BMRB Entry 34367

Name: NMR structure of peptide 8, characterized by a trans-4-cyclohexyl-Pro, with a dramatic reduction in activity on E. coli ATCC and lost effect on P. aeruginosa.
Published: 2019-10-10

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PDB ID: 6qxc
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34367
MolProbity Validation Chart

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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:

NMR structure of peptide 8, characterized by a trans-4-cyclohexyl-Pro, with a dramatic reduction in activity on E. coli ATCC and lost effect on P. aeruginosa.

Deposition date:

2019-03-07

Original release date:

2019-10-10

Authors:

Brancaccio, D.; Carotenuto, A.; Merlino, F.; Grieco, P.; Novellino, E.

Citation:

Citation: Buommino, E.; Carotenuto, A.; Antignano, I.; Bellavita, R.; Casciaro, B.; Loffredo, M.; Merlino, F.; Novellino, E.; Mangoni, M.; Nocera, F.; Brancaccio, D.; Punzi, P.; Roversi, D.; Ingenito, R.; Bianchi, E.; Grieco, P.. "The Outcomes of Decorated Prolines in the Discovery of Antimicrobial Peptides from Temporin-L." Chemmedchem 14, 1283-1290 (2019).
PubMed: 31087626

Assembly members:

Assembly members:
entity_1, polymer, 14 residues, 1692.120 Da.

Natural source:

Natural source: Common Name: Pseudis bolbodactyla Taxonomy ID: 428381 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Pseudis bolbodactyla

Experimental source:

Experimental source: Production method: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: FVXWFSKFLGRILX

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
spectral_peak_list
- spectral_peak_list_1

Data type	Count
1H chemical shifts	112

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 14 residues - 1692.120 Da.

1

PHE

VAL

PH6

TRP

PHE

SER

LYS

PHE

LEU

GLY

2

ARG

ILE

LEU

NH2

Samples:

sample_1: SDS, [U-100% 2H], 200 mM; D2O, [U-99% 2H], 10 % v/v; peptide 2 mM; H2O 90 % v/v

sample_conditions_1: ionic strength: 0 mM; pH: 5.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
1D 1H	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
2D DQF-COSY	sample_1	isotropic	sample_conditions_1

Software:

CYANA, Guntert P., Guntert, Mumenthaler and Wuthrich - refinement, structure calculation

CARA, Keller and Wuthrich - chemical shift assignment, peak picking

NMR - processing

NMR spectrometers:

Varian INOVA 700 MHz