BMRB Entry 25460

Name: Solution structure of Fungus protein B9WZW9_MAGOR
Published: 2015-10-12

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PDB ID: 2myw
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25460
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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:

Solution structure of Fungus protein B9WZW9_MAGOR

Deposition date:

2015-01-30

Original release date:

2015-10-12

Authors:

de Guillen, Karine

Citation:

Citation: de Guillen, Karine; Ortiz-Vallejo, Diana; Gracy, Jerome; Fournier, Elisabeth; Kroj, Thomas; Padilla, Andre. "Structure analysis uncovers a highly diverse but structurally conserved effector family in phytopathogenic fungi" PLOS PATHOG. 11, e1005228-e1005228 (2015).
PubMed: 26506000

Assembly members:

Assembly members:
AVR-Pia, polymer, 97 residues, 8885.165 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 Vector: pET-SP

Entity Sequences (FASTA):

Entity Sequences (FASTA):
AVR-Pia: APQDNTSMGSSHHHHHHSSG RENLYFQGHMAAPARFCVYY DGHLPATRVLLMYVRIGTTA TITARGHEFEVEAKDQNCKV ILTNGKQAPDWLAAEPY

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	228
15N chemical shifts	81
1H chemical shifts	510

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	AVR-Pia	1

Entities:

Entity 1, AVR-Pia 97 residues - 8885.165 Da.

the sequence "APQDNTSMGSSHHHHHHSSGRENLYFQGHM" is the His-TAG and the TEV cleavage site

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

PHE

CYS

VAL

TYR

5

ASP

GLY

HIS

LEU

PRO

ALA

THR

ARG

VAL

LEU

6

LEU

MET

TYR

VAL

ARG

ILE

GLY

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:

13C-15N: AVR-Pia, [U-13C; U-15N], 1 ± 0.1 mM; D2O 10%; H2O 90%; potassium-sodium phosphate 20 mM; NaCl 150 mM

15N: AVR-Pia, [U-15N], 1 ± 0.1 mM; D2O 10%; H2O 90%; potassium-sodium phosphate 20 mM; NaCl 150 mM

D2O: AVR-Pia 1 ± 0.1 mM; D2O 100%; potassium-sodium phosphate 20 mM; NaCl 150 mM

sample_conditions_1: ionic strength: 0.15 M; pH: 5.4; pressure: 1 atm; temperature: 305 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	15N	isotropic	sample_conditions_1
2D 1H-15N HSQC	13C-15N	isotropic	sample_conditions_1
3D HNCO	13C-15N	isotropic	sample_conditions_1
3D HNCA	13C-15N	isotropic	sample_conditions_1
3D HN(COCA)CB	13C-15N	isotropic	sample_conditions_1
3D HN(CO)CA	13C-15N	isotropic	sample_conditions_1
3D HNCACB	13C-15N	isotropic	sample_conditions_1
3D 1H-15N NOESY	13C-15N	isotropic	sample_conditions_1
3D 1H-15N TOCSY	13C-15N	isotropic	sample_conditions_1
2D 1H-1H NOESY	D2O	isotropic	sample_conditions_1
2D 1H-1H TOCSY	D2O	isotropic	sample_conditions_1
2D DQF-COSY	D2O	isotropic	sample_conditions_1

Software:

TOPSPIN v2.1, Bruker Biospin - collection, processing

CCPNMR, CCPN - data analysis

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

TALOS+ v1.2, Cornilescu, Delaglio and Bax - data analysis

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

NMR spectrometers:

Bruker Avance 700 MHz
Bruker Avance 500 MHz