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Database: PDB
Entry: 3VKX
LinkDB: 3VKX
Original site: 3VKX 
HEADER    DNA BINDING PROTEIN                     26-NOV-11   3VKX              
TITLE     STRUCTURE OF PCNA                                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROLIFERATING CELL NUCLEAR ANTIGEN;                        
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: PCNA, CYCLIN;                                               
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: PCNA;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    NUCLEI, DNA BINDING PROTEIN                                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.HASHIMOTO,A.HISHIKI,T.SHIMIZU,M.SATO,C.PUNCHIHEWA,M.CONNELLY,       
AUTHOR   2 M.ACTIS,B.WADDELL,V.PAGALA,N.FUJII                                   
REVDAT   2   14-AUG-13 3VKX    1       JRNL                                     
REVDAT   1   14-MAR-12 3VKX    0                                                
JRNL        AUTH   C.PUNCHIHEWA,A.INOUE,A.HISHIKI,Y.FUJIKAWA,M.CONNELLY,        
JRNL        AUTH 2 B.EVISON,Y.SHAO,R.HEATH,I.KURAOKA,P.RODRIGUES,H.HASHIMOTO,   
JRNL        AUTH 3 M.KAWANISHI,M.SATO,T.YAGI,N.FUJII                            
JRNL        TITL   IDENTIFICATION OF SMALL MOLECULE PROLIFERATING CELL NUCLEAR  
JRNL        TITL 2 ANTIGEN (PCNA) INHIBITOR THAT DISRUPTS INTERACTIONS WITH     
JRNL        TITL 3 PIP-BOX PROTEINS AND INHIBITS DNA REPLICATION                
JRNL        REF    J.BIOL.CHEM.                  V. 287 14289 2012              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   22383522                                                     
JRNL        DOI    10.1074/JBC.M112.353201                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0117                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 26564                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.205                           
REMARK   3   R VALUE            (WORKING SET) : 0.203                           
REMARK   3   FREE R VALUE                     : 0.249                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1408                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.15                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1703                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 91.84                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4060                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 87                           
REMARK   3   BIN FREE R VALUE                    : 0.4280                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1907                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 54                                      
REMARK   3   SOLVENT ATOMS            : 116                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 58.12                          
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  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.147         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.150         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.121         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.796        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.962                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.940                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1980 ; 0.009 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  1294 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2679 ; 1.302 ; 2.009       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  3191 ; 0.798 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   246 ; 6.271 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    80 ;42.206 ;25.625       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   359 ;14.609 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     8 ;14.267 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   317 ; 0.073 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2144 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   356 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 5                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A   255                          
REMARK   3    RESIDUE RANGE :   A   301        A   301                          
REMARK   3    RESIDUE RANGE :   A   262        A   268                          
REMARK   3    RESIDUE RANGE :   A   269        A   300                          
REMARK   3    RESIDUE RANGE :   A   302        A   385                          
REMARK   3    ORIGIN FOR THE GROUP (A): -17.1176  18.4420  35.9729              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0734 T22:   0.0647                                     
REMARK   3      T33:   0.0892 T12:  -0.0466                                     
REMARK   3      T13:   0.0563 T23:  -0.0115                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3926 L22:   0.7107                                     
REMARK   3      L33:   0.4731 L12:   0.0713                                     
REMARK   3      L13:   0.3267 L23:   0.4336                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0193 S12:   0.0398 S13:  -0.0331                       
REMARK   3      S21:  -0.0577 S22:   0.0588 S23:  -0.1033                       
REMARK   3      S31:  -0.0181 S32:   0.0655 S33:  -0.0782                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3VKX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 05-DEC-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB095173.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 05-MAR-11                          
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : BL-5A                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1                                  
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 28025                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: 2ZVM                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 71.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.24                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 21 3                           
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290       5555   Z,X,Y                                                   
REMARK 290       6555   Z+1/2,-X+1/2,-Y                                         
REMARK 290       7555   -Z+1/2,-X,Y+1/2                                         
REMARK 290       8555   -Z,X+1/2,-Y+1/2                                         
REMARK 290       9555   Y,Z,X                                                   
REMARK 290      10555   -Y,Z+1/2,-X+1/2                                         
REMARK 290      11555   Y+1/2,-Z+1/2,-X                                         
REMARK 290      12555   -Y+1/2,-Z,X+1/2                                         
REMARK 290      13555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290      14555   -X,-Y+1/2,Z                                             
REMARK 290      15555   -X+1/2,Y,-Z                                             
REMARK 290      16555   X,-Y,-Z+1/2                                             
REMARK 290      17555   Z+1/2,X+1/2,Y+1/2                                       
REMARK 290      18555   Z,-X,-Y+1/2                                             
REMARK 290      19555   -Z,-X+1/2,Y                                             
REMARK 290      20555   -Z+1/2,X,-Y                                             
REMARK 290      21555   Y+1/2,Z+1/2,X+1/2                                       
REMARK 290      22555   -Y+1/2,Z,-X                                             
REMARK 290      23555   Y,-Z,-X+1/2                                             
REMARK 290      24555   -Y,-Z+1/2,X                                             
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       71.55350            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       71.55350            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       71.55350            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       71.55350            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       71.55350            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       71.55350            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY2   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   6  0.000000  0.000000  1.000000       71.55350            
REMARK 290   SMTRY2   6 -1.000000  0.000000  0.000000       71.55350            
REMARK 290   SMTRY3   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   7  0.000000  0.000000 -1.000000       71.55350            
REMARK 290   SMTRY2   7 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  1.000000  0.000000       71.55350            
REMARK 290   SMTRY1   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY2   8  1.000000  0.000000  0.000000       71.55350            
REMARK 290   SMTRY3   8  0.000000 -1.000000  0.000000       71.55350            
REMARK 290   SMTRY1   9  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   9  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY3   9  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  10  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  10  0.000000  0.000000  1.000000       71.55350            
REMARK 290   SMTRY3  10 -1.000000  0.000000  0.000000       71.55350            
REMARK 290   SMTRY1  11  0.000000  1.000000  0.000000       71.55350            
REMARK 290   SMTRY2  11  0.000000  0.000000 -1.000000       71.55350            
REMARK 290   SMTRY3  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  12  0.000000 -1.000000  0.000000       71.55350            
REMARK 290   SMTRY2  12  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY3  12  1.000000  0.000000  0.000000       71.55350            
REMARK 290   SMTRY1  13  1.000000  0.000000  0.000000       71.55350            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       71.55350            
REMARK 290   SMTRY3  13  0.000000  0.000000  1.000000       71.55350            
REMARK 290   SMTRY1  14 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  14  0.000000 -1.000000  0.000000       71.55350            
REMARK 290   SMTRY3  14  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1  15 -1.000000  0.000000  0.000000       71.55350            
REMARK 290   SMTRY2  15  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  15  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1  16  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  16  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000       71.55350            
REMARK 290   SMTRY1  17  0.000000  0.000000  1.000000       71.55350            
REMARK 290   SMTRY2  17  1.000000  0.000000  0.000000       71.55350            
REMARK 290   SMTRY3  17  0.000000  1.000000  0.000000       71.55350            
REMARK 290   SMTRY1  18  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY2  18 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3  18  0.000000 -1.000000  0.000000       71.55350            
REMARK 290   SMTRY1  19  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY2  19 -1.000000  0.000000  0.000000       71.55350            
REMARK 290   SMTRY3  19  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY1  20  0.000000  0.000000 -1.000000       71.55350            
REMARK 290   SMTRY2  20  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3  20  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY1  21  0.000000  1.000000  0.000000       71.55350            
REMARK 290   SMTRY2  21  0.000000  0.000000  1.000000       71.55350            
REMARK 290   SMTRY3  21  1.000000  0.000000  0.000000       71.55350            
REMARK 290   SMTRY1  22  0.000000 -1.000000  0.000000       71.55350            
REMARK 290   SMTRY2  22  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY3  22 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  23  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  23  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY3  23 -1.000000  0.000000  0.000000       71.55350            
REMARK 290   SMTRY1  24  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  24  0.000000  0.000000 -1.000000       71.55350            
REMARK 290   SMTRY3  24  1.000000  0.000000  0.000000        0.00000            
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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8870 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 33850 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -225.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 350   BIOMT2   2  1.000000  0.000000  0.000000       71.55350            
REMARK 350   BIOMT3   2  0.000000 -1.000000  0.000000       71.55350            
REMARK 350   BIOMT1   3  0.000000  1.000000  0.000000      -71.55350            
REMARK 350   BIOMT2   3  0.000000  0.000000 -1.000000       71.55350            
REMARK 350   BIOMT3   3 -1.000000  0.000000  0.000000        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     SER A   186                                                      
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     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 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    MET A 244      -46.11   -159.98                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE T3 A 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 262                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 263                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 264                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 265                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 266                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 267                 
DBREF  3VKX A    1   261  UNP    P12004   PCNA_HUMAN       1    261             
SEQRES   1 A  261  MET PHE GLU ALA ARG LEU VAL GLN GLY SER ILE LEU LYS          
SEQRES   2 A  261  LYS VAL LEU GLU ALA LEU LYS ASP LEU ILE ASN GLU ALA          
SEQRES   3 A  261  CYS TRP ASP ILE SER SER SER GLY VAL ASN LEU GLN SER          
SEQRES   4 A  261  MET ASP SER SER HIS VAL SER LEU VAL GLN LEU THR LEU          
SEQRES   5 A  261  ARG SER GLU GLY PHE ASP THR TYR ARG CYS ASP ARG ASN          
SEQRES   6 A  261  LEU ALA MET GLY VAL ASN LEU THR SER MET SER LYS ILE          
SEQRES   7 A  261  LEU LYS CYS ALA GLY ASN GLU ASP ILE ILE THR LEU ARG          
SEQRES   8 A  261  ALA GLU ASP ASN ALA ASP THR LEU ALA LEU VAL PHE GLU          
SEQRES   9 A  261  ALA PRO ASN GLN GLU LYS VAL SER ASP TYR GLU MET LYS          
SEQRES  10 A  261  LEU MET ASP LEU ASP VAL GLU GLN LEU GLY ILE PRO GLU          
SEQRES  11 A  261  GLN GLU TYR SER CYS VAL VAL LYS MET PRO SER GLY GLU          
SEQRES  12 A  261  PHE ALA ARG ILE CYS ARG ASP LEU SER HIS ILE GLY ASP          
SEQRES  13 A  261  ALA VAL VAL ILE SER CYS ALA LYS ASP GLY VAL LYS PHE          
SEQRES  14 A  261  SER ALA SER GLY GLU LEU GLY ASN GLY ASN ILE LYS LEU          
SEQRES  15 A  261  SER GLN THR SER ASN VAL ASP LYS GLU GLU GLU ALA VAL          
SEQRES  16 A  261  THR ILE GLU MET ASN GLU PRO VAL GLN LEU THR PHE ALA          
SEQRES  17 A  261  LEU ARG TYR LEU ASN PHE PHE THR LYS ALA THR PRO LEU          
SEQRES  18 A  261  SER SER THR VAL THR LEU SER MET SER ALA ASP VAL PRO          
SEQRES  19 A  261  LEU VAL VAL GLU TYR LYS ILE ALA ASP MET GLY HIS LEU          
SEQRES  20 A  261  LYS TYR TYR LEU ALA PRO LYS ILE GLU ASP GLU GLU GLY          
SEQRES  21 A  261  SER                                                          
HET     T3  A 301      23                                                       
HET    SO4  A 262       5                                                       
HET    SO4  A 263       5                                                       
HET    SO4  A 264       5                                                       
HET    SO4  A 265       5                                                       
HET    SO4  A 266       5                                                       
HET    SO4  A 267       5                                                       
HET     CL  A 268       1                                                       
HETNAM      T3 3,5,3'TRIIODOTHYRONINE                                           
HETNAM     SO4 SULFATE ION                                                      
HETNAM      CL CHLORIDE ION                                                     
HETSYN      T3 T3; THYROID HORMONE; LIOTHYRONINE                                
FORMUL   2   T3    C15 H12 I3 N O4                                              
FORMUL   3  SO4    6(O4 S 2-)                                                   
FORMUL   9   CL    CL 1-                                                        
FORMUL  10  HOH   *116(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    
SHEET    1   A 5 THR A  59  ARG A  61  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  GLU A 104   N  ILE A  87           
SHEET    5   A 5 VAL A 111  LYS A 117 -1  O  TYR A 114   N  LEU A 101           
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  52   N  VAL A  35           
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  ILE A 241   O  GLY A 245           
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  VAL A 137   O  LEU A 227           
SHEET    9   B 9 THR A 196  MET A 199 -1  O  THR A 196   N  LYS A 138           
SHEET    1   C 4 ASN A 177  SER A 183  0                                        
SHEET    2   C 4 GLY A 166  SER A 172 -1  N  VAL A 167   O  LEU A 182           
SHEET    3   C 4 ALA A 157  CYS A 162 -1  N  SER A 161   O  LYS A 168           
SHEET    4   C 4 VAL A 203  ALA A 208 -1  O  LEU A 205   N  ILE A 160           
SITE     1 AC1 10 MET A  40  LEU A  47  GLY A 127  PRO A 129                    
SITE     2 AC1 10 GLN A 131  ASP A 232  PRO A 234  TYR A 250                    
SITE     3 AC1 10 ILE A 255  HOH A 379                                          
SITE     1 AC2  6 GLY A 142  GLU A 143  ARG A 146  HOH A 359                    
SITE     2 AC2  6 HOH A 364  HOH A 378                                          
SITE     1 AC3  3 LYS A 168  LYS A 181  HOH A 356                               
SITE     1 AC4  6 ARG A  53  GLU A 238  LYS A 240  GLY A 245                    
SITE     2 AC4  6 HIS A 246  HOH A 357                                          
SITE     1 AC5  2 ARG A 146  ARG A 149                                          
SITE     1 AC6  7 TYR A 133  SER A 228  VAL A 236  GLU A 238                    
SITE     2 AC6  7 LYS A 248  TYR A 250  HOH A 323                               
SITE     1 AC7  5 GLN A  49  THR A  51  HIS A 246  HOH A 357                    
SITE     2 AC7  5 HOH A 376                                                     
CRYST1  143.107  143.107  143.107  90.00  90.00  90.00 I 21 3       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      0.006988  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006988  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006988        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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