Biological Magnetic Resonance Data Bank

A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 16241

Title: Plantaricin J in TFE   PubMed: 19538999

Deposition date: 2009-04-06 Original release date: 2009-06-25

Authors: Rogne, Per; Haugen, Christofer; Kristiansen, Per Eugen; Nissen-Meyer, Jon

Citation: Rogne, Per; Haugen, Christofer; Fimland, Gunnar; Nissen-Meyer, Jon; Kristiansen, Per Eugen. "Three-dimensional structure of the two-peptide bacteriocin plantaricin JK"  Peptides 30, 1613-1621 (2009).

Assembly members:
PlnJ, polymer, 25 residues, 2935.335 Da.

Natural source:   Common Name: Lactobacillus plantarum   Taxonomy ID: 1590   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Lactobacillus plantarum

Experimental source:   Production method: chemical synthesis

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts88
15N chemical shifts27
1H chemical shifts180
coupling constants19

Additional metadata:

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


Entity Assembly IDEntity NameEntity ID


Entity 1, PlnJ 25 residues - 2935.335 Da.



Unlabeled: PlnJ 1 mM; TFE, [U-99% 2H], 50%; TFA 0.1%; DSS 0.2 mM

sample_conditions_1: pH: 2.5; pressure: 1 atm; temperature: 297 K


NameSampleSample stateSample conditions
2D 1H-15N HSQCUnlabeledisotropicsample_conditions_1
2D 1H-13C HSQCUnlabeledisotropicsample_conditions_1
2D 1H-1H COSYUnlabeledisotropicsample_conditions_1
2D DQF-COSYUnlabeledisotropicsample_conditions_1
2D 1H-1H TOCSYUnlabeledisotropicsample_conditions_1
2D 1H-1H NOESYUnlabeledisotropicsample_conditions_1


TOPSPIN v1.3, Bruker Biospin - collection, processing

SPARKY, Goddard - chemical shift assignment, peak picking

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

ACME, Delaglio, Zhengrong and Bax - data analysis

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

Molmol v2k2, Koradi, Billeter and Wuthrich - data analysis

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

BMRB 16239
EMBL CAA64198 CCC77915
GB AAS21883 ABC59149 ACO06038 ADE08245 ADN97562
REF WP_003641973 WP_015379769 WP_033611278 YP_004888429

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