PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
7890717-6	1995	MMP-2 cleaves at the same Gly-Ile/Leu bond in the collagen alpha chains as interstitial collagenases with kcat and Km values similar to that of MMP-1.	Isoleucine	30-33	matrix metallopeptidase 2	Homo sapiens	0-5	
29989088-8	2018	We herein report 4 novel inhibitor candidates of Asp-Ile-Phe, Asp-Ile-Tyr, Asp-Ile-Lys and Hser-Gly-Phe with high potency and selectivity binding to MMP-2, as well as 6 novel inhibitor candidates of Chg-Ile-Ile, Chg-Ile-Leu, Chg-Ile-Glu, Chg-Ile-Met, Chg-Val-Ile and Chg-Val-Leu selectively binding to MMP-7.	Isoleucine	53-56	matrix metallopeptidase 2	Homo sapiens	149-154	
25375834-7	2014	Similarly, a natural substrate of MMP-2, Ace-Gln-Gly ~ Ile-Ala-Gly-Nme, can be converted to an inhibiting compound by two replacements, Ile by Cys and Gly by the d isomer of Cys, favoring formation of the zinc finger motif.	Isoleucine	55-58	matrix metallopeptidase 2	Homo sapiens	34-39	
25375834-7	2014	Similarly, a natural substrate of MMP-2, Ace-Gln-Gly ~ Ile-Ala-Gly-Nme, can be converted to an inhibiting compound by two replacements, Ile by Cys and Gly by the d isomer of Cys, favoring formation of the zinc finger motif.	Isoleucine	136-139	matrix metallopeptidase 2	Homo sapiens	34-39	
18570467-7	2008	However, the rupture of the Gly( P 1) approximately Ile( P 1") amide bond is destabilized in the static QM/MM calculations, owing to the positioning of the Ile( P 1") side chain inside the MMP-2 S 1" pocket and to the inability of simple energy miminization methodologies to properly relax complex systems.	Isoleucine	52-55	matrix metallopeptidase 2	Homo sapiens	189-194	
18570467-7	2008	However, the rupture of the Gly( P 1) approximately Ile( P 1") amide bond is destabilized in the static QM/MM calculations, owing to the positioning of the Ile( P 1") side chain inside the MMP-2 S 1" pocket and to the inability of simple energy miminization methodologies to properly relax complex systems.	Isoleucine	156-159	matrix metallopeptidase 2	Homo sapiens	189-194	
10976799-7	2000	MMP-2 (Mr 72 000 type IV collagenase; gelatinase A) was found to cleave the substrates at two sites, a Gly-Ile bond and a Gly-Gln bond.	Isoleucine	107-110	matrix metallopeptidase 2	Homo sapiens	0-5	
10559137-3	1999	The amino acid sequences in interstitial collagen (Gly-Leu/Ile) and laminin-5 (Ala-Leu) that are cleaved by MMP-2 are homologous to a region (Gly(32)-Leu(33)) within human big endothelin-1[1 to 38] (big ET-1).	Isoleucine	59-62	matrix metallopeptidase 2	Homo sapiens	108-113	
20641641-17	2004	A peptide, GGPRQITAG, was found to be a MMP-2/9 substrate from a phage library and is cleaved between Gln (Q) and Ile (I) residues (14).	Isoleucine	114-117	matrix metallopeptidase 2	Homo sapiens	40-47	
20641641-21	2004	The NIR fluorescence signal will increase when the Gln-Ile bond is cleaved by MMP-2/9, releasing fragments that contain Cy5.5.	Isoleucine	55-58	matrix metallopeptidase 2	Homo sapiens	78-85