PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
32736114-9	2020	In silico docking methods elucidate the contribution of hydrogen bonds and hydrophobic contacts towards the binding of 2"-OH-PCB61 and 2"-OH-PCB65 with CES1 and CES2.	Hydrogen	56-64	carboxylesterase 1	Homo sapiens	152-156	
22429570-2	2012	Quantitative pharmacophore models were generated using HypoGen module of Discovery Studio 2.1, whereby the best pharmacophore model possessing two hydrophobic, one ring aromatic, and one hydrogen bond acceptor feature for inhibition of acyl coenzyme A cholesterol acyltransferase showed a very good correlation coefficient (r = 0.942) along with satisfactory cost analysis.	Hydrogen	187-195	carboxylesterase 1	Homo sapiens	236-279	
8496932-4	1993	Only replacement of amide bonds with isosterases having both hydrogen bond donor and acceptor functionalities yielded compounds retaining ACAT inhibitory activity.	Hydrogen	61-69	carboxylesterase 1	Homo sapiens	138-142	
30486721-13	2019	In silico docking showed that hydrogen bonds and hydrophobic interactions contributed to the inhibition of Schisandrin B on CES1, Anwuligan on CES2, and Schisandrin B on CES2.	Hydrogen	30-38	carboxylesterase 1	Homo sapiens	124-128	
31617515-3	2019	Isotope labeling studies along with B3LYP geometry optimization DFT modeling studies indicate a mechanism involving a Re-H-Re bridging complex that leads to a dimeric Re-Re(eta2-H2) state prior to dissociating H2 gas.	Hydrogen	178-180	carboxylesterase 1	Homo sapiens	118-122	
28602090-8	2017	This is the rate-determining step in the reaction cycle and is followed by hydrogen-atom transfer from the CE1-H group of trimethyl histidine substrate to iron(II)-superoxo.	Hydrogen	75-83	carboxylesterase 1	Homo sapiens	107-110