BMRB Entry 34278

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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/BMR34278
MolProbity Validation Chart

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Title:
Plantaricin S-a in 100 mM DPC micelles. This is the alpha 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 alpha protein, polymer, 27 residues, 2926.441 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 alpha protein: RNKLAYNMGHYAGKATIFGL AAWALLA

Data sets:
Data typeCount
13C chemical shifts67
15N chemical shifts24
1H chemical shifts200

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 27 residues - 2926.441 Da.

1   ARGASNLYSLEUALATYRASNMETGLYHIS
2   TYRALAGLYLYSALATHRILEPHEGLYLEU
3   ALAALATRPALALEULEUALA

Samples:

sample_1: Plantaricin Sb 1 ± 0.05 mM; DSS 0.2 ± 0.01 mM; DPC, [U-100% 2H], 100 ± 0.05 mM

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

Experiments:

NameSampleSample stateSample conditions
1D protonsample_1anisotropicsample_conditions_1
2D NOESYsample_1anisotropicsample_conditions_1
2D DQF-COSYsample_1anisotropicsample_conditions_1
2D TOCSYsample_1anisotropicsample_conditions_1
2D 1H-13C HSQCsample_1anisotropicsample_conditions_1
2D 1H-15N HSQCsample_1anisotropicsample_conditions_1

Software:

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

CARA, Keller and Wuthrich - chemical shift assignment

SPARKY, Goddard - peak picking

TOPSPIN v2.4, Bruker Biospin - collection

TALOS, Cornilescu, Delaglio and Bax - data analysis

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