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 11315

Title: Solution structure of the RING domain of the Non-SMC element 1 protein

Deposition date: 2010-08-10 Original release date: 2011-08-19

Authors: Miyamoto, K.; Sato, M.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.

Citation: Miyamoto, K.; Sato, M.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.. "Solution structure of the RING domain of the Non-SMC element 1 protein"  .

Assembly members:
RING domain, polymer, 74 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: P041101-04

Entity Sequences (FASTA):
RING domain: GSSGSSGRETYPDAVKICNI CHSLLIQGQSCETCGIRMHL PCVAKYFQSNAEPRCPHCND YWPHEIPKSGPSSG

Data sets:
Data typeCount
13C chemical shifts280
15N chemical shifts61
1H chemical shifts428

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 74 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYARGGLUTHR
2   TYRPROASPALAVALLYSILECYSASNILE
3   CYSHISSERLEULEUILEGLNGLYGLNSER
4   CYSGLUTHRCYSGLYILEARGMETHISLEU
5   PROCYSVALALALYSTYRPHEGLNSERASN
6   ALAGLUPROARGCYSPROHISCYSASNASP
7   TYRTRPPROHISGLUILEPROLYSSERGLY
8   PROSERSERGLY

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

1   ZN

Samples:

sample_1: RING domain, [U-13C; U-15N], 1.27 mM; d-Tris-HCl 20 mM; NaCl 100 mM; d-DTT 1 mM; NaN3 0.02%; ZnCl2 0.05 mM; NTA 0.1 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 v2.6, Bruker - collection

NMRPipe v20031121, Delaglio, F. - processing

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

Kujira v0.925, Kobayashi, N. - data analysis

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

NMR spectrometers:

  • Bruker AVANCE 800 MHz

Related Database Links:

PDB
DBJ BAG38039
EMBL CAH91065
GB AAH18938 AIC61504 EAW55754 EAW55756 EAW55757
REF NP_001125616 NP_659547 XP_003807806 XP_003916752 XP_004057436
SP Q5RAZ5 Q8WV22
AlphaFold Q5RAZ5 Q8WV22

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