PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
31276316-2	2019	CPR shows a stringent preference for NADPH over the less expensive cofactor, NADH, economically limiting its use as a biocatalyst.	NAD	77-81	cytochrome p450 oxidoreductase	Homo sapiens	0-3	
31276316-3	2019	The complexity of cofactor-linked CPR protein dynamics and the incomplete understanding of the interaction of CPR with both cofactors and electron acceptors present challenges for the successful rational engineering of a CPR with enhanced activity with NADH.	NAD	253-257	cytochrome p450 oxidoreductase	Homo sapiens	34-37	
31276316-3	2019	The complexity of cofactor-linked CPR protein dynamics and the incomplete understanding of the interaction of CPR with both cofactors and electron acceptors present challenges for the successful rational engineering of a CPR with enhanced activity with NADH.	NAD	253-257	cytochrome p450 oxidoreductase	Homo sapiens	110-113	
31276316-3	2019	The complexity of cofactor-linked CPR protein dynamics and the incomplete understanding of the interaction of CPR with both cofactors and electron acceptors present challenges for the successful rational engineering of a CPR with enhanced activity with NADH.	NAD	253-257	cytochrome p450 oxidoreductase	Homo sapiens	110-113	
31276316-4	2019	Here, we report a rational evolution approach to enhance the activity of CPR with NADH, in which mutations were introduced into the NADPH-binding flavin adenine dinucleotide (FAD) domain.	NAD	82-86	cytochrome p450 oxidoreductase	Homo sapiens	73-76	
31276316-5	2019	Multiple CPR mutants that used NADH more effectively than the wild-type CPR in the reduction of the surrogate electron acceptor, cytochrome c were found.	NAD	31-35	cytochrome p450 oxidoreductase	Homo sapiens	9-12	
31276316-5	2019	Multiple CPR mutants that used NADH more effectively than the wild-type CPR in the reduction of the surrogate electron acceptor, cytochrome c were found.	NAD	31-35	cytochrome p450 oxidoreductase	Homo sapiens	72-75