BMRB Entry 27801
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27801
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Title: Backbone 1H, 13C, and 15N chemical shift assignments for RCAN1 residues 128-164 PubMed: 32936779
Deposition date: 2019-02-25 Original release date: 2020-07-09
Authors: Peti, Wolfgang; Page, Rebecca; Li, Yang; Sheftic, Sarah; Grigoriu, Simina
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:
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: THMT
Entity Sequences (FASTA):
RCAN1_residues_128-164: GHMNYDLLYAISKLGPGEKY
ELHAATDTTPSVVITVCESD
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 65 |
15N chemical shifts | 34 |
1H chemical shifts | 34 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | RCAN1 residues 128-164 | 1 |
Entities:
Entity 1, RCAN1 residues 128-164 40 residues - Formula weight is not available
GHM are cloning artefact; 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: RCAN1 residues 128-164, [U-99% 15N], 0.6 mM; sodium phosphate 20 mM; sodium chloride 50 mM; TCEP 0.5 mM
sample_2: RCAN1 residues 128-164, [U-99% 13C; U-99% 15N], 0.6 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 HSQC | sample_1 | isotropic | sample_conditions_1 |
3D HNCA | sample_2 | isotropic | sample_conditions_1 |
3D HN(CO)CA | sample_2 | isotropic | sample_conditions_1 |
3D HNCACB | sample_2 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
Software:
TOPSPIN, Bruker Biospin - collection, processing
XEASY, 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