PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
2350549-8	1990	Distance geometry calculations suggest that in the structure of the thrombin-bound hirudin peptides all the charged residues lie on the opposite side of a hydrophobic cluster formed by the nonpolar side chains of residues Phe(56), Ile(59), Pro(60), Tyr(63), and Leu(64).	Leucine	262-265	coagulation factor II, thrombin	Bos taurus	68-76	
1332764-4	1992	The hydrophobic side chains of residues Leu(P4) and Pro(P2) reside on the same side of the peptide backbone as indicated by transferred NOEs and were found by modeling to fit into a hydrophobic cage around the thrombin active site.	Leucine	40-43	coagulation factor II, thrombin	Bos taurus	210-218	
6326805-3	1984	The radiolabeled prothrombin synthesized in the cell-free system was then subjected to automated Edman degradation and shown to contain a leader sequence of at least 30 residues that was rich in leucine, phenylalanine, and alanine.	Leucine	195-202	coagulation factor II, thrombin	Bos taurus	17-28	
14340066-10	1965	The proposed amino acid sequence is: Asp-Asp-Ser-Ile/Leu-Asp-Ser-Leu/Ile-ArgThis peptide is released by lamprey thrombin but not by bovine thrombin.	Leucine	53-56	coagulation factor II, thrombin	Bos taurus	112-120