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 11219

Title: Solution structure of the first SH3 domain of human sorbin and Sh3 domain-containing protein 1

Deposition date: 2010-07-22 Original release date: 2011-07-21

Authors: Qin, X.; Nagashima, T.; Hayashi, F.; Yokoyama, S.

Citation: Qin, X.; Nagashima, T.; Hayashi, F.; Yokoyama, S.. "Solution structure of the first SH3 domain of human sorbin and Sh3 domain-containing protein 1"  . ., .-..

Assembly members:
SH3 domain, polymer, 68 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   Host organism: E. coli - cell free

Entity Sequences (FASTA):
SH3 domain: GSSGSSGRPARAKFDFKAQT LKELPLQKGDIVYIYKQIDQ NWYEGEHHGRVGIFPRTYIE LLSGPSSG

Data sets:
Data typeCount
13C chemical shifts295
15N chemical shifts63
1H chemical shifts457

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Sorbin and SH3 domain-containing protein 11

Entities:

Entity 1, Sorbin and SH3 domain-containing protein 1 68 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYARGPROALA
2   ARGALALYSPHEASPPHELYSALAGLNTHR
3   LEULYSGLULEUPROLEUGLNLYSGLYASP
4   ILEVALTYRILETYRLYSGLNILEASPGLN
5   ASNTRPTYRGLUGLYGLUHISHISGLYARG
6   VALGLYILEPHEPROARGTHRTYRILEGLU
7   LEULEUSERGLYPROSERSERGLY

Samples:

sample_1: SH3 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: 298 K

Experiments:

NameSampleSample stateSample conditions
3D 15N-separated NOESYsample_1isotropiccondition_1
3D 13C-separated NOESYsample_1isotropiccondition_1

Software:

VNMR v6.1C, Varian - collection

NMRPipe v20031121, Delaglio, F. - processing

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

Kujira v0.9296, Kobayashi N. - data analysis

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

NMR spectrometers:

  • Varian INOVA 800 MHz
  • Varian INOVA 900 MHz

Related Database Links:

PDB
GB KFP25985 KFV06230 KFZ48496

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