PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
25809265-2	2015	Using small-angle x-ray scattering and nuclear magnetic resonance data, we describe the conformational free-energy landscape of the NADPH-cytochrome P450 reductase (CPR), a typical bidomain redox enzyme composed of two covalently-bound flavin domains, under various experimental conditions.	4,6-dinitro-o-cresol	236-242	cytochrome p450 oxidoreductase	Homo sapiens	132-163	
25809265-2	2015	Using small-angle x-ray scattering and nuclear magnetic resonance data, we describe the conformational free-energy landscape of the NADPH-cytochrome P450 reductase (CPR), a typical bidomain redox enzyme composed of two covalently-bound flavin domains, under various experimental conditions.	4,6-dinitro-o-cresol	236-242	cytochrome p450 oxidoreductase	Homo sapiens	165-168