PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
6325898-3	1983	It showed the following similarities to the normal C1q molecule: a high glycine content and the presence of hydroxyproline and hydroxylysine; subunits with apparent mol.	Hydroxylysine	127-140	complement C1q A chain	Homo sapiens	51-54	
3007627-7	1986	The C1q contains hydroxyproline, hydroxylysine, a high percentage of glycine and approximately 7% carbohydrate.	Hydroxylysine	33-46	complement C1q A chain	Homo sapiens	4-7	
6970196-6	1980	C1q contained hydroxyproline, hydroxylysine, a high percentage of glycine and approximately 9% carbohydrate and 14.8% nitrogen.	Hydroxylysine	30-43	complement C1q A chain	Homo sapiens	0-3	
6976996-6	1982	C1q contained hydroxyproline, hydroxylysine and high percentage of glycine.	Hydroxylysine	30-43	complement C1q A chain	Homo sapiens	0-3	
4352715-11	1972	Both human and rabbit subcomponent C1q contained hydroxyproline, hydroxylysine, a high percentage of glycine and approximately 8% carbohydrate.	Hydroxylysine	65-78	complement C1q A chain	Homo sapiens	35-38	
444207-2	1979	Human C1q, a subcomponent of the first component of complement, contains 67 disaccharides (glucosylgalactose) and 2.4 monosaccharides (galactose) linked to hydroxylysine in one molecule.	Hydroxylysine	156-169	complement C1q A chain	Homo sapiens	6-9	
444207-17	1979	Similarities between the extent of glycosylation of hydroxylysine residues in collagen-like regions in the subcomponent C1q molecule and that of the collagenous constituents of human glomerular basement membranes, aortic intima, skin A- and B-chains and of bovine anterior lens capsule are discussed.	Hydroxylysine	52-65	complement C1q A chain	Homo sapiens	120-123