BMRB Entry 18334

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/BMR18334
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title:
NMR spatial structure of the trypsin inhibitor BWI-2c from the buckwheat seeds
Deposition date:
2012-03-19
Original release date:
2012-05-29
Authors:
Mineev, Konstantin; Vassilevski, Alexander; Oparin, Peter; Grishin, Eugene; Egorov, Tsezi
Citation:

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).
PubMed: 22612157

Assembly members:

Assembly members:
bwi2c, polymer, 41 residues, 5196.967 Da.

Natural source:

Natural source:   Common Name: Common Buckwheat   Taxonomy ID: 3617   Superkingdom: Eukaryota   Kingdom: Viridiplantae   Genus/species: Fagopyrum esculentum

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-32b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
bwi2c: SEKPQQELEECQNVCRMKRW STEMVHRCEKKCEEKFERQQ R

Data sets:
Data typeCount
13C chemical shifts21
15N chemical shifts45
1H chemical shifts282

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1trypsin inhibitor BWI-2c1

Entities:

Entity 1, trypsin inhibitor BWI-2c 41 residues - 5196.967 Da.

1   SERGLULYSPROGLNGLNGLULEUGLUGLU
2   CYSGLNASNVALCYSARGMETLYSARGTRP
3   SERTHRGLUMETVALHISARGCYSGLULYS
4   LYSCYSGLUGLULYSPHEGLUARGGLNGLN
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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D HNHBsample_1isotropicsample_conditions_1
2D DQF-COSYsample_2isotropicsample_conditions_1
2D 1H-1H TOCSYsample_2isotropicsample_conditions_1
2D 1H-1H NOESYsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_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

Related Database Links:

PDB
SP P86794
AlphaFold P86794

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks