BMRB Entry 34468

Name: Solution structure of the antifungal protein PAFC
Published: 2020-10-23

Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR34468

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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 PAFC

Deposition date: 2019-12-19 Original release date: 2020-10-23

Authors: Czajlik, A.; Holzknecht, J.; Marx, F.; Batta, G.

Citation: Czajlik, A.; Holzknecht, J.; Marx, F.; Batta, G.. "Solution structure and dynamics of the antifungal protein PAFC" . ., .-..

Assembly members:
entity_1, polymer, 64 residues, 6639.278 Da.

Natural source: Common Name: Penicillium rubens Wisconsin 54-1255 Taxonomy ID: 500485 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Penicillium rubens

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

Entity Sequences (FASTA):
entity_1: DTCGGGYGVDQRRTNSPCQA SNGDRHFCGCDRTGIVECKG GKWTEIQDCGGASCRGVSQG GARC

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	220
15N chemical shifts	68
1H chemical shifts	346

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 64 residues - 6639.278 Da.

1

ASP

THR

CYS

GLY

TYR

GLY

VAL

ASP

2

GLN

ARG

THR

ASN

SER

PRO

CYS

GLN

ALA

3

SER

ASN

GLY

ASP

ARG

HIS

PHE

CYS

GLY

CYS

4

ASP

ARG

THR

GLY

ILE

VAL

GLU

CYS

LYS

GLY

5

GLY

LYS

TRP

THR

GLU

ILE

GLN

ASP

CYS

GLY

6

GLY

ALA

SER

CYS

ARG

GLY

VAL

SER

GLN

GLY

7

GLY

ALA

ARG

CYS

Samples:

sample_1: acetic acid, [U-100% 2H], 20 mM; PAFC 1.5 mM; H2O 95%; D2O, [U-2H], 5%

sample_2: acetic acid, [U-100% 2H], 20 mM; PAFC, [U-100% 13C; U-100% 15N], 650 uM; 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-15N HSQC	sample_2	isotropic	sample_conditions_2
2D 1H-13C HSQC	sample_2	isotropic	sample_conditions_2
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_2	isotropic	sample_conditions_2
3D HN(COCA)CB	sample_2	isotropic	sample_conditions_2
3D HNCACB	sample_2	isotropic	sample_conditions_2
3D HN(CO)CA	sample_2	isotropic	sample_conditions_2
3D HNCA	sample_2	isotropic	sample_conditions_2
3D HNHA	sample_2	isotropic	sample_conditions_2
3D 1H-15N TOCSY	sample_2	isotropic	sample_conditions_2
3D HN(CA)CO	sample_2	isotropic	sample_conditions_2
3D HNCO	sample_2	isotropic	sample_conditions_2
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_2
3D 1H-13C NOESY aliphatic	sample_2	isotropic	sample_conditions_2

Software:

TALOS vN, Cornilescu, Delaglio and Bax - refinement

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

CcpNmr Analysis v2.4.2, CCPN - chemical shift assignment, peak picking

TopSpin v3.1, Bruker Biospin - processing

NMR spectrometers:

Bruker AVANCE III 700.13 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts