BMRB Entry 19859
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19859
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Title: Solution structure of the mature form, GK cecropin-like peptide from Ae. aegypti mosquito PubMed: 25162372
Deposition date: 2014-03-16 Original release date: 2015-01-26
Authors: Padilla, Andre; Misse, Dorothee
Citation: Godreuil, Sylvain; Leban, Nadia; Padilla, Andre; Hamel, Rodolphe; Luplertlop, Natthanej; Chauffour, Aurelie; Vittecoq, Marion; Hoh, Francois; Thomas, Frederic; Sougakoff, Wladimir; Lionne, Corinne; Yssel, Hans; Misse, Dorothee. "Aedesin: structure and antimicrobial activity against multidrug resistant bacterial strains" Plos One 9, e105441-e105441 (2014).
Assembly members:
cecropin_GK, polymer, 36 residues, 3686.604 Da.
Natural source: Common Name: yellow fever mosquito Taxonomy ID: 7159 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Aedes aegypti
Experimental source: Production method: chemical synthesis
Entity Sequences (FASTA):
cecropin_GK: GGLKKLGKKLEGAGKRVFKA
SEKALPVVVGIKAIGK
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 53 |
| 15N chemical shifts | 27 |
| 1H chemical shifts | 244 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | GK cecropin-like peptide | 1 |
Entities:
Entity 1, GK cecropin-like peptide 36 residues - 3686.604 Da.
Mature form of the immature, signal sequence-containing form MK
| 1 | GLY | GLY | LEU | LYS | LYS | LEU | GLY | LYS | LYS | LEU | ||||
| 2 | GLU | GLY | ALA | GLY | LYS | ARG | VAL | PHE | LYS | ALA | ||||
| 3 | SER | GLU | LYS | ALA | LEU | PRO | VAL | VAL | VAL | GLY | ||||
| 4 | ILE | LYS | ALA | ILE | GLY | LYS |
Samples:
sample_1: cecropin GK 0.784 mM; Na phosphate 5.00 mM; K phosphate 0.88 mM; NaCl 68.50 mM; KCl 1.35 mM
sample_2: cecropin GK 0.784 mM; Na phosphate 5.00 mM; K phosphate 0.88 mM; NaCl 68.50 mM; KCl 1.35 mM
sample_conditions_1: ionic strength: 0.090 M; pH: 7.4; pressure: 1 atm; temperature: 283 K
sample_conditions_2: ionic strength: 0.090 M; pH: 7.4; pressure: 1 atm; temperature: 302 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_2 |
| 2D 1H-13C HSQC | 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:
TOPSPIN v3.2, Bruker Biospin - collection
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution
CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
TALOS, Cornilescu, Delaglio and Bax - data analysis
NMR spectrometers:
- Bruker Avance 700 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts