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 27260

Title: Backbone chemical shift assignments of apo calmodulin bound to the NaV1.7 IQ motif peptide   PubMed: 29728980

Deposition date: 2017-09-20 Original release date: 2018-05-08

Authors: Isbell, Holly; Kilpatrick, Adina; Shea, Madeline

Citation: Isbell, Holly; Kilpatrick, Adina; Lin, Zesen; Mahling, Ryan; Shea, Madeline. "Backbone resonance assignments of complexes of apo human calmodulin bound to IQ motif peptides of voltage-dependent sodium channels NaV1.1, NaV1.4 and NaV1.7"  Biomol. NMR Assignments 12, 283-289 (2018).

Assembly members:
Calmodulin, polymer, 148 residues, Formula weight is not available
voltage-gated_sodium_channel_NaV1.7_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_NaV1.7_IQ_motif_peptide: GPGSKRKQEDVSATVIQRAY RRYRLRQNVKN

Data sets:
Data typeCount
13C chemical shifts518
15N chemical shifts171
1H chemical shifts171

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Calmodulin1
2NaV1.7 IQ Motif2

Entities:

Entity 1, Calmodulin 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, NaV1.7 IQ Motif 31 residues - Formula weight is not available

First four residues (GPGS) are part of a 3C protease cleavage site (numbered -4 to -1). NaV1.7 residue 1885 is residue 5 of the peptide.

1   GLYPROGLYSERLYSARGLYSGLNGLUASP
2   VALSERALATHRVALILEGLNARGALATYR
3   ARGARGTYRARGLEUARGGLNASNVALLYS
4   ASN

Samples:

sample_1: Calmodulin, [U-99% 13C; U-99% 15N], 1.0 mM; voltage-gated sodium channel NaV1.7 IQ motif peptide, [U-99% 13C; U-99% 15N], 1.0 mM; EDTA 0.1 mM; potassium chloride 100 mM; imidazole, [U-99% 2H], 10 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 HN(CO)CACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

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

NMR spectrometers:

  • Bruker Avance 500 MHz

Related Database Links:

UNP P62158 Q15858
NCBI 801 6335

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts