Extended Data Fig. 6: C^α-CEST profiles of ¹³C,¹⁵N-labeled L-ANAC046_319-338 peptide with 5% RST.

A concentration of 1 mM¹³C,¹⁵N-L-ANAC046_319-338 with 50 µM RST was used in the CEST experiment to ensure 5% saturation based on the Kd from ITC. The used pulse sequences modulate HSQCs as a function of i−1 carbon saturation. Hence the HSQC peak of residue e.g. S321 is modulated as a function of K320 carbon saturation. The profiles shown correspond to the C^α of the residue given at each plot. The pulse sequence used cannot probe the C^α of G325 in the peptide. The dots show the experimental data while the line shows the fit. The vertical grey dotted, and solid lines correspond to the chemical shift given from the fit of the peptide’s unbound and bound states, respectively. Residuals are shown above each plot. The additional smaller dips in the CEST profile of D328 could not be recaptured in the ¹⁵N-CEST or ¹³C’-CEST profiles, suggesting they originate form noise.