BMRB Entry 18607

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18607
MolProbity Validation Chart

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Title:
Solution structure of an avirulence protein AvrPzi-t from pathogen Magnaportheoryzae
Deposition date:
2012-07-23
Original release date:
2013-02-14
Authors:
Zhang, Zhi-min; Zhang, Xu; Zhou, Ziren; Hu, Hong-yu; Liu, Miali; Zhou, Bo; Zhou, Jiahai
Citation:

Citation: Zhang, Zhi-Min; Zhang, Xu; Zhou, Zi-Ren; Hu, Hong-Yu; Liu, Maili; Zhou, Bo; Zhou, Jiahai. "Solution structure of the Magnaporthe oryzae avirulence protein AvrPiz-t."  J. Biomol. NMR 55, 219-223 (2013).
PubMed: 23334361

Assembly members:

Assembly members:
Avrpiz-t, polymer, 80 residues, 8751.062 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: ppSUMO

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Avrpiz-t: SFVQCNHHLLYNGRHWGTIR KKAGWAVRFYEEKPGQPKRL VAICKNASPVHCNYLKCTNL AAGFSAGTSTDVLSSGTVGS

Data sets:
Data typeCount
13C chemical shifts302
15N chemical shifts85
1H chemical shifts497

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1Avrpiz-t1

Entities:

Entity 1, Avrpiz-t 80 residues - 8751.062 Da.

1   SERPHEVALGLNCYSASNHISHISLEULEU
2   TYRASNGLYARGHISTRPGLYTHRILEARG
3   LYSLYSALAGLYTRPALAVALARGPHETYR
4   GLUGLULYSPROGLYGLNPROLYSARGLEU
5   VALALAILECYSLYSASNALASERPROVAL
6   HISCYSASNTYRLEULYSCYSTHRASNLEU
7   ALAALAGLYPHESERALAGLYTHRSERTHR
8   ASPVALLEUSERSERGLYTHRVALGLYSER

Samples:

sample_1: Avrpiz-t, [U-100% 13C; U-100% 15N], 0.3 mM; D2O 90%; H2O 10%

sample_2: Avrpiz-t, [U-100% 15N], 0.3 mM; D2O 100%

sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 293 K

sample_conditions_2: pH: 6.5; temperature: 293 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 HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_2
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1

Software:

ARIA, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax, Goddard, Linge, O'Donoghue and Nilges - chemical shift assignment, processing, structure solution

NMR spectrometers:

  • Bruker INOVA 800 MHz
  • Varian INOVA 600 MHz

Related Database Links:

PDB
EMBL CCC41985 CCD21890 CCD21891 CCD21894 CCD21896
GB ACF39937 AEX97148 EAQ70816 EHA46544 ELQ40553
REF XP_003721287

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