BMRB Entry 25636

Name: Solution structure of AVR-Pia
Published: 2015-10-12

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PDB ID: 2n37
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25636
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: Solution structure of AVR-Pia PubMed: 26362280

Deposition date: 2015-05-28 Original release date: 2015-10-12

Authors: Ose, Toyoyuki; Oikawa, Azusa; Nakamura, Yukiko; Maenaka, Katsumi; Higuchi, Yuya; Satoh, Yuki; Fujiwara, Shiho; Demura, Makoto; Sone, Teruo

Citation: Ose, Toyoyuki; Oikawa, Azusa; Nakamura, Yukiko; Maenaka, Katsumi; Higuchi, Yuya; Satoh, Yuki; Fujiwara, Shiho; Demura, Makoto; Sone, Teruo; Kamiya, Masakatsu. "Solution structure of an avirulence protein, AVR-Pia, from Magnaporthe oryzae" J. Biomol. NMR 63, 229-235 (2015).

Assembly members:
entity, polymer, 66 residues, 7391.511 Da.

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

Experimental source: Production method: recombinant technology Host organism: Escherichia coli

Entity Sequences (FASTA):
entity: APARFCVYYDGHLPATRVLL MYVRIGTTATITARGHEFEV EAKDQNCKVILTNGKQAPDW LAAEPY

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
heteronucl_NOEs
- heteronuclear_noe_list_1
heteronucl_T1_relaxation
- heteronuclear_T1_list_1
heteronucl_T2_relaxation
- heteronuclear_T2_list_1

Data type	Count
13C chemical shifts	196
15N chemical shifts	61
1H chemical shifts	461
T1 relaxation values	61
T2 relaxation values	61
heteronuclear NOE values	61

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity	1

Entities:

Entity 1, entity 66 residues - 7391.511 Da.

1

ALA

PRO

ALA

ARG

PHE

CYS

VAL

TYR

ASP

2

GLY

HIS

LEU

PRO

ALA

THR

ARG

VAL

LEU

3

MET

TYR

VAL

ARG

ILE

GLY

THR

ALA

THR

4

ILE

THR

ALA

ARG

GLY

HIS

GLU

PHE

GLU

VAL

5

GLU

ALA

LYS

ASP

GLN

ASN

CYS

LYS

VAL

ILE

6

LEU

THR

ASN

GLY

LYS

GLN

ALA

PRO

ASP

TRP

7

LEU

ALA

GLU

PRO

TYR

Samples:

sample_1: AVR-Pia, [U-100% 13C; U-100% 15N], 1 mM; sodium phosphate 10 mM; sodium chloride 20 mM; D2O 10%; H2O 90%

sample_2: AVR-Pia 1 mM; sodium phosphate 10 mM; sodium chloride 20 mM; D2O 10%; H2O 90%

sample_conditions_1: ionic strength: 20 mM; pH: 6.5; pressure: 1 atm; temperature: 308 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_2	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_2	isotropic	sample_conditions_1
2D 1H-15N heteronuclear NOE	sample_1	isotropic	sample_conditions_1
2D 1H-15N T1	sample_1	isotropic	sample_conditions_1
2D 1H-15N T2	sample_1	isotropic	sample_conditions_1

Software:

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

NMR spectrometers:

Bruker DMX 500 MHz
JEOL ECA 600 MHz

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