PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
1547237-6	1992	The global folding of these conformations is similar to that in the thrombin-bound state, as indicated by NOE"s involving the side-chain protons of residues Phe(56), Ile(59), Pro(60), Tyr(63), and Leu(64).	Isoleucine	166-169	coagulation factor II, thrombin	Homo sapiens	68-76	
1547237-9	1992	An analysis of the side-chain rotamers revealed that, upon binding to thrombin, there may be a rotation around the alpha CH-beta CH bond of Ile(59) such that Ile(59) adopts a gauche- (chi 1 = +60) conformation in contrast to the highly populated trans (chi 1 = -60) found for Ile(59) in the free peptide.	Isoleucine	140-143	coagulation factor II, thrombin	Homo sapiens	70-78	
1547237-9	1992	An analysis of the side-chain rotamers revealed that, upon binding to thrombin, there may be a rotation around the alpha CH-beta CH bond of Ile(59) such that Ile(59) adopts a gauche- (chi 1 = +60) conformation in contrast to the highly populated trans (chi 1 = -60) found for Ile(59) in the free peptide.	Isoleucine	158-161	coagulation factor II, thrombin	Homo sapiens	70-78	
1547237-9	1992	An analysis of the side-chain rotamers revealed that, upon binding to thrombin, there may be a rotation around the alpha CH-beta CH bond of Ile(59) such that Ile(59) adopts a gauche- (chi 1 = +60) conformation in contrast to the highly populated trans (chi 1 = -60) found for Ile(59) in the free peptide.	Isoleucine	158-161	coagulation factor II, thrombin	Homo sapiens	70-78	
1547237-11	1992	The apparent preference for a gauche- (chi 1 = +60) side-chain conformation of Ile(59) in the bound state may be explained by the existence of a positively charged arginine residue among the hydrophobic residues in the thrombin exosite.	Isoleucine	79-82	coagulation factor II, thrombin	Homo sapiens	219-227