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Database: PDB
Entry: 4AYC
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HEADER    LIGASE                                  20-JUN-12   4AYC              
TITLE     RNF8 RING DOMAIN STRUCTURE                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: E3 UBIQUITIN-PROTEIN LIGASE RNF8;                          
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RING DOMAIN, RESIDUES 351-485;                             
COMPND   5 SYNONYM: RING FINGER PROTEIN 8;                                      
COMPND   6 EC: 6.3.2.-;                                                         
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: E3 UBIQUITIN-PROTEIN LIGASE RNF8;                          
COMPND  10 CHAIN: B;                                                            
COMPND  11 FRAGMENT: RING DOMAIN, RESIDUES 351-485;                             
COMPND  12 SYNONYM: RING FINGER PROTEIN 8;                                      
COMPND  13 EC: 6.3.2.-;                                                         
COMPND  14 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_VARIANT: PLYSS;                                    
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_VECTOR: PGEX6P;                                    
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  17 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  18 EXPRESSION_SYSTEM_VARIANT: PLYSS;                                    
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_VECTOR: PGEX6P                                     
KEYWDS    LIGASE, DNA DAMAGE, K63 CHAINS                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    F.MATTIROLI,J.H.A.VISSERS,W.J.VAN DIJK,P.IKPA,E.CITTERIO,W.VERMEULEN, 
AUTHOR   2 J.A.MARTEIJN,T.K.SIXMA                                               
REVDAT   1   26-SEP-12 4AYC    0                                                
JRNL        AUTH   F.MATTIROLI,J.H.A.VISSERS,W.J.VAN DIJK,P.IKPA,E.CITTERIO,    
JRNL        AUTH 2 W.VERMEULEN,J.A.MARTEIJN,T.K.SIXMA                           
JRNL        TITL   RNF168 UBIQUITINATES K13-15 ON H2A/H2AX TO DRIVE DNA DAMAGE  
JRNL        TITL 2 SIGNALING                                                    
JRNL        REF    CELL(CAMBRIDGE,MASS.)         V. 150  1182 2012              
JRNL        REFN                   ISSN 0092-8674                               
JRNL        PMID   22980979                                                     
JRNL        DOI    10.1016/J.CELL.2012.08.005                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0029                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,                      
REMARK   3                 STEINER,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) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.29                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.90                          
REMARK   3   NUMBER OF REFLECTIONS             : 26652                          
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) : 0.20136                         
REMARK   3   R VALUE            (WORKING SET) : 0.19973                         
REMARK   3   FREE R VALUE                     : 0.22948                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 1414                            
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) : 1.900                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.949                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1762                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 91.14                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.296                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 79                           
REMARK   3   BIN FREE R VALUE                    : 0.348                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2209                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 93                                      
REMARK   3   SOLVENT ATOMS            : 58                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) :  50.632                        
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.23                                                 
REMARK   3    B22 (A**2) : -0.46                                                
REMARK   3    B33 (A**2) : 0.23                                                 
REMARK   3    B12 (A**2) : 0.00                                                 
REMARK   3    B13 (A**2) : -0.00                                                
REMARK   3    B23 (A**2) : -0.00                                                
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A):   0.143       
REMARK   3   ESU BASED ON FREE R VALUE                       (A):   0.132       
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A):   0.108       
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2):   7.513       
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.959                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.953                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2327 ; 0.008 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  2310 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3127 ; 1.231 ; 2.010       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  5374 ; 0.742 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   279 ; 4.567 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   113 ;33.672 ;25.575       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   500 ;13.007 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    15 ;11.763 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   360 ; 0.076 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2515 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   484 ; 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   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED 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  : 8                                          
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   348        A   370                          
REMARK   3    ORIGIN FOR THE GROUP (A): -11.1630  80.9370  25.8610              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4972 T22:   0.0831                                     
REMARK   3      T33:   0.3551 T12:   0.1100                                     
REMARK   3      T13:   0.1278 T23:   0.0373                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2277 L22:  30.0862                                     
REMARK   3      L33:   5.0347 L12:  -3.5257                                     
REMARK   3      L13:  -2.1799 L23:   5.5107                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1568 S12:  -0.0577 S13:   0.1088                       
REMARK   3      S21:   0.7178 S22:   0.0914 S23:   0.2477                       
REMARK   3      S31:  -0.2793 S32:  -0.0517 S33:  -0.2481                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   371        A   398                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.2310  45.4630  29.7480              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7860 T22:   0.1478                                     
REMARK   3      T33:   0.6592 T12:   0.1254                                     
REMARK   3      T13:   0.0634 T23:   0.0360                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.0254 L22:  37.8520                                     
REMARK   3      L33:   0.9862 L12: -12.3335                                     
REMARK   3      L13:   1.9784 L23:  -6.0732                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3942 S12:  -0.1559 S13:   0.0021                       
REMARK   3      S21:   1.3575 S22:   0.4439 S23:   0.0672                       
REMARK   3      S31:  -0.2721 S32:  -0.1081 S33:  -0.0497                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   399        A   465                          
REMARK   3    RESIDUE RANGE :   A   900        A   901                          
REMARK   3    ORIGIN FOR THE GROUP (A):   8.1000  14.1960  27.5510              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1923 T22:   0.0193                                     
REMARK   3      T33:   0.2932 T12:  -0.0472                                     
REMARK   3      T13:  -0.0467 T23:   0.0193                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2183 L22:   5.4460                                     
REMARK   3      L33:   1.4446 L12:   0.5543                                     
REMARK   3      L13:  -0.1061 L23:  -0.5527                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0326 S12:  -0.0248 S13:  -0.0302                       
REMARK   3      S21:   0.3469 S22:  -0.0232 S23:  -0.3027                       
REMARK   3      S31:  -0.1949 S32:   0.0716 S33:   0.0558                       
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 :   A   466        A   483                          
REMARK   3    ORIGIN FOR THE GROUP (A):  15.1250  25.1520  18.3560              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3281 T22:   0.0653                                     
REMARK   3      T33:   0.3390 T12:  -0.0778                                     
REMARK   3      T13:  -0.0763 T23:   0.0426                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.0547 L22:  11.5486                                     
REMARK   3      L33:   8.1965 L12:  -2.3377                                     
REMARK   3      L13:  -3.6278 L23:   0.3640                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2016 S12:  -0.0116 S13:   0.3064                       
REMARK   3      S21:   0.1786 S22:  -0.0450 S23:  -0.6669                       
REMARK   3      S31:  -0.1506 S32:   0.2889 S33:  -0.1565                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   358        B   402                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.3580  51.3780  20.8380              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5558 T22:   0.1421                                     
REMARK   3      T33:   0.6209 T12:   0.0859                                     
REMARK   3      T13:   0.0029 T23:   0.0467                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7408 L22:  47.2799                                     
REMARK   3      L33:   0.5826 L12:   3.8556                                     
REMARK   3      L13:  -0.5175 L23:  -5.0636                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1232 S12:   0.0582 S13:   0.1720                       
REMARK   3      S21:  -0.5201 S22:   0.2420 S23:  -0.0849                       
REMARK   3      S31:   0.0750 S32:  -0.0539 S33:  -0.1188                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   403        B   440                          
REMARK   3    RESIDUE RANGE :   B   900        B   901                          
REMARK   3    ORIGIN FOR THE GROUP (A): -13.1410   9.5970  23.8890              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1308 T22:   0.1003                                     
REMARK   3      T33:   0.5098 T12:  -0.0023                                     
REMARK   3      T13:  -0.0037 T23:   0.0283                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.0732 L22:   4.2495                                     
REMARK   3      L33:   1.6041 L12:  -0.5894                                     
REMARK   3      L13:  -1.1832 L23:   0.2965                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0062 S12:   0.5139 S13:   0.0193                       
REMARK   3      S21:  -0.0540 S22:  -0.0381 S23:   0.8475                       
REMARK   3      S31:  -0.1684 S32:  -0.3511 S33:   0.0318                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   441        B   467                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.1240  15.7030  29.0480              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1912 T22:   0.0587                                     
REMARK   3      T33:   0.4280 T12:   0.0080                                     
REMARK   3      T13:   0.0366 T23:   0.0146                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1303 L22:   4.2478                                     
REMARK   3      L33:   3.2347 L12:  -0.5307                                     
REMARK   3      L13:  -0.7834 L23:  -0.4876                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0767 S12:   0.0748 S13:   0.3557                       
REMARK   3      S21:   0.4082 S22:  -0.0438 S23:   0.5427                       
REMARK   3      S31:  -0.2611 S32:  -0.2887 S33:  -0.0329                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   468        B   485                          
REMARK   3    ORIGIN FOR THE GROUP (A): -15.3060  15.9520  38.5200              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6645 T22:   0.3462                                     
REMARK   3      T33:   0.6863 T12:   0.1124                                     
REMARK   3      T13:   0.2615 T23:   0.0317                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.2762 L22:   8.9392                                     
REMARK   3      L33:   5.5758 L12:   1.7241                                     
REMARK   3      L13:  -0.9008 L23:  -0.2956                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3059 S12:  -0.7798 S13:   0.1146                       
REMARK   3      S21:   2.0628 S22:   0.2984 S23:   0.9096                       
REMARK   3      S31:  -0.1936 S32:  -0.3817 S33:  -0.6043                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED :  MASK                                                
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: RELATIVE TO THE PUBLICATION TWO SIDECHAINS
REMARK   3   WERE ADDED TO THE MODEL (RESIDUES A482 AND B485) RESULTING IN      
REMARK   3    SLIGHTLY DIFFERENT STATISTICS.                                    
REMARK   4                                                                      
REMARK   4 4AYC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 10-SEP-12.                  
REMARK 100 THE PDBE ID CODE IS EBI-52952.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 05-FEB-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 193                                
REMARK 200  PH                             : 6.9                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X06SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.282                              
REMARK 200  MONOCHROMATOR                  : FIXED-EXIT LN2 COOLED              
REMARK 200                                   DOUBLE CRYSTAL                     
REMARK 200                                   MONOCHROMATOR                      
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL (PILATUS 6M)                 
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS                            
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 28115                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.90                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 47.37                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY                : 6.9                                
REMARK 200  R MERGE                    (I) : 0.04                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 25.80                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.9                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.60                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.70                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: SHELXD                                                
REMARK 200 STARTING MODEL: NONE                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.1                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.8                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M NA CACODYLATE, PH 6.9,             
REMARK 280  2.5 M AMMONIUM SULPHATE, 0.8 MM                                     
REMARK 280  N,N-BIS(3-D-GLUCONAMIDOPROPYL)DEOXYCHOLAMIDE                        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-Y+1/2,-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 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       23.68700            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000      106.85850            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       23.68700            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000      106.85850            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 12650 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 31500 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -163.2 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 350   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  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     LEU A   484                                                      
REMARK 465     PHE A   485                                                      
REMARK 465     LEU B   348                                                      
REMARK 465     GLY B   349                                                      
REMARK 465     SER B   350                                                      
REMARK 465     MET B   351                                                      
REMARK 465     GLU B   352                                                      
REMARK 465     GLU B   353                                                      
REMARK 465     LEU B   354                                                      
REMARK 465     ASN B   355                                                      
REMARK 465     ARG B   356                                                      
REMARK 465     SER B   357                                                      
REMARK 465     LYS B   358                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   ND2B ASN A   394     OE2B GLU A   398              1.73            
REMARK 500   ND1  HIS A   420    ZN     ZN A  1484              2.07            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ALA A 419        3.70     85.42                                   
REMARK 500    ILE A 435       57.65    -98.52                                   
REMARK 500    ALA B 419        1.83     83.71                                   
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  ZN A1484                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN A1485                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1486                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1487                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1488                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CPQ A1489                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN B1486                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN B1487                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B1488                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL  B1489                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2CSW   RELATED DB: PDB                                   
REMARK 900  SOLUTION STRUCTURE OF THE FHA DOMAIN OF HUMAN                       
REMARK 900  UBIQUITINLIGASE PROTEIN RNF8                                        
DBREF  4AYC A  351   485  UNP    O76064   RNF8_HUMAN     351    485             
DBREF  4AYC B  351   485  UNP    O76064   RNF8_HUMAN     351    485             
SEQADV 4AYC LEU A  348  UNP  O76064              EXPRESSION TAG                 
SEQADV 4AYC GLY A  349  UNP  O76064              EXPRESSION TAG                 
SEQADV 4AYC SER A  350  UNP  O76064              EXPRESSION TAG                 
SEQADV 4AYC LEU B  348  UNP  O76064              EXPRESSION TAG                 
SEQADV 4AYC GLY B  349  UNP  O76064              EXPRESSION TAG                 
SEQADV 4AYC SER B  350  UNP  O76064              EXPRESSION TAG                 
SEQRES   1 A  138  LEU GLY SER MET GLU GLU LEU ASN ARG SER LYS LYS ASP          
SEQRES   2 A  138  PHE GLU ALA ILE ILE GLN ALA LYS ASN LYS GLU LEU GLU          
SEQRES   3 A  138  GLN THR LYS GLU GLU LYS GLU LYS MET GLN ALA GLN LYS          
SEQRES   4 A  138  GLU GLU VAL LEU SER HIS MET ASN ASP VAL LEU GLU ASN          
SEQRES   5 A  138  GLU LEU GLN CYS ILE ILE CYS SER GLU TYR PHE ILE GLU          
SEQRES   6 A  138  ALA VAL THR LEU ASN CYS ALA HIS SER PHE CYS SER TYR          
SEQRES   7 A  138  CYS ILE ASN GLU TRP MET LYS ARG LYS ILE GLU CYS PRO          
SEQRES   8 A  138  ILE CYS ARG LYS ASP ILE LYS SER LYS THR TYR SER LEU          
SEQRES   9 A  138  VAL LEU ASP ASN CYS ILE ASN LYS MET VAL ASN ASN LEU          
SEQRES  10 A  138  SER SER GLU VAL LYS GLU ARG ARG ILE VAL LEU ILE ARG          
SEQRES  11 A  138  GLU ARG LYS ALA LYS ARG LEU PHE                              
SEQRES   1 B  138  LEU GLY SER MET GLU GLU LEU ASN ARG SER LYS LYS ASP          
SEQRES   2 B  138  PHE GLU ALA ILE ILE GLN ALA LYS ASN LYS GLU LEU GLU          
SEQRES   3 B  138  GLN THR LYS GLU GLU LYS GLU LYS MET GLN ALA GLN LYS          
SEQRES   4 B  138  GLU GLU VAL LEU SER HIS MET ASN ASP VAL LEU GLU ASN          
SEQRES   5 B  138  GLU LEU GLN CYS ILE ILE CYS SER GLU TYR PHE ILE GLU          
SEQRES   6 B  138  ALA VAL THR LEU ASN CYS ALA HIS SER PHE CYS SER TYR          
SEQRES   7 B  138  CYS ILE ASN GLU TRP MET LYS ARG LYS ILE GLU CYS PRO          
SEQRES   8 B  138  ILE CYS ARG LYS ASP ILE LYS SER LYS THR TYR SER LEU          
SEQRES   9 B  138  VAL LEU ASP ASN CSO ILE ASN LYS MET VAL ASN ASN LEU          
SEQRES  10 B  138  SER SER GLU VAL LYS GLU ARG ARG ILE VAL LEU ILE ARG          
SEQRES  11 B  138  GLU ARG LYS ALA LYS ARG LEU PHE                              
MODRES 4AYC CSO B  456  CYS  S-HYDROXYCYSTEINE                                  
HET     ZN  A1484       1                                                       
HET     ZN  A1485       1                                                       
HET    SO4  A1486       5                                                       
HET    SO4  A1487       5                                                       
HET    SO4  A1488       5                                                       
HET    CPQ  A1489      60                                                       
HET    CSO  B 456       7                                                       
HET     ZN  B1486       1                                                       
HET     ZN  B1487       1                                                       
HET    GOL  B1488       6                                                       
HET     CL  B1489       1                                                       
HETNAM     CSO S-HYDROXYCYSTEINE                                                
HETNAM      ZN ZINC ION                                                         
HETNAM     SO4 SULFATE ION                                                      
HETNAM     CPQ N,N-BIS(3-D-GLUCONAMIDOPROPYL)DEOXYCHOLAMIDE                     
HETNAM     GOL GLYCEROL                                                         
HETNAM      CL CHLORIDE ION                                                     
HETSYN     CPQ DEOXY-BIGCHAP                                                    
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   2  CSO    C3 H7 N O3 S                                                 
FORMUL   3   ZN    4(ZN 2+)                                                     
FORMUL   4  SO4    3(O4 S 2-)                                                   
FORMUL   5  CPQ    C42 H75 N3 O15                                               
FORMUL   6  GOL    C3 H8 O3                                                     
FORMUL   7   CL    CL 1-                                                        
FORMUL   8  HOH   *58(H2 O)                                                     
HELIX    1   1 GLY A  349  LEU A  401  1                                  53    
HELIX    2   2 SER A  424  MET A  431  1                                   8    
HELIX    3   3 SER A  450  ASN A  462  1                                  13    
HELIX    4   4 SER A  465  ALA A  481  1                                  17    
HELIX    5   5 ASP B  360  GLU B  400  1                                  41    
HELIX    6   6 SER B  424  LYS B  434  1                                  11    
HELIX    7   7 SER B  450  ASN B  462  1                                  13    
HELIX    8   8 SER B  465  ARG B  479  1                                  15    
SHEET    1  AA 3 SER A 421  CYS A 423  0                                        
SHEET    2  AA 3 ALA A 413  LEU A 416 -1  O  VAL A 414   N  PHE A 422           
SHEET    3  AA 3 LYS A 447  TYR A 449 -1  O  THR A 448   N  THR A 415           
SHEET    1  BA 3 SER B 421  CYS B 423  0                                        
SHEET    2  BA 3 ALA B 413  LEU B 416 -1  O  VAL B 414   N  PHE B 422           
SHEET    3  BA 3 LYS B 447  TYR B 449 -1  O  THR B 448   N  THR B 415           
SITE     1 AC1  4 CYS A 418  HIS A 420  CYS A 437  CYS A 440                    
SITE     1 AC2  4 CYS A 403  CYS A 406  CYS A 423  CYS A 426                    
SITE     1 AC3  3 SER A 465  SER A 466  GLU A 467                               
SITE     1 AC4  3 LYS A 442  ASP A 443  TYR B 449                               
SITE     1 AC5  5 LEU A 354  ARG A 477  ALA A 481  LYS A 482                    
SITE     2 AC5  5 PHE B 361                                                     
SITE     1 AC6 10 ILE A 405  GLU A 429  TRP A 430  LYS A 432                    
SITE     2 AC6 10 ARG A 433  LYS A 434  HOH A2021  TYR B 425                    
SITE     3 AC6 10 CYS B 426  ARG B 479                                          
SITE     1 AC7  4 CYS B 418  HIS B 420  CYS B 437  CYS B 440                    
SITE     1 AC8  4 CYS B 403  CYS B 406  CYS B 423  CYS B 426                    
SITE     1 AC9  5 MET A 431  ILE A 444  LYS A 445  LYS A 447                    
SITE     2 AC9  5 MET B 431                                                     
SITE     1 BC1  1 ASP B 443                                                     
CRYST1   47.374  213.717   34.102  90.00  90.00  90.00 P 21 21 2     8          
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      0.021109  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.004679  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.029324        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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