  LYS E   6           
SHEET    4   H 5 GLN E  41  PHE E  45 -1  N  ARG E  42   O  VAL E  70           
SHEET    5   H 5 LYS E  48  GLN E  49 -1  O  LYS E  48   N  PHE E  45           
CISPEP   1 ILE A  128    PRO A  129          0        -1.33                     
CISPEP   2 THR A  185    SER A  186          0         4.52                     
CISPEP   3 THR B  185    SER B  186          0        -1.02                     
CISPEP   4 ASP C  257    GLU C  258          0        -6.97                     
CRYST1  161.055  161.055   97.357  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      0.006209  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006209  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010271        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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