BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 34468

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:
Data typeCount
13C chemical shifts220
15N chemical shifts68
1H chemical shifts346

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 64 residues - 6639.278 Da.

1   ASPTHRCYSGLYGLYGLYTYRGLYVALASP
2   GLNARGARGTHRASNSERPROCYSGLNALA
3   SERASNGLYASPARGHISPHECYSGLYCYS
4   ASPARGTHRGLYILEVALGLUCYSLYSGLY
5   GLYLYSTRPTHRGLUILEGLNASPCYSGLY
6   GLYALASERCYSARGGLYVALSERGLNGLY
7   GLYALAARGCYS

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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_2isotropicsample_conditions_2
2D 1H-13C HSQCsample_2isotropicsample_conditions_2
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_2
3D HN(COCA)CBsample_2isotropicsample_conditions_2
3D HNCACBsample_2isotropicsample_conditions_2
3D HN(CO)CAsample_2isotropicsample_conditions_2
3D HNCAsample_2isotropicsample_conditions_2
3D HNHAsample_2isotropicsample_conditions_2
3D 1H-15N TOCSYsample_2isotropicsample_conditions_2
3D HN(CA)COsample_2isotropicsample_conditions_2
3D HNCOsample_2isotropicsample_conditions_2
3D HCCH-TOCSYsample_2isotropicsample_conditions_2
3D 1H-13C NOESY aliphaticsample_2isotropicsample_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