PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
21828056-7	2011	By comparing the apo and inhibited caspase-2 structures, we propose that the disruption of a non-conserved salt bridge between Glu-217 and the invariant Arg-378 is important for the activation of caspase-2.	Arginine	153-156	caspase 2	Homo sapiens	35-44	
21828056-7	2011	By comparing the apo and inhibited caspase-2 structures, we propose that the disruption of a non-conserved salt bridge between Glu-217 and the invariant Arg-378 is important for the activation of caspase-2.	Arginine	153-156	caspase 2	Homo sapiens	196-205	
33011746-8	2020	Importantly, a multiple alignment has demonstrated that both Serine-384 and Arg-378 residues are highly conservative across all members of caspase family, which allows us to suggest that this diade is indispensable for caspase processing and activity.	Arginine	76-79	caspase 2	Homo sapiens	139-146	
33011746-8	2020	Importantly, a multiple alignment has demonstrated that both Serine-384 and Arg-378 residues are highly conservative across all members of caspase family, which allows us to suggest that this diade is indispensable for caspase processing and activity.	Arginine	76-79	caspase 2	Homo sapiens	219-226