Protein structure prediction (PSP) is predicting the three-dimensional of protein from its amino acid sequence only based on the information hidden in the protein sequence. One of the efficient tools to describe this information is protein energy functions. Despite the advancements in biology and computer science, PSP is still a challenging problem due to its large protein conformation space and inaccurate energy functions. In this study, PSP is treated as a many-objective optimization problem and four conflicting energy functions are used as different objectives to be optimized. A novel Pareto-dominance-archive and Coordinated-selection-strategy-based Many-objective-optimizer (PCM) is proposed to perform the conformation search. In it, convergence and diversity-based selection metrics are used to enable PCM to find near-native proteins with well-distributed energy values, while a Pareto-dominance-based archive is proposed to save more potential conformations that can guide the search to more promising conformation areas. The experimental results on thirty-four benchmark proteins demonstrate the significant superiority of PCM in comparison with other single, multiple, and many-objective evolutionary algorithms. Additionally, the inherent characteristics of iterative search of PCM can also give more insights into the dynamic progress of protein folding besides the final predicted static tertiary structure. All these confirm that PCM is a fast, easy-to-use, and fruitful solution generation method for PSP.