BMRB Entry 53252
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR53252
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
All files associated with the entry
Citation: Machner, Lisa; Shaikhqasem, Alaa; Hamdi, Farzad; Gruber, Tobias; Wiebe, Felix; Breithaupt, Constanze; Kniest, Judith; Lewitzky, Marc; Parthier, Christoph; Kyrilis, Fotios; Balbach, Jochen; Kastritis, Panagiotis; Feller, Stephan; Stubbs, Milton. "Mechanism of SHP2 activation by bis-Tyr-phosphorylated Gab1" Structure ., .-..
Assembly members:
entity_1, polymer, 106 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: pETSumo
Entity Sequences (FASTA):
entity_1: MTSRRWFHPNITGVEAENLL
LTRGVDGSFLARPSKSNPGD
FTLSVRRNGAVTHIKIQNTG
DYYDLYGGEKFATLAELVQY
YMEHHGQLKEKNGDVIELKY
PLNCAD
- assigned_chemical_shifts
| Data type | Count |
| 15N chemical shifts | 90 |
| 1H chemical shifts | 90 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | N-SH2 | 1 |
Entities:
Entity 1, N-SH2 106 residues - Formula weight is not available
| 1 | MET | THR | SER | ARG | ARG | TRP | PHE | HIS | PRO | ASN | ||||
| 2 | ILE | THR | GLY | VAL | GLU | ALA | GLU | ASN | LEU | LEU | ||||
| 3 | LEU | THR | ARG | GLY | VAL | ASP | GLY | SER | PHE | LEU | ||||
| 4 | ALA | ARG | PRO | SER | LYS | SER | ASN | PRO | GLY | ASP | ||||
| 5 | PHE | THR | LEU | SER | VAL | ARG | ARG | ASN | GLY | ALA | ||||
| 6 | VAL | THR | HIS | ILE | LYS | ILE | GLN | ASN | THR | GLY | ||||
| 7 | ASP | TYR | TYR | ASP | LEU | TYR | GLY | GLY | GLU | LYS | ||||
| 8 | PHE | ALA | THR | LEU | ALA | GLU | LEU | VAL | GLN | TYR | ||||
| 9 | TYR | MET | GLU | HIS | HIS | GLY | GLN | LEU | LYS | GLU | ||||
| 10 | LYS | ASN | GLY | ASP | VAL | ILE | GLU | LEU | LYS | TYR | ||||
| 11 | PRO | LEU | ASN | CYS | ALA | ASP |
Samples:
sample_1: N-SH2, [U-100% 13C; U-100% 15N], 750 uM; Bis Tris / HCl 20 mM; NaCl 50 mM
sample_conditions_1: ionic strength: 0.05 M; pH: 6.0; pressure: 1 atm; temperature: 298.15 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRView - 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 peaks
SPARKY: Backbone
or all simulated peaks