PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
8420956-0	1993	Role of tyrosine residue 264 of RecA for the binding of cofactor and DNA.	Tyrosine	8-16	RAD51 recombinase	Homo sapiens	32-36	
8420956-1	1993	The tyrosine fluorescence of the RecA protein is quenched by about 15% upon binding of the cofactor analog adenosine 5"-O-(3-thiotriphosphate) (ATP gamma S).	Tyrosine	4-12	RAD51 recombinase	Homo sapiens	33-37	
8420956-4	1993	Upon DNA binding, a change of tyrosine fluorescence is observed both with the modified protein and with wild type RecA, indicating that DNA binding affects the environment of other tyrosine residues than Tyr-264.	Tyrosine	30-38	RAD51 recombinase	Homo sapiens	114-118	
8420956-4	1993	Upon DNA binding, a change of tyrosine fluorescence is observed both with the modified protein and with wild type RecA, indicating that DNA binding affects the environment of other tyrosine residues than Tyr-264.	Tyrosine	181-189	RAD51 recombinase	Homo sapiens	114-118	
8420956-4	1993	Upon DNA binding, a change of tyrosine fluorescence is observed both with the modified protein and with wild type RecA, indicating that DNA binding affects the environment of other tyrosine residues than Tyr-264.	Tyrosine	204-207	RAD51 recombinase	Homo sapiens	114-118	
8420956-7	1993	Tyr-264 may be an important residue for the allosteric effect induced by the cofactor for the binding of DNA to RecA.	Tyrosine	0-3	RAD51 recombinase	Homo sapiens	112-116	
8420956-10	1993	The fact that we observe no interaction of ATP gamma S with Tyr-103 (as evidenced from absence of fluorescence change) but instead with Tyr-264 may suggest an important conformational difference between the RecA complexes with, respectively, ADP and ATP.	Tyrosine	136-139	RAD51 recombinase	Homo sapiens	207-211