PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
9390185-2	1997	Here, we study the accessibility of the fluorescein covalently attached to the Lys515 at the nucleotide binding domain of the ATPase to the small collisional quencher iodide at pH 6 and 8, as well as the effect of ligand binding (La3+, La(3+)-nucleotide, and Ca2+).	lanthanum(3+)	230-234	dynein axonemal heavy chain 8	Homo sapiens	126-132	
9390185-6	1997	Taken together, these findings show the presence of structural flexibility in the FITC binding site and suggest a structural modulation of the Ca(2+)-ATPase nucleotide binding domain by pH and La3+ binding through long-range link-age mechanisms.	lanthanum(3+)	193-197	dynein axonemal heavy chain 8	Homo sapiens	150-156	
691040-6	1978	In other experiments, the use of La3+ to inhibit the Ca2+-pump allowed an estimate of the ATPase activity associated with Ca2+ extrusion.	lanthanum(3+)	33-37	dynein axonemal heavy chain 8	Homo sapiens	90-96