PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
8506114-4	1993	This preliminary data was reinforced by the affinity purification of AChE by immobilized post-infection IgG, and the immunoprecipitation of AChE activity from ES by post-infection IgG.	Einsteinium	159-161	acetylcholinesterase (Cartwright blood group)	Homo sapiens	140-144	
16854005-1	2005	Molecular dynamics (MD) simulations and hydrogen bonding energy (HBE) calculations have been performed on the prereactive enzyme-substrate complexes (ES), transition states (TS1), and intermediates (INT1) for acetylcholinesterase (AChE)-catalyzed hydrolysis of acetylcholine (ACh), butyrylcholinesterase (BChE)-catalyzed hydrolysis of ACh, and BChE-catalyzed hydrolysis of (+)/(-)-cocaine to examine the protein environmental effects on the catalytic reactions.	Einsteinium	150-152	acetylcholinesterase (Cartwright blood group)	Homo sapiens	209-229	
22064271-5	2011	This high activity of DHP was checked by molecular modeling which showed that DHP could not be considered as a bivalent ligand due to its incapability to occupy the esteratic site (ES) region of the 3D crystal structure of hAChE.	Einsteinium	181-183	acetylcholinesterase (Cartwright blood group)	Homo sapiens	223-228