PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
1824702-11	1991	Trypsin proteolysis studies indicate that the [Ala-163]recA and [Asn-160]recA proteins, like the wild-type recA protein, are organized into carboxyl-terminal and amino-terminal domains of nearly equal size.	Asparagine	65-68	RAD51 recombinase	Homo sapiens	73-77	
1824702-11	1991	Trypsin proteolysis studies indicate that the [Ala-163]recA and [Asn-160]recA proteins, like the wild-type recA protein, are organized into carboxyl-terminal and amino-terminal domains of nearly equal size.	Asparagine	65-68	RAD51 recombinase	Homo sapiens	73-77	
1824702-12	1991	According to this structural model, the [Ala-163]recA and [Asn-160]recA mutations may lie in a linker region joining these two domains.	Asparagine	59-62	RAD51 recombinase	Homo sapiens	67-71	
1824702-13	1991	We speculate that the [Ala-163]recA and [Asn-160]recA mutations interfere with an ATP-dependent conformational change of the recA protein that perhaps involves a change in the relative orientation of the carboxyl-terminal and amino-terminal domains.	Asparagine	41-44	RAD51 recombinase	Homo sapiens	49-53	
1824702-13	1991	We speculate that the [Ala-163]recA and [Asn-160]recA mutations interfere with an ATP-dependent conformational change of the recA protein that perhaps involves a change in the relative orientation of the carboxyl-terminal and amino-terminal domains.	Asparagine	41-44	RAD51 recombinase	Homo sapiens	49-53