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 25460

Title: Solution structure of Fungus protein B9WZW9_MAGOR   PubMed: 26506000

Deposition date: 2015-01-30 Original release date: 2015-10-12

Authors: de Guillen, Karine

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).

Assembly members:
AVR-Pia, polymer, 97 residues, 8885.165 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

Entity Sequences (FASTA):
AVR-Pia: APQDNTSMGSSHHHHHHSSG RENLYFQGHMAAPARFCVYY DGHLPATRVLLMYVRIGTTA TITARGHEFEVEAKDQNCKV ILTNGKQAPDWLAAEPY

Data sets:
Data typeCount
13C chemical shifts228
15N chemical shifts81
1H chemical shifts510

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1AVR-Pia1

Entities:

Entity 1, AVR-Pia 97 residues - 8885.165 Da.

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

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

Samples:

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

15N: AVR-Pia, [U-15N], 1 ± 0.1 mM; D2O 10%; H2O 90%; potassium-sodium phosphate 20 mM; NaCl 150 mM

D2O: AVR-Pia 1 ± 0.1 mM; D2O 100%; potassium-sodium phosphate 20 mM; NaCl 150 mM

sample_conditions_1: ionic strength: 0.15 M; pH: 5.4; pressure: 1 atm; temperature: 305 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQC15Nisotropicsample_conditions_1
2D 1H-15N HSQC13C-15Nisotropicsample_conditions_1
3D HNCO13C-15Nisotropicsample_conditions_1
3D HNCA13C-15Nisotropicsample_conditions_1
3D HN(COCA)CB13C-15Nisotropicsample_conditions_1
3D HN(CO)CA13C-15Nisotropicsample_conditions_1
3D HNCACB13C-15Nisotropicsample_conditions_1
3D 1H-15N NOESY13C-15Nisotropicsample_conditions_1
3D 1H-15N TOCSY13C-15Nisotropicsample_conditions_1
2D 1H-1H NOESYD2Oisotropicsample_conditions_1
2D 1H-1H TOCSYD2Oisotropicsample_conditions_1
2D DQF-COSYD2Oisotropicsample_conditions_1

Software:

TOPSPIN v2.1, Bruker Biospin - collection, processing

CCPNMR, CCPN - data analysis

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 B9WZW9_MAGOR

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