PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
9537992-0	1998	Structural evidence for the presence of a secondary calcium binding site in human alpha-lactalbumin.	Calcium	52-59	lactalbumin alpha	Homo sapiens	82-99	
9537992-1	1998	The high-resolution X-ray crystal structure of human alpha-lactalbumin (at 1.8 A) in the presence of an elevated level of calcium reveals a new secondary calcium binding site, 7.9 A away from the primary calcium binding site known in all alpha-lactalbumin structures so far.	Calcium	122-129	lactalbumin alpha	Homo sapiens	53-70	
9537992-1	1998	The high-resolution X-ray crystal structure of human alpha-lactalbumin (at 1.8 A) in the presence of an elevated level of calcium reveals a new secondary calcium binding site, 7.9 A away from the primary calcium binding site known in all alpha-lactalbumin structures so far.	Calcium	154-161	lactalbumin alpha	Homo sapiens	53-70	
9537992-1	1998	The high-resolution X-ray crystal structure of human alpha-lactalbumin (at 1.8 A) in the presence of an elevated level of calcium reveals a new secondary calcium binding site, 7.9 A away from the primary calcium binding site known in all alpha-lactalbumin structures so far.	Calcium	154-161	lactalbumin alpha	Homo sapiens	238-255	
9537992-1	1998	The high-resolution X-ray crystal structure of human alpha-lactalbumin (at 1.8 A) in the presence of an elevated level of calcium reveals a new secondary calcium binding site, 7.9 A away from the primary calcium binding site known in all alpha-lactalbumin structures so far.	Calcium	154-161	lactalbumin alpha	Homo sapiens	53-70	
9537992-1	1998	The high-resolution X-ray crystal structure of human alpha-lactalbumin (at 1.8 A) in the presence of an elevated level of calcium reveals a new secondary calcium binding site, 7.9 A away from the primary calcium binding site known in all alpha-lactalbumin structures so far.	Calcium	154-161	lactalbumin alpha	Homo sapiens	238-255	
9537992-7	1998	The proximity of the manganese and calcium binding region and the location of the functional site on one side of the charged surface of the alpha-lactalbumin molecule suggest that these binding sites might play a role in the formation of the lactose synthase complex.	Calcium	35-42	lactalbumin alpha	Homo sapiens	140-157