PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
23028781-7	2012	Structure comparison and mutagenesis identify an Arg neighboring to the Sirt5 nicotinamide binding pocket as a mediator of nicotinamide resistance, and statistical sequence analyses along with testing further Sirtuins reveal a network of coevolved residues likely defining a nicotinamide-insensitive Sirtuin deacetylase family.	Arginine	49-52	sirtuin 5	Homo sapiens	72-77	
23028781-8	2012	The same Arg was recently reported to render Sirt5 a preferential desuccinylase, and we find that this Sirt5 activity is highly sensitive to nicotinamide inhibition.	Arginine	9-12	sirtuin 5	Homo sapiens	45-50	
23028781-8	2012	The same Arg was recently reported to render Sirt5 a preferential desuccinylase, and we find that this Sirt5 activity is highly sensitive to nicotinamide inhibition.	Arginine	9-12	sirtuin 5	Homo sapiens	103-108	
23028781-9	2012	Analysis of Sirt5 structures and activity data suggest that an Arg/succinate interaction is the molecular basis of the differential nicotinamide sensitivities of the two Sirt5 activities.	Arginine	63-66	sirtuin 5	Homo sapiens	12-17	
23028781-9	2012	Analysis of Sirt5 structures and activity data suggest that an Arg/succinate interaction is the molecular basis of the differential nicotinamide sensitivities of the two Sirt5 activities.	Arginine	63-66	sirtuin 5	Homo sapiens	170-175	
22076378-5	2011	The preference for succinyl and malonyl groups was explained by the presence of an arginine residue (Arg(105)) and tyrosine residue (Tyr(102)) in the acyl pocket of Sirt5.	Arginine	83-91	sirtuin 5	Homo sapiens	165-170	
22076378-5	2011	The preference for succinyl and malonyl groups was explained by the presence of an arginine residue (Arg(105)) and tyrosine residue (Tyr(102)) in the acyl pocket of Sirt5.	Arginine	101-104	sirtuin 5	Homo sapiens	165-170