Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51881
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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).
PubMed: 38123684
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 type | Count |
13C chemical shifts | 280 |
15N chemical shifts | 96 |
1H chemical shifts | 96 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | ARPP19 | 1 |
Entity 1, ARPP19 114 residues - 12517 Da.
112 amino acid protein starting at "MSA"
1 | GLY | HIS | MET | SER | ALA | GLU | VAL | PRO | GLU | ALA | ||||
2 | ALA | SER | ALA | GLU | GLU | GLN | LYS | GLU | MET | GLU | ||||
3 | ASP | LYS | VAL | THR | SER | PRO | GLU | LYS | ALA | GLU | ||||
4 | GLU | ALA | LYS | LEU | LYS | ALA | ARG | TYR | PRO | HIS | ||||
5 | LEU | GLY | GLN | LYS | PRO | GLY | GLY | SER | ASP | PHE | ||||
6 | LEU | ARG | LYS | ARG | LEU | GLN | LYS | GLY | GLN | LYS | ||||
7 | TYR | PHE | ASP | SER | GLY | ASP | TYR | ASN | MET | ALA | ||||
8 | LYS | ALA | LYS | MET | LYS | ASN | LYS | GLN | LEU | PRO | ||||
9 | THR | ALA | ALA | PRO | ASP | LYS | THR | GLU | VAL | THR | ||||
10 | GLY | ASP | HIS | ILE | PRO | THR | PRO | GLN | ASP | LEU | ||||
11 | PRO | GLN | ARG | LYS | PRO | SER | LEU | VAL | ALA | SER | ||||
12 | LYS | LEU | ALA | GLY |
sample_1: ARPP19, [U-99% 15N], 500 uM; ARPP19, [U-99% 13C; U-99% 15N], 500 uM
sample_conditions_1: ionic strength: 150 mM; pH: 6.3; pressure: 1 atm; temperature: 283 K
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
3D HNCA | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
3D (H)CC(CO)NH | sample_1 | isotropic | sample_conditions_1 |
TOPSPIN - collection, processing
CARA - chemical shift assignment, peak picking
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks