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 15129

Title: Solution structure of the first SH3 domain of human Vinexin and its interaction with the peptides from Vinculin   PubMed: 17467669

Deposition date: 2007-02-02 Original release date: 2007-05-21

Authors: Zhang, J.; Yao, B.; Wu, J.; Shi, Y.

Citation: Zhang, J.; Yao, B.; Wu, J.; Shi, Y.. "Solution structure of the first SH3 domain of human Vinexin and its interaction with the vinculin peptides"  Biochem. Biophys. Res. Commun. 357, 931-937 (2007).

Assembly members:
Vinexin, polymer, 65 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   Host organism: Escherichia coli   Vector: PET22b(+)

Entity Sequences (FASTA):
Vinexin: MKAARLKFDFQAQSPKELTL QKGDIVYIHKEVDKNWLEGE HHGRLGIFPANYVEVLPLEH HHHHH

Data sets:
Data typeCount
13C chemical shifts242
15N chemical shifts58
1H chemical shifts410

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SH31

Entities:

Entity 1, SH3 65 residues - Formula weight is not available

1   METLYSALAALAARGLEULYSPHEASPPHE
2   GLNALAGLNSERPROLYSGLULEUTHRLEU
3   GLNLYSGLYASPILEVALTYRILEHISLYS
4   GLUVALASPLYSASNTRPLEUGLUGLYGLU
5   HISHISGLYARGLEUGLYILEPHEPROALA
6   ASNTYRVALGLUVALLEUPROLEUGLUHIS
7   HISHISHISHISHIS

Samples:

sample_1: Vinexin, [U-100% 13C; U-100% 15N], 1.2 mM; phosphate buffer 50 mM; NaCl 50 mM; DTT 1 mM; EDTA 1 mM

sample_conditions_1: pH: 6.2; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D_15N-separated_NOESYsample_1isotropicsample_conditions_1
3D_13C-separated_NOESYsample_1isotropicsample_conditions_1

Software:

NMRPipe v2.2, Delaglio, F. - processing

SPARKY v3, Goddard, T.D., Kneller, D.G. - data analysis

CNSSOLVE v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution

Molmol v2K.2, Koradi - data analysis

NMR spectrometers:

  • Bruker AVANCE 600 MHz

Related Database Links:

BMRB 11242
PDB
REF XP_004332006

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