BMRB Entry 10273

Title:
Solution structures of the TGS domain of human developmentally-regulated GTP-binding protein 1
Deposition date:
2008-12-15
Original release date:
2009-12-14
Authors:
Sato, M.; Koshiba, S.; Watanabe, S.; Harada, T.; Kigawa, T.; Yokoyama, S.
Citation:

Citation: Sato, M.; Koshiba, S.; Watanabe, S.; Harada, T.; Kigawa, T.; Yokoyama, S.. "Solution structures of the TGS domain of human developmentally-regulated GTP-binding protein 1"  .

Assembly members:

Assembly members:
TGS domain, polymer, 93 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   Vector: P051011-16

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts406
15N chemical shifts81
1H chemical shifts634

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1TGS domain1

Entities:

Entity 1, TGS domain 93 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYTYRLEULYS
2   LEUVALARGILETYRTHRLYSPROLYSGLY
3   GLNLEUPROASPTYRTHRSERPROVALVAL
4   LEUPROTYRSERARGTHRTHRVALGLUASP
5   PHECYSMETLYSILEHISLYSASNLEUILE
6   LYSGLUPHELYSTYRALALEUVALTRPGLY
7   LEUSERVALLYSHISASNPROGLNLYSVAL
8   GLYLYSASPHISTHRLEUGLUASPGLUASP
9   VALILEGLNILEVALLYSLYSSERGLYPRO
10   SERSERGLY

Samples:

sample_1: TGS domain, [U-13C; U-15N], 1 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 13C-separated NOESYsample_1isotropiccondition_1
3D 15N-separated NOESYsample_1isotropiccondition_1

Software:

xwinnmr v3.5, Bruker - collection

NMRPipe v20031121, Delaglio, F. - processing

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

Kujira v0.9827, Kobayashi, N. - data analysis

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

NMR spectrometers:

  • Bruker AVANCE 700 MHz

Related Database Links:

PDB
DBJ BAA01555 BAC38030 BAE25890 BAE33021 BAG38025
EMBL CAA06775 CAB61403 CAG30374 CAG46856 CAK54479
GB AAD12240 AAH19285 AAH20803 AAH39649 AAH88410
REF NP_001009685 NP_001029863 NP_001162241 NP_001164823 NP_001253866
SP P32233 Q3MHP5 Q9Y295
TPG DAA20497 DAA22636
AlphaFold Q3MHP5 P32233 Q9Y295

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