BMRB Entry 19339

Title:
Backbone assignment of the R8 domain of talin.
Deposition date:
2013-07-05
Original release date:
2018-09-19
Authors:
Goult, Ben; Zacharchenko, Thomas; Bate, Neil; Critchley, David; Barsukov, Igor
Citation:

Citation: Zacharchenko, Thomas; Qian, Xiaolan; Goult, Benjamin; Jethwa, Devina; Almeida, Teresa; Ballestrem, Christoph; Critchley, David; Lowy, Douglas; Barsukov, Igor. "LD Motif Recognition by Talin: Structure of the Talin-DLC1 Complex."  Structure 24, 1130-1141 (2016).
PubMed: 27265849

Assembly members:

Assembly members:
R8, polymer, 133 residues, 13970.6 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

Data sets:
Data typeCount
13C chemical shifts392
15N chemical shifts125
1H chemical shifts125

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1R81

Entities:

Entity 1, R8 133 residues - 13970.6 Da.

Residues 1-6 (1452-1457) represent a non-native affinity tag

1   GLYILEASPPROPHETHRGLNGLNGLYLEU
2   VALGLUPROTHRGLNPHEALAARGALAASN
3   GLNALAILEGLNMETALACYSGLNSERLEU
4   GLYGLUPROGLYCYSTHRGLNALAGLNVAL
5   LEUSERALAALATHRILEVALALALYSHIS
6   THRSERALALEUCYSASNSERCYSARGLEU
7   ALASERALAARGTHRALAASNPROTHRALA
8   LYSARGGLNPHEVALGLNSERALALYSGLU
9   VALALAASNSERTHRALAASNLEUVALLYS
10   THRILELYSALALEUASPGLYASPPHETHR
11   GLUGLUASNARGALAGLNCYSARGALAALA
12   THRALAPROLEULEUGLUALAVALASPASN
13   LEUSERALAPHEALASERASNPROGLUPHE
14   SERSERVAL

Samples:

sample_1: talin R8, [U-100% 13C; U-100% 15N], 0.8 ± 0.05 mM; DTT 2 ± 0.05 mM; sodium phosphate 20 ± 0.05 mM; sodium chloride 50 ± 0.05 mM; H2O 90%; D2O 10%

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 HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACOsample_1isotropicsample_conditions_1

Software:

TOPSPIN v3.2, Bruker Biospin - collection, processing

Analysis v2.2.2, CCPN - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Bruker DRX 800 MHz

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