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

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