PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
26494047-8	2016	In addition, four novel ACE inhibitory peptides were isolated, and their amino acids sequences were identified as Val-Gly-Pro-Tyr, Phe-Thr-Tyr-Val-Pro-Gly, Phe-Thr-Tyr-Val-Pro-Gly-Ala and Phe-Gln-Ala-Val-Trp-Ala-Gly, respectively.	Valine	114-117	angiotensin I converting enzyme	Homo sapiens	24-27	
32854180-8	2020	Of these peptides, Isoleucine-Lysine- Glutamic Acid-Valine-Threonine-Glutamic Acid-Arginine (IKEVTER) demonstrated the highest ACE inhibitory activity.	Valine	52-58	angiotensin I converting enzyme	Homo sapiens	127-130	
17439247-7	2007	Thus the high affinity of RXPA380 for the testis ACE/somatic ACE C domain is explained by the interaction of these bulky moieties with residues unique to these domains, specifically Phe 391, Val 379, and Val 380, that are not found in the N domain.	Valine	191-194	angiotensin I converting enzyme	Homo sapiens	49-52	
24596454-9	2014	Based on molecular docking studies, we propose that in ACE-1 inhibition IPP and VPP share a similar cis configuration between the first aliphatic (isoleucine or valine) and the second (proline) amino acid residues and more different configurations between two proline residues.	Valine	161-167	angiotensin I converting enzyme	Homo sapiens	55-60	
21348305-6	2010	Peptides showed high ACE inhibitory activity when the N-terminal was hydrophobic amino acid such as Val and C-terminal tripeptide contained Phe, Trp or Arg.	Valine	100-103	angiotensin I converting enzyme	Homo sapiens	21-24	
17439247-7	2007	Thus the high affinity of RXPA380 for the testis ACE/somatic ACE C domain is explained by the interaction of these bulky moieties with residues unique to these domains, specifically Phe 391, Val 379, and Val 380, that are not found in the N domain.	Valine	191-194	angiotensin I converting enzyme	Homo sapiens	61-64	
17439247-7	2007	Thus the high affinity of RXPA380 for the testis ACE/somatic ACE C domain is explained by the interaction of these bulky moieties with residues unique to these domains, specifically Phe 391, Val 379, and Val 380, that are not found in the N domain.	Valine	204-207	angiotensin I converting enzyme	Homo sapiens	49-52	
17439247-7	2007	Thus the high affinity of RXPA380 for the testis ACE/somatic ACE C domain is explained by the interaction of these bulky moieties with residues unique to these domains, specifically Phe 391, Val 379, and Val 380, that are not found in the N domain.	Valine	204-207	angiotensin I converting enzyme	Homo sapiens	61-64