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 19423

Title: Solution structure of the Vav1 SH2 domain complexed with a Syk-derived singly phosphorylated peptide   PubMed: 23955592

Deposition date: 2013-08-13 Original release date: 2013-08-26

Authors: Chen, Chih-Hong; Piraner, Dan; Gorenstein, Nina; Geahlen, Robert; Post, Carol

Citation: Chen, Chih-Hong; Piraner, Dan; Gorenstein, Nina; Geahlen, Robert; Beth Post, Carol. "Differential recognition of syk-binding sites by each of the two phosphotyrosine-binding pockets of the Vav SH2 domain."  Biopolymers 99, 897-907 (2013).

Assembly members:
entity_1, polymer, 106 residues, 12335.253 Da.
entity_2, polymer, 13 residues, 1594.495 Da.
O-PHOSPHOTYROSINE, non-polymer, 261.168 Da.

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
entity_1: HMQDLSVHLWYAGPMERAGA ESILANRSDGTFLVRQRVKD AAEFAISIKYNVEVKHIKIM TAEGLYRITEKKAFRGLTEL VEFYQQNSLKDCFKSLDTTL QFPFKE
entity_2: DTEVYESPXADPE

Data sets:
Data typeCount
13C chemical shifts315
15N chemical shifts92
1H chemical shifts681

Additional metadata:

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

BMRB 17632
PDB 2CRH 2LCT 2MC1 2ROR
DBJ BAG36112 BAG62721 BAJ21026
EMBL CAA34383 CAA58783
GB AAC25011 AAH13361 AAI23647 AIC59346 EAW69057
REF NP_001071542 NP_001245135 NP_001245136 NP_001254762 NP_005419
SP P15498 Q08DN7
TPG DAA27902

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