PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
8318164-4	1993	p21 is thought to be activated by the binding of GTP in place of GDP to the protein.	Guanosine Diphosphate	65-68	H3 histone pseudogene 16	Homo sapiens	0-3	
8318164-5	1993	We have previously constructed the three-dimensional structure of the p21 protein bound to GDP from an available alpha-carbon tracing of this protein using a combination of molecular dynamics and energy minimization (Dykes, et al., J. Biomol.	Guanosine Diphosphate	91-94	H3 histone pseudogene 16	Homo sapiens	70-73	
8318164-9	1993	In this communication we compare our computed structure for the p21-GDP complex to this x-ray crystal structure.	Guanosine Diphosphate	68-71	H3 histone pseudogene 16	Homo sapiens	64-67	
8318164-15	1993	Both of these regions have been found in x-ray crystallographic studies of p21-GDP and p21-GTP complexes to undergo significant changes in conformation upon the binding of GTP in place of GDP to the protein.	Guanosine Diphosphate	79-82	H3 histone pseudogene 16	Homo sapiens	75-78	
8318164-15	1993	Both of these regions have been found in x-ray crystallographic studies of p21-GDP and p21-GTP complexes to undergo significant changes in conformation upon the binding of GTP in place of GDP to the protein.	Guanosine Diphosphate	188-191	H3 histone pseudogene 16	Homo sapiens	75-78	
8318164-15	1993	Both of these regions have been found in x-ray crystallographic studies of p21-GDP and p21-GTP complexes to undergo significant changes in conformation upon the binding of GTP in place of GDP to the protein.	Guanosine Diphosphate	188-191	H3 histone pseudogene 16	Homo sapiens	87-90