PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
3463986-1	1986	A high-resolution x-ray crystallographic investigation of the complex between carboxypeptidase A (CPA; peptidyl-L-amino-acid hydrolase, EC 3.4.17.1) and the slowly hydrolyzed substrate glycyl-L-tyrosine was done at -9 degrees C. Although this enzyme-substrate complex has been the subject of earlier crystallographic investigation, a higher resolution electron-density map of the complex with greater occupancy of the substrate was desired.	glycyltyrosine	185-202	carboxypeptidase A1	Homo sapiens	78-96	
3463986-1	1986	A high-resolution x-ray crystallographic investigation of the complex between carboxypeptidase A (CPA; peptidyl-L-amino-acid hydrolase, EC 3.4.17.1) and the slowly hydrolyzed substrate glycyl-L-tyrosine was done at -9 degrees C. Although this enzyme-substrate complex has been the subject of earlier crystallographic investigation, a higher resolution electron-density map of the complex with greater occupancy of the substrate was desired.	glycyltyrosine	185-202	carboxypeptidase A1	Homo sapiens	98-101	
9801832-1	1998	The X-ray crystal structure of the complex of carboxypeptidase A (CPA) and Gly-Tyr, has been documented.	glycyltyrosine	75-82	carboxypeptidase A1	Homo sapiens	46-64	
9801832-1	1998	The X-ray crystal structure of the complex of carboxypeptidase A (CPA) and Gly-Tyr, has been documented.	glycyltyrosine	75-82	carboxypeptidase A1	Homo sapiens	66-69	
9801832-2	1998	The crystal structure reveals that both the amide carbonyl oxygen and the terminal amino nitrogen of Gly-Tyr coordinate to the active site zinc ion of CPA in a bidentate fashion, whereby the zinc-bound water molecule is displaced by the amino group.	glycyltyrosine	101-108	carboxypeptidase A1	Homo sapiens	151-154