BMRB Entry 26009

Name: Antimicrobial peptide protegrin PG-5
Published: 2016-09-29

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PDB ID: 2nc7
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR26009
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: Antimicrobial peptide protegrin PG-5 PubMed: 27589857

Deposition date: 2016-03-21 Original release date: 2016-09-29

Authors: Kolosova, Olga; Klochkova, Evelina; Aganov, Albert; Klochkov, Vladimir

Citation: Usachev, Konstantin; Kolosova, Olga; Klochkova, Evelina; Aganov, Albert; Klochkov, Vladimir; Usachev, Konstantin; Kolosova, Olga; Klochkova, Evelina; Aganov, Albert; Klochkov, Vladimir. "Oligomerization of the antimicrobial peptide Protegrin-5 in a membrane-mimicking environment. Structural studies by high-resolution NMR spectroscopy" Eur. Biophy. J. 46, 293-300 (2017).

Assembly members:
PG-5, polymer, 18 residues, 2106.591 Da.

Natural source: Common Name: Sus scrofa Taxonomy ID: 9823 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Sus scrofa

Experimental source: Production method: chemical synthesis

Entity Sequences (FASTA):
PG-5: RGGRLCYCRPRFCVCVGR

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
1H chemical shifts	119

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Antimicrobial peptide protegrin PG-5	1

Entities:

Entity 1, Antimicrobial peptide protegrin PG-5 18 residues - 2106.591 Da.

1

ARG

GLY

ARG

LEU

CYS

TYR

CYS

ARG

PRO

2

ARG

PHE

CYS

VAL

CYS

VAL

GLY

ARG

Samples:

sample_1: PG-5 3 mg/mL; DPC, [U-99% 2H], 20 mg/mL; H2O 450 uL; D2O, [U-99% 2H], 50 uL

sample_conditions_1: temperature: 293 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D DQF-COSY	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

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY, Goddard - chemical shift assignment, chemical shift calculation, peak picking

X-PLOR_NIH, Schwieters, Kuszewski, Tjandra and Clore - structure solution

NMR spectrometers:

Bruker Avance 700 MHz