Recently, the concept of "nearest-neighbor NMR" is proposed, that enables to guess the chemical shift range of the target spin by observing the scaler-coupled neighbor spin. This is accomplished without explicitly evolving the target spin, but instead by manipulating the spin-state of the target spins . For instance, in the HNCA experiments, the Cβ spin-states are flipped by band-selective inversion pulses applied at the center of the Cα evolution period. The splitting pattern of the observed Cα signal due to the 𝐽 $%$& coupling depends on the Cβ chemical shift and a particular design of the inversion pulse, enabling to guess the Cβ frequency range. However, to clearly identify a doublet for ' 𝐽 $$ of ~35 Hz for aliphatic C spins, ~20 Hz resolution or ~50 ms evolution is required. Even for perdeuterated proteins under 60 kHz MAS or protonated proteins under ~100 kHz MAS, T2' for Cα is typically <30 ms 8 , thus this method is not generally useful for solid protein samples.