BMRB Entry 25474

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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/BMR25474
MolProbity Validation Chart

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Title:
NMR structure of Protegrin-3 (PG3) in the presence of DPC micelles
Deposition date:
2015-02-06
Original release date:
2015-03-23
Authors:
Usachev, K.; Efimov, S.; Kolosova, O.; Klochkova, E.; Aganov, A.; Klochkov, V.
Citation:

Citation: Usachev, Konstantin; Efimov, Sergey; Kolosova, Olga; Klochkova, Evelina; Aganov, Albert; Klochkov, Vladimir. "Antimicrobial peptide protegrin-3 adopt an antiparallel dimer in the presence of DPC micelles: a high-resolution NMR study"  J. Biomol. NMR 62, 71-79 (2015).
PubMed: 25786621

Assembly members:

Assembly members:
PG3_monomer, polymer, 18 residues, 2066.527 Da.

Natural source:

Natural source:   Common Name: not available   Taxonomy ID: not available   Superkingdom: not available   Kingdom: not available   Genus/species: not available not available

Experimental source:

Experimental source:   Production method: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
PG3_monomer: RGGGLCYCRRRFCVCVGR

Data sets:
Data typeCount
13C chemical shifts56
15N chemical shifts14
1H chemical shifts122

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Protegrin-3 (PG3)1

Entities:

Entity 1, Protegrin-3 (PG3) 18 residues - 2066.527 Da.

1   ARGGLYGLYGLYLEUCYSTYRCYSARGARG
2   ARGPHECYSVALCYSVALGLYARG

Samples:

sample_1: PG3_monomer 3 mg; TSP, [U-99% 2H], 0.01%; DPC, [U-99% 2H], 20 mg

sample_conditions_1: temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D DQF-COSYsample_1isotropicsample_conditions_1
2D 1H-1H COSYsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment, peak picking

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

X-PLOR_NIH, Schwieters, Kuszewski, Tjandra and Clore - structure solution

NMR spectrometers:

  • Bruker Avance 700 MHz

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