BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 52492

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

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

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

Entity Sequences (FASTA):
entity_1: HMRSSNDYTSQMYSAKPYAH ILSVPVSETAYPGQTQYQTL QQTQPYAVYEE

Data sets:
Data typeCount
13C chemical shifts152
15N chemical shifts46
1H chemical shifts46

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1Eya31

Entities:

Entity 1, Eya3 51 residues - 5946.5 Da.

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

1   HISMETARGSERSERASNASPTYRTHRSER
2   GLNMETTYRSERALALYSPROTYRALAHIS
3   ILELEUSERVALPROVALSERGLUTHRALA
4   TYRPROGLYGLNTHRGLNTYRGLNTHRLEU
5   GLNGLNTHRGLNPROTYRALAVALTYRGLU
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:

NameSampleSample stateSample conditions
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_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 shifts
SPARKY: Backbone or all simulated shifts