PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
30900874-2	2019	In this report, biochemical analysis with various divalent cations was used to demonstrate that NNRTIs and divalent cation-dNTP complexes are mutually exclusive, inhibiting each other"s binding to RT/primer/template (RT-P/T) complexes.	Parathion	123-127	MORN repeat containing 4	Homo sapiens	217-223	
30900874-3	2019	The binding of catalytically competent divalent cation-dNTP complexes to RT-P/T was measured with Mg2+, Mn2+, Zn2+, Co2+, and Ni2+ using Ca2+, a noncatalytic cation, for displacement.	Parathion	55-59	MORN repeat containing 4	Homo sapiens	73-79	
30900874-6	2019	Filtration assays demonstrated that divalent cation-dNTP complexes inhibited the binding of 14C-labeled EFV to RT-P/T with stronger binding complexes formed with Mn2+ inhibiting more potently than those with Mg2+.	Parathion	52-56	MORN repeat containing 4	Homo sapiens	111-117	
30900874-7	2019	Conversely, filter binding assays demonstrated that EFV inhibited 3H-labeled dNTP binding to RT-P/T complexes with displacement of Mn2+-dNTP complexes requiring much greater concentrations of EFV than the more weakly bound Mg2+-dNTP complexes.	Parathion	77-81	MORN repeat containing 4	Homo sapiens	93-99	
30900874-7	2019	Conversely, filter binding assays demonstrated that EFV inhibited 3H-labeled dNTP binding to RT-P/T complexes with displacement of Mn2+-dNTP complexes requiring much greater concentrations of EFV than the more weakly bound Mg2+-dNTP complexes.	Parathion	136-140	MORN repeat containing 4	Homo sapiens	93-99	
30900874-7	2019	Conversely, filter binding assays demonstrated that EFV inhibited 3H-labeled dNTP binding to RT-P/T complexes with displacement of Mn2+-dNTP complexes requiring much greater concentrations of EFV than the more weakly bound Mg2+-dNTP complexes.	Parathion	136-140	MORN repeat containing 4	Homo sapiens	93-99