BMRB Entry 16163
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16163
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Title: NMR structure of the N-terminal domain of kindlin1 PubMed: 19804783
Deposition date: 2009-02-09 Original release date: 2009-12-01
Authors: Goult, Benjamin
Citation: Goult, Benjamin; Bouaouina, Mohamed; Harburger, David; Bate, Neil; Patel, Bipin; Anthis, Nicholas; Campbell, Iain; Calderwood, David; Barsukov, Igor; Roberts, Gordon; Critchley, David. "The structure of the N-terminus of kindlin-1: a domain important for alphaiibbeta3 integrin activation." J. Mol. Biol. 394, 944-956 (2009).
Assembly members:
F0, polymer, 102 residues, Formula weight is not available
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):
F0: GIDPFTMLSSGDLTSASWEL
VVRVDHANGEQQTEITLRVS
GDLHIGGVMLKLVEQMNIAQ
DWSDYALWWEQKRCWLLKTH
WTLDKCGVQADANLLFTPQH
KM
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 442 |
| 15N chemical shifts | 118 |
| 1H chemical shifts | 720 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | F0 | 1 |
Entities:
Entity 1, F0 102 residues - Formula weight is not available
Residues -5 to 0 represent a non-native affinity tag
| 1 | GLY | ILE | ASP | PRO | PHE | THR | MET | LEU | SER | SER | ||||
| 2 | GLY | ASP | LEU | THR | SER | ALA | SER | TRP | GLU | LEU | ||||
| 3 | VAL | VAL | ARG | VAL | ASP | HIS | ALA | ASN | GLY | GLU | ||||
| 4 | GLN | GLN | THR | GLU | ILE | THR | LEU | ARG | VAL | SER | ||||
| 5 | GLY | ASP | LEU | HIS | ILE | GLY | GLY | VAL | MET | LEU | ||||
| 6 | LYS | LEU | VAL | GLU | GLN | MET | ASN | ILE | ALA | GLN | ||||
| 7 | ASP | TRP | SER | ASP | TYR | ALA | LEU | TRP | TRP | GLU | ||||
| 8 | GLN | LYS | ARG | CYS | TRP | LEU | LEU | LYS | THR | HIS | ||||
| 9 | TRP | THR | LEU | ASP | LYS | CYS | GLY | VAL | GLN | ALA | ||||
| 10 | ASP | ALA | ASN | LEU | LEU | PHE | THR | PRO | GLN | HIS | ||||
| 11 | LYS | MET |
Samples:
15N: F0, [U-100% 15N], 200 ± 5 uM; DTT 2 ± 0.1 mM; sodium phosphate 20 ± 0.3 mM; sodium chloride 50 ± 0.3 mM; H2O 90%; D2O 10%
double: F0, [U-100% 13C; U-100% 15N], 200 ± 5 uM; DTT 2 ± 0.1 mM; sodium phosphate 20 ± 0.3 mM; sodium chloride 50 ± 0.3 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 | 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 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 |
Software:
TOPSPIN v2.1, Bruker Biospin - collection, processing
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - peak picking, structure solution
ANALYSIS v1.15, CCPN - chemical shift assignment, data analysis, peak picking
ARIA v1.2, Linge, O, . - refinement, structure solution
NMR spectrometers:
- Bruker DRX 600 MHz
- Bruker DRX 600 MHz
- Bruker DRX 800 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts