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 30068

Title: M. Oryzae effector AVR-Pia mutant H3   PubMed: 28087830

Deposition date: 2016-04-21 Original release date: 2017-03-23

Authors: Padilla, Andre; deGuillen, Karine

Citation: Ortiz, Diana; de Guillen, Karine; Cesari, Stella; Chalvon, Veronique; Gracy, Jerome; Padilla, Andre; Kroj, Thomas. "Recognition of the Magnaporthe oryzae Effector AVR-Pia by the Decoy Domain of the Rice NLR Immune Receptor RGA5."  Plant Cell 29, 156-168 (2017).

Assembly members:
Antivirulence protein AVR-Pia, polymer, 97 residues, 10830.049 Da.

Natural source:   Common Name: Rice blast fungus   Taxonomy ID: 318829   Superkingdom: Eukaryota   Kingdom: Fungi   Genus/species: Magnaporthe oryzae

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli BL21(DE3)

Entity Sequences (FASTA):
Antivirulence protein AVR-Pia: APQDNTSMGSSHHHHHHSSG RENLYFQGHMAAPARSCVYY DGHLPATRVLLMYVRIGNTA TITARGHEFEVEAKDQNCKV ILTNGKQAPDWLAAEPY

Data sets:
Data typeCount
13C chemical shifts152
15N chemical shifts75
1H chemical shifts522

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 97 residues - 10830.049 Da.

1   ALAPROGLNASPASNTHRSERMETGLYSER
2   SERHISHISHISHISHISHISSERSERGLY
3   ARGGLUASNLEUTYRPHEGLNGLYHISMET
4   ALAALAPROALAARGSERCYSVALTYRTYR
5   ASPGLYHISLEUPROALATHRARGVALLEU
6   LEUMETTYRVALARGILEGLYASNTHRALA
7   THRILETHRALAARGGLYHISGLUPHEGLU
8   VALGLUALALYSASPGLNASNCYSLYSVAL
9   ILELEUTHRASNGLYLYSGLNALAPROASP
10   TRPLEUALAALAGLUPROTYR

Samples:

sample_1: AVR-Pia-H3, [U-15N], 1 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 150 mM; pH: 5.4; pressure: 1 atm; temperature: 305 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-13C TOCSYsample_1isotropicsample_conditions_1

Software:

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

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

TOPSPIN v3.2, Bruker Biospin - chemical shift assignment

NMR spectrometers:

  • Bruker AvanceIII 700 MHz

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