BMRB Entry 19139

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR19139

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Title:
Backbone chemical shift assignments of the talin rod domain, R7 (residues 1357-1653 (delta1454-1586))
Deposition date:
2013-04-03
Original release date:
2018-06-05
Authors:
Goult, Benjamin; Bate, Neil; Gingras, Alexandre; Barsukov, Igor; Critchley, David
Citation:

Citation: Bouchet, Benjamin; Gough, Rosemarie; Ammon, York-Christoph; van de Willige, Dieudonnee; Post, Harm; Jacquemet, Guillaume; Altelaar, Af Maarten; Heck, Albert Jr; Goult, Benjamin; Akhmanova, Anna. "Talin-KANK1 interaction controls the recruitment of cortical microtubule stabilizing complexes to focal adhesions"  Elife 5, e18124-e18124 (2016).
PubMed: 27410476

Assembly members:

Assembly members:
R7, polymer, 180 residues, 18971 Da.

Natural source:

Natural source:   Common Name: House 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: pet151-TOPO

Entity Sequences (FASTA):

Entity Sequences (FASTA):
R7: GIDPFTGSAPGQKECDNALR QLETVRELLENPVQPINDMS YFGCLDSVMENSKVLGEAMT GISQNAKNGNLPEFGDAIAT ASKALCGFTEAAAQAAYLVG VSDPNVDQISPEGRAAMEPI VISAKTMLESAGGLIQTARA LAVNPRDPPRWSVLAGHSRT VSDSIKKLITSMRDKAPGQL

Data sets:
Data typeCount
13C chemical shifts504
15N chemical shifts165
1H chemical shifts165

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1R71

Entities:

Entity 1, R7 180 residues - 18971 Da.

Residues 1349-1356 represent a non-native affinity tag. Residues 1454-1584 inclusive deleted from construct.

1   GLYILEASPPROPHETHRGLYSERALAPRO
2   GLYGLNLYSGLUCYSASPASNALALEUARG
3   GLNLEUGLUTHRVALARGGLULEULEUGLU
4   ASNPROVALGLNPROILEASNASPMETSER
5   TYRPHEGLYCYSLEUASPSERVALMETGLU
6   ASNSERLYSVALLEUGLYGLUALAMETTHR
7   GLYILESERGLNASNALALYSASNGLYASN
8   LEUPROGLUPHEGLYASPALAILEALATHR
9   ALASERLYSALALEUCYSGLYPHETHRGLU
10   ALAALAALAGLNALAALATYRLEUVALGLY
11   VALSERASPPROASNVALASPGLNILESER
12   PROGLUGLYARGALAALAMETGLUPROILE
13   VALILESERALALYSTHRMETLEUGLUSER
14   ALAGLYGLYLEUILEGLNTHRALAARGALA
15   LEUALAVALASNPROARGASPPROPROARG
16   TRPSERVALLEUALAGLYHISSERARGTHR
17   VALSERASPSERILELYSLYSLEUILETHR
18   SERMETARGASPLYSALAPROGLYGLNLEU

Samples:

sample_1: R7, [U-100% 13C; U-100% 15N], 0.8 ± 0.05 mM; D2O, [U-100% 2H], 10 ± 0.1 %; sodium chloride 50 ± 0.05 mM; sodium phosphate 20 ± 0.05 mM; DTT 2 ± 0.05 mM; H2O 90 ± 0.1 %

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

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1

Software:

TOPSPIN v3.1 - 1

NMR spectrometers:

  • Bruker DRX 600 MHz

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