BMRB Entry 25957

Name: Structure of D19S variant of the Penicillium Antifungal Protein (PAF)
Published: 2017-01-12

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PDB ID: 2nb0
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25957
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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:

Structure of D19S variant of the Penicillium Antifungal Protein (PAF)

Deposition date:

2016-01-18

Original release date:

2017-01-12

Authors:

Fizil, Adam; Batta, Gyula

Citation:

Citation: Sonderegger, Christoph; Fizil, Adam; Burtscher, Laura; Komaromi, Istvan; Czajlik, Andras; Munoz, Alberto; Hegedus, Nikoletta; Read, Nick; Batta, Gyula; Marx, Florentine. "D19S Mutation of the Cationic, Cysteine-Rich Protein PAF: Novel Insights into Its Structural Dynamics, Thermal Unfolding and Antifungal Function" Plos One 12, e0169920-e0169920 (2017).
PubMed: 28072824

Assembly members:

Assembly members:
PAFD19S, polymer, 55 residues, 6235.121 Da.

Natural source:

Natural source: Common Name: ascomycetes Taxonomy ID: 5076 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Penicillium chrisogenum

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Penicillium chrisogenum Vector: pSK275

Entity Sequences (FASTA):

Entity Sequences (FASTA):
PAFD19S: AKYTGKCTKSKNECKYKNSA GKDTFIKCPKFDNKKCTKDN NKCTVDTYNNAVDCD

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	112
15N chemical shifts	60
1H chemical shifts	278

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	PAFD19S	1

Entities:

Entity 1, PAFD19S 55 residues - 6235.121 Da.

1

ALA

LYS

TYR

THR

GLY

LYS

CYS

THR

LYS

SER

2

LYS

ASN

GLU

CYS

LYS

TYR

LYS

ASN

SER

ALA

3

GLY

LYS

ASP

THR

PHE

ILE

LYS

CYS

PRO

LYS

4

PHE

ASP

ASN

LYS

CYS

THR

LYS

ASP

ASN

5

ASN

LYS

CYS

THR

VAL

ASP

THR

TYR

ASN

6

ALA

VAL

ASP

CYS

ASP

Samples:

sample_1: PAFD19S, [U-100% 15N], 1.7 mM; D2O, [U-2H], 5 v/v; H2O 95 v/v; sodium chloride 40 mM; sodium phosphate 10 mM; potassium phosphate 0.04%

sample_conditions_1: ionic strength: 0.02 M; pH: 5.8; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	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
3D HNHA	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v2.1, Bruker Biospin - collection, processing

CARA v1.9, Keller and Wuthrich - chemical shift assignment, data analysis, peak picking

CYANA v2.1, Guntert, Braun and Wuthrich - structure solution

ATNOS-CANDID, Herrmann, Guntert and Wuthrich - chemical shift assignment, peak picking, structure solution

TALOS vTalos +, Cornilescu, Delaglio and Bax - refinement

NMR spectrometers:

Bruker Avance 500 MHz
Bruker DRX 700 MHz

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