BMRB Entry 27740
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27740
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Title: Backbone chemical shift assignments of the calcium-saturated human calmodulin C-domain bound to the human NaV1.2 IQ motif peptide PubMed: 33770503
Deposition date: 2018-12-21 Original release date: 2021-07-21
Authors: Mahling, Ryan; Shea, Madeline
Citation: Mahling, Ryan; Hovey, Liam; Isbell, Holly; Marx, Dagan; Miller, Mark; Kilpatrick, Adina; Weaver, Lisa; Yoder, Jesse; Kim, Elaine; Andresen, Corinne; Li, Shuxiang; Shea, Madeline. "Na V 1.2 EFL domain allosterically enhances Ca 2+ binding to sites I and II of WT and pathogenic calmodulin mutants bound to the channel CTD" Structure 29, 1339-1356 (2021).
Assembly members:
Calmodulin_C-domain, polymer, 73 residues, Formula weight is not available
voltage-gated_sodium_channel_NaV1.2_IQ_motif_peptide, polymer, 31 residues, Formula weight is not available
entity_CA, non-polymer, 40.078 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: pT7-7
Entity Sequences (FASTA):
Calmodulin_C-domain: MKDTDSEEEIREAFRVFDKD
GNGYISAAELRHVMTNLGEK
LTDEEVDEMIREADIDGDGQ
VNYEEFVQMMTAK
voltage-gated_sodium_channel_NaV1.2_IQ_motif_peptide: GPGSKRKQEEVSAIIIQRAY
RRYLLKQKVKK
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 291 |
| 15N chemical shifts | 97 |
| 1H chemical shifts | 97 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Calmodulin C-domain | 1 |
| 2 | Nav | 2 |
| 3 | Calcium, 1 | 3 |
| 4 | Calcium, 2 | 3 |
Entities:
Entity 1, Calmodulin C-domain 73 residues - Formula weight is not available
Initial methionine is residue 76 of calmodulin
| 1 | MET | LYS | ASP | THR | ASP | SER | GLU | GLU | GLU | ILE | ||||
| 2 | ARG | GLU | ALA | PHE | ARG | VAL | PHE | ASP | LYS | ASP | ||||
| 3 | GLY | ASN | GLY | TYR | ILE | SER | ALA | ALA | GLU | LEU | ||||
| 4 | ARG | HIS | VAL | MET | THR | ASN | LEU | GLY | GLU | LYS | ||||
| 5 | LEU | THR | ASP | GLU | GLU | VAL | ASP | GLU | MET | ILE | ||||
| 6 | ARG | GLU | ALA | ASP | ILE | ASP | GLY | ASP | GLY | GLN | ||||
| 7 | VAL | ASN | TYR | GLU | GLU | PHE | VAL | GLN | MET | MET | ||||
| 8 | THR | ALA | LYS |
Entity 2, Nav 31 residues - Formula weight is not available
First four residues (GPGS) are part of a 3C protease cleavage site (numbered -4 to -1). NaV1.2 residue 1901 is residue 5 of the peptide.
| 1 | GLY | PRO | GLY | SER | LYS | ARG | LYS | GLN | GLU | GLU | ||||
| 2 | VAL | SER | ALA | ILE | ILE | ILE | GLN | ARG | ALA | TYR | ||||
| 3 | ARG | ARG | TYR | LEU | LEU | LYS | GLN | LYS | VAL | LYS | ||||
| 4 | LYS |
Entity 3, Calcium, 1 - Ca - 40.078 Da.
| 1 | CA |
Samples:
sample_1: Calmodulin C-domain, [U-99% 13C; U-99% 15N], 0.8 mM; voltage-gated sodium channel NaV1.2 IQ motif peptide, [U-99% 13C; U-99% 15N], 0.8 mM; imidazole 10 mM; potassium chloride 100 mM; sodium azide 0.01 % w/v; calcium chloride, [U-99% 13C; U-99% 15N], 10 mM
sample_conditions_1: ionic strength: 120 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
Software:
VNMRJ, Varian - collection
NMRpipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
Analysis, CCPN - chemical shift assignment, data analysis, peak picking
NMR spectrometers:
- Varian INOVA 600 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts