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 10245

Title: Solution structures of the SH3 domain of human megakaryocyte-associated tyrosine-protein kinase.

Deposition date: 2008-10-24 Original release date: 2009-11-03

Authors: Sato, M.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.

Citation: Sato, M.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.. "Solution structures of the SH3 domain of human megakaryocyte-associated tyrosine-protein kinase."  . ., .-..

Assembly members:
SH3 domain, polymer, 81 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

Entity Sequences (FASTA):
SH3 domain: GSSGSSGRMPTRRWAPGTQC ITKCEHTRPKPGELAFRKGD VVTILEACENKSWYRVKHHT SGQEGLLAAGALRERSGPSS G

Data sets:
Data typeCount
13C chemical shifts313
15N chemical shifts69
1H chemical shifts488

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SH3 domain1

Entities:

Entity 1, SH3 domain 81 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYARGMETPRO
2   THRARGARGTRPALAPROGLYTHRGLNCYS
3   ILETHRLYSCYSGLUHISTHRARGPROLYS
4   PROGLYGLULEUALAPHEARGLYSGLYASP
5   VALVALTHRILELEUGLUALACYSGLUASN
6   LYSSERTRPTYRARGVALLYSHISHISTHR
7   SERGLYGLNGLUGLYLEULEUALAALAGLY
8   ALALEUARGGLUARGSERGLYPROSERSER
9   GLY

Samples:

sample_1: SH3 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: 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 v0.9295, Kobayashi, N. - data analysis

CYANA v1.0.7, Guntert, P. - refinement, structure solution

NMR spectrometers:

  • Bruker AVANCE 800 MHz

Related Database Links:

PDB
GB AAA16703

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