BMRB Entry 34891

Name: Solution structure of the antifungal protein NFAP2
Published: 2025-08-08

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34891

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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 the antifungal protein NFAP2

Deposition date:

2024-01-13

Original release date:

2025-08-08

Authors:

Czajlik, A.; Galgoczy, L.; Toth, L.; Ambrus, A.; Gai, J.; Batta, G.

Citation:

Citation: Czajlik, A.; Gai, J.; Galgoczy, L.; Toth, L.; Ambrus, A.; Batta, G.. "Solution Structure and Dynamical Properties of the Antifungal Miniprotein NFAP2" .

Assembly members:

Assembly members:
entity_1, polymer, 52 residues, 5573.350 Da.

Natural source:

Natural source: Common Name: Aspergillus fischeri NRRL 181 Taxonomy ID: 331117 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Aspergillus fischeri

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Penicillium rubens Wisconsin 54-1255 Vector: pSK275

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: IATSPYYACNCPNNCKHKKG SGCKYHSGPSDKSKVISGKC EWQGGQLNCIAT

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	186
15N chemical shifts	50
1H chemical shifts	313

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 52 residues - 5573.350 Da.

1

ILE

ALA

THR

SER

PRO

TYR

ALA

CYS

ASN

2

CYS

PRO

ASN

CYS

LYS

HIS

LYS

GLY

3

SER

GLY

CYS

LYS

TYR

HIS

SER

GLY

PRO

SER

4

ASP

LYS

SER

LYS

VAL

ILE

SER

GLY

LYS

CYS

5

GLU

TRP

GLN

GLY

GLN

LEU

ASN

CYS

ILE

6

ALA

THR

Samples:

sample_1: NFAP2, [U-10% 13C; U-100% 15N], 375 uM; acetic acid, [U-100% 2H], 20 mM; H2O 95%; D2O, [U-100% 2H], 5%

sample_conditions_1: ionic strength: 0.007 M; pH: 4.5; 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
3D HNHA	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(COCA)CB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1

Software:

X-PLOR NIH v3.8, Schwieters, Kuszewski, Tjandra and Clore - refinement

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

CcpNmr Analysis v2.5.2, CCPN - chemical shift assignment, peak picking

TopSpin v4.05, Bruker Biospin - processing

NMR spectrometers:

Bruker AVANCE NEO 700 MHz

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