BMRB Entry 34782

Name: The NMR structure of the MAX28 effector from Magnaporthe oryzae
Published: 2023-01-31

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PDB ID: 8c8a
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34782
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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: The NMR structure of the MAX28 effector from Magnaporthe oryzae PubMed: 35657473

Deposition date: 2023-01-19 Original release date: 2023-01-31

Authors: Lahfa, M.; Padilla, A.; de Guillen, K.; Kroj, T.; Roumestand, C.; Barthe, P.

Citation: Lahfa, Mounia; Padilla, Andre; de Guillen, Karine; Pissarra, Joana; Raji, Mouna; Cesari, Stella; Kroj, Thomas; Gladieux, Pierre; Roumestand, Christian; Barthe, Philippe. "1H, 13C, 15N backbone and side-chain NMR assignments for three MAX effectors from Magnaporthe oryzae" Biomol. NMR Assign. 16, 305-309 (2022).

Assembly members:
entity_1, polymer, 129 residues, 13135.021 Da.

Natural source: Common Name: Pyricularia oryzae 70-15 Taxonomy ID: 242507 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Pyricularia oryzae

Experimental source: Production method: recombinant technology Host organism: Escherichia coli BL21(DE3)

Entity Sequences (FASTA):
entity_1: GPHMAAPTPVPGIFDIFKKP VPTSCKLALTNGNKREVDAM LLPPSGTTILSDTSGAGVFT AKVNSKCEFTSVSPALPTGF KIEGSVDKEGKPPKSSTKPD TAAGTKPSTKPSTKTGSKTG TKTGTKAQA

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
15N chemical shifts	86
1H chemical shifts	562

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1

Entities:

Entity 1, unit_1 129 residues - 13135.021 Da.

1

GLY

PRO

HIS

MET

ALA

PRO

THR

PRO

VAL

2

PRO

GLY

ILE

PHE

ASP

ILE

PHE

LYS

PRO

3

VAL

PRO

THR

SER

CYS

LYS

LEU

ALA

LEU

THR

4

ASN

GLY

ASN

LYS

ARG

GLU

VAL

ASP

ALA

MET

5

LEU

PRO

SER

GLY

THR

ILE

LEU

6

SER

ASP

THR

SER

GLY

ALA

GLY

VAL

PHE

THR

7

ALA

LYS

VAL

ASN

SER

LYS

CYS

GLU

PHE

THR

8

SER

VAL

SER

PRO

ALA

LEU

PRO

THR

GLY

PHE

9

LYS

ILE

GLU

GLY

SER

VAL

ASP

LYS

GLU

GLY

10

LYS

PRO

LYS

SER

THR

LYS

PRO

ASP

11

THR

ALA

GLY

THR

LYS

PRO

SER

THR

LYS

12

PRO

SER

THR

LYS

THR

GLY

SER

LYS

THR

GLY

13

THR

LYS

THR

GLY

THR

LYS

ALA

GLN

ALA

Samples:

sample_1: MAX28, [U-15N], 0.4 mM; sodium phosphate 10 mM; sodium chloride 150 mM

sample_2: MAX28, [U-15N], 0.4 mM; sodium phosphate 10 mM; sodium chloride 150 mM

sample_conditions_1: ionic strength: 150 mM; pH: 6.8; pressure: 1 atm; temperature: 300 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_2	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_2	isotropic	sample_conditions_1
2D DQF-COSY	sample_2	isotropic	sample_conditions_1

Software:

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

CYANA v3.98.13, Guntert, Mumenthaler and Wuthrich - structure calculation

CINDY v2.1, Padilla, A. - chemical shift assignment

TopSpin v3.6, Bruker Biospin - peak picking

NMR spectrometers:

Bruker AVANCE III 700 MHz
Bruker AVANCE III 800 MHz

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