BMRB Entry 34731

Name: The NMR structure of the MAX47 effector from Magnaporthe Oryzae
Published: 2023-04-18

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PDB ID: 7zkd
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34731
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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:

The NMR structure of the MAX47 effector from Magnaporthe Oryzae

Deposition date:

2022-04-12

Original release date:

2023-04-18

Authors:

Lahfa, M.; Padilla, A.; de Guillen, K.; Pissarra, J.; Raji, M.; Cesari, S.; Kroj, T.; Gladieux, P.; Roumestand, C.; Barthe, P.

Citation:

Citation: Lahfa, M.; Padilla, A.; de Guillen, K.; Pissarra, J.; Raji, M.; Cesari, S.; Kroj, T.; Gladieux, P.; Roumestand, C.; Barthe, P.. "1H, 13C, 15N backbone and side-chain NMR assignments for three MAX effectors from Magnaporthe oryzae" Biomol. NMR Assign. 16, 305-309 (2022).
PubMed: 35657473

Assembly members:

Assembly members:
entity_1, polymer, 95 residues, 10780.053 Da.

Natural source:

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

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GPHMNNVMASSSSDTDSDSS PDRGLSRMCCVYKIHPGGNI WSTKKGEQAWFRRRFSKYEV MAYDRCNLEWGFSGKPRGLT FEFLWDKEAAADGTC

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	249
15N chemical shifts	93
1H chemical shifts	574

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 95 residues - 10780.053 Da.

1

GLY

PRO

HIS

MET

ASN

VAL

MET

ALA

SER

2

SER

ASP

THR

ASP

SER

ASP

SER

3

PRO

ASP

ARG

GLY

LEU

SER

ARG

MET

CYS

4

VAL

TYR

LYS

ILE

HIS

PRO

GLY

ASN

ILE

5

TRP

SER

THR

LYS

GLY

GLU

GLN

ALA

TRP

6

PHE

ARG

PHE

SER

LYS

TYR

GLU

VAL

7

MET

ALA

TYR

ASP

ARG

CYS

ASN

LEU

GLU

TRP

8

GLY

PHE

SER

GLY

LYS

PRO

ARG

GLY

LEU

THR

9

PHE

GLU

PHE

LEU

TRP

ASP

LYS

GLU

ALA

10

ALA

ASP

GLY

THR

CYS

Samples:

sample_1: MAX47, [U-15N], 0.5 mM; sodium acetate 25 mM; DTT 2 mM

sample_2: MAX47, [U-13C; U-15N], 0.5 mM; sodium acetate 25 mM; DTT 2 mM

sample_conditions_1: ionic strength: 0 mM; pH: 4.6; pressure: 1 atm; temperature: 305 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
3D HNCA	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D HN(CO)CA	sample_2	isotropic	sample_conditions_1
3D HN(COCA)CB	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1
3D HCACO	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 peaks
SPARKY: Backbone or all simulated peaks