BMRB Entry 34170

Name: Solution structure of antifungal protein NFAP
Published: 2018-07-23

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PDB ID: 5oqs
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR34170
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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 structure of antifungal protein NFAP

Deposition date:

2017-08-14

Original release date:

2018-07-23

Authors:

Hajdu, D.; Czajlik, A.; Marx, F.; Galgoczy, L.; Batta, G.

Citation:

Citation: Hajdu, Dorottya; Huber, Anna; Czajlik, Andras; Toth, Liliana; Kele, Zoltan; Kocsube, Sandor; Fizil, Adam; Marx, Florentine; Galgoczy, Laszlo; Batta, Gyula. "Solution structure and novel insights into phylogeny and mode of action of the Neosartorya (Aspergillus) fischeri antifungal protein (NFAP)" Int. J. Biol. Macromol. 129, 511-522 (2019).
PubMed: 30738898

Assembly members:

Assembly members:
entity_1, polymer, 57 residues, 6639.575 Da.

Natural source:

Natural source: Common Name: Neosartorya fischeri Taxonomy ID: 331117 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Neosartorya fischeri

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Penicillium chrysogenum Vector: pSK275nfappaf_signal

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: LEYKGECFTKDNTCKYKIDG KTYLAKCPSAANTKCEKDGN KCTYDSYNRKVKCDFRH

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	218
15N chemical shifts	59
1H chemical shifts	347

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 57 residues - 6639.575 Da.

1

LEU

GLU

TYR

LYS

GLY

GLU

CYS

PHE

THR

LYS

2

ASP

ASN

THR

CYS

LYS

TYR

LYS

ILE

ASP

GLY

3

LYS

THR

TYR

LEU

ALA

LYS

CYS

PRO

SER

ALA

4

ALA

ASN

THR

LYS

CYS

GLU

LYS

ASP

GLY

ASN

5

LYS

CYS

THR

TYR

ASP

SER

TYR

ASN

ARG

LYS

6

VAL

LYS

CYS

ASP

PHE

ARG

HIS

Samples:

sample_1: acetic acid, [U-100% 2H], 20 mM; NFAP, [U-100% 15N], 1.1 mM; H2O 95%; D2O, [U-2H], 5%

sample_2: acetic acid, [U-100% 2H], 20 mM; NFAP, [U-100% 13C; U-100% 15N], 1 mM; H2O 95%; D2O, [U-2H], 5%

sample_conditions_1: ionic strength: 0.007 M; pH: 4.5; pressure: 1 atm; temperature: 298 K

sample_conditions_2: ionic strength: 0.007 M; pH: 4.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_2	isotropic	sample_conditions_2
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_2
2D 1H-13C HSQC	sample_2	isotropic	sample_conditions_2
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_2	isotropic	sample_conditions_2
3D HN(COCA)CB	sample_2	isotropic	sample_conditions_2
3D HNHA	sample_2	isotropic	sample_conditions_2
3D HN(CO)CA	sample_2	isotropic	sample_conditions_2
3D HNCACB	sample_2	isotropic	sample_conditions_2
3D HNCA	sample_2	isotropic	sample_conditions_2
3D 1H-15N TOCSY	sample_2	isotropic	sample_conditions_2
3D HNCO	sample_2	isotropic	sample_conditions_2

Software:

CARA v1.9.0, Keller and Wuthrich - chemical shift assignment

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure calculation

TALOS v+, Cornilescu, Delaglio and Bax - refinement

TOPSPIN v3.0, Bruker Biospin - processing

NMR spectrometers:

Bruker AvanceII 500.13 MHz
Bruker AvanceII 700.13 MHz

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