PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
2586490-1	1989	Several structurally related series of folate analogs were studied as substrates for mouse liver folylpolyglutamate synthetase (FPGS).	Folic Acid	39-45	folylpolyglutamyl synthetase	Mus musculus	97-126	
2586490-1	1989	Several structurally related series of folate analogs were studied as substrates for mouse liver folylpolyglutamate synthetase (FPGS).	Folic Acid	39-45	folylpolyglutamyl synthetase	Mus musculus	128-132	
2586490-3	1989	A series of 2,4-diaminopyrimidine dihydrofolate reductase inhibitors were found to be substrates for FPGS; these are the first known compounds without a fused ring system analogous to the pteridine ring of the folate molecule that are substrates for FPGS.	Folic Acid	41-47	folylpolyglutamyl synthetase	Mus musculus	101-105	
2586490-3	1989	A series of 2,4-diaminopyrimidine dihydrofolate reductase inhibitors were found to be substrates for FPGS; these are the first known compounds without a fused ring system analogous to the pteridine ring of the folate molecule that are substrates for FPGS.	Folic Acid	41-47	folylpolyglutamyl synthetase	Mus musculus	250-254	
2586490-6	1989	It was concluded that neither the 2-amino group nor an intact pyrazine ring of folates and folate analogs are essential for the binding of folates to the active site of mouse liver FPGS but that the pyrazine ring probably serves to position other regions of the folate molecule that interact with amino acid residues in the active site.	Folic Acid	139-146	folylpolyglutamyl synthetase	Mus musculus	181-185	
2586490-7	1989	It was also inferred from these observations that the volume within the active site of FPGS above/below the pyrazine ring or near the 10-position of folate derivatives are regions of limited bulk tolerance; binding of folate analogs with substituents at these positions probably distorts the active site.	Folic Acid	149-155	folylpolyglutamyl synthetase	Mus musculus	87-91	
2586490-7	1989	It was also inferred from these observations that the volume within the active site of FPGS above/below the pyrazine ring or near the 10-position of folate derivatives are regions of limited bulk tolerance; binding of folate analogs with substituents at these positions probably distorts the active site.	Folic Acid	218-224	folylpolyglutamyl synthetase	Mus musculus	87-91