PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
23633953-6	2013	A comparison between Ubc13-bound and wild-type free OspI structures revealed that Ubc13 binding induces notable structural reassembly of the catalytic pocket, suggesting that substrate binding might be involved in the catalysis of OspI.	ospi	52-56	ubiquitin conjugating enzyme E2 N	Homo sapiens	21-26	
23633953-6	2013	A comparison between Ubc13-bound and wild-type free OspI structures revealed that Ubc13 binding induces notable structural reassembly of the catalytic pocket, suggesting that substrate binding might be involved in the catalysis of OspI.	ospi	52-56	ubiquitin conjugating enzyme E2 N	Homo sapiens	82-87	
23633953-6	2013	A comparison between Ubc13-bound and wild-type free OspI structures revealed that Ubc13 binding induces notable structural reassembly of the catalytic pocket, suggesting that substrate binding might be involved in the catalysis of OspI.	ospi	231-235	ubiquitin conjugating enzyme E2 N	Homo sapiens	21-26	
23633953-6	2013	A comparison between Ubc13-bound and wild-type free OspI structures revealed that Ubc13 binding induces notable structural reassembly of the catalytic pocket, suggesting that substrate binding might be involved in the catalysis of OspI.	ospi	231-235	ubiquitin conjugating enzyme E2 N	Homo sapiens	82-87	
23633953-7	2013	The OspI-binding sites in Ubc13 largely overlap with the binding residues for host ubiquitin E3 ligases and a deubiquitinating enzyme, which suggests that the bacterial effector and host proteins exploit the same surface on Ubc13 for specific recognition.	ospi	4-8	ubiquitin conjugating enzyme E2 N	Homo sapiens	26-31	
23633953-7	2013	The OspI-binding sites in Ubc13 largely overlap with the binding residues for host ubiquitin E3 ligases and a deubiquitinating enzyme, which suggests that the bacterial effector and host proteins exploit the same surface on Ubc13 for specific recognition.	ospi	4-8	ubiquitin conjugating enzyme E2 N	Homo sapiens	224-229