PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
8722020-4	1995	Elongation factor Tu (EF-Tu) undergoes a dramatic structural transition from its GDP-bound form to its active GTP-bound form, in which it binds aa-tRNA (aminoacyl-tRNA) in ternary complex.	Guanosine Diphosphate	81-84	eukaryotic translation elongation factor 1 alpha 1	Homo sapiens	0-20	
8722020-4	1995	Elongation factor Tu (EF-Tu) undergoes a dramatic structural transition from its GDP-bound form to its active GTP-bound form, in which it binds aa-tRNA (aminoacyl-tRNA) in ternary complex.	Guanosine Diphosphate	81-84	eukaryotic translation elongation factor 1 alpha 1	Homo sapiens	22-27	
8722020-5	1995	The effects of substitution mutations at three sites in domain I of EF-Tu, Gln124, Leu120, and Tyr160, all of which point into the domain I-domain III interface in both the GTP and GDP conformations of EF-Tu, were examined.	Guanosine Diphosphate	181-184	eukaryotic translation elongation factor 1 alpha 1	Homo sapiens	68-73	
8722020-5	1995	The effects of substitution mutations at three sites in domain I of EF-Tu, Gln124, Leu120, and Tyr160, all of which point into the domain I-domain III interface in both the GTP and GDP conformations of EF-Tu, were examined.	Guanosine Diphosphate	181-184	eukaryotic translation elongation factor 1 alpha 1	Homo sapiens	202-207