PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
22542899-9	2012	The overall findings indicate that in FNR the volume of the residue at position 266 is essential to attain the catalytic architecture between the nicotinamide and isoalloxazine rings at the active site and, therefore, for an efficient HT process.	isoalloxazine	163-176	ferredoxin reductase	Homo sapiens	38-41	
12359874-2	2002	A conserved aromatic residue in the FNR module of NOS shields the isoalloxazine ring of FAD and is known to regulate NADPH binding affinity and specificity in related flavoproteins.	isoalloxazine	66-79	ferredoxin reductase	Homo sapiens	36-39	
21538059-5	2012	In particular, the side chain of the C-terminal Y303 in Anabaena FNR appears key to providing the optimum geometry by reducing the stacking probability between the isoalloxazine and nicotinamide rings, thus providing the required co-linearity and distance among the N5 of the flavin cofactor, the C4 of the coenzyme nicotinamide and the hydride that has to be transferred between them.	isoalloxazine	164-177	ferredoxin reductase	Homo sapiens	65-68	
20471952-7	2010	The architecture of the WT FNR active site precisely contributes to reduce the stacking probability between the isoalloxazine and nicotinamide rings in the catalytically competent complex, modulating the angle and distance between the N5 of the FAD isoalloxazine and the C4 of the coenzyme nicotinamide to values that ensure efficient HT processes.	isoalloxazine	112-125	ferredoxin reductase	Homo sapiens	27-30	
11577105-1	2001	In ferredoxin-NADP(+) reductase (FNR), FAD is bound outside of an anti-parallel beta-barrel with the isoalloxazine lying in a two-tyrosine pocket.	isoalloxazine	101-114	ferredoxin reductase	Homo sapiens	3-31	
11577105-1	2001	In ferredoxin-NADP(+) reductase (FNR), FAD is bound outside of an anti-parallel beta-barrel with the isoalloxazine lying in a two-tyrosine pocket.	isoalloxazine	101-114	ferredoxin reductase	Homo sapiens	33-36	
11053423-8	2001	The [2Fe-2S] cluster of Adx and the isoalloxazine rings of FAD of AR are 10 A apart suggesting a possible electron transfer route between these redox centers.	isoalloxazine	36-49	ferredoxin reductase	Homo sapiens	66-68	
7626622-6	1995	The conserved sequence contains a tyrosine residue (Tyr-44) which, based on the X-ray crystal structure of ferredoxin-NADP+ reductase, is postulated to participate in FAD binding through van der Waals contact with the isoalloxazine ring and a hydrogen bond to the 3"-hydroxy of the ribityl moiety.	isoalloxazine	218-231	ferredoxin reductase	Homo sapiens	107-133	
7677850-1	1995	The crystal structure of ferredoxin-NADP+ reductase (FNR) suggests that Ser96 is directly involved in hydride transfer between the isoalloxazine moiety of FAD and the nicotinamide ring of NADP(H).	isoalloxazine	131-144	ferredoxin reductase	Homo sapiens	25-51	
7677850-1	1995	The crystal structure of ferredoxin-NADP+ reductase (FNR) suggests that Ser96 is directly involved in hydride transfer between the isoalloxazine moiety of FAD and the nicotinamide ring of NADP(H).	isoalloxazine	131-144	ferredoxin reductase	Homo sapiens	53-56