PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
1510968-1	1992	The function of a highly mobile loop in Escherichia coli dihydrofolate reductase was studied by constructing a mutant (DL1) using cassette mutagenesis that had four residues deleted in the middle section of the loop (Met16-Ala19) and a glycine inserted to seal the gap.	Glycine	236-243	Dihydrofolate reductase	Escherichia coli	57-80	
9749924-0	1998	Effects of the length of a glycine linker connecting the N-and C-termini of a circularly permuted dihydrofolate reductase.	Glycine	27-34	Dihydrofolate reductase	Escherichia coli	98-121	
9572847-9	1998	The introduction of glycine into the modified betaF-betaG loop, however, generally eliminated conformational changes required by DeltaG121 DHFR to attain the Michaelis complex.	Glycine	20-27	Dihydrofolate reductase	Escherichia coli	139-143	
9504406-0	1998	Nonadditive effects of double mutations at the flexible loops, glycine-67 and glycine-121, of Escherichia coli dihydrofolate reductase on its stability and function.	Glycine	63-70	Dihydrofolate reductase	Escherichia coli	111-134	
9504406-0	1998	Nonadditive effects of double mutations at the flexible loops, glycine-67 and glycine-121, of Escherichia coli dihydrofolate reductase on its stability and function.	Glycine	78-85	Dihydrofolate reductase	Escherichia coli	111-134	
9398309-0	1997	Evidence for a functional role of the dynamics of glycine-121 of Escherichia coli dihydrofolate reductase obtained from kinetic analysis of a site-directed mutant.	Glycine	50-57	Dihydrofolate reductase	Escherichia coli	82-105	
9398309-1	1997	Two-dimensional heteronuclear (1H-15N) nuclear magnetic relaxation studies of dihydrofolate reductase (DHFR) from Escherichia coli have demonstrated that glycine-121 which is 19 A from the catalytic center of the enzyme has large-amplitude backbone motions on the nanosecond time scale [Epstein, D. M., Benkovic, S. J., and Wright, P. E. (1995) Biochemistry 34, 11037-11048].	Glycine	154-161	Dihydrofolate reductase	Escherichia coli	78-101	
9398309-1	1997	Two-dimensional heteronuclear (1H-15N) nuclear magnetic relaxation studies of dihydrofolate reductase (DHFR) from Escherichia coli have demonstrated that glycine-121 which is 19 A from the catalytic center of the enzyme has large-amplitude backbone motions on the nanosecond time scale [Epstein, D. M., Benkovic, S. J., and Wright, P. E. (1995) Biochemistry 34, 11037-11048].	Glycine	154-161	Dihydrofolate reductase	Escherichia coli	103-107	
15065854-0	2004	Pivotal role of Gly 121 in dihydrofolate reductase from Escherichia coli: the altered structure of a mutant enzyme may form the basis of its diminished catalytic performance.	Glycine	16-19	Dihydrofolate reductase	Escherichia coli	27-50	
15065854-1	2004	The structure and folding of dihydrofolate reductase (DHFR) from Escherichia coli and the mutant G121V-DHFR, in which glycine 121 in the exterior FG loop was replaced with valine, were studied by molecular dynamics simulations and CD and fluorescence spectroscopy.	Glycine	118-125	Dihydrofolate reductase	Escherichia coli	54-58	
15065854-1	2004	The structure and folding of dihydrofolate reductase (DHFR) from Escherichia coli and the mutant G121V-DHFR, in which glycine 121 in the exterior FG loop was replaced with valine, were studied by molecular dynamics simulations and CD and fluorescence spectroscopy.	Glycine	118-125	Dihydrofolate reductase	Escherichia coli	103-107	
8383626-2	1993	We report here on a Tn5tac1 insertion in Escherichia coli that results in a conditional (IPTG-elicited) folA mutant phenotype: During aerobic growth, IPTG caused decreased synthesis of dihydrofolate reductase (DHFR; encoded by the folA gene) and hypersensitivity to trimethoprim (a DHFR inhibitor); during anaerobic growth, IPTG elicited auxotrophy that was satisfied by thymine or glycine or threonine.	Glycine	382-389	Dihydrofolate reductase	Escherichia coli	185-208