BMRB Entry 11338

Title:
Solution structure of the RWD domain of human RWD domain containing protein 1
Deposition date:
2010-08-10
Original release date:
2011-08-19
Authors:
Yoneyama, M.; Tomizawa, T.; Koshiba, S.; Watabe, S.; Harada, T.; Kigawa, T.; Yokoyama, S.
Citation:

Citation: Yoneyama, M.; Tomizawa, T.; Koshiba, S.; Watabe, S.; Harada, T.; Kigawa, T.; Yokoyama, S.. "Solution structure of the RWD domain of human RWD domain containing protein 1"  .

Assembly members:

Assembly members:
RWD domain, polymer, 128 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: P060522-12

Data sets:
Data typeCount
13C chemical shifts552
15N chemical shifts130
1H chemical shifts878

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1RWD domain1

Entities:

Entity 1, RWD domain 128 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYMETTHRASP
2   TYRGLYGLUGLUGLNARGASNGLULEUGLU
3   ALALEUGLUSERILETYRPROASPSERPHE
4   THRVALLEUSERGLUASNPROPROSERPHE
5   THRILETHRVALTHRSERGLUALAGLYGLU
6   ASNASPGLUTHRVALGLNTHRTHRLEULYS
7   PHETHRTYRSERGLULYSTYRPROASPGLU
8   ALAPROLEUTYRGLUILEPHESERGLNGLU
9   ASNLEUGLUASPASNASPVALSERASPILE
10   LEULYSLEULEUALALEUGLNALAGLUGLU
11   ASNLEUGLYMETVALMETILEPHETHRLEU
12   VALTHRALAVALGLNGLULYSLEUASNGLU
13   ILEVALASPGLNILELYSTHRARG

Samples:

sample_1: RWD domain, [U-13C; U-15N], 1.19 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 v0.9820, Kobayashi, N. - data analysis

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

NMR spectrometers:

  • Bruker AVANCE 800 MHz

Related Database Links:

PDB
DBJ BAB23927 BAB27511 BAB28287 BAF83416 BAI46567
EMBL CAC24710
GB AAD27733 AAD40376 AAH15802 AAH62136 AAI02911
REF NP_001029898 NP_001253784 NP_001296170 NP_057036 NP_079890
SP Q99ND9 Q9CQK7 Q9H446
TPG DAA26307
AlphaFold Q9H446 Q99ND9 Q9CQK7

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