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. 2022 Feb 2;16(1):147–151. doi: 10.1007/s12104-022-10072-9

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© The Author(s) 2022

Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 1 — Two-dimensional NMR spectra of CaM bound to unlabeled CNGB1-CaMBD peptide. A ¹⁵N–¹ H HSQC spectrum recorded at 600 MHz ¹H frequency was analyzed to determine backbone resonance assignments. B Expanded view of resonance assignments from the spectrally crowded region highlighted by the dashed box. C Constant-time ¹³C–¹H HSQC spectrum was analyzed to determine side chain resonance assignments. Representative resonance assignments are indicated by residue labels; complete assignments are available as BMRB accession no. 51222