PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
24786171-4	2014	By employing Born-Oppenheimer ab initio QM/MM molecular dynamics simulations with umbrella sampling, a state-of-the-art approach to simulate enzyme reactions, we have characterized the covalent inhibition mechanism between AChE and the nerve toxin soman and determined its free energy profile for the first time.	oppenheimer	18-29	acetylcholinesterase (Cartwright blood group)	Homo sapiens	223-227	
20550161-8	2010	In comparison with previous theoretical investigations of the AChE catalytic mechanism, our current study clearly demonstrates the power and advantages of employing Born-Oppenheimer ab initio QM/MM MD simulations in characterizing enzyme reaction mechanisms.	oppenheimer	170-181	acetylcholinesterase (Cartwright blood group)	Homo sapiens	62-66	
22984913-4	2012	By employing Born-Oppenheimer ab initio QM/MM molecular dynamics simulations with umbrella sampling, a state-of-the-art approach to simulate enzyme reactions, we have characterized the aging mechanism of soman phosphonylated AChE and determined its free energy profile.	oppenheimer	18-29	acetylcholinesterase (Cartwright blood group)	Homo sapiens	225-229