BMRB Entry 20032

Name: Solution structure of Gelatinase Biosynthesis-Activating Pheromone (GBAP), a 11-residue peptide lactone, from the Gram-positive bacterium Enterococcus faecalis
Published: 2009-04-04

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR20032

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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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

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:

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).
PubMed: 18996993

Assembly members:

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

Natural source:

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

Experimental source:

Experimental source: Production method: recombinant technology

Entity Sequences (FASTA):

Entity Sequences (FASTA):
GBAP: QNSPNIFGQWM

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
15N chemical shifts	10
1H chemical shifts	60

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	GBAP	1

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

GLN

ASN

SER

PRO

ASN

ILE

PHE

GLY

GLN

TRP

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:

Name	Sample	Sample state	Sample conditions
2D DQF-COSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_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 HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks