PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
17643990-2	2007	Molecular modelling studies suggest that cryptolepine is able to fit into the active site of NQO2 and thus raising the possibility that nitro-analogues of 1 could act as bioreductive prodrugs and be selectively reduced by NQO1 and NQO2 to more toxic species in cancer cells in which these enzymes are over-expressed.	nitro	136-141	N-ribosyldihydronicotinamide:quinone reductase 2	Homo sapiens	93-97	
17643990-2	2007	Molecular modelling studies suggest that cryptolepine is able to fit into the active site of NQO2 and thus raising the possibility that nitro-analogues of 1 could act as bioreductive prodrugs and be selectively reduced by NQO1 and NQO2 to more toxic species in cancer cells in which these enzymes are over-expressed.	nitro	136-141	N-ribosyldihydronicotinamide:quinone reductase 2	Homo sapiens	231-235	
16129418-4	2005	The complex structure indicates the essentiality of the two nitro groups: one nitro group forms hydrogen bonds with the side-chain of Asn161 of QR2 to hold the other nitro group in position for the reduction.	nitro	60-65	N-ribosyldihydronicotinamide:quinone reductase 2	Homo sapiens	144-147	
16129418-4	2005	The complex structure indicates the essentiality of the two nitro groups: one nitro group forms hydrogen bonds with the side-chain of Asn161 of QR2 to hold the other nitro group in position for the reduction.	nitro	78-83	N-ribosyldihydronicotinamide:quinone reductase 2	Homo sapiens	144-147	
16129418-4	2005	The complex structure indicates the essentiality of the two nitro groups: one nitro group forms hydrogen bonds with the side-chain of Asn161 of QR2 to hold the other nitro group in position for the reduction.	nitro	78-83	N-ribosyldihydronicotinamide:quinone reductase 2	Homo sapiens	144-147