BMRB Entry 27995
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27995
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Title: chemical shift assignments for phosphorylated RCAN1 residues 89-197 PubMed: 32936779
Deposition date: 2019-08-09 Original release date: 2020-07-09
Authors: Peti, Wolfgang; Li, Yang; Page, Rebecca
Citation: Li, Yang; Sheftic, Sarah; Grigoriu, Simina; Schwieters, Charles; Page, Rebecca; Peti, Wolfgang. "The structure of the RCAN1:CN complex explains the inhibition of and substrate recruitment by calcineurin" Sci. Adv. 6, 3681-3681 (2020).
Assembly members:
phosphorylated_RCAN1_89-197, polymer, 112 residues, Formula weight is not available
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):
phosphorylated_RCAN1_89-197: GHMLHIGSSHLAPPNPDKQF
LIXPPAXPPVGWKQVEDAXP
VINYDLLYAISKLGPGEKYE
LHAATDXXPSVVITVCESDQ
EKEEEEEMERMRRPKPKIIQ
TRRPEYXPIHLS
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 170 |
| 15N chemical shifts | 87 |
| 1H chemical shifts | 87 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | RCAN1 | 1 |
Entities:
Entity 1, RCAN1 112 residues - Formula weight is not available
GHM are cloning artifact; RCAN1 sequence starts with LHIG; residues S108, S112, T124, T152, T153 and T192 are phosphorylated.
| 1 | GLY | HIS | MET | LEU | HIS | ILE | GLY | SER | SER | HIS | ||||
| 2 | LEU | ALA | PRO | PRO | ASN | PRO | ASP | LYS | GLN | PHE | ||||
| 3 | LEU | ILE | SEP | PRO | PRO | ALA | SEP | PRO | PRO | VAL | ||||
| 4 | GLY | TRP | LYS | GLN | VAL | GLU | ASP | ALA | TPO | PRO | ||||
| 5 | VAL | ILE | ASN | TYR | ASP | LEU | LEU | TYR | ALA | ILE | ||||
| 6 | SER | LYS | LEU | GLY | PRO | GLY | GLU | LYS | TYR | GLU | ||||
| 7 | LEU | HIS | ALA | ALA | THR | ASP | TPO | TPO | PRO | SER | ||||
| 8 | VAL | VAL | ILE | THR | VAL | CYS | GLU | SER | ASP | GLN | ||||
| 9 | GLU | LYS | GLU | GLU | GLU | GLU | GLU | MET | GLU | ARG | ||||
| 10 | MET | ARG | ARG | PRO | LYS | PRO | LYS | ILE | ILE | GLN | ||||
| 11 | THR | ARG | ARG | PRO | GLU | TYR | TPO | PRO | ILE | HIS | ||||
| 12 | LEU | SER |
Samples:
sample_1: phosphorylated RCAN1 89-197, [U-99% 13C; U-99% 15N], 0.4 mM; HEPES 20 mM; sodium chloride 50 mM; TCEP 0.5 mM
sample_conditions_1: ionic strength: 50 mM; pH: 6.8; pressure: 1 atm; temperature: 283 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | 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 |
Software:
TOPSPIN, Bruker Biospin - collection, processing
CARA, Keller and Wuthrich - chemical shift assignment
NMR spectrometers:
- Bruker Avance 600 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts