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 17555

Title: Chemical shift assignments of the VBS1 domain of talin   PubMed: 22351767

Deposition date: 2011-03-30 Original release date: 2012-05-10

Authors: Goult, Ben; Gingras, Alex; Bate, Neil; Banno, Asoka; Ginsberg, Mark; Roberts, Gordon; Barsukov, Igor; Critchley, David

Citation: Banno, Asoka; Goult, Benjamin; Lee, Hosup; Bate, Neil; Critchley, David; Ginsberg, Mark. "Subcellular Localization of Talin Is Regulated by Inter-domain Interactions."  J. Biol. Chem. 287, 13799-13812 (2012).

Assembly members:
vbs1, polymer, 180 residues, Formula weight is not available

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

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pet151

Entity Sequences (FASTA):
vbs1: GIDPFTRGHMPPLTSAQQAL TGTINSSMQAVQAAQATLDD FETLPPLGQDAASKAWRKNK MDESKHEIHSQVDAITAGTA SVVNLTAGDPAETDYTAVGC AVTTISSNLTEMSRGVKLLA ALLEDEGGNGRPLLQAAKGL AGAVSELLRSAQPASAEPRQ NLLQAAGNVGQASGELLQQI

Data sets:
Data typeCount
13C chemical shifts324
15N chemical shifts163
1H chemical shifts162

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1vbs11

Entities:

Entity 1, vbs1 180 residues - Formula weight is not available

Residues 1-6 represent a non-native affinity tag

1   GLYILEASPPROPHETHRARGGLYHISMET
2   PROPROLEUTHRSERALAGLNGLNALALEU
3   THRGLYTHRILEASNSERSERMETGLNALA
4   VALGLNALAALAGLNALATHRLEUASPASP
5   PHEGLUTHRLEUPROPROLEUGLYGLNASP
6   ALAALASERLYSALATRPARGLYSASNLYS
7   METASPGLUSERLYSHISGLUILEHISSER
8   GLNVALASPALAILETHRALAGLYTHRALA
9   SERVALVALASNLEUTHRALAGLYASPPRO
10   ALAGLUTHRASPTYRTHRALAVALGLYCYS
11   ALAVALTHRTHRILESERSERASNLEUTHR
12   GLUMETSERARGGLYVALLYSLEULEUALA
13   ALALEULEUGLUASPGLUGLYGLYASNGLY
14   ARGPROLEULEUGLNALAALALYSGLYLEU
15   ALAGLYALAVALSERGLULEULEUARGSER
16   ALAGLNPROALASERALAGLUPROARGGLN
17   ASNLEULEUGLNALAALAGLYASNVALGLY
18   GLNALASERGLYGLULEULEUGLNGLNILE

Samples:

sample_1: vbs1, [U-100% 13C; U-100% 15N], 0.8 ± 0.05 mM; D2O, [U-100% 2H], 10 ± 0.1 %; DTT 2 ± 0.01 mM; sodium phosphate 20 ± 0.1 mM; sodium chloride 50 ± 0.1 mM; H2O 90 ± 0.1 %

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 CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1

Software:

TOPSPIN v2.1, Bruker Biospin - collection, processing

CCPNAnalysis v1.5, CCPN - chemical shift assignment, peak picking, processing

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