PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
31841328-3	2020	Molecular docking predicted that RGM-(Hyp)-GF and the ACE residues of Glu384, His513 and Lys511 formed hydrogen-bonding interactions at distances of 2.57, 2.99 and 2.42+3.0 A. RGL-(Hyp)-GL formed hydrogen bonds with Lys511 and Tyr523 and generated hydrogen-bonding interactions with His387 and Glu411 in the zinc(II) complexation motif at distances of 2.74 and 3.03+1.93 A.	Hydrogen	103-111	angiotensin I converting enzyme	Bos taurus	54-57	
32066337-4	2021	The results showed two conditions which appear to be essential that peptides presented ACE inhibition capacity: i) to interact with Zn2+ coordinated residues, such as His383, His387, and Glu411, by short hydrogen bonds, for peptides with high inhibitory capacity in vitro, as ALNEINQFYQK (IACE = 80.7%), NAVPITPTLNR (IACE = 80.7%), and FALPQYLK (IACE = 79.0%); or interact by electrostatic and hydrophobic interactions with the same residues, for peptides with intermediate inhibition capacity in vitro, as HQGLPQEVLNENLLR (IACE = 49.2%), FFVAPFPEVFGK (IACE = 47.8%) and YLGYLEQLLR (IACE = 47.8%); ii) to interact with the S1 active site residues (Ala354, Glu384, and Tyr523) by hydrogen bonds.	Hydrogen	204-212	angiotensin I converting enzyme	Bos taurus	87-90	
32066337-4	2021	The results showed two conditions which appear to be essential that peptides presented ACE inhibition capacity: i) to interact with Zn2+ coordinated residues, such as His383, His387, and Glu411, by short hydrogen bonds, for peptides with high inhibitory capacity in vitro, as ALNEINQFYQK (IACE = 80.7%), NAVPITPTLNR (IACE = 80.7%), and FALPQYLK (IACE = 79.0%); or interact by electrostatic and hydrophobic interactions with the same residues, for peptides with intermediate inhibition capacity in vitro, as HQGLPQEVLNENLLR (IACE = 49.2%), FFVAPFPEVFGK (IACE = 47.8%) and YLGYLEQLLR (IACE = 47.8%); ii) to interact with the S1 active site residues (Ala354, Glu384, and Tyr523) by hydrogen bonds.	Hydrogen	679-687	angiotensin I converting enzyme	Bos taurus	87-90	
31841328-3	2020	Molecular docking predicted that RGM-(Hyp)-GF and the ACE residues of Glu384, His513 and Lys511 formed hydrogen-bonding interactions at distances of 2.57, 2.99 and 2.42+3.0 A. RGL-(Hyp)-GL formed hydrogen bonds with Lys511 and Tyr523 and generated hydrogen-bonding interactions with His387 and Glu411 in the zinc(II) complexation motif at distances of 2.74 and 3.03+1.93 A.	Hydrogen	196-204	angiotensin I converting enzyme	Bos taurus	54-57	
31841328-3	2020	Molecular docking predicted that RGM-(Hyp)-GF and the ACE residues of Glu384, His513 and Lys511 formed hydrogen-bonding interactions at distances of 2.57, 2.99 and 2.42+3.0 A. RGL-(Hyp)-GL formed hydrogen bonds with Lys511 and Tyr523 and generated hydrogen-bonding interactions with His387 and Glu411 in the zinc(II) complexation motif at distances of 2.74 and 3.03+1.93 A.	Hydrogen	196-204	angiotensin I converting enzyme	Bos taurus	54-57