PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
23292652-2	2013	Using structural and biochemical approaches to study the role of the conserved asparagine to ubiquitin conjugation by Ubc13-Mms2, we conclude that the importance of this residue stems primarily from its structural role in stabilizing an active site loop.	Asparagine	79-89	ubiquitin conjugating enzyme E2 N	Homo sapiens	118-123	
31070815-4	2019	However, these simulations contradict another popular hypothesis that supposes that the negative charge on the intermediate is stabilized by a highly conserved asparagine (Asn79 in Ubc13).	Asparagine	160-170	ubiquitin conjugating enzyme E2 N	Homo sapiens	181-186	
28772203-1	2017	The role of a highly conserved active site asparagine (N79) in the ubiquitin conjugating enzyme, Ubc13, is probed using molecular dynamics simulations.	Asparagine	43-53	ubiquitin conjugating enzyme E2 N	Homo sapiens	97-102