BMRB Entry 30341

Name: PawL-Derived Peptide PLP-2
Published: 2018-03-01

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PDB ID: 6axi
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30341
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:

PawL-Derived Peptide PLP-2

Deposition date:

2017-09-06

Original release date:

2018-03-01

Authors:

Fisher, M.; Mylne, J.; Howard, M.

Citation:

Citation: Fisher, Mark; Zhang, Jingjing; Taylor, Nicolas; Howard, Mark; Berkowitz, Oliver; Debowski, Aleksandra; Behsaz, Bahar; Whelan, James; Pevzner, Pavel; Mylne, Joshua. "A family of small, cyclic peptides buried in preproalbumin since the Eocene epoch" Plant Direct 2, e00042-e00042 (2018).
PubMed: 30417166

Assembly members:

Assembly members:
ASP-LEU-PHE-VAL-PRO-PRO-ILE-ASP, polymer, 8 residues, 915.041 Da.

Natural source:

Natural source: Common Name: Senecio pinnatifolius Taxonomy ID: 904569 Superkingdom: Eukaryota Kingdom: Viridiplantae Genus/species: Senecio Pinnatifolius

Experimental source:

Experimental source: Production method: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
ASP-LEU-PHE-VAL-PRO-PRO-ILE-ASP: DLFVPPID

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
spectral_peak_list

Data type	Count
13C chemical shifts	26
1H chemical shifts	55

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 8 residues - 915.041 Da.

1

ASP

LEU

PHE

VAL

PRO

ILE

ASP

Samples:

sample_1: PLP-2 2.0 ± 0.2 mg/mL

sample_conditions_1: pH: 4.5; pressure: 1 atm; temperature: 298 K

Experiments:

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

Software:

CcpNMR v2.4.2, CCPN - data analysis

TOPSPIN v3.5, Bruker Biospin - collection

YASARA v16.7.22, Elmar Krieger - refinement, structure calculation

NMR spectrometers:

Bruker AvanceIII 600 MHz