BMRB Entry 15458
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15458
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Title: NMR Structure of the F0 domain (residues 1-85) of the Talin FERM domain
Deposition date: 2007-09-05 Original release date: 2010-02-18
Authors: Goult, Benjamin; Elliott, Paul; Roberts, Gordon; Critchley, David; Barsukov, Igor
Citation: Goult, Benjamin. "The NMR structure of the F0F1 double domain from the Talin Ferm domain" .
Assembly members:
F0_domain_of_Talin, polymer, 91 residues, 10339.090 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 Vector: PET-151
Entity Sequences (FASTA):
F0_domain_of_Talin: GIDPFTMVALSLKISIGNVV
KTMQFEPSTMVYDACRMIRE
RIPEALAGPPNDFGLFLSDD
DPKKGIWLEAGKALDYYMLR
NGDTMEYRKKQ
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 365 |
| 15N chemical shifts | 84 |
| 1H chemical shifts | 599 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity | 1 |
Entities:
Entity 1, entity 91 residues - 10339.090 Da.
Residues -5 to 0 represent a non-native affinity tag
| 1 | GLY | ILE | ASP | PRO | PHE | THR | MET | VAL | ALA | LEU | ||||
| 2 | SER | LEU | LYS | ILE | SER | ILE | GLY | ASN | VAL | VAL | ||||
| 3 | LYS | THR | MET | GLN | PHE | GLU | PRO | SER | THR | MET | ||||
| 4 | VAL | TYR | ASP | ALA | CYS | ARG | MET | ILE | ARG | GLU | ||||
| 5 | ARG | ILE | PRO | GLU | ALA | LEU | ALA | GLY | PRO | PRO | ||||
| 6 | ASN | ASP | PHE | GLY | LEU | PHE | LEU | SER | ASP | ASP | ||||
| 7 | ASP | PRO | LYS | LYS | GLY | ILE | TRP | LEU | GLU | ALA | ||||
| 8 | GLY | LYS | ALA | LEU | ASP | TYR | TYR | MET | LEU | ARG | ||||
| 9 | ASN | GLY | ASP | THR | MET | GLU | TYR | ARG | LYS | LYS | ||||
| 10 | GLN |
Samples:
double-labelled: F0 domain of Talin, [U-100% 13C; U-100% 15N], 1 mM; NaCl 50 mM
single-labelled: F0 domain of Talin, [U-100% 15N], 1 mM; NaCl 50 mM
unlabelled: F0 domain of Talin 1 mM; NaCl 50 mM
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 | single-labelled | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | double-labelled | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | double-labelled | isotropic | sample_conditions_1 |
| 3D HNCO | double-labelled | isotropic | sample_conditions_1 |
| 3D HNCA | double-labelled | isotropic | sample_conditions_1 |
| 3D HNCACB | double-labelled | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | double-labelled | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | double-labelled | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | single-labelled | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | double-labelled | isotropic | sample_conditions_1 |
Software:
TOPSPIN v2.0, Bruker Biospin - collection, processing
CcpNMR v11, CCPN - chemical shift assignment, data analysis, peak picking
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution
ARIA v1.2, Linge, O'Donoghue and Nilges - refinement
NMR spectrometers:
- Bruker DRX 600 MHz
- Bruker DRX 600 MHz
- Bruker DRX 800 MHz
Related Database Links:
| BMRB | 15615 |
| PDB | |
| DBJ | BAC65702 BAE27781 |
| EMBL | CAA39588 |
| GB | AAI50811 EDL02466 EDL02467 EDL98751 EDL98752 |
| PRF | 1617167A |
| REF | NP_001034114 NP_035732 XP_002918927 XP_003341683 XP_003407647 |
| SP | P26039 |
| AlphaFold | P26039 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts