BMRB Entry 51682
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51682
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Title: Chemical_shift_FAM122A_29-120 PubMed: 38123684
Deposition date: 2022-11-01 Original release date: 2023-10-19
Authors: Vos, Margaret; Page, Rebecca; Peti, Wolfgang
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, 94 residues, 10405 Da.
Natural source: Common Name: Mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pTHMT
Entity Sequences (FASTA):
entity_1: HMGGGLRRSNSAPLIHGLSD
SSPVFQAEAPSARRNSTTFP
SRHGLLLPASPVRMHSSRLH
QIKQEEGMDLINRETVHERE
VQTAMQISHSWEES
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 243 |
| 15N chemical shifts | 83 |
| 1H chemical shifts | 83 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | FAM122A_29-120 | 1 |
Entities:
Entity 1, FAM122A_29-120 94 residues - 10405 Da.
FAM122A residues 29-120; 92 residues starting from with GGG
| 1 | HIS | MET | GLY | GLY | GLY | LEU | ARG | ARG | SER | ASN | ||||
| 2 | SER | ALA | PRO | LEU | ILE | HIS | GLY | LEU | SER | ASP | ||||
| 3 | SER | SER | PRO | VAL | PHE | GLN | ALA | GLU | ALA | PRO | ||||
| 4 | SER | ALA | ARG | ARG | ASN | SER | THR | THR | PHE | PRO | ||||
| 5 | SER | ARG | HIS | GLY | LEU | LEU | LEU | PRO | ALA | SER | ||||
| 6 | PRO | VAL | ARG | MET | HIS | SER | SER | ARG | LEU | HIS | ||||
| 7 | GLN | ILE | LYS | GLN | GLU | GLU | GLY | MET | ASP | LEU | ||||
| 8 | ILE | ASN | ARG | GLU | THR | VAL | HIS | GLU | ARG | GLU | ||||
| 9 | VAL | GLN | THR | ALA | MET | GLN | ILE | SER | HIS | SER | ||||
| 10 | TRP | GLU | GLU | SER |
Samples:
sample_1: FAM122A_29-120, [U-99% 15N], 400 uM; FAM122A_29-120, [U-99% 13C; U-99% 15N], 400 uM; Na2HPO4 20 mM; NaCl 150 mM; TCEP 0.5 mM
sample_conditions_1: ionic strength: 150 mM; pH: 6.3; pressure: 1 atm; temperature: 283 K
Experiments:
| 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 HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D (H)CC(CO)NH | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v4.1.1 - collection, processing
CARA vCARA_1.9 - chemical shift assignment
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