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 10213

Title: Solution structure of the GUCT domain from human ATP-dependent RNA helicase DDX50, DEAD box protein 50   PubMed: 18615715

Authors: Ohnishi, S.; Paakkonen, K.; Guntert, P.; Sato, M.; Koshiba, S.; Harada, T.; Watanabe, S.; Kigawa, T.; Yokoyama, S.

Citation: Ohnishi, Satoshi; Paakkonen, Kimmo; Koshiba, Seizo; Tochio, Naoya; Sato, Manami; Kobayashi, Naohiro; Harada, Takushi; Watanabe, Satoru; Muto, Yutaka; Guntert, Peter; Tanaka, Akiko; Kigawa, Takanori; Yokoyama, Shigeyuki. "Solution structure of the GUCT domain from human RNA helicase II/Gubeta reveals the RRM fold, but implausible RNA interactions."  Proteins 74, 133-144 (2008).

Assembly members:
GUCT domain, polymer, 92 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

Entity Sequences (FASTA):
GUCT domain: GSSGSSGFEPRSLITSDKGF VTMTLESLEEIQDVSCAWKE LNRKLSSNAVSQITRMCLLK GNMGVCFDVPTTESERLQAE WHDSDWILSVPA

Data sets:
Data typeCount
13C chemical shifts387
15N chemical shifts88
1H chemical shifts603

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1GUCT domain1

Entities:

Entity 1, GUCT domain 92 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYPHEGLUPRO
2   ARGSERLEUILETHRSERASPLYSGLYPHE
3   VALTHRMETTHRLEUGLUSERLEUGLUGLU
4   ILEGLNASPVALSERCYSALATRPLYSGLU
5   LEUASNARGLYSLEUSERSERASNALAVAL
6   SERGLNILETHRARGMETCYSLEULEULYS
7   GLYASNMETGLYVALCYSPHEASPVALPRO
8   THRTHRGLUSERGLUARGLEUGLNALAGLU
9   TRPHISASPSERASPTRPILELEUSERVAL
10   PROALA

Samples:

sample_1: GUCT domain, [U-13C; U-15N], 0.9 mM; d-TrisHCl 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 13C-separated NOESYsample_1isotropiccondition_1
3D 15N-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 v0.9816, Kobayashi, N. - data analysis

CYANA v2.1, Guntert, P. - structure solution

OPALp, Koradi, R. - refinement

NMR spectrometers:

  • Bruker AVANCE 800 MHz

Related Database Links:

PDB
DBJ BAG57047 BAG62959
EMBL CAB70733
GB AAH00210 AAH00272 AAH18637 AAK29402 ABM83473
REF NP_001245111 NP_076950 XP_002756344 XP_002820928 XP_003258245
SP Q9BQ39