PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
11917030-11	2002	Because the function of the discriminatory residue depends on its specific spatial disposition this strongly suggests a similar architecture for the P protein dNTP-binding pocket as in other RTs.	Parathion	159-163	OCA2 melanosomal transmembrane protein	Homo sapiens	149-158	
17900649-2	2008	Thus, we mutated Phe 436, a bulky amino acid with aromatic side chain, at the putative dNTP-binding cleft in reverse transcriptase (RT) domain of P protein to smaller amino acids (Gly or Val), and examined RNA polymerase activity.	Parathion	87-91	OCA2 melanosomal transmembrane protein	Homo sapiens	146-155