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Database: PDB
Entry: 4RJF
LinkDB: 4RJF
Original site: 4RJF 
HEADER    REPLICATION                             09-OCT-14   4RJF              
TITLE     CRYSTAL STRUCTURE OF THE HUMAN SLIDING CLAMP AT 2.0 ANGSTROM          
TITLE    2 RESOLUTION                                                           
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: CYCLIN-DEPENDENT KINASE INHIBITOR 1;                       
COMPND   8 CHAIN: B, D, F;                                                      
COMPND   9 FRAGMENT: 22 C TERMINAL RESIDUES (139 - 160);                        
COMPND  10 SYNONYM: CDK-INTERACTING PROTEIN 1, MELANOMA DIFFERENTIATION-        
COMPND  11 ASSOCIATED PROTEIN 6, MDA-6, P21;                                    
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MUTATION: 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 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PMCSG19;                                  
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 SYNTHETIC: YES;                                                      
SOURCE  13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  14 ORGANISM_COMMON: HUMAN;                                              
SOURCE  15 ORGANISM_TAXID: 9606;                                                
SOURCE  16 OTHER_DETAILS: P21 PEPTIDE CHEMICALLY SYNTHESIZED                    
KEYWDS    SLIDING CLAMP, PROCESSIVITY FACTOR, P21, DNA POLYMERASE, NUCLEUS,     
KEYWDS   2 REPLICATION                                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.J.KROKER,J.B.BRUNING                                                
REVDAT   1   26-AUG-15 4RJF    0                                                
JRNL        AUTH   A.J.KROKER,J.B.BRUNING                                       
JRNL        TITL   P21 EXPLOITS RESIDUE TYR151 AS A TETHER FOR HIGH-AFFINITY    
JRNL        TITL 2 PCNA BINDING.                                                
JRNL        REF    BIOCHEMISTRY                  V.  54  3483 2015              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   25972089                                                     
JRNL        DOI    10.1021/ACS.BIOCHEM.5B00241                                  
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.01 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX                                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : TWIN_LSQ_F                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.01                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.27                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.980                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 63385                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.155                           
REMARK   3   R VALUE            (WORKING SET) : 0.148                           
REMARK   3   FREE R VALUE                     : 0.189                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.120                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1976                            
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 19.8886 -  4.8163    0.97     4383   149  0.1388 0.1496        
REMARK   3     2  4.8163 -  3.8318    0.97     4371   136  0.1206 0.1714        
REMARK   3     3  3.8318 -  3.3501    0.97     4398   139  0.1371 0.1862        
REMARK   3     4  3.3501 -  3.0449    0.97     4342   143  0.1438 0.1627        
REMARK   3     5  3.0449 -  2.8273    0.97     4386   140  0.1508 0.2164        
REMARK   3     6  2.8273 -  2.6611    0.97     4384   139  0.1612 0.1800        
REMARK   3     7  2.6611 -  2.5281    0.97     4388   140  0.1647 0.1736        
REMARK   3     8  2.5281 -  2.4182    0.97     4348   139  0.1693 0.2612        
REMARK   3     9  2.4182 -  2.3253    0.97     4385   138  0.1782 0.2038        
REMARK   3    10  2.3253 -  2.2451    0.97     4410   146  0.1801 0.2725        
REMARK   3    11  2.2451 -  2.1750    0.97     4303   140  0.1856 0.2176        
REMARK   3    12  2.1750 -  2.1129    0.97     4424   141  0.1951 0.2532        
REMARK   3    13  2.1129 -  2.0574    0.97     4367   140  0.2003 0.2536        
REMARK   3    14  2.0574 -  2.0072    0.97     4390   146  0.2149 0.3063        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
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)     : NULL             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.770           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 28.60                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 26.15                          
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: 0.4900                                                   
REMARK   3   OPERATOR: -H,-K,L                                                  
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.002           6358                                  
REMARK   3   ANGLE     :  0.631           8566                                  
REMARK   3   CHIRALITY :  0.025           1007                                  
REMARK   3   PLANARITY :  0.003           1093                                  
REMARK   3   DIHEDRAL  : 12.848           2375                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
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 4RJF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-OCT-14.                  
REMARK 100 THE RCSB ID CODE IS RCSB087420.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-JUL-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU MICROMAX-007 HF             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : RIGAKU VARIMAX HF MIRRORS          
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV++                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 63388                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.007                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 41.410                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 7.100                              
REMARK 200  R MERGE                    (I) : 0.05500                            
REMARK 200  R SYM                      (I) : 0.05500                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 25.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.01                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.06                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.44900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.800                              
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: 1AXC                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.34                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.58                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.08M STRONTIUM CHLORIDE HEXAHYDRATE,    
REMARK 280  0.02M MAGNESIUM CHLORIDE HEXAHYDRATE, 0.04M SODIUM CACODYLATE       
REMARK 280  TRIHYDRATE (PH7.0), 20% V/V (+/-)-2-METHYL-2,4-PENTANEDIOL AND      
REMARK 280  0.012M SPERMINE TETRAHYDROCHLORIDE, FINAL [PCNA] = 11.6MG/ML =      
REMARK 280  0.40MM, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 289K             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 3                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
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 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.866025 -0.500000  0.000000      247.63130            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3 -0.500000  0.866025  0.000000     -214.45500            
REMARK 350   BIOMT2   3 -0.866025 -0.500000  0.000000      123.81565            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -0.500000 -0.866025  0.000000      142.97000            
REMARK 350   BIOMT2   2  0.866025 -0.500000  0.000000      247.63130            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3 -0.500000  0.866025  0.000000     -142.97000            
REMARK 350   BIOMT2   3 -0.866025 -0.500000  0.000000      247.63130            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350   BIOMT1   2 -0.500000 -0.866025  0.000000       71.48500            
REMARK 350   BIOMT2   2  0.866025 -0.500000  0.000000      123.81565            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3 -0.500000  0.866025  0.000000      -71.48500            
REMARK 350   BIOMT2   3 -0.866025 -0.500000  0.000000      123.81565            
REMARK 350   BIOMT3   3  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     GLU A   256                                                      
REMARK 465     ASP A   257                                                      
REMARK 465     GLU A   258                                                      
REMARK 465     GLU A   259                                                      
REMARK 465     GLY A   260                                                      
REMARK 465     SER A   261                                                      
REMARK 465     GLY B   139                                                      
REMARK 465     VAL C   188                                                      
REMARK 465     ASP C   189                                                      
REMARK 465     GLU C   256                                                      
REMARK 465     ASP C   257                                                      
REMARK 465     GLU C   258                                                      
REMARK 465     GLU C   259                                                      
REMARK 465     GLY C   260                                                      
REMARK 465     SER C   261                                                      
REMARK 465     GLY D   139                                                      
REMARK 465     ARG D   140                                                      
REMARK 465     ASN E   107                                                      
REMARK 465     GLN E   108                                                      
REMARK 465     ASN E   187                                                      
REMARK 465     VAL E   188                                                      
REMARK 465     ASP E   189                                                      
REMARK 465     LYS E   190                                                      
REMARK 465     GLU E   256                                                      
REMARK 465     ASP E   257                                                      
REMARK 465     GLU E   258                                                      
REMARK 465     GLU E   259                                                      
REMARK 465     GLY E   260                                                      
REMARK 465     SER E   261                                                      
REMARK 465     GLY F   139                                                      
REMARK 465     ARG F   140                                                      
REMARK 465     LYS F   141                                                      
REMARK 465     ARG F   142                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ASN A  95    CG   OD1  ND2                                       
REMARK 470     ASP A  97    CG   OD1  OD2                                       
REMARK 470     ASP A 165    CG   OD1  OD2                                       
REMARK 470     ASN A 187    CG   OD1  ND2                                       
REMARK 470     VAL A 188    CG1  CG2                                            
REMARK 470     ASP A 189    CG   OD1  OD2                                       
REMARK 470     GLU A 198    CG   CD   OE1  OE2                                  
REMARK 470     ILE A 255    CG1  CG2  CD1                                       
REMARK 470     ARG B 140    N    CA   CB   CG   CD   NE   CZ                    
REMARK 470     ARG B 140    NH1  NH2                                            
REMARK 470     LYS B 141    CG   CD   CE   NZ                                   
REMARK 470     GLU C  17    CB   CG   CD   OE1  OE2                             
REMARK 470     LEU C  22    CB   CG   CD1  CD2                                  
REMARK 470     TRP C  28    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP C  28    CZ3  CH2                                            
REMARK 470     SER C  39    CB   OG                                             
REMARK 470     ASN C  95    CG   OD1  ND2                                       
REMARK 470     ASP C  97    CB   CG   OD1  OD2                                  
REMARK 470     SER C 186    N                                                   
REMARK 470     GLU C 191    CG   CD   OE1  OE2                                  
REMARK 470     LYS D 141    N    CA   O    CB   CG   CD   CE                    
REMARK 470     LYS D 141    NZ                                                  
REMARK 470     HIS D 152    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLU E 109    CG   CD   OE1  OE2                                  
REMARK 470     ASP E 113    CG   OD1  OD2                                       
REMARK 470     SER E 152    OG                                                  
REMARK 470     LYS E 164    CG   CD   CE   NZ                                   
REMARK 470     LEU E 182    CG   CD1  CD2                                       
REMARK 470     ILE E 255    CG1  CG2  CD1                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    HIS A  44       16.37     59.96                                   
REMARK 500    GLU A  93     -156.64   -101.08                                   
REMARK 500    ASN A  95       30.04    -95.27                                   
REMARK 500    ASP A  97       30.21    -98.44                                   
REMARK 500    PRO A 106       45.59    -79.09                                   
REMARK 500    GLU A 109      -13.23   -170.55                                   
REMARK 500    ALA A 163     -154.22   -105.55                                   
REMARK 500    ASN A 187       44.68    -72.97                                   
REMARK 500    LYS A 190     -166.64   -163.56                                   
REMARK 500    GLU A 191      -45.87   -160.72                                   
REMARK 500    MET A 244      -73.47   -134.98                                   
REMARK 500    ARG B 142      -45.40   -147.82                                   
REMARK 500    SER C  39      145.73   -173.97                                   
REMARK 500    GLN C 108        9.17     51.87                                   
REMARK 500    GLU C 109       40.04    -98.93                                   
REMARK 500    LYS C 110      118.13   -163.85                                   
REMARK 500    MET C 244      -42.46   -141.71                                   
REMARK 500    ARG D 142       28.28   -147.23                                   
REMARK 500    LYS E  20        0.19    -65.95                                   
REMARK 500    ALA E 163     -168.07   -127.17                                   
REMARK 500    PRO E 234      144.13    -38.81                                   
REMARK 500    ALA E 242      105.44    -39.70                                   
REMARK 500    MET E 244      -42.60   -137.42                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH E 755        DISTANCE =  5.43 ANGSTROMS                       
REMARK 525    HOH E 794        DISTANCE =  7.63 ANGSTROMS                       
DBREF  4RJF A    1   261  UNP    P12004   PCNA_HUMAN       1    261             
DBREF  4RJF B  139   160  UNP    P38936   CDN1A_HUMAN    139    160             
DBREF  4RJF C    1   261  UNP    P12004   PCNA_HUMAN       1    261             
DBREF  4RJF D  139   160  UNP    P38936   CDN1A_HUMAN    139    160             
DBREF  4RJF E    1   261  UNP    P12004   PCNA_HUMAN       1    261             
DBREF  4RJF F  139   160  UNP    P38936   CDN1A_HUMAN    139    160             
SEQADV 4RJF PHE B  151  UNP  P38936    TYR   151 ENGINEERED MUTATION            
SEQADV 4RJF PHE D  151  UNP  P38936    TYR   151 ENGINEERED MUTATION            
SEQADV 4RJF PHE F  151  UNP  P38936    TYR   151 ENGINEERED MUTATION            
SEQRES   1 A  261  MET PHE GLU ALA ARG LEU VAL GLN GLY SER ILE LEU LYS          
SEQRES   2 A  261  LYS VAL LEU GLU ALA LEU LYS ASP LEU ILE ASN GLU ALA          
SEQRES   3 A  261  CYS TRP ASP ILE SER SER SER GLY VAL ASN LEU GLN SER          
SEQRES   4 A  261  MET ASP SER SER HIS VAL SER LEU VAL GLN LEU THR LEU          
SEQRES   5 A  261  ARG SER GLU GLY PHE ASP THR TYR ARG CYS ASP ARG ASN          
SEQRES   6 A  261  LEU ALA MET GLY VAL ASN LEU THR SER MET SER LYS ILE          
SEQRES   7 A  261  LEU LYS CYS ALA GLY ASN GLU ASP ILE ILE THR LEU ARG          
SEQRES   8 A  261  ALA GLU ASP ASN ALA ASP THR LEU ALA LEU VAL PHE GLU          
SEQRES   9 A  261  ALA PRO ASN GLN GLU LYS VAL SER ASP TYR GLU MET LYS          
SEQRES  10 A  261  LEU MET ASP LEU ASP VAL GLU GLN LEU GLY ILE PRO GLU          
SEQRES  11 A  261  GLN GLU TYR SER CYS VAL VAL LYS MET PRO SER GLY GLU          
SEQRES  12 A  261  PHE ALA ARG ILE CYS ARG ASP LEU SER HIS ILE GLY ASP          
SEQRES  13 A  261  ALA VAL VAL ILE SER CYS ALA LYS ASP GLY VAL LYS PHE          
SEQRES  14 A  261  SER ALA SER GLY GLU LEU GLY ASN GLY ASN ILE LYS LEU          
SEQRES  15 A  261  SER GLN THR SER ASN VAL ASP LYS GLU GLU GLU ALA VAL          
SEQRES  16 A  261  THR ILE GLU MET ASN GLU PRO VAL GLN LEU THR PHE ALA          
SEQRES  17 A  261  LEU ARG TYR LEU ASN PHE PHE THR LYS ALA THR PRO LEU          
SEQRES  18 A  261  SER SER THR VAL THR LEU SER MET SER ALA ASP VAL PRO          
SEQRES  19 A  261  LEU VAL VAL GLU TYR LYS ILE ALA ASP MET GLY HIS LEU          
SEQRES  20 A  261  LYS TYR TYR LEU ALA PRO LYS ILE GLU ASP GLU GLU GLY          
SEQRES  21 A  261  SER                                                          
SEQRES   1 B   22  GLY ARG LYS ARG ARG GLN THR SER MET THR ASP PHE PHE          
SEQRES   2 B   22  HIS SER LYS ARG ARG LEU ILE PHE SER                          
SEQRES   1 C  261  MET PHE GLU ALA ARG LEU VAL GLN GLY SER ILE LEU LYS          
SEQRES   2 C  261  LYS VAL LEU GLU ALA LEU LYS ASP LEU ILE ASN GLU ALA          
SEQRES   3 C  261  CYS TRP ASP ILE SER SER SER GLY VAL ASN LEU GLN SER          
SEQRES   4 C  261  MET ASP SER SER HIS VAL SER LEU VAL GLN LEU THR LEU          
SEQRES   5 C  261  ARG SER GLU GLY PHE ASP THR TYR ARG CYS ASP ARG ASN          
SEQRES   6 C  261  LEU ALA MET GLY VAL ASN LEU THR SER MET SER LYS ILE          
SEQRES   7 C  261  LEU LYS CYS ALA GLY ASN GLU ASP ILE ILE THR LEU ARG          
SEQRES   8 C  261  ALA GLU ASP ASN ALA ASP THR LEU ALA LEU VAL PHE GLU          
SEQRES   9 C  261  ALA PRO ASN GLN GLU LYS VAL SER ASP TYR GLU MET LYS          
SEQRES  10 C  261  LEU MET ASP LEU ASP VAL GLU GLN LEU GLY ILE PRO GLU          
SEQRES  11 C  261  GLN GLU TYR SER CYS VAL VAL LYS MET PRO SER GLY GLU          
SEQRES  12 C  261  PHE ALA ARG ILE CYS ARG ASP LEU SER HIS ILE GLY ASP          
SEQRES  13 C  261  ALA VAL VAL ILE SER CYS ALA LYS ASP GLY VAL LYS PHE          
SEQRES  14 C  261  SER ALA SER GLY GLU LEU GLY ASN GLY ASN ILE LYS LEU          
SEQRES  15 C  261  SER GLN THR SER ASN VAL ASP LYS GLU GLU GLU ALA VAL          
SEQRES  16 C  261  THR ILE GLU MET ASN GLU PRO VAL GLN LEU THR PHE ALA          
SEQRES  17 C  261  LEU ARG TYR LEU ASN PHE PHE THR LYS ALA THR PRO LEU          
SEQRES  18 C  261  SER SER THR VAL THR LEU SER MET SER ALA ASP VAL PRO          
SEQRES  19 C  261  LEU VAL VAL GLU TYR LYS ILE ALA ASP MET GLY HIS LEU          
SEQRES  20 C  261  LYS TYR TYR LEU ALA PRO LYS ILE GLU ASP GLU GLU GLY          
SEQRES  21 C  261  SER                                                          
SEQRES   1 D   22  GLY ARG LYS ARG ARG GLN THR SER MET THR ASP PHE PHE          
SEQRES   2 D   22  HIS SER LYS ARG ARG LEU ILE PHE SER                          
SEQRES   1 E  261  MET PHE GLU ALA ARG LEU VAL GLN GLY SER ILE LEU LYS          
SEQRES   2 E  261  LYS VAL LEU GLU ALA LEU LYS ASP LEU ILE ASN GLU ALA          
SEQRES   3 E  261  CYS TRP ASP ILE SER SER SER GLY VAL ASN LEU GLN SER          
SEQRES   4 E  261  MET ASP SER SER HIS VAL SER LEU VAL GLN LEU THR LEU          
SEQRES   5 E  261  ARG SER GLU GLY PHE ASP THR TYR ARG CYS ASP ARG ASN          
SEQRES   6 E  261  LEU ALA MET GLY VAL ASN LEU THR SER MET SER LYS ILE          
SEQRES   7 E  261  LEU LYS CYS ALA GLY ASN GLU ASP ILE ILE THR LEU ARG          
SEQRES   8 E  261  ALA GLU ASP ASN ALA ASP THR LEU ALA LEU VAL PHE GLU          
SEQRES   9 E  261  ALA PRO ASN GLN GLU LYS VAL SER ASP TYR GLU MET LYS          
SEQRES  10 E  261  LEU MET ASP LEU ASP VAL GLU GLN LEU GLY ILE PRO GLU          
SEQRES  11 E  261  GLN GLU TYR SER CYS VAL VAL LYS MET PRO SER GLY GLU          
SEQRES  12 E  261  PHE ALA ARG ILE CYS ARG ASP LEU SER HIS ILE GLY ASP          
SEQRES  13 E  261  ALA VAL VAL ILE SER CYS ALA LYS ASP GLY VAL LYS PHE          
SEQRES  14 E  261  SER ALA SER GLY GLU LEU GLY ASN GLY ASN ILE LYS LEU          
SEQRES  15 E  261  SER GLN THR SER ASN VAL ASP LYS GLU GLU GLU ALA VAL          
SEQRES  16 E  261  THR ILE GLU MET ASN GLU PRO VAL GLN LEU THR PHE ALA          
SEQRES  17 E  261  LEU ARG TYR LEU ASN PHE PHE THR LYS ALA THR PRO LEU          
SEQRES  18 E  261  SER SER THR VAL THR LEU SER MET SER ALA ASP VAL PRO          
SEQRES  19 E  261  LEU VAL VAL GLU TYR LYS ILE ALA ASP MET GLY HIS LEU          
SEQRES  20 E  261  LYS TYR TYR LEU ALA PRO LYS ILE GLU ASP GLU GLU GLY          
SEQRES  21 E  261  SER                                                          
SEQRES   1 F   22  GLY ARG LYS ARG ARG GLN THR SER MET THR ASP PHE PHE          
SEQRES   2 F   22  HIS SER LYS ARG ARG LEU ILE PHE SER                          
FORMUL   7  HOH   *1927(H2 O)                                                   
HELIX    1   1 GLY A    9  ALA A   18  1                                  10    
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  SER A  152  1                                  12    
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 SER B  146  PHE B  150  5                                   5    
HELIX    8   8 GLY C    9  ALA C   18  1                                  10    
HELIX    9   9 GLU C   55  PHE C   57  5                                   3    
HELIX   10  10 LEU C   72  LYS C   80  1                                   9    
HELIX   11  11 SER C  141  SER C  152  1                                  12    
HELIX   12  12 LEU C  209  THR C  216  1                                   8    
HELIX   13  13 LYS C  217  SER C  222  5                                   6    
HELIX   14  14 SER D  146  PHE D  150  5                                   5    
HELIX   15  15 GLY E    9  ALA E   18  1                                  10    
HELIX   16  16 LEU E   72  LYS E   80  1                                   9    
HELIX   17  17 SER E  141  SER E  152  1                                  12    
HELIX   18  18 LEU E  209  THR E  216  1                                   8    
HELIX   19  19 LYS E  217  SER E  222  5                                   6    
HELIX   20  20 SER F  146  PHE F  150  5                                   5    
SHEET    1   A 5 THR A  59  CYS A  62  0                                        
SHEET    2   A 5 PHE A   2  LEU A   6 -1  N  GLU A   3   O  ARG A  61           
SHEET    3   A 5 ILE A  87  ALA A  92 -1  O  ILE A  88   N  LEU A   6           
SHEET    4   A 5 THR A  98  GLU A 104 -1  O  ALA A 100   N  ARG A  91           
SHEET    5   A 5 VAL A 111  LYS A 117 -1  O  MET A 116   N  LEU A  99           
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  GLY A  34   N  SER A  31           
SHEET    4   B 9 SER A  46  ARG A  53 -1  O  LEU A  52   N  VAL A  35           
SHEET    5   B 9 GLY A 245  LEU A 251 -1  O  HIS A 246   N  THR A  51           
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  THR A 226   O  GLU A 238           
SHEET    8   B 9 CYS A 135  PRO A 140 -1  N  CYS A 135   O  MET A 229           
SHEET    9   B 9 THR A 196  MET A 199 -1  O  GLU A 198   N  VAL A 136           
SHEET    1   C 2 LEU A 121  GLY A 127  0                                        
SHEET    2   C 2 HIS B 152  ILE B 158 -1  O  LYS B 154   N  GLN A 125           
SHEET    1   D 4 GLY A 176  SER A 183  0                                        
SHEET    2   D 4 GLY A 166  GLY A 173 -1  N  VAL A 167   O  LEU A 182           
SHEET    3   D 4 ALA A 157  CYS A 162 -1  N  SER A 161   O  LYS A 168           
SHEET    4   D 4 VAL A 203  ALA A 208 -1  O  VAL A 203   N  CYS A 162           
SHEET    1   E 2 LYS A 254  ILE A 255  0                                        
SHEET    2   E 2 ARG B 143  GLN B 144 -1  O  ARG B 143   N  ILE A 255           
SHEET    1   F 5 THR C  59  CYS C  62  0                                        
SHEET    2   F 5 PHE C   2  LEU C   6 -1  N  GLU C   3   O  ARG C  61           
SHEET    3   F 5 ILE C  87  ALA C  92 -1  O  ILE C  88   N  LEU C   6           
SHEET    4   F 5 THR C  98  GLU C 104 -1  O  ALA C 100   N  ARG C  91           
SHEET    5   F 5 VAL C 111  LYS C 117 -1  O  TYR C 114   N  LEU C 101           
SHEET    1   G 9 LEU C  66  ASN C  71  0                                        
SHEET    2   G 9 GLU C  25  SER C  31 -1  N  ALA C  26   O  VAL C  70           
SHEET    3   G 9 GLY C  34  MET C  40 -1  O  ASN C  36   N  ASP C  29           
SHEET    4   G 9 SER C  46  ARG C  53 -1  O  LEU C  52   N  VAL C  35           
SHEET    5   G 9 GLY C 245  LEU C 251 -1  O  LYS C 248   N  GLN C  49           
SHEET    6   G 9 LEU C 235  ILE C 241 -1  N  VAL C 237   O  TYR C 249           
SHEET    7   G 9 THR C 224  MET C 229 -1  N  SER C 228   O  VAL C 236           
SHEET    8   G 9 CYS C 135  PRO C 140 -1  N  MET C 139   O  VAL C 225           
SHEET    9   G 9 THR C 196  MET C 199 -1  O  GLU C 198   N  VAL C 136           
SHEET    1   H 2 LEU C 121  GLY C 127  0                                        
SHEET    2   H 2 HIS D 152  ILE D 158 -1  O  HIS D 152   N  GLY C 127           
SHEET    1   I 4 GLY C 176  SER C 183  0                                        
SHEET    2   I 4 GLY C 166  GLY C 173 -1  N  VAL C 167   O  LEU C 182           
SHEET    3   I 4 ALA C 157  ALA C 163 -1  N  ALA C 163   O  GLY C 166           
SHEET    4   I 4 VAL C 203  ALA C 208 -1  O  PHE C 207   N  VAL C 158           
SHEET    1   J 5 THR E  59  CYS E  62  0                                        
SHEET    2   J 5 PHE E   2  LEU E   6 -1  N  GLU E   3   O  ARG E  61           
SHEET    3   J 5 ILE E  87  ALA E  92 -1  O  ALA E  92   N  PHE E   2           
SHEET    4   J 5 THR E  98  GLU E 104 -1  O  VAL E 102   N  THR E  89           
SHEET    5   J 5 VAL E 111  LYS E 117 -1  O  MET E 116   N  LEU E  99           
SHEET    1   K 9 LEU E  66  ASN E  71  0                                        
SHEET    2   K 9 GLU E  25  ILE E  30 -1  N  ALA E  26   O  VAL E  70           
SHEET    3   K 9 GLY E  34  MET E  40 -1  O  ASN E  36   N  ASP E  29           
SHEET    4   K 9 SER E  46  ARG E  53 -1  O  LEU E  52   N  VAL E  35           
SHEET    5   K 9 GLY E 245  LEU E 251 -1  O  HIS E 246   N  THR E  51           
SHEET    6   K 9 LEU E 235  ILE E 241 -1  N  VAL E 237   O  TYR E 249           
SHEET    7   K 9 THR E 224  MET E 229 -1  N  SER E 228   O  VAL E 236           
SHEET    8   K 9 CYS E 135  PRO E 140 -1  N  CYS E 135   O  MET E 229           
SHEET    9   K 9 THR E 196  MET E 199 -1  O  GLU E 198   N  VAL E 136           
SHEET    1   L 2 ASP E 122  LEU E 126  0                                        
SHEET    2   L 2 SER F 153  LEU F 157 -1  O  LYS F 154   N  GLN E 125           
SHEET    1   M 4 GLY E 176  SER E 183  0                                        
SHEET    2   M 4 GLY E 166  GLY E 173 -1  N  GLY E 173   O  GLY E 176           
SHEET    3   M 4 ALA E 157  CYS E 162 -1  N  SER E 161   O  LYS E 168           
SHEET    4   M 4 VAL E 203  ALA E 208 -1  O  LEU E 205   N  ILE E 160           
SSBOND   1 CYS E  135    CYS E  162                          1555   1555  2.03  
CISPEP   1 ASN A  107    GLN A  108          0        -3.42                     
CRYST1  142.970  142.970   41.410  90.00  90.00 120.00 P 3           9          
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      0.006994  0.004038  0.000000        0.00000                         
SCALE2      0.000000  0.008077  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.024149        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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