PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
11014304-2	2000	Chemical modification of potato apyrase suggests that tryptophan residues are close to the nucleotide binding site.	Tryptophan	54-64	apyrase	Solanum tuberosum	32-39	
11014304-3	2000	Kd values (+/- Ca2+) for the complexes of apyrase with the non-hydrolysable phosphonate adenine nucleotide analogues, adenosine 5"-(beta,gamma-methylene) triphosphate and adenosine 5"-(alpha,beta-methylene) diphosphate, were obtained from quenching of the intrinsic enzyme fluorescence.	phosphonate adenine nucleotide	76-106	apyrase	Solanum tuberosum	42-49	
11014304-3	2000	Kd values (+/- Ca2+) for the complexes of apyrase with the non-hydrolysable phosphonate adenine nucleotide analogues, adenosine 5"-(beta,gamma-methylene) triphosphate and adenosine 5"-(alpha,beta-methylene) diphosphate, were obtained from quenching of the intrinsic enzyme fluorescence.	5'-adenylyl (beta,gamma-methylene)diphosphonate	118-166	apyrase	Solanum tuberosum	42-49	
11014304-3	2000	Kd values (+/- Ca2+) for the complexes of apyrase with the non-hydrolysable phosphonate adenine nucleotide analogues, adenosine 5"-(beta,gamma-methylene) triphosphate and adenosine 5"-(alpha,beta-methylene) diphosphate, were obtained from quenching of the intrinsic enzyme fluorescence.	alpha,beta-methyleneadenosine 5'-diphosphate	171-218	apyrase	Solanum tuberosum	42-49	
11014304-5	2000	1,N6-ethenoadenosine triphosphate and 1,N6-ethenoadenosine diphosphate) were hydrolysed by apyrase in the presence of Ca2+, indicating binding to the active site.	1,n6-ethenoadenosine triphosphate	0-33	apyrase	Solanum tuberosum	91-98	
11014304-5	2000	1,N6-ethenoadenosine triphosphate and 1,N6-ethenoadenosine diphosphate) were hydrolysed by apyrase in the presence of Ca2+, indicating binding to the active site.	1,N(6)-ethenoadenosine diphosphate	38-70	apyrase	Solanum tuberosum	91-98