PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
25672880-4	2015	Our results suggest that the serine plays a crucial role in maintaining the closed conformation of wild-type GK and the GMP recognition.	guanosine 5'-monophosphorothioate	120-123	guanylate kinase 1	Homo sapiens	109-111	
25672880-6	2015	Furthermore, the free energy profiles (FEPs) obtained by metadymanics clearly demonstrate that the open-closed conformational transition in WT GK is positive correlated with the process of GMP binding, indicating the GMP-induced closing motion of GK enzyme, which is not observed in the mutant.	guanosine 5'-monophosphorothioate	189-192	guanylate kinase 1	Homo sapiens	143-145	
25672880-6	2015	Furthermore, the free energy profiles (FEPs) obtained by metadymanics clearly demonstrate that the open-closed conformational transition in WT GK is positive correlated with the process of GMP binding, indicating the GMP-induced closing motion of GK enzyme, which is not observed in the mutant.	guanosine 5'-monophosphorothioate	189-192	guanylate kinase 1	Homo sapiens	247-249	
25672880-6	2015	Furthermore, the free energy profiles (FEPs) obtained by metadymanics clearly demonstrate that the open-closed conformational transition in WT GK is positive correlated with the process of GMP binding, indicating the GMP-induced closing motion of GK enzyme, which is not observed in the mutant.	guanosine 5'-monophosphorothioate	217-220	guanylate kinase 1	Homo sapiens	143-145	
25672880-6	2015	Furthermore, the free energy profiles (FEPs) obtained by metadymanics clearly demonstrate that the open-closed conformational transition in WT GK is positive correlated with the process of GMP binding, indicating the GMP-induced closing motion of GK enzyme, which is not observed in the mutant.	guanosine 5'-monophosphorothioate	217-220	guanylate kinase 1	Homo sapiens	247-249