PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
23474396-6	2013	Basic significance in AChE activity inhibition has the type of halogen in vinyl group.	Halogens	63-70	acetylcholinesterase (Cartwright blood group)	Homo sapiens	22-26	
18343905-8	2008	The results indicated that substitution of halogen and methyl groups by hydrogen at aromatic ring of the benzothiazepine decreased the affinity of these molecules towards enzyme that may be due to the polar non-polar repulsions of these moieties with the amino acid residues in the active site of AChE.	Halogens	43-50	acetylcholinesterase (Cartwright blood group)	Homo sapiens	297-301	
5689803-0	1968	Acetylcholinesterase hydrolysis of halogen substituted acetylcholines.	Halogens	35-42	acetylcholinesterase (Cartwright blood group)	Homo sapiens	0-20	
28629119-7	2017	Molecular docking analyses were conducted for potential AChE and BChE inhibitors, and the results demonstrated that the peripheral anionic sites of target proteins were predominant binding sites for these compounds through hydrogen bonds and halogen interactions instead of hydrophobic interactions in the catalytic active site.	Halogens	242-249	acetylcholinesterase (Cartwright blood group)	Homo sapiens	56-60