BMRB Entry 11341

Title:
Solution structure of the RING domain of the human tripartite motif-containing protein 39
Deposition date:
2010-08-10
Original release date:
2011-08-19
Authors:
Miyamoto, K.; Sato, M.; Koshiba, S.; Watanabe, S.; Harada, T.; Kigawa, T.; Yokoyama, S.
Citation:

Citation: Miyamoto, K.; Sato, M.; Koshiba, S.; Watanabe, S.; Harada, T.; Kigawa, T.; Yokoyama, S.. "Solution structure of the RING domain of the human tripartite motif-containing protein 39"  .

Assembly members:

Assembly members:
RING domain, polymer, 58 residues, Formula weight is not available
ZN, non-polymer, 65.409 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: cell free synthesis   Host organism: E. coli - cell free   Vector: P060828-17

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts234
15N chemical shifts53
1H chemical shifts365

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1RING domain1
2ZINC ION no.12
3ZINC ION no.22

Entities:

Entity 1, RING domain 58 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYALALEUGLU
2   ASNLEUGLNVALGLUALASERCYSSERVAL
3   CYSLEUGLUTYRLEULYSGLUPROVALILE
4   ILEGLUCYSGLYHISASNPHECYSLYSALA
5   CYSILETHRARGTRPTRPGLUASPLEUGLU
6   ARGASPPHEPROCYSPROVALCYS

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

1   ZN

Samples:

sample_1: RING domain, [U-13C; U-15N], 1.06 mM; d-Tris-HCl 20 mM; NaCl 100 mM; d-DTT 1 mM; NaN3 0.02%; ZnCl2 0.05 mM; IDA 1.0 mM; H2O 90%; D2O 10%

condition_1: ionic strength: 120 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D 13C-separated NOESYsample_1isotropiccondition_1
3D 15N-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 v0.9820, Kobayashi, N. - data analysis

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

NMR spectrometers:

  • Bruker AVANCE 800 MHz

Related Database Links:

PDB
DBJ BAB16374 BAB16375 BAC35409 BAD13703 BAD13704
EMBL CAE84052 CAH90337
GB AAH07661 AAH31540 AAH34985 AAP36034 AAP36295
REF NP_001065263 NP_001121951 NP_001125160 NP_001186048 NP_067076
SP Q1XHU0 Q6MFZ5 Q9ESN2 Q9HCM9
AlphaFold Q1XHU0 Q6MFZ5 Q9ESN2 Q9HCM9

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