BMRB Entry 16959
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16959
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Title: Chemical shift assignments of the Talin F1F2 double domain (residues 86-303 (delta D139-D168)) PubMed: 20947018
Deposition date: 2010-05-27 Original release date: 2014-03-10
Authors: Goult, Ben; Barsukov, Igor; Roberts, Gordon; Critchley, David
Citation: Elliott, Paul; Goult, Benjamin; Kopp, Petra; Bate, Neil; Grossmann, J.; Roberts, Gordon; Critchley, David; Barsukov, Igor. "The Structure of the talin head reveals a novel extended conformation of the FERM domain." Structure 18, 1288-1299 (2010).
Assembly members:
F1F2, polymer, 194 residues, 22616.8 Da.
Natural source: Common Name: Mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
F1F2: GIDPFTRPLKIRMLDGTVKT
IMVDDSKTVTDMLMTICARI
GITNHDEYSLVRELMEEKKD
ELNWLDHGRTLREQGVEEHE
TLLLRRKFFYSDQNVDSRDP
VQLNLLYVQARDDILNGSHP
VSFDKACEFAGFQCQIQFGP
HNEQKHKAGFLDLKDFLPKE
YVKQKGERKIFQAHKNCGQM
SEIEAKVRYVKLAR
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 558 |
15N chemical shifts | 185 |
1H chemical shifts | 185 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | F1F2 | 1 |
Entities:
Entity 1, F1F2 194 residues - 22616.8 Da.
Residues 1-6 (80-85) represent a non-native affinity tag
1 | GLY | ILE | ASP | PRO | PHE | THR | ARG | PRO | LEU | LYS | ||||
2 | ILE | ARG | MET | LEU | ASP | GLY | THR | VAL | LYS | THR | ||||
3 | ILE | MET | VAL | ASP | ASP | SER | LYS | THR | VAL | THR | ||||
4 | ASP | MET | LEU | MET | THR | ILE | CYS | ALA | ARG | ILE | ||||
5 | GLY | ILE | THR | ASN | HIS | ASP | GLU | TYR | SER | LEU | ||||
6 | VAL | ARG | GLU | LEU | MET | GLU | GLU | LYS | LYS | ASP | ||||
7 | GLU | LEU | ASN | TRP | LEU | ASP | HIS | GLY | ARG | THR | ||||
8 | LEU | ARG | GLU | GLN | GLY | VAL | GLU | GLU | HIS | GLU | ||||
9 | THR | LEU | LEU | LEU | ARG | ARG | LYS | PHE | PHE | TYR | ||||
10 | SER | ASP | GLN | ASN | VAL | ASP | SER | ARG | ASP | PRO | ||||
11 | VAL | GLN | LEU | ASN | LEU | LEU | TYR | VAL | GLN | ALA | ||||
12 | ARG | ASP | ASP | ILE | LEU | ASN | GLY | SER | HIS | PRO | ||||
13 | VAL | SER | PHE | ASP | LYS | ALA | CYS | GLU | PHE | ALA | ||||
14 | GLY | PHE | GLN | CYS | GLN | ILE | GLN | PHE | GLY | PRO | ||||
15 | HIS | ASN | GLU | GLN | LYS | HIS | LYS | ALA | GLY | PHE | ||||
16 | LEU | ASP | LEU | LYS | ASP | PHE | LEU | PRO | LYS | GLU | ||||
17 | TYR | VAL | LYS | GLN | LYS | GLY | GLU | ARG | LYS | ILE | ||||
18 | PHE | GLN | ALA | HIS | LYS | ASN | CYS | GLY | GLN | MET | ||||
19 | SER | GLU | ILE | GLU | ALA | LYS | VAL | ARG | TYR | VAL | ||||
20 | LYS | LEU | ALA | ARG |
Samples:
sample_1: F1F2, [U-99% 13C; U-99% 15N], 1 ± 0.05 mM; sodium chloride 50 ± 0.05 mM; sodium phosphate 20 ± 0.05 mM; DTT 2 ± 0.05 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
3D HNCA | sample_1 | isotropic | sample_conditions_1 |
3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v2, Bruker Biospin - collection, processing
Analysis v2.1.3, CCPN - chemical shift assignment, data analysis, peak picking
NMR spectrometers:
- Bruker DRX 800 MHz
- Bruker DRX 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts