BMRB Entry 18313

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR18313
MolProbity Validation Chart

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Title:
Solution Structure of the A domain of talin
Deposition date:
2012-03-06
Original release date:
2013-02-11
Authors:
Goult, Ben; Gingras, Alex; Bate, Neil; Roberts, Gordon; Barsukov, Igor; Critchley, David
Citation:

Citation: Goult, Ben; Bate, Neil; Gingras, Alex; Roberts, Gordon; Barsukov, Igor; Critchley, David. "RIAM and vinculin binding to talin are mutually exclusive and regulate adhesion assembly and turnover"  J. Biol. Chem. ., .-..

Assembly members:

Assembly members:
Domain_A, polymer, 138 residues, 13915.918 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET151TOPO

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Domain_A: GIDPFTLVQRLEHAAKQAAA SATQTIAAAQHAASAPKASA GPQPLLVQSCKAVAEQIPLL VQGVRGSQAQPDSPSAQLAL IAASQSFLQPGGKMVAAAKA SVPTIQDQASAMQLSQCAKN LGTALAELRTAAQKAQEA

Data sets:
Data typeCount
13C chemical shifts552
15N chemical shifts145
1H chemical shifts934

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1A domain of talin1

Entities:

Entity 1, A domain of talin 138 residues - 13915.918 Da.

Residues 1-6 represent a non-native affinity tag

1   GLYILEASPPROPHETHRLEUVALGLNARG
2   LEUGLUHISALAALALYSGLNALAALAALA
3   SERALATHRGLNTHRILEALAALAALAGLN
4   HISALAALASERALAPROLYSALASERALA
5   GLYPROGLNPROLEULEUVALGLNSERCYS
6   LYSALAVALALAGLUGLNILEPROLEULEU
7   VALGLNGLYVALARGGLYSERGLNALAGLN
8   PROASPSERPROSERALAGLNLEUALALEU
9   ILEALAALASERGLNSERPHELEUGLNPRO
10   GLYGLYLYSMETVALALAALAALALYSALA
11   SERVALPROTHRILEGLNASPGLNALASER
12   ALAMETGLNLEUSERGLNCYSALALYSASN
13   LEUGLYTHRALALEUALAGLULEUARGTHR
14   ALAALAGLNLYSALAGLNGLUALA

Samples:

15N: Domain A, [U-100% 15N], 0.8 ± 0.05 mM; D2O, [U-100% 2H], 10 ± 0.05 %; sodium chloride 50 ± 0.05 mM; sodium phosphate 20 ± 0.05 mM; DTT 2 ± 0.05 mM

double: Domain A, [U-100% 13C; U-100% 15N], 0.8 ± 0.05 mM; D2O, [U-100% 2H], 10 ± 0.05 %; sodium chloride 50 ± 0.05 mM; sodium phosphate 20 ± 0.05 mM; DTT 2 ± 0.05 mM

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

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQC15Nisotropicsample_conditions_1
2D 1H-13C HSQCdoubleisotropicsample_conditions_1
3D 1H-15N NOESY15Nisotropicsample_conditions_1
3D 1H-13C NOESYdoubleisotropicsample_conditions_1
3D CBCA(CO)NHdoubleisotropicsample_conditions_1
3D HNCOdoubleisotropicsample_conditions_1
3D HNCAdoubleisotropicsample_conditions_1
3D HCCH-TOCSYdoubleisotropicsample_conditions_1
3D HNCACBdoubleisotropicsample_conditions_1
3D HN(CO)CAdoubleisotropicsample_conditions_1

Software:

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

Analysis v2.1.5, CCPN - chemical shift assignment, data analysis, peak picking, refinement

TOPSPIN v2.1, Bruker Biospin - collection, processing

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

NMR spectrometers:

  • Bruker DMX 600 MHz
  • Bruker ARX 800 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 Q9Y490

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