BMRB Entry 25555
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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/BMR25555
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Title: Structure of PvHCt, an antimicrobial peptide from shrimp litopenaeus vannamei
Deposition date: 2015-03-27 Original release date: 2015-05-26
Authors: Petit, Vanessa; Rolland, Jean-Luc; Blond, Alain; Djediat, Chakib; Peduzzi, Jean; Goulard, Christophe; Bachere, Evelyne; Dupont, Joelle; Destoumieux-Garzon, Delphine; Rebuffat, Sylvie
Citation: Petit, Vanessa; Rolland, Jean-Luc; Blond, Alain; Djediat, Chakib; Peduzzi, Jean; Goulard, Christophe; Bachere, Evelyne; Dupont, Joelle; Destoumieux-Garzon, Delphine; Rebuffat, Sylvie. "THE HEMOCYANIN-DERIVED PVHCT IS AN ALPHA-HELICAL ANTIFUNGAL PEPTIDE THAT SPECIFICALLY PERMEABILIZES FUNGAL MEMBRANES" J. Biol. Chem. ., .-..
Assembly members:
entity, polymer, 23 residues, 2758.086 Da.
Natural source: Common Name: white shrimp Taxonomy ID: 6689 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Litopenaeus vannamei
Experimental source: Production method: chemical synthesis
Entity Sequences (FASTA):
entity: FEDLPNFGHIQVKVFNHGEH
IHH
- assigned_chemical_shifts
| Data type | Count |
| 1H chemical shifts | 160 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity | 1 |
Entities:
Entity 1, entity 23 residues - 2758.086 Da.
| 1 | PHE | GLU | ASP | LEU | PRO | ASN | PHE | GLY | HIS | ILE | ||||
| 2 | GLN | VAL | LYS | VAL | PHE | ASN | HIS | GLY | GLU | HIS | ||||
| 3 | ILE | HIS | HIS |
Samples:
sample_1: entity 3.5 mM; DPC, [U-99% 2H], 350 mM; H2O 90%; D2O, [U-2H], 10%
sample_conditions_1: pH: 3.5; pressure: 1 atm; temperature: 313 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-1H 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 |
Software:
xwinnmr v3.1, Bruker Biospin - chemical shift assignment, processing
TOPSPIN v3.2, Bruker Biospin - chemical shift assignment, processing
AURELIA v3.8, BRUKER - peak picking
X-PLOR v3.851, Brunger - refinement
NMR spectrometers:
- Bruker Avance 400 MHz