BMRB Entry 19110
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR19110
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Title: NMR assignments of PI3-SH3 aided by protonless NMR spectroscopy PubMed: 23832674
Deposition date: 2013-03-26 Original release date: 2013-08-15
Authors: Hsu, Shang-Te Danny
Citation: Hsu, Shang-Te Danny. "NMR assignments of PI3-SH3 domain aided by protonless NMR spectroscopy." Biomol. NMR Assignments ., .-. (2013).
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
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:
BMRB | 16448 17121 |
PDB | |
EMBL | CAH92731 |
GB | AAA79511 AAH94795 EAW51312 EAW51313 EFB13241 |
REF | NP_001126593 NP_001248126 NP_777000 NP_852664 XP_001491621 |
SP | P23727 P27986 Q5R685 |
TPG | DAA17994 |
Download simulated HSQC data in one of the following formats:
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SPARKY: Backbone
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