TY - JOUR
T1 - Development of the four-body corrected fragment molecular orbital (FMO4) method
AU - Nakano, Tatsuya
AU - Mochizuki, Yuji
AU - Yamashita, Katsumi
AU - Watanabe, Chiduru
AU - Fukuzawa, Kaori
AU - Segawa, Katsunori
AU - Okiyama, Yoshio
AU - Tsukamoto, Takayuki
AU - Tanaka, Shigenori
N1 - Funding Information:
This work was supported by the RISS project at the Institute of Industrial Science (IIS) of the University of Tokyo. Y.M. and K.F. acknowledge the SFR-aid by Rikkyo University as well. Machine time of the Earth Simulator (ES2) was supplied by the Japan Agency for Marine-Earth Science and Technology (JAMSTEC). The authors thank Dr. Yuto Komeiji for critical comments on the manuscript.
Copyright:
Copyright 2012 Elsevier B.V., All rights reserved.
PY - 2012/1/27
Y1 - 2012/1/27
N2 - The four-body corrected fragment molecular orbital (FMO4) method was implemented at the second-order Møller-Plesset perturbation (MP2) level. A series of accuracy tests relative to the previous two-body and three-body treatments were performed. As expected, FMO4 provided better accuracy in total energies in comparison with the reference values by regular MO calculations. A nonconventional fragmentation by separating main and side chains in amino acid residues was examined for Ala-pentamer and Chignolin, where the four-body corrections were shown to be substantial. A large complex of HIV-1 protease (total 198 residues) with lopinavir was calculated as well. Furthermore, this new FMO scheme was successfully applied to adamantane-shaped clusters with three-dimensional bonding framework.
AB - The four-body corrected fragment molecular orbital (FMO4) method was implemented at the second-order Møller-Plesset perturbation (MP2) level. A series of accuracy tests relative to the previous two-body and three-body treatments were performed. As expected, FMO4 provided better accuracy in total energies in comparison with the reference values by regular MO calculations. A nonconventional fragmentation by separating main and side chains in amino acid residues was examined for Ala-pentamer and Chignolin, where the four-body corrections were shown to be substantial. A large complex of HIV-1 protease (total 198 residues) with lopinavir was calculated as well. Furthermore, this new FMO scheme was successfully applied to adamantane-shaped clusters with three-dimensional bonding framework.
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U2 - 10.1016/j.cplett.2011.12.004
DO - 10.1016/j.cplett.2011.12.004
M3 - Article
AN - SCOPUS:84855904082
SN - 0009-2614
VL - 523
SP - 128
EP - 133
JO - Chemical Physics Letters
JF - Chemical Physics Letters
ER -
