BMRB Entry 34279

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34279
MolProbity Validation Chart

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Title:
PLANTARICIN S-B IN 100 MM DPC MICELLES. THIS IS THE BETA PART OF THE BACTERIOCIN PLANTARICIN S
Deposition date:
2018-06-01
Original release date:
2019-03-04
Authors:
Ekblad, B.; Kristiansen, P.
Citation:

Citation: Ekblad, B.; Kristiansen, P.. "NMR structures and mutational analysis of the two peptides constituting the bacteriocin plantaricin S."  Sci. Rep. 9, 2333-2333 (2019).
PubMed: 30787405

Assembly members:

Assembly members:
Plantaricin S beta protein, polymer, 26 residues, 2877.255 Da.

Natural source:

Natural source:   Common Name: Lactobacillus plantarum   Taxonomy ID: 1590   Superkingdom: Bacteria   Kingdom: Terrabacteria   Genus/species: Lactobacillus plantarum

Experimental source:

Experimental source:   Production method: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Plantaricin S beta protein: KKKKQSWYAAAGDAIVSFGE GFLNAW

Data sets:
Data typeCount
13C chemical shifts82
15N chemical shifts27
1H chemical shifts185

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 26 residues - 2877.255 Da.

1   LYSLYSLYSLYSGLNSERTRPTYRALAALA
2   ALAGLYASPALAILEVALSERPHEGLYGLU
3   GLYPHELEUASNALATRP

Samples:

sample_1: Plantaricin S-b 1 ± 0.1 mM; H2O 95 ± 0.1 %; D2O, [U-2H], 5 ± 0.1 %; DPC, [U-2H], 100 ± 5 mM; DSS 0.2 ± 0.01 mM

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
1D protonsample_1isotropicsample_conditions_1
2D DQF-COSYsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1

Software:

CNS v1.3, Brunger, Adams, Clore, Gros, Nilges and Read - refinement, structure calculation

TALOS, Cornilescu, Delaglio and Bax - data analysis

CARA, Keller and Wuthrich - chemical shift assignment

SPARKY, Goddard - peak picking

TOPSPIN v2.4, Bruker Biospin - collection

NMR spectrometers:

  • Bruker AvanceII 600 MHz

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