BMRB Entry 15050
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR15050
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Citation: Campagna, Sylvie; Saint, Nathalie; Molle, Gerard; Aumelas, Andre. "Structure and mechanism of action of the antimicrobial peptide piscidin" Biochemistry 46, 1771-1778 (2007).
PubMed: 17253775
Assembly members:
piscidin-1, polymer, 23 residues, Formula weight is not available
Natural source: Common Name: striped bass Taxonomy ID: 34816 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Morone saxatilis
Experimental source: Production method: chemical synthesis
Entity Sequences (FASTA):
piscidin-1: FFHHIFRGIVHVGKTIHRLV
TGX
- assigned_chemical_shifts
| Data type | Count |
| 1H chemical shifts | 160 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | piscidin-1 | 1 |
Entities:
Entity 1, piscidin-1 23 residues - Formula weight is not available
The C-terminus is amidated
| 1 | PHE | PHE | HIS | HIS | ILE | PHE | ARG | GLY | ILE | VAL | ||||
| 2 | HIS | VAL | GLY | LYS | THR | ILE | HIS | ARG | LEU | VAL | ||||
| 3 | THR | GLY | NH2 |
Samples:
sample_1: piscidin-1 1 ± 0.1 mM
sample_2: piscidin-1 1 ± 0.1 mM; DPC 39 mM
sample_conditions_1: pH: 5.0; pressure: 1 atm; temperature: 300 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D DQF-COSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H COSY | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_2 | isotropic | sample_conditions_1 |
Software:
DYANA v1.5, Guntert, Braun and Wuthrich - structure solution
xwinnmr, Bruker Biospin - chemical shift assignment, collection, processing
NMR spectrometers:
- Bruker Avance 600 MHz