PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
29476645-1	2018	Angiotensin-1-converting enzyme (ACE) is a zinc metallopeptidase that consists of two homologous catalytic domains (known as nACE and cACE) with different substrate specificities.	nace	125-129	angiotensin I converting enzyme	Homo sapiens	0-31	
29476645-1	2018	Angiotensin-1-converting enzyme (ACE) is a zinc metallopeptidase that consists of two homologous catalytic domains (known as nACE and cACE) with different substrate specificities.	nace	125-129	angiotensin I converting enzyme	Homo sapiens	33-36	
29476645-2	2018	Based on kinetic studies it was previously reported that sampatrilat, a tight-binding inhibitor of ACE, Ki = 13.8 nm and 171.9 nm for cACE and nACE respectively [Sharma et al., Journal of Chemical Information and Modeling (2016), 56, 2486-2494], was 12.4-fold more selective for cACE.	nace	143-147	angiotensin I converting enzyme	Homo sapiens	99-102	
29476645-4	2018	Here, we report a detailed three-dimensional structural analysis of sampatrilat and samAsp binding to ACE using high-resolution crystal structures elucidated by X-ray crystallography, which provides a molecular basis for differences in inhibitor affinity and selectivity for nACE and cACE.	nace	275-279	angiotensin I converting enzyme	Homo sapiens	102-105