Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27094
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Citation: Mahling, Ryan; Kilpatrick, Adina; Shea, Madeline. "Backbone resonance assignments of complexes of human voltage-dependent sodium channel NaV1.2 IQ motif peptide bound to apo calmodulin and to the C-domain fragment of apo calmodulin" Biomol. NMR Assignments 11, 297-303 (2017).
PubMed: 28823028
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
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
Data type | Count |
13C chemical shifts | 286 |
15N chemical shifts | 98 |
1H chemical shifts | 98 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks