PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
30431391-1	2019	According to the X-ray crystal structures of CYP17A1 (including its complexes with inhibitors), it is shown that a hydrogen bond exists between CYP17A1 and its inhibitors (such as abiraterone and TOK-001).	abiraterone	180-191	cytochrome P450 family 17 subfamily A member 1	Homo sapiens	45-52	
30431391-1	2019	According to the X-ray crystal structures of CYP17A1 (including its complexes with inhibitors), it is shown that a hydrogen bond exists between CYP17A1 and its inhibitors (such as abiraterone and TOK-001).	abiraterone	180-191	cytochrome P450 family 17 subfamily A member 1	Homo sapiens	144-151	
30431391-2	2019	Previous short MD simulations (50 ns) suggested that the binding of abiraterone to CYP17A1 is stronger than that of TOK-001.	abiraterone	68-79	cytochrome P450 family 17 subfamily A member 1	Homo sapiens	83-90	
30431391-3	2019	In this work, by carrying out long atomistic MD simulations (200 ns) of CYP17A1 and its complexes with abiraterone and TOK-001, we observed a binding mode between CYP17A1 and abiraterone, which is different from the binding mode between CYP17A1 and TOK-001.	abiraterone	103-114	cytochrome P450 family 17 subfamily A member 1	Homo sapiens	72-79	
30431391-3	2019	In this work, by carrying out long atomistic MD simulations (200 ns) of CYP17A1 and its complexes with abiraterone and TOK-001, we observed a binding mode between CYP17A1 and abiraterone, which is different from the binding mode between CYP17A1 and TOK-001.	abiraterone	103-114	cytochrome P450 family 17 subfamily A member 1	Homo sapiens	163-170	
30431391-3	2019	In this work, by carrying out long atomistic MD simulations (200 ns) of CYP17A1 and its complexes with abiraterone and TOK-001, we observed a binding mode between CYP17A1 and abiraterone, which is different from the binding mode between CYP17A1 and TOK-001.	abiraterone	103-114	cytochrome P450 family 17 subfamily A member 1	Homo sapiens	163-170	
30431391-3	2019	In this work, by carrying out long atomistic MD simulations (200 ns) of CYP17A1 and its complexes with abiraterone and TOK-001, we observed a binding mode between CYP17A1 and abiraterone, which is different from the binding mode between CYP17A1 and TOK-001.	abiraterone	175-186	cytochrome P450 family 17 subfamily A member 1	Homo sapiens	72-79	
30431391-3	2019	In this work, by carrying out long atomistic MD simulations (200 ns) of CYP17A1 and its complexes with abiraterone and TOK-001, we observed a binding mode between CYP17A1 and abiraterone, which is different from the binding mode between CYP17A1 and TOK-001.	abiraterone	175-186	cytochrome P450 family 17 subfamily A member 1	Homo sapiens	163-170	
30431391-3	2019	In this work, by carrying out long atomistic MD simulations (200 ns) of CYP17A1 and its complexes with abiraterone and TOK-001, we observed a binding mode between CYP17A1 and abiraterone, which is different from the binding mode between CYP17A1 and TOK-001.	abiraterone	175-186	cytochrome P450 family 17 subfamily A member 1	Homo sapiens	163-170	
30431391-4	2019	In the case of abiraterone binding, the unfilled volume in the active site cavity increases the freedom of movement of abiraterone within CYP17A1, leading to the collective motions of the helices G and B" as well as the breaking of hydrogen bond existing between the 3beta-OH group of abiraterone and N202 of CYP17A1.	abiraterone	15-26	cytochrome P450 family 17 subfamily A member 1	Homo sapiens	138-145	
30431391-4	2019	In the case of abiraterone binding, the unfilled volume in the active site cavity increases the freedom of movement of abiraterone within CYP17A1, leading to the collective motions of the helices G and B" as well as the breaking of hydrogen bond existing between the 3beta-OH group of abiraterone and N202 of CYP17A1.	abiraterone	15-26	cytochrome P450 family 17 subfamily A member 1	Homo sapiens	309-316	
30431391-4	2019	In the case of abiraterone binding, the unfilled volume in the active site cavity increases the freedom of movement of abiraterone within CYP17A1, leading to the collective motions of the helices G and B" as well as the breaking of hydrogen bond existing between the 3beta-OH group of abiraterone and N202 of CYP17A1.	abiraterone	119-130	cytochrome P450 family 17 subfamily A member 1	Homo sapiens	138-145	
30431391-4	2019	In the case of abiraterone binding, the unfilled volume in the active site cavity increases the freedom of movement of abiraterone within CYP17A1, leading to the collective motions of the helices G and B" as well as the breaking of hydrogen bond existing between the 3beta-OH group of abiraterone and N202 of CYP17A1.	abiraterone	119-130	cytochrome P450 family 17 subfamily A member 1	Homo sapiens	309-316	
30431391-4	2019	In the case of abiraterone binding, the unfilled volume in the active site cavity increases the freedom of movement of abiraterone within CYP17A1, leading to the collective motions of the helices G and B" as well as the breaking of hydrogen bond existing between the 3beta-OH group of abiraterone and N202 of CYP17A1.	abiraterone	119-130	cytochrome P450 family 17 subfamily A member 1	Homo sapiens	138-145	
30431391-4	2019	In the case of abiraterone binding, the unfilled volume in the active site cavity increases the freedom of movement of abiraterone within CYP17A1, leading to the collective motions of the helices G and B" as well as the breaking of hydrogen bond existing between the 3beta-OH group of abiraterone and N202 of CYP17A1.	abiraterone	119-130	cytochrome P450 family 17 subfamily A member 1	Homo sapiens	309-316	
30431391-6	2019	By pulling the two inhibitors (abiraterone and TOK-001) out of the binding pocket in CYP17A1, we discovered that abiraterone and TOK-001 were moved from their binding sites to the surface of protein similarly through the channels formed by the helices G and B".	abiraterone	31-42	cytochrome P450 family 17 subfamily A member 1	Homo sapiens	85-92	
30431391-6	2019	By pulling the two inhibitors (abiraterone and TOK-001) out of the binding pocket in CYP17A1, we discovered that abiraterone and TOK-001 were moved from their binding sites to the surface of protein similarly through the channels formed by the helices G and B".	abiraterone	113-124	cytochrome P450 family 17 subfamily A member 1	Homo sapiens	85-92	
30431391-7	2019	In addition, based on the free energy calculations, one can see that it is energetically favorable for the two inhibitors (abiraterone and TOK-001) to enter into the binding pocket in CYP17A1.	abiraterone	123-134	cytochrome P450 family 17 subfamily A member 1	Homo sapiens	184-191