BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 20032

Title: Solution structure of Gelatinase Biosynthesis-Activating Pheromone (GBAP), a 11-residue peptide lactone, from the Gram-positive bacterium Enterococcus faecalis   PubMed: 18996993

Deposition date: 2008-07-16 Original release date: 2009-04-04

Authors: Nagata, Koji; Nishiguchi, Kenzo; Kameda, Yasuhiro; Sonomoto, Kenji; Nakayama, Jiro; Tanokura, Masaru

Citation: Nishiguchi, Kenzo; Nagata, Koji; Tanokura, Masaru; Sonomoto, Kenji; Nakayama, Jiro. "Structure-Activity Relationship of Gelatinase Biosynthesis-Activating Pheromone of Enterococcus faecalis"  J. Bacteriol. 191, 641-650 (2009).

Assembly members:
GBAP, polymer, 11 residues, 1303.470 Da.

Natural source:   Common Name: Enterococcus faecalis   Taxonomy ID: 1351   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Enterococcus faecalis

Experimental source:   Production method: recombinant technology

Entity Sequences (FASTA):
GBAP: QNSPNIFGQWM

Data sets:
Data typeCount
15N chemical shifts10
1H chemical shifts60

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1GBAP1

Entities:

Entity 1, GBAP 11 residues - 1303.470 Da.

GBAP consists of 11 amino acid residues with a lactone linkage between the alpha-carboxyl group at the C-terminal Met11 and the gamma-hydroxyl group of Ser3.

1   GLNASNSERPROASNILEPHEGLYGLNTRP
2   MET

Samples:

sample_1: GBAP 1.5 mM; H2O 90%; D2O, [U-100% 2H], 10%

sample_conditions_1: pH: 6.0; temperature: 283 K

Experiments:

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

Software:

VNMR, Varian - collection

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

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

SPARKY, Goddard - chemical shift assignment

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

NMR spectrometers:

  • Varian INOVA 500 MHz

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