BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 25636

Title: Solution structure of AVR-Pia   PubMed: 26362280

Authors: Ose, Toyoyuki; Oikawa, Azusa; Nakamura, Yukiko; Maenaka, Katsumi; Higuchi, Yuya; Satoh, Yuki; Fujiwara, Shiho; Demura, Makoto; Sone, Teruo

Citation: Ose, Toyoyuki; Oikawa, Azusa; Nakamura, Yukiko; Maenaka, Katsumi; Higuchi, Yuya; Satoh, Yuki; Fujiwara, Shiho; Demura, Makoto; Sone, Teruo; Kamiya, Masakatsu. "Solution structure of an avirulence protein, AVR-Pia, from Magnaporthe oryzae"  J. Biomol. NMR 63, 229-235 (2015).

Assembly members:
entity, polymer, 66 residues, 7391.511 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):
entity: APARFCVYYDGHLPATRVLL MYVRIGTTATITARGHEFEV EAKDQNCKVILTNGKQAPDW LAAEPY

Data sets:
Data typeCount
13C chemical shifts196
15N chemical shifts61
1H chemical shifts461
T1 relaxation values61
T2 relaxation values61
heteronuclear NOE values61

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 66 residues - 7391.511 Da.

1   ALAPROALAARGPHECYSVALTYRTYRASP
2   GLYHISLEUPROALATHRARGVALLEULEU
3   METTYRVALARGILEGLYTHRTHRALATHR
4   ILETHRALAARGGLYHISGLUPHEGLUVAL
5   GLUALALYSASPGLNASNCYSLYSVALILE
6   LEUTHRASNGLYLYSGLNALAPROASPTRP
7   LEUALAALAGLUPROTYR

Samples:

sample_1: AVR-Pia, [U-100% 13C; U-100% 15N], 1 mM; sodium phosphate 10 mM; sodium chloride 20 mM; D2O 10%; H2O 90%

sample_2: AVR-Pia 1 mM; sodium phosphate 10 mM; sodium chloride 20 mM; D2O 10%; H2O 90%

sample_conditions_1: ionic strength: 20 mM; pH: 6.5; pressure: 1 atm; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_2isotropicsample_conditions_1
2D 1H-1H NOESYsample_2isotropicsample_conditions_1
2D 1H-15N heteronuclear NOEsample_1isotropicsample_conditions_1
2D 1H-15N T1sample_1isotropicsample_conditions_1
2D 1H-15N T2sample_1isotropicsample_conditions_1

Software:

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

NMR spectrometers:

  • Bruker DMX 500 MHz
  • JEOL ECA 600 MHz

Related Database Links: