BMRB Entry 16149

Title:
Plantaricin K in TFE
Deposition date:
2009-01-30
Original release date:
2009-06-25
Authors:
Rogne, Per; Haugen, Mads Christofer; Nissen-Meyer, Jon; Kristiansen, Per Eugen
Citation:

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).
PubMed: 19538999

Assembly members:

Assembly members:
PlnK, polymer, 32 residues, 3509.989 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
PlnK: RRSRKNGIGYAIGYAFGAVE RAVLGGSRDYNK

Data sets:
Data typeCount
13C chemical shifts114
15N chemical shifts31
1H chemical shifts215

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1PlnK1

Entities:

Entity 1, PlnK 32 residues - 3509.989 Da.

1   ARGARGSERARGLYSASNGLYILEGLYTYR
2   ALAILEGLYTYRALAPHEGLYALAVALGLU
3   ARGALAVALLEUGLYGLYSERARGASPTYR
4   ASNLYS

Samples:

sample_1: PlnK 1 mM; TFE, [U-99% 2H], 90%; H2O 10%; TFA 0.1%; DSS 0.2 mM

sample_conditions_1: pH: 2.5; pressure: 1 atm; temperature: 312 K

Experiments:

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

Software:

TOPSPIN v1.3, Bruker Biospin - collection, processing

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

SPARKY, Goddard - chemical shift assignment, data analysis, peak picking

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

Molmol v2k2, Koradi, Billeter and Wuthrich - data analysis

ACME v2001.006.11.26, Delaglio, Zhengrong and Bax - data analysis

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

BMRB 16148
PDB
EMBL CAA64197 CCC77914 CDN27149
GB AAS21882 ACO06037 ADE08244 ADN97561 AFJ79559
REF WP_003641972 WP_011100996 WP_033611279 YP_004888428

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