BMRB Entry 11336

Title:
Solution Structure of the RING domain of the human ring finger protein 4
Deposition date:
2010-08-10
Original release date:
2011-08-19
Authors:
Miyamoto, K.; Yoneyama, M.; Tomizawa, T.; Koshiba, S.; Watanabe, S.; Harada, T.; Kigawa, T.; Yokoyama, S.
Citation:

Citation: Miyamoto, K.; Yoneyama, M.; Tomizawa, T.; Koshiba, S.; Watanabe, S.; Harada, T.; Kigawa, T.; Yokoyama, S.. "Solution Structure of the RING domain of the human ring finger protein 4"  .

Assembly members:

Assembly members:
RING domain, polymer, 69 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: P060327-06

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts265
15N chemical shifts63
1H chemical shifts418

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 69 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYTHRGLYLEU
2   ARGPROSERGLYTHRVALSERCYSPROILE
3   CYSMETASPGLYTYRSERGLUILEVALGLN
4   ASNGLYARGLEUILEVALSERTHRGLUCYS
5   GLYHISVALPHECYSSERGLNCYSLEUARG
6   ASPSERLEULYSASNALAASNTHRCYSPRO
7   THRCYSARGLYSLYSILEASNHISLYS

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

1   ZN

Samples:

sample_1: RING domain, [U-13C; U-15N], 1.03 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 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 v0.9820, Kobayashi, N. - data analysis

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

NMR spectrometers:

  • Bruker AVANCE 800 MHz

Related Database Links:

PDB
DBJ BAA19122 BAG35433 BAG54620 BAG73691
GB AAC35248 AAC52022 AAH31935 AAH62024 AAL06715
REF NP_001171938 NP_002929 NP_062055 XP_003890937 XP_004038387
SP O88846 P78317
AlphaFold P78317 O88846

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