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