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 17070

Title: SOLUTION STRUCTURE OF THE R6 DOMAIN OF TALIN   PubMed: 23389036

Deposition date: 2010-07-22 Original release date: 2013-02-04

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

Citation: Goult, Benjamin; Zacharchenko, Thomas; 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. 288, 8238-8249 (2013).

Assembly members:
talin_domain_C, polymer, 158 residues, 16488.461 Da.

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

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

Entity Sequences (FASTA):
talin_domain_C: GIDPFTQRDVDNALRAVGDA SKRLLSDLLPPSTGTFQEAQ SRLNEAAAGLNQAATELVQA SRGTPQDLARASGRFGQDFS TFLEAGVEMAGQAPSQEDRA QVVSNLKGISMSSSKLLLAA KALSTDPASPNLKSQLAAAA RAVTDSINQLITMCTQQA

Data sets:
Data typeCount
13C chemical shifts484
15N chemical shifts166
1H chemical shifts1040

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1talin_domain_C1

Entities:

Entity 1, talin_domain_C 158 residues - 16488.461 Da.

Residues 1-6 (1200-1205) represent a non-native affinity tag

1   GLYILEASPPROPHETHRGLNARGASPVAL
2   ASPASNALALEUARGALAVALGLYASPALA
3   SERLYSARGLEULEUSERASPLEULEUPRO
4   PROSERTHRGLYTHRPHEGLNGLUALAGLN
5   SERARGLEUASNGLUALAALAALAGLYLEU
6   ASNGLNALAALATHRGLULEUVALGLNALA
7   SERARGGLYTHRPROGLNASPLEUALAARG
8   ALASERGLYARGPHEGLYGLNASPPHESER
9   THRPHELEUGLUALAGLYVALGLUMETALA
10   GLYGLNALAPROSERGLNGLUASPARGALA
11   GLNVALVALSERASNLEULYSGLYILESER
12   METSERSERSERLYSLEULEULEUALAALA
13   LYSALALEUSERTHRASPPROALASERPRO
14   ASNLEULYSSERGLNLEUALAALAALAALA
15   ARGALAVALTHRASPSERILEASNGLNLEU
16   ILETHRMETCYSTHRGLNGLNALA

Samples:

sample_1: talin_domain_C, [U-100% 15N], 1 ± 0.05 mM; D2O, [U-100% 2H], 5 ± 0.05 %; DTT 2 ± 0.01 mM; sodium chloride 50 ± 0.01 mM; TRIS 20 ± 0.01 mM; H2O 90 ± 0.01 %; D2O 5 ± 0.01 %

sample_2: talin_domain_C, [U-100% 13C; U-100% 15N], 1 ± 0.05 mM; D2O, [U-100% 2H], 5 ± 0.05 %; DTT 2 ± 0.01 mM; sodium chloride 50 ± 0.01 mM; TRIS 20 ± 0.01 mM; H2O 90 ± 0.01 %; D2O 5 ± 0.01 %

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
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1

Software:

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

TOPSPIN v2.1, Bruker Biospin - collection, processing

CcpNMR v1.13, CCPN - chemical shift assignment, data analysis, peak picking, refinement

ARIA v1.2, Linge, O'Donoghue and Nilges - geometry optimization, refinement, structure solution

TALOS, Cornilescu, Delaglio and Bax - data analysis, geometry optimization

NMR spectrometers:

  • Bruker DRX 800 MHz
  • Bruker DRX 600 MHz
  • Bruker DRX 600 MHz

Related Database Links:

PDB
DBJ BAA82979 BAC65702 BAE27781 BAG09941
EMBL CAA39588
GB AAD13152 AAF23322 AAF27330 AAH42923 AAI00263
PRF 1617167A
REF NP_001034114 NP_001192357 NP_006280 NP_035732 XP_001084941
SP P26039 Q9Y490
TPG DAA26829
AlphaFold P26039

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