BMRB Entry 34027
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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/BMR34027
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NMR-STAR v3 text file.
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Title: NMR spatial structure of Tk-hefu peptide PubMed: 31533989
Deposition date: 2016-07-28 Original release date: 2017-08-11
Authors: Mineev, K.; Berkut, A.; Novikova, E.; Oparin, P.; Grishin, E.; Arseniev, A.; Vassilevski, A.
Citation: Berkut, Antonina; Chugunov, Anton; Mineev, Konstantin; Peigneur, Steve; Tabakmakher, Valentin; Krylov, Nikolay; Oparin, Peter; Lihonosova, Alyona; Novikova, Ekaterina; Arseniev, Alexander; Grishin, Eugene; Tytgat, Jan; Efremov, Roman; Vassilevski, Alexander. "Protein surface topography as a tool to enhance the selective activity of a potassium channel blocker" J. Biol. Chem. 294, 18349-18359 (2019).
Assembly members:
entity_1, polymer, 28 residues, 3565.082 Da.
Natural source: Common Name: Wheat Taxonomy ID: 376535 Superkingdom: Eukaryota Kingdom: Viridiplantae Genus/species: Triticum kiharae
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity_1: ADDRCYRMCQRYHDRREKKQ
CKEGCRYG
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 10 |
| 15N chemical shifts | 34 |
| 1H chemical shifts | 174 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 28 residues - 3565.082 Da.
| 1 | ALA | ASP | ASP | ARG | CYS | TYR | ARG | MET | CYS | GLN | ||||
| 2 | ARG | TYR | HIS | ASP | ARG | ARG | GLU | LYS | LYS | GLN | ||||
| 3 | CYS | LYS | GLU | GLY | CYS | ARG | TYR | GLY |
Samples:
sample_1: Tk-hefu, [U-99% 15N], 1 mM; sodium azide 0.001%
sample_conditions_1: ionic strength: 20 mM; pH: 5.7; pressure: 1 atm; temperature: 303 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D DQF-COSY | sample_1 | isotropic | sample_conditions_1 |
Software:
CARA v1.9.4, Keller and Wuthrich - chemical shift assignment
CYANA v3.97, Guntert, Mumenthaler and Wuthrich - structure calculation
TOPSPIN v3.2, Bruker Biospin - processing
NMR spectrometers:
- Bruker Avance 700 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts