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)) PubMed: 27410476
Deposition date: 2013-04-03 Original release date: 2018-06-05
Authors: Goult, Benjamin; Bate, Neil; Gingras, Alexandre; Barsukov, Igor; Critchley, David
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).
Assembly members:
R7, polymer, 180 residues, 18971 Da.
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-TOPO
Entity Sequences (FASTA):
R7: GIDPFTGSAPGQKECDNALR
QLETVRELLENPVQPINDMS
YFGCLDSVMENSKVLGEAMT
GISQNAKNGNLPEFGDAIAT
ASKALCGFTEAAAQAAYLVG
VSDPNVDQISPEGRAAMEPI
VISAKTMLESAGGLIQTARA
LAVNPRDPPRWSVLAGHSRT
VSDSIKKLITSMRDKAPGQL
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 504 |
15N chemical shifts | 165 |
1H chemical shifts | 165 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | R7 | 1 |
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 | GLY | ILE | ASP | PRO | PHE | THR | GLY | SER | ALA | PRO | |
2 | GLY | GLN | LYS | GLU | CYS | ASP | ASN | ALA | LEU | ARG | |
3 | GLN | LEU | GLU | THR | VAL | ARG | GLU | LEU | LEU | GLU | |
4 | ASN | PRO | VAL | GLN | PRO | ILE | ASN | ASP | MET | SER | |
5 | TYR | PHE | GLY | CYS | LEU | ASP | SER | VAL | MET | GLU | |
6 | ASN | SER | LYS | VAL | LEU | GLY | GLU | ALA | MET | THR | |
7 | GLY | ILE | SER | GLN | ASN | ALA | LYS | ASN | GLY | ASN | |
8 | LEU | PRO | GLU | PHE | GLY | ASP | ALA | ILE | ALA | THR | |
9 | ALA | SER | LYS | ALA | LEU | CYS | GLY | PHE | THR | GLU | |
10 | ALA | ALA | ALA | GLN | ALA | ALA | TYR | LEU | VAL | GLY | |
11 | VAL | SER | ASP | PRO | ASN | VAL | ASP | GLN | ILE | SER | |
12 | PRO | GLU | GLY | ARG | ALA | ALA | MET | GLU | PRO | ILE | |
13 | VAL | ILE | SER | ALA | LYS | THR | MET | LEU | GLU | SER | |
14 | ALA | GLY | GLY | LEU | ILE | GLN | THR | ALA | ARG | ALA | |
15 | LEU | ALA | VAL | ASN | PRO | ARG | ASP | PRO | PRO | ARG | |
16 | TRP | SER | VAL | LEU | ALA | GLY | HIS | SER | ARG | THR | |
17 | VAL | SER | ASP | SER | ILE | LYS | LYS | LEU | ILE | THR | |
18 | SER | MET | ARG | ASP | LYS | ALA | PRO | GLY | GLN | LEU |
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:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
3D HNCA | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
3D HN(CA)CO | sample_1 | isotropic | sample_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 shifts
SPARKY: Backbone
or all simulated shifts