BMRB Entry 17588

Name: Solution structure of the RXLR effector P. capsici AVR3a4
Published: 2012-05-09

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PDB ID: 2lc2
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR17588
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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution structure of the RXLR effector P. capsici AVR3a4

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:

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).
PubMed: 21821794

Assembly members:

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

Natural source:

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

Experimental source:

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

Entity Sequences (FASTA):

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

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	458
15N chemical shifts	110
1H chemical shifts	715

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	AVR3a4	1

Entities:

Entity 1, AVR3a4 108 residues - 12039.568 Da.

1

GLY

SER

GLY

SER

GLY

ASN

VAL

ASP

2

SER

ASN

GLN

ASN

LYS

ALA

SER

MET

LEU

GLN

3

ALA

ARG

LEU

ASN

ASP

GLU

ALA

GLY

THR

4

ARG

LEU

ARG

VAL

HIS

GLU

SER

ASP

5

THR

GLU

ARG

GLY

PHE

LEU

GLU

LYS

ALA

6

ALA

VAL

LYS

MET

ALA

LYS

ALA

ILE

MET

7

ALA

ASP

PRO

ASN

LYS

ALA

ASP

GLU

VAL

TYR

8

LYS

TRP

ALA

ASP

LYS

GLY

TYR

THR

LEU

9

THR

GLN

MET

SER

ASN

PHE

LEU

LYS

SER

LYS

10

THR

ALA

GLY

LYS

TYR

ASP

ARG

VAL

TYR

ASN

11

GLY

TYR

VAL

ILE

HIS

LEU

ASP

TYR

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:

Name	Sample	Sample state	Sample conditions
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_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