HEADER LIGASE 11-JAN-11 2Y4W
TITLE SOLUTION STRUCTURE OF HUMAN UBIQUITIN CONJUGATING ENZYME
TITLE 2 RAD6B
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UBIQUITIN-CONJUGATING ENZYME E2 B;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: RAD6 HOMOLOG B, UBIQUITIN CARRIER PROTEIN B,
COMPND 5 UBIQUITIN-CONJUGATING ENZYME E2-17 KDA, UBIQUITIN-PROTEIN LIGASE
COMPND 6 B, HR6B, HHR6B, RAD6B;
COMPND 7 EC: 6.3.2.19;
COMPND 8 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: PLIS
KEYWDS LIGASE, DNA DAMAGE, DNA REPAIR, UBIQUITINATION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR A.HUANG,R.G.HIBBERT,R.N.DEJONG,D.DAS,T.K.SIXMA,R.BOELENS
REVDAT 2 27-JUN-12 2Y4W 1 JRNL REMARK VERSN
REVDAT 1 11-MAY-11 2Y4W 0
JRNL AUTH A.HUANG,R.G.HIBBERT,R.N.DEJONG,D.DAS,T.K.SIXMA,R.BOELENS
JRNL TITL SYMMETRY AND ASYMMETRY OF THE RING-RING DIMER OF RAD18
JRNL REF J.MOL.BIOL. V. 410 424 2011
JRNL REFN ISSN 0022-2836
JRNL PMID 21549715
JRNL DOI 10.1016/J.JMB.2011.04.051
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,READ,
REMARK 3 : RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINMENT ACCORDING TO RECOORD
REMARK 3 APPROACH
REMARK 4
REMARK 4 2Y4W COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 05-JAN-11.
REMARK 100 THE PDBE ID CODE IS EBI-46914.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 310.0
REMARK 210 PH : 8.0
REMARK 210 IONIC STRENGTH : 300MM
REMARK 210 PRESSURE : 1.0 ATM
REMARK 210 SAMPLE CONTENTS : 50MM KH2PO4/K2HPO4 (PH 8.0),
REMARK 210 300 MM NACL, 1 MM DTT,
REMARK 210 95%/5% H2O/D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D 1H-15N HSQC, 2D 1H-13C
REMARK 210 HSQC, 2D 1H-1H NOESY, 3D
REMARK 210 CBCA(CO)NH, 3D C(CO)NH, 3D
REMARK 210 HNCO, 3D HNCA, 3D HNCACB,
REMARK 210 3D HBHA(CO)NH, 3D HN(CO)CA,
REMARK 210 3D HCCH-TOCSY, 3D 1H-15N
REMARK 210 NOESY, 3D 1H-13C NOESY, 3D
REMARK 210 HNCACO, 3D CNH-NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : SPARKY
REMARK 210 METHOD USED : CYANA
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE
REMARK 210 NMR SPECTROSCOPY ON 13C, 15N-LABELED RAD6B
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
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 HD21 ASN A 117 H ASN A 119 1.50
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 1 ASP A 19 84.10 -162.30
REMARK 500 1 SER A 29 -89.20 -96.76
REMARK 500 1 ASN A 32 176.58 -55.34
REMARK 500 1 GLU A 62 -83.72 -60.63
REMARK 500 1 PRO A 67 109.15 -47.02
REMARK 500 1 SER A 120 75.07 56.70
REMARK 500 1 GLU A 132 -73.46 -93.69
REMARK 500 2 SER A 2 103.84 59.65
REMARK 500 2 ASP A 19 81.42 -165.70
REMARK 500 2 SER A 29 -83.21 -86.26
REMARK 500 2 ASN A 32 -172.89 -63.31
REMARK 500 2 PRO A 47 0.09 -65.45
REMARK 500 2 GLU A 62 -77.84 -61.35
REMARK 500 2 PRO A 68 -177.27 -69.56
REMARK 500 2 ARG A 71 138.28 -171.31
REMARK 500 2 GLN A 93 -162.97 -100.89
REMARK 500 2 PRO A 118 26.36 -76.90
REMARK 500 2 GLU A 132 -78.68 -88.14
REMARK 500 3 ASP A 19 81.60 -150.23
REMARK 500 3 SER A 29 -70.34 -65.42
REMARK 500 3 GLU A 30 -39.64 -173.45
REMARK 500 3 ASN A 31 99.58 -65.98
REMARK 500 3 ASN A 32 -167.97 56.12
REMARK 500 3 PRO A 47 5.39 -68.41
REMARK 500 3 GLU A 62 -82.08 -58.48
REMARK 500 3 GLN A 93 -159.91 -76.40
REMARK 500 3 PRO A 116 -175.16 -68.74
REMARK 500 3 GLU A 132 -81.98 -82.04
REMARK 500 4 ASP A 19 86.57 -156.57
REMARK 500 4 GLU A 30 -80.61 62.86
REMARK 500 4 ASN A 32 -174.21 -59.27
REMARK 500 4 PRO A 43 -171.73 -69.63
REMARK 500 4 GLU A 61 88.02 -62.38
REMARK 500 4 GLU A 62 -79.35 -134.93
REMARK 500 4 GLN A 93 -162.54 -73.08
REMARK 500 4 PRO A 116 -174.14 -69.52
REMARK 500 4 PRO A 118 23.74 -77.77
REMARK 500 4 GLU A 132 -83.75 -102.39
REMARK 500 4 ASN A 150 90.61 56.93
REMARK 500 4 ASP A 151 -10.63 -140.83
REMARK 500 5 ASP A 19 85.18 -164.20
REMARK 500 5 SER A 29 -81.29 -88.24
REMARK 500 5 GLU A 62 -83.80 -57.51
REMARK 500 5 PRO A 68 -174.57 -65.72
REMARK 500 5 GLN A 93 -164.08 -77.29
REMARK 500 5 SER A 120 75.08 -154.27
REMARK 500 5 GLU A 132 -80.15 -101.46
REMARK 500 6 ASP A 19 85.32 -151.13
REMARK 500 6 SER A 29 -68.22 -94.56
REMARK 500 6 GLU A 30 -35.42 -133.24
REMARK 500
REMARK 500 THIS ENTRY HAS 191 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
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 2Y4W A 1 152 UNP P63146 UBE2B_HUMAN 1 152
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
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 VAL A 102 GLU A 115 1 14
HELIX 4 4 ASN A 123 ASN A 133 1 11
HELIX 5 5 ASN A 133 SER A 148 1 16
SHEET 1 AA 4 VAL A 24 ALA A 27 0
SHEET 2 AA 4 ASN A 37 PHE A 41 -1 O ASN A 37 N ALA A 27
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
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
MODEL 1
(ATOM LINES ARE NOT SHOWN.)
END
