BMRB Entry 30775

Name: Solution NMR structure of neuroVAL, a derived peptide from wasp
Published: 2020-12-14

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PDB ID: 7jgx
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30775
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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 NMR structure of neuroVAL, a derived peptide from wasp

Deposition date:

2020-07-20

Original release date:

2020-12-14

Authors:

Muller, J.; Craik, D.; Koehbach, J.

Citation:

Citation: Muller, Jessica; Lawrence, Nicole; Chan, Lai Yue; Harvey, Peta; Elliott, Alysha; Blaskovich, Mark; Goncalves, Jacqueline; Galante, Priscilla; Mortari, Marcia; Toffoli-Kadri, Monica; Koehbach, Johannes; Craik, David. "Antimicrobial and anticancer properties of synthetic peptides derived from the wasp Parachartergus fraternus" Chembiochem 22, 1415-1423 (2021).
PubMed: 33244888

Assembly members:

Assembly members:
entity_1, polymer, 14 residues, 1535.853 Da.

Natural source:

Natural source: Common Name: Parachartergus fraternus Taxonomy ID: 91406 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Parachartergus fraternus

Experimental source:

Experimental source: Production method: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: IFWLFRGKADVALX

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	41
15N chemical shifts	12
1H chemical shifts	87

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1

Entities:

Entity 1, unit_1 14 residues - 1535.853 Da.

1

ILE

PHE

TRP

LEU

PHE

ARG

GLY

LYS

ALA

ASP

2

VAL

ALA

LEU

NH2

Samples:

sample_1: peptide 1.0 mM

sample_conditions_1: pH: 3.9; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1

Software:

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

CcpNmr Analysis, CCPN - chemical shift assignment

NMR spectrometers:

Bruker AVANCE III HD 600 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks