BMRB Entry 31168

Name: NMR solution structure of Paws Derived Peptide-25 (PDP-25)
Published: 2025-05-07

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PDB ID: 9bf4
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR31168
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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

NMR solution structure of Paws Derived Peptide-25 (PDP-25)

Deposition date:

2024-04-16

Original release date:

2025-05-07

Authors:

Hajiaghaalipour, F.; Wong, W.; Payne, C.; Fisher, M.; Clark, R.; Mylne, J.; Rosengren, K.

Citation:

Citation: Hajiaghaalipour, F.; Wong, W.; Payne, C.; Fischer, M.; Clark, R.; Mylne, J.; Rosengren, K.. "Paws Derived Peptides with two difulfides adopt different structural folds." .

Assembly members:

Assembly members:
entity_1, polymer, 31 residues, 3382.841 Da.

Natural source:

Natural source: Common Name: Zinnia haageana Taxonomy ID: 1525732 Superkingdom: Eukaryota Kingdom: Viridiplantae Genus/species: Zinnia haageana

Experimental source:

Experimental source: Production method: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GFCWGDLCVPYGTCSQLPPW LQDMCAAASFD

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	80
15N chemical shifts	27
1H chemical shifts	168

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 31 residues - 3382.841 Da.

1

GLY

PHE

CYS

TRP

GLY

ASP

LEU

CYS

VAL

PRO

2

TYR

GLY

THR

CYS

SER

GLN

LEU

PRO

TRP

3

LEU

GLN

ASP

MET

CYS

ALA

SER

PHE

4

ASP

Samples:

sample_1: PDP-25 2 mg/mL

sample_conditions_1: ionic strength: 0 mM; pH: 3.5; 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:

TopSpin, Bruker Biospin - collection, processing

CARA, Keller and Wuthrich - chemical shift assignment

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

CNS v1.21, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

NMR spectrometers:

Bruker AVANCE III HD 700 MHz

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