PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
9184148-0	1997	The oligosaccharide side chain on Asn-135 of alpha-antithrombin, absent in beta-antithrombin, decreases the heparin affinity of the inhibitor by affecting the heparin-induced conformational change.	Asparagine	34-37	serpin family C member 1	Homo sapiens	51-63	
9184148-0	1997	The oligosaccharide side chain on Asn-135 of alpha-antithrombin, absent in beta-antithrombin, decreases the heparin affinity of the inhibitor by affecting the heparin-induced conformational change.	Asparagine	34-37	serpin family C member 1	Homo sapiens	80-92	
9184148-1	1997	The beta-form of antithrombin, lacking a carbohydrate side chain on Asn-135, is known to bind heparin more tightly than the fully glycosylated alpha-form.	Asparagine	68-71	serpin family C member 1	Homo sapiens	17-29	
9184148-7	1997	The carbohydrate side chain at Asn-135 thus reduces the heparin affinity of alpha-antithrombin primarily by interfering with the heparin-induced conformational change.	Asparagine	31-34	serpin family C member 1	Homo sapiens	82-94