BMRB Entry 16239

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16239
MolProbity Validation Chart

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Title:
Plantaricin J in DPC-micelles
Deposition date:
2009-04-03
Original release date:
2009-06-25
Authors:
Rogne, Per; Haugen, Christofer; Kristiansen, Per Eugen; Nissen-Meyer, Jon
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:
PlnJ, polymer, 25 residues, Formula weight is not available

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: recombinant technology   Host organism: Escherichia coli   Vector: pGEV2-PlnJ

Entity Sequences (FASTA):

Entity Sequences (FASTA):
PlnJ: GAWKNFWSSLRKGFYDGEAG RAIRR

Data sets:
Data typeCount
13C chemical shifts80
15N chemical shifts24
1H chemical shifts180
coupling constants18

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1PlnJ1

Entities:

Entity 1, PlnJ 25 residues - Formula weight is not available

1   GLYALATRPLYSASNPHETRPSERSERLEU
2   ARGLYSGLYPHETYRASPGLYGLUALAGLY
3   ARGALAILEARGARG

Samples:

sample_1: PlnJ, [U-95% 15N], 0.6 mM; DPC, [U-99% 2H], 100 mM; DSS 0.2 mM; D2O, [U-2H], 10%; TFA 0.1%; H2O 90%

sample_2: PlnJ 1 mM; DPC, [U-99% 2H], 170 mM; TFA 0.1%; DSS 0.2 mM; D2O, [U-2H], 10%; H2O 90%

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

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-1H COSYsample_1isotropicsample_conditions_1
2D DQF-COSYsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
2D 1H-1H COSYsample_2isotropicsample_conditions_1
2D DQF-COSYsample_2isotropicsample_conditions_1
2D 1H-1H TOCSYsample_2isotropicsample_conditions_1
2D 1H-1H NOESYsample_2isotropicsample_conditions_1

Software:

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 16241
PDB
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 peaks
SPARKY: Backbone or all simulated peaks