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 27095

Title: Backbone chemical shift assignments of apo calmodulin 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, polymer, 148 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: ADQLTEEQIAEFKEAFSLFD KDGDGTITTKELGTVMRSLG QNPTEAELQDMINEVDADGN GTIDFPEFLTMMARKMKDTD SEEEIREAFRVFDKDGNGYI SAAELRHVMTNLGEKLTDEE VDEMIREADIDGDGQVNYEE FVQMMTAK
Voltage-gated_sodium_channel_NaV1-2_IQ_motif_peptide: GPGSKRKQEEVSAIIIQRAY RRYLLKQKVKK

Data typeCount
13C chemical shifts515
15N chemical shifts179
1H chemical shifts179

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Calmodulin, major conformer1
2Calmodulin, minor conformer1
3NaV1.2 IQ motif peptide, major conformer2
4NaV1.2 IQ motif peptide, minor conformer2

Entities:

Entity 1, Calmodulin, major conformer 148 residues - Formula weight is not available

Initial alanine is residue 1.

1   ALAASPGLNLEUTHRGLUGLUGLNILEALA
2   GLUPHELYSGLUALAPHESERLEUPHEASP
3   LYSASPGLYASPGLYTHRILETHRTHRLYS
4   GLULEUGLYTHRVALMETARGSERLEUGLY
5   GLNASNPROTHRGLUALAGLULEUGLNASP
6   METILEASNGLUVALASPALAASPGLYASN
7   GLYTHRILEASPPHEPROGLUPHELEUTHR
8   METMETALAARGLYSMETLYSASPTHRASP
9   SERGLUGLUGLUILEARGGLUALAPHEARG
10   VALPHEASPLYSASPGLYASNGLYTYRILE
11   SERALAALAGLULEUARGHISVALMETTHR
12   ASNLEUGLYGLULYSLEUTHRASPGLUGLU
13   VALASPGLUMETILEARGGLUALAASPILE
14   ASPGLYASPGLYGLNVALASNTYRGLUGLU
15   PHEVALGLNMETMETTHRALALYS

Entity 2, NaV1.2 IQ motif peptide, major conformer 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, [U-99% 13C; U-99% 15N], 0.95 mM; Voltage-gated sodium channel NaV1.2 IQ motif peptide, [U-99% 13C; U-99% 15N], 0.95 mM; imidazole, [U-99% 2H], 10 mM; potassium chloride 100 mM; EDTA 0.1 mM; sodium azide 0.01%

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