BMRB Entry 19110
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR19110
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Citation: Hsu, Shang-Te Danny. "NMR assignments of PI3-SH3 domain aided by protonless NMR spectroscopy." Biomol. NMR Assignments ., .-. (2013).
PubMed: 23832674
Assembly members:
PI3-SH3, polymer, 86 residues, Formula weight is not available
Natural source: Common Name: Humans Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET14b
Entity Sequences (FASTA):
PI3-SH3: GSMSAEGYQYRALYDYKKER
EEDIDLHLGDILTVNKGSLV
ALGFSDGQEAKPEEIGWLNG
YNETTGERGDFPGTYVEYIG
RKKISP
- assigned_chemical_shifts
| Data type | Count |
| 1H chemical shifts | 459 |
| 13C chemical shifts | 328 |
| 15N chemical shifts | 92 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | PI3-SH3 | 1 |
Entities:
Entity 1, PI3-SH3 86 residues - Formula weight is not available
| 1 | GLY | SER | MET | SER | ALA | GLU | GLY | TYR | GLN | TYR | ||||
| 2 | ARG | ALA | LEU | TYR | ASP | TYR | LYS | LYS | GLU | ARG | ||||
| 3 | GLU | GLU | ASP | ILE | ASP | LEU | HIS | LEU | GLY | ASP | ||||
| 4 | ILE | LEU | THR | VAL | ASN | LYS | GLY | SER | LEU | VAL | ||||
| 5 | ALA | LEU | GLY | PHE | SER | ASP | GLY | GLN | GLU | ALA | ||||
| 6 | LYS | PRO | GLU | GLU | ILE | GLY | TRP | LEU | ASN | GLY | ||||
| 7 | TYR | ASN | GLU | THR | THR | GLY | GLU | ARG | GLY | ASP | ||||
| 8 | PHE | PRO | GLY | THR | TYR | VAL | GLU | TYR | ILE | GLY | ||||
| 9 | ARG | LYS | LYS | ILE | SER | PRO |
Samples:
sample_1: PI3-SH3, [U-98% 13C; U-98% 15N], 0.5 mM; potassium phosphate 50 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 0.05 M; pH: 6; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 2D CON | sample_1 | isotropic | sample_conditions_1 |
| 2D COCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
No software information available
NMR spectrometers:
- Bruker Avance 500 MHz
Related Database Links:
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks