Here, we propose an alternative approach that encodes the Cβ chemical shifts as the signal intensity changes, instead of the splitting pattern, of the scalar-coupled Cα spins. This is accomplished by inserting a spin echo period and a z-filter just before the regular Cα evolution period. At the center of the echo period of the length 1/+2𝐽 $%$& ,, an encoding pulse, as we call it the BE (C-Beta chemical shift Encoding) pulse, is applied, which we carefully designed using the optimal control (OC) theory. In this design, the echo block of only 1/+2𝐽 $%$& ,, rather than a full 1/+𝐽 $%$& , period, is used to convert the Cα in-phase coherence to the anti-phase with respect to the Cα-Cβ scalar-coupling. Also, there is no need to resolve the J-splitting during the Cα evolution. Thus, the total transverse Cα evolution can be made well shorter than 20 ms, mitigating the T2' limitation. This opens up the concept of the nearest-neighbor encoding, for the first time, to solid proteins. Other previously reported spectral editing techniques that provide amino acid type information are based on DEPT 9 or constant-time HSQC by ' 𝐽 $( . Therefore, they are not applicable to perdeuterated protein samples. We demonstrate applicability of the BE-experiments under 70 kHz MAS condition to the signal assignment of a microcrystalline protein GB1. Applicability to membrane protein and larger crystalline protein are also discussed. The same method should be equally useful for solution NMR of large molecular-weight proteins.