BMRB Entry 25631

Name: structure of ace-pvhct-nh2
Published: 2015-06-15

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PDB ID: 2n30
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25631
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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:

structure of ace-pvhct-nh2

Deposition date:

2015-05-19

Original release date:

2015-06-15

Authors:

petit, vanessa; rolland, jean-luc; blond, alain; djediat, chakib; peduzzi, jean; goulard, christophe; bachere, evelyne; dupont, joelle; destoumieux-garzon, delphine; rebuffat, sylvie

Citation:

Citation: Petit, Vanessa; Rolland, Jean-luc; Blond, Alain; Djediat, Chakib; Peduzzi, Jean; Goulard, Christophe; Bachere, Evelyne; Dupont, Joelle; Destoumieux-garzon, Delphine; Rebuffat, Sylvie. "A hemocyanin-derived antimicrobial peptide from the penaeid shrimp adopts an alpha-helical structure that specifically permeabilizes fungal membranes" Biochim. Biophys. Acta 1860, 557-568 (2016).
PubMed: 26708991

Assembly members:

Assembly members:
entity_1, polymer, 25 residues, 2756.093 Da.

Natural source:

Natural source: Common Name: not available Taxonomy ID: not available Superkingdom: not available Kingdom: not available Genus/species: not available not available

Experimental source:

Experimental source: Production method: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: XFEDLPNFGHIQVKVFNHGE HIHHX

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
1H chemical shifts	154

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 25 residues - 2756.093 Da.

1

ACE

PHE

GLU

ASP

LEU

PRO

ASN

PHE

GLY

HIS

2

ILE

GLN

VAL

LYS

VAL

PHE

ASN

HIS

GLY

GLU

3

HIS

ILE

HIS

NH2

Samples:

sample_1: methanol, [U-99% 2H], 3.5 mM; entity_1 3.5 mM

sample_conditions_1: pressure: 1 atm; temperature: 303 K

Experiments:

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

Software:

xwinnmr v3.1, Bruker Biospin - chemical shift assignment, processing

TOPSPIN v3.2, Bruker Biospin - chemical shift assignment, processing

AURELIA v3.8, Neidig, Geyer, Gorler, Antz, Saffrich, Beneicke, Kalbitzer - data analysis, peak picking

X-PLOR v3.851, Brunger - refinement

NMR spectrometers:

Bruker Avance 400 MHz