BMRB Entry 52492

Name: Sequence-Specific Backbone assignment of the PP2A-binding domain (aa 62-108) of Eya3
Published: 2024-07-05

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52492

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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:

Sequence-Specific Backbone assignment of the PP2A-binding domain (aa 62-108) of Eya3

Deposition date:

2024-06-04

Original release date:

2024-07-05

Authors:

Godek, Rachel; Peti, Wolfgang; Page, Rebecca

Citation:

Citation: Godek, Rachel; Padi, Sathish; Peti, Wolfgang; Page, Rebecca. "Cryo-EM structures of PP2A:B55-Eya3 and PP2A:B55-p107 define PP2A:B55 substrate recruitment" .

Assembly members:

Assembly members:
entity_1, polymer, 51 residues, 5946.5 Da.

Natural source:

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: HMRSSNDYTSQMYSAKPYAH ILSVPVSETAYPGQTQYQTL QQTQPYAVYEE

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	152
15N chemical shifts	46
1H chemical shifts	46

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Eya3	1

Entities:

Entity 1, Eya3 51 residues - 5946.5 Da.

Human Eyes absent homolog 3; residues 62-108; Eya 3 starting with RSSNDY

1

HIS

MET

ARG

SER

ASN

ASP

TYR

THR

SER

2

GLN

MET

TYR

SER

ALA

LYS

PRO

TYR

ALA

HIS

3

ILE

LEU

SER

VAL

PRO

VAL

SER

GLU

THR

ALA

4

TYR

PRO

GLY

GLN

THR

GLN

TYR

GLN

THR

LEU

5

GLN

THR

GLN

PRO

TYR

ALA

VAL

TYR

GLU

6

GLU

Samples:

sample_1: Eya3, [U-99% 15N], 170 uM; Eya3, [U-99% 13C; U-99% 15N], 170 uM; Na2HPO4/NaH2PO4 10 mM; NaCl 200 mM; TCEP 0.5 mM

sample_conditions_1: ionic strength: 200 mM; pH: 6.5; pressure: 1 atm; temperature: 283 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1

Software:

CARA v1.9 - chemical shift assignment

TOPSPIN v4.1.4 - collection, processing

NMR spectrometers:

Bruker AVANCE NEO 800 MHz

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