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 17350

Title: SOLUTION STRUCTURE OF THE R2 DOMAIN OF TALIN

Deposition date: 2010-12-07 Original release date: 2013-02-04

Authors: Goult, Benjamin; Gingras, Alexandre; Bate, Neil; Roberts, Gordon; Barsukov, Igor; Critchley, David

Citation: Goult, Benjamin; Zacharchenko, Tom; Bate, Neil; Tsang, Ricky; Hey, Fiona; Gingras, Alexandre; Elliott, Paul; Roberts, Gordon; Ballestrem, Christoph; Critchley, David; Barsukov, Igor. "RIAM and vinculin binding to talin are mutually exclusive and regulate adhesion assembly and turnover"  J. Biol. Chem. ., .-..

Assembly members:
vbs2a, polymer, 138 residues, Formula weight is not available

Natural source:   Common Name: Mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pet151TOPO

Entity Sequences (FASTA):
vbs2a: GIDPFTIGESDTDPHFQDVL MQLANAVASAAAALVLKAKS VAQRTEDSGLQTQVIAAATQ CALSTSQLVACTKVVAPTIS SPVCQEQLVEAGRLVAKAVE GCVSASQAATEDGQLLRGVG AAATAVTQALNELLQHVK

Data sets:
Data typeCount
13C chemical shifts396
15N chemical shifts131
1H chemical shifts131

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1vbs2a1

Entities:

Entity 1, vbs2a 138 residues - Formula weight is not available

Residues 1-6 (residues 649-654) represent a non-native affinity tag

1   GLYILEASPPROPHETHRILEGLYGLUSER
2   ASPTHRASPPROHISPHEGLNASPVALLEU
3   METGLNLEUALAASNALAVALALASERALA
4   ALAALAALALEUVALLEULYSALALYSSER
5   VALALAGLNARGTHRGLUASPSERGLYLEU
6   GLNTHRGLNVALILEALAALAALATHRGLN
7   CYSALALEUSERTHRSERGLNLEUVALALA
8   CYSTHRLYSVALVALALAPROTHRILESER
9   SERPROVALCYSGLNGLUGLNLEUVALGLU
10   ALAGLYARGLEUVALALALYSALAVALGLU
11   GLYCYSVALSERALASERGLNALAALATHR
12   GLUASPGLYGLNLEULEUARGGLYVALGLY
13   ALAALAALATHRALAVALTHRGLNALALEU
14   ASNGLULEULEUGLNHISVALLYS

Samples:

sample_1: vbs2a, [U-100% 13C; U-100% 15N], 1 ± 0.05 mM; DTT 2 ± 0.05 mM; sodium chloride 50 ± 0.05 mM; sodium phosphate 20 ± 0.05 mM; D2O 10 ± 0.1 %; H2O 90%

sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1

Software:

TOPSPIN v2.1, Bruker Biospin - collection, processing

CCPNAnalysis v1.15, CCPN - chemical shift assignment, data analysis, peak picking

TALOS, Cornilescu, Delaglio and Bax - Dihedral angle prediction

NMR spectrometers:

  • Bruker DRX 600 MHz

Related Database Links:

PDB
DBJ BAA82979 BAC65702 BAE27781 BAG09941
EMBL CAA39588
GB AAD13152 AAF23322 AAF27330 AAH42923 AAI50811
PRF 1617167A
REF NP_001034114 NP_001192357 NP_006280 NP_035732 XP_001084941
SP P26039 Q9Y490
TPG DAA26829

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