PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
16285725-1	2005	A series of L-nitroarginine-based dipeptide inhibitors are highly selective for neuronal nitric oxide synthase (nNOS) over the endothelial isoform (eNOS).	Dipeptides	34-43	nitric oxide synthase 1	Homo sapiens	80-110	
16285725-1	2005	A series of L-nitroarginine-based dipeptide inhibitors are highly selective for neuronal nitric oxide synthase (nNOS) over the endothelial isoform (eNOS).	Dipeptides	34-43	nitric oxide synthase 1	Homo sapiens	112-116	
16285725-2	2005	Crystal structures of these dipeptides bound to both isoforms revealed two different conformations, curled in nNOS and extended in eNOS, corresponding to higher and lower binding affinity to the two isoforms, respectively.	Dipeptides	28-38	nitric oxide synthase 1	Homo sapiens	110-114	
16285725-5	2005	Another residue farther away from the active site, Met336 in nNOS (Val106 in eNOS), is in contact with bulkier dipeptide inhibitors.	Dipeptides	111-120	nitric oxide synthase 1	Homo sapiens	61-65	
16285725-7	2005	Here we report crystal structures and inhibition constants for bulkier dipeptide inhibitors bound to nNOS and eNOS that illustrate the important role played by residues near the entry to the active site in isoform selective inhibition.	Dipeptides	71-80	nitric oxide synthase 1	Homo sapiens	101-105