BMRB Entry 51019
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51019
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Title: Backbone 1H, 13C and 15N chemical shift assignments for the C-Terminal non-phosphorylated intrinsically disordered Gab1 PubMed: 34929201
Deposition date: 2021-07-15 Original release date: 2021-08-16
Authors: Gruber, Tobias
Citation: Gruber, Tobias; Lewitzky, Marc; Machner, Lisa; Weininger, Ulrich; Feller, Stephan M.; Balbach, Jochen. "Macromolecular crowding induces a binding competent transient structure in intrinsically disordered Gab1" J. Mol. Biol. 434, 167407-167407 (2021).
Assembly members:
entity_1, polymer, 82 residues, Formula weight is not available
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET42a
Entity Sequences (FASTA):
entity_1: SSPMIKPKGDKQVEYLDLDL
DSGKSTPPRKQKSSGSGSSV
ADERVDYVVVDQQKTLALKS
TREAWTDGRQSTESETPAKS
VK
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 202 |
| 15N chemical shifts | 69 |
| 1H chemical shifts | 69 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | C-Terminus of Gab1 | 1 |
Entities:
Entity 1, C-Terminus of Gab1 82 residues - Formula weight is not available
| 1 | SER | SER | PRO | MET | ILE | LYS | PRO | LYS | GLY | ASP | ||||
| 2 | LYS | GLN | VAL | GLU | TYR | LEU | ASP | LEU | ASP | LEU | ||||
| 3 | ASP | SER | GLY | LYS | SER | THR | PRO | PRO | ARG | LYS | ||||
| 4 | GLN | LYS | SER | SER | GLY | SER | GLY | SER | SER | VAL | ||||
| 5 | ALA | ASP | GLU | ARG | VAL | ASP | TYR | VAL | VAL | VAL | ||||
| 6 | ASP | GLN | GLN | LYS | THR | LEU | ALA | LEU | LYS | SER | ||||
| 7 | THR | ARG | GLU | ALA | TRP | THR | ASP | GLY | ARG | GLN | ||||
| 8 | SER | THR | GLU | SER | GLU | THR | PRO | ALA | LYS | SER | ||||
| 9 | VAL | LYS |
Samples:
sample_1: C-Terminus of Gab1, [U-100% 13C; U-100% 15N], 0.9 mM
sample_conditions_1: ionic strength: 0.05 M; pH: 6.2; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N TROSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRbox - chemical shift assignment
NMR spectrometers:
- Bruker AVANCE III 800 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts