BMRB Entry 16913
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16913
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Title: The solution structure of the squash aspartic acid proteinase inhibitor (SQAPI) PubMed: 20538608
Deposition date: 2010-05-05 Original release date: 2010-07-26
Authors: Headey, Stephen; MacAskill, Ursula; Wright, Michelle; Claridge, Jolyon; Edwards, Patrick; Farley, Peter; Christeller, John; Laing, William; Pascal, Steven
Citation: Headey, Stephen; Macaskill, Ursula; Wright, Michele; Claridge, Jolyon; Edwards, Patrick; Farley, Peter; Christeller, John; Laing, William; Pascal, Steven. "Solution structure of the squash aspartic acid proteinase inhibitor (SQAPI) and mutational analysis of pepsin inhibition." J. Biol. Chem. 285, 27019-27025 (2010).
Assembly members:
SQAPI, polymer, 95 residues, 10421.041 Da.
Natural source: Common Name: winter squash Taxonomy ID: 3661 Superkingdom: Eukaryota Kingdom: Viridiplantae Genus/species: Cucurbita maxima
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
SQAPI: GPGPAIGEVIGISVNDPRVK
EIAEFALKQHAEQNLILAGV
DAGQIIKGIPHWDNYYNLIL
SAKHSPHEFSKFYNVVVLEK
ASDNSLKLVAFVPLF
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 421 |
| 1H chemical shifts | 674 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | SQAPI | 1 |
Entities:
Entity 1, SQAPI 95 residues - 10421.041 Da.
| 1 | GLY | PRO | GLY | PRO | ALA | ILE | GLY | GLU | VAL | ILE | ||||
| 2 | GLY | ILE | SER | VAL | ASN | ASP | PRO | ARG | VAL | LYS | ||||
| 3 | GLU | ILE | ALA | GLU | PHE | ALA | LEU | LYS | GLN | HIS | ||||
| 4 | ALA | GLU | GLN | ASN | LEU | ILE | LEU | ALA | GLY | VAL | ||||
| 5 | ASP | ALA | GLY | GLN | ILE | ILE | LYS | GLY | ILE | PRO | ||||
| 6 | HIS | TRP | ASP | ASN | TYR | TYR | ASN | LEU | ILE | LEU | ||||
| 7 | SER | ALA | LYS | HIS | SER | PRO | HIS | GLU | PHE | SER | ||||
| 8 | LYS | PHE | TYR | ASN | VAL | VAL | VAL | LEU | GLU | LYS | ||||
| 9 | ALA | SER | ASP | ASN | SER | LEU | LYS | LEU | VAL | ALA | ||||
| 10 | PHE | VAL | PRO | LEU | PHE |
Samples:
sample_1: SQAPI, [U-98% 13C; U-98% 15N], 0.6 mM; H2O 90%; D2O 10%
sample_conditions_1: pH: 3; pressure: 1 atm; temperature: 323 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 |
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCCONH TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D (HB)CB(CGCD)HD | sample_1 | isotropic | sample_conditions_1 |
| 2D (HB)CB(CGCDCE)HE | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESYHSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESYHSQC | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v2.0, Bruker Biospin - processing
XEASY v1.4, Bartels et al. - data analysis
NMR spectrometers:
- Bruker Avance 700 MHz