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 11326

Title: Solution structure of the RING domain of the human RING finger protein 146

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

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

Citation: Miyamoto, K.; Kigawa, T.; Sato, M.; Koshiba, S.; Inoue, M.; Yokoyama, S.. "Solution structure of the RING domain of the human RING finger protein 146"  .

Assembly members:
RING domain, polymer, 71 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: P050302-12

Entity Sequences (FASTA):
RING domain: GSSGSSGNTAPSLTVPECAI CLQTCVHPVSLPCKHVFCYL CVKGASWLGKRCALCRQEIP EDFLDSGPSSG

Data sets:
Data typeCount
13C chemical shifts266
15N chemical shifts56
1H chemical shifts422

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 71 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYASNTHRALA
2   PROSERLEUTHRVALPROGLUCYSALAILE
3   CYSLEUGLNTHRCYSVALHISPROVALSER
4   LEUPROCYSLYSHISVALPHECYSTYRLEU
5   CYSVALLYSGLYALASERTRPLEUGLYLYS
6   ARGCYSALALEUCYSARGGLNGLUILEPRO
7   GLUASPPHELEUASPSERGLYPROSERSER
8   GLY

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

1   ZN

Samples:

sample_1: RING domain, [U-13C; U-15N], 1.34 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 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 v0.9321, Kobayashi, N. - data analysis

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

NMR spectrometers:

  • Bruker AVANCE 800 MHz

Related Database Links:

PDB
DBJ BAB28015 BAB55108 BAB55196 BAB55359 BAE31549
EMBL CAB66763 CAC85986 CAG38545 CAH89794 CAH90287
GB AAH08235 AAH50795 AAH83675 AAI02140 AIC52443
REF NP_001012060 NP_001070448 NP_001103666 NP_001103667 NP_001103668
SP E1B7X3 Q2PFU6 Q3T139 Q5REL3 Q5XIK5
TPG DAA20901 DAA26356
AlphaFold Q5XIK5 E1B7X3 Q2PFU6 Q3T139 Q5REL3

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