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Biological Magnetic Resonance Data Bank


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BMRB Entry 17443

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17443
MolProbity Validation Chart

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Title: Solution structure of human ubiquitin conjugating enzyme Rad6b   PubMed: 21549715

Deposition date: 2011-02-04 Original release date: 2011-05-12

Authors: Huang, Anding; Hibbert, R.; Dejong, R.; Das, D.; Sixma, T.; Boelens, R.

Citation: Huang, Anding; Hibbert, Richard; de Jong, Rob; Das, Devashish; Sixma, Titia; Boelens, Rolf. "Symmetry and Asymmetry of the RING-RING Dimer of Rad18."  J. Mol. Biol. 410, 424-435 (2011).

Assembly members:
UBIQUITIN-CONJUGATING_ENZYME_E2_B, polymer, 152 residues, 17307.2685 Da.

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
UBIQUITIN-CONJUGATING_ENZYME_E2_B: MSTPARRRLMRDFKRLQEDP PVGVSGAPSENNIMQWNAVI FGPEGTPFEDGTFKLVIEFS EEYPNKPPTVRFLSKMFHPN VYADGSICLDILQNRWSPTY DVSSILTSIQSLLDEPNPNS PANSQAAQLYQENKREYEKR VSAIVEQSWNDS

Data sets:
Data typeCount
13C chemical shifts581
15N chemical shifts140
1H chemical shifts971

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1UBIQUITIN-CONJUGATING ENZYME E2 B1

Entities:

Entity 1, UBIQUITIN-CONJUGATING ENZYME E2 B 152 residues - 17307.2685 Da.

1   METSERTHRPROALAARGARGARGLEUMET
2   ARGASPPHELYSARGLEUGLNGLUASPPRO
3   PROVALGLYVALSERGLYALAPROSERGLU
4   ASNASNILEMETGLNTRPASNALAVALILE
5   PHEGLYPROGLUGLYTHRPROPHEGLUASP
6   GLYTHRPHELYSLEUVALILEGLUPHESER
7   GLUGLUTYRPROASNLYSPROPROTHRVAL
8   ARGPHELEUSERLYSMETPHEHISPROASN
9   VALTYRALAASPGLYSERILECYSLEUASP
10   ILELEUGLNASNARGTRPSERPROTHRTYR
11   ASPVALSERSERILELEUTHRSERILEGLN
12   SERLEULEUASPGLUPROASNPROASNSER
13   PROALAASNSERGLNALAALAGLNLEUTYR
14   GLNGLUASNLYSARGGLUTYRGLULYSARG
15   VALSERALAILEVALGLUGLNSERTRPASN
16   ASPSER

Samples:

sample_1: UBIQUITIN-CONJUGATING ENZYME E2 B 1 mM

sample_conditions_1: ionic strength: 300.000 mM; pH: 8.000; pressure: 1.000 atm; temperature: 310.000 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1solutionsample_conditions_1
2D 1H-13C HSQCsample_1solutionsample_conditions_1
2D 1H-1H NOESYsample_1solutionsample_conditions_1
3D CBCA(CO)NHsample_1solutionsample_conditions_1
3D C(CO)NHsample_1solutionsample_conditions_1
3D HNCOsample_1solutionsample_conditions_1
3D HNCAsample_1solutionsample_conditions_1
3D HNCACBsample_1solutionsample_conditions_1
3D HBHA(CO)NHsample_1solutionsample_conditions_1
3D HN(CO)CAsample_1solutionsample_conditions_1
3D HCCH-TOCSYsample_1solutionsample_conditions_1
3D 1H-15N NOESYsample_1solutionsample_conditions_1
3D 1H-13C NOESYsample_1solutionsample_conditions_1
3D HNCACOsample_1solutionsample_conditions_1
3D CNH-NOESYsample_1solutionsample_conditions_1

Software:

AutoDep v4.3, PDBe - na

CNS vany, BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE- - refinement

SPARKY vany, Goddard - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 750 MHz

Related Database Links:

UNP UBE2B_HUMAN
PDB
DBJ BAB26934 BAB27570 BAE28135 BAE40998 BAE88681
EMBL CAA37339 CAA65602 CAG28562 CAJ83014
GB AAA21087 AAA31492 AAA35982 AAB60669 AAC52884
PRF 2016220A
REF NP_001005124 NP_001032536 NP_001075765 NP_001085320 NP_001181362
SP P63146 P63147 P63148 P63149 Q32P99
TPG DAA27462

Download simulated HSQC data in one of the following formats:
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SPARKY: Backbone or all simulated shifts