BMRB Entry 11295

Title:
Solution structure of the RWD domain of human protein C21orf6
Deposition date:
2010-08-09
Original release date:
2011-08-19
Authors:
Yoneyama, M.; Kigawa, T.; Saito, K.; Tochio, N.; Koshiba, S.; Inoue, M.; Yokoyama, S.
Citation:

Citation: Yoneyama, M.; Kigawa, T.; Saito, K.; Tochio, N.; Koshiba, S.; Inoue, M.; Yokoyama, S.. "Solution structure of the RWD domain of human protein C21orf6"  .

Assembly members:

Assembly members:
RWD domain, polymer, 152 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: P050302-87

Data sets:
Data typeCount
13C chemical shifts613
15N chemical shifts147
1H chemical shifts996

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1RWD domain1

Entities:

Entity 1, RWD domain 152 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYGLUGLNALA
2   GLUALAGLNLEUALAGLULEUASPLEULEU
3   ALASERMETPHEPROGLYGLUASNGLULEU
4   ILEVALASNASPGLNLEUALAVALALAGLU
5   LEULYSASPCYSILEGLULYSLYSTHRMET
6   GLUGLYARGSERSERLYSVALTYRPHETHR
7   ILEASNMETASNLEUASPVALSERASPGLU
8   LYSMETALAMETPHESERLEUALACYSILE
9   LEUPROPHELYSTYRPROALAVALLEUPRO
10   GLUILETHRVALARGSERVALLEULEUSER
11   ARGSERGLNGLNTHRGLNLEUASNTHRASP
12   LEUTHRALAPHELEUGLNLYSHISCYSHIS
13   GLYASPVALCYSILELEUASNALATHRGLU
14   TRPVALARGGLUHISALASERGLYTYRVAL
15   SERARGASPTHRSERSERSERGLYPROSER
16   SERGLY

Samples:

sample_1: RWD domain, [U-13C; U-15N], 1.26 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: 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 v20030801, Delaglio, F. - processing

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

Kujira v0.9318, Kobayashi, N. - data analysis

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

NMR spectrometers:

  • Bruker AVANCE 800 MHz

Related Database Links:

PDB
DBJ BAA90913 BAD97077 BAK64033
EMBL CAB88085 CAB90431
GB AAH12546 AAH17912 AAK14918 ADQ32121 AIC50494
REF NP_001267094 NP_058636 XP_003813235 XP_003927746 XP_004062697
SP P57060
AlphaFold P57060

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