BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 27094

Title: Backbone chemical shift assignments of the apo calmodulin C-domain bound to the NaV1.2 IQ motif peptide   PubMed: 28823028

Authors: Mahling, Ryan; Kilpatrick, Adina; Shea, Madeline

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 ., .-. (2017).

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

Entity Sequences (FASTA):
Calmodulin_C-domain: MKDTDSEEEIREAFRVFDKD GNGYISAAELRHVMTNLGEK LTDEEVDEMIREADIDGDGQ VNYEEFVQMMTAK
Voltage-gated_sodium_channel_NaV1-2_IQ_motif_peptide: GPGSKRKQEEVSAIIIQRAY RRYLLKQKVKK

Data sets:
Data typeCount
13C chemical shifts286
15N chemical shifts98
1H chemical shifts98

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1Calmodulin C-domain1
2NaV1.2 IQ motif peptide2

Entities:

Entity 1, Calmodulin C-domain 73 residues - Formula weight is not available

Initial methionine is residue 76 of calmodulin.

1   METLYSASPTHRASPSERGLUGLUGLUILE
2   ARGGLUALAPHEARGVALPHEASPLYSASP
3   GLYASNGLYTYRILESERALAALAGLULEU
4   ARGHISVALMETTHRASNLEUGLYGLULYS
5   LEUTHRASPGLUGLUVALASPGLUMETILE
6   ARGGLUALAASPILEASPGLYASPGLYGLN
7   VALASNTYRGLUGLUPHEVALGLNMETMET
8   THRALALYS

Entity 2, NaV1.2 IQ motif peptide 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   GLYPROGLYSERLYSARGLYSGLNGLUGLU
2   VALSERALAILEILEILEGLNARGALATYR
3   ARGARGTYRLEULEULYSGLNLYSVALLYS
4   LYS

Samples:

sample_1: Calmodulin C-domain, [U-99% 13C; U-99% 15N], 0.85 mM; Voltage-gated sodium channel NaV1.2 IQ motif peptide, [U-99% 13C; U-99% 15N], 0.85 mM; potassium chloride 100 mM; imidazole 10 mM; sodium azide 0.01%; EDTA 0.1 mM

sample_conditions_1: ionic strength: 100 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1

Software:

VNMRJ v2.1B, Varian - collection

NMRPipe, (NMRpipe) Delaglio, Grzesiek, Vuister, Zhu, Pfeifer, and Bax - processing

Analysis, (Analysis) CCPN - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Varian INOVA 600 MHz

Related Database Links:

NCBI AAD45181.1 NP_001035232.1
UniProt P62158 Q99250