TABLE 3.

ComQum-X results for the active site in myoglobin compound II (Hersleth et al., 2002)

					Distance to Fe (PM)
Ox. state	Ligand	His	wA	ΔEQM1 kJ/mol	NPor	NHis	O	O–N/H	Rfree	R
III	H2O	HID	0.25	41.9	202–209	212	206	259/107	0.20594	0.18058
III			1.0	56.2	199–206	210	200	262/107	0.20572	0.18020
III	OH−	HID	0.25	22.8	199–204	209	182	277/100	0.20560	0.18041
III			1.0	34.9	197–203	208	185	272/100	0.20561	0.18020
III		HIE	0.25	33.4	198–204	207	185	273/171	0.20565	0.18048
III			1.0	34.6	196–203	208	188	271/168	0.20568	0.18020
III		HIP	0.25	41.9	199–203	205	191	259/143	0.20594	0.18047
III			1.0	44.8	197–203	207	192	264/150	0.20577	0.18018
III	O2−	HIE	0.25	34.1	199–204	211	174	273/167	0.20587	0.18068
III			1.0	44.0	197–203	209	182	271/163	0.20579	0.18027
IV	OH−	HID	0.25	40.9	198–204	209	177	271/105	0.20573	0.18055
IV			1.0	47.9	197–203	209	183	271/104	0.20569	0.18024
IV		HIE	0.25	32.8	197–204	207	184	273/170	0.20567	0.18050
IV			1.0	34.4	196–203	208	187	270/168	0.20570	0.18027
IV		HIP	0.25	44.9	196–205	206	186	270/164	0.20564	0.18047
IV			1.0	45.9	195–204	207	189	270/163	0.20565	0.18020
IV	O2−	HIE	0.25	33.3	200–205	211	169	280/177	0.20587	0.18075
IV			1.0	46.2	197–204	210	176	276/173	0.20579	0.18037
IV		HIP	0.25	129.3	200–204	211	171	270/160	0.20572	0.18068
IV			1.0	152.2	197–204	210	179	271/161	0.20567	0.18032
V	O2−	HIE	0.25	41.4	200–204	210	169	277/174	0.20590	0.18075
V			1.0	51.5	197–204	209	176	274/170	0.20583	0.18037
V		HIP	0.25	125.1	200–204	210	170	275/167	0.20570	0.18062
V			1.0	146.5	197–203	209	178	274/167	0.20570	0.18033
Crystal					197–205	214	192	270/−	0.20593	0.18010

Fe–ligand distances, strain energies (ΔE_QM1), and R-factors are tabulated for the various oxidation and protonation states.