BMRB Entry 30068

Name: M. Oryzae effector AVR-Pia mutant H3
Published: 2017-03-23

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PDB ID: 5jhj
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30068
MolProbity Validation Chart

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

M. Oryzae effector AVR-Pia mutant H3

Deposition date:

2016-04-21

Original release date:

2017-03-23

Authors:

Padilla, Andre; deGuillen, Karine

Citation:

Citation: Ortiz, Diana; de Guillen, Karine; Cesari, Stella; Chalvon, Veronique; Gracy, Jerome; Padilla, Andre; Kroj, Thomas. "Recognition of the Magnaporthe oryzae Effector AVR-Pia by the Decoy Domain of the Rice NLR Immune Receptor RGA5." Plant Cell 29, 156-168 (2017).
PubMed: 28087830

Assembly members:

Assembly members:
Antivirulence protein AVR-Pia, polymer, 97 residues, 10830.049 Da.

Natural source:

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

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli BL21(DE3) Vector: PET-SP

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Antivirulence protein AVR-Pia: APQDNTSMGSSHHHHHHSSG RENLYFQGHMAAPARSCVYY DGHLPATRVLLMYVRIGNTA TITARGHEFEVEAKDQNCKV ILTNGKQAPDWLAAEPY

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	152
15N chemical shifts	75
1H chemical shifts	522

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 97 residues - 10830.049 Da.

1

ALA

PRO

GLN

ASP

ASN

THR

SER

MET

GLY

SER

2

SER

HIS

SER

GLY

3

ARG

GLU

ASN

LEU

TYR

PHE

GLN

GLY

HIS

MET

4

ALA

PRO

ALA

ARG

SER

CYS

VAL

TYR

5

ASP

GLY

HIS

LEU

PRO

ALA

THR

ARG

VAL

LEU

6

LEU

MET

TYR

VAL

ARG

ILE

GLY

ASN

THR

ALA

7

THR

ILE

THR

ALA

ARG

GLY

HIS

GLU

PHE

GLU

8

VAL

GLU

ALA

LYS

ASP

GLN

ASN

CYS

LYS

VAL

9

ILE

LEU

THR

ASN

GLY

LYS

GLN

ALA

PRO

ASP

10

TRP

LEU

ALA

GLU

PRO

TYR

Samples:

sample_1: AVR-Pia-H3, [U-15N], 1 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 150 mM; pH: 5.4; pressure: 1 atm; temperature: 305 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C TOCSY	sample_1	isotropic	sample_conditions_1

Software:

CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

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

TOPSPIN v3.2, Bruker Biospin - chemical shift assignment

NMR spectrometers:

Bruker AvanceIII 700 MHz

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