Biological Magnetic Resonance Data Bank

A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 15259

Title: LactococcinGa in DPC and TFE   PubMed: 18187052

Deposition date: 2007-05-22 Original release date: 2008-02-21

Authors: Rogne, Per; Fimland, Gunnar; Nissen-Meyer, Jon; Kristiansen, Per

Citation: Rogne, Per; Fimland, Gunnar; Nissen-Meyer, Jon; Kristiansen, Per. "Three-dimensional structure of the two peptides that constitutes the two-peptide bacteriocin Lactococcin G"  Biochim. Biophys. Acta. 1784, 543-554 (2008).

Assembly members:
lcnGa, polymer, 39 residues, 4317.912 Da.

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

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pGEV2

Entity Sequences (FASTA):

Data sets:
Data typeCount
15N chemical shifts91
1H chemical shifts506

Additional metadata:

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Entity Assembly IDEntity NameEntity ID


Entity 1, lcnGa 39 residues - 4317.912 Da.



lcnGa_DPC: lcnGa, [U-15N], 1 mM; DPC, [U-2H], 200 mM; TFA 0.1%; D2O 10%; DSS 0.2 mM

lcnGaTFE: lcnG a TFE, [U-15N], 1 mM; TFE, [U-2H], 90%; TFA 0.1%; DSS 0.2 mM

25C: pH: 2.8; pressure: 1 atm; temperature: 298 K


NameSampleSample stateSample conditions
2D 1H-15N HSQClcnGa_DPCisotropic25C
2D 1H-1H NOESYlcnGa_DPCisotropic25C
2D 1H-1H TOCSYlcnGa_DPCisotropic25C
3D 1H-15N NOESYlcnGa_DPCisotropic25C
3D 1H-15N TOCSYlcnGa_DPCisotropic25C
2D 1H-15N HSQClcnGaTFEisotropic25C
2D 1H-1H TOCSYlcnGaTFEisotropic25C
2D 1H-1H NOESYlcnGaTFEisotropic25C
3D 1H-15N TOCSYlcnGaTFEisotropic25C
3D 1H-15N NOESYlcnGaTFEisotropic25C


VNMR, Varian - collection

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

CARA v1.4.1, Keller and Wuthrich - chemical shift assignment, data analysis

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

TALOS, Cornilescu, Delaglio and Bax - torsion angle prediction

Molmol v2k.2, Koradi, Billeter and Wuthrich - RMSD value calculation, Structure visualization

TOPSPIN v1.3, Bruker Biospin - collection, processing

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Bruker Avance 600 MHz

Related Database Links:


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