BMRB Entry 26328
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR26328
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Title: Backbone assignment of the N-terminal SH2 domain of PI3K PubMed: 36282120
Deposition date: 2022-03-19 Original release date: 2023-06-05
Authors: Hosoe, Yuhi; Miyanoiri, Yohei; Re, Suyong; Asahina, Yuya; Kawakami, Toru; Kuroda, Mataka; Mizuguchi, Kenji; Oda, Masayuki
Citation: Hosoe, Yuhi; Miyanoiri, Yohei; Re, Suyong; Ochi, Saki; Asahina, Yuya; Kawakami, Toru; Kuroda, Masataka; Mizuguchi, Kenji; Oda, Masayuki. "Structural dynamics of the N-terminal SH2 domain of PI3K in its free and CD28-bound states" FEBS J. 290, 2366-2378 (2023).
Assembly members:
N-terminal SH2 domain of PI3K, polymer, 107 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: pGEX
Entity Sequences (FASTA):
N-terminal SH2 domain of PI3K: SNMSLQNAEWYWGDISREEV
NEKLRDTADGTFLVRDASTK
MHGDYTLTLRKGGNNKLIKI
FHRDGKYGFSDPLTFSSVVE
LINHYRNESLAQYNPKLDVK
LLYPVSK
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 301 |
| 15N chemical shifts | 100 |
| 1H chemical shifts | 100 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | nSH2 of PI3K | 1 |
Entities:
Entity 1, nSH2 of PI3K 107 residues - Formula weight is not available
| 1 | SER | ASN | MET | SER | LEU | GLN | ASN | ALA | GLU | TRP | ||||
| 2 | TYR | TRP | GLY | ASP | ILE | SER | ARG | GLU | GLU | VAL | ||||
| 3 | ASN | GLU | LYS | LEU | ARG | ASP | THR | ALA | ASP | GLY | ||||
| 4 | THR | PHE | LEU | VAL | ARG | ASP | ALA | SER | THR | LYS | ||||
| 5 | MET | HIS | GLY | ASP | TYR | THR | LEU | THR | LEU | ARG | ||||
| 6 | LYS | GLY | GLY | ASN | ASN | LYS | LEU | ILE | LYS | ILE | ||||
| 7 | PHE | HIS | ARG | ASP | GLY | LYS | TYR | GLY | PHE | SER | ||||
| 8 | ASP | PRO | LEU | THR | PHE | SER | SER | VAL | VAL | GLU | ||||
| 9 | LEU | ILE | ASN | HIS | TYR | ARG | ASN | GLU | SER | LEU | ||||
| 10 | ALA | GLN | TYR | ASN | PRO | LYS | LEU | ASP | VAL | LYS | ||||
| 11 | LEU | LEU | TYR | PRO | VAL | SER | LYS |
Samples:
sample_1: N-terminal SH2 domain of PI3K, [U-99% 13C; U-99% 15N], 0.1 – 0.3 mM; potassium phosphate 10 mM; sodium 2,2-dimethyl-2-silapentane-5-sulfonate 0.01 % v/v; H2O 90%; D2O, [U-2H], 10%
sample_conditions_1: ionic strength: 10 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRFAM-SPARKY - chemical shift assignment
TOPSPIN - processing
TOPSPIN - collection
NMR spectrometers:
- Bruker AVANCE III HD 600 MHz
Related Database Links:
| PDB |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts