BMRB Entry 17792
Click here to enlarge.
PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR17792
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: 3D solution structure of antimicrobial peptide aurelin PubMed: 23137541
Deposition date: 2011-07-20 Original release date: 2012-08-30
Authors: Shenkarev, Zakhar; Altukhov, Dmitry
Citation: Shenkarev, Zakhar; Panteleev, Pavel; Balandin, Sergey; Gizatullina, Albina; Altukhov, Dmitry; Finkina, Ekaterina; Kokryakov, Vladimir; Arseniev, Alexander; Ovchinnikova, Tatiana. "Recombinant expression and solution structure of antimicrobial peptide aurelin from jellyfish Aurelia aurita." Biochem. Biophys. Res. Commun. 429, 63-69 (2012).
Assembly members:
aurelin, polymer, 40 residues, 4313.036 Da.
Natural source: Common Name: jellyfish Taxonomy ID: 6145 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Aurelia aurita
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
aurelin: AACSDRAHGHICESFKSFCK
DSGRNGVKLRANCKKTCGLC
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 107 |
| 15N chemical shifts | 39 |
| 1H chemical shifts | 255 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | aurelin | 1 |
Entities:
Entity 1, aurelin 40 residues - 4313.036 Da.
| 1 | ALA | ALA | CYS | SER | ASP | ARG | ALA | HIS | GLY | HIS | |
| 2 | ILE | CYS | GLU | SER | PHE | LYS | SER | PHE | CYS | LYS | |
| 3 | ASP | SER | GLY | ARG | ASN | GLY | VAL | LYS | LEU | ARG | |
| 4 | ALA | ASN | CYS | LYS | LYS | THR | CYS | GLY | LEU | CYS |
Samples:
sample_1: aurelin, [U-100% 15N], 1 mM; H20 95%; D20 5%
sample_2: aurelin, [U-100% 15N], 1 mM; H20 95%; D20 5%
sample_3: aurelin, [U-100% 15N], 1 mM; D20 100%
sample_conditions_1: ionic strength: 0 M; pH: 4.5; pressure: 1 atm; temperature: 303 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 DQF-COSY | sample_3 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_2 | isotropic | sample_conditions_1 |
| 3D HNHA | sample_2 | isotropic | sample_conditions_1 |
| 3D HNHB | sample_2 | isotropic | sample_conditions_1 |
Software:
CYANA, Guntert, Mumenthaler and Wuthrich - data analysis
XEASY, Keller and Wuthrich - chemical shift assignment, peak picking
NMR spectrometers:
- Bruker Avance 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts