24276 J. Phys. Chem. B, Vol. 110, No. 47, 2006
2006, Volume 110B Kaori Fukuzawa,* Yuji Mochizuki, Shigenori Tanaka, Kazuo Kitaura, and Tatsuya Nakano: Molecular Interactions between Estrogen Receptor and Its Ligand Studied by the ab Initio Fragment Molecular Orbital Method The numerical results compiled in our published paper have slightly been changed by improving an inconsistency of the frozen-core setting in monomer and dimer treatments of the FMO-MP2 calculations. The corrected results, however, have not affected our qualitative discussions. In Table 2, the MP2 energies are corrected, and the discussions in the original paper referring to the numerical values of Table 2 should be superseded by those of the corrected table. Corrections for Figure 4, which are very minor, are available in the Supporting Information. Because the total IFIEs between the ligand and all residues of ER are corrected to -96.1 and -101.1 kcal/mol at the MP2/6-31G and 6-31G* levels, respectively, the statement in the original paper concerning the energy difference (30 kcal/mol) between these two levels should be replaced by the following statement (p 16107): The energies at the MP2/6-31G and 6-31G* levels were similar. The addition of the polarization function slightly affected the interaction with hydrophobic residues. Atomic charges and electron densities calculated at the MP2 level are also corrected (Figure 6). The numerical values in the original paper should be corrected after eq 3 (p 16108) as follows: The ∆q for Glu353 indicated a large positive value, 0.122 e, and that for EST indicated a similar negative value, -0.109 e. Those for Arg394 and His524 also indicated small negative values, -0.024 e and -0.017 e, respec-
Figure 6. The difference in electron densities (∆F) between complexed and individual component molecules; ∆F ) F(complex) - (F(ER) + F(ligand)) calculated at the MP2/6-31G* level. The stick representation refers to EST, a water molecule, and residues (Glu353, Thr347, Arg394, His524, and Leu525) with significant ∆F values. The line representation is the CR backbone. The red (minus) and blue (plus) represent the sign of the isosurfaces at (0.002 e/bohr3.
tively. The ∆q for Thr347 was smaller, 0.010 e, and this residue was therefore thought to have a lesser contribution to the CT interaction. The overall discussions about the results and conclusions of the original paper are not affected. Supporting Information Available: Figure 4 including numerical corrections for the MP2 energies. This material is available free of charge via the Internet at http://pubs.acs.org.
TABLE 2: IFIEs between EST and each amino acid residue of the ERa method basis set attractive interactions
repulsive interactions bcharged/polarized chydrophobic dtotal
HF STO-3G Glu353 His524 Arg394 Thr347 Water Glu330 Met522 Lys531 Asp351 Val392 Ala350 Glu542 Ala405 Asp538 Glu380 Arg412 Lys529 Gly344 Arg352 Leu391 Met388 Leu525 -54.48 12.02 -42.46
-39.28 -5.98 -5.27 -1.92 -1.02 -0.92 -0.82 -0.74 -0.71 -0.66 -0.64 -0.51 -0.49 -0.47 -0.45 -0.44 -0.38 -0.38 1.83 2.35 2.51 5.15
6-31G Glu353 Arg394 Thr347 His524 Met522 Met343 Water Glu330 Lys531 Met528 Gly344 Val392 Asp538 Ala350 Glu542 Leu346 Glu380 Arg436 Leu391 Arg352 Met388 Leu525 -50.42 4.95 -45.48
-27.92 -8.75 -5.41 -5.26 -2.44 -1.85 -1.59 -1.27 -1.02 -1.02 -1.00 -0.89 -0.77 -0.74 -0.72 -0.72 -0.67 -0.62 1.79 2.69 2.76 4.64
MP2 6-31G*
Glu353 Arg394 Thr347 His524 Met522 Met343 Glu330 Lys531 Met528 Gly344 Val392 Asp538 Glu542 Ala350 Arg412 Leu346 Glu380 Arg436 Leu391 Met388 Arg352 Leu525 -45.42 5.15 -40.26
-27.75 -7.10 -5.04 -3.89 -2.21 -1.58 -1.20 -0.92 -0.91 -0.84 -0.78 -0.74 -0.69 -0.66 -0.62 -0.61 -0.61 -0.60 1.68 2.38 2.52 4.41
6-31G** Glu353 Arg394 Thr347 His524 Met522 Met343 Glu330 Lys531 Met528 Gly344 Val392 Asp538 Glu542 Ala350 Arg412 Arg436 Glu380 Asp351 Leu391 Met388 Arg352 Leu525 -45.11 5.77 -39.34
-28.19 -7.00 -4.87 -3.61 -2.19 -1.57 -1.17 -0.87 -0.83 -0.79 -0.74 -0.73 -0.68 -0.62 -0.61 -0.60 -0.60 -0.57 1.70 2.35 2.43 4.53
6-31G Glu353 Arg394 His524 Thr347 Phe404 Met343 Leu346 Met522 Ala350 Leu387 Water Leu384 Met421 Met388 Glu330 Leu391 Ile424 Met528 Leu354 Glu419 Glu339 Arg352 -62.66 -33.46 -96.13
-29.59 -10.48 -8.74 -8.11 -4.46 -3.66 -3.59 -3.29 -3.07 -3.04 -2.90 -2.00 -1.94 -1.75 -1.27 -1.18 -1.17 -1.16 0.96 1.00 1.25 2.69
6-31G* Glu353 Arg394 His524 Thr347 Phe404 Leu387 Leu346 Met343 Met522 Ala350 Met388 Water Leu384 Met421 Leu391 Ile424 Glu330 Met528 Glu423 Glu419 Glu339 Arg352 -63.31 -37.77 -101.07
-32.23 -9.11 -8.80 -7.98 -5.12 -3.71 -3.60 -3.55 -3.32 -3.28 -2.52 -2.48 -2.12 -2.04 -1.63 -1.29 -1.20 -1.13 0.90 0.95 1.11 2.52
a Only selected values with stronger interactions are shown, and they are listed in order of the interaction energy values. Hydrophobic residues are indicated as bold characters. Energies are in kcal/mol. b Sum of all IFIEs between EST and each charged or polarized residue in the ER. c Sum of all IFIEs between EST and each hydrophobic residue in the ER. d Sum of all IFIEs between EST and each residue in the ER.
10.1021/jp065705n CCC: $33.50 © 2006 American Chemical Society Published on Web 11/08/2006
