BMRB Entry 30889

Name: Solution NMR Structure of PawS-Derived Peptide PDP-24
Published: 2021-03-26

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PDB ID: 7m3u
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30889
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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:

Solution NMR Structure of PawS-Derived Peptide PDP-24

Deposition date:

2021-03-19

Original release date:

2021-03-26

Authors:

Payne, C.; Rosengren, K.

Citation:

Citation: Payne, Colton; Vadlamani, Grishma; Hajiaghaalipour, Fatemeh; Muhammad, Taj; Fisher, Mark; Andersson, Hakan; Goransson, Ulf; Clark, Richard; Bond, Charles; Mylne, Joshua; Rosengren, K Johan. "Solution NMR and racemic crystallography provide insights into a novel structural class of cyclic plant peptides" RSC Chem. Biol. 2, 1682-1691 (2021).
PubMed: 34977583

Assembly members:

Assembly members:
entity_1, polymer, 27 residues, 3038.417 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: GFCWQHTCLPSGCADFPWPV GHQCFPD

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	60
15N chemical shifts	22
1H chemical shifts	169

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 27 residues - 3038.417 Da.

1

GLY

PHE

CYS

TRP

GLN

HIS

THR

CYS

LEU

PRO

2

SER

GLY

CYS

ALA

ASP

PHE

PRO

TRP

PRO

VAL

3

GLY

HIS

GLN

CYS

PHE

PRO

ASP

Samples:

sample_1: PDP-24 2 mg/mL

sample_2: PDP-24 2 mg/mL

sample_conditions_1: ionic strength: 0 mM; pH: 3.5; pressure: 1 atm; temperature: 288 K

sample_conditions_2: ionic strength: 0 mM; pH: 3.5; pressure: 1 atm; temperature: 293 K

sample_conditions_3: ionic strength: 0 mM; pH: 3.5; pressure: 1 atm; temperature: 298 K

sample_conditions_4: ionic strength: 0 mM; pH: 3.5; pressure: 1 atm; temperature: 303 K

sample_conditions_5: ionic strength: 0 mM; pH: 3.5; pressure: 1 atm; temperature: 308 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_3
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_3
2D 1H-13C HSQC	sample_2	isotropic	sample_conditions_3
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_3
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_5
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_4
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_2

Software:

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement, structure calculation

CARA, Keller and Wuthrich - chemical shift assignment, peak picking

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

NMR spectrometers:

Bruker AVANCE III 900 MHz

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