BMRB Entry 11303

Title:
An extended conformation of the RWD domain of human Ring finger protein 25
Deposition date:
2010-08-09
Original release date:
2011-08-19
Authors:
Yoneyama, M.; Tochio, N.; Koshiba, S.; Watabe, S.; Harada, T.; Kigawa, T.; Yokoyama, S.
Citation:

Citation: Yoneyama, M.; Tochio, N.; Koshiba, S.; Watabe, S.; Harada, T.; Kigawa, T.; Yokoyama, S.. "An extended conformation of the RWD domain of human Ring finger protein 25"  .

Assembly members:

Assembly members:
RWD domain, polymer, 137 residues, Formula weight is not available

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: P051212-01

Data sets:
Data typeCount
13C chemical shifts567
15N chemical shifts129
1H chemical shifts911

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1RWD domain1

Entities:

Entity 1, RWD domain 137 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYGLUGLUASP
2   TRPVALLEUPROSERGLUVALGLUVALLEU
3   GLUSERILETYRLEUASPGLULEUGLNVAL
4   ILELYSGLYASNGLYARGTHRSERPROTRP
5   GLUILETYRILETHRLEUHISPROALATHR
6   ALAGLUASPGLNASPSERGLNTYRVALCYS
7   PHETHRLEUVALLEUGLNVALPROALAGLU
8   TYRPROHISGLUVALPROGLNILESERILE
9   ARGASNPROARGGLYLEUSERASPGLUGLN
10   ILEHISTHRILELEUGLNVALLEUGLYHIS
11   VALALALYSALAGLYLEUGLYTHRALAMET
12   LEUTYRGLULEUILEGLULYSGLYLYSGLU
13   ILELEUTHRASPASNASNILEPROHISGLY
14   GLNSERGLYPROSERSERGLY

Samples:

sample_1: RWD domain, [U-13C; U-15N], 0.94 mM; d-Tris-HCl 20 mM; NaCl 100 mM; d-DTT 1 mM; NaN3 0.02%; 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 v3.5, Bruker - collection

NMRPipe v20030801, Delaglio, F. - processing

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

Kujira v0.9736, Kobayashi, N. - data analysis

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

NMR spectrometers:

  • Bruker AVANCE 800 MHz

Related Database Links:

PDB
DBJ BAD96245 BAF82190 BAI45678
GB AAH15612 ADZ15417 AIC52126 EAW70645 EHH21677
REF NP_071898 XP_002749840 XP_003818674 XP_003908009 XP_003925575
SP Q96BH1
AlphaFold Q96BH1

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