The Cα and Cβ chemical shifts are critical for the protein backbone resonance assignment. Here, we proposed a new approach that encodes the information of the Cβ chemical shift onto the signal intensity of its scalar-coupled Cα peak, rather than its J-splitting pattern. This allows to shorten the total transverse evolution time and opened the concept of the nearest neighbor NMR to systems with relatively short T2', including solid proteins and large molecular-weight proteins in solution. The encoding is achieved by inserting a spin-echo period with a refocusing pulse designed by the optimal control theory, which we dubbed the BE-block, just before the Cα evolution period. In this study, the BE-block were embedded into 3D-CANH and CAcoNH experiments, the minimum set of sequences for the sequential assignment, and validated for the sequential assignment of microcrystalline protein GB1. Without any user-intervention, an automated protocol correctly assigned 53 out of 55 residues using the BE-experiment and automated signal assignment program FLYA. Applications to more challenging proteins, Proteorhodopsin and Maltose Binding Protein, were also investigated, and we proposed a minimal dataset for a reasonable assignment success rate when combined with the present BE-experiments.