BMRB Entry 20032
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR20032
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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
- assigned_chemical_shifts
| Data type | Count |
| 15N chemical shifts | 10 |
| 1H chemical shifts | 60 |
Additional metadata:
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SPARKY: Backbone
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