PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
23586781-8	2013	Crystal structures of our NHA analogues bound to nNOS have been determined, revealing the presence of an active site water molecule only in the presence of singly methylated analogues.	Water	117-122	nitric oxide synthase 1	Homo sapiens	49-53	
18052254-1	2008	Fully coupled nitric oxide synthase (NOS) catalyzes formation of nitric oxide (NO), l-citrulline, NADP+, and water from l-arginine, NADPH, and oxygen.	Water	109-114	nitric oxide synthase 1	Homo sapiens	14-35	
17425297-3	2007	X-ray crystal structures of complexes of nNOS with two nNOS-selective inhibitors, (4S)-N-{4-amino-5-[(2-aminoethylamino]pentyl}-N"-nitroguanidine (1) and 4-N-(Nomega-nitro-l-argininyl)-trans-4-amino-l-proline amide (2), led to the discovery of a conserved structural water molecule that was hydrogen bonded between the two heme propionates and the inhibitors (Figure 2).	Water	267-272	nitric oxide synthase 1	Homo sapiens	41-45	
17425297-6	2007	X-ray crystal structures of nNOS with inhibitors 3 and 5 bound verified that the N-hydroxyl group had, indeed, displaced the structural water molecule and provided a direct interaction with the heme propionate moiety (Figures 5 and 6).	Water	136-141	nitric oxide synthase 1	Homo sapiens	28-32	
32302123-5	2020	X-ray crystallography indicates that the amino groups of some compounds occupy a water-filled pocket surrounding an nNOS-specific aspartate residue (absent in eNOS).	Water	81-86	nitric oxide synthase 1	Homo sapiens	116-120	
16804678-5	2006	The detailed hydrogen-bonding geometries depicted in the active site of nNOS structures indicate that it is the ordered active-site water molecule rather than the substrate itself that would most likely serve as a direct proton donor to the diatomic ligands (CO, NO, as well as O(2)) bound to the heme.	Water	132-137	nitric oxide synthase 1	Homo sapiens	72-76	
16814584-1	2006	Neuronal NOS (nNOS) is a constitutively expressed enzyme that catalyzes the oxidation of L-arginine and water to L-citrulline and the gas nitric oxide (NO).	Water	104-109	nitric oxide synthase 1	Homo sapiens	14-18	
10090758-8	1999	1,2H ENDOR of NOHA bound to holo-nNOS in H2O and D2O discloses the presence of a single resolved exchangeable proton (H1) 4.8 A from Fe and very near the heme normal.	Water	41-44	nitric oxide synthase 1	Homo sapiens	33-37	
26035438-10	2015	The nearby exchangeable proton in both the no-substrate and Arg-containing nNOS samples is located outside the H-bonding range and, on the basis of the obtained structural constraints, can belong to the active site water (or OH).	Water	215-220	nitric oxide synthase 1	Homo sapiens	75-79