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Database: PDB
Entry: 2YBF
LinkDB: 2YBF
Original site: 2YBF 
HEADER    LIGASE                                  08-MAR-11   2YBF              
TITLE     COMPLEX OF RAD18 (RAD6 BINDING DOMAIN) WITH RAD6B                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: UBIQUITIN-CONJUGATING ENZYME E2 B;                         
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: RAD6 HOMOLOG B, HR6B, HHR6B, UBIQUITIN CARRIER PROTEIN B,   
COMPND   5 UBIQUITIN-CONJUGATING ENZYME E2-17 KDA, UBIQUITIN-PROTEIN LIGASE B,  
COMPND   6 RAD6B;                                                               
COMPND   7 EC: 6.3.2.19;                                                        
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: E3 UBIQUITIN-PROTEIN LIGASE RAD18;                         
COMPND  11 CHAIN: B;                                                            
COMPND  12 FRAGMENT: RAD6-BINDING DOMAIN, RESIDUES 340-366;                     
COMPND  13 SYNONYM: POSTREPLICATION REPAIR PROTEIN RAD18, HHR18, HRAD18, RING   
COMPND  14 FINGER PROTEIN 73;                                                   
COMPND  15 EC: 6.3.2.-;                                                         
COMPND  16 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_VECTOR: PET28A;                                    
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 SYNTHETIC: YES;                                                      
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606                                                 
KEYWDS    LIGASE, E2 UBIQUITIN CONJUGATING ENZYME, E3 UBIQUITIN LIGASE,         
KEYWDS   2 TRANSLESION SYNTHESIS, PCNA UBIQUITINATION                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.G.HIBBERT,T.K.SIXMA                                                 
REVDAT   2   20-DEC-23 2YBF    1       REMARK LINK                              
REVDAT   1   20-APR-11 2YBF    0                                                
JRNL        AUTH   R.G.HIBBERT,A.HUANG,R.BOELENS,T.K.SIXMA                      
JRNL        TITL   E3 LIGASE RAD18 PROMOTES MONOUBIQUITINATION RATHER THAN      
JRNL        TITL 2 UBIQUITIN CHAIN FORMATION BY E2 ENZYME RAD6.                 
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 108  5590 2011              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   21422291                                                     
JRNL        DOI    10.1073/PNAS.1017516108                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0099                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 24.92                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 11364                          
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) : 0.201                           
REMARK   3   R VALUE            (WORKING SET) : 0.199                           
REMARK   3   FREE R VALUE                     : 0.242                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 599                             
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) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.05                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 741                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 91.02                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2300                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 39                           
REMARK   3   BIN FREE R VALUE                    : 0.2520                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1390                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 15                                      
REMARK   3   SOLVENT ATOMS            : 85                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 22.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 29.22                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.95000                                             
REMARK   3    B22 (A**2) : -0.95000                                             
REMARK   3    B33 (A**2) : 1.43000                                              
REMARK   3    B12 (A**2) : -0.48000                                             
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.220         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.181         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.124         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.518         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.942                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.905                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1486 ; 0.006 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  1056 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2022 ; 0.927 ; 1.962       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  2571 ; 0.779 ; 3.001       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   183 ; 4.598 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    81 ;33.864 ;24.568       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   259 ;11.705 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    12 ;13.113 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   207 ; 0.057 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1656 ; 0.003 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   297 ; 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):   881 ; 0.359 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   340 ; 0.078 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1440 ; 0.681 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   605 ; 1.095 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   575 ; 1.785 ; 4.500       
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  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     3        A    20                          
REMARK   3    ORIGIN FOR THE GROUP (A):  34.9012  21.7186  -7.3071              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0143 T22:   0.1123                                     
REMARK   3      T33:   0.0252 T12:   0.0061                                     
REMARK   3      T13:   0.0066 T23:  -0.0194                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.2756 L22:  19.5811                                     
REMARK   3      L33:   4.1273 L12:   6.5613                                     
REMARK   3      L13:  -1.9980 L23:   1.7102                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2423 S12:   0.3319 S13:  -0.1754                       
REMARK   3      S21:  -0.2617 S22:   0.2525 S23:   0.2959                       
REMARK   3      S31:  -0.0494 S32:   0.0331 S33:  -0.0102                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    21        A   131                          
REMARK   3    RESIDUE RANGE :   A  1153        A  1153                          
REMARK   3    ORIGIN FOR THE GROUP (A):  23.1538  32.1658   2.5521              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0512 T22:   0.0644                                     
REMARK   3      T33:   0.0114 T12:  -0.0144                                     
REMARK   3      T13:  -0.0104 T23:   0.0140                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.0694 L22:   1.6006                                     
REMARK   3      L33:   3.0827 L12:  -0.1843                                     
REMARK   3      L13:  -0.9635 L23:   1.4535                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0710 S12:   0.0963 S13:   0.0998                       
REMARK   3      S21:  -0.0773 S22:   0.0039 S23:   0.1001                       
REMARK   3      S31:  -0.1456 S32:  -0.0801 S33:   0.0671                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   132        A   152                          
REMARK   3    ORIGIN FOR THE GROUP (A):  22.5875  46.2326  13.8887              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3321 T22:   0.1782                                     
REMARK   3      T33:   0.3517 T12:  -0.0339                                     
REMARK   3      T13:   0.0306 T23:  -0.1924                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  26.6128 L22:   5.8483                                     
REMARK   3      L33:  10.2139 L12:  -4.2649                                     
REMARK   3      L13:   9.0321 L23:  -3.0610                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.7950 S12:  -1.2771 S13:   2.2020                       
REMARK   3      S21:   0.8416 S22:   0.1411 S23:   0.3587                       
REMARK   3      S31:  -1.2852 S32:  -0.4983 S33:   0.6539                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   341        B   361                          
REMARK   3    ORIGIN FOR THE GROUP (A):  37.1547  30.9396  10.6826              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0946 T22:   0.1746                                     
REMARK   3      T33:   0.0603 T12:   0.0348                                     
REMARK   3      T13:  -0.0224 T23:  -0.0744                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  10.1623 L22:   6.2544                                     
REMARK   3      L33:  10.8143 L12:  -0.0860                                     
REMARK   3      L13:  -1.9034 L23:  -1.6299                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0020 S12:  -0.6075 S13:  -0.1317                       
REMARK   3      S21:   0.6848 S22:   0.0999 S23:  -0.1633                       
REMARK   3      S31:  -0.2483 S32:   0.1125 S33:  -0.1019                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : 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 2YBF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 08-MAR-11.                  
REMARK 100 THE DEPOSITION ID IS D_1290047534.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-MAR-09                          
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               : ESRF                               
REMARK 200  BEAMLINE                       : ID23-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.873                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 12029                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 24.920                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY                : 12.90                              
REMARK 200  R MERGE                    (I) : 0.13000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.11                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 12.10                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.72000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.700                              
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: PDB ENTRY 1AYZ                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 38.10                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.99                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.5                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/6                                            
REMARK 290       6555   X-Y,X,Z+5/6                                             
REMARK 290       7555   Y,X,-Z+2/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+1/3                                          
REMARK 290      10555   -Y,-X,-Z+1/6                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+5/6                                            
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      111.38000            
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       55.69000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       83.53500            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       27.84500            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      139.22500            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      111.38000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000       55.69000            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       27.84500            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000       83.53500            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000      139.22500            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2470 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 9470 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -47.4 KCAL/MOL                        
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 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     MET A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     SER B   340                                                      
REMARK 465     LYS B   362                                                      
REMARK 465     LYS B   363                                                      
REMARK 465     ILE B   364                                                      
REMARK 465     ALA B   365                                                      
REMARK 465     GLY B   366                                                      
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    GLU A  30     -113.33     44.06                                   
REMARK 500    ASP A  50       -1.03     77.17                                   
REMARK 500    GLN A  93     -110.15   -130.25                                   
REMARK 500    GLU A 132      -67.47    -90.66                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A1155  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SO4 A1154   O1                                                     
REMARK 620 2 SO4 A1154   O4   48.0                                              
REMARK 620 3 HOH A2004   O   106.0  67.7                                        
REMARK 620 4 HOH A2006   O   103.6 119.6  76.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME A 1153                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1154                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 1155                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1362                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2YB6   RELATED DB: PDB                                   
REMARK 900 NATIVE HUMAN RAD6                                                    
REMARK 900 RELATED ID: 2Y4W   RELATED DB: PDB                                   
REMARK 900 SOLUTION STRUCTURE OF HUMAN UBIQUITIN CONJUGATING ENZYME RAD6B       
REMARK 900 RELATED ID: 1NXA   RELATED DB: PDB                                   
REMARK 900 HOMOLOGY MODELED UBIQUITIN-PROTEIN LIGASE B                          
REMARK 900 RELATED ID: 1JAS   RELATED DB: PDB                                   
REMARK 900 HSUBC2B                                                              
REMARK 900 RELATED ID: 2Y43   RELATED DB: PDB                                   
REMARK 900 RAD18 UBIQUITIN LIGASE RING DOMAIN STRUCTURE                         
DBREF  2YBF A    1   152  UNP    P63146   UBE2B_HUMAN      1    152             
DBREF  2YBF B  340   366  UNP    Q9NS91   RAD18_HUMAN    340    366             
SEQRES   1 A  152  MET SER THR PRO ALA ARG ARG ARG LEU MET ARG ASP PHE          
SEQRES   2 A  152  LYS ARG LEU GLN GLU ASP PRO PRO VAL GLY VAL SER GLY          
SEQRES   3 A  152  ALA PRO SER GLU ASN ASN ILE MET GLN TRP ASN ALA VAL          
SEQRES   4 A  152  ILE PHE GLY PRO GLU GLY THR PRO PHE GLU ASP GLY THR          
SEQRES   5 A  152  PHE LYS LEU VAL ILE GLU PHE SER GLU GLU TYR PRO ASN          
SEQRES   6 A  152  LYS PRO PRO THR VAL ARG PHE LEU SER LYS MET PHE HIS          
SEQRES   7 A  152  PRO ASN VAL TYR ALA ASP GLY SER ILE CYS LEU ASP ILE          
SEQRES   8 A  152  LEU GLN ASN ARG TRP SER PRO THR TYR ASP VAL SER SER          
SEQRES   9 A  152  ILE LEU THR SER ILE GLN SER LEU LEU ASP GLU PRO ASN          
SEQRES  10 A  152  PRO ASN SER PRO ALA ASN SER GLN ALA ALA GLN LEU TYR          
SEQRES  11 A  152  GLN GLU ASN LYS ARG GLU TYR GLU LYS ARG VAL SER ALA          
SEQRES  12 A  152  ILE VAL GLU GLN SER TRP ASN ASP SER                          
SEQRES   1 B   27  SER LYS TYR ARG LYS LYS HIS LYS SER GLU PHE GLN LEU          
SEQRES   2 B   27  LEU VAL ASP GLN ALA ARG LYS GLY TYR LYS LYS ILE ALA          
SEQRES   3 B   27  GLY                                                          
HET    BME  A1153       4                                                       
HET    SO4  A1154       5                                                       
HET     NA  A1155       1                                                       
HET    SO4  B1362       5                                                       
HETNAM     BME BETA-MERCAPTOETHANOL                                             
HETNAM     SO4 SULFATE ION                                                      
HETNAM      NA SODIUM ION                                                       
FORMUL   3  BME    C2 H6 O S                                                    
FORMUL   4  SO4    2(O4 S 2-)                                                   
FORMUL   5   NA    NA 1+                                                        
FORMUL   7  HOH   *85(H2 O)                                                     
HELIX    1   1 THR A    3  ASP A   19  1                                  17    
HELIX    2   2 LEU A   89  GLN A   93  5                                   5    
HELIX    3   3 ASP A  101  GLU A  115  1                                  15    
HELIX    4   4 ASN A  123  GLU A  132  1                                  10    
HELIX    5   5 ASN A  133  SER A  148  1                                  16    
HELIX    6   6 LYS B  341  HIS B  346  1                                   6    
HELIX    7   7 HIS B  346  LYS B  359  1                                  14    
SHEET    1  AA 4 VAL A  24  SER A  29  0                                        
SHEET    2  AA 4 ASN A  32  PHE A  41 -1  N  ASN A  32   O  SER A  29           
SHEET    3  AA 4 THR A  52  GLU A  58 -1  O  PHE A  53   N  ILE A  40           
SHEET    4  AA 4 THR A  69  PHE A  72 -1  O  THR A  69   N  GLU A  58           
LINK         O1  SO4 A1154                NA    NA A1155     1555   1555  2.98  
LINK         O4  SO4 A1154                NA    NA A1155     1555   1555  2.85  
LINK        NA    NA A1155                 O   HOH A2004     1555   1555  3.18  
LINK        NA    NA A1155                 O   HOH A2006     1555  12554  2.56  
CISPEP   1 TYR A   63    PRO A   64          0         8.23                     
SITE     1 AC1  4 PHE A  13  CYS A  88  GLN A  93  ASN A  94                    
SITE     1 AC2  5 ARG A   7  ARG A   8  ARG A  11   NA A1155                    
SITE     2 AC2  5 HOH A2001                                                     
SITE     1 AC3  3 ARG A  11  SO4 A1154  HOH A2006                               
SITE     1 AC4  3 LYS B 341  TYR B 342  ARG B 343                               
CRYST1   58.210   58.210  167.070  90.00  90.00 120.00 P 65 2 2     12          
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      0.017179  0.009918  0.000000        0.00000                         
SCALE2      0.000000  0.019837  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005986        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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