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 11343

Title: Solution structure of the RING domain of the RING finger and CHY zinc finger domain-containing protein 1 from Mus musculus

Authors: Miyamoto, K.; Yoneyama, M.; Koshiba, S.; Watanabe, S.; Harada, T.; Kigawa, T.; Yokoyama, S.

Citation: Miyamoto, K.; Yoneyama, M.; Koshiba, S.; Watanabe, S.; Harada, T.; Kigawa, T.; Yokoyama, S.. "Solution structure of the RING domain of the RING finger and CHY zinc finger domain-containing protein 1 from Mus musculus"  . ., .-..

Assembly members:
RING domain, polymer, 55 residues, Formula weight is not available
ZN, non-polymer, 65.409 Da.

Natural source:   Common Name: house mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

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

Entity Sequences (FASTA):
RING domain: GSSGSSGCPICLEDIHTSRV VAHVLPCGHLLHRTCYEEML KEGYRCPLCSGPSSG

Data sets:
Data typeCount
13C chemical shifts221
15N chemical shifts46
1H chemical shifts336

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 55 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYCYSPROILE
2   CYSLEUGLUASPILEHISTHRSERARGVAL
3   VALALAHISVALLEUPROCYSGLYHISLEU
4   LEUHISARGTHRCYSTYRGLUGLUMETLEU
5   LYSGLUGLYTYRARGCYSPROLEUCYSSER
6   GLYPROSERSERGLY

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

1   ZN

Samples:

sample_1: RING domain, [U-13C; U-15N], 1.13 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: 296 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
REF XP_003479597 XP_006142996 XP_013965461 XP_013965464