PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
26899411-6	2016	The same patches are simulated for the Vpu double mutant, Vpu-DD, in which the two serines 52 and 56 are replaced by aspartic acid.	Aspartic Acid	117-130	Vpu	Human immunodeficiency virus 1	39-42	
26899411-6	2016	The same patches are simulated for the Vpu double mutant, Vpu-DD, in which the two serines 52 and 56 are replaced by aspartic acid.	Aspartic Acid	117-130	Vpu	Human immunodeficiency virus 1	58-61	
8107101-11	1994	The two CK-2 phosphorylation sites are conserved in all known Vpu sequences and represent the consensus Ser52GlyAsn(Glu/Asp)Ser(Glu/Asp)Gly(Glu/Asp)59.	Aspartic Acid	120-123	Vpu	Human immunodeficiency virus 1	62-65	
8107101-11	1994	The two CK-2 phosphorylation sites are conserved in all known Vpu sequences and represent the consensus Ser52GlyAsn(Glu/Asp)Ser(Glu/Asp)Gly(Glu/Asp)59.	Aspartic Acid	132-135	Vpu	Human immunodeficiency virus 1	62-65	
8107101-11	1994	The two CK-2 phosphorylation sites are conserved in all known Vpu sequences and represent the consensus Ser52GlyAsn(Glu/Asp)Ser(Glu/Asp)Gly(Glu/Asp)59.	Aspartic Acid	132-135	Vpu	Human immunodeficiency virus 1	62-65	
25352594-3	2014	Vpu-induced IRF3 cleavage is mediated by caspases and occurs mainly at Asp-121.	Aspartic Acid	71-74	Vpu	Human immunodeficiency virus 1	0-3