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 11164

Title: Solution structure of the Zinc finger, C3HC4 type (RING finger) domain of TNF receptor-associated factor 3

Deposition date: 2010-04-15 Original release date: 2011-05-05

Authors: Abe, H.; Miyamoto, K.; Tochio, N.; Yoneyama, M.; Kigawa, T.; Yokoyama, S.

Citation: Abe, H.; Miyamoto, K.; Tochio, N.; Yoneyama, M.; Kigawa, T.; Yokoyama, S.. "Solution structure of the Zinc finger, C3HC4 type (RING finger) domain of TNF receptor-associated factor 3"  .

Assembly members:
RING-type, residues 8-66, polymer, 66 residues, Formula weight is not available
ZN, 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: cell free synthesis   Host organism: E. coli - cell free   Vector: P060515-13

Entity Sequences (FASTA):
RING-type, residues 8-66: GSSGSSGFVKTVEDKYKCEK CHLVLCSPKQTECGHRFCES CMAALLSSSSPKCTACQESI VKDKVF

Data sets:
Data typeCount
13C chemical shifts270
15N chemical shifts59
1H chemical shifts413

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1RING-type, residues 8-661
2ZINC ION no.12
3ZINC ION no.22

Entities:

Entity 1, RING-type, residues 8-66 66 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYPHEVALLYS
2   THRVALGLUASPLYSTYRLYSCYSGLULYS
3   CYSHISLEUVALLEUCYSSERPROLYSGLN
4   THRGLUCYSGLYHISARGPHECYSGLUSER
5   CYSMETALAALALEULEUSERSERSERSER
6   PROLYSCYSTHRALACYSGLNGLUSERILE
7   VALLYSASPLYSVALPHE

Entity 2, ZINC ION no.1 - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: RING-type, residues 8-66, [U-13C; U-15N], 1.10 mM; d-Tris-HCl 20 mM; NaCl 100 mM; d-DTT 1 mM; NaN3 0.02%; ZnCl2 50 uM; IDA 1 mM; H2O 90%; D2O 10%

condition_1: ionic strength: 120 mM; pH: 7.0; pressure: 1 atm; temperature: 296 K

Experiments:

NameSampleSample stateSample conditions
3D 15N-separated NOESYsample_1isotropiccondition_1
3D 13C-separated NOESYsample_1isotropiccondition_1

Software:

xwinnmr v3.5, Bruker - collection

NMRPipe v20031121, Delaglio, F. - processing

NMRView v5.0.4, Johnson, B. A. - data analysis

Kujira v0.9747, Kobayashi, N. - data analysis

CYANA v2.0.17, Guntert, P. - structure solution

NMR spectrometers:

  • Bruker AVANCE 800 MHz

Related Database Links:

PDB
DBJ BAH13910 BAI45792
EMBL CAD62311
GB AAA56753 AAA65732 AAA68195 AAC50112 AAH75086
REF NP_001186356 NP_003291 NP_663777 NP_663778 XP_004055781
SP Q13114
AlphaFold Q13114

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts