PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
25483606-0	2015	Replacement of water molecules in a phosphate binding site by furanoside-appended lin-benzoguanine ligands of tRNA-guanine transglycosylase (TGT).	Water	15-20	queuine tRNA-ribosyltransferase catalytic subunit 1	Homo sapiens	110-139	
31624816-3	2019	In vitro addition of a trilysine peptide onto a guanine radical cation generated in a TGT oligonucleotide is so efficient that competitive addition of a water molecule, giving rise to 8-oxo-7,8-dihydroguanine, is not observed.	Water	153-158	queuine tRNA-ribosyltransferase catalytic subunit 1	Homo sapiens	86-89	
25483606-0	2015	Replacement of water molecules in a phosphate binding site by furanoside-appended lin-benzoguanine ligands of tRNA-guanine transglycosylase (TGT).	Water	15-20	queuine tRNA-ribosyltransferase catalytic subunit 1	Homo sapiens	141-144	
23247390-3	2012	In this study, we investigate the displacement of water molecules by an apolar probe in the binding pocket of two proteins, cyclin-dependent kinase 2 and tRNA-guanine transglycosylase, using the method of enveloping distribution sampling (EDS) to obtain free enthalpy differences.	Water	50-55	queuine tRNA-ribosyltransferase catalytic subunit 1	Homo sapiens	154-183