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 17588

Title: Solution structure of the RXLR effector P. capsici AVR3a4   PubMed: 21821794

Deposition date: 2011-04-12 Original release date: 2012-05-09

Authors: Li, Hua; Koshiba, Seizo; Yaeno, Takashi; Sato, Manami; Watanabe, Satoru; Harada, Takushi; Shirasu, Ken; Kigawa, Takanori

Citation: Yaeno, Takashi; Li, Hua; Chaparro-Garcia, Angela; Schornack, Sebastian; Koshiba, Seizo; Watanabe, Satoru; Kigawa, Takanori; Kamoun, Sophien; Shirasu, Ken. "Phosphatidylinositol monophosphate-binding interface in the oomycete RXLR effector AVR3a is required for its stability in host cells to modulate plant immunity."  Proc. Natl. Acad. Sci. U.S.A. 108, 14682-14687 (2011).

Assembly members:
AVR3a4, polymer, 108 residues, 12039.568 Da.

Natural source:   Common Name: Phytophthora capsici   Taxonomy ID: 4784   Superkingdom: Eukaryota   Kingdom: not available   Genus/species: Phytophthora capsici

Experimental source:   Production method: recombinant technology   Host organism: E. coli - cell free

Entity Sequences (FASTA):
AVR3a4: GSSGSSGNVDSNQNKASMLQ ARLNDEAGGTRLLRVHHESD TEERGFLEKAAVKKMAKAIM ADPNKADEVYKKWADKGYTL TQMSNFLKSKTAGKYDRVYN GYVIHLDY

Data sets:
Data typeCount
13C chemical shifts458
15N chemical shifts110
1H chemical shifts715

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1AVR3a41

Entities:

Entity 1, AVR3a4 108 residues - 12039.568 Da.

1   GLYSERSERGLYSERSERGLYASNVALASP
2   SERASNGLNASNLYSALASERMETLEUGLN
3   ALAARGLEUASNASPGLUALAGLYGLYTHR
4   ARGLEULEUARGVALHISHISGLUSERASP
5   THRGLUGLUARGGLYPHELEUGLULYSALA
6   ALAVALLYSLYSMETALALYSALAILEMET
7   ALAASPPROASNLYSALAASPGLUVALTYR
8   LYSLYSTRPALAASPLYSGLYTYRTHRLEU
9   THRGLNMETSERASNPHELEULYSSERLYS
10   THRALAGLYLYSTYRASPARGVALTYRASN
11   GLYTYRVALILEHISLEUASPTYR

Samples:

sample_1: AVR3a4, [U-100% 13C; U-100% 15N], 1.11 mM; TRIS, [U-100% 2H], 20 mM; sodium chloride 300 mM; DTT, [U-100% 2H], 1 mM; sodium azide 0.02%; D2O 10%; H2O 90%

sample_conditions_1: ionic strength: 320 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

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

Software:

CYANA v2.0.17, Guntert, Mumenthaler and Wuthrich - structure solution

TOPSPIN v2.1, Bruker Biospin - collection

NMRPipe v20090801, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRView v5.0.4, Johnson, One Moon Scientific - data analysis

Kujira v0.9843, Kobayashi, N. - data analysis

NMR spectrometers:

  • Bruker Avance 700 MHz

Related Database Links:

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