PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
4519646-2	1973	The translocated N-acetyl-Phe-tRNA, bound to the ribosomal donor site, prevents further interaction of EF-G with the ribosome, for it inhibits the GTP hydrolysis that takes place in the presence of EF-G and ribosomes and it decreases the formation of either the GDP.EF-G.fusidic acid.ribosome complex or the 5"-guanylylmethylenediphosphonate.EF-G.ribosome complex.	Guanosine Diphosphate	262-265	G elongation factor mitochondrial 1	Homo sapiens	198-202	
4519646-2	1973	The translocated N-acetyl-Phe-tRNA, bound to the ribosomal donor site, prevents further interaction of EF-G with the ribosome, for it inhibits the GTP hydrolysis that takes place in the presence of EF-G and ribosomes and it decreases the formation of either the GDP.EF-G.fusidic acid.ribosome complex or the 5"-guanylylmethylenediphosphonate.EF-G.ribosome complex.	Guanosine Diphosphate	262-265	G elongation factor mitochondrial 1	Homo sapiens	103-107	
4519646-2	1973	The translocated N-acetyl-Phe-tRNA, bound to the ribosomal donor site, prevents further interaction of EF-G with the ribosome, for it inhibits the GTP hydrolysis that takes place in the presence of EF-G and ribosomes and it decreases the formation of either the GDP.EF-G.fusidic acid.ribosome complex or the 5"-guanylylmethylenediphosphonate.EF-G.ribosome complex.	Guanosine Diphosphate	262-265	G elongation factor mitochondrial 1	Homo sapiens	198-202	
4519646-2	1973	The translocated N-acetyl-Phe-tRNA, bound to the ribosomal donor site, prevents further interaction of EF-G with the ribosome, for it inhibits the GTP hydrolysis that takes place in the presence of EF-G and ribosomes and it decreases the formation of either the GDP.EF-G.fusidic acid.ribosome complex or the 5"-guanylylmethylenediphosphonate.EF-G.ribosome complex.	Guanosine Diphosphate	262-265	G elongation factor mitochondrial 1	Homo sapiens	198-202