BMRB Entry 18334
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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/BMR18334
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Title: NMR spatial structure of the trypsin inhibitor BWI-2c from the buckwheat seeds PubMed: 22612157
Deposition date: 2012-03-19 Original release date: 2012-05-29
Authors: Mineev, Konstantin; Vassilevski, Alexander; Oparin, Peter; Grishin, Eugene; Egorov, Tsezi
Citation: Oparin, Peter; Mineev, Konstantin; Dunaevsky, Yakov; Arseniev, Alexander; Belozersky, Mikhail; Grishin, Eugene; Egorov, Tsezi; Vassilevski, Alexander. "Buckwheat trypsin inhibitor with helical hairpin structure belongs to a new family of plant defence peptides." Biochem. J. 446, 69-77 (2012).
Assembly members:
bwi2c, polymer, 41 residues, 5196.967 Da.
Natural source: Common Name: Common Buckwheat Taxonomy ID: 3617 Superkingdom: Eukaryota Kingdom: Viridiplantae Genus/species: Fagopyrum esculentum
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
bwi2c: SEKPQQELEECQNVCRMKRW
STEMVHRCEKKCEEKFERQQ
R
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 21 |
| 15N chemical shifts | 45 |
| 1H chemical shifts | 282 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | trypsin inhibitor BWI-2c | 1 |
Entities:
Entity 1, trypsin inhibitor BWI-2c 41 residues - 5196.967 Da.
| 1 | SER | GLU | LYS | PRO | GLN | GLN | GLU | LEU | GLU | GLU | ||||
| 2 | CYS | GLN | ASN | VAL | CYS | ARG | MET | LYS | ARG | TRP | ||||
| 3 | SER | THR | GLU | MET | VAL | HIS | ARG | CYS | GLU | LYS | ||||
| 4 | LYS | CYS | GLU | GLU | LYS | PHE | GLU | ARG | GLN | GLN | ||||
| 5 | ARG |
Samples:
sample_1: bwi2c, [U-100% 15N], 1 mM; sodium azide 1 mM; sodium chloride 20 mM; H2O 90%; D2O 10%
sample_2: bwi2c 1 mM; sodium azide 1 mM; sodium chloride 20 mM; D2O 100%
sample_conditions_1: ionic strength: 20 mM; pH: 6.8; pressure: 1 atm; temperature: 273 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | 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 |
| 3D HNHA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNHB | sample_1 | isotropic | sample_conditions_1 |
| 2D DQF-COSY | 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 |
| 2D 1H-13C HSQC | sample_2 | isotropic | sample_conditions_1 |
Software:
CARA v1.8.3, Keller and Wuthrich - chemical shift assignment, data analysis, peak picking
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis, processing
TOPSPIN v2.1, Bruker Biospin - collection, processing
CYANA v3.0, Guntert, Mumenthaler and Wuthrich - data analysis, structure solution
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