BMRB Entry 10313

Title:
Solution structure of the PH domain of PIP2-dependent ARF1 GTPase-activating protein from human
Deposition date:
2009-03-11
Original release date:
2010-03-11
Authors:
Li, H.; Tomizawa, T.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.; RIKEN, Structural
Citation:

Citation: Li, H.; Tomizawa, T.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.. "Solution structure of the PH domain of PIP2-dependent ARF1 GTPase-activating protein from human"  .

Assembly members:

Assembly members:
PH domain, polymer, 114 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: P050801-06

Data sets:
Data typeCount
13C chemical shifts477
15N chemical shifts111
1H chemical shifts749

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1PH domain1

Entities:

Entity 1, PH domain 114 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYTYRGLYSER
2   GLULYSLYSGLYTYRLEULEULYSLYSSER
3   ASPGLYILEARGLYSVALTRPGLNARGARG
4   LYSCYSSERVALLYSASNGLYILELEUTHR
5   ILESERHISALATHRSERASNARGGLNPRO
6   ALALYSLEUASNLEULEUTHRCYSGLNVAL
7   LYSPROASNALAGLUASPLYSLYSSERPHE
8   ASPLEUILESERHISASNARGTHRTYRHIS
9   PHEGLNALAGLUASPGLUGLNASPTYRVAL
10   ALATRPILESERVALLEUTHRASNSERLYS
11   GLUGLUALALEUTHRMETALAPHESERGLY
12   PROSERSERGLY

Samples:

sample_1: PH domain, [U-13C; U-15N], 1.18 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 v0.932, Kobayashi, N. - data analysis

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

NMR spectrometers:

  • Bruker AVANCE 800 MHz

Related Database Links:

PDB

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