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 10211

Title: Solution structure of the SH3 domain of human Tyrosine-protein kinase ITK/TSK

Deposition date: 2008-03-18 Original release date: 2009-03-18

Authors: Abe, H.; Miyamoto, K.; Tochio, N.; Sato, M.; Koshiba, S.; Harada, T.; Watanabe, S.; Kigawa, T.; Yokoyama, S.

Citation: Abe, H.; Miyamoto, K.; Tochio, N.; Sato, M.; Koshiba, S.; Harada, T.; Watanabe, S.; Kigawa, T.; Yokoyama, S.. "Solution structure of the SH3 domain of human Tyrosine-protein kinase ITK/TSK"  .

Assembly members:
SH3 domain, polymer, 85 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   Vector: P060821-01

Entity Sequences (FASTA):
SH3 domain: GSSGSSGEDNRRPLWEPEET VVIALYDYQTNDPQELALRR NEEYCLLDSSEIHWWRVQDR NGHEGYVPSSYLVEKSPNNL ETYEW

Data sets:
Data typeCount
13C chemical shifts365
15N chemical shifts86
1H chemical shifts559

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SH3 domain1

Entities:

Entity 1, SH3 domain 85 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYGLUASPASN
2   ARGARGPROLEUTRPGLUPROGLUGLUTHR
3   VALVALILEALALEUTYRASPTYRGLNTHR
4   ASNASPPROGLNGLULEUALALEUARGARG
5   ASNGLUGLUTYRCYSLEULEUASPSERSER
6   GLUILEHISTRPTRPARGVALGLNASPARG
7   ASNGLYHISGLUGLYTYRVALPROSERSER
8   TYRLEUVALGLULYSSERPROASNASNLEU
9   GLUTHRTYRGLUTRP

Samples:

sample_1: SH3 domain, [U-13C; U-15N], 1.20 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:

xwinnmr v3.5, Bruker - collection

NMRPipe v20031121, Delaglio, F - processing

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

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

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

NMR spectrometers:

  • Bruker AVANCE 800 MHz

Related Database Links:

BMRB 18119
PDB
DBJ BAA02873 BAD92859 BAG35699 BAJ20704
GB AAA36748 AAB28072 AAI09078 AAI09079 AAQ02517
REF NP_001253373 NP_005537 XP_001136073 XP_002744141 XP_003268620
SP Q08881
AlphaFold Q08881

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