BMRB Entry 10250

Title:
Solution structure of the PH domain of human Docking protein BRDG1
Deposition date:
2008-11-20
Original release date:
2009-11-20
Authors:
Li, H.; Tomizawa, T.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.
Citation:

Citation: Li, H.; Tomizawa, T.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.. "Solution structure of the PH domain of human Docking protein BRDG1"  .

Assembly members:

Assembly members:
PH domain, polymer, 149 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: P040301-57

Data sets:
Data typeCount
13C chemical shifts673
15N chemical shifts143
1H chemical shifts1057

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1PH domain1

Entities:

Entity 1, PH domain 149 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYGLNGLUARG
2   LEULYSILETHRALALEUPROLEUTYRPHE
3   GLUGLYPHELEULEUILELYSARGSERGLY
4   TYRARGGLUTYRGLUHISTYRTRPTHRGLU
5   LEUARGGLYTHRTHRLEUPHEPHETYRTHR
6   ASPLYSLYSSERILEILETYRVALASPLYS
7   LEUASPILEVALASPLEUTHRCYSLEUTHR
8   GLUGLNASNSERTHRGLULYSASNCYSALA
9   LYSPHETHRLEUVALLEUPROLYSGLUGLU
10   VALGLNLEULYSTHRGLUASNTHRGLUSER
11   GLYGLUGLUTRPARGGLYPHEILELEUTHR
12   VALTHRGLULEUSERVALPROGLNASNVAL
13   SERLEULEUPROGLYGLNVALILELYSLEU
14   HISGLUVALLEUGLUARGGLULYSLYSARG
15   ARGILEGLUSERGLYPROSERSERGLY

Samples:

sample_1: PH domain, [U-13C; U-15N], 1.00 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 13C-separated NOESYsample_1isotropiccondition_1
3D 15N-separated NOESYsample_1isotropiccondition_1

Software:

xwinnmr v2.6, Bruker - collection

NMRPipe v20031121, Delaglio, F. - processing

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

Kujira v0.913, Kobayashi, N. - data analysis

CYANA v1.0.7, Guentert, 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