Chemical shift assignments of the C-terminal domain of CaBP1 bound to the IQ-motif of voltage-gated Ca2+ channel (CaV1.2)

Figures

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  Fig. 1. A Two-dimensional 15N-1H HSQC NMR spectrum of 15N-labeled full-length CaBP1 (blue) and CaBP1C (red) both bound to unlabeled CaV1.2 IQ peptide at pH 7.5 recorded at 600-MHz 1H frequency. B Constant-time 13C-1H HSQC spectrum of 13C-labeled CaBP1C bound to unlabeled IQ peptide. C Expanded view of the spectrally crowded region from panel A. Representative assignments are indicated by the labeled peaks; complete assignments are available as BMRB accession no. 51518

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  Fig. 2. Secondary structure of CaBP1C bound to CaV1.2 IQ. TALOS ANN-secondary structure probability plotted as a function of residue number. Secondary structure elements are represented as green cylinders (helix) and blue arrows (β-strand)

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  Fig. 3. A Amide chemical shift perturbation for CaBP1C caused by the binding of IQ peptide. Chemical shift perturbation (CSP) was calculated as CSP = {(HNA–HNB)2 + (15NA–15NB)2}1/2. HNA and HNB are HN chemical shift of CaBP1C in the presence versus absence of IQ peptide, and 15NA and 15NB are 15N chemical shift of CaBP1C in the presence versus absence of IQ peptide. Chemical shifts of CaBP1C (in the absence of IQ) were obtained from BMRB 15623. B Crystal structure of the C-terminal domain of CaBP1 (Findeisen and Minor 2010). Exposed hydrophobic residues with the largest chemical shift perturbation are highlighted in red