PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
32999062-4	2020	Lesion bypass is accomplished using a unique protein-template mechanism in which the templating base is evicted from the DNA helix and the incoming dCTP hydrogen bonds with an arginine side chain of Rev1.	Hydrogen	153-161	deoxycytidyl transferase	Saccharomyces cerevisiae S288C	199-203	
17960914-2	2007	The X-ray crystal structure of the Rev1p-DNA-dCTP ternary complex showed that Rev1p utilizes an unusual mechanism of nucleotide incorporation whereby the template residue is displaced from the DNA double helix and the side chain of Arg-324 forms hydrogen bonds with the incoming dCTP.	Hydrogen	246-254	deoxycytidyl transferase	Saccharomyces cerevisiae S288C	78-83	
16195463-3	2005	Instead, the template G is evicted from the DNA helix, and it makes optimal hydrogen bonds with a segment of Rev1.	Hydrogen	76-84	deoxycytidyl transferase	Saccharomyces cerevisiae S288C	109-113	
17960914-2	2007	The X-ray crystal structure of the Rev1p-DNA-dCTP ternary complex showed that Rev1p utilizes an unusual mechanism of nucleotide incorporation whereby the template residue is displaced from the DNA double helix and the side chain of Arg-324 forms hydrogen bonds with the incoming dCTP.	Hydrogen	246-254	deoxycytidyl transferase	Saccharomyces cerevisiae S288C	35-40