BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 18677

Title: 1H, 13C and 15N Assignments of the RING domain in ubiquitin ligase gp78   PubMed: 23942235

Deposition date: 2012-08-27 Original release date: 2013-08-26

Authors: Das, Ranabir; Linag, Yuhe; Mariano, Jennifer; Li, Jess; Huang, Tao; King, Aaren; Weissman, Allan; Ji, Xinhua; Byrd, R. Andrew

Citation: Das, Ranabir; Liang, Yu-He; Mariano, Jennifer; Li, Jess; Huang, Tao; King, Aaren; Tarasov, Sergey; Weissman, Allan; Ji, Xinhua; Byrd, R. Andrew. "Allosteric regulation of E2:E3 interactions promote a processive ubiquitination machine."  EMBO J. 32, 2504-2516 (2013).

Assembly members:
gp78RING, polymer, 58 residues, 6473.385 Da.
ZINC ION, non-polymer, 65.409 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):
gp78RING: AVATPEELAVNNDDCAICWD SMQAARKLPCGHLFHNSCLR SWLEQDTSCPTCRMSLNI

Data sets:
Data typeCount
13C chemical shifts232
15N chemical shifts70
1H chemical shifts352

Additional metadata:

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Related Database Links:

PDB 2LXH 2LXP 4LAD
DBJ BAE01277 BAE34049 BAE41974 BAE87377 BAK63135
GB AAD56721 AAD56722 AAH17043 AAH34538 AAH40338
REF NP_001039439 NP_001135 NP_001267243 NP_035917 XP_001091030
SP Q9R049 Q9UKV5
TPG DAA20037

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