BMRB Entry 25944

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25944
MolProbity Validation Chart

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Title:
Solution structure of AVR3a_60-147 from Phytophthora infestans
Deposition date:
2016-01-08
Original release date:
2017-01-05
Authors:
Matena, Anja; Bayer, Peter; Zhukov, Igor; Stanek, Jan; Kozminski, Wiktor; van West, Pieter; Wawra, Stephan
Citation:

Citation: Wawra, Stephan; Trusch, Franziska; Matena, Anja; Apostolakis, Kostis; Linne, Uwe; Zhukov, Igor; Stanek, Jan; Kozminski, Wiktor; Davidson, Ian; Secombes, Chris; Bayer, Peter; van West, Pieter. "The RxLR Motif of the Host Targeting Effector AVR3a of Phytophthora infestans Is Cleaved before Secretion."  Plant Cell 29, 1184-1195 (2017).
PubMed: 28522546

Assembly members:

Assembly members:
entity, polymer, 102 residues, 11511.177 Da.

Natural source:

Natural source:   Common Name: potato late blight agent   Taxonomy ID: 4787   Superkingdom: Eukaryota   Kingdom: not available   Genus/species: Phytophthora infestans

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET21b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: PNFNLASLNEEMFNVAALTK RADAKKLAKQLMGNDKLADA AYIWWQHNRVTLDQIDTFLK LASRKTQGAKYNQIYNSYMM HLGLTGYEPNSSSVDKLAAA LE

Data sets:
Data typeCount
13C chemical shifts374
15N chemical shifts102
1H chemical shifts649

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 102 residues - 11511.177 Da.

Residues 88-102 represent a non-native linker to a 6-fold His-tag at the C-terminus of the protein.

1   PROASNPHEASNLEUALASERLEUASNGLU
2   GLUMETPHEASNVALALAALALEUTHRLYS
3   ARGALAASPALALYSLYSLEUALALYSGLN
4   LEUMETGLYASNASPLYSLEUALAASPALA
5   ALATYRILETRPTRPGLNHISASNARGVAL
6   THRLEUASPGLNILEASPTHRPHELEULYS
7   LEUALASERARGLYSTHRGLNGLYALALYS
8   TYRASNGLNILETYRASNSERTYRMETMET
9   HISLEUGLYLEUTHRGLYTYRGLUPROASN
10   SERSERSERVALASPLYSLEUALAALAALA
11   LEUGLU

Samples:

all_samples: Potassium phosphate 50 mM; D2O 10%; H2O 90%; DSS 50 uM; entity 300 uM

all_samples2: Potassium phosphate 50 mM; D2O 10%; H2O 90%; DSS 50 uM; entity, [U-100% 15N], 300 uM

all_samples3: Potassium phosphate 50 mM; D2O 10%; H2O 90%; DSS 50 uM; entity, [U-100% 13C; U-100% 15N], 300 uM

sample_conditions_1: ionic strength: 0.05 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCall_samplesisotropicsample_conditions_1
2D 1H-1H COSYall_samplesisotropicsample_conditions_1
2D 1H-1H TOCSYall_samplesisotropicsample_conditions_1
2D 1H-1H NOESYall_samplesisotropicsample_conditions_1
3D HCCH-COSYall_samplesisotropicsample_conditions_1
3D HCCH-TOCSYall_samplesisotropicsample_conditions_1
3D HBHANHall_samplesisotropicsample_conditions_1
3D HBHA(CO)NHall_samplesisotropicsample_conditions_1
13C-NOESY-HSQCall_samplesisotropicsample_conditions_1
15N-NOESY-HSQCall_samplesisotropicsample_conditions_1
3D HNCOall_samplesisotropicsample_conditions_1
4D HNCOCAall_samplesisotropicsample_conditions_1
4D HNCACOall_samplesisotropicsample_conditions_1
4D HBHACBCANHall_samplesisotropicsample_conditions_1

Software:

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

NMR spectrometers:

  • Bruker Avance 700 MHz
  • Varian VNMRS 700 MHz

Related Database Links:

UNP Q572D3
AlphaFold Q572D3

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