BMRB Entry 34755

Name: NMR structure of the antimicrobial peptide Of-Pis1 in DPC micelles
Published: 2022-11-28

Click here to enlarge.

PDB ID: 8b1l
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34755
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

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

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

NMR structure of the antimicrobial peptide Of-Pis1 in DPC micelles

Deposition date:

2022-09-10

Original release date:

2022-11-28

Authors:

Alaimo, N.; Bischetti, M.; Gallo, M.; Cicero, D.

Citation:

Citation: Bischetti, M.; Alaimo, N.; Nardelli, F.; Punzi, P.; Amiariei, C.; Ingenito, R.; Musco, G.; Gallo, M.; Cicero, D.. "Structural insights on the selective interaction of the histidine-rich piscidin antimicrobial peptide Of-Pis1 with membranes" Biochim. Biophys. Acta Biomembr. 1865, 184080-184080 (2023).
PubMed: 36328080

Assembly members:

Assembly members:
entity_1, polymer, 24 residues, 2583.042 Da.

Natural source:

Natural source: Common Name: barred knifejaw Taxonomy ID: 163134 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Oplegnathus fasciatus

Experimental source:

Experimental source: Production method: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: FLGMLLHGVGHAIHGLIHGK QNVE

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
spectral_peak_list
- spectral_peak_list_1

Data type	Count
13C chemical shifts	84
1H chemical shifts	170

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1

Entities:

Entity 1, unit_1 24 residues - 2583.042 Da.

1

PHE

LEU

GLY

MET

LEU

HIS

GLY

VAL

GLY

2

HIS

ALA

ILE

HIS

GLY

LEU

ILE

HIS

GLY

LYS

3

GLN

ASN

VAL

GLU

Samples:

sample_1: Of-Pis1 3 mM; DPC, [U-2H], 60 mM; sodium phosphate 20 mM

sample_conditions_1: ionic strength: 40 mM; pH: 5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	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

Software:

TopSpin, Bruker Biospin - collection

NMRView, Johnson, One Moon Scientific - chemical shift assignment, data analysis, peak picking

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

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure calculation

NMR spectrometers:

Bruker AVANCE 600 MHz