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 51882

Title: MASTL-phosphorylated ARPP19   PubMed: 38123684

Deposition date: 2023-03-20 Original release date: 2023-03-23

Authors: Vos, Margaret; Peti, Wolfgang; Page, Rebecca

Citation: Padi, Sathish; Vos, Margaret; Godek, Rachel; Fuller, James; Kruse, Thomas; Hein, Jamin; Nilsson, Jakob; Kelker, Matthew; Page, Rebecca; Peti, Wolfgang. "Cryo-EM structures of PP2A:B55-FAM122A and PP2A:B55-ARPP19"  Nature 625, 195-203 (2024).

Assembly members:
entity_1, polymer, 114 residues, 12517 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: GHMSAEVPEAASAEEQKEME DKVTSPEKAEEAKLKARYPH LGQKPGGSDFLRKRLQKGQK YFDSGDYNMAKAKMKNKQLP TAAPDKTEVTGDHIPTPQDL PQRKPSLVASKLAG

Data sets:
Data typeCount
13C chemical shifts275
15N chemical shifts96
1H chemical shifts96

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1MASTL-phosphorylated ARPP191

Entities:

Entity 1, MASTL-phosphorylated ARPP19 114 residues - 12517 Da.

cAMP-regulated phosphoprotein 19, 112 amino acids starting from "MSA", S62 and S104 are phosphorylated.

1   GLYHISMETSERALAGLUVALPROGLUALA
2   ALASERALAGLUGLUGLNLYSGLUMETGLU
3   ASPLYSVALTHRSERPROGLULYSALAGLU
4   GLUALALYSLEULYSALAARGTYRPROHIS
5   LEUGLYGLNLYSPROGLYGLYSERASPPHE
6   LEUARGLYSARGLEUGLNLYSGLYGLNLYS
7   TYRPHEASPSEPGLYASPTYRASNMETALA
8   LYSALALYSMETLYSASNLYSGLNLEUPRO
9   THRALAALAPROASPLYSTHRGLUVALTHR
10   GLYASPHISILEPROTHRPROGLNASPLEU
11   PROGLNARGLYSPROSEPLEUVALALASER
12   LYSLEUALAGLY

Samples:

sample_1: MASTL-phosphorylated ARPP19, [U-99% 15N], 80 uM; MASTL-phosphorylated ARPP19, [U-99% 13C; U-99% 15N], 80 uM

sample_conditions_1: ionic strength: 150 mM; pH: 6.3; pressure: 1 atm; temperature: 283 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1

Software:

TOPSPIN vTopspin 4.1.1 - collection, processing

CARA - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker AVANCE NEO 600 MHz

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