BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 11153

Title: Solution structure of the SH3 domain of 130 kDa phosphatidylinositol 4,5-biphosphate-dependent ARF1 GTPase-activating protein

Deposition date: 2010-04-15 Original release date: 2011-05-05

Authors: Abe, H.; Tochio, N.; Miyamoto, K.; Saito, K.; Kigawa, T.; Yokoyama, S.

Citation: Abe, H.; Tochio, N.; Miyamoto, K.; Saito, K.; Kigawa, T.; Yokoyama, S.. "Solution structure of the SH3 domain of 130 kDa phosphatidylinositol 4,5-biphosphate-dependent ARF1 GTPase-activating protein"  .

Assembly members:
SH3 domain, polymer, 76 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' 'E. coli - cell free

Entity Sequences (FASTA):
SH3 domain: GSSGSSGNKVRRVKTIYDCQ ADNDDELTFIEGEVIIVTGE EDQEWWIGHIEGQPERKGVF PVSFVHILSDSGPSSG

Data sets:
Data typeCount
13C chemical shifts296
15N chemical shifts69
1H chemical shifts468

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SH3 domain1

Entities:

Entity 1, SH3 domain 76 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYASNLYSVAL
2   ARGARGVALLYSTHRILETYRASPCYSGLN
3   ALAASPASNASPASPGLULEUTHRPHEILE
4   GLUGLYGLUVALILEILEVALTHRGLYGLU
5   GLUASPGLNGLUTRPTRPILEGLYHISILE
6   GLUGLYGLNPROGLUARGLYSGLYVALPHE
7   PROVALSERPHEVALHISILELEUSERASP
8   SERGLYPROSERSERGLY

Samples:

sample_1: SH3 domain' '[U-13C; U-15N]; natural abundance; natural abundance; natural abundance; natural abundance; .; .

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 v20031121, Delaglio, F. - processing

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

Kujira v0.9747, Kobayashi, N. - data analysis

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

NMR spectrometers:

  • Bruker AVANCE 800 MHz

Related Database Links:

BMRB 11081 11082
PDB
DBJ BAA86563 BAC65759 BAE27250 BAE34783
EMBL CAD97831
GB AAB82338 AAC98349 AAC98350 AAH02201 AAH48818
REF NP_001037710 NP_001234925 NP_001263390 NP_001263391 NP_001263392
SP Q1AAU6 Q9QWY8 Q9ULH1

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts