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