BMRB Entry 15411
Click here to enlarge.
            
                PDB ID: 
                
                
                Entry in NMR Restraints Grid
                Validation report in NRG-CING
            Chem Shift validation:  AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15411
MolProbity Validation Chart            
                    NMR-STAR file interactive viewer.
                    NMR-STAR v3 text file.
                    NMR-STAR v2.1 text file (deprecated)
                    XML gzip file.
                    RDF gzip file.
                    All files associated with the entry
                
Title: NMR structure of the talin C-terminal actin binding site PubMed: 19636914
Deposition date: 2007-07-30 Original release date: 2008-01-17
Authors: Goult, Benjamin; Gingras, Alexandre; Bate, Neil; Critchley, David; Barsukov, Igor
Citation: Goult, Benjamin; Gingras, Alexandre; Bate, Neil; Roberts, Gordon; Critchley, David; Barsukov, Igor. "NMR assignment of the C-terminal actin-binding domain of talin" Biomol. NMR Assignments 2, 17-19 (2008).
Assembly members:
Talin_c-terminal_actin_binding_site_(ABS3), polymer, 189 residues,   19385.072 Da.
Natural source: Common Name: not available Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
Talin_c-terminal_actin_binding_site_(ABS3): GIDPFTDPTVIAENELLGAA
AAIEAAAKKLEQLKPRAKPK
EADESLNFEEQILEAAKSIA
AATSALVKAASAAQRELVAQ
GKVGAIPANALDDGQWSQGL
ISAARMVAAATNNLCEAANA
AVQGHASQEKLISSAKQVAA
STAQLLVACKVKADQDSEAM
KRLQAAGNAVKRASDNLVKA
AQKAAAFED
- assigned_chemical_shifts
 
| Data type | Count | 
| 13C chemical shifts | 774 | 
| 15N chemical shifts | 203 | 
| 1H chemical shifts | 1285 | 
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID | 
|---|---|---|
| 1 | Talin c-terminal acting binding domain | 1 | 
Entities:
Entity 1, Talin c-terminal acting binding domain 189 residues - 19385.072 Da.
Residues 1-6 represent a non-native affinity tag
| 1 | GLY | ILE | ASP | PRO | PHE | THR | ASP | PRO | THR | VAL | ||||
| 2 | ILE | ALA | GLU | ASN | GLU | LEU | LEU | GLY | ALA | ALA | ||||
| 3 | ALA | ALA | ILE | GLU | ALA | ALA | ALA | LYS | LYS | LEU | ||||
| 4 | GLU | GLN | LEU | LYS | PRO | ARG | ALA | LYS | PRO | LYS | ||||
| 5 | GLU | ALA | ASP | GLU | SER | LEU | ASN | PHE | GLU | GLU | ||||
| 6 | GLN | ILE | LEU | GLU | ALA | ALA | LYS | SER | ILE | ALA | ||||
| 7 | ALA | ALA | THR | SER | ALA | LEU | VAL | LYS | ALA | ALA | ||||
| 8 | SER | ALA | ALA | GLN | ARG | GLU | LEU | VAL | ALA | GLN | ||||
| 9 | GLY | LYS | VAL | GLY | ALA | ILE | PRO | ALA | ASN | ALA | ||||
| 10 | LEU | ASP | ASP | GLY | GLN | TRP | SER | GLN | GLY | LEU | ||||
| 11 | ILE | SER | ALA | ALA | ARG | MET | VAL | ALA | ALA | ALA | ||||
| 12 | THR | ASN | ASN | LEU | CYS | GLU | ALA | ALA | ASN | ALA | ||||
| 13 | ALA | VAL | GLN | GLY | HIS | ALA | SER | GLN | GLU | LYS | ||||
| 14 | LEU | ILE | SER | SER | ALA | LYS | GLN | VAL | ALA | ALA | ||||
| 15 | SER | THR | ALA | GLN | LEU | LEU | VAL | ALA | CYS | LYS | ||||
| 16 | VAL | LYS | ALA | ASP | GLN | ASP | SER | GLU | ALA | MET | ||||
| 17 | LYS | ARG | LEU | GLN | ALA | ALA | GLY | ASN | ALA | VAL | ||||
| 18 | LYS | ARG | ALA | SER | ASP | ASN | LEU | VAL | LYS | ALA | ||||
| 19 | ALA | GLN | LYS | ALA | ALA | ALA | PHE | GLU | ASP | 
Samples:
unlabelled: Talin c-terminal actin binding site (ABS3) 1 ± 0.1 mM; Sodium Phosphate 20 mM; NaCl 50 mM; DTT 2 mM; H2O 90%; D2O 10%
15N: Talin c-terminal actin binding site (ABS3), [U-15N], 1 ± 0.1 mM; Sodium Phosphate 20 mM; NaCl 50 mM; DTT 2 mM; H2O 90%; D2O 10%
double: Talin c-terminal actin binding site (ABS3), [U-13C; U-15N], 1 ± 0.1 mM; Sodium Phosphate 20 mM; NaCl 50 mM; DTT 2 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 50 mM; pH: 6.0; pressure: 1 atm; temperature: 318.15 K
Experiments:
| Name | Sample | Sample state | Sample conditions | 
|---|---|---|---|
| 2D 1H-15N HSQC | 15N | isotropic | sample_conditions_1 | 
| 2D 1H-13C HSQC | double | isotropic | sample_conditions_1 | 
| 3D HNCO | double | isotropic | sample_conditions_1 | 
| 3D HNCA | double | isotropic | sample_conditions_1 | 
| 3D CBCA(CO)NH | double | isotropic | sample_conditions_1 | 
| 3D HNCACB | double | isotropic | sample_conditions_1 | 
| 3D HCCH-TOCSY | double | isotropic | sample_conditions_1 | 
| 3D 1H-15N NOESY | 15N | isotropic | sample_conditions_1 | 
| 3D 1H-13C NOESY | double | isotropic | sample_conditions_1 | 
| 3D HBHA(CO)NH | double | isotropic | sample_conditions_1 | 
| 2D 1H-1H TOCSY | unlabelled | isotropic | sample_conditions_1 | 
| 2D 1H-1H NOESY | unlabelled | isotropic | sample_conditions_1 | 
| 3D HN(CO)CA | double | isotropic | sample_conditions_1 | 
| 4D 13C, 13C HMQC-NOESY-HSQC | double | isotropic | sample_conditions_1 | 
Software:
ARIA v1.2, Linge, O, . - refinement, structure solution
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - chemical shift assignment, chemical shift calculation, structure solution
TOPSPIN, Bruker Biospin - collection, processing
ANALYSIS v11, CCPN - chemical shift assignment, peak picking
TALOS, Cornilescu, Delaglio and Bax - geometry optimization
NMR spectrometers:
- Bruker DRX 800 MHz
 - Bruker DRX 600 MHz
 - Bruker DRX 600 MHz
 
Related Database Links:
| PDB | |
| DBJ | BAA82979 BAC65702 BAE27781 BAE41923 BAE42391 | 
| EMBL | CAA39588 | 
| GB | AAD13152 AAF23322 AAF27330 AAH18557 AAH42923 | 
| PRF | 1617167A | 
| REF | NP_001034114 NP_001192357 NP_006280 NP_035732 XP_001504543 | 
| SP | P26039 Q9Y490 | 
| TPG | DAA26829 | 
Download simulated HSQC data in one of the following formats:
            
CSV: Backbone
            or all simulated shifts
            
SPARKY: Backbone
            or all simulated shifts