BMRB Entry 17547
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR17547
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Dubovskii, Peter; Vassilevski, Alexander; Slavokhotova, Anna; Odintsova, Tatyana; Grishin, Eugene; Egorov, Tsezi; Arseniev, Alexander. "Solution structure of a defense peptide from wheat with a 10-cysteine motif." Biochem. Biophys. Res. Commun. 411, 14-18 (2011).
PubMed: 21704019
Assembly members:
Hevein-type Antifungal Peptide with a Unique 10-Cysteine Motif, polymer, 44 residues, 4450.046 Da.
Natural source: Common Name: wheat Taxonomy ID: 376535 Superkingdom: Eukaryota Kingdom: Viridiplantae Genus/species: Triticum kiharae
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-32b
Entity Sequences (FASTA):
Hevein-type Antifungal Peptide with a Unique 10-Cysteine Motif: AQRCGDQARGAKCPNCLCCG
KYGFCGSGDAYCGAGSCQSQ
CRGC
- assigned_chemical_shifts
| Data type | Count |
| 1H chemical shifts | 243 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Hevein-type Antifungal Peptide with a Unique 10-Cysteine Motif | 1 |
Entities:
Entity 1, Hevein-type Antifungal Peptide with a Unique 10-Cysteine Motif 44 residues - 4450.046 Da.
| 1 | ALA | GLN | ARG | CYS | GLY | ASP | GLN | ALA | ARG | GLY | ||||
| 2 | ALA | LYS | CYS | PRO | ASN | CYS | LEU | CYS | CYS | GLY | ||||
| 3 | LYS | TYR | GLY | PHE | CYS | GLY | SER | GLY | ASP | ALA | ||||
| 4 | TYR | CYS | GLY | ALA | GLY | SER | CYS | GLN | SER | GLN | ||||
| 5 | CYS | ARG | GLY | CYS |
Samples:
sample_1: entity 0.5 ± 0.05 mM; H2O 90%; D2O 10%
sample_2: entity 0.5 ± 0.05 mM; D2O 100%
sample_conditions_1: pH: 6.0; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D DQF-COSY | sample_1 | isotropic | sample_conditions_1 |
| 2D DQF-COSY | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_2 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v2.2, BRUKER - collection, processing
XEASY, Bartels et al. - chemical shift assignment, chemical shift calculation, peak picking
CYANA v2.0, Guntert, Mumenthaler and Wuthrich - structure solution
Molmol v2.1-2.6, Koradi, Billeter and Wuthrich - visualization
NMR spectrometers:
- Bruker Avance-1 700 MHz