BMRB Entry 19832

Title:
Structure of the antimicrobial peptide LsbB in DPC micelles
Deposition date:
2014-03-05
Original release date:
2014-07-14
Authors:
Kristiansen, Per Eugen; Ovchinnikov, Kirill; Diep, Dzung Bao
Citation:

Citation: Ovchinnikov, Kirill; Kristiansen, Per; Uzelac, Gordana; Topisirovic, Ljubisa; Kojic, Milan; Nissen-Meyer, Jon; Nes, Ingolf; Diep, Dzung. "Defining the Structure and Receptor Binding Domain of the Leaderless Bacteriocin LsbB."  J. Biol. Chem. 289, 23838-23845 (2014).
PubMed: 24993828

Assembly members:

Assembly members:
Molecule_1, polymer, 30 residues, 3409.9902 Da.

Natural source:

Natural source:   Common Name: firmicutes   Taxonomy ID: 1358   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Lactococcus lactis

Experimental source:

Experimental source:   Production method: chemical synthesis   Host organism: not applicable

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Molecule_1: MKTILRFVAGYDIASHKKKT GGYPWERGKA

Data sets:
Data typeCount
13C chemical shifts98
15N chemical shifts28
1H chemical shifts230

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1antimicrobial peptide LsbB1

Entities:

Entity 1, antimicrobial peptide LsbB 30 residues - 3409.9902 Da.

1   METLYSTHRILELEUARGPHEVALALAGLY
2   TYRASPILEALASERHISLYSLYSLYSTHR
3   GLYGLYTYRPROTRPGLUARGGLYLYSALA

Samples:

sample_1: Molecule_1 1.0 ± 0.1 mM; DSS 0.2 ± 0.02 mM; DPC, [U-99% 2H], 200 ± 10 mM; H2O 95%; D2O 5%

sample_conditions_1: pressure: 1 atm; temperature: 298 K

Experiments:

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

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

SPARKY, Goddard - peak picking

TOPSPIN v2.4, Bruker Biospin - collection

CARA, Keller and Wuthrich - chemical shift assignment

TALOS v+, Cornilescu, Delaglio and Bax - data analysis

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

BMRB 19833
PDB
GB AAP73814 AGY45983
REF NP_861549 WP_011116717

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