BMRB Entry 6456
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR6456
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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
- assigned_chemical_shifts
Data type | Count |
1H chemical shifts | 642 |
13C chemical shifts | 321 |
15N chemical shifts | 84 |
Additional metadata:
Related Database Links:
PDB | 1WA7 |
EMBL | CAC84294 CAC84987 CAC84987 CAC84294 |
GB | AAA72928 |
PIR | A34770 A34770 |
SP | P22575 |
SWISS-PROT | P22575 |
GenBank | AAA72928 |
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