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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15457
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
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Citation: Goult, Benjamin; Bate, Neil; Anthis, Nicholas; Wegener, Kate; Gingras, Alexandre; Patel, Bipin; Barsukov, Igor; Campbell, Iain; Roberts, Gordon; Critchley, David. "The Structure of an Interdomain Complex That Regulates Talin Activity" J. Biol. Chem. 284, 15097-15106 (2009).
PubMed: 19297334
Assembly members:
1655-1822, polymer, 174 residues, 18254.602 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
Data type | Count |
13C chemical shifts | 708 |
15N chemical shifts | 172 |
1H chemical shifts | 1154 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | 1655-1822 | 1 |
Entity 1, 1655-1822 174 residues - 18254.602 Da.
Residues 1-6 represent a non-native expression tag
1 | GLY | ILE | ASP | PRO | PHE | THR | ALA | PRO | GLY | GLN | ||||
2 | LEU | GLU | CYS | GLU | THR | ALA | ILE | ALA | ALA | LEU | ||||
3 | ASN | SER | CYS | LEU | ARG | ASP | LEU | ASP | GLN | ALA | ||||
4 | SER | LEU | ALA | ALA | VAL | SER | GLN | GLN | LEU | ALA | ||||
5 | PRO | ARG | GLU | GLY | ILE | SER | GLN | GLU | ALA | LEU | ||||
6 | HIS | THR | GLN | MET | LEU | THR | ALA | VAL | GLN | GLU | ||||
7 | ILE | SER | HIS | LEU | ILE | GLU | PRO | LEU | ALA | SER | ||||
8 | ALA | ALA | ARG | ALA | GLU | ALA | SER | GLN | LEU | GLY | ||||
9 | HIS | LYS | VAL | SER | GLN | MET | ALA | GLN | TYR | PHE | ||||
10 | GLU | PRO | LEU | THR | LEU | ALA | ALA | VAL | GLY | ALA | ||||
11 | ALA | SER | LYS | THR | LEU | SER | HIS | PRO | GLN | GLN | ||||
12 | MET | ALA | LEU | LEU | ASP | GLN | THR | LYS | THR | LEU | ||||
13 | ALA | GLU | SER | ALA | LEU | GLN | LEU | LEU | TYR | THR | ||||
14 | ALA | LYS | GLU | ALA | GLY | GLY | ASN | PRO | LYS | GLN | ||||
15 | ALA | ALA | HIS | THR | GLN | GLU | ALA | LEU | GLU | GLU | ||||
16 | ALA | VAL | GLN | MET | MET | THR | GLU | ALA | VAL | GLU | ||||
17 | ASP | LEU | THR | THR | THR | LEU | ASN | GLU | ALA | ALA | ||||
18 | SER | ALA | ALA | GLY |
unlabelled: 1655-1822 1 ± 0.05 mM; NaCl 50 mM
15n: 1655-1822, [U-100% 15N], 1 ± 0.05 mM; NaCl 50 mM
double: 1655-1822, [U-100% 13C; U-100% 15N], 1 ± 0.05 mM; NaCl 50 mM
sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 308 K
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 CBCA(CO)NH | double | isotropic | sample_conditions_1 |
3D HNCO | double | isotropic | sample_conditions_1 |
3D HNCA | double | isotropic | sample_conditions_1 |
3D HNCACB | double | isotropic | sample_conditions_1 |
3D HBHA(CO)NH | double | isotropic | sample_conditions_1 |
3D HN(CO)CA | 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 |
TOPSPIN v2.0, Bruker Biospin - collection, processing
ANALYSIS v1.015, 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
PDB | |
DBJ | BAA82979 BAC65702 BAE27781 BAE41923 BAE42391 |
EMBL | CAA39588 |
GB | AAD13152 AAF23322 AAF27330 AAH18557 AAH42923 |
PRF | 1617167A |
REF | NP_001034114 NP_006280 NP_035732 XP_001084941 XP_001504543 |
SP | P26039 Q9Y490 |
AlphaFold | P26039 Q9Y490 |
Download HSQC peak lists in one of the following formats:
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