BindingDB Reactant_set_id	Ligand SMILES	Ligand InChI	Ligand InChI Key	BindingDB MonomerID	BindingDB Ligand Name	Target Name	Target Source Organism According to Curator or DataSource	Ki (nM)	IC50 (nM)	Kd (nM)	EC50 (nM)	kon (M-1-s-1)	koff (s-1)	pH	Temp (C)	Curation/DataSource	Article DOI	BindingDB Entry DOI	PMID	PubChem AID	Patent Number	Authors	Institution	Link to Ligand in BindingDB	Link to Target in BindingDB	Link to Ligand-Target Pair in BindingDB	Ligand HET ID in PDB	PDB ID(s) for Ligand-Target Complex	PubChem CID of Ligand	PubChem SID of Ligand	ChEBI ID of Ligand	ChEMBL ID of Ligand	DrugBank ID of Ligand	IUPHAR_GRAC ID of Ligand	KEGG ID of Ligand	ZINC ID of Ligand	Number of Protein Chains in Target (>1 implies a multichain complex)	BindingDB Target Chain Sequence	PDB ID(s) of Target Chain	UniProt (SwissProt) Recommended Name of Target Chain	UniProt (SwissProt) Entry Name of Target Chain	UniProt (SwissProt) Primary ID of Target Chain	UniProt (SwissProt) Secondary ID(s) of Target Chain	UniProt (SwissProt) Alternative ID(s) of Target Chain	UniProt (TrEMBL) Submitted Name of Target Chain	UniProt (TrEMBL) Entry Name of Target Chain	UniProt (TrEMBL) Primary ID of Target Chain	UniProt (TrEMBL) Secondary ID(s) of Target Chain	UniProt (TrEMBL) Alternative ID(s) of Target Chain
406898	FC1(F)C[C@@H](C#N)N(C1)C(=O)CNC(=O)c1cccc2ccccc12	InChI=1S/C18H15F2N3O2/c19-18(20)8-13(9-21)23(11-18)16(24)10-22-17(25)15-7-3-5-12-4-1-2-6-14(12)15/h1-7,13H,8,10-11H2,(H,22,25)/t13-/m0/s1	YJNMDFARAFJSEZ-ZDUSSCGKSA-N	50382283	CHEMBL2022530::US9346814, Ref. Cmpd No 1 (Example 2)	Prolyl endopeptidase FAP			 110					8.3	37.00 C	US Patent		10.7270/Q2W37V6D		aid1802953	US9346814	Jansen, K; De Meester, I; Heirbaut, L; Cheng, JD; Joossens, J; Augustyns, K; Van Der Veken, P	Universiteit Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50382283	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50382283&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			66561557	160861366		CHEMBL2022530				ZINC84615945	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
406899	O=C(CNC(=O)c1cccc2ccccc12)N1CCCC1C#N	InChI=1S/C18H17N3O2/c19-11-14-7-4-10-21(14)17(22)12-20-18(23)16-9-3-6-13-5-1-2-8-15(13)16/h1-3,5-6,8-9,14H,4,7,10,12H2,(H,20,23)	HSIDTMLTVRFYGR-UHFFFAOYSA-N	233320	US9346814, Ref. Cmpd No 2	Prolyl endopeptidase FAP			 670					8.3	37.00 C	US Patent		10.7270/Q2W37V6D		aid1802953	US9346814	Jansen, K; De Meester, I; Heirbaut, L; Cheng, JD; Joossens, J; Augustyns, K; Van Der Veken, P	Universiteit Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=233320	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=233320&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			73224265	340093413							1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
406900	O=C(CNC(=O)c1cnc2ccccc2c1)N1CCC[C@H]1C#N	InChI=1S/C17H16N4O2/c18-9-14-5-3-7-21(14)16(22)11-20-17(23)13-8-12-4-1-2-6-15(12)19-10-13/h1-2,4,6,8,10,14H,3,5,7,11H2,(H,20,23)/t14-/m0/s1	HNRNBVNSDXARCW-AWEZNQCLSA-N	233321	US9346814, Ref. Cmpd No 3 (Example 5)	Prolyl endopeptidase FAP			 5300					8.3	37.00 C	US Patent		10.7270/Q2W37V6D		aid1802953	US9346814	Jansen, K; De Meester, I; Heirbaut, L; Cheng, JD; Joossens, J; Augustyns, K; Van Der Veken, P	Universiteit Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=233321	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=233321&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			71667225	340093414							1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
406901	O=C(CNC(=O)c1cc2ccccc2[nH]1)N1CCCC1C#N			233325	US9346814, Ref. Cmpd No 4	Prolyl endopeptidase FAP			 15400					8.3	37.00 C	US Patent		10.7270/Q2W37V6D		aid1802953	US9346814	Jansen, K; De Meester, I; Heirbaut, L; Cheng, JD; Joossens, J; Augustyns, K; Van Der Veken, P	Universiteit Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=233325	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=233325&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			129010653	340093418							1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
406902	O=C(CNC(=O)c1c[nH]c2ccccc12)N1CCCC1C#N			233326	US9346814, Ref. Cmpd No 5	Prolyl endopeptidase FAP			 3600					8.3	37.00 C	US Patent		10.7270/Q2W37V6D		aid1802953	US9346814	Jansen, K; De Meester, I; Heirbaut, L; Cheng, JD; Joossens, J; Augustyns, K; Van Der Veken, P	Universiteit Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=233326	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=233326&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			78140030	340093419							1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
406903	O=C(CNC(=O)c1cccc2cccnc12)N1CCC[C@H]1C#N	InChI=1S/C17H16N4O2/c18-10-13-6-3-9-21(13)15(22)11-20-17(23)14-7-1-4-12-5-2-8-19-16(12)14/h1-2,4-5,7-8,13H,3,6,9,11H2,(H,20,23)/t13-/m0/s1	DTZGFBWXCPGCKM-ZDUSSCGKSA-N	50434189	CHEMBL2385280::US9346814, Ref. Cmpd No 6 (Example 7)	Prolyl endopeptidase FAP			 2170					8.3	37.00 C	US Patent		10.7270/Q2W37V6D		aid1802953	US9346814	Jansen, K; De Meester, I; Heirbaut, L; Cheng, JD; Joossens, J; Augustyns, K; Van Der Veken, P	Universiteit Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50434189	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50434189&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			71667227	175446506		CHEMBL2385280				ZINC96270299	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
406904	O=C(CNC(=O)c1cccc2ncccc12)N1CCC[C@H]1C#N	InChI=1S/C17H16N4O2/c18-10-12-4-3-9-21(12)16(22)11-20-17(23)14-5-1-7-15-13(14)6-2-8-19-15/h1-2,5-8,12H,3-4,9,11H2,(H,20,23)/t12-/m0/s1	XSKKWTLPSOKUFE-LBPRGKRZSA-N	50434159	CHEMBL2385277::US9346814, Ref Cmpd No 7 (example 17)	Prolyl endopeptidase FAP			 420					8.3	37.00 C	US Patent		10.7270/Q2W37V6D		aid1802953	US9346814	Jansen, K; De Meester, I; Heirbaut, L; Cheng, JD; Joossens, J; Augustyns, K; Van Der Veken, P	Universiteit Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50434159	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50434159&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			71655625	175446476		CHEMBL2385277				ZINC96270269	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
406905	O=C(CNC(=O)c1cncc2ccccc12)N1CCCC1C#N	InChI=1S/C17H16N4O2/c18-8-13-5-3-7-21(13)16(22)11-20-17(23)15-10-19-9-12-4-1-2-6-14(12)15/h1-2,4,6,9-10,13H,3,5,7,11H2,(H,20,23)	YNGPRBCXHBASGU-UHFFFAOYSA-N	233327	US9346814, Ref Cmpd No 8	Prolyl endopeptidase FAP			>100000					8.3	37.00 C	US Patent		10.7270/Q2W37V6D		aid1802953	US9346814	Jansen, K; De Meester, I; Heirbaut, L; Cheng, JD; Joossens, J; Augustyns, K; Van Der Veken, P	Universiteit Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=233327	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=233327&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			78140062	340093420							1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
406906	O=C(CNC(=O)c1ccnc2ccccc12)N1CCC[C@H]1C#N	InChI=1S/C17H16N4O2/c18-10-12-4-3-9-21(12)16(22)11-20-17(23)14-7-8-19-15-6-2-1-5-13(14)15/h1-2,5-8,12H,3-4,9,11H2,(H,20,23)/t12-/m0/s1	MTHMMXFBHKGAAI-LBPRGKRZSA-N	50434188	CHEMBL2385281::US9346814, Cmpd No 2 Example 3	Prolyl endopeptidase FAP			>100000					8.3	37.00 C	US Patent		10.7270/Q2W37V6D		aid1802953	US9346814	Jansen, K; De Meester, I; Heirbaut, L; Cheng, JD; Joossens, J; Augustyns, K; Van Der Veken, P	Universiteit Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50434188	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50434188&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			71655554	175446505		CHEMBL2385281				ZINC96270298	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
406907	O=C(CNC(=O)c1ccnc2ccccc12)N1CCCC1C#N	InChI=1S/C17H16N4O2/c18-10-12-4-3-9-21(12)16(22)11-20-17(23)14-7-8-19-15-6-2-1-5-13(14)15/h1-2,5-8,12H,3-4,9,11H2,(H,20,23)	MTHMMXFBHKGAAI-UHFFFAOYSA-N	233328	US9346814, Ref Cmpd No 9	Prolyl endopeptidase FAP			>100000					8.3	37.00 C	US Patent		10.7270/Q2W37V6D		aid1802953	US9346814	Jansen, K; De Meester, I; Heirbaut, L; Cheng, JD; Joossens, J; Augustyns, K; Van Der Veken, P	Universiteit Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=233328	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=233328&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			78140029	340093421							1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
406908	O=C(CNC(=O)c1cccc2cnccc12)N1CCCC1C#N	InChI=1S/C17H16N4O2/c18-9-13-4-2-8-21(13)16(22)11-20-17(23)15-5-1-3-12-10-19-7-6-14(12)15/h1,3,5-7,10,13H,2,4,8,11H2,(H,20,23)	DSIXHJMXKMIOFX-UHFFFAOYSA-N	233329	US9346814, Ref Cmpd No 10	Prolyl endopeptidase FAP			>100000					8.3	37.00 C	US Patent		10.7270/Q2W37V6D		aid1802953	US9346814	Jansen, K; De Meester, I; Heirbaut, L; Cheng, JD; Joossens, J; Augustyns, K; Van Der Veken, P	Universiteit Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=233329	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=233329&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			78140064	340093422							1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
406909	FC1(F)C[C@@H](C#N)N(C1)C(=O)CNC(=O)c1ccnc2ccccc12	InChI=1S/C17H14F2N4O2/c18-17(19)7-11(8-20)23(10-17)15(24)9-22-16(25)13-5-6-21-14-4-2-1-3-12(13)14/h1-6,11H,7,9-10H2,(H,22,25)/t11-/m0/s1	PUOOCZVRHBHJRS-NSHDSACASA-N	50009366	CHEMBL3233842::US11504364, Compound Ref.-Comp.::US9346814, Cmpd No 1, Example 1	Prolyl endopeptidase FAP			 3.2					8.3	37.00 C	US Patent		10.7270/Q2W37V6D		aid1802953	US9346814	Jansen, K; De Meester, I; Heirbaut, L; Cheng, JD; Joossens, J; Augustyns, K; Van Der Veken, P	Universiteit Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50009366	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50009366&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			71621488	242057372		CHEMBL3233842					1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
406910	O=C(CNC(=O)c1ccnc2ccccc12)N1CCC[C@H]1C#N	InChI=1S/C17H16N4O2/c18-10-12-4-3-9-21(12)16(22)11-20-17(23)14-7-8-19-15-6-2-1-5-13(14)15/h1-2,5-8,12H,3-4,9,11H2,(H,20,23)/t12-/m0/s1	MTHMMXFBHKGAAI-LBPRGKRZSA-N	50434188	CHEMBL2385281::US9346814, Cmpd No 2 Example 3	Prolyl endopeptidase FAP			 10.3					8.3	37.00 C	US Patent		10.7270/Q2W37V6D		aid1802953	US9346814	Jansen, K; De Meester, I; Heirbaut, L; Cheng, JD; Joossens, J; Augustyns, K; Van Der Veken, P	Universiteit Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50434188	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50434188&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			71655554	175446505		CHEMBL2385281				ZINC96270298	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
406911	Cc1cc(C(=O)NCC(=O)N2CCC[C@H]2C#N)c2ccccc2n1	InChI=1S/C18H18N4O2/c1-12-9-15(14-6-2-3-7-16(14)21-12)18(24)20-11-17(23)22-8-4-5-13(22)10-19/h2-3,6-7,9,13H,4-5,8,11H2,1H3,(H,20,24)/t13-/m0/s1	XTSOTMGJBJQAAZ-ZDUSSCGKSA-N	50434176	CHEMBL2385293::US9346814, Cmpd No 3 Example 4	Prolyl endopeptidase FAP			 670					8.3	37.00 C	US Patent		10.7270/Q2W37V6D		aid1802953	US9346814	Jansen, K; De Meester, I; Heirbaut, L; Cheng, JD; Joossens, J; Augustyns, K; Van Der Veken, P	Universiteit Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50434176	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50434176&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			71667081	175446493		CHEMBL2385293				ZINC96270286	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
406912	O=C(CNC(=O)c1ccncc1)N1CCC[C@H]1C#N	InChI=1S/C13H14N4O2/c14-8-11-2-1-7-17(11)12(18)9-16-13(19)10-3-5-15-6-4-10/h3-6,11H,1-2,7,9H2,(H,16,19)/t11-/m0/s1	QNDFOEYFDNZPFT-NSHDSACASA-N	50009334	CHEMBL3233554::US9346814, Cmpd No 4 Example 6	Prolyl endopeptidase FAP			 63					8.3	37.00 C	US Patent		10.7270/Q2W37V6D		aid1802953	US9346814	Jansen, K; De Meester, I; Heirbaut, L; Cheng, JD; Joossens, J; Augustyns, K; Van Der Veken, P	Universiteit Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50009334	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50009334&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			71667226	103922390		CHEMBL3233554				ZINC95616104	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
406913	Cc1nc2ccccc2c(C(=O)NCC(=O)N2CCC[C@H]2C#N)c1O	InChI=1S/C18H18N4O3/c1-11-17(24)16(13-6-2-3-7-14(13)21-11)18(25)20-10-15(23)22-8-4-5-12(22)9-19/h2-3,6-7,12,24H,4-5,8,10H2,1H3,(H,20,25)/t12-/m0/s1	QPYHHKIZAVGBJJ-LBPRGKRZSA-N	50434175	CHEMBL2385294::US9346814, Cmpd No 5 Example 8	Prolyl endopeptidase FAP			 5900					8.3	37.00 C	US Patent		10.7270/Q2W37V6D		aid1802953	US9346814	Jansen, K; De Meester, I; Heirbaut, L; Cheng, JD; Joossens, J; Augustyns, K; Van Der Veken, P	Universiteit Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50434175	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50434175&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			71655556	175446492		CHEMBL2385294				ZINC96270285	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
406914	Fc1ccc2nccc(C(=O)NCC(=O)N3CCC[C@H]3C#N)c2c1	InChI=1S/C17H15FN4O2/c18-11-3-4-15-14(8-11)13(5-6-20-15)17(24)21-10-16(23)22-7-1-2-12(22)9-19/h3-6,8,12H,1-2,7,10H2,(H,21,24)/t12-/m0/s1	CRWCYVOHVXAEMF-LBPRGKRZSA-N	50434166	CHEMBL2385270::US9346814, Cmpd No 6 Example 9	Prolyl endopeptidase FAP			 10.3					8.3	37.00 C	US Patent		10.7270/Q2W37V6D		aid1802953	US9346814	Jansen, K; De Meester, I; Heirbaut, L; Cheng, JD; Joossens, J; Augustyns, K; Van Der Veken, P	Universiteit Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50434166	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50434166&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			71667229	175446483		CHEMBL2385270				ZINC96270276	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
406915	Clc1ccc2nccc(C(=O)NCC(=O)N3CCC[C@H]3C#N)c2c1	InChI=1S/C17H15ClN4O2/c18-11-3-4-15-14(8-11)13(5-6-20-15)17(24)21-10-16(23)22-7-1-2-12(22)9-19/h3-6,8,12H,1-2,7,10H2,(H,21,24)/t12-/m0/s1	KPLYEVMFCDTZKW-LBPRGKRZSA-N	50434168	CHEMBL2385301::US9346814, Cmpd No 7 Example 10	Prolyl endopeptidase FAP			 14					8.3	37.00 C	US Patent		10.7270/Q2W37V6D		aid1802953	US9346814	Jansen, K; De Meester, I; Heirbaut, L; Cheng, JD; Joossens, J; Augustyns, K; Van Der Veken, P	Universiteit Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50434168	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50434168&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			71667230	175446485		CHEMBL2385301				ZINC96270278	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
406916	FC(F)(F)Oc1ccc2nccc(C(=O)NCC(=O)N3CCC[C@H]3C#N)c2c1	InChI=1S/C18H15F3N4O3/c19-18(20,21)28-12-3-4-15-14(8-12)13(5-6-23-15)17(27)24-10-16(26)25-7-1-2-11(25)9-22/h3-6,8,11H,1-2,7,10H2,(H,24,27)/t11-/m0/s1	VSNIZLIYSJARCU-NSHDSACASA-N	50434167	CHEMBL2385302::US9346814, Cmpd No 8 Example 11	Prolyl endopeptidase FAP			 12					8.3	37.00 C	US Patent		10.7270/Q2W37V6D		aid1802953	US9346814	Jansen, K; De Meester, I; Heirbaut, L; Cheng, JD; Joossens, J; Augustyns, K; Van Der Veken, P	Universiteit Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50434167	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50434167&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			71667231	175446484		CHEMBL2385302				ZINC96270277	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
406917	Clc1cccc2c(ccnc12)C(=O)NCC(=O)N1CCC[C@H]1C#N	InChI=1S/C17H15ClN4O2/c18-14-5-1-4-12-13(6-7-20-16(12)14)17(24)21-10-15(23)22-8-2-3-11(22)9-19/h1,4-7,11H,2-3,8,10H2,(H,21,24)/t11-/m0/s1	GVEVKFYZSMHFEB-NSHDSACASA-N	50434162	CHEMBL2385274::US9346814, Cmpd No 9 Example 12	Prolyl endopeptidase FAP			 190					8.3	37.00 C	US Patent		10.7270/Q2W37V6D		aid1802953	US9346814	Jansen, K; De Meester, I; Heirbaut, L; Cheng, JD; Joossens, J; Augustyns, K; Van Der Veken, P	Universiteit Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50434162	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50434162&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			71667375	175446479		CHEMBL2385274				ZINC96270272	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
406918	Brc1cccc2c(ccnc12)C(=O)NCC(=O)N1CCC[C@H]1C#N	InChI=1S/C17H15BrN4O2/c18-14-5-1-4-12-13(6-7-20-16(12)14)17(24)21-10-15(23)22-8-2-3-11(22)9-19/h1,4-7,11H,2-3,8,10H2,(H,21,24)/t11-/m0/s1	KEZAZIKPPLGXGR-NSHDSACASA-N	50434161	CHEMBL2385275::US9346814, Cmpd No 10 Example 13	Prolyl endopeptidase FAP			 370					8.3	37.00 C	US Patent		10.7270/Q2W37V6D		aid1802953	US9346814	Jansen, K; De Meester, I; Heirbaut, L; Cheng, JD; Joossens, J; Augustyns, K; Van Der Veken, P	Universiteit Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50434161	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50434161&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			71667376	175446478		CHEMBL2385275				ZINC96270271	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
406919	COc1ccc2nccc(C(=O)NCC(=O)N3CCC[C@H]3C#N)c2c1	InChI=1S/C18H18N4O3/c1-25-13-4-5-16-15(9-13)14(6-7-20-16)18(24)21-11-17(23)22-8-2-3-12(22)10-19/h4-7,9,12H,2-3,8,11H2,1H3,(H,21,24)/t12-/m0/s1	YPWQFVMQCFSLCP-LBPRGKRZSA-N	50434165	CHEMBL2385271::US9346814, Cmpd No 11 Example 14	Prolyl endopeptidase FAP			 9.2					8.3	37.00 C	US Patent		10.7270/Q2W37V6D		aid1802953	US9346814	Jansen, K; De Meester, I; Heirbaut, L; Cheng, JD; Joossens, J; Augustyns, K; Van Der Veken, P	Universiteit Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50434165	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50434165&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			71667377	175446482		CHEMBL2385271				ZINC96270275	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
406920	Brc1ccc2c(ccnc2c1)C(=O)NCC(=O)N1CCC[C@H]1C#N	InChI=1S/C17H15BrN4O2/c18-11-3-4-13-14(5-6-20-15(13)8-11)17(24)21-10-16(23)22-7-1-2-12(22)9-19/h3-6,8,12H,1-2,7,10H2,(H,21,24)/t12-/m0/s1	INQYLMGAPQGWDT-LBPRGKRZSA-N	50434163	CHEMBL2385273::US9346814, Cmpd No 12 Example 15	Prolyl endopeptidase FAP			 6.2					8.3	37.00 C	US Patent		10.7270/Q2W37V6D		aid1802953	US9346814	Jansen, K; De Meester, I; Heirbaut, L; Cheng, JD; Joossens, J; Augustyns, K; Van Der Veken, P	Universiteit Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50434163	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50434163&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			71667378	175446480		CHEMBL2385273				ZINC96270273	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
406921	Clc1ccc2c(ccnc2c1)C(=O)NCC(=O)N1CCC[C@H]1C#N	InChI=1S/C17H15ClN4O2/c18-11-3-4-13-14(5-6-20-15(13)8-11)17(24)21-10-16(23)22-7-1-2-12(22)9-19/h3-6,8,12H,1-2,7,10H2,(H,21,24)/t12-/m0/s1	NERXNBIHCGOYFQ-LBPRGKRZSA-N	50434164	CHEMBL2385272::US9346814, Cmpd No 13 Example 16	Prolyl endopeptidase FAP			 7.1					8.3	37.00 C	US Patent		10.7270/Q2W37V6D		aid1802953	US9346814	Jansen, K; De Meester, I; Heirbaut, L; Cheng, JD; Joossens, J; Augustyns, K; Van Der Veken, P	Universiteit Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50434164	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50434164&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			73356493	175446481		CHEMBL2385272				ZINC96270274	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
406922	O=C(CNC(=O)c1ccnc(c1)-c1ccccc1)N1CCC[C@H]1C#N	InChI=1S/C19H18N4O2/c20-12-16-7-4-10-23(16)18(24)13-22-19(25)15-8-9-21-17(11-15)14-5-2-1-3-6-14/h1-3,5-6,8-9,11,16H,4,7,10,13H2,(H,22,25)/t16-/m0/s1	XLDGEWVOCOXLNE-INIZCTEOSA-N	50009339	CHEMBL3233558::US9346814, Cmpd No 14 Example 18	Prolyl endopeptidase FAP			 290					8.3	37.00 C	US Patent		10.7270/Q2W37V6D		aid1802953	US9346814	Jansen, K; De Meester, I; Heirbaut, L; Cheng, JD; Joossens, J; Augustyns, K; Van Der Veken, P	Universiteit Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50009339	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50009339&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			89705195	103922395		CHEMBL3233558					1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
406923	COc1ccc(cc1OC)-c1cc(ccn1)C(=O)NCC(=O)N1CCC[C@H]1C#N	InChI=1S/C21H22N4O4/c1-28-18-6-5-14(11-19(18)29-2)17-10-15(7-8-23-17)21(27)24-13-20(26)25-9-3-4-16(25)12-22/h5-8,10-11,16H,3-4,9,13H2,1-2H3,(H,24,27)/t16-/m0/s1	PEIGQCUUABOKIO-INIZCTEOSA-N	50009340	CHEMBL3233559::US9346814, Cmpd No 15 Example 19	Prolyl endopeptidase FAP			 220					8.3	37.00 C	US Patent		10.7270/Q2W37V6D		aid1802953	US9346814	Jansen, K; De Meester, I; Heirbaut, L; Cheng, JD; Joossens, J; Augustyns, K; Van Der Veken, P	Universiteit Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50009340	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50009340&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			71667379	103922396		CHEMBL3233559				ZINC26404600	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
406924	O=C(CNC(=O)c1ccnc(c1)-c1ccc(cc1)C#N)N1CCC[C@H]1C#N	InChI=1S/C20H17N5O2/c21-11-14-3-5-15(6-4-14)18-10-16(7-8-23-18)20(27)24-13-19(26)25-9-1-2-17(25)12-22/h3-8,10,17H,1-2,9,13H2,(H,24,27)/t17-/m0/s1	NPTPMAMSSQKOKH-KRWDZBQOSA-N	50009341	CHEMBL3233560::US9346814, Cmpd No 16 Example 20	Prolyl endopeptidase FAP			 270					8.3	37.00 C	US Patent		10.7270/Q2W37V6D		aid1802953	US9346814	Jansen, K; De Meester, I; Heirbaut, L; Cheng, JD; Joossens, J; Augustyns, K; Van Der Veken, P	Universiteit Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50009341	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50009341&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			71667380	103922397		CHEMBL3233560					1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
406925	Cn1cncc1C(=O)NCC(=O)N1CCC[C@H]1C#N	InChI=1S/C12H15N5O2/c1-16-8-14-6-10(16)12(19)15-7-11(18)17-4-2-3-9(17)5-13/h6,8-9H,2-4,7H2,1H3,(H,15,19)/t9-/m0/s1	ZLOHMZQDNJLLNP-VIFPVBQESA-N	50009345	CHEMBL3233564::US9346814, Cmpd No 17 Example 21	Prolyl endopeptidase FAP			 1370					8.3	37.00 C	US Patent		10.7270/Q2W37V6D		aid1802953	US9346814	Jansen, K; De Meester, I; Heirbaut, L; Cheng, JD; Joossens, J; Augustyns, K; Van Der Veken, P	Universiteit Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50009345	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50009345&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			89705223	103922401		CHEMBL3233564					1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
406926	Cc1ncsc1C(=O)NCC(=O)N1CCC[C@H]1C#N	InChI=1S/C12H14N4O2S/c1-8-11(19-7-15-8)12(18)14-6-10(17)16-4-2-3-9(16)5-13/h7,9H,2-4,6H2,1H3,(H,14,18)/t9-/m0/s1	PCAKJIOLXFXXJM-VIFPVBQESA-N	50009348	CHEMBL3233568::US9346814, Cmpd No 18 Example 22	Prolyl endopeptidase FAP			 2500					8.3	37.00 C	US Patent		10.7270/Q2W37V6D		aid1802953	US9346814	Jansen, K; De Meester, I; Heirbaut, L; Cheng, JD; Joossens, J; Augustyns, K; Van Der Veken, P	Universiteit Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50009348	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50009348&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			71667381	103922404		CHEMBL3233568				ZINC13823406	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
406927	Cc1ncoc1C(=O)NCC(=O)N1CCC[C@H]1C#N	InChI=1S/C12H14N4O3/c1-8-11(19-7-15-8)12(18)14-6-10(17)16-4-2-3-9(16)5-13/h7,9H,2-4,6H2,1H3,(H,14,18)/t9-/m0/s1	UPQFPOMWLDEBGI-VIFPVBQESA-N	50009349	CHEMBL3233569::US9346814, Cmpd No 19 Example 23	Prolyl endopeptidase FAP			 10200					8.3	37.00 C	US Patent		10.7270/Q2W37V6D		aid1802953	US9346814	Jansen, K; De Meester, I; Heirbaut, L; Cheng, JD; Joossens, J; Augustyns, K; Van Der Veken, P	Universiteit Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50009349	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50009349&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			71667510	103922405		CHEMBL3233569				ZINC13823404	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
406928	O=C(CNC(=O)C1CCNCC1)N1CCC[C@H]1C#N	InChI=1S/C13H20N4O2/c14-8-11-2-1-7-17(11)12(18)9-16-13(19)10-3-5-15-6-4-10/h10-11,15H,1-7,9H2,(H,16,19)/t11-/m0/s1	AAKIUXAGDURVCO-NSHDSACASA-N	50009343	CHEMBL3233562::US9346814, Cmpd No 20 Example 24	Prolyl endopeptidase FAP			 750					8.3	37.00 C	US Patent		10.7270/Q2W37V6D		aid1802953	US9346814	Jansen, K; De Meester, I; Heirbaut, L; Cheng, JD; Joossens, J; Augustyns, K; Van Der Veken, P	Universiteit Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50009343	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50009343&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			89704942	103922399		CHEMBL3233562				ZINC26404675	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
406929	Clc1cccc2nccc(C(=O)NCC(=O)N3CCC[C@H]3C#N)c12	InChI=1S/C17H15ClN4O2/c18-13-4-1-5-14-16(13)12(6-7-20-14)17(24)21-10-15(23)22-8-2-3-11(22)9-19/h1,4-7,11H,2-3,8,10H2,(H,21,24)/t11-/m0/s1	ALYYADQHQGUFHD-NSHDSACASA-N	50434170	CHEMBL2385299::US9346814, Cmpd No 21 Example 25	Prolyl endopeptidase FAP			 9.9					8.3	37.00 C	US Patent		10.7270/Q2W37V6D		aid1802953	US9346814	Jansen, K; De Meester, I; Heirbaut, L; Cheng, JD; Joossens, J; Augustyns, K; Van Der Veken, P	Universiteit Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50434170	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50434170&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			71655622	175446487		CHEMBL2385299				ZINC96270280	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
406930	Brc1cccc2nccc(C(=O)NCC(=O)N3CCC[C@H]3C#N)c12	InChI=1S/C17H15BrN4O2/c18-13-4-1-5-14-16(13)12(6-7-20-14)17(24)21-10-15(23)22-8-2-3-11(22)9-19/h1,4-7,11H,2-3,8,10H2,(H,21,24)/t11-/m0/s1	XTSDSKNXFWPJCS-NSHDSACASA-N	50434169	CHEMBL2385300::US9346814, Cmpd No 22 Example 26	Prolyl endopeptidase FAP			 11					8.3	37.00 C	US Patent		10.7270/Q2W37V6D		aid1802953	US9346814	Jansen, K; De Meester, I; Heirbaut, L; Cheng, JD; Joossens, J; Augustyns, K; Van Der Veken, P	Universiteit Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50434169	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50434169&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			71655623	175446486		CHEMBL2385300				ZINC96270279	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
406931	Cc1cccc2nccc(C(=O)NCC(=O)N3CCC[C@H]3C#N)c12	InChI=1S/C18H18N4O2/c1-12-4-2-6-15-17(12)14(7-8-20-15)18(24)21-11-16(23)22-9-3-5-13(22)10-19/h2,4,6-8,13H,3,5,9,11H2,1H3,(H,21,24)/t13-/m0/s1	SPPRVRBKPIWARX-ZDUSSCGKSA-N	50009360	CHEMBL3233835::US9346814, Cmpd No 23 Example 27	Prolyl endopeptidase FAP			 4.3					8.3	37.00 C	US Patent		10.7270/Q2W37V6D		aid1802953	US9346814	Jansen, K; De Meester, I; Heirbaut, L; Cheng, JD; Joossens, J; Augustyns, K; Van Der Veken, P	Universiteit Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50009360	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50009360&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			89705096	242057366		CHEMBL3233835					1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
406932	COc1ccc2nccc(C(=O)NCC(=O)N3CC(F)(F)C[C@H]3C#N)c2c1	InChI=1S/C18H16F2N4O3/c1-27-12-2-3-15-14(6-12)13(4-5-22-15)17(26)23-9-16(25)24-10-18(19,20)7-11(24)8-21/h2-6,11H,7,9-10H2,1H3,(H,23,26)/t11-/m0/s1	WVYNDXWJAOOXTA-NSHDSACASA-N	50009331	CHEMBL3233843::US9346814, Cmpd No 24 Example 28	Prolyl endopeptidase FAP			 8.5					8.3	37.00 C	US Patent		10.7270/Q2W37V6D		aid1802953	US9346814	Jansen, K; De Meester, I; Heirbaut, L; Cheng, JD; Joossens, J; Augustyns, K; Van Der Veken, P	Universiteit Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50009331	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50009331&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			89705275	103922387		CHEMBL3233843				ZINC26403406	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
406933	O=C(CNC(=O)c1ccnc2cccc(-c3ccccc3)c12)N1CCC[C@H]1C#N	InChI=1S/C23H20N4O2/c24-14-17-8-5-13-27(17)21(28)15-26-23(29)19-11-12-25-20-10-4-9-18(22(19)20)16-6-2-1-3-7-16/h1-4,6-7,9-12,17H,5,8,13,15H2,(H,26,29)/t17-/m0/s1	KECCJDBJEXGJCW-KRWDZBQOSA-N	50009362	CHEMBL3233838::US9346814, Cmpd No 25 Example 29	Prolyl endopeptidase FAP			 70					8.3	37.00 C	US Patent		10.7270/Q2W37V6D		aid1802953	US9346814	Jansen, K; De Meester, I; Heirbaut, L; Cheng, JD; Joossens, J; Augustyns, K; Van Der Veken, P	Universiteit Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50009362	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50009362&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			89704970	242057368		CHEMBL3233838					1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
406934	O=C(CNC(=O)c1ccnc2cc(Nc3ccccc3)ccc12)N1CCC[C@H]1C#N	InChI=1S/C23H21N5O2/c24-14-18-7-4-12-28(18)22(29)15-26-23(30)20-10-11-25-21-13-17(8-9-19(20)21)27-16-5-2-1-3-6-16/h1-3,5-6,8-11,13,18,27H,4,7,12,15H2,(H,26,30)/t18-/m0/s1	JYZCEZUNDURZDS-SFHVURJKSA-N	50009361	CHEMBL3233837::US9346814, Cmpd No 25 Example 30	Prolyl endopeptidase FAP			 59					8.3	37.00 C	US Patent		10.7270/Q2W37V6D		aid1802953	US9346814	Jansen, K; De Meester, I; Heirbaut, L; Cheng, JD; Joossens, J; Augustyns, K; Van Der Veken, P	Universiteit Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50009361	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50009361&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			89705100	242057367		CHEMBL3233837					1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
406935	O=C(CNC(=O)c1ccnc2cc(ccc12)-c1ccccc1)N1CCC[C@H]1C#N	InChI=1S/C23H20N4O2/c24-14-18-7-4-12-27(18)22(28)15-26-23(29)20-10-11-25-21-13-17(8-9-19(20)21)16-5-2-1-3-6-16/h1-3,5-6,8-11,13,18H,4,7,12,15H2,(H,26,29)/t18-/m0/s1	YUCQGCQXOAXMDQ-SFHVURJKSA-N	50009332	CHEMBL3233836::US9346814, Cmpd No 26 Example 31	Prolyl endopeptidase FAP			 64					8.3	37.00 C	US Patent		10.7270/Q2W37V6D		aid1802953	US9346814	Jansen, K; De Meester, I; Heirbaut, L; Cheng, JD; Joossens, J; Augustyns, K; Van Der Veken, P	Universiteit Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50009332	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50009332&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			89705273	103922388		CHEMBL3233836					1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
406936	Cc1ccc2c(ccnc2c1)C(=O)NCC(=O)N1CCC[C@H]1[N+]#[C-]	InChI=1S/C18H18N4O2/c1-12-5-6-13-14(7-8-20-15(13)10-12)18(24)21-11-17(23)22-9-3-4-16(22)19-2/h5-8,10,16H,3-4,9,11H2,1H3,(H,21,24)/t16-/m0/s1	QCKHSJAFAMATFO-INIZCTEOSA-N	233322	US9346814, Cmpd No 27 Example 32	Prolyl endopeptidase FAP			 6.9					8.3	37.00 C	US Patent		10.7270/Q2W37V6D		aid1802953	US9346814	Jansen, K; De Meester, I; Heirbaut, L; Cheng, JD; Joossens, J; Augustyns, K; Van Der Veken, P	Universiteit Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=233322	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=233322&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			129010652	340093415							1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
406937	COc1ccc(cc1)-c1nc2c(ccnc2[nH]1)C(=O)NCC(=O)N1CCC[C@H]1C#N	InChI=1S/C21H20N6O3/c1-30-15-6-4-13(5-7-15)19-25-18-16(8-9-23-20(18)26-19)21(29)24-12-17(28)27-10-2-3-14(27)11-22/h4-9,14H,2-3,10,12H2,1H3,(H,24,29)(H,23,25,26)/t14-/m0/s1	KNEATCQGGFDGRB-AWEZNQCLSA-N	50009356	CHEMBL3233574::US9346814, Cmpd No 28 Example 33	Prolyl endopeptidase FAP			<200					8.3	37.00 C	US Patent		10.7270/Q2W37V6D		aid1802953	US9346814	Jansen, K; De Meester, I; Heirbaut, L; Cheng, JD; Joossens, J; Augustyns, K; Van Der Veken, P	Universiteit Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50009356	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50009356&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			89704940	242057362		CHEMBL3233574					1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
406938	O=C(CNC(=O)C1=CC=NC2=NC=CC12)N1CCC[C@H]1C#N	InChI=1S/C15H15N5O2/c16-8-10-2-1-7-20(10)13(21)9-19-15(22)12-4-6-18-14-11(12)3-5-17-14/h3-6,10-11H,1-2,7,9H2,(H,19,22)/t10-,11?/m0/s1	NDABCLYNIIWVRI-VUWPPUDQSA-N	233323	US9346814, Cmpd No 29 Example 34	Prolyl endopeptidase FAP			 40					8.3	37.00 C	US Patent		10.7270/Q2W37V6D		aid1802953	US9346814	Jansen, K; De Meester, I; Heirbaut, L; Cheng, JD; Joossens, J; Augustyns, K; Van Der Veken, P	Universiteit Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=233323	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=233323&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			89712285	340093416							1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
406939	O=C(CNC(=O)c1ccnc2ncnn12)N1CCC[C@H]1C#N	InChI=1S/C13H13N7O2/c14-6-9-2-1-5-19(9)11(21)7-16-12(22)10-3-4-15-13-17-8-18-20(10)13/h3-4,8-9H,1-2,5,7H2,(H,16,22)/t9-/m0/s1	JYTXLAIYDQBXKG-VIFPVBQESA-N	50009357	CHEMBL3233575::US9346814, Cmpd No 30 Example 35	Prolyl endopeptidase FAP			 3200					8.3	37.00 C	US Patent		10.7270/Q2W37V6D		aid1802953	US9346814	Jansen, K; De Meester, I; Heirbaut, L; Cheng, JD; Joossens, J; Augustyns, K; Van Der Veken, P	Universiteit Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50009357	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50009357&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			89705098	242057363		CHEMBL3233575					1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
406940	OC[C@@H](NC(=O)c1ccnc2ccccc12)C(=O)N1CCC[C@H]1C#N	InChI=1S/C18H18N4O3/c19-10-12-4-3-9-22(12)18(25)16(11-23)21-17(24)14-7-8-20-15-6-2-1-5-13(14)15/h1-2,5-8,12,16,23H,3-4,9,11H2,(H,21,24)/t12-,16+/m0/s1	PSQZNYNIMSKARP-BLLLJJGKSA-N	50009313	CHEMBL3233538::US9346814, Cmpd No 31 Example 36	Prolyl endopeptidase FAP			 6000					8.3	37.00 C	US Patent		10.7270/Q2W37V6D		aid1802953	US9346814	Jansen, K; De Meester, I; Heirbaut, L; Cheng, JD; Joossens, J; Augustyns, K; Van Der Veken, P	Universiteit Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50009313	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50009313&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			89705076	103922369		CHEMBL3233538				ZINC13823333	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
406941	C[C@@H](NC(=O)c1ccnc2ccccc12)C(=O)N1CCC[C@H]1C#N	InChI=1S/C18H18N4O2/c1-12(18(24)22-10-4-5-13(22)11-19)21-17(23)15-8-9-20-16-7-3-2-6-14(15)16/h2-3,6-9,12-13H,4-5,10H2,1H3,(H,21,23)/t12-,13+/m1/s1	CJZDFIOVUXAMNO-OLZOCXBDSA-N	50009314	CHEMBL3233539::US9346814, Cmpd No 32 Example 37	Prolyl endopeptidase FAP			 3400					8.3	37.00 C	US Patent		10.7270/Q2W37V6D		aid1802953	US9346814	Jansen, K; De Meester, I; Heirbaut, L; Cheng, JD; Joossens, J; Augustyns, K; Van Der Veken, P	Universiteit Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50009314	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50009314&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			89705242	103922370		CHEMBL3233539				ZINC13823260	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
406942	O=C(CNC(=O)c1ccnc2cnccc12)N1CCC[C@H]1C#N	InChI=1S/C16H15N5O2/c17-8-11-2-1-7-21(11)15(22)10-20-16(23)13-4-6-19-14-9-18-5-3-12(13)14/h3-6,9,11H,1-2,7,10H2,(H,20,23)/t11-/m0/s1	VLGXXWPDZBNZCC-NSHDSACASA-N	50009358	CHEMBL3233833::US9346814, Cmpd No 33 Example 38	Prolyl endopeptidase FAP			 28					8.3	37.00 C	US Patent		10.7270/Q2W37V6D		aid1802953	US9346814	Jansen, K; De Meester, I; Heirbaut, L; Cheng, JD; Joossens, J; Augustyns, K; Van Der Veken, P	Universiteit Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50009358	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50009358&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			89705103	242057364		CHEMBL3233833					1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
406943	O=C(Cc1ccncc1)NCC(=O)N1CCC[C@H]1C#N	InChI=1S/C14H16N4O2/c15-9-12-2-1-7-18(12)14(20)10-17-13(19)8-11-3-5-16-6-4-11/h3-6,12H,1-2,7-8,10H2,(H,17,19)/t12-/m0/s1	QWDLZJWJBMCYCH-LBPRGKRZSA-N	50009342	CHEMBL3233561::US9346814, Cmpd No 34 Example 39	Prolyl endopeptidase FAP			 3300					8.3	37.00 C	US Patent		10.7270/Q2W37V6D		aid1802953	US9346814	Jansen, K; De Meester, I; Heirbaut, L; Cheng, JD; Joossens, J; Augustyns, K; Van Der Veken, P	Universiteit Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50009342	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50009342&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			89705045	103922398		CHEMBL3233561				ZINC26404931	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
406944	O=C(Cc1c[nH]cn1)NCC(=O)N1CCC[C@H]1C#N	InChI=1S/C12H15N5O2/c13-5-10-2-1-3-17(10)12(19)7-15-11(18)4-9-6-14-8-16-9/h6,8,10H,1-4,7H2,(H,14,16)(H,15,18)/t10-/m0/s1	SXYMSDCEMARUFK-JTQLQIEISA-N	50009333	CHEMBL3233567::US9346814, Cmpd No 35 Example 40	Prolyl endopeptidase FAP			 7200					8.3	37.00 C	US Patent		10.7270/Q2W37V6D		aid1802953	US9346814	Jansen, K; De Meester, I; Heirbaut, L; Cheng, JD; Joossens, J; Augustyns, K; Van Der Veken, P	Universiteit Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50009333	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50009333&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			89705179	103922389		CHEMBL3233567				ZINC26398600	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
406945	O=C(CNC(=O)c1cnn[nH]1)N1CCC[C@H]1C#N	InChI=1S/C10H12N6O2/c11-4-7-2-1-3-16(7)9(17)6-12-10(18)8-5-13-15-14-8/h5,7H,1-3,6H2,(H,12,18)(H,13,14,15)/t7-/m0/s1	AUGPBTYKMNUDPD-ZETCQYMHSA-N	50009346	CHEMBL3233565::US9346814, Cmpd No 36 Example 41	Prolyl endopeptidase FAP			 5700					8.3	37.00 C	US Patent		10.7270/Q2W37V6D		aid1802953	US9346814	Jansen, K; De Meester, I; Heirbaut, L; Cheng, JD; Joossens, J; Augustyns, K; Van Der Veken, P	Universiteit Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50009346	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50009346&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			89712515	103922402		CHEMBL3233565					1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
406946	O=C(CNC(=O)c1nc[nH]n1)N1CCC[C@H]1C#N			233324	US9346814, Cmpd No 37 Example 42	Prolyl endopeptidase FAP			 22400					8.3	37.00 C	US Patent		10.7270/Q2W37V6D		aid1802953	US9346814	Jansen, K; De Meester, I; Heirbaut, L; Cheng, JD; Joossens, J; Augustyns, K; Van Der Veken, P	Universiteit Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=233324	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=233324&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			89704955	340093417							1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
406947	Oc1cnc2ccccc2c1C(=O)NCC(=O)N1CCC[C@H]1C#N	InChI=1S/C17H16N4O3/c18-8-11-4-3-7-21(11)15(23)10-20-17(24)16-12-5-1-2-6-13(12)19-9-14(16)22/h1-2,5-6,9,11,22H,3-4,7,10H2,(H,20,24)/t11-/m0/s1	SFRHBBXTBPBKRA-NSHDSACASA-N	50434171	CHEMBL2385298::US9346814, Cmpd No 38 Example 43	Prolyl endopeptidase FAP			 160					8.3	37.00 C	US Patent		10.7270/Q2W37V6D		aid1802953	US9346814	Jansen, K; De Meester, I; Heirbaut, L; Cheng, JD; Joossens, J; Augustyns, K; Van Der Veken, P	Universiteit Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50434171	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50434171&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			73347360	175446488		CHEMBL2385298				ZINC96270281	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50088300	Fc1ccc(cc1)-c1cn(CC(=O)N2CCC[C@H]2C#N)nn1	InChI=1S/C15H14FN5O/c16-12-5-3-11(4-6-12)14-9-20(19-18-14)10-15(22)21-7-1-2-13(21)8-17/h3-6,9,13H,1-2,7,10H2/t13-/m0/s1	QYEKQOYAYJWVDT-ZDUSSCGKSA-N	50009328	CHEMBL3233551	Prolyl endopeptidase FAP			 19300							ChEMBL	10.1021/jm500031w	10.7270/Q2P84DFW	24617858			Jansen, K; Heirbaut, L; Verkerk, R; Cheng, JD; Joossens, J; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50009328	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50009328&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			90655549	103922384		CHEMBL3233551				ZINC96178793	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50088340	O=C(CNC(=O)c1ncn[nH]1)N1CCC[C@H]1C#N	InChI=1S/C10H12N6O2/c11-4-7-2-1-3-16(7)8(17)5-12-10(18)9-13-6-14-15-9/h6-7H,1-3,5H2,(H,12,18)(H,13,14,15)/t7-/m0/s1	LTHNMKNDEOGPBM-ZETCQYMHSA-N	50009347	CHEMBL3233566	Prolyl endopeptidase FAP			 22400							ChEMBL	10.1021/jm500031w	10.7270/Q2P84DFW	24617858			Jansen, K; Heirbaut, L; Verkerk, R; Cheng, JD; Joossens, J; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50009347	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50009347&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			89704955	103922403		CHEMBL3233566				ZINC26483023	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50088344	CN(CC(=O)N1CCC[C@H]1C#N)CC(=O)N1CCC[C@H]1C#N	InChI=1S/C15H21N5O2/c1-18(10-14(21)19-6-2-4-12(19)8-16)11-15(22)20-7-3-5-13(20)9-17/h12-13H,2-7,10-11H2,1H3/t12-,13-/m0/s1	VHQNGIYGVDQVQD-STQMWFEESA-N	50009325	CHEMBL3233549	Prolyl endopeptidase FAP			 28000							ChEMBL	10.1021/jm500031w	10.7270/Q2P84DFW	24617858			Jansen, K; Heirbaut, L; Verkerk, R; Cheng, JD; Joossens, J; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50009325	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50009325&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			90655547	103922381		CHEMBL3233549				ZINC96178792	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50088345	O=C(Cn1cc(nn1)-c1ccccc1)N1CCC[C@H]1C#N	InChI=1S/C15H15N5O/c16-9-13-7-4-8-20(13)15(21)11-19-10-14(17-18-19)12-5-2-1-3-6-12/h1-3,5-6,10,13H,4,7-8,11H2/t13-/m0/s1	CXRDIYCIXJOTBY-ZDUSSCGKSA-N	50009327	CHEMBL3233550	Prolyl endopeptidase FAP			 28000							ChEMBL	10.1021/jm500031w	10.7270/Q2P84DFW	24617858			Jansen, K; Heirbaut, L; Verkerk, R; Cheng, JD; Joossens, J; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50009327	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50009327&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			90655548	103922383		CHEMBL3233550				ZINC95609903	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50088346	CN(CC(=O)N1CCC[C@H]1C#N)Cc1ccnc2ccccc12	InChI=1S/C18H20N4O/c1-21(13-18(23)22-10-4-5-15(22)11-19)12-14-8-9-20-17-7-3-2-6-16(14)17/h2-3,6-9,15H,4-5,10,12-13H2,1H3/t15-/m0/s1	HORGXJBYAFYHNY-HNNXBMFYSA-N	50009324	CHEMBL3233548	Prolyl endopeptidase FAP			 28100							ChEMBL	10.1021/jm500031w	10.7270/Q2P84DFW	24617858			Jansen, K; Heirbaut, L; Verkerk, R; Cheng, JD; Joossens, J; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50009324	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50009324&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			90655546	103922380		CHEMBL3233548					1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50088349	CN(CC(=O)N1CCC[C@H]1C#N)C(=O)c1ccnc2ccccc12	InChI=1S/C18H18N4O2/c1-21(12-17(23)22-10-4-5-13(22)11-19)18(24)15-8-9-20-16-7-3-2-6-14(15)16/h2-3,6-9,13H,4-5,10,12H2,1H3/t13-/m0/s1	NLIXCGBSWRSMCZ-ZDUSSCGKSA-N	50009317	CHEMBL3233542	Prolyl endopeptidase FAP			 37000							ChEMBL	10.1021/jm500031w	10.7270/Q2P84DFW	24617858			Jansen, K; Heirbaut, L; Verkerk, R; Cheng, JD; Joossens, J; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50009317	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50009317&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			90655540	103922373		CHEMBL3233542				ZINC13823355	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50088367	C[C@H](NC(=O)c1ccnc2ccccc12)C(=O)N1CCC[C@H]1C#N	InChI=1S/C18H18N4O2/c1-12(18(24)22-10-4-5-13(22)11-19)21-17(23)15-8-9-20-16-7-3-2-6-14(15)16/h2-3,6-9,12-13H,4-5,10H2,1H3,(H,21,23)/t12-,13-/m0/s1	CJZDFIOVUXAMNO-STQMWFEESA-N	50009315	CHEMBL3233540	Prolyl endopeptidase FAP			>100000							ChEMBL	10.1021/jm500031w	10.7270/Q2P84DFW	24617858			Jansen, K; Heirbaut, L; Verkerk, R; Cheng, JD; Joossens, J; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50009315	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50009315&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			90655538	103922371		CHEMBL3233540				ZINC13823317	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50088389	O=C(CN(C1CC1)C(=O)c1ccnc2ccccc12)N1CCC[C@H]1C#N	InChI=1S/C20H20N4O2/c21-12-15-4-3-11-23(15)19(25)13-24(14-7-8-14)20(26)17-9-10-22-18-6-2-1-5-16(17)18/h1-2,5-6,9-10,14-15H,3-4,7-8,11,13H2/t15-/m0/s1	SZHQMQDOBHYIJA-HNNXBMFYSA-N	50009318	CHEMBL3233543	Prolyl endopeptidase FAP			>100000							ChEMBL	10.1021/jm500031w	10.7270/Q2P84DFW	24617858			Jansen, K; Heirbaut, L; Verkerk, R; Cheng, JD; Joossens, J; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50009318	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50009318&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			90655541	103922374		CHEMBL3233543				ZINC13823367	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50088394	COCCN(CC(=O)N1CCC[C@H]1C#N)C(=O)c1ccnc2ccccc12	InChI=1S/C20H22N4O3/c1-27-12-11-23(14-19(25)24-10-4-5-15(24)13-21)20(26)17-8-9-22-18-7-3-2-6-16(17)18/h2-3,6-9,15H,4-5,10-12,14H2,1H3/t15-/m0/s1	QIQBJVQENOLCBL-HNNXBMFYSA-N	50009320	CHEMBL3233545	Prolyl endopeptidase FAP			>100000							ChEMBL	10.1021/jm500031w	10.7270/Q2P84DFW	24617858			Jansen, K; Heirbaut, L; Verkerk, R; Cheng, JD; Joossens, J; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50009320	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50009320&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			90655543	103922376		CHEMBL3233545				ZINC13823311	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50088420	CC(C)CCN(CC(=O)N1CCC[C@H]1C#N)C(=O)c1ccnc2ccccc12	InChI=1S/C22H26N4O2/c1-16(2)10-13-25(15-21(27)26-12-5-6-17(26)14-23)22(28)19-9-11-24-20-8-4-3-7-18(19)20/h3-4,7-9,11,16-17H,5-6,10,12-13,15H2,1-2H3/t17-/m0/s1	WLKJRDDXFQEKNZ-KRWDZBQOSA-N	50009321	CHEMBL3233546	Prolyl endopeptidase FAP			>100000							ChEMBL	10.1021/jm500031w	10.7270/Q2P84DFW	24617858			Jansen, K; Heirbaut, L; Verkerk, R; Cheng, JD; Joossens, J; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50009321	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50009321&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			90655544	103922377		CHEMBL3233546				ZINC01915283	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50088430	O=C(CCc1cn(CC(=O)N2CCC[C@H]2C#N)nn1)N1Cc2ccccc2C1	InChI=1S/C20H22N6O2/c21-10-18-6-3-9-26(18)20(28)14-25-13-17(22-23-25)7-8-19(27)24-11-15-4-1-2-5-16(15)12-24/h1-2,4-5,13,18H,3,6-9,11-12,14H2/t18-/m0/s1	KXWJQHHCYYJBCT-SFHVURJKSA-N	50009329	CHEMBL3233552	Prolyl endopeptidase FAP			>100000							ChEMBL	10.1021/jm500031w	10.7270/Q2P84DFW	24617858			Jansen, K; Heirbaut, L; Verkerk, R; Cheng, JD; Joossens, J; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50009329	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50009329&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			90655550	103922385		CHEMBL3233552				ZINC26396595	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50088376	O=C(NC1(CC1)C(=O)N1CCC[C@H]1C#N)c1ccnc2ccccc12	InChI=1S/C19H18N4O2/c20-12-13-4-3-11-23(13)18(25)19(8-9-19)22-17(24)15-7-10-21-16-6-2-1-5-14(15)16/h1-2,5-7,10,13H,3-4,8-9,11H2,(H,22,24)/t13-/m0/s1	QMSPXZINNSNSNF-ZDUSSCGKSA-N	50009316	CHEMBL3233541	Prolyl endopeptidase FAP			>100000							ChEMBL	10.1021/jm500031w	10.7270/Q2P84DFW	24617858			Jansen, K; Heirbaut, L; Verkerk, R; Cheng, JD; Joossens, J; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50009316	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50009316&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			90655539	103922372		CHEMBL3233541				ZINC01915280	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50088527	Nc1ccc(cc1)C(=O)NCC(=O)N1CCC[C@H]1C#N	InChI=1S/C14H16N4O2/c15-8-12-2-1-7-18(12)13(19)9-17-14(20)10-3-5-11(16)6-4-10/h3-6,12H,1-2,7,9,16H2,(H,17,20)/t12-/m0/s1	IQIRBDLGQIDXDG-LBPRGKRZSA-N	50009350	CHEMBL3233570	Prolyl endopeptidase FAP			 10300							ChEMBL	10.1021/jm500031w	10.7270/Q2P84DFW	24617858			Jansen, K; Heirbaut, L; Verkerk, R; Cheng, JD; Joossens, J; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50009350	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50009350&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			90655556	242057358		CHEMBL3233570					1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50088530	Clc1ccc(CN(CC(=O)N2CCC[C@H]2C#N)C(=O)c2ccnc3ccccc23)cc1	InChI=1S/C24H21ClN4O2/c25-18-9-7-17(8-10-18)15-28(16-23(30)29-13-3-4-19(29)14-26)24(31)21-11-12-27-22-6-2-1-5-20(21)22/h1-2,5-12,19H,3-4,13,15-16H2/t19-/m0/s1	ZVTXKOFGZCKPFO-IBGZPJMESA-N	50009319	CHEMBL3233544	Prolyl endopeptidase FAP			>12500							ChEMBL	10.1021/jm500031w	10.7270/Q2P84DFW	24617858			Jansen, K; Heirbaut, L; Verkerk, R; Cheng, JD; Joossens, J; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50009319	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50009319&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			90655542	103922375		CHEMBL3233544				ZINC13823282	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50088531	O=C(Cn1cc(nn1)-c1cccc2ccccc12)N1CCC[C@H]1C#N	InChI=1S/C19H17N5O/c20-11-15-7-4-10-24(15)19(25)13-23-12-18(21-22-23)17-9-3-6-14-5-1-2-8-16(14)17/h1-3,5-6,8-9,12,15H,4,7,10,13H2/t15-/m0/s1	JEQIFYGURRYDHI-HNNXBMFYSA-N	50009330	CHEMBL3233553	Prolyl endopeptidase FAP			>12500							ChEMBL	10.1021/jm500031w	10.7270/Q2P84DFW	24617858			Jansen, K; Heirbaut, L; Verkerk, R; Cheng, JD; Joossens, J; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50009330	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50009330&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			90655551	103922386		CHEMBL3233553				ZINC26398592	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50088534	COCCN(CC(=O)N1CCC[C@H]1C#N)Cc1ccnc2ccccc12	InChI=1S/C20H24N4O2/c1-26-12-11-23(15-20(25)24-10-4-5-17(24)13-21)14-16-8-9-22-19-7-3-2-6-18(16)19/h2-3,6-9,17H,4-5,10-12,14-15H2,1H3/t17-/m0/s1	KPKFBZFHTVBXOB-KRWDZBQOSA-N	50009322	CHEMBL3233547	Prolyl endopeptidase FAP			 15500							ChEMBL	10.1021/jm500031w	10.7270/Q2P84DFW	24617858			Jansen, K; Heirbaut, L; Verkerk, R; Cheng, JD; Joossens, J; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50009322	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50009322&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			90655545	103922378		CHEMBL3233547				ZINC13823266	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50088535	COc1cccc2nccc(C(=O)NCC(=O)N3CCC[C@H]3C#N)c12	InChI=1S/C18H18N4O3/c1-25-15-6-2-5-14-17(15)13(7-8-20-14)18(24)21-11-16(23)22-9-3-4-12(22)10-19/h2,5-8,12H,3-4,9,11H2,1H3,(H,21,24)/t12-/m0/s1	UYMLFTZHDJPISZ-LBPRGKRZSA-N	50009363	CHEMBL3233839	Prolyl endopeptidase FAP			 16600							ChEMBL	10.1021/jm500031w	10.7270/Q2P84DFW	24617858			Jansen, K; Heirbaut, L; Verkerk, R; Cheng, JD; Joossens, J; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50009363	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50009363&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			89705244	242057369		CHEMBL3233839					1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50088537	O=C(Cc1c[nH]cn1)NCC(=O)N1CCC[C@H]1C#N	InChI=1S/C12H15N5O2/c13-5-10-2-1-3-17(10)12(19)7-15-11(18)4-9-6-14-8-16-9/h6,8,10H,1-4,7H2,(H,14,16)(H,15,18)/t10-/m0/s1	SXYMSDCEMARUFK-JTQLQIEISA-N	50009333	CHEMBL3233567::US9346814, Cmpd No 35 Example 40	Prolyl endopeptidase FAP			 7200							ChEMBL	10.1021/jm500031w	10.7270/Q2P84DFW	24617858			Jansen, K; Heirbaut, L; Verkerk, R; Cheng, JD; Joossens, J; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50009333	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50009333&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			89705179	103922389		CHEMBL3233567				ZINC26398600	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50088539	FC1(F)C[C@@H](C#N)N(C1)C(=O)CNC(=O)c1ccnc2cccc(C#N)c12	InChI=1S/C18H13F2N5O2/c19-18(20)6-12(8-22)25(10-18)15(26)9-24-17(27)13-4-5-23-14-3-1-2-11(7-21)16(13)14/h1-5,12H,6,9-10H2,(H,24,27)/t12-/m0/s1	HWHCDLSGDGKOSD-LBPRGKRZSA-N	50009374	CHEMBL3233845	Prolyl endopeptidase FAP			 7200							ChEMBL	10.1021/jm500031w	10.7270/Q2P84DFW	24617858			Jansen, K; Heirbaut, L; Verkerk, R; Cheng, JD; Joossens, J; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50009374	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50009374&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			90655563	242057377		CHEMBL3233845					1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50088544	FC1(F)C[C@@H](C#N)N(C1)C(=O)CNC(=O)c1ccnc2cccc(Br)c12	InChI=1S/C17H13BrF2N4O2/c18-12-2-1-3-13-15(12)11(4-5-22-13)16(26)23-8-14(25)24-9-17(19,20)6-10(24)7-21/h1-5,10H,6,8-9H2,(H,23,26)/t10-/m0/s1	OVPLVZCYQCLIBW-JTQLQIEISA-N	50009373	CHEMBL3233844	Prolyl endopeptidase FAP			 9000							ChEMBL	10.1021/jm500031w	10.7270/Q2P84DFW	24617858			Jansen, K; Heirbaut, L; Verkerk, R; Cheng, JD; Joossens, J; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50009373	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50009373&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			89705152	242057376		CHEMBL3233844					1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50088550	Cc1ncoc1C(=O)NCC(=O)N1CCC[C@H]1C#N	InChI=1S/C12H14N4O3/c1-8-11(19-7-15-8)12(18)14-6-10(17)16-4-2-3-9(16)5-13/h7,9H,2-4,6H2,1H3,(H,14,18)/t9-/m0/s1	UPQFPOMWLDEBGI-VIFPVBQESA-N	50009349	CHEMBL3233569::US9346814, Cmpd No 19 Example 23	Prolyl endopeptidase FAP			 10200							ChEMBL	10.1021/jm500031w	10.7270/Q2P84DFW	24617858			Jansen, K; Heirbaut, L; Verkerk, R; Cheng, JD; Joossens, J; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50009349	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50009349&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			71667510	103922405		CHEMBL3233569				ZINC13823404	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50088552	FC1(F)C[C@@H](C#N)N(C1)C(=O)CNC(=O)c1ccnc2ccccc12	InChI=1S/C17H14F2N4O2/c18-17(19)7-11(8-20)23(10-17)15(24)9-22-16(25)13-5-6-21-14-4-2-1-3-12(13)14/h1-6,11H,7,9-10H2,(H,22,25)/t11-/m0/s1	PUOOCZVRHBHJRS-NSHDSACASA-N	50009366	CHEMBL3233842::US11504364, Compound Ref.-Comp.::US9346814, Cmpd No 1, Example 1	Prolyl endopeptidase FAP			 3.2							ChEMBL	10.1021/jm500031w	10.7270/Q2P84DFW	24617858			Jansen, K; Heirbaut, L; Verkerk, R; Cheng, JD; Joossens, J; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50009366	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50009366&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			71621488	242057372		CHEMBL3233842					1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50088553	F[C@H]1C[C@@H](C#N)N(C1)C(=O)CNC(=O)c1ccnc2ccccc12	InChI=1S/C17H15FN4O2/c18-11-7-12(8-19)22(10-11)16(23)9-21-17(24)14-5-6-20-15-4-2-1-3-13(14)15/h1-6,11-12H,7,9-10H2,(H,21,24)/t11-,12-/m0/s1	ORRRPUSEMSKTEW-RYUDHWBXSA-N	50009364	CHEMBL3233840	Prolyl endopeptidase FAP			 3.3							ChEMBL	10.1021/jm500031w	10.7270/Q2P84DFW	24617858			Jansen, K; Heirbaut, L; Verkerk, R; Cheng, JD; Joossens, J; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50009364	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50009364&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			90655559	242057370		CHEMBL3233840					1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50088555	OB(O)[C@@H]1CCCN1C(=O)CNC(=O)c1ccnc2ccccc12	InChI=1S/C16H18BN3O4/c21-15(20-9-3-6-14(20)17(23)24)10-19-16(22)12-7-8-18-13-5-2-1-4-11(12)13/h1-2,4-5,7-8,14,23-24H,3,6,9-10H2,(H,19,22)/t14-/m0/s1	KDSKSYZDLVUANF-AWEZNQCLSA-N	50009370	CHEMBL3233847	Prolyl endopeptidase FAP			 3.7							ChEMBL	10.1021/jm500031w	10.7270/Q2P84DFW	24617858			Jansen, K; Heirbaut, L; Verkerk, R; Cheng, JD; Joossens, J; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50009370	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50009370&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			89705109	242057374		CHEMBL3233847					1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50088556	Cc1cccc2nccc(C(=O)NCC(=O)N3CCC[C@H]3C#N)c12	InChI=1S/C18H18N4O2/c1-12-4-2-6-15-17(12)14(7-8-20-15)18(24)21-11-16(23)22-9-3-5-13(22)10-19/h2,4,6-8,13H,3,5,9,11H2,1H3,(H,21,24)/t13-/m0/s1	SPPRVRBKPIWARX-ZDUSSCGKSA-N	50009360	CHEMBL3233835::US9346814, Cmpd No 23 Example 27	Prolyl endopeptidase FAP			 4.3							ChEMBL	10.1021/jm500031w	10.7270/Q2P84DFW	24617858			Jansen, K; Heirbaut, L; Verkerk, R; Cheng, JD; Joossens, J; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50009360	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50009360&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			89705096	242057366		CHEMBL3233835					1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50088557	Cc1ccc2c(ccnc2c1)C(=O)NCC(=O)N1CCC[C@H]1C#N	InChI=1S/C18H18N4O2/c1-12-4-5-14-15(6-7-20-16(14)9-12)18(24)21-11-17(23)22-8-2-3-13(22)10-19/h4-7,9,13H,2-3,8,11H2,1H3,(H,21,24)/t13-/m0/s1	ZXCBAKXWAIOPLD-ZDUSSCGKSA-N	50009359	CHEMBL3233834	Prolyl endopeptidase FAP			 6.9							ChEMBL	10.1021/jm500031w	10.7270/Q2P84DFW	24617858			Jansen, K; Heirbaut, L; Verkerk, R; Cheng, JD; Joossens, J; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50009359	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50009359&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			89705081	242057365		CHEMBL3233834					1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50088558	COc1ccc2nccc(C(=O)NCC(=O)N3CC(F)(F)C[C@H]3C#N)c2c1	InChI=1S/C18H16F2N4O3/c1-27-12-2-3-15-14(6-12)13(4-5-22-15)17(26)23-9-16(25)24-10-18(19,20)7-11(24)8-21/h2-6,11H,7,9-10H2,1H3,(H,23,26)/t11-/m0/s1	WVYNDXWJAOOXTA-NSHDSACASA-N	50009331	CHEMBL3233843::US9346814, Cmpd No 24 Example 28	Prolyl endopeptidase FAP			 8.5							ChEMBL	10.1021/jm500031w	10.7270/Q2P84DFW	24617858			Jansen, K; Heirbaut, L; Verkerk, R; Cheng, JD; Joossens, J; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50009331	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50009331&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			89705275	103922387		CHEMBL3233843				ZINC26403406	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50088559	O=C(CNC(=O)c1ccnc2ccccc12)N1CCC[C@H]1C#N	InChI=1S/C17H16N4O2/c18-10-12-4-3-9-21(12)16(22)11-20-17(23)14-7-8-19-15-6-2-1-5-13(14)15/h1-2,5-8,12H,3-4,9,11H2,(H,20,23)/t12-/m0/s1	MTHMMXFBHKGAAI-LBPRGKRZSA-N	50434188	CHEMBL2385281::US9346814, Cmpd No 2 Example 3	Prolyl endopeptidase FAP			 10							ChEMBL	10.1021/jm500031w	10.7270/Q2P84DFW	24617858			Jansen, K; Heirbaut, L; Verkerk, R; Cheng, JD; Joossens, J; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50434188	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50434188&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			71655554	175446505		CHEMBL2385281				ZINC96270298	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50088560	Brc1cccc2nccc(C(=O)NCC(=O)N3CCC[C@H]3C#N)c12	InChI=1S/C17H15BrN4O2/c18-13-4-1-5-14-16(13)12(6-7-20-14)17(24)21-10-15(23)22-8-2-3-11(22)9-19/h1,4-7,11H,2-3,8,10H2,(H,21,24)/t11-/m0/s1	XTSDSKNXFWPJCS-NSHDSACASA-N	50434169	CHEMBL2385300::US9346814, Cmpd No 22 Example 26	Prolyl endopeptidase FAP			 11							ChEMBL	10.1021/jm500031w	10.7270/Q2P84DFW	24617858			Jansen, K; Heirbaut, L; Verkerk, R; Cheng, JD; Joossens, J; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50434169	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50434169&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			71655623	175446486		CHEMBL2385300				ZINC96270279	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50088562	FC1(F)C[C@@H](C#N)N(C1)C(=O)[C@@H]1C[C@@H](CC(=O)N2Cc3ccccc3C2)C(=O)N1	InChI=1S/C20H20F2N4O3/c21-20(22)7-15(8-23)26(11-20)19(29)16-5-14(18(28)24-16)6-17(27)25-9-12-3-1-2-4-13(12)10-25/h1-4,14-16H,5-7,9-11H2,(H,24,28)/t14-,15-,16-/m0/s1	XEYZLQVNZFQPGD-JYJNAYRXSA-N	50326392	(2S)-1-({(2S,4S)-4-[2-(1,3-Dihydro-2H-isoindol-2-yl)-2-oxoethyl]-5-oxopyrrolidin-2-yl}carbonyl)-4,4-difluoropyrrolidine-2-carbonitrile::CHEMBL1243153	Prolyl endopeptidase FAP			 17							ChEMBL	10.1021/jm500031w	10.7270/Q2P84DFW	24617858			Jansen, K; Heirbaut, L; Verkerk, R; Cheng, JD; Joossens, J; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50326392	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50326392&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			46917048	123105507		CHEMBL1243153				ZINC64573975	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50088624	C[C@@H](NC(=O)c1ccncc1)C(=O)N1CCC[C@H]1B(O)O	InChI=1S/C13H18BN3O4/c1-9(16-12(18)10-4-6-15-7-5-10)13(19)17-8-2-3-11(17)14(20)21/h4-7,9,11,20-21H,2-3,8H2,1H3,(H,16,18)/t9-,11+/m1/s1	DRBWRJPFNOBNIO-KOLCDFICSA-N	50431242	CHEMBL2333026	Prolyl endopeptidase FAP			 25							ChEMBL	10.1021/jm500031w	10.7270/Q2P84DFW	24617858			Jansen, K; Heirbaut, L; Verkerk, R; Cheng, JD; Joossens, J; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50431242	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50431242&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			71655266	164160117		CHEMBL2333026					1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50088625	O=C(CNC(=O)c1ccnc2cnccc12)N1CCC[C@H]1C#N	InChI=1S/C16H15N5O2/c17-8-11-2-1-7-21(11)15(22)10-20-16(23)13-4-6-19-14-9-18-5-3-12(13)14/h3-6,9,11H,1-2,7,10H2,(H,20,23)/t11-/m0/s1	VLGXXWPDZBNZCC-NSHDSACASA-N	50009358	CHEMBL3233833::US9346814, Cmpd No 33 Example 38	Prolyl endopeptidase FAP			 28							ChEMBL	10.1021/jm500031w	10.7270/Q2P84DFW	24617858			Jansen, K; Heirbaut, L; Verkerk, R; Cheng, JD; Joossens, J; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50009358	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50009358&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			89705103	242057364		CHEMBL3233833					1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50088626	O=C(CNC(=O)c1ccnc2[nH]ccc12)N1CCC[C@H]1C#N	InChI=1S/C15H15N5O2/c16-8-10-2-1-7-20(10)13(21)9-19-15(22)12-4-6-18-14-11(12)3-5-17-14/h3-6,10H,1-2,7,9H2,(H,17,18)(H,19,22)/t10-/m0/s1	VLLQATRRTWXIFV-JTQLQIEISA-N	50009352	CHEMBL3233572	Prolyl endopeptidase FAP			 40							ChEMBL	10.1021/jm500031w	10.7270/Q2P84DFW	24617858			Jansen, K; Heirbaut, L; Verkerk, R; Cheng, JD; Joossens, J; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50009352	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50009352&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			89705136	242057360		CHEMBL3233572					1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50088628	O=C(CNC(=O)c1ccnc2cc(Nc3ccccc3)ccc12)N1CCC[C@H]1C#N	InChI=1S/C23H21N5O2/c24-14-18-7-4-12-28(18)22(29)15-26-23(30)20-10-11-25-21-13-17(8-9-19(20)21)27-16-5-2-1-3-6-16/h1-3,5-6,8-11,13,18,27H,4,7,12,15H2,(H,26,30)/t18-/m0/s1	JYZCEZUNDURZDS-SFHVURJKSA-N	50009361	CHEMBL3233837::US9346814, Cmpd No 25 Example 30	Prolyl endopeptidase FAP			 59							ChEMBL	10.1021/jm500031w	10.7270/Q2P84DFW	24617858			Jansen, K; Heirbaut, L; Verkerk, R; Cheng, JD; Joossens, J; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50009361	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50009361&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			89705100	242057367		CHEMBL3233837					1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50088629	O=C(CNC(=O)c1ccncc1)N1CCC[C@H]1C#N	InChI=1S/C13H14N4O2/c14-8-11-2-1-7-17(11)12(18)9-16-13(19)10-3-5-15-6-4-10/h3-6,11H,1-2,7,9H2,(H,16,19)/t11-/m0/s1	QNDFOEYFDNZPFT-NSHDSACASA-N	50009334	CHEMBL3233554::US9346814, Cmpd No 4 Example 6	Prolyl endopeptidase FAP			 63							ChEMBL	10.1021/jm500031w	10.7270/Q2P84DFW	24617858			Jansen, K; Heirbaut, L; Verkerk, R; Cheng, JD; Joossens, J; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50009334	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50009334&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			71667226	103922390		CHEMBL3233554				ZINC95616104	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50088630	O=C(CNC(=O)c1ccnc2cccc(-c3ccccc3)c12)N1CCC[C@H]1C#N	InChI=1S/C23H20N4O2/c24-14-17-8-5-13-27(17)21(28)15-26-23(29)19-11-12-25-20-10-4-9-18(22(19)20)16-6-2-1-3-7-16/h1-4,6-7,9-12,17H,5,8,13,15H2,(H,26,29)/t17-/m0/s1	KECCJDBJEXGJCW-KRWDZBQOSA-N	50009362	CHEMBL3233838::US9346814, Cmpd No 25 Example 29	Prolyl endopeptidase FAP			 64							ChEMBL	10.1021/jm500031w	10.7270/Q2P84DFW	24617858			Jansen, K; Heirbaut, L; Verkerk, R; Cheng, JD; Joossens, J; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50009362	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50009362&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			89704970	242057368		CHEMBL3233838					1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50088631	CC(C)[C@H](N)C(=O)N1CCC[C@H]1B(O)O	InChI=1S/C9H19BN2O3/c1-6(2)8(11)9(13)12-5-3-4-7(12)10(14)15/h6-8,14-15H,3-5,11H2,1-2H3/t7-,8-/m0/s1	FKCMADOPPWWGNZ-YUMQZZPRSA-N	50050513	(R)-1-((S)-2-amino-3-methylbutanoyl)pyrrolidin-2-ylboronic acid::(S)-2-Amino-1-((R)-2-dihydroxyboron-pyrrolidin-1-yl)-3-methyl-butan-1-one::(S)-2-Amino-3-methyl-2-boronic acid-1-pyrrolidin-1-yl-butan-1-one::Boronic acid derivative::CHEMBL67279::Ketopyrrolidine derivative::Pyrrolidine derivative::US11096924, DASH-inhibitors 2504 C::US11504364, Compound Val-boroPro::US11559537, Compound 2054-Val-boro-Pro	Prolyl endopeptidase FAP			 66							ChEMBL	10.1021/jm500031w	10.7270/Q2P84DFW	24617858			Jansen, K; Heirbaut, L; Verkerk, R; Cheng, JD; Joossens, J; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50050513	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50050513&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			6918572	103947674		CHEMBL67279					1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50088632	O=C(CNC(=O)c1ccnc2cc(ccc12)-c1ccccc1)N1CCC[C@H]1C#N	InChI=1S/C23H20N4O2/c24-14-18-7-4-12-27(18)22(28)15-26-23(29)20-10-11-25-21-13-17(8-9-19(20)21)16-5-2-1-3-6-16/h1-3,5-6,8-11,13,18H,4,7,12,15H2,(H,26,29)/t18-/m0/s1	YUCQGCQXOAXMDQ-SFHVURJKSA-N	50009332	CHEMBL3233836::US9346814, Cmpd No 26 Example 31	Prolyl endopeptidase FAP			 70							ChEMBL	10.1021/jm500031w	10.7270/Q2P84DFW	24617858			Jansen, K; Heirbaut, L; Verkerk, R; Cheng, JD; Joossens, J; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50009332	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50009332&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			89705273	103922388		CHEMBL3233836					1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50088634	Brc1cc(ccn1)C(=O)NCC(=O)N1CCC[C@H]1C#N	InChI=1S/C13H13BrN4O2/c14-11-6-9(3-4-16-11)13(20)17-8-12(19)18-5-1-2-10(18)7-15/h3-4,6,10H,1-2,5,8H2,(H,17,20)/t10-/m0/s1	OBPHWPOFNKZVTB-JTQLQIEISA-N	50009336	CHEMBL3233556	Prolyl endopeptidase FAP			 126							ChEMBL	10.1021/jm500031w	10.7270/Q2P84DFW	24617858			Jansen, K; Heirbaut, L; Verkerk, R; Cheng, JD; Joossens, J; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50009336	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50009336&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			90655553	103922392		CHEMBL3233556				ZINC95609925	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50088635	Nc1cc(ccn1)C(=O)NCC(=O)N1CCC[C@H]1C#N	InChI=1S/C13H15N5O2/c14-7-10-2-1-5-18(10)12(19)8-17-13(20)9-3-4-16-11(15)6-9/h3-4,6,10H,1-2,5,8H2,(H2,15,16)(H,17,20)/t10-/m0/s1	LJJSDBXIIMKYCD-JTQLQIEISA-N	50009337	CHEMBL3233557	Prolyl endopeptidase FAP			 138							ChEMBL	10.1021/jm500031w	10.7270/Q2P84DFW	24617858			Jansen, K; Heirbaut, L; Verkerk, R; Cheng, JD; Joossens, J; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50009337	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50009337&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			90655554	103922393		CHEMBL3233557				ZINC95609986	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50088636	O=C(CNC(=O)c1ccnnc1)N1CCC[C@H]1C#N	InChI=1S/C12H13N5O2/c13-6-10-2-1-5-17(10)11(18)8-14-12(19)9-3-4-15-16-7-9/h3-4,7,10H,1-2,5,8H2,(H,14,19)/t10-/m0/s1	UZLOJGKSOYCGNC-JTQLQIEISA-N	50009344	CHEMBL3233563	Prolyl endopeptidase FAP			 164							ChEMBL	10.1021/jm500031w	10.7270/Q2P84DFW	24617858			Jansen, K; Heirbaut, L; Verkerk, R; Cheng, JD; Joossens, J; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50009344	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50009344&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			90655555	103922400		CHEMBL3233563					1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50088637	ClCC(=O)[C@@H]1CCCN1C(=O)CNC(=O)c1ccnc2ccccc12	InChI=1S/C18H18ClN3O3/c19-10-16(23)15-6-3-9-22(15)17(24)11-21-18(25)13-7-8-20-14-5-2-1-4-12(13)14/h1-2,4-5,7-8,15H,3,6,9-11H2,(H,21,25)/t15-/m0/s1	DUYGEGPWDDIKKU-HNNXBMFYSA-N	50009372	CHEMBL3233848	Prolyl endopeptidase FAP			 177							ChEMBL	10.1021/jm500031w	10.7270/Q2P84DFW	24617858			Jansen, K; Heirbaut, L; Verkerk, R; Cheng, JD; Joossens, J; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50009372	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50009372&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			90655562	242057375		CHEMBL3233848					1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50088638	Fc1ccc(cc1)-c1nc2c(ccnc2[nH]1)C(=O)NCC(=O)N1CCC[C@H]1C#N	InChI=1S/C20H17FN6O2/c21-13-5-3-12(4-6-13)18-25-17-15(7-8-23-19(17)26-18)20(29)24-11-16(28)27-9-1-2-14(27)10-22/h3-8,14H,1-2,9,11H2,(H,24,29)(H,23,25,26)/t14-/m0/s1	AIGXGABJOMVELA-AWEZNQCLSA-N	50009354	CHEMBL3233573	Prolyl endopeptidase FAP			<200							ChEMBL	10.1021/jm500031w	10.7270/Q2P84DFW	24617858			Jansen, K; Heirbaut, L; Verkerk, R; Cheng, JD; Joossens, J; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50009354	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50009354&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			90655558	242057361		CHEMBL3233573					1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50088639	COc1ccc(cc1)-c1nc2c(ccnc2[nH]1)C(=O)NCC(=O)N1CCC[C@H]1C#N	InChI=1S/C21H20N6O3/c1-30-15-6-4-13(5-7-15)19-25-18-16(8-9-23-20(18)26-19)21(29)24-12-17(28)27-10-2-3-14(27)11-22/h4-9,14H,2-3,10,12H2,1H3,(H,24,29)(H,23,25,26)/t14-/m0/s1	KNEATCQGGFDGRB-AWEZNQCLSA-N	50009356	CHEMBL3233574::US9346814, Cmpd No 28 Example 33	Prolyl endopeptidase FAP			<200							ChEMBL	10.1021/jm500031w	10.7270/Q2P84DFW	24617858			Jansen, K; Heirbaut, L; Verkerk, R; Cheng, JD; Joossens, J; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50009356	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50009356&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			89704940	242057362		CHEMBL3233574					1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50088640	COc1ccc(cc1OC)-c1cc(ccn1)C(=O)NCC(=O)N1CCC[C@H]1C#N	InChI=1S/C21H22N4O4/c1-28-18-6-5-14(11-19(18)29-2)17-10-15(7-8-23-17)21(27)24-13-20(26)25-9-3-4-16(25)12-22/h5-8,10-11,16H,3-4,9,13H2,1-2H3,(H,24,27)/t16-/m0/s1	PEIGQCUUABOKIO-INIZCTEOSA-N	50009340	CHEMBL3233559::US9346814, Cmpd No 15 Example 19	Prolyl endopeptidase FAP			 220							ChEMBL	10.1021/jm500031w	10.7270/Q2P84DFW	24617858			Jansen, K; Heirbaut, L; Verkerk, R; Cheng, JD; Joossens, J; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50009340	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50009340&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			71667379	103922396		CHEMBL3233559				ZINC26404600	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50088641	O=C(CNC(=O)c1ccnc(c1)-c1ccc(cc1)C#N)N1CCC[C@H]1C#N	InChI=1S/C20H17N5O2/c21-11-14-3-5-15(6-4-14)18-10-16(7-8-23-18)20(27)24-13-19(26)25-9-1-2-17(25)12-22/h3-8,10,17H,1-2,9,13H2,(H,24,27)/t17-/m0/s1	NPTPMAMSSQKOKH-KRWDZBQOSA-N	50009341	CHEMBL3233560::US9346814, Cmpd No 16 Example 20	Prolyl endopeptidase FAP			 270							ChEMBL	10.1021/jm500031w	10.7270/Q2P84DFW	24617858			Jansen, K; Heirbaut, L; Verkerk, R; Cheng, JD; Joossens, J; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50009341	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50009341&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			71667380	103922397		CHEMBL3233560					1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50088642	O=C(CNC(=O)c1ccnc(c1)-c1ccccc1)N1CCC[C@H]1C#N	InChI=1S/C19H18N4O2/c20-12-16-7-4-10-23(16)18(24)13-22-19(25)15-8-9-21-17(11-15)14-5-2-1-3-6-14/h1-3,5-6,8-9,11,16H,4,7,10,13H2,(H,22,25)/t16-/m0/s1	XLDGEWVOCOXLNE-INIZCTEOSA-N	50009339	CHEMBL3233558::US9346814, Cmpd No 14 Example 18	Prolyl endopeptidase FAP			 290							ChEMBL	10.1021/jm500031w	10.7270/Q2P84DFW	24617858			Jansen, K; Heirbaut, L; Verkerk, R; Cheng, JD; Joossens, J; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50009339	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50009339&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			89705195	103922395		CHEMBL3233558					1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50088644	CC#CCn1c(nc2n(C)c(=O)n(Cc3nc(C)c4ccccc4n3)c(=O)c12)N1CCC[C@@H](N)C1	InChI=1S/C25H28N8O2/c1-4-5-13-32-21-22(29-24(32)31-12-8-9-17(26)14-31)30(3)25(35)33(23(21)34)15-20-27-16(2)18-10-6-7-11-19(18)28-20/h6-7,10-11,17H,8-9,12-15,26H2,1-3H3/t17-/m1/s1	LTXREWYXXSTFRX-QGZVFWFLSA-N	50228403	(R)-8-(3-aminopiperidin-1-yl)-7-(but-2-ynyl)-3-methyl-1-((4-methylquinazolin-2-yl)methyl)-1H-purine-2,6(3H,7H)-dione::8-[(3R)-3-Aminopiperidin-1-yl]-7-but-2-yn-1-yl-3-methyl-1-[(4-methylquinazolin-2-yl)methyl]-3,7-dihydro-1H-purine-2,6-dione::CHEMBL237500::LINAGLIPTIN::US10202383, Example 2(142)::US10358449, Linagliptin::US9255098, Linagliptin::US9321791, 2(142)::US9556175, 2(142)	Prolyl endopeptidase FAP			 370							ChEMBL	10.1021/jm500031w	10.7270/Q2P84DFW	24617858			Jansen, K; Heirbaut, L; Verkerk, R; Cheng, JD; Joossens, J; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50228403	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50228403&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	356	2RGU,6Y0F	10096344	104097872	68610	CHEMBL237500	DB08882	6318		ZINC03820029	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50088646	O=C(CNC(=O)C1CCNCC1)N1CCC[C@H]1C#N	InChI=1S/C13H20N4O2/c14-8-11-2-1-7-17(11)12(18)9-16-13(19)10-3-5-15-6-4-10/h10-11,15H,1-7,9H2,(H,16,19)/t11-/m0/s1	AAKIUXAGDURVCO-NSHDSACASA-N	50009343	CHEMBL3233562::US9346814, Cmpd No 20 Example 24	Prolyl endopeptidase FAP			 750							ChEMBL	10.1021/jm500031w	10.7270/Q2P84DFW	24617858			Jansen, K; Heirbaut, L; Verkerk, R; Cheng, JD; Joossens, J; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50009343	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50009343&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			89704942	103922399		CHEMBL3233562				ZINC26404675	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50088647	Clc1cc(ccn1)C(=O)NCC(=O)N1CCC[C@H]1C#N	InChI=1S/C13H13ClN4O2/c14-11-6-9(3-4-16-11)13(20)17-8-12(19)18-5-1-2-10(18)7-15/h3-4,6,10H,1-2,5,8H2,(H,17,20)/t10-/m0/s1	XWOCACGCHOXVHP-JTQLQIEISA-N	50009335	CHEMBL3233555	Prolyl endopeptidase FAP			 760							ChEMBL	10.1021/jm500031w	10.7270/Q2P84DFW	24617858			Jansen, K; Heirbaut, L; Verkerk, R; Cheng, JD; Joossens, J; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50009335	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50009335&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			90655552	103922391		CHEMBL3233555				ZINC96178794	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50088652	F[C@@H]1C[C@@H](C#N)N(C1)C(=O)CNC(=O)c1ccnc2ccccc12	InChI=1S/C17H15FN4O2/c18-11-7-12(8-19)22(10-11)16(23)9-21-17(24)14-5-6-20-15-4-2-1-3-13(14)15/h1-6,11-12H,7,9-10H2,(H,21,24)/t11-,12+/m1/s1	ORRRPUSEMSKTEW-NEPJUHHUSA-N	50009365	CHEMBL3233841	Prolyl endopeptidase FAP			 1000							ChEMBL	10.1021/jm500031w	10.7270/Q2P84DFW	24617858			Jansen, K; Heirbaut, L; Verkerk, R; Cheng, JD; Joossens, J; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50009365	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50009365&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			90655560	242057371		CHEMBL3233841					1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50088654	Cn1cncc1C(=O)NCC(=O)N1CCC[C@H]1C#N	InChI=1S/C12H15N5O2/c1-16-8-14-6-10(16)12(19)15-7-11(18)17-4-2-3-9(17)5-13/h6,8-9H,2-4,7H2,1H3,(H,15,19)/t9-/m0/s1	ZLOHMZQDNJLLNP-VIFPVBQESA-N	50009345	CHEMBL3233564::US9346814, Cmpd No 17 Example 21	Prolyl endopeptidase FAP			 1370							ChEMBL	10.1021/jm500031w	10.7270/Q2P84DFW	24617858			Jansen, K; Heirbaut, L; Verkerk, R; Cheng, JD; Joossens, J; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50009345	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50009345&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			89705223	103922401		CHEMBL3233564					1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50088659	Cc1ncsc1C(=O)NCC(=O)N1CCC[C@H]1C#N	InChI=1S/C12H14N4O2S/c1-8-11(19-7-15-8)12(18)14-6-10(17)16-4-2-3-9(16)5-13/h7,9H,2-4,6H2,1H3,(H,14,18)/t9-/m0/s1	PCAKJIOLXFXXJM-VIFPVBQESA-N	50009348	CHEMBL3233568::US9346814, Cmpd No 18 Example 22	Prolyl endopeptidase FAP			 2500							ChEMBL	10.1021/jm500031w	10.7270/Q2P84DFW	24617858			Jansen, K; Heirbaut, L; Verkerk, R; Cheng, JD; Joossens, J; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50009348	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50009348&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			71667381	103922404		CHEMBL3233568				ZINC13823406	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50088662	O=C(CNC(=O)c1ccnc2ncnn12)N1CCC[C@H]1C#N	InChI=1S/C13H13N7O2/c14-6-9-2-1-5-19(9)11(21)7-16-12(22)10-3-4-15-13-17-8-18-20(10)13/h3-4,8-9H,1-2,5,7H2,(H,16,22)/t9-/m0/s1	JYTXLAIYDQBXKG-VIFPVBQESA-N	50009357	CHEMBL3233575::US9346814, Cmpd No 30 Example 35	Prolyl endopeptidase FAP			 3200							ChEMBL	10.1021/jm500031w	10.7270/Q2P84DFW	24617858			Jansen, K; Heirbaut, L; Verkerk, R; Cheng, JD; Joossens, J; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50009357	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50009357&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			89705098	242057363		CHEMBL3233575					1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50088663	O=C(Cc1ccncc1)NCC(=O)N1CCC[C@H]1C#N	InChI=1S/C14H16N4O2/c15-9-12-2-1-7-18(12)14(20)10-17-13(19)8-11-3-5-16-6-4-11/h3-6,12H,1-2,7-8,10H2,(H,17,19)/t12-/m0/s1	QWDLZJWJBMCYCH-LBPRGKRZSA-N	50009342	CHEMBL3233561::US9346814, Cmpd No 34 Example 39	Prolyl endopeptidase FAP			 3300							ChEMBL	10.1021/jm500031w	10.7270/Q2P84DFW	24617858			Jansen, K; Heirbaut, L; Verkerk, R; Cheng, JD; Joossens, J; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50009342	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50009342&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			89705045	103922398		CHEMBL3233561				ZINC26404931	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50088664	C[C@@H](NC(=O)c1ccnc2ccccc12)C(=O)N1CCC[C@H]1C#N	InChI=1S/C18H18N4O2/c1-12(18(24)22-10-4-5-13(22)11-19)21-17(23)15-8-9-20-16-7-3-2-6-14(15)16/h2-3,6-9,12-13H,4-5,10H2,1H3,(H,21,23)/t12-,13+/m1/s1	CJZDFIOVUXAMNO-OLZOCXBDSA-N	50009314	CHEMBL3233539::US9346814, Cmpd No 32 Example 37	Prolyl endopeptidase FAP			 3400							ChEMBL	10.1021/jm500031w	10.7270/Q2P84DFW	24617858			Jansen, K; Heirbaut, L; Verkerk, R; Cheng, JD; Joossens, J; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50009314	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50009314&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			89705242	103922370		CHEMBL3233539				ZINC13823260	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50088666	O=C(CNC(=O)c1ccnc2ccccc12)N1CCCC1	InChI=1S/C16H17N3O2/c20-15(19-9-3-4-10-19)11-18-16(21)13-7-8-17-14-6-2-1-5-12(13)14/h1-2,5-8H,3-4,9-11H2,(H,18,21)	HNILXENRYUEFQQ-UHFFFAOYSA-N	50009368	CHEMBL3233846	Prolyl endopeptidase FAP			 5100							ChEMBL	10.1021/jm500031w	10.7270/Q2P84DFW	24617858			Jansen, K; Heirbaut, L; Verkerk, R; Cheng, JD; Joossens, J; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50009368	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50009368&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			90655561	242057373		CHEMBL3233846					1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50088668	O=C(CNC(=O)c1cnn[nH]1)N1CCC[C@H]1C#N	InChI=1S/C10H12N6O2/c11-4-7-2-1-3-16(7)9(17)6-12-10(18)8-5-13-15-14-8/h5,7H,1-3,6H2,(H,12,18)(H,13,14,15)/t7-/m0/s1	AUGPBTYKMNUDPD-ZETCQYMHSA-N	50009346	CHEMBL3233565::US9346814, Cmpd No 36 Example 41	Prolyl endopeptidase FAP			 5700							ChEMBL	10.1021/jm500031w	10.7270/Q2P84DFW	24617858			Jansen, K; Heirbaut, L; Verkerk, R; Cheng, JD; Joossens, J; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50009346	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50009346&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			89712515	103922402		CHEMBL3233565					1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50088671	OC[C@@H](NC(=O)c1ccnc2ccccc12)C(=O)N1CCC[C@H]1C#N	InChI=1S/C18H18N4O3/c19-10-12-4-3-9-22(12)18(25)16(11-23)21-17(24)14-7-8-20-15-6-2-1-5-13(14)15/h1-2,5-8,12,16,23H,3-4,9,11H2,(H,21,24)/t12-,16+/m0/s1	PSQZNYNIMSKARP-BLLLJJGKSA-N	50009313	CHEMBL3233538::US9346814, Cmpd No 31 Example 36	Prolyl endopeptidase FAP			 6000							ChEMBL	10.1021/jm500031w	10.7270/Q2P84DFW	24617858			Jansen, K; Heirbaut, L; Verkerk, R; Cheng, JD; Joossens, J; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50009313	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50009313&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			89705076	103922369		CHEMBL3233538				ZINC13823333	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50088675	FC(F)(F)C(=O)Nc1ccc(cc1)C(=O)NCC(=O)N1CCC[C@H]1C#N	InChI=1S/C16H15F3N4O3/c17-16(18,19)15(26)22-11-5-3-10(4-6-11)14(25)21-9-13(24)23-7-1-2-12(23)8-20/h3-6,12H,1-2,7,9H2,(H,21,25)(H,22,26)/t12-/m0/s1	ZCTZDRRIVCTEJP-LBPRGKRZSA-N	50009351	CHEMBL3233571	Prolyl endopeptidase FAP			 7100							ChEMBL	10.1021/jm500031w	10.7270/Q2P84DFW	24617858			Jansen, K; Heirbaut, L; Verkerk, R; Cheng, JD; Joossens, J; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50009351	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50009351&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			90655557	242057359		CHEMBL3233571					1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50931695	FC(F)(F)[C@H]1C[C@@H](C#N)N(C1)C(=O)CNC(=O)c1cccc2ccccc12	InChI=1S/C19H16F3N3O2/c20-19(21,22)13-8-14(9-23)25(11-13)17(26)10-24-18(27)16-7-3-5-12-4-1-2-6-15(12)16/h1-7,13-14H,8,10-11H2,(H,24,27)/t13-,14-/m0/s1	QTTLXPRANRJVOU-KBPBESRZSA-N	50382255	CHEMBL2022533	Prolyl endopeptidase FAP			>100000							ChEMBL	10.1016/j.bmcl.2012.03.107	10.7270/Q27D2W5P	22525314			Ryabtsova, O; Jansen, K; Van Goethem, S; Joossens, J; Cheng, JD; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp (UA)	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50382255	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50382255&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			70691906	160861338		CHEMBL2022533				ZINC84604504	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50931767	O=C(CNC(=O)c1ccccc1)N1CCCC1	InChI=1S/C13H16N2O2/c16-12(15-8-4-5-9-15)10-14-13(17)11-6-2-1-3-7-11/h1-3,6-7H,4-5,8-10H2,(H,14,17)	CXSUVQOSBPNFDM-UHFFFAOYSA-N	50382276	CHEMBL2022523	Prolyl endopeptidase FAP			>100000							ChEMBL	10.1016/j.bmcl.2012.03.107	10.7270/Q27D2W5P	22525314			Ryabtsova, O; Jansen, K; Van Goethem, S; Joossens, J; Cheng, JD; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp (UA)	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50382276	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50382276&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			56877	160861359		CHEMBL2022523				ZINC01999960	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50931768	CC(C)(C)NC(=O)[C@@H]1CCCN1C(=O)CNC(=O)c1ccccc1	InChI=1S/C18H25N3O3/c1-18(2,3)20-17(24)14-10-7-11-21(14)15(22)12-19-16(23)13-8-5-4-6-9-13/h4-6,8-9,14H,7,10-12H2,1-3H3,(H,19,23)(H,20,24)/t14-/m0/s1	JELRFPRTNDTTHM-AWEZNQCLSA-N	50382277	CHEMBL2022524	Prolyl endopeptidase FAP			>25000							ChEMBL	10.1016/j.bmcl.2012.03.107	10.7270/Q27D2W5P	22525314			Ryabtsova, O; Jansen, K; Van Goethem, S; Joossens, J; Cheng, JD; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp (UA)	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50382277	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50382277&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			70689751	160861360		CHEMBL2022524				ZINC84596955	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50931769	O=C(CNC(=O)c1cccc2ccccc12)N1CCCC[C@H]1C#N	InChI=1S/C19H19N3O2/c20-12-15-8-3-4-11-22(15)18(23)13-21-19(24)17-10-5-7-14-6-1-2-9-16(14)17/h1-2,5-7,9-10,15H,3-4,8,11,13H2,(H,21,24)/t15-/m0/s1	XTLCRXIPSGQUNE-HNNXBMFYSA-N	50382286	CHEMBL2022535	Prolyl endopeptidase FAP			>50000							ChEMBL	10.1016/j.bmcl.2012.03.107	10.7270/Q27D2W5P	22525314			Ryabtsova, O; Jansen, K; Van Goethem, S; Joossens, J; Cheng, JD; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp (UA)	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50382286	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50382286&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			70693956	160861369		CHEMBL2022535				ZINC84604870	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50931777	CC(C)[C@H](N)C(=O)N1CCC[C@H]1B(O)O	InChI=1S/C9H19BN2O3/c1-6(2)8(11)9(13)12-5-3-4-7(12)10(14)15/h6-8,14-15H,3-5,11H2,1-2H3/t7-,8-/m0/s1	FKCMADOPPWWGNZ-YUMQZZPRSA-N	50050513	(R)-1-((S)-2-amino-3-methylbutanoyl)pyrrolidin-2-ylboronic acid::(S)-2-Amino-1-((R)-2-dihydroxyboron-pyrrolidin-1-yl)-3-methyl-butan-1-one::(S)-2-Amino-3-methyl-2-boronic acid-1-pyrrolidin-1-yl-butan-1-one::Boronic acid derivative::CHEMBL67279::Ketopyrrolidine derivative::Pyrrolidine derivative::US11096924, DASH-inhibitors 2504 C::US11504364, Compound Val-boroPro::US11559537, Compound 2054-Val-boro-Pro	Prolyl endopeptidase FAP			 66							ChEMBL	10.1016/j.bmcl.2012.03.107	10.7270/Q27D2W5P	22525314			Ryabtsova, O; Jansen, K; Van Goethem, S; Joossens, J; Cheng, JD; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp (UA)	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50050513	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50050513&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			6918572	103947674		CHEMBL67279					1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50931778	FC1(F)C[C@@H](C#N)N(C1)C(=O)CNC(=O)c1cccc2ccccc12	InChI=1S/C18H15F2N3O2/c19-18(20)8-13(9-21)23(11-18)16(24)10-22-17(25)15-7-3-5-12-4-1-2-6-14(12)15/h1-7,13H,8,10-11H2,(H,22,25)/t13-/m0/s1	YJNMDFARAFJSEZ-ZDUSSCGKSA-N	50382283	CHEMBL2022530::US9346814, Ref. Cmpd No 1 (Example 2)	Prolyl endopeptidase FAP			 110							ChEMBL	10.1016/j.bmcl.2012.03.107	10.7270/Q27D2W5P	22525314			Ryabtsova, O; Jansen, K; Van Goethem, S; Joossens, J; Cheng, JD; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp (UA)	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50382283	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50382283&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			66561557	160861366		CHEMBL2022530				ZINC84615945	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50931780	F[C@H]1C[C@@H](C#N)N(C1)C(=O)CNC(=O)c1cccc2ccccc12	InChI=1S/C18H16FN3O2/c19-13-8-14(9-20)22(11-13)17(23)10-21-18(24)16-7-3-5-12-4-1-2-6-15(12)16/h1-7,13-14H,8,10-11H2,(H,21,24)/t13-,14-/m0/s1	JIRNJLZNEMWKIK-KBPBESRZSA-N	50382281	CHEMBL2022528	Prolyl endopeptidase FAP			 126							ChEMBL	10.1016/j.bmcl.2012.03.107	10.7270/Q27D2W5P	22525314			Ryabtsova, O; Jansen, K; Van Goethem, S; Joossens, J; Cheng, JD; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp (UA)	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50382281	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50382281&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			66561555	160861364		CHEMBL2022528				ZINC84616479	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50931782	O=C(CNC(=O)c1cccc2ccccc12)N1CCC[C@H]1C#N	InChI=1S/C18H17N3O2/c19-11-14-7-4-10-21(14)17(22)12-20-18(23)16-9-3-6-13-5-1-2-8-15(13)16/h1-3,5-6,8-9,14H,4,7,10,12H2,(H,20,23)/t14-/m0/s1	HSIDTMLTVRFYGR-AWEZNQCLSA-N	50326374	(S)-N-(2-(2-cyanopyrrolidin-1-yl)-2-oxoethyl)-1-naphthamide::CHEMBL1243374	Prolyl endopeptidase FAP			 670							ChEMBL	10.1016/j.bmcl.2012.03.107	10.7270/Q27D2W5P	22525314			Ryabtsova, O; Jansen, K; Van Goethem, S; Joossens, J; Cheng, JD; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp (UA)	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50326374	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50326374&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			16040457	123105489		CHEMBL1243374				ZINC34884435	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50931783	FC1(F)C[C@@H](C#N)N(C1)C(=O)CNC(=O)c1ccccc1	InChI=1S/C14H13F2N3O2/c15-14(16)6-11(7-17)19(9-14)12(20)8-18-13(21)10-4-2-1-3-5-10/h1-5,11H,6,8-9H2,(H,18,21)/t11-/m0/s1	INJITBQMFDNYGO-NSHDSACASA-N	50382282	CHEMBL2022529	Prolyl endopeptidase FAP			 850							ChEMBL	10.1016/j.bmcl.2012.03.107	10.7270/Q27D2W5P	22525314			Ryabtsova, O; Jansen, K; Van Goethem, S; Joossens, J; Cheng, JD; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp (UA)	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50382282	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50382282&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			66561556	160861365		CHEMBL2022529				ZINC84616481	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50931786	Fc1ccc(cc1F)-c1cn(CC(=O)NCC(=O)N2CCC[C@H]2C#N)nn1	InChI=1S/C17H16F2N6O2/c18-13-4-3-11(6-14(13)19)15-9-24(23-22-15)10-16(26)21-8-17(27)25-5-1-2-12(25)7-20/h3-4,6,9,12H,1-2,5,8,10H2,(H,21,26)/t12-/m0/s1	PBCGPJOUIDJSHJ-LBPRGKRZSA-N	50382274	CHEMBL2022521	Prolyl endopeptidase FAP			 1300							ChEMBL	10.1016/j.bmcl.2012.03.107	10.7270/Q27D2W5P	22525314			Ryabtsova, O; Jansen, K; Van Goethem, S; Joossens, J; Cheng, JD; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp (UA)	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50382274	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50382274&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			70693953	160861357		CHEMBL2022521				ZINC33134815	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50931787	O=C(CNC(=O)c1cccc(c1)-c1ccccc1)N1CCC[C@H]1C#N	InChI=1S/C20H19N3O2/c21-13-18-10-5-11-23(18)19(24)14-22-20(25)17-9-4-8-16(12-17)15-6-2-1-3-7-15/h1-4,6-9,12,18H,5,10-11,14H2,(H,22,25)/t18-/m0/s1	FJWRWAFBWCAAQZ-SFHVURJKSA-N	50382267	CHEMBL2022513	Prolyl endopeptidase FAP			 1400							ChEMBL	10.1016/j.bmcl.2012.03.107	10.7270/Q27D2W5P	22525314			Ryabtsova, O; Jansen, K; Van Goethem, S; Joossens, J; Cheng, JD; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp (UA)	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50382267	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50382267&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			70681357	160861350		CHEMBL2022513				ZINC84635943	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50931790	Clc1ccc(cc1)C(C(=O)NCC(=O)N1CCC[C@H]1C#N)c1ccc(Cl)cc1	InChI=1S/C21H19Cl2N3O2/c22-16-7-3-14(4-8-16)20(15-5-9-17(23)10-6-15)21(28)25-13-19(27)26-11-1-2-18(26)12-24/h3-10,18,20H,1-2,11,13H2,(H,25,28)/t18-/m0/s1	RJDRVPZZIUCYOD-SFHVURJKSA-N	50382253	CHEMBL2022508	Prolyl endopeptidase FAP			 1900							ChEMBL	10.1016/j.bmcl.2012.03.107	10.7270/Q27D2W5P	22525314			Ryabtsova, O; Jansen, K; Van Goethem, S; Joossens, J; Cheng, JD; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp (UA)	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50382253	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50382253&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			70693949	160861336		CHEMBL2022508				ZINC84602451	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50931791	COc1cccc(c1)C(=O)NCC(=O)N1CCC[C@H]1C#N	InChI=1S/C15H17N3O3/c1-21-13-6-2-4-11(8-13)15(20)17-10-14(19)18-7-3-5-12(18)9-16/h2,4,6,8,12H,3,5,7,10H2,1H3,(H,17,20)/t12-/m0/s1	IQIYWEWUYQHYOE-LBPRGKRZSA-N	50382288	CHEMBL2024673	Prolyl endopeptidase FAP			 2400							ChEMBL	10.1016/j.bmcl.2012.03.107	10.7270/Q27D2W5P	22525314			Ryabtsova, O; Jansen, K; Van Goethem, S; Joossens, J; Cheng, JD; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp (UA)	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50382288	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50382288&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			70681469	160861371		CHEMBL2024673				ZINC84616049	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50931793	Fc1ccc(cc1)C(N1CCN(CC(=O)NCC(=O)N2CCC[C@H]2C#N)CC1)c1ccc(F)cc1	InChI=1S/C26H29F2N5O2/c27-21-7-3-19(4-8-21)26(20-5-9-22(28)10-6-20)32-14-12-31(13-15-32)18-24(34)30-17-25(35)33-11-1-2-23(33)16-29/h3-10,23,26H,1-2,11-15,17-18H2,(H,30,34)/t23-/m0/s1	ITQFEESMKGHJPM-QHCPKHFHSA-N	50382258	CHEMBL2022516	Prolyl endopeptidase FAP			 2700							ChEMBL	10.1016/j.bmcl.2012.03.107	10.7270/Q27D2W5P	22525314			Ryabtsova, O; Jansen, K; Van Goethem, S; Joossens, J; Cheng, JD; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp (UA)	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50382258	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50382258&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			70693951	160861341		CHEMBL2022516				ZINC84619819	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50931794	CC(C)(C)OC(=O)N1CCN(CC1)c1cn(CC(=O)NCC(=O)N2CCC[C@H]2C#N)nn1	InChI=1S/C20H30N8O4/c1-20(2,3)32-19(31)26-9-7-25(8-10-26)16-13-27(24-23-16)14-17(29)22-12-18(30)28-6-4-5-15(28)11-21/h13,15H,4-10,12,14H2,1-3H3,(H,22,29)/t15-/m0/s1	KFZZQZJGMJGLDZ-HNNXBMFYSA-N	50382275	CHEMBL2022522	Prolyl endopeptidase FAP			 2700							ChEMBL	10.1016/j.bmcl.2012.03.107	10.7270/Q27D2W5P	22525314			Ryabtsova, O; Jansen, K; Van Goethem, S; Joossens, J; Cheng, JD; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp (UA)	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50382275	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50382275&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			70685560	160861358		CHEMBL2022522				ZINC84632789	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50931796	O=C(CNC(=O)c1ccccc1)N1CCC[C@H]1C#N	InChI=1S/C14H15N3O2/c15-9-12-7-4-8-17(12)13(18)10-16-14(19)11-5-2-1-3-6-11/h1-3,5-6,12H,4,7-8,10H2,(H,16,19)/t12-/m0/s1	ZABQVUZXDYHZPO-LBPRGKRZSA-N	50382254	CHEMBL2024672	Prolyl endopeptidase FAP			 3500							ChEMBL	10.1016/j.bmcl.2012.03.107	10.7270/Q27D2W5P	22525314			Ryabtsova, O; Jansen, K; Van Goethem, S; Joossens, J; Cheng, JD; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp (UA)	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50382254	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50382254&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			15951642	160861337		CHEMBL2024672				ZINC33352988	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50931797	COc1ccc(cc1OC1CCCC1)C(=O)NCC(=O)N1CCC[C@H]1C#N	InChI=1S/C20H25N3O4/c1-26-17-9-8-14(11-18(17)27-16-6-2-3-7-16)20(25)22-13-19(24)23-10-4-5-15(23)12-21/h8-9,11,15-16H,2-7,10,13H2,1H3,(H,22,25)/t15-/m0/s1	BEJSIQLVRYUNRD-HNNXBMFYSA-N	50382264	CHEMBL2022510	Prolyl endopeptidase FAP			 3700							ChEMBL	10.1016/j.bmcl.2012.03.107	10.7270/Q27D2W5P	22525314			Ryabtsova, O; Jansen, K; Van Goethem, S; Joossens, J; Cheng, JD; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp (UA)	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50382264	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50382264&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			70689750	160861347		CHEMBL2022510				ZINC84602455	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50931798	Clc1ccc(CC(=O)NCC(=O)N2CCC[C@H]2C#N)cc1	InChI=1S/C15H16ClN3O2/c16-12-5-3-11(4-6-12)8-14(20)18-10-15(21)19-7-1-2-13(19)9-17/h3-6,13H,1-2,7-8,10H2,(H,18,20)/t13-/m0/s1	UOSJMPWHXCJRPO-ZDUSSCGKSA-N	50382262	CHEMBL2022507	Prolyl endopeptidase FAP			 3900							ChEMBL	10.1016/j.bmcl.2012.03.107	10.7270/Q27D2W5P	22525314			Ryabtsova, O; Jansen, K; Van Goethem, S; Joossens, J; Cheng, JD; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp (UA)	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50382262	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50382262&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			70685558	160861345		CHEMBL2022507				ZINC84616008	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50931799	[N-]=[N+]=N[C@H]1C[C@@H](C#N)N(C1)C(=O)CNC(=O)c1cccc2ccccc12	InChI=1S/C18H16N6O2/c19-9-14-8-13(22-23-20)11-24(14)17(25)10-21-18(26)16-7-3-5-12-4-1-2-6-15(12)16/h1-7,13-14H,8,10-11H2,(H,21,26)/t13-,14-/m0/s1	IPKHAZSRZNIQAI-KBPBESRZSA-N	50382279	CHEMBL2022526	Prolyl endopeptidase FAP			 4100							ChEMBL	10.1016/j.bmcl.2012.03.107	10.7270/Q27D2W5P	22525314			Ryabtsova, O; Jansen, K; Van Goethem, S; Joossens, J; Cheng, JD; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp (UA)	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50382279	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50382279&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			70693954	160861362		CHEMBL2022526				ZINC84616477	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50931800	FC(F)(F)Oc1ccc(cc1)C(=O)NCC(=O)N1CCC[C@H]1C#N	InChI=1S/C15H14F3N3O3/c16-15(17,18)24-12-5-3-10(4-6-12)14(23)20-9-13(22)21-7-1-2-11(21)8-19/h3-6,11H,1-2,7,9H2,(H,20,23)/t11-/m0/s1	HOTVTJAOELXOOP-NSHDSACASA-N	50382263	CHEMBL2022509	Prolyl endopeptidase FAP			 4700							ChEMBL	10.1016/j.bmcl.2012.03.107	10.7270/Q27D2W5P	22525314			Ryabtsova, O; Jansen, K; Van Goethem, S; Joossens, J; Cheng, JD; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp (UA)	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50382263	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50382263&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			70696068	160861346		CHEMBL2022509				ZINC84602453	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50931803	COc1cccc(c1)S(=O)(=O)NCC(=O)N1CCC[C@H]1C#N	InChI=1S/C14H17N3O4S/c1-21-12-5-2-6-13(8-12)22(19,20)16-10-14(18)17-7-3-4-11(17)9-15/h2,5-6,8,11,16H,3-4,7,10H2,1H3/t11-/m0/s1	DTKPPUMQPVCMBK-NSHDSACASA-N	50382269	CHEMBL2022515	Prolyl endopeptidase FAP			 5100							ChEMBL	10.1016/j.bmcl.2012.03.107	10.7270/Q27D2W5P	22525314			Ryabtsova, O; Jansen, K; Van Goethem, S; Joossens, J; Cheng, JD; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp (UA)	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50382269	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50382269&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			70693950	160861352		CHEMBL2022515				ZINC84619818	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50931806	C=C1C[C@@H](C#N)N(C1)C(=O)CNC(=O)c1cccc2ccccc12	InChI=1S/C19H17N3O2/c1-13-9-15(10-20)22(12-13)18(23)11-21-19(24)17-8-4-6-14-5-2-3-7-16(14)17/h2-8,15H,1,9,11-12H2,(H,21,24)/t15-/m0/s1	XIQKWOFLZYKFMT-HNNXBMFYSA-N	50382257	CHEMBL2022531	Prolyl endopeptidase FAP			 6700							ChEMBL	10.1016/j.bmcl.2012.03.107	10.7270/Q27D2W5P	22525314			Ryabtsova, O; Jansen, K; Van Goethem, S; Joossens, J; Cheng, JD; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp (UA)	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50382257	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50382257&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			70683455	160861340		CHEMBL2022531				ZINC84632782	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50931807	O=C(Cc1cccs1)NCC(=O)N1CCC[C@H]1C#N	InChI=1S/C13H15N3O2S/c14-8-10-3-1-5-16(10)13(18)9-15-12(17)7-11-4-2-6-19-11/h2,4,6,10H,1,3,5,7,9H2,(H,15,17)/t10-/m0/s1	BNNRSCBPHPLKSC-JTQLQIEISA-N	50382261	CHEMBL2022506	Prolyl endopeptidase FAP			 6800							ChEMBL	10.1016/j.bmcl.2012.03.107	10.7270/Q27D2W5P	22525314			Ryabtsova, O; Jansen, K; Van Goethem, S; Joossens, J; Cheng, JD; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp (UA)	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50382261	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50382261&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			70685557	160861344		CHEMBL2022506				ZINC84633981	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50931808	O=C(CNC(=O)c1ccc2ccccc2c1)N1CCC[C@H]1C#N	InChI=1S/C18H17N3O2/c19-11-16-6-3-9-21(16)17(22)12-20-18(23)15-8-7-13-4-1-2-5-14(13)10-15/h1-2,4-5,7-8,10,16H,3,6,9,12H2,(H,20,23)/t16-/m0/s1	INDDLILZWSZTPZ-INIZCTEOSA-N	50382268	CHEMBL2022514	Prolyl endopeptidase FAP			 7500							ChEMBL	10.1016/j.bmcl.2012.03.107	10.7270/Q27D2W5P	22525314			Ryabtsova, O; Jansen, K; Van Goethem, S; Joossens, J; Cheng, JD; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp (UA)	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50382268	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50382268&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			70691901	160861351		CHEMBL2022514				ZINC84619817	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50931809	O=C(CNC(=O)c1ccc(cc1)-c1cccs1)N1CCC[C@H]1C#N	InChI=1S/C18H17N3O2S/c19-11-15-3-1-9-21(15)17(22)12-20-18(23)14-7-5-13(6-8-14)16-4-2-10-24-16/h2,4-8,10,15H,1,3,9,12H2,(H,20,23)/t15-/m0/s1	BJKYXNIAGSVTCP-HNNXBMFYSA-N	50382266	CHEMBL2022512	Prolyl endopeptidase FAP			 8100							ChEMBL	10.1016/j.bmcl.2012.03.107	10.7270/Q27D2W5P	22525314			Ryabtsova, O; Jansen, K; Van Goethem, S; Joossens, J; Cheng, JD; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp (UA)	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50382266	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50382266&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			70696069	160861349		CHEMBL2022512				ZINC84602460	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50931810	O=C(CCc1ccccc1)NCC(=O)N1CCC[C@H]1C#N	InChI=1S/C16H19N3O2/c17-11-14-7-4-10-19(14)16(21)12-18-15(20)9-8-13-5-2-1-3-6-13/h1-3,5-6,14H,4,7-10,12H2,(H,18,20)/t14-/m0/s1	JGRKLZOYDCJADH-AWEZNQCLSA-N	50382260	CHEMBL2022505	Prolyl endopeptidase FAP			 9400							ChEMBL	10.1016/j.bmcl.2012.03.107	10.7270/Q27D2W5P	22525314			Ryabtsova, O; Jansen, K; Van Goethem, S; Joossens, J; Cheng, JD; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp (UA)	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50382260	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50382260&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			70683454	160861343		CHEMBL2022505				ZINC84616006	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50931812	Fc1ccc(CN2CCN(CC2)C(=O)CCC(=O)NCC(=O)N2CCC[C@H]2C#N)cc1	InChI=1S/C22H28FN5O3/c23-18-5-3-17(4-6-18)16-26-10-12-27(13-11-26)21(30)8-7-20(29)25-15-22(31)28-9-1-2-19(28)14-24/h3-6,19H,1-2,7-13,15-16H2,(H,25,29)/t19-/m0/s1	TZAGITFKZZAYTH-IBGZPJMESA-N	50382272	CHEMBL2022519	Prolyl endopeptidase FAP			 10300							ChEMBL	10.1016/j.bmcl.2012.03.107	10.7270/Q27D2W5P	22525314			Ryabtsova, O; Jansen, K; Van Goethem, S; Joossens, J; Cheng, JD; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp (UA)	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50382272	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50382272&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			70693952	160861355		CHEMBL2022519				ZINC84618084	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50931813	Fc1ccc(CNC(=O)CCC(=O)NCC(=O)N2CCC[C@H]2C#N)cc1	InChI=1S/C18H21FN4O3/c19-14-5-3-13(4-6-14)11-21-16(24)7-8-17(25)22-12-18(26)23-9-1-2-15(23)10-20/h3-6,15H,1-2,7-9,11-12H2,(H,21,24)(H,22,25)/t15-/m0/s1	TXILAFXSFBBAJD-HNNXBMFYSA-N	50382270	CHEMBL2022517	Prolyl endopeptidase FAP			 12000							ChEMBL	10.1016/j.bmcl.2012.03.107	10.7270/Q27D2W5P	22525314			Ryabtsova, O; Jansen, K; Van Goethem, S; Joossens, J; Cheng, JD; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp (UA)	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50382270	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50382270&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			70691902	160861353		CHEMBL2022517				ZINC84619820	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50931815	CC(C)CC(=O)NCC(=O)N1CCC[C@H]1C#N	InChI=1S/C12H19N3O2/c1-9(2)6-11(16)14-8-12(17)15-5-3-4-10(15)7-13/h9-10H,3-6,8H2,1-2H3,(H,14,16)/t10-/m0/s1	XCXDAEWFUWZUBU-JTQLQIEISA-N	50382256	CHEMBL2024674	Prolyl endopeptidase FAP			 14000							ChEMBL	10.1016/j.bmcl.2012.03.107	10.7270/Q27D2W5P	22525314			Ryabtsova, O; Jansen, K; Van Goethem, S; Joossens, J; Cheng, JD; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp (UA)	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50382256	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50382256&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			70681470	160861339		CHEMBL2024674				ZINC84632689	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50931816	Clc1cccc(Cl)c1C(=O)NCC(=O)N1CCC[C@H]1C#N	InChI=1S/C14H13Cl2N3O2/c15-10-4-1-5-11(16)13(10)14(21)18-8-12(20)19-6-2-3-9(19)7-17/h1,4-5,9H,2-3,6,8H2,(H,18,21)/t9-/m0/s1	CEQDXLZRRYUVKY-VIFPVBQESA-N	50382265	CHEMBL2022511	Prolyl endopeptidase FAP			 14600							ChEMBL	10.1016/j.bmcl.2012.03.107	10.7270/Q27D2W5P	22525314			Ryabtsova, O; Jansen, K; Van Goethem, S; Joossens, J; Cheng, JD; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp (UA)	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50382265	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50382265&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			70687705	160861348		CHEMBL2022511				ZINC84602457	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50931818	[N-]=[N+]=N[C@H]1C[C@@H](C#N)N(C1)C(=O)CNC(=O)c1ccccc1	InChI=1S/C14H14N6O2/c15-7-12-6-11(18-19-16)9-20(12)13(21)8-17-14(22)10-4-2-1-3-5-10/h1-5,11-12H,6,8-9H2,(H,17,22)/t11-,12-/m0/s1	IEKVJTRASXFLGU-RYUDHWBXSA-N	50382278	CHEMBL2022525	Prolyl endopeptidase FAP			 17500							ChEMBL	10.1016/j.bmcl.2012.03.107	10.7270/Q27D2W5P	22525314			Ryabtsova, O; Jansen, K; Van Goethem, S; Joossens, J; Cheng, JD; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp (UA)	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50382278	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50382278&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			70691903	160861361		CHEMBL2022525				ZINC84634730	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50931819	Fc1ccc(cc1)C(N1CCN(CC1)C(=O)CCC(=O)NCC(=O)N1CCC[C@H]1C#N)c1ccc(F)cc1	InChI=1S/C28H31F2N5O3/c29-22-7-3-20(4-8-22)28(21-5-9-23(30)10-6-21)34-16-14-33(15-17-34)26(37)12-11-25(36)32-19-27(38)35-13-1-2-24(35)18-31/h3-10,24,28H,1-2,11-17,19H2,(H,32,36)/t24-/m0/s1	MMSXBRWGWZXQBP-DEOSSOPVSA-N	50382273	CHEMBL2022520	Prolyl endopeptidase FAP			 19900							ChEMBL	10.1016/j.bmcl.2012.03.107	10.7270/Q27D2W5P	22525314			Ryabtsova, O; Jansen, K; Van Goethem, S; Joossens, J; Cheng, JD; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp (UA)	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50382273	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50382273&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			70685559	160861356		CHEMBL2022520				ZINC33096891	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50931820	Fc1ccc(cc1)C(NC(=O)CCC(=O)NCC(=O)N1CCC[C@H]1C#N)c1ccc(F)cc1	InChI=1S/C24H24F2N4O3/c25-18-7-3-16(4-8-18)24(17-5-9-19(26)10-6-17)29-22(32)12-11-21(31)28-15-23(33)30-13-1-2-20(30)14-27/h3-10,20,24H,1-2,11-13,15H2,(H,28,31)(H,29,32)/t20-/m0/s1	HNYOSYHIRFAFLV-FQEVSTJZSA-N	50382271	CHEMBL2022518	Prolyl endopeptidase FAP			 20000							ChEMBL	10.1016/j.bmcl.2012.03.107	10.7270/Q27D2W5P	22525314			Ryabtsova, O; Jansen, K; Van Goethem, S; Joossens, J; Cheng, JD; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp (UA)	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50382271	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50382271&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			70687706	160861354		CHEMBL2022518				ZINC84632305	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50931822	CCC1C[C@@H](C#N)N(C1)C(=O)CNC(=O)c1cccc2ccccc12	InChI=1S/C20H21N3O2/c1-2-14-10-16(11-21)23(13-14)19(24)12-22-20(25)18-9-5-7-15-6-3-4-8-17(15)18/h3-9,14,16H,2,10,12-13H2,1H3,(H,22,25)/t14?,16-/m0/s1	FCBMNMZZMXCXAF-WMCAAGNKSA-N	50382285	CHEMBL2022532	Prolyl endopeptidase FAP			 42000							ChEMBL	10.1016/j.bmcl.2012.03.107	10.7270/Q27D2W5P	22525314			Ryabtsova, O; Jansen, K; Van Goethem, S; Joossens, J; Cheng, JD; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp (UA)	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50382285	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50382285&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			70691905	160861368		CHEMBL2022532				ZINC84634754	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50931823	OC12CC3CC(C1)CC(C3)(C2)NCC(=O)N1CCC[C@H]1C#N	InChI=1S/C17H25N3O2/c18-9-14-2-1-3-20(14)15(21)10-19-16-5-12-4-13(6-16)8-17(22,7-12)11-16/h12-14,19,22H,1-8,10-11H2/t12?,13?,14-,16?,17?/m0/s1	SYOKIDBDQMKNDQ-XWTIBIIYSA-N	11695	(2S)-1-{2-[(3-hydroxyadamantan-1-yl)amino]acetyl}pyrrolidine-2-carbonitrile::CHEMBL142703::NVP-LAF237	Prolyl endopeptidase FAP			 52000							ChEMBL	10.1016/j.bmcl.2012.03.107	10.7270/Q27D2W5P	22525314			Ryabtsova, O; Jansen, K; Van Goethem, S; Joossens, J; Cheng, JD; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp (UA)	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=11695	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=11695&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			6918537	46512217		CHEMBL142703	DB04876	6310		ZINC13523046	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50931828	O=C(CCCc1ccccc1)N1CCC[C@@H]1C(=O)N1CCC[C@H]1C#N	InChI=1S/C20H25N3O2/c21-15-17-10-5-13-22(17)20(25)18-11-6-14-23(18)19(24)12-4-9-16-7-2-1-3-8-16/h1-3,7-8,17-18H,4-6,9-14H2/t17-,18+/m0/s1	SPXFAUXQZWJGCJ-ZWKOTPCHSA-N	50382287	CHEMBL2024671	Prolyl endopeptidase FAP			>100000							ChEMBL	10.1016/j.bmcl.2012.03.107	10.7270/Q27D2W5P	22525314			Ryabtsova, O; Jansen, K; Van Goethem, S; Joossens, J; Cheng, JD; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp (UA)	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50382287	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50382287&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			70685696	160861370		CHEMBL2024671				ZINC84602442	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50931829	N[C@@H](CC(=O)N1CCn2c(C1)nnc2C(F)(F)F)Cc1cc(F)c(F)cc1F	InChI=1S/C16H15F6N5O/c17-10-6-12(19)11(18)4-8(10)3-9(23)5-14(28)26-1-2-27-13(7-26)24-25-15(27)16(20,21)22/h4,6,9H,1-3,5,7,23H2/t9-/m1/s1	MFFMDFFZMYYVKS-SECBINFHSA-N	11162	(1R)-3-oxo-3-[3-(trifluoroethyl)-5,6-dihydro[1,2,4]triazolo[4,3-a]pyrazin-7(8H)-yl]-1-(2,4,5-trifluorobenzyl)propylamine::(3R)-3-amino-1-[3-(trifluoromethyl)-5H,6H,7H,8H-[1,2,4]triazolo[3,4-a]pyrazin-7-yl]-4-(2,4,5-trifluorophenyl)butan-1-one hydrochloride::CHEMBL393336::MK-0431::Sitagliptin::Sitagliptin (13)::Triazolopiperazine Analogue 1::US10479798, Compound MK0431	Prolyl endopeptidase FAP			>100000							ChEMBL	10.1016/j.bmcl.2012.03.107	10.7270/Q27D2W5P	22525314			Ryabtsova, O; Jansen, K; Van Goethem, S; Joossens, J; Cheng, JD; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp (UA)	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=11162	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=11162&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	715	1X70,4FFW	4369359	46511716		CHEMBL393336	DB01261			ZINC01489478	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50931830	[N-]=[N+]=N[C@@H]1C[C@@H](C#N)N(C1)C(=O)CNC(=O)c1cccc2ccccc12	InChI=1S/C18H16N6O2/c19-9-14-8-13(22-23-20)11-24(14)17(25)10-21-18(26)16-7-3-5-12-4-1-2-6-15(12)16/h1-7,13-14H,8,10-11H2,(H,21,26)/t13-,14+/m1/s1	IPKHAZSRZNIQAI-KGLIPLIRSA-N	50382280	CHEMBL2022527	Prolyl endopeptidase FAP			>100000							ChEMBL	10.1016/j.bmcl.2012.03.107	10.7270/Q27D2W5P	22525314			Ryabtsova, O; Jansen, K; Van Goethem, S; Joossens, J; Cheng, JD; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp (UA)	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50382280	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50382280&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			70691904	160861363		CHEMBL2022527				ZINC84616478	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50931831	CC1C[C@@H](C#N)N(C1)C(=O)CNC(=O)c1ccccc1	InChI=1S/C15H17N3O2/c1-11-7-13(8-16)18(10-11)14(19)9-17-15(20)12-5-3-2-4-6-12/h2-6,11,13H,7,9-10H2,1H3,(H,17,20)/t11?,13-/m0/s1	QFUAZYZEIRCQSP-YUZLPWPTSA-N	50382284	CHEMBL2021934	Prolyl endopeptidase FAP			>100000							ChEMBL	10.1016/j.bmcl.2012.03.107	10.7270/Q27D2W5P	22525314			Ryabtsova, O; Jansen, K; Van Goethem, S; Joossens, J; Cheng, JD; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp (UA)	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50382284	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50382284&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			70693955	160861367		CHEMBL2021934				ZINC84616485	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50931832	O=C(CNC(=O)c1ccccc1)N1CCCC[C@H]1C#N	InChI=1S/C15H17N3O2/c16-10-13-8-4-5-9-18(13)14(19)11-17-15(20)12-6-2-1-3-7-12/h1-3,6-7,13H,4-5,8-9,11H2,(H,17,20)/t13-/m0/s1	OTFXIFLLRODAGY-ZDUSSCGKSA-N	50382259	CHEMBL2022534	Prolyl endopeptidase FAP			>100000							ChEMBL	10.1016/j.bmcl.2012.03.107	10.7270/Q27D2W5P	22525314			Ryabtsova, O; Jansen, K; Van Goethem, S; Joossens, J; Cheng, JD; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp (UA)	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50382259	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50382259&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			70689752	160861342		CHEMBL2022534				ZINC84604868	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50974965	O=C(OCc1ccccc1)N1CCC[C@H]1C(=O)N1CCCC1	InChI=1S/C17H22N2O3/c20-16(18-10-4-5-11-18)15-9-6-12-19(15)17(21)22-13-14-7-2-1-3-8-14/h1-3,7-8,15H,4-6,9-13H2/t15-/m0/s1	VJDNUCLKCQKXMM-HNNXBMFYSA-N	50316820	(S)-benzyl 2-(pyrrolidine-1-carbonyl)pyrrolidine-1-carboxylate::CHEMBL1088406	Prolyl endopeptidase FAP			>100000							ChEMBL	10.1021/jm301060g	10.7270/Q2SN0B3S	23121075			Van der Veken, P; Fulop, V; Rea, D; Gerard, M; Van Elzen, R; Joossens, J; Cheng, JD; Baekelandt, V; De Meester, I; Lambeir, AM; Augustyns, K	University of Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50316820	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50316820&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			688304	104151181		CHEMBL1088406				ZINC00057064	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50974963	[N-]=[N+]=N[C@H]1C[C@H](N(C1)C(=O)OCc1ccccc1)C(=O)N1CCCC1	InChI=1S/C17H21N5O3/c18-20-19-14-10-15(16(23)21-8-4-5-9-21)22(11-14)17(24)25-12-13-6-2-1-3-7-13/h1-3,6-7,14-15H,4-5,8-12H2/t14-,15-/m0/s1	CRXCLWPNSBSEQL-GJZGRUSLSA-N	50399744	CHEMBL2178977	Prolyl endopeptidase FAP			>100000							ChEMBL	10.1021/jm301060g	10.7270/Q2SN0B3S	23121075			Van der Veken, P; Fulop, V; Rea, D; Gerard, M; Van Elzen, R; Joossens, J; Cheng, JD; Baekelandt, V; De Meester, I; Lambeir, AM; Augustyns, K	University of Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50399744	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50399744&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			71459092	163348768		CHEMBL2178977				ZINC95578181	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50974964	O=C(CCCc1ccccc1)N1CCC[C@H]1C(=O)N1CCCC1	InChI=1S/C19H26N2O2/c22-18(12-6-10-16-8-2-1-3-9-16)21-15-7-11-17(21)19(23)20-13-4-5-14-20/h1-3,8-9,17H,4-7,10-15H2/t17-/m0/s1	HDRSLHFTJYMQIL-KRWDZBQOSA-N	50051539	(S)-4-phenyl-1-(2-(pyrrolidine-1-carbonyl)pyrrolidin-1-yl)butan-1-one::4-Phenyl-1-[(S)-2-(pyrrolidine-1-carbonyl)-pyrrolidin-1-yl]-butan-1-one::4-Phenyl-1-[2-(pyrrolidine-1-carbonyl)-pyrrolidin-1-yl]-butan-1-one::CHEMBL289651::SUAM-1221	Prolyl endopeptidase FAP			>100000							ChEMBL	10.1021/jm301060g	10.7270/Q2SN0B3S	23121075			Van der Veken, P; Fulop, V; Rea, D; Gerard, M; Van Elzen, R; Joossens, J; Cheng, JD; Baekelandt, V; De Meester, I; Lambeir, AM; Augustyns, K	University of Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50051539	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50051539&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			3081017	103948537		CHEMBL289651				ZINC13491619	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50974941	CC(C)(C)OC(=O)NCc1cn(nn1)[C@H]1C[C@H](N(C1)C(=O)CCCc1ccccc1)C(=O)N1CCC[C@H]1C#N	InChI=1S/C28H37N7O4/c1-28(2,3)39-27(38)30-17-21-18-35(32-31-21)23-15-24(26(37)33-14-8-12-22(33)16-29)34(19-23)25(36)13-7-11-20-9-5-4-6-10-20/h4-6,9-10,18,22-24H,7-8,11-15,17,19H2,1-3H3,(H,30,38)/t22-,23-,24-/m0/s1	HMJOYYGIKBZMGB-HJOGWXRNSA-N	50399717	CHEMBL2178959	Prolyl endopeptidase FAP			>100000							ChEMBL	10.1021/jm301060g	10.7270/Q2SN0B3S	23121075			Van der Veken, P; Fulop, V; Rea, D; Gerard, M; Van Elzen, R; Joossens, J; Cheng, JD; Baekelandt, V; De Meester, I; Lambeir, AM; Augustyns, K	University of Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50399717	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50399717&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			71457236	163348741		CHEMBL2178959				ZINC95576383	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50974942	[N-]=[N+]=N[C@H]1C[C@H](N(C1)C(=O)CCCc1ccccc1)C(=O)N1CCC[C@H]1C#N	InChI=1S/C20H24N6O2/c21-13-17-9-5-11-25(17)20(28)18-12-16(23-24-22)14-26(18)19(27)10-4-8-15-6-2-1-3-7-15/h1-3,6-7,16-18H,4-5,8-12,14H2/t16-,17-,18-/m0/s1	BDHAYCWUCJOADB-BZSNNMDCSA-N	50399718	CHEMBL2178958	Prolyl endopeptidase FAP			>100000							ChEMBL	10.1021/jm301060g	10.7270/Q2SN0B3S	23121075			Van der Veken, P; Fulop, V; Rea, D; Gerard, M; Van Elzen, R; Joossens, J; Cheng, JD; Baekelandt, V; De Meester, I; Lambeir, AM; Augustyns, K	University of Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50399718	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50399718&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			71462596	163348742		CHEMBL2178958				ZINC95575730	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50974943	O=C(CCCc1ccccc1)N1CCC[C@H]1C(=O)N1CCC[C@H]1C#N	InChI=1S/C20H25N3O2/c21-15-17-10-5-13-22(17)20(25)18-11-6-14-23(18)19(24)12-4-9-16-7-2-1-3-8-16/h1-3,7-8,17-18H,4-6,9-14H2/t17-,18-/m0/s1	SPXFAUXQZWJGCJ-ROUUACIJSA-N	50155838	(S)-1-((S)-1-(4-phenylbutanoyl)pyrrolidine-2-carbonyl)pyrrolidine-2-carbonitrile::(S)-1-[(S)-1-(4-Phenyl-butyryl)-pyrrolidine-2-carbonyl]-pyrrolidine-2-carbonitrile::CHEMBL189620	Prolyl endopeptidase FAP			>10000							ChEMBL	10.1021/jm301060g	10.7270/Q2SN0B3S	23121075			Van der Veken, P; Fulop, V; Rea, D; Gerard, M; Van Elzen, R; Joossens, J; Cheng, JD; Baekelandt, V; De Meester, I; Lambeir, AM; Augustyns, K	University of Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50155838	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50155838&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	2P6	4AN0	11198569	104043205		CHEMBL189620				ZINC13584669	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50974944	CC(C)(C)OC(=O)NCc1cn(nn1)[C@@H]1C[C@H](N(C1)C(=O)CCCc1ccccc1)C(=O)N1CCCC1	InChI=1S/C27H38N6O4/c1-27(2,3)37-26(36)28-17-21-18-33(30-29-21)22-16-23(25(35)31-14-7-8-15-31)32(19-22)24(34)13-9-12-20-10-5-4-6-11-20/h4-6,10-11,18,22-23H,7-9,12-17,19H2,1-3H3,(H,28,36)/t22-,23+/m1/s1	XZWNABGHXTWXJY-PKTZIBPZSA-N	50399719	CHEMBL2178957	Prolyl endopeptidase FAP			>100000							ChEMBL	10.1021/jm301060g	10.7270/Q2SN0B3S	23121075			Van der Veken, P; Fulop, V; Rea, D; Gerard, M; Van Elzen, R; Joossens, J; Cheng, JD; Baekelandt, V; De Meester, I; Lambeir, AM; Augustyns, K	University of Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50399719	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50399719&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			71460901	163348743		CHEMBL2178957				ZINC95576277	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50974945	[N-]=[N+]=N[C@@H]1C[C@H](N(C1)C(=O)CCCc1ccccc1)C(=O)N1CCCC1	InChI=1S/C19H25N5O2/c20-22-21-16-13-17(19(26)23-11-4-5-12-23)24(14-16)18(25)10-6-9-15-7-2-1-3-8-15/h1-3,7-8,16-17H,4-6,9-14H2/t16-,17+/m1/s1	COFDNGGDLKZPRK-SJORKVTESA-N	50399721	CHEMBL2178955	Prolyl endopeptidase FAP			>100000							ChEMBL	10.1021/jm301060g	10.7270/Q2SN0B3S	23121075			Van der Veken, P; Fulop, V; Rea, D; Gerard, M; Van Elzen, R; Joossens, J; Cheng, JD; Baekelandt, V; De Meester, I; Lambeir, AM; Augustyns, K	University of Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50399721	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50399721&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			71450086	163348745		CHEMBL2178955				ZINC95575795	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50974946	O=C(CCCc1ccccc1)N1C[C@H](C[C@H]1C(=O)N1CCCC1)n1cc(CN2CCNCC2)nn1	InChI=1S/C26H37N7O2/c34-25(10-6-9-21-7-2-1-3-8-21)32-20-23(17-24(32)26(35)31-13-4-5-14-31)33-19-22(28-29-33)18-30-15-11-27-12-16-30/h1-3,7-8,19,23-24,27H,4-6,9-18,20H2/t23-,24-/m0/s1	ZSJCNAYNTHHHOM-ZEQRLZLVSA-N	50399722	CHEMBL2178975	Prolyl endopeptidase FAP			>100000							ChEMBL	10.1021/jm301060g	10.7270/Q2SN0B3S	23121075			Van der Veken, P; Fulop, V; Rea, D; Gerard, M; Van Elzen, R; Joossens, J; Cheng, JD; Baekelandt, V; De Meester, I; Lambeir, AM; Augustyns, K	University of Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50399722	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50399722&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			71453723	163348746		CHEMBL2178975				ZINC95579227	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50974947	CC(C)(C)OC(=O)N1CCN(Cc2cn(nn2)[C@H]2C[C@H](N(C2)C(=O)CCCc2ccccc2)C(=O)N2CCCC2)CC1	InChI=1S/C31H45N7O4/c1-31(2,3)42-30(41)36-18-16-34(17-19-36)21-25-22-38(33-32-25)26-20-27(29(40)35-14-7-8-15-35)37(23-26)28(39)13-9-12-24-10-5-4-6-11-24/h4-6,10-11,22,26-27H,7-9,12-21,23H2,1-3H3/t26-,27-/m0/s1	LPMUXXBRNGPFML-SVBPBHIXSA-N	50399723	CHEMBL2178974	Prolyl endopeptidase FAP			>100000							ChEMBL	10.1021/jm301060g	10.7270/Q2SN0B3S	23121075			Van der Veken, P; Fulop, V; Rea, D; Gerard, M; Van Elzen, R; Joossens, J; Cheng, JD; Baekelandt, V; De Meester, I; Lambeir, AM; Augustyns, K	University of Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50399723	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50399723&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			71451902	163348747		CHEMBL2178974				ZINC95575845	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50974948	O=C(CCCc1ccccc1)N1C[C@H](C[C@H]1C(=O)N1CCCC1)n1cc(CN2CCOCC2)nn1	InChI=1S/C26H36N6O3/c33-25(10-6-9-21-7-2-1-3-8-21)31-20-23(17-24(31)26(34)30-11-4-5-12-30)32-19-22(27-28-32)18-29-13-15-35-16-14-29/h1-3,7-8,19,23-24H,4-6,9-18,20H2/t23-,24-/m0/s1	FHDVBADBEQSCNW-ZEQRLZLVSA-N	50399724	CHEMBL2178973	Prolyl endopeptidase FAP			>100000							ChEMBL	10.1021/jm301060g	10.7270/Q2SN0B3S	23121075			Van der Veken, P; Fulop, V; Rea, D; Gerard, M; Van Elzen, R; Joossens, J; Cheng, JD; Baekelandt, V; De Meester, I; Lambeir, AM; Augustyns, K	University of Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50399724	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50399724&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			71457240	163348748		CHEMBL2178973				ZINC95579697	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50974949	NCc1cn(nn1)[C@H]1C[C@H](N(C1)C(=O)CCCc1ccccc1)C(=O)N1CCCC1	InChI=1S/C22H30N6O2/c23-14-18-15-28(25-24-18)19-13-20(22(30)26-11-4-5-12-26)27(16-19)21(29)10-6-9-17-7-2-1-3-8-17/h1-3,7-8,15,19-20H,4-6,9-14,16,23H2/t19-,20-/m0/s1	SLJFWBKCONXRCQ-PMACEKPBSA-N	50399726	CHEMBL2178971	Prolyl endopeptidase FAP			>100000							ChEMBL	10.1021/jm301060g	10.7270/Q2SN0B3S	23121075			Van der Veken, P; Fulop, V; Rea, D; Gerard, M; Van Elzen, R; Joossens, J; Cheng, JD; Baekelandt, V; De Meester, I; Lambeir, AM; Augustyns, K	University of Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50399726	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50399726&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			71450089	163348750		CHEMBL2178971				ZINC95566047	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50974950	O=C(CCCc1ccccc1)N1C[C@H](C[C@H]1C(=O)N1CCCC1)n1cc(nn1)-c1ccccn1	InChI=1S/C26H30N6O2/c33-25(13-8-11-20-9-2-1-3-10-20)31-18-21(17-24(31)26(34)30-15-6-7-16-30)32-19-23(28-29-32)22-12-4-5-14-27-22/h1-5,9-10,12,14,19,21,24H,6-8,11,13,15-18H2/t21-,24-/m0/s1	OMBBTNGSWHFDOL-URXFXBBRSA-N	50399728	CHEMBL2178969	Prolyl endopeptidase FAP			>100000							ChEMBL	10.1021/jm301060g	10.7270/Q2SN0B3S	23121075			Van der Veken, P; Fulop, V; Rea, D; Gerard, M; Van Elzen, R; Joossens, J; Cheng, JD; Baekelandt, V; De Meester, I; Lambeir, AM; Augustyns, K	University of Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50399728	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50399728&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			71459091	163348752		CHEMBL2178969				ZINC95578716	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50974951	O=C(OCc1ccccc1)N1C[C@H](C[C@H]1C(=O)N1CCCC1)n1cc(nn1)-c1ccccn1	InChI=1S/C24H26N6O3/c31-23(28-12-6-7-13-28)22-14-19(30-16-21(26-27-30)20-10-4-5-11-25-20)15-29(22)24(32)33-17-18-8-2-1-3-9-18/h1-5,8-11,16,19,22H,6-7,12-15,17H2/t19-,22-/m0/s1	YDHVNENQKDYTSG-UGKGYDQZSA-N	50399729	CHEMBL2178968	Prolyl endopeptidase FAP			>100000							ChEMBL	10.1021/jm301060g	10.7270/Q2SN0B3S	23121075			Van der Veken, P; Fulop, V; Rea, D; Gerard, M; Van Elzen, R; Joossens, J; Cheng, JD; Baekelandt, V; De Meester, I; Lambeir, AM; Augustyns, K	University of Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50399729	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50399729&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			71460903	163348753		CHEMBL2178968				ZINC95575094	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50974952	Brc1ccc(cc1)-c1cn(nn1)[C@H]1C[C@H](N(C1)C(=O)CCCc1ccccc1)C(=O)N1CCCC1	InChI=1S/C27H30BrN5O2/c28-22-13-11-21(12-14-22)24-19-33(30-29-24)23-17-25(27(35)31-15-4-5-16-31)32(18-23)26(34)10-6-9-20-7-2-1-3-8-20/h1-3,7-8,11-14,19,23,25H,4-6,9-10,15-18H2/t23-,25-/m0/s1	REMTXTLDXIZVKS-ZCYQVOJMSA-N	50399730	CHEMBL2178967	Prolyl endopeptidase FAP			>100000							ChEMBL	10.1021/jm301060g	10.7270/Q2SN0B3S	23121075			Van der Veken, P; Fulop, V; Rea, D; Gerard, M; Van Elzen, R; Joossens, J; Cheng, JD; Baekelandt, V; De Meester, I; Lambeir, AM; Augustyns, K	University of Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50399730	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50399730&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			71457238	163348754		CHEMBL2178967				ZINC95571613	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50974953	Clc1ccccc1-c1cn(nn1)[C@H]1C[C@H](N(C1)C(=O)CCCc1ccccc1)C(=O)N1CCCC1	InChI=1S/C27H30ClN5O2/c28-23-13-5-4-12-22(23)24-19-33(30-29-24)21-17-25(27(35)31-15-6-7-16-31)32(18-21)26(34)14-8-11-20-9-2-1-3-10-20/h1-5,9-10,12-13,19,21,25H,6-8,11,14-18H2/t21-,25-/m0/s1	NGVSKMRZCNELBT-OFVILXPXSA-N	50399731	CHEMBL2178966	Prolyl endopeptidase FAP			>5000							ChEMBL	10.1021/jm301060g	10.7270/Q2SN0B3S	23121075			Van der Veken, P; Fulop, V; Rea, D; Gerard, M; Van Elzen, R; Joossens, J; Cheng, JD; Baekelandt, V; De Meester, I; Lambeir, AM; Augustyns, K	University of Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50399731	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50399731&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			71459090	163348755		CHEMBL2178966				ZINC95573454	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50974954	Fc1ccc(cc1F)-c1cn(nn1)[C@H]1C[C@H](N(C1)C(=O)CCCc1ccccc1)C(=O)N1CCCC1	InChI=1S/C27H29F2N5O2/c28-22-12-11-20(15-23(22)29)24-18-34(31-30-24)21-16-25(27(36)32-13-4-5-14-32)33(17-21)26(35)10-6-9-19-7-2-1-3-8-19/h1-3,7-8,11-12,15,18,21,25H,4-6,9-10,13-14,16-17H2/t21-,25-/m0/s1	DEQVLBIWXHYBPS-OFVILXPXSA-N	50399732	CHEMBL2178965	Prolyl endopeptidase FAP			>5000							ChEMBL	10.1021/jm301060g	10.7270/Q2SN0B3S	23121075			Van der Veken, P; Fulop, V; Rea, D; Gerard, M; Van Elzen, R; Joossens, J; Cheng, JD; Baekelandt, V; De Meester, I; Lambeir, AM; Augustyns, K	University of Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50399732	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50399732&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			71460902	163348756		CHEMBL2178965				ZINC95579923	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50974955	Fc1ccc(-c2cn(nn2)[C@H]2C[C@H](N(C2)C(=O)CCCc2ccccc2)C(=O)N2CCCC2)c(F)c1	InChI=1S/C27H29F2N5O2/c28-20-11-12-22(23(29)15-20)24-18-34(31-30-24)21-16-25(27(36)32-13-4-5-14-32)33(17-21)26(35)10-6-9-19-7-2-1-3-8-19/h1-3,7-8,11-12,15,18,21,25H,4-6,9-10,13-14,16-17H2/t21-,25-/m0/s1	GXPGTUGZWGADDE-OFVILXPXSA-N	50399733	CHEMBL2178964	Prolyl endopeptidase FAP			>5000							ChEMBL	10.1021/jm301060g	10.7270/Q2SN0B3S	23121075			Van der Veken, P; Fulop, V; Rea, D; Gerard, M; Van Elzen, R; Joossens, J; Cheng, JD; Baekelandt, V; De Meester, I; Lambeir, AM; Augustyns, K	University of Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50399733	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50399733&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			71451901	163348757		CHEMBL2178964				ZINC95575714	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50974956	CC(C)(C)OC(=O)NCc1cn(nn1)[C@H]1C[C@H](N(C1)C(=O)CCCc1ccccc1)C(=O)N1CCCC1	InChI=1S/C27H38N6O4/c1-27(2,3)37-26(36)28-17-21-18-33(30-29-21)22-16-23(25(35)31-14-7-8-15-31)32(19-22)24(34)13-9-12-20-10-5-4-6-11-20/h4-6,10-11,18,22-23H,7-9,12-17,19H2,1-3H3,(H,28,36)/t22-,23-/m0/s1	XZWNABGHXTWXJY-GOTSBHOMSA-N	50399737	CHEMBL2178960	Prolyl endopeptidase FAP			>100000							ChEMBL	10.1021/jm301060g	10.7270/Q2SN0B3S	23121075			Van der Veken, P; Fulop, V; Rea, D; Gerard, M; Van Elzen, R; Joossens, J; Cheng, JD; Baekelandt, V; De Meester, I; Lambeir, AM; Augustyns, K	University of Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50399737	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50399737&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			71457237	163348761		CHEMBL2178960				ZINC95573868	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50974957	CC(C)(C)OC(=O)NCc1cn(nn1)[C@H]1C[C@H](N(C1)C(=O)OCc1ccccc1)C(=O)N1CCCC1	InChI=1S/C25H34N6O5/c1-25(2,3)36-23(33)26-14-19-15-31(28-27-19)20-13-21(22(32)29-11-7-8-12-29)30(16-20)24(34)35-17-18-9-5-4-6-10-18/h4-6,9-10,15,20-21H,7-8,11-14,16-17H2,1-3H3,(H,26,33)/t20-,21-/m0/s1	LWHMUBUYHQTDMK-SFTDATJTSA-N	50399738	CHEMBL2179408	Prolyl endopeptidase FAP			>100000							ChEMBL	10.1021/jm301060g	10.7270/Q2SN0B3S	23121075			Van der Veken, P; Fulop, V; Rea, D; Gerard, M; Van Elzen, R; Joossens, J; Cheng, JD; Baekelandt, V; De Meester, I; Lambeir, AM; Augustyns, K	University of Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50399738	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50399738&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			71455494	163348762		CHEMBL2179408				ZINC95576274	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50974958	O=C(CCCc1ccccc1)N1C[C@H](C[C@H]1C(=O)N1CCCC1)n1cc(nn1)C1CCCCC1	InChI=1S/C27H37N5O2/c33-26(15-9-12-21-10-3-1-4-11-21)31-19-23(18-25(31)27(34)30-16-7-8-17-30)32-20-24(28-29-32)22-13-5-2-6-14-22/h1,3-4,10-11,20,22-23,25H,2,5-9,12-19H2/t23-,25-/m0/s1	RBLIZQQDPZHRGB-ZCYQVOJMSA-N	50399739	CHEMBL2179407	Prolyl endopeptidase FAP			>5000							ChEMBL	10.1021/jm301060g	10.7270/Q2SN0B3S	23121075			Van der Veken, P; Fulop, V; Rea, D; Gerard, M; Van Elzen, R; Joossens, J; Cheng, JD; Baekelandt, V; De Meester, I; Lambeir, AM; Augustyns, K	University of Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50399739	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50399739&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			71453762	163348763		CHEMBL2179407				ZINC95571699	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50974959	O=C(CCCc1ccccc1)N1C[C@H](C[C@H]1C(=O)N1CCCC1)n1cc(nn1)C1CC1	InChI=1S/C24H31N5O2/c30-23(10-6-9-18-7-2-1-3-8-18)28-16-20(29-17-21(25-26-29)19-11-12-19)15-22(28)24(31)27-13-4-5-14-27/h1-3,7-8,17,19-20,22H,4-6,9-16H2/t20-,22-/m0/s1	VBMSSHPBPUWMQA-UNMCSNQZSA-N	50399740	CHEMBL2179406	Prolyl endopeptidase FAP			>100000							ChEMBL	10.1021/jm301060g	10.7270/Q2SN0B3S	23121075			Van der Veken, P; Fulop, V; Rea, D; Gerard, M; Van Elzen, R; Joossens, J; Cheng, JD; Baekelandt, V; De Meester, I; Lambeir, AM; Augustyns, K	University of Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50399740	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50399740&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			71451939	163348764		CHEMBL2179406				ZINC95575642	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50974960	C[Si](C)(C)c1cn(nn1)[C@H]1C[C@H](N(C1)C(=O)OCc1ccccc1)C(=O)N1CCCC1	InChI=1S/C22H31N5O3Si/c1-31(2,3)20-15-27(24-23-20)18-13-19(21(28)25-11-7-8-12-25)26(14-18)22(29)30-16-17-9-5-4-6-10-17/h4-6,9-10,15,18-19H,7-8,11-14,16H2,1-3H3/t18-,19-/m0/s1	AMUXFUKEWVWFMP-OALUTQOASA-N	50399741	CHEMBL2179405	Prolyl endopeptidase FAP			>100000							ChEMBL	10.1021/jm301060g	10.7270/Q2SN0B3S	23121075			Van der Veken, P; Fulop, V; Rea, D; Gerard, M; Van Elzen, R; Joossens, J; Cheng, JD; Baekelandt, V; De Meester, I; Lambeir, AM; Augustyns, K	University of Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50399741	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50399741&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			71462641	163348765		CHEMBL2179405					1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50974961	O=C(OCc1ccccc1)N1C[C@H](C[C@H]1C(=O)N1CCCC1)n1ccnn1	InChI=1S/C19H23N5O3/c25-18(22-9-4-5-10-22)17-12-16(24-11-8-20-21-24)13-23(17)19(26)27-14-15-6-2-1-3-7-15/h1-3,6-8,11,16-17H,4-5,9-10,12-14H2/t16-,17-/m0/s1	OLDLWKNPJIIOPY-IRXDYDNUSA-N	50399742	CHEMBL2178979	Prolyl endopeptidase FAP			>100000							ChEMBL	10.1021/jm301060g	10.7270/Q2SN0B3S	23121075			Van der Veken, P; Fulop, V; Rea, D; Gerard, M; Van Elzen, R; Joossens, J; Cheng, JD; Baekelandt, V; De Meester, I; Lambeir, AM; Augustyns, K	University of Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50399742	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50399742&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			71460904	163348766		CHEMBL2178979				ZINC95573302	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
50974962	[N-]=[N+]=N[C@H]1C[C@H](N(C1)C(=O)CCCc1ccccc1)C(=O)N1CCCC1	InChI=1S/C19H25N5O2/c20-22-21-16-13-17(19(26)23-11-4-5-12-23)24(14-16)18(25)10-6-9-15-7-2-1-3-8-15/h1-3,7-8,16-17H,4-6,9-14H2/t16-,17-/m0/s1	COFDNGGDLKZPRK-IRXDYDNUSA-N	50399743	CHEMBL2178978	Prolyl endopeptidase FAP			>100000							ChEMBL	10.1021/jm301060g	10.7270/Q2SN0B3S	23121075			Van der Veken, P; Fulop, V; Rea, D; Gerard, M; Van Elzen, R; Joossens, J; Cheng, JD; Baekelandt, V; De Meester, I; Lambeir, AM; Augustyns, K	University of Antwerp	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50399743	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50399743&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			71455458	163348767		CHEMBL2178978				ZINC95575258	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
51063916	O=C(COc1ccc2ccccc2c1)NCC(=O)N1CCC[C@H]1C#N	InChI=1S/C19H19N3O3/c20-11-16-6-3-9-22(16)19(24)12-21-18(23)13-25-17-8-7-14-4-1-2-5-15(14)10-17/h1-2,4-5,7-8,10,16H,3,6,9,12-13H2,(H,21,23)/t16-/m0/s1	GLMWHSHSMVDUQV-INIZCTEOSA-N	50434185	CHEMBL2385284	Prolyl endopeptidase FAP			 14000							ChEMBL	10.1021/ml300410d	10.7270/Q2KP83J7	24900696			Jansen, K; Heirbaut, L; Cheng, JD; Joossens, J; Ryabtsova, O; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp (UA)	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50434185	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50434185&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			73350449	175446502		CHEMBL2385284				ZINC96270295	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
51063917	O=C(CNC(=O)c1cc2ccccc2[nH]1)N1CCC[C@H]1C#N	InChI=1S/C16H16N4O2/c17-9-12-5-3-7-20(12)15(21)10-18-16(22)14-8-11-4-1-2-6-13(11)19-14/h1-2,4,6,8,12,19H,3,5,7,10H2,(H,18,22)/t12-/m0/s1	DLKKIDNRLYBRGP-LBPRGKRZSA-N	50434186	CHEMBL2385283	Prolyl endopeptidase FAP			 15400							ChEMBL	10.1021/ml300410d	10.7270/Q2KP83J7	24900696			Jansen, K; Heirbaut, L; Cheng, JD; Joossens, J; Ryabtsova, O; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp (UA)	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50434186	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50434186&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			73350448	175446503		CHEMBL2385283				ZINC96270296	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
51063918	O=C(CNC(=O)c1c[nH]c2ccccc12)N1CCC[C@H]1C#N	InChI=1S/C16H16N4O2/c17-8-11-4-3-7-20(11)15(21)10-19-16(22)13-9-18-14-6-2-1-5-12(13)14/h1-2,5-6,9,11,18H,3-4,7,10H2,(H,19,22)/t11-/m0/s1	JUEILIJRHXPVKI-NSHDSACASA-N	50434187	CHEMBL2385282	Prolyl endopeptidase FAP			 3600							ChEMBL	10.1021/ml300410d	10.7270/Q2KP83J7	24900696			Jansen, K; Heirbaut, L; Cheng, JD; Joossens, J; Ryabtsova, O; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp (UA)	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50434187	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50434187&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			71655555	175446504		CHEMBL2385282				ZINC96270297	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
51063919	O=C(CNC(=O)c1ccnc2ccccc12)N1CCC[C@H]1C#N	InChI=1S/C17H16N4O2/c18-10-12-4-3-9-21(12)16(22)11-20-17(23)14-7-8-19-15-6-2-1-5-13(14)15/h1-2,5-8,12H,3-4,9,11H2,(H,20,23)/t12-/m0/s1	MTHMMXFBHKGAAI-LBPRGKRZSA-N	50434188	CHEMBL2385281::US9346814, Cmpd No 2 Example 3	Prolyl endopeptidase FAP		 3.0								ChEMBL	10.1021/ml300410d	10.7270/Q2KP83J7	24900696			Jansen, K; Heirbaut, L; Cheng, JD; Joossens, J; Ryabtsova, O; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp (UA)	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50434188	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50434188&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			71655554	175446505		CHEMBL2385281				ZINC96270298	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
51063920	O=C(CNC(=O)c1ccnc2ccccc12)N1CCC[C@H]1C#N	InChI=1S/C17H16N4O2/c18-10-12-4-3-9-21(12)16(22)11-20-17(23)14-7-8-19-15-6-2-1-5-13(14)15/h1-2,5-8,12H,3-4,9,11H2,(H,20,23)/t12-/m0/s1	MTHMMXFBHKGAAI-LBPRGKRZSA-N	50434188	CHEMBL2385281::US9346814, Cmpd No 2 Example 3	Prolyl endopeptidase FAP			 10							ChEMBL	10.1021/ml300410d	10.7270/Q2KP83J7	24900696			Jansen, K; Heirbaut, L; Cheng, JD; Joossens, J; Ryabtsova, O; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp (UA)	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50434188	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50434188&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			71655554	175446505		CHEMBL2385281				ZINC96270298	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
51063921	CC#CCn1c(nc2n(C)c(=O)n(Cc3nc(C)c4ccccc4n3)c(=O)c12)N1CCC[C@@H](N)C1	InChI=1S/C25H28N8O2/c1-4-5-13-32-21-22(29-24(32)31-12-8-9-17(26)14-31)30(3)25(35)33(23(21)34)15-20-27-16(2)18-10-6-7-11-19(18)28-20/h6-7,10-11,17H,8-9,12-15,26H2,1-3H3/t17-/m1/s1	LTXREWYXXSTFRX-QGZVFWFLSA-N	50228403	(R)-8-(3-aminopiperidin-1-yl)-7-(but-2-ynyl)-3-methyl-1-((4-methylquinazolin-2-yl)methyl)-1H-purine-2,6(3H,7H)-dione::8-[(3R)-3-Aminopiperidin-1-yl]-7-but-2-yn-1-yl-3-methyl-1-[(4-methylquinazolin-2-yl)methyl]-3,7-dihydro-1H-purine-2,6-dione::CHEMBL237500::LINAGLIPTIN::US10202383, Example 2(142)::US10358449, Linagliptin::US9255098, Linagliptin::US9321791, 2(142)::US9556175, 2(142)	Prolyl endopeptidase FAP			 370							ChEMBL	10.1021/ml300410d	10.7270/Q2KP83J7	24900696			Jansen, K; Heirbaut, L; Cheng, JD; Joossens, J; Ryabtsova, O; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp (UA)	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50228403	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50228403&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	356	2RGU,6Y0F	10096344	104097872	68610	CHEMBL237500	DB08882	6318		ZINC03820029	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
51063922	CC(C)[C@H](N)C(=O)N1CCC[C@H]1B(O)O	InChI=1S/C9H19BN2O3/c1-6(2)8(11)9(13)12-5-3-4-7(12)10(14)15/h6-8,14-15H,3-5,11H2,1-2H3/t7-,8-/m0/s1	FKCMADOPPWWGNZ-YUMQZZPRSA-N	50050513	(R)-1-((S)-2-amino-3-methylbutanoyl)pyrrolidin-2-ylboronic acid::(S)-2-Amino-1-((R)-2-dihydroxyboron-pyrrolidin-1-yl)-3-methyl-butan-1-one::(S)-2-Amino-3-methyl-2-boronic acid-1-pyrrolidin-1-yl-butan-1-one::Boronic acid derivative::CHEMBL67279::Ketopyrrolidine derivative::Pyrrolidine derivative::US11096924, DASH-inhibitors 2504 C::US11504364, Compound Val-boroPro::US11559537, Compound 2054-Val-boro-Pro	Prolyl endopeptidase FAP			 70							ChEMBL	10.1021/ml300410d	10.7270/Q2KP83J7	24900696			Jansen, K; Heirbaut, L; Cheng, JD; Joossens, J; Ryabtsova, O; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp (UA)	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50050513	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50050513&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			6918572	103947674		CHEMBL67279					1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
51063923	O=C(CNC(=O)c1cccc2cccnc12)N1CCC[C@H]1C#N	InChI=1S/C17H16N4O2/c18-10-13-6-3-9-21(13)15(22)11-20-17(23)14-7-1-4-12-5-2-8-19-16(12)14/h1-2,4-5,7-8,13H,3,6,9,11H2,(H,20,23)/t13-/m0/s1	DTZGFBWXCPGCKM-ZDUSSCGKSA-N	50434189	CHEMBL2385280::US9346814, Ref. Cmpd No 6 (Example 7)	Prolyl endopeptidase FAP			 2170							ChEMBL	10.1021/ml300410d	10.7270/Q2KP83J7	24900696			Jansen, K; Heirbaut, L; Cheng, JD; Joossens, J; Ryabtsova, O; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp (UA)	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50434189	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50434189&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			71667227	175446506		CHEMBL2385280				ZINC96270299	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
51063924	O=C(CNC(=O)c1cccc2ccncc12)N1CCC[C@H]1C#N	InChI=1S/C17H16N4O2/c18-9-13-4-2-8-21(13)16(22)11-20-17(23)14-5-1-3-12-6-7-19-10-15(12)14/h1,3,5-7,10,13H,2,4,8,11H2,(H,20,23)/t13-/m0/s1	HADDFSYWKHROFL-ZDUSSCGKSA-N	50434190	CHEMBL2385279	Prolyl endopeptidase FAP			 158							ChEMBL	10.1021/ml300410d	10.7270/Q2KP83J7	24900696			Jansen, K; Heirbaut, L; Cheng, JD; Joossens, J; Ryabtsova, O; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp (UA)	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50434190	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50434190&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			71655627	175446507		CHEMBL2385279				ZINC96270300	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
51063925	O=C(CNC(=O)c1cccc2cnccc12)N1CCC[C@H]1C#N	InChI=1S/C17H16N4O2/c18-9-13-4-2-8-21(13)16(22)11-20-17(23)15-5-1-3-12-10-19-7-6-14(12)15/h1,3,5-7,10,13H,2,4,8,11H2,(H,20,23)/t13-/m0/s1	DSIXHJMXKMIOFX-ZDUSSCGKSA-N	50434191	CHEMBL2385278	Prolyl endopeptidase FAP			 107							ChEMBL	10.1021/ml300410d	10.7270/Q2KP83J7	24900696			Jansen, K; Heirbaut, L; Cheng, JD; Joossens, J; Ryabtsova, O; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp (UA)	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50434191	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50434191&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			71655626	175446508		CHEMBL2385278				ZINC96270301	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
51063926	O=C(CNC(=O)c1cccc2ncccc12)N1CCC[C@H]1C#N	InChI=1S/C17H16N4O2/c18-10-12-4-3-9-21(12)16(22)11-20-17(23)14-5-1-7-15-13(14)6-2-8-19-15/h1-2,5-8,12H,3-4,9,11H2,(H,20,23)/t12-/m0/s1	XSKKWTLPSOKUFE-LBPRGKRZSA-N	50434159	CHEMBL2385277::US9346814, Ref Cmpd No 7 (example 17)	Prolyl endopeptidase FAP			 420							ChEMBL	10.1021/ml300410d	10.7270/Q2KP83J7	24900696			Jansen, K; Heirbaut, L; Cheng, JD; Joossens, J; Ryabtsova, O; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp (UA)	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50434159	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50434159&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			71655625	175446476		CHEMBL2385277				ZINC96270269	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
51063927	O=C(CNC(=O)c1cncc2ccccc12)N1CCC[C@H]1C#N	InChI=1S/C17H16N4O2/c18-8-13-5-3-7-21(13)16(22)11-20-17(23)15-10-19-9-12-4-1-2-6-14(12)15/h1-2,4,6,9-10,13H,3,5,7,11H2,(H,20,23)/t13-/m0/s1	YNGPRBCXHBASGU-ZDUSSCGKSA-N	50434160	CHEMBL2385276	Prolyl endopeptidase FAP			 4800							ChEMBL	10.1021/ml300410d	10.7270/Q2KP83J7	24900696			Jansen, K; Heirbaut, L; Cheng, JD; Joossens, J; Ryabtsova, O; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp (UA)	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50434160	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50434160&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			71655624	175446477		CHEMBL2385276				ZINC96270270	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
51063928	Brc1cccc2c(ccnc12)C(=O)NCC(=O)N1CCC[C@H]1C#N	InChI=1S/C17H15BrN4O2/c18-14-5-1-4-12-13(6-7-20-16(12)14)17(24)21-10-15(23)22-8-2-3-11(22)9-19/h1,4-7,11H,2-3,8,10H2,(H,21,24)/t11-/m0/s1	KEZAZIKPPLGXGR-NSHDSACASA-N	50434161	CHEMBL2385275::US9346814, Cmpd No 10 Example 13	Prolyl endopeptidase FAP			 370							ChEMBL	10.1021/ml300410d	10.7270/Q2KP83J7	24900696			Jansen, K; Heirbaut, L; Cheng, JD; Joossens, J; Ryabtsova, O; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp (UA)	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50434161	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50434161&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			71667376	175446478		CHEMBL2385275				ZINC96270271	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
51063929	Clc1cccc2c(ccnc12)C(=O)NCC(=O)N1CCC[C@H]1C#N	InChI=1S/C17H15ClN4O2/c18-14-5-1-4-12-13(6-7-20-16(12)14)17(24)21-10-15(23)22-8-2-3-11(22)9-19/h1,4-7,11H,2-3,8,10H2,(H,21,24)/t11-/m0/s1	GVEVKFYZSMHFEB-NSHDSACASA-N	50434162	CHEMBL2385274::US9346814, Cmpd No 9 Example 12	Prolyl endopeptidase FAP			 190							ChEMBL	10.1021/ml300410d	10.7270/Q2KP83J7	24900696			Jansen, K; Heirbaut, L; Cheng, JD; Joossens, J; Ryabtsova, O; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp (UA)	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50434162	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50434162&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			71667375	175446479		CHEMBL2385274				ZINC96270272	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
51063930	Brc1ccc2c(ccnc2c1)C(=O)NCC(=O)N1CCC[C@H]1C#N	InChI=1S/C17H15BrN4O2/c18-11-3-4-13-14(5-6-20-15(13)8-11)17(24)21-10-16(23)22-7-1-2-12(22)9-19/h3-6,8,12H,1-2,7,10H2,(H,21,24)/t12-/m0/s1	INQYLMGAPQGWDT-LBPRGKRZSA-N	50434163	CHEMBL2385273::US9346814, Cmpd No 12 Example 15	Prolyl endopeptidase FAP			 6.2							ChEMBL	10.1021/ml300410d	10.7270/Q2KP83J7	24900696			Jansen, K; Heirbaut, L; Cheng, JD; Joossens, J; Ryabtsova, O; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp (UA)	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50434163	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50434163&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			71667378	175446480		CHEMBL2385273				ZINC96270273	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
51063931	Clc1ccc2c(ccnc2c1)C(=O)NCC(=O)N1CCC[C@H]1C#N	InChI=1S/C17H15ClN4O2/c18-11-3-4-13-14(5-6-20-15(13)8-11)17(24)21-10-16(23)22-7-1-2-12(22)9-19/h3-6,8,12H,1-2,7,10H2,(H,21,24)/t12-/m0/s1	NERXNBIHCGOYFQ-LBPRGKRZSA-N	50434164	CHEMBL2385272::US9346814, Cmpd No 13 Example 16	Prolyl endopeptidase FAP			 7.1							ChEMBL	10.1021/ml300410d	10.7270/Q2KP83J7	24900696			Jansen, K; Heirbaut, L; Cheng, JD; Joossens, J; Ryabtsova, O; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp (UA)	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50434164	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50434164&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			73356493	175446481		CHEMBL2385272				ZINC96270274	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
51063932	COc1ccc2nccc(C(=O)NCC(=O)N3CCC[C@H]3C#N)c2c1	InChI=1S/C18H18N4O3/c1-25-13-4-5-16-15(9-13)14(6-7-20-16)18(24)21-11-17(23)22-8-2-3-12(22)10-19/h4-7,9,12H,2-3,8,11H2,1H3,(H,21,24)/t12-/m0/s1	YPWQFVMQCFSLCP-LBPRGKRZSA-N	50434165	CHEMBL2385271::US9346814, Cmpd No 11 Example 14	Prolyl endopeptidase FAP			 9.2							ChEMBL	10.1021/ml300410d	10.7270/Q2KP83J7	24900696			Jansen, K; Heirbaut, L; Cheng, JD; Joossens, J; Ryabtsova, O; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp (UA)	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50434165	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50434165&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			71667377	175446482		CHEMBL2385271				ZINC96270275	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
51063933	Fc1ccc2nccc(C(=O)NCC(=O)N3CCC[C@H]3C#N)c2c1	InChI=1S/C17H15FN4O2/c18-11-3-4-15-14(8-11)13(5-6-20-15)17(24)21-10-16(23)22-7-1-2-12(22)9-19/h3-6,8,12H,1-2,7,10H2,(H,21,24)/t12-/m0/s1	CRWCYVOHVXAEMF-LBPRGKRZSA-N	50434166	CHEMBL2385270::US9346814, Cmpd No 6 Example 9	Prolyl endopeptidase FAP			 10							ChEMBL	10.1021/ml300410d	10.7270/Q2KP83J7	24900696			Jansen, K; Heirbaut, L; Cheng, JD; Joossens, J; Ryabtsova, O; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp (UA)	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50434166	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50434166&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			71667229	175446483		CHEMBL2385270				ZINC96270276	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
51063934	FC(F)(F)Oc1ccc2nccc(C(=O)NCC(=O)N3CCC[C@H]3C#N)c2c1	InChI=1S/C18H15F3N4O3/c19-18(20,21)28-12-3-4-15-14(8-12)13(5-6-23-15)17(27)24-10-16(26)25-7-1-2-11(25)9-22/h3-6,8,11H,1-2,7,10H2,(H,24,27)/t11-/m0/s1	VSNIZLIYSJARCU-NSHDSACASA-N	50434167	CHEMBL2385302::US9346814, Cmpd No 8 Example 11	Prolyl endopeptidase FAP			 12							ChEMBL	10.1021/ml300410d	10.7270/Q2KP83J7	24900696			Jansen, K; Heirbaut, L; Cheng, JD; Joossens, J; Ryabtsova, O; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp (UA)	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50434167	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50434167&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			71667231	175446484		CHEMBL2385302				ZINC96270277	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
51063935	Clc1ccc2nccc(C(=O)NCC(=O)N3CCC[C@H]3C#N)c2c1	InChI=1S/C17H15ClN4O2/c18-11-3-4-15-14(8-11)13(5-6-20-15)17(24)21-10-16(23)22-7-1-2-12(22)9-19/h3-6,8,12H,1-2,7,10H2,(H,21,24)/t12-/m0/s1	KPLYEVMFCDTZKW-LBPRGKRZSA-N	50434168	CHEMBL2385301::US9346814, Cmpd No 7 Example 10	Prolyl endopeptidase FAP			 14							ChEMBL	10.1021/ml300410d	10.7270/Q2KP83J7	24900696			Jansen, K; Heirbaut, L; Cheng, JD; Joossens, J; Ryabtsova, O; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp (UA)	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50434168	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50434168&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			71667230	175446485		CHEMBL2385301				ZINC96270278	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
51063936	Brc1cccc2nccc(C(=O)NCC(=O)N3CCC[C@H]3C#N)c12	InChI=1S/C17H15BrN4O2/c18-13-4-1-5-14-16(13)12(6-7-20-14)17(24)21-10-15(23)22-8-2-3-11(22)9-19/h1,4-7,11H,2-3,8,10H2,(H,21,24)/t11-/m0/s1	XTSDSKNXFWPJCS-NSHDSACASA-N	50434169	CHEMBL2385300::US9346814, Cmpd No 22 Example 26	Prolyl endopeptidase FAP		 4.1								ChEMBL	10.1021/ml300410d	10.7270/Q2KP83J7	24900696			Jansen, K; Heirbaut, L; Cheng, JD; Joossens, J; Ryabtsova, O; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp (UA)	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50434169	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50434169&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			71655623	175446486		CHEMBL2385300				ZINC96270279	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
51063937	Brc1cccc2nccc(C(=O)NCC(=O)N3CCC[C@H]3C#N)c12	InChI=1S/C17H15BrN4O2/c18-13-4-1-5-14-16(13)12(6-7-20-14)17(24)21-10-15(23)22-8-2-3-11(22)9-19/h1,4-7,11H,2-3,8,10H2,(H,21,24)/t11-/m0/s1	XTSDSKNXFWPJCS-NSHDSACASA-N	50434169	CHEMBL2385300::US9346814, Cmpd No 22 Example 26	Prolyl endopeptidase FAP			 11							ChEMBL	10.1021/ml300410d	10.7270/Q2KP83J7	24900696			Jansen, K; Heirbaut, L; Cheng, JD; Joossens, J; Ryabtsova, O; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp (UA)	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50434169	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50434169&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			71655623	175446486		CHEMBL2385300				ZINC96270279	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
51063938	Clc1cccc2nccc(C(=O)NCC(=O)N3CCC[C@H]3C#N)c12	InChI=1S/C17H15ClN4O2/c18-13-4-1-5-14-16(13)12(6-7-20-14)17(24)21-10-15(23)22-8-2-3-11(22)9-19/h1,4-7,11H,2-3,8,10H2,(H,21,24)/t11-/m0/s1	ALYYADQHQGUFHD-NSHDSACASA-N	50434170	CHEMBL2385299::US9346814, Cmpd No 21 Example 25	Prolyl endopeptidase FAP			 9.9							ChEMBL	10.1021/ml300410d	10.7270/Q2KP83J7	24900696			Jansen, K; Heirbaut, L; Cheng, JD; Joossens, J; Ryabtsova, O; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp (UA)	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50434170	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50434170&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			71655622	175446487		CHEMBL2385299				ZINC96270280	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
51063939	Oc1cnc2ccccc2c1C(=O)NCC(=O)N1CCC[C@H]1C#N	InChI=1S/C17H16N4O3/c18-8-11-4-3-7-21(11)15(23)10-20-17(24)16-12-5-1-2-6-13(12)19-9-14(16)22/h1-2,5-6,9,11,22H,3-4,7,10H2,(H,20,24)/t11-/m0/s1	SFRHBBXTBPBKRA-NSHDSACASA-N	50434171	CHEMBL2385298::US9346814, Cmpd No 38 Example 43	Prolyl endopeptidase FAP			 160							ChEMBL	10.1021/ml300410d	10.7270/Q2KP83J7	24900696			Jansen, K; Heirbaut, L; Cheng, JD; Joossens, J; Ryabtsova, O; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp (UA)	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50434171	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50434171&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			73347360	175446488		CHEMBL2385298				ZINC96270281	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
51063940	O=C(CNC(=O)c1c2CCCCc2nc2ccccc12)N1CCC[C@H]1C#N	InChI=1S/C21H22N4O2/c22-12-14-6-5-11-25(14)19(26)13-23-21(27)20-15-7-1-3-9-17(15)24-18-10-4-2-8-16(18)20/h1,3,7,9,14H,2,4-6,8,10-11,13H2,(H,23,27)/t14-/m0/s1	NSDWPMUKFKHERI-AWEZNQCLSA-N	50434172	CHEMBL2385297	Prolyl endopeptidase FAP			 770							ChEMBL	10.1021/ml300410d	10.7270/Q2KP83J7	24900696			Jansen, K; Heirbaut, L; Cheng, JD; Joossens, J; Ryabtsova, O; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp (UA)	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50434172	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50434172&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			73347359	175446489		CHEMBL2385297				ZINC96270282	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
51063941	COc1ccc(cc1)-c1cc(C(=O)NCC(=O)N2CCC[C@H]2C#N)c2ccccc2n1	InChI=1S/C24H22N4O3/c1-31-18-10-8-16(9-11-18)22-13-20(19-6-2-3-7-21(19)27-22)24(30)26-15-23(29)28-12-4-5-17(28)14-25/h2-3,6-11,13,17H,4-5,12,15H2,1H3,(H,26,30)/t17-/m0/s1	ZOZXAKSTNNIXSO-KRWDZBQOSA-N	50434173	CHEMBL2385296	Prolyl endopeptidase FAP			>10000							ChEMBL	10.1021/ml300410d	10.7270/Q2KP83J7	24900696			Jansen, K; Heirbaut, L; Cheng, JD; Joossens, J; Ryabtsova, O; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp (UA)	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50434173	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50434173&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			71655557	175446490		CHEMBL2385296				ZINC96270283	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
51063942	O=C(CNC(=O)c1cc(=O)[nH]c2ccccc12)N1CCC[C@H]1C#N	InChI=1S/C17H16N4O3/c18-9-11-4-3-7-21(11)16(23)10-19-17(24)13-8-15(22)20-14-6-2-1-5-12(13)14/h1-2,5-6,8,11H,3-4,7,10H2,(H,19,24)(H,20,22)/t11-/m0/s1	KOXPKYHLIKMCPU-NSHDSACASA-N	50434174	CHEMBL2385295	Prolyl endopeptidase FAP			 1000							ChEMBL	10.1021/ml300410d	10.7270/Q2KP83J7	24900696			Jansen, K; Heirbaut, L; Cheng, JD; Joossens, J; Ryabtsova, O; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp (UA)	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50434174	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50434174&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			73354936	175446491		CHEMBL2385295				ZINC96270284	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
51063943	Cc1nc2ccccc2c(C(=O)NCC(=O)N2CCC[C@H]2C#N)c1O	InChI=1S/C18H18N4O3/c1-11-17(24)16(13-6-2-3-7-14(13)21-11)18(25)20-10-15(23)22-8-4-5-12(22)9-19/h2-3,6-7,12,24H,4-5,8,10H2,1H3,(H,20,25)/t12-/m0/s1	QPYHHKIZAVGBJJ-LBPRGKRZSA-N	50434175	CHEMBL2385294::US9346814, Cmpd No 5 Example 8	Prolyl endopeptidase FAP			 5900							ChEMBL	10.1021/ml300410d	10.7270/Q2KP83J7	24900696			Jansen, K; Heirbaut, L; Cheng, JD; Joossens, J; Ryabtsova, O; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp (UA)	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50434175	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50434175&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			71655556	175446492		CHEMBL2385294				ZINC96270285	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
51063944	Cc1cc(C(=O)NCC(=O)N2CCC[C@H]2C#N)c2ccccc2n1	InChI=1S/C18H18N4O2/c1-12-9-15(14-6-2-3-7-16(14)21-12)18(24)20-11-17(23)22-8-4-5-13(22)10-19/h2-3,6-7,9,13H,4-5,8,11H2,1H3,(H,20,24)/t13-/m0/s1	XTSOTMGJBJQAAZ-ZDUSSCGKSA-N	50434176	CHEMBL2385293::US9346814, Cmpd No 3 Example 4	Prolyl endopeptidase FAP			 670							ChEMBL	10.1021/ml300410d	10.7270/Q2KP83J7	24900696			Jansen, K; Heirbaut, L; Cheng, JD; Joossens, J; Ryabtsova, O; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp (UA)	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50434176	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50434176&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			71667081	175446493		CHEMBL2385293				ZINC96270286	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
51063945	O=C(CN1Cc2ccccc2C1=O)N1CCC[C@H]1C#N	InChI=1S/C15H15N3O2/c16-8-12-5-3-7-18(12)14(19)10-17-9-11-4-1-2-6-13(11)15(17)20/h1-2,4,6,12H,3,5,7,9-10H2/t12-/m0/s1	JNHNUZDMIYRMDE-LBPRGKRZSA-N	50434177	CHEMBL2385292	Prolyl endopeptidase FAP			 42000							ChEMBL	10.1021/ml300410d	10.7270/Q2KP83J7	24900696			Jansen, K; Heirbaut, L; Cheng, JD; Joossens, J; Ryabtsova, O; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp (UA)	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50434177	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50434177&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			73356496	175446494		CHEMBL2385292				ZINC96270287	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
51063946	OC12CC3CC(C1)CC(C3)(C2)C(=O)NCC(=O)N1CCC[C@H]1C#N	InChI=1S/C18H25N3O3/c19-9-14-2-1-3-21(14)15(22)10-20-16(23)17-5-12-4-13(6-17)8-18(24,7-12)11-17/h12-14,24H,1-8,10-11H2,(H,20,23)/t12?,13?,14-,17?,18?/m0/s1	UWBZSVXHRVYSEZ-JPVBRBBMSA-N	50434178	CHEMBL2385291	Prolyl endopeptidase FAP			 2100							ChEMBL	10.1021/ml300410d	10.7270/Q2KP83J7	24900696			Jansen, K; Heirbaut, L; Cheng, JD; Joossens, J; Ryabtsova, O; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp (UA)	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50434178	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50434178&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			73348871	175446495		CHEMBL2385291				ZINC96270288	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
51063947	O=C(CNc1ccc(cn1)C#N)NCC(=O)N1CCC[C@H]1C#N	InChI=1S/C15H16N6O2/c16-6-11-3-4-13(18-8-11)19-9-14(22)20-10-15(23)21-5-1-2-12(21)7-17/h3-4,8,12H,1-2,5,9-10H2,(H,18,19)(H,20,22)/t12-/m0/s1	FFDPUUZDAMRRCD-LBPRGKRZSA-N	50434179	CHEMBL2385290	Prolyl endopeptidase FAP			 11800							ChEMBL	10.1021/ml300410d	10.7270/Q2KP83J7	24900696			Jansen, K; Heirbaut, L; Cheng, JD; Joossens, J; Ryabtsova, O; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp (UA)	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50434179	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50434179&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			73356495	175446496		CHEMBL2385290				ZINC96270289	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
51063948	O=C(CNS(=O)(=O)c1cccc2ccccc12)N1CCC[C@H]1C#N	InChI=1S/C17H17N3O3S/c18-11-14-7-4-10-20(14)17(21)12-19-24(22,23)16-9-3-6-13-5-1-2-8-15(13)16/h1-3,5-6,8-9,14,19H,4,7,10,12H2/t14-/m0/s1	HRIKQHHODIYSSE-AWEZNQCLSA-N	50434180	CHEMBL2385289	Prolyl endopeptidase FAP			 17600							ChEMBL	10.1021/ml300410d	10.7270/Q2KP83J7	24900696			Jansen, K; Heirbaut, L; Cheng, JD; Joossens, J; Ryabtsova, O; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp (UA)	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50434180	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50434180&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			73353425	175446497		CHEMBL2385289				ZINC96270290	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
51063949	O=C(COc1ccc2ccccc2c1)N1CCC[C@H]1C#N	InChI=1S/C17H16N2O2/c18-11-15-6-3-9-19(15)17(20)12-21-16-8-7-13-4-1-2-5-14(13)10-16/h1-2,4-5,7-8,10,15H,3,6,9,12H2/t15-/m0/s1	CODCBQWQVMLWTN-HNNXBMFYSA-N	50434181	CHEMBL2385288	Prolyl endopeptidase FAP			>12500							ChEMBL	10.1021/ml300410d	10.7270/Q2KP83J7	24900696			Jansen, K; Heirbaut, L; Cheng, JD; Joossens, J; Ryabtsova, O; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp (UA)	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50434181	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50434181&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			73345857	175446498		CHEMBL2385288				ZINC96270291	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
51063950	O=C(COc1cccc2ccccc12)N1CCC[C@H]1C#N	InChI=1S/C17H16N2O2/c18-11-14-7-4-10-19(14)17(20)12-21-16-9-3-6-13-5-1-2-8-15(13)16/h1-3,5-6,8-9,14H,4,7,10,12H2/t14-/m0/s1	GXTNNLMFNYTVNV-AWEZNQCLSA-N	50434182	CHEMBL2385287	Prolyl endopeptidase FAP			>12500							ChEMBL	10.1021/ml300410d	10.7270/Q2KP83J7	24900696			Jansen, K; Heirbaut, L; Cheng, JD; Joossens, J; Ryabtsova, O; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp (UA)	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50434182	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50434182&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			73353424	175446499		CHEMBL2385287				ZINC96270292	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
51063951	O=C(Cc1cccc2ccccc12)NCC(=O)N1CCC[C@H]1C#N	InChI=1S/C19H19N3O2/c20-12-16-8-4-10-22(16)19(24)13-21-18(23)11-15-7-3-6-14-5-1-2-9-17(14)15/h1-3,5-7,9,16H,4,8,10-11,13H2,(H,21,23)/t16-/m0/s1	WVPYKTIDGGNPHQ-INIZCTEOSA-N	50434183	CHEMBL2385286	Prolyl endopeptidase FAP			 8500							ChEMBL	10.1021/ml300410d	10.7270/Q2KP83J7	24900696			Jansen, K; Heirbaut, L; Cheng, JD; Joossens, J; Ryabtsova, O; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp (UA)	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50434183	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50434183&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			73356494	175446500		CHEMBL2385286				ZINC96270293	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321							
51063952	O=C(COc1cccc2ccccc12)NCC(=O)N1CCC[C@H]1C#N	InChI=1S/C19H19N3O3/c20-11-15-7-4-10-22(15)19(24)12-21-18(23)13-25-17-9-3-6-14-5-1-2-8-16(14)17/h1-3,5-6,8-9,15H,4,7,10,12-13H2,(H,21,23)/t15-/m0/s1	VRVJKJRGXAIUNH-HNNXBMFYSA-N	50434184	CHEMBL2385285	Prolyl endopeptidase FAP			 9400							ChEMBL	10.1021/ml300410d	10.7270/Q2KP83J7	24900696			Jansen, K; Heirbaut, L; Cheng, JD; Joossens, J; Ryabtsova, O; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P	University of Antwerp (UA)	http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50434184	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10010&target=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search	http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50434184&enzyme=Prolyl+endopeptidase+FAP&column=ki&startPg=0&Increment=50&submit=Search			73350450	175446501		CHEMBL2385285				ZINC96270294	1	MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPNWISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYGDGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVSSERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGRTDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQLTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYSERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD		Prolyl endopeptidase FAP	SEPR_MOUSE	P97321