BMRB Entry 25459

Title:
Solution structure of Fungus protein Q8J180_MAGGR
Deposition date:
2015-01-30
Original release date:
2015-10-12
Authors:
de Guillen, Karine
Citation:

Citation: de Guillen, Karine; Ortiz-Vallejo, Diana; Gracy, Jerome; Fournier, Elisabeth; Kroj, Thomas; Padilla, Andre. "Structure analysis uncovers a highly diverse but structurally conserved effector family in phytopathogenic fungi"  PLOS PATHOG. 11, e1005228-e1005228 (2015).
PubMed: 26506000

Assembly members:

Assembly members:
AVR1-CO39, polymer, 98 residues, 9136.090 Da.

Natural source:

Natural source:   Common Name: Rice blast fungus   Taxonomy ID: 148305   Superkingdom: Eukaryota   Kingdom: Fungi   Genus/species: Magnaporthe grisea

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-SP

Data sets:
Data typeCount
13C chemical shifts238
15N chemical shifts86
1H chemical shifts493

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1AVR1-CO391

Entities:

Entity 1, AVR1-CO39 98 residues - 9136.090 Da.

the sequence "APQDNTSMGSSHHHHHHSSGRENLYFQGHM" is the His-TAG and the TEV cleavage site

1   ALAPROGLNASPASNTHRSERMETGLYSER
2   SERHISHISHISHISHISHISSERSERGLY
3   ARGGLUASNLEUTYRPHEGLNGLYHISMET
4   ALATRPLYSASPCYSILEILEGLNARGTYR
5   LYSASPGLYASPVALASNASNILETYRTHR
6   ALAASNARGASNGLUGLUILETHRILEGLU
7   GLUTYRLYSVALPHEVALASNGLUALACYS
8   HISPROTYRPROVALILELEUPROASPARG
9   SERVALLEUSERGLYASPPHETHRSERALA
10   TYRALAASPASPASPGLUSERCYS

Samples:

13C-15N: AVR1-CO39, [U-13C; U-15N], 1 ± 0.1 mM; D2O 10%; H2O 90%; sodium phosphate 20 mM; NaCl 150 mM; DTT 1 mM

15N: AVR1-CO39, [U-15N], 1 ± 0.1 mM; D2O 10%; H2O 90%; sodium phosphate 20 mM; NaCl 150 mM; DTT 1 mM

D2O: AVR1-CO39 1 ± 0.1 mM; D2O 100%; sodium phosphate 20 mM; NaCl 150 mM; DTT 1 mM

H2O: AVR1-CO39 1 ± 0.1 mM; D2O 10%; H2O 90%; sodium phosphate 20 mM; NaCl 150 mM; DTT 1 mM

sample_conditions_1: ionic strength: 0.15 M; pH: 6.8; pressure: 1 atm; temperature: 305 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQC15Nisotropicsample_conditions_1
2D 1H-15N HSQC13C-15Nisotropicsample_conditions_1
2D 1H-13C HSQC13C-15Nisotropicsample_conditions_1
3D HNCO13C-15Nisotropicsample_conditions_1
3D HNCA13C-15Nisotropicsample_conditions_1
3D HN(COCA)CB13C-15Nisotropicsample_conditions_1
3D 1H-15N NOESY13C-15Nisotropicsample_conditions_1
3D 1H-15N TOCSY13C-15Nisotropicsample_conditions_1
2D 1H-1H NOESYH2Oisotropicsample_conditions_1
2D 1H-1H NOESYD2Oisotropicsample_conditions_1
2D 1H-1H TOCSYH2Oisotropicsample_conditions_1
2D DQF-COSYH2Oisotropicsample_conditions_1
3D HNCACB13C-15Nisotropicsample_conditions_1
3D HN(CO)CA13C-15Nisotropicsample_conditions_1

Software:

TOPSPIN v2.1, Bruker Biospin - collection, processing

CCPN, CCPN - data analysis, peak picking

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

TALOS+ v1.2, Cornilescu, Delaglio and Bax - data analysis

CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

NMR spectrometers:

  • Bruker Avance 700 MHz
  • Bruker Avance 500 MHz

Related Database Links:

UNP Q8J180_MAGGR
AlphaFold Q8J180

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