BMRB Entry 27996
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27996
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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).
PubMed: 32936779
Assembly members:
Calcineurin catalytic subunit A residues 27-348, polymer, 327 residues, Formula weight is not available
RCAN1 residues 128-164, polymer, 40 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: RP1B
Entity Sequences (FASTA):
Calcineurin catalytic subunit A residues 27-348: GHMHRLTAKEVFDNDGKPRV
DILKAHLMKEGRLEESVALR
IITEGASILRQEKNLLDIDA
PVTVCGDIHGQFFDLMKLFE
VGGSPANTRYLFLGDYVDRG
YFSIECVLYLWALKILYPKT
LFLLRGNHECRHLTEYFTFK
QECKIKYSERVYDACMDAFD
CLPLAALMNQQFLCVHGGLS
PEINTLDDIRKLDRFKEPPA
YGPMCDILWSDPLEDFGNEK
TQEHFTHNTVRGCSYFYSYP
AVCEFLQHNNLLSILRAHEA
QDAGYRMYRKSQTTGFPSLI
TIFSAPNYLDVYNNKAAVLK
YENNVMNIRQFNCSPHPYWL
PNFMDDD
RCAN1 residues 128-164: GHMNYDLLYAISKLGPGEKY
ELHAATDTTPSVVITVCESD
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 206 |
| 15N chemical shifts | 111 |
| 1H chemical shifts | 111 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Calcineurin | 1 |
| 2 | RCAN1 | 2 |
Entities:
Entity 1, Calcineurin 327 residues - Formula weight is not available
GHM are cloning artifact; calcineurin sequence starts with HRLT; the C-terminal DD are introduced to increase solubility.
| 1 | GLY | HIS | MET | HIS | ARG | LEU | THR | ALA | LYS | GLU | ||||
| 2 | VAL | PHE | ASP | ASN | ASP | GLY | LYS | PRO | ARG | VAL | ||||
| 3 | ASP | ILE | LEU | LYS | ALA | HIS | LEU | MET | LYS | GLU | ||||
| 4 | GLY | ARG | LEU | GLU | GLU | SER | VAL | ALA | LEU | ARG | ||||
| 5 | ILE | ILE | THR | GLU | GLY | ALA | SER | ILE | LEU | ARG | ||||
| 6 | GLN | GLU | LYS | ASN | LEU | LEU | ASP | ILE | ASP | ALA | ||||
| 7 | PRO | VAL | THR | VAL | CYS | GLY | ASP | ILE | HIS | GLY | ||||
| 8 | GLN | PHE | PHE | ASP | LEU | MET | LYS | LEU | PHE | GLU | ||||
| 9 | VAL | GLY | GLY | SER | PRO | ALA | ASN | THR | ARG | TYR | ||||
| 10 | LEU | PHE | LEU | GLY | ASP | TYR | VAL | ASP | ARG | GLY | ||||
| 11 | TYR | PHE | SER | ILE | GLU | CYS | VAL | LEU | TYR | LEU | ||||
| 12 | TRP | ALA | LEU | LYS | ILE | LEU | TYR | PRO | LYS | THR | ||||
| 13 | LEU | PHE | LEU | LEU | ARG | GLY | ASN | HIS | GLU | CYS | ||||
| 14 | ARG | HIS | LEU | THR | GLU | TYR | PHE | THR | PHE | LYS | ||||
| 15 | GLN | GLU | CYS | LYS | ILE | LYS | TYR | SER | GLU | ARG | ||||
| 16 | VAL | TYR | ASP | ALA | CYS | MET | ASP | ALA | PHE | ASP | ||||
| 17 | CYS | LEU | PRO | LEU | ALA | ALA | LEU | MET | ASN | GLN | ||||
| 18 | GLN | PHE | LEU | CYS | VAL | HIS | GLY | GLY | LEU | SER | ||||
| 19 | PRO | GLU | ILE | ASN | THR | LEU | ASP | ASP | ILE | ARG | ||||
| 20 | LYS | LEU | ASP | ARG | PHE | LYS | GLU | PRO | PRO | ALA | ||||
| 21 | TYR | GLY | PRO | MET | CYS | ASP | ILE | LEU | TRP | SER | ||||
| 22 | ASP | PRO | LEU | GLU | ASP | PHE | GLY | ASN | GLU | LYS | ||||
| 23 | THR | GLN | GLU | HIS | PHE | THR | HIS | ASN | THR | VAL | ||||
| 24 | ARG | GLY | CYS | SER | TYR | PHE | TYR | SER | TYR | PRO | ||||
| 25 | ALA | VAL | CYS | GLU | PHE | LEU | GLN | HIS | ASN | ASN | ||||
| 26 | LEU | LEU | SER | ILE | LEU | ARG | ALA | HIS | GLU | ALA | ||||
| 27 | GLN | ASP | ALA | GLY | TYR | ARG | MET | TYR | ARG | LYS | ||||
| 28 | SER | GLN | THR | THR | GLY | PHE | PRO | SER | LEU | ILE | ||||
| 29 | THR | ILE | PHE | SER | ALA | PRO | ASN | TYR | LEU | ASP | ||||
| 30 | VAL | TYR | ASN | ASN | LYS | ALA | ALA | VAL | LEU | LYS | ||||
| 31 | TYR | GLU | ASN | ASN | VAL | MET | ASN | ILE | ARG | GLN | ||||
| 32 | PHE | ASN | CYS | SER | PRO | HIS | PRO | TYR | TRP | LEU | ||||
| 33 | PRO | ASN | PHE | MET | ASP | ASP | ASP |
Entity 2, RCAN1 40 residues - Formula weight is not available
GHM are cloning artifact; RCAN1 sequence starts with NYDL
| 1 | GLY | HIS | MET | ASN | TYR | ASP | LEU | LEU | TYR | ALA | |
| 2 | ILE | SER | LYS | LEU | GLY | PRO | GLY | GLU | LYS | TYR | |
| 3 | GLU | LEU | HIS | ALA | ALA | THR | ASP | THR | THR | PRO | |
| 4 | SER | VAL | VAL | ILE | THR | VAL | CYS | GLU | SER | ASP |
Samples:
sample_1: Calcineurin catalytic subunit A residues 27-348, [U-13C; U-15N; U-2H], 0.13 mM; RCAN1 residues 128-164 0.65 mM; sodium phosphate 20 mM; sodium chloride 50 mM; TCEP 0.5 mM
sample_conditions_1: ionic strength: 50 mM; pH: 6.8; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N TROSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN, Bruker Biospin - collection, processing
CARA, Keller and Wuthrich - chemical shift assignment
NMR spectrometers:
- Bruker Avance 850 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks