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 6456

Title: NMR STRUCTURE OF THE SH3 DOMAIN OF HUMAN LYN TYROSINE KINASE   PubMed: 16155203

Deposition date: 2005-01-12 Original release date: 2005-10-17

Authors: Bauer, Finn; Schweimer, Kristian; Hoffmann, Silke; Roesch, Paul; Sticht, Heinrich

Citation: Bauer, Finn; Schweimer, Kristian; Meiselbach, Heike; Hoffmann, Silke; Roesch, Paul; Sticht, Heinrich. "Structural characterization of Lyn-SH3 domain in complex with a herpesviral protein reveals an extended recognition motif that enhances binding affinity"  Protein Sci. 14, 2487-2498 (2005).

Assembly members:
SH3 domain of the Lyn kinase, polymer, 68 residues, Formula weight is not available
Tyrosine kinase interacting protein, polymer, 23 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: recombinant technology

Entity Sequences (FASTA):
SH3 domain of the Lyn kinase: GPLGSPEEQGDIVVALYPYD GIHPDDLSFKKGEKMKVLEE HGEWWKAKSLLTKKEGFIPS NYVAKLNT
Tyrosine kinase interacting protein: TWDPGMPTPPLPPRPANLGE RQA

Data sets:
Data typeCount
1H chemical shifts642
13C chemical shifts321
15N chemical shifts84

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Related Database Links:

PDB 1WA7
EMBL CAC84294 CAC84987 CAC84987 CAC84294
GB AAA72928
PIR A34770 A34770
SP P22575
SWISS-PROT P22575
GenBank AAA72928

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