PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
19850376-2	2010	A comparison of several crystal structures of MK2 shows that differences in active and inactive conformations result in large part from structural variations within the conformations of the glycine rich loop (p-loop) regions.	Glycine	190-197	MAPK activated protein kinase 2	Homo sapiens	46-49	
24316826-2	2013	In a previous report, it was shown that MK2 in complex with the selective inhibitor TEI-I01800 adopts an alpha-helical glycine-rich loop that is induced by the stable nonplanar conformer of TEI-I01800.	Glycine	119-126	MAPK activated protein kinase 2	Homo sapiens	40-43	
24316826-4	2013	MK2-TEI-L03090 has a beta-sheet glycine-rich loop in common with other kinases, as predicted.	Glycine	32-39	MAPK activated protein kinase 2	Homo sapiens	0-3	
24121337-2	2013	The crystal structure of the MK2-TEI-I01800 complex has been reported; its Gly-rich loop was found to form an alpha-helix, not a beta-sheet as has been observed for other Ser/Thr kinases.	Glycine	75-78	MAPK activated protein kinase 2	Homo sapiens	29-32	
24121337-4	2013	Interestingly, the Gly-rich loop of CDK2 formed a beta-sheet that was different from that of MK2.	Glycine	19-22	MAPK activated protein kinase 2	Homo sapiens	93-96	
24121337-5	2013	In MK2, TEI-I01800 changed the secondary structure of the Gly-rich loop from a beta-sheet to an alpha-helix by collision between Leu70 and a p-ethoxyphenyl group at the 7-position and bound to MK2.	Glycine	58-61	MAPK activated protein kinase 2	Homo sapiens	3-6	
24121337-5	2013	In MK2, TEI-I01800 changed the secondary structure of the Gly-rich loop from a beta-sheet to an alpha-helix by collision between Leu70 and a p-ethoxyphenyl group at the 7-position and bound to MK2.	Glycine	58-61	MAPK activated protein kinase 2	Homo sapiens	193-196	
20057052-0	2010	Structural analysis of an MK2-inhibitor complex: insight into the regulation of the secondary structure of the Gly-rich loop by TEI-I01800.	Glycine	111-114	MAPK activated protein kinase 2	Homo sapiens	26-29	
20057052-3	2010	The MK2 structure in the MK2-TEI-I01800 complex is composed of two domains, as observed for other Ser/Thr kinases; however, the Gly-rich loop in the N-terminal domain forms an alpha-helix structure and not a beta-sheet.	Glycine	128-131	MAPK activated protein kinase 2	Homo sapiens	4-7	
20057052-3	2010	The MK2 structure in the MK2-TEI-I01800 complex is composed of two domains, as observed for other Ser/Thr kinases; however, the Gly-rich loop in the N-terminal domain forms an alpha-helix structure and not a beta-sheet.	Glycine	128-131	MAPK activated protein kinase 2	Homo sapiens	25-28	
20057052-6	2010	The MK2-TEI-I01800 complex structure is the first active MK2 with an alpha-helical Gly-rich loop and TEI-I01800 regulates the secondary structure of the Gly-rich loop.	Glycine	83-86	MAPK activated protein kinase 2	Homo sapiens	4-7	
20057052-6	2010	The MK2-TEI-I01800 complex structure is the first active MK2 with an alpha-helical Gly-rich loop and TEI-I01800 regulates the secondary structure of the Gly-rich loop.	Glycine	83-86	MAPK activated protein kinase 2	Homo sapiens	57-60	
20057052-6	2010	The MK2-TEI-I01800 complex structure is the first active MK2 with an alpha-helical Gly-rich loop and TEI-I01800 regulates the secondary structure of the Gly-rich loop.	Glycine	153-156	MAPK activated protein kinase 2	Homo sapiens	4-7	
20057052-6	2010	The MK2-TEI-I01800 complex structure is the first active MK2 with an alpha-helical Gly-rich loop and TEI-I01800 regulates the secondary structure of the Gly-rich loop.	Glycine	153-156	MAPK activated protein kinase 2	Homo sapiens	57-60