PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
16153625-7	2006	Substitution of residue 72 from a helix former leucine to a helix breaker, proline, is predicted to change the secondary structure of the C-terminal helix and subsequently alter the interaction between apo C-II and LPL.	Leucine	47-54	apolipoprotein C2	Homo sapiens	202-210	
6328478-5	1984	The pCII -711 clone contains a 36-bp DNA sequence upstream from that specifying the NH2-terminal threonine which, when read in frame, specifies the amino acid sequence Leu-Val-Leu-Leu-Val-Leu-Gly-Phe-Glu-Val-Gln-Gly and may be part of an apo CII signal peptide.	Leucine	168-171	apolipoprotein C2	Homo sapiens	238-245	
6328478-5	1984	The pCII -711 clone contains a 36-bp DNA sequence upstream from that specifying the NH2-terminal threonine which, when read in frame, specifies the amino acid sequence Leu-Val-Leu-Leu-Val-Leu-Gly-Phe-Glu-Val-Gln-Gly and may be part of an apo CII signal peptide.	Leucine	176-179	apolipoprotein C2	Homo sapiens	238-245