BMRB Entry 30033
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30033
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Title: Solution Structure of Hge36: Scorpine-like Peptide from Hadrurus Gertschi
Deposition date: 2016-03-09 Original release date: 2016-06-24
Authors: Flores-Solis, D.; Rodriguez De La Vega, R.; del Rio-Portilla, F.
Citation: Flores-Solis, D.; Toledano-Magana, Y.; Rodriguez-Lima, O.; Rodriguez De La Vega, R.; Cano-Sanchez, P.; del Rio-Portilla, F.. "Solution Structure of Hge36: Scorpine-like Peptide from Hadrurus Gertschi" . ., .-..
Assembly members:
entity_1, polymer, 48 residues, 5310.272 Da.
Natural source: Common Name: Scorpion Taxonomy ID: 380989 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Hadrurus gertschi
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity_1: VHKMAKNQFGCFANVDVKGD
CKRHCKAEDKEGICHGTKCK
CGVPISYL
- assigned_chemical_shifts
- spectral_peak_list
Data type | Count |
13C chemical shifts | 139 |
15N chemical shifts | 50 |
1H chemical shifts | 331 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 48 residues - 5310.272 Da.
1 | VAL | HIS | LYS | MET | ALA | LYS | ASN | GLN | PHE | GLY | ||||
2 | CYS | PHE | ALA | ASN | VAL | ASP | VAL | LYS | GLY | ASP | ||||
3 | CYS | LYS | ARG | HIS | CYS | LYS | ALA | GLU | ASP | LYS | ||||
4 | GLU | GLY | ILE | CYS | HIS | GLY | THR | LYS | CYS | LYS | ||||
5 | CYS | GLY | VAL | PRO | ILE | SER | TYR | LEU |
Samples:
sample_1: Hge36 3.0 ± 0.1 mM
sample_2: Hge36, [U-13C; U-15N], 3.0 ± 0.1 mM
sample_conditions_1: ionic strength: 3 mM; pH: 3.0; pressure: 585 mmHg; temperature: 298 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D DQF-COSY | sample_1 | isotropic | sample_conditions_1 |
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_2 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC | sample_2 | isotropic | sample_conditions_1 |
3D HNCACB | sample_2 | isotropic | sample_conditions_1 |
3D HN(CO)CA | sample_2 | isotropic | sample_conditions_1 |
3D HNCA | sample_2 | isotropic | sample_conditions_1 |
3D HNCO | sample_2 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_2 | isotropic | sample_conditions_1 |
3D 1H-15N TOCSY | sample_2 | isotropic | sample_conditions_1 |
2D 1H-1H TOCSY | sample_2 | isotropic | sample_conditions_1 |
2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
AMBER, Case, Darden, Cheatham III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement
CARA, Keller and Wuthrich - chemical shift assignment, data analysis, peak picking
CYANA, Guntert, Mumenthaler and Wuthrich - chemical shift assignment, structure calculation
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMR spectrometers:
- Varian INOVA 500 MHz
- Bruker AvanceIII 700 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts