PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
690134-1	1978	Polypeptide sequence determination and assignment of the oligosaccharide attachment site in C5a.	Oligosaccharides	57-72	complement C5a receptor 1	Homo sapiens	92-95	
690134-11	1978	The carbohydrate portion of C5a exists as a single complex oligosaccharide unit attached to an asparagine at position 64.	Carbohydrates	4-16	complement C5a receptor 1	Homo sapiens	28-31	
690134-11	1978	The carbohydrate portion of C5a exists as a single complex oligosaccharide unit attached to an asparagine at position 64.	Oligosaccharides	59-74	complement C5a receptor 1	Homo sapiens	28-31	
690134-11	1978	The carbohydrate portion of C5a exists as a single complex oligosaccharide unit attached to an asparagine at position 64.	Asparagine	95-105	complement C5a receptor 1	Homo sapiens	28-31	
690134-12	1978	An unusual feature of the C5a molecule is its large content of half-cystine, which accounts for more than 9% of its total residues.	Cystine	68-75	complement C5a receptor 1	Homo sapiens	26-29	
690134-13	1978	Two repeating Cys sequences occur in the linear structure and 6 of the 7 half-cystines in C5a are located at nearly identical positions to those in the human C3a molecule.	Cysteine	14-17	complement C3	Homo sapiens	158-161	
690134-13	1978	Two repeating Cys sequences occur in the linear structure and 6 of the 7 half-cystines in C5a are located at nearly identical positions to those in the human C3a molecule.	Cystine	78-86	complement C5a receptor 1	Homo sapiens	90-93	
690134-13	1978	Two repeating Cys sequences occur in the linear structure and 6 of the 7 half-cystines in C5a are located at nearly identical positions to those in the human C3a molecule.	Cystine	78-86	complement C3	Homo sapiens	158-161	
690134-21	1978	Removal of the COOH-terminal arginyl residue from C5a reduces chemotactic activity; therefore, the terminal portion of this molecule appears to play an active role in stimulating leukocyte migration.	Carbonic Acid	15-19	complement C5a receptor 1	Homo sapiens	50-53	
690134-21	1978	Removal of the COOH-terminal arginyl residue from C5a reduces chemotactic activity; therefore, the terminal portion of this molecule appears to play an active role in stimulating leukocyte migration.	arginyl	29-36	complement C5a receptor 1	Homo sapiens	50-53	
690134-23	1978	Since methionine assumes a special functional importance in the formyl-Met peptides, attention is focused on the single methionyl residue in C5a.	Methionine	6-16	complement C5a receptor 1	Homo sapiens	141-144	
690134-24	1978	This methionyl residue, located near the COOH terminus of the molecule, may play an active role in the functional expression of C5a as a chemotactic factor.	Carbonic Acid	41-45	complement C5a receptor 1	Homo sapiens	128-131