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We extend the Effective Fragment Molecular Orbital (EFMO) method to thefrozen domain approach where only the geometry of an active part is optimized,while the many-body polarization effects are considered for the whole system.The new approach efficiently mapped out the entire reaction path of chorismatemutase in less than four days using 80 cores on 20 nodes, where the wholesystem containing 2398 atoms is treated in the ab initio fashion without usingany force fields. The reaction path is constructed automatically with the onlyassumption of defining the reaction coordinate a priori. We determine thereaction barrier of chorismate mutase to be $18.3\pm 3.5$ kcal mol$^{-1}$ forMP2/cc-pVDZ and $19.3\pm 3.6$ for MP2/cc-pVTZ in an ONIOM approach usingEFMO-RHF/6-31G(d) for the high and low layers, respectively.

Mapping Enzymatic Catalysis using the Effective Fragment Molecular Orbital Method: Towards all ab initio Biochemistry