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 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: 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:
RWD domain, polymer, 128 residues, Formula weight is not available

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

Entity Sequences (FASTA):
RWD domain: GSSGSSGMTDYGEEQRNELE ALESIYPDSFTVLSENPPSF TITVTSEAGENDETVQTTLK FTYSEKYPDEAPLYEIFSQE NLEDNDVSDILKLLALQAEE NLGMVMIFTLVTAVQEKLNE IVDQIKTR

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

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