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 50867541 COC[C@H]1CN(Cc2ccccn2)C(=O)[C@@H]2CCC[C@H]1N2S(=O)(=O)c1cc(Cl)cc(Cl)c1 InChI=1S/C22H25Cl2N3O4S/c1-31-14-15-12-26(13-18-5-2-3-8-25-18)22(28)21-7-4-6-20(15)27(21)32(29,30)19-10-16(23)9-17(24)11-19/h2-3,5,8-11,15,20-21H,4,6-7,12-14H2,1H3/t15-,20-,21+/m1/s1 CLJZLDBGGLGZDB-LPTQZCDUSA-N 50263407 CHEMBL4090599 Peptidyl-prolyl cis-trans isomerase FKBP1B Homo sapiens 1.2 ChEMBL 10.1021/acs.jmedchem.8b00137 10.7270/Q2833VGW 29578710 Pomplun, S; Sippel, C; Hähle, A; Tay, D; Shima, K; Klages, A; Ünal, CM; Rieß, B; Toh, HT; Hansen, G; Yoon, HS; Bracher, A; Preiser, P; Rupp, J; Steinert, M; Hausch, F Max Planck Institute of Psychiatry http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50263407 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50000503&target=Peptidyl-prolyl+cis-trans+isomerase+FKBP1B&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50263407&enzyme=Peptidyl-prolyl+cis-trans+isomerase+FKBP1B&column=ki&startPg=0&Increment=50&submit=Search 137642835 404341476 1 MGVEIETISPGDGRTFPKKGQTCVVHYTGMLQNGKKFDSSRDRNKPFKFRIGKQEVIKGFEEGAAQMSLGQRAKLTCTPDVAYGATGHPGVIPPNATLIFDVELLNLE 1C9H,1FKK,1FKL,4C02,5HKG,5T15,5T9M,5T9N,5T9R,5T9S,5T9V,5TA3,5TAL,5TAM,5TAN,5TAP,5TAQ,5TAS,5TAT,5TAU,5TAV,5TAW,5TAX,5TAY,5TAZ,5TB0,5TB1,5TB2,5TB3,5TB4,6JGZ,6JH6,6JHN,6JI0,6JI8,6JII,6JIU,6JIY,6JRR,6JRS,6M2W,6PV6,6W1N,6WOT,6WOU,6WOV,6X32,6X33,6X34,6X35,6X36,7CF9,7JMF,7JMG,7JMH,7JMI,7JMJ,7M6A,7M6L,7T64,7T65,7U9Q,7U9R,7U9T,7U9X,7U9Z,7UA1,7UA3,7UA4,7UA5,7UA9,7VML,7VMM,7VMN,7VMO,7VMP,7VMQ,7VMR,7VMS,8DUJ,8DVE,8SEN,8SEO,8SEP,8SEQ,8SER,8SES,8SET Peptidyl-prolyl cis-trans isomerase FKBP1B FKB1B_HUMAN P68106 Q13664 Q16645 Q53TM2 Q9BQ40 50043480 CC[C@@H]1NC(=O)[C@H](C(O)C(C)C\C=C\C)N(C)C(=O)[C@@H](C(C)C)N(C)C(=O)[C@H](CC(C)C)N(C)C(=O)[C@@H](CC(C)C)N(C)C(=O)[C@@H](C)NC(=O)[C@@H](Cc2ccccc2)NC(=O)[C@@H](CC(C)C)N(C)C(=O)[C@@H](NC(=O)[C@H](CC(C)C)N(C)C(=O)[C@@H](C)N(C)C1=O)C(C)C InChI=1S/C69H117N11O12/c1-25-27-31-45(15)58(81)57-62(85)71-49(26-2)65(88)74(18)47(17)64(87)75(19)52(35-40(5)6)61(84)73-55(43(11)12)68(91)76(20)51(34-39(3)4)60(83)72-50(38-48-32-29-28-30-33-48)59(82)70-46(16)63(86)77(21)53(36-41(7)8)66(89)78(22)54(37-42(9)10)67(90)79(23)56(44(13)14)69(92)80(57)24/h25,27-30,32-33,39-47,49-58,81H,26,31,34-38H2,1-24H3,(H,70,82)(H,71,85)(H,72,83)(H,73,84)/b27-25+/t45?,46-,47-,49+,50-,51-,52+,53-,54+,55+,56-,57+,58?/m1/s1 RSLBTQJZWBITFN-YDQQYGCFSA-N 50029190 15-Benzyl-30-ethyl-33-(1-hydroxy-2-methyl-hex-4-enyl)-6,9,18,24-tetraisobutyl-3,21-diisopropyl-1,4,7,10,12,19,25,27,28-nonamethyl-1,4,7,10,13,16,19,22,25,28,31undecaaza-cyclotritriacontan-2,5,8,11,14,17,20,23,26,29,32-undecaone::CHEMBL2370706 Peptidyl-prolyl cis-trans isomerase FKBP1B Homo sapiens 6 ChEMBL 10.1021/jm00021a005 10.7270/Q2X34WGK 7473543 Hu, MK; Badger, A; Rich, DH University of Wisconsin-Madison http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50029190 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50000503&target=Peptidyl-prolyl+cis-trans+isomerase+FKBP1B&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50029190&enzyme=Peptidyl-prolyl+cis-trans+isomerase+FKBP1B&column=ki&startPg=0&Increment=50&submit=Search 73356149 103938261 CHEMBL2370706 1 MGVEIETISPGDGRTFPKKGQTCVVHYTGMLQNGKKFDSSRDRNKPFKFRIGKQEVIKGFEEGAAQMSLGQRAKLTCTPDVAYGATGHPGVIPPNATLIFDVELLNLE 1C9H,1FKK,1FKL,4C02,5HKG,5T15,5T9M,5T9N,5T9R,5T9S,5T9V,5TA3,5TAL,5TAM,5TAN,5TAP,5TAQ,5TAS,5TAT,5TAU,5TAV,5TAW,5TAX,5TAY,5TAZ,5TB0,5TB1,5TB2,5TB3,5TB4,6JGZ,6JH6,6JHN,6JI0,6JI8,6JII,6JIU,6JIY,6JRR,6JRS,6M2W,6PV6,6W1N,6WOT,6WOU,6WOV,6X32,6X33,6X34,6X35,6X36,7CF9,7JMF,7JMG,7JMH,7JMI,7JMJ,7M6A,7M6L,7T64,7T65,7U9Q,7U9R,7U9T,7U9X,7U9Z,7UA1,7UA3,7UA4,7UA5,7UA9,7VML,7VMM,7VMN,7VMO,7VMP,7VMQ,7VMR,7VMS,8DUJ,8DVE,8SEN,8SEO,8SEP,8SEQ,8SER,8SES,8SET Peptidyl-prolyl cis-trans isomerase FKBP1B FKB1B_HUMAN P68106 Q13664 Q16645 Q53TM2 Q9BQ40 50043481 CC[C@@H]1NC(=O)[C@H]([C@H](O)C(C)C\C=C\C)N(C)C(=O)[C@@H](C(C)C)N(C)C(=O)[C@H](CC(C)C)N(C)C(=O)[C@@H](CC(C)C)N(C)C(=O)[C@H](CO)NC(=O)[C@@H](Cc2ccccc2)NC(=O)[C@@H](CC(C)C)N(C)C(=O)[C@@H](NC(=O)[C@H](CC(C)C)N(C)C(=O)CN(C)C1=O)C(C)C InChI=1S/C68H115N11O13/c1-23-25-29-45(15)58(82)57-62(86)69-47(24-2)63(87)73(16)37-54(81)74(17)50(32-39(3)4)61(85)72-55(43(11)12)67(91)75(18)51(33-40(5)6)60(84)70-48(36-46-30-27-26-28-31-46)59(83)71-49(38-80)64(88)76(19)52(34-41(7)8)65(89)77(20)53(35-42(9)10)66(90)78(21)56(44(13)14)68(92)79(57)22/h23,25-28,30-31,39-45,47-53,55-58,80,82H,24,29,32-38H2,1-22H3,(H,69,86)(H,70,84)(H,71,83)(H,72,85)/b25-23+/t45?,47-,48+,49-,50-,51+,52+,53-,55-,56+,57-,58+/m0/s1 MGQGFRQOSWVMPG-GYKXRLDESA-N 50029192 15-Benzyl-30-ethyl-12-hydroxymethyl-33-(1-hydroxy-2-methyl-hex-4-enyl)-6,9,18,24-tetraisobutyl-3,21-diisopropyl-1,4,7,10,19,25,28-heptamethyl-1,4,7,10,13,16,19,22,25,28,31undecaaza-cyclotritriacontan-2,5,8,11,14,17,20,23,26,29,32-undecaone::CHEMBL2370707 Peptidyl-prolyl cis-trans isomerase FKBP1B Homo sapiens 6 ChEMBL 10.1021/jm00021a005 10.7270/Q2X34WGK 7473543 Hu, MK; Badger, A; Rich, DH University of Wisconsin-Madison http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50029192 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50000503&target=Peptidyl-prolyl+cis-trans+isomerase+FKBP1B&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50029192&enzyme=Peptidyl-prolyl+cis-trans+isomerase+FKBP1B&column=ki&startPg=0&Increment=50&submit=Search 73353071 103938263 CHEMBL2370707 1 MGVEIETISPGDGRTFPKKGQTCVVHYTGMLQNGKKFDSSRDRNKPFKFRIGKQEVIKGFEEGAAQMSLGQRAKLTCTPDVAYGATGHPGVIPPNATLIFDVELLNLE 1C9H,1FKK,1FKL,4C02,5HKG,5T15,5T9M,5T9N,5T9R,5T9S,5T9V,5TA3,5TAL,5TAM,5TAN,5TAP,5TAQ,5TAS,5TAT,5TAU,5TAV,5TAW,5TAX,5TAY,5TAZ,5TB0,5TB1,5TB2,5TB3,5TB4,6JGZ,6JH6,6JHN,6JI0,6JI8,6JII,6JIU,6JIY,6JRR,6JRS,6M2W,6PV6,6W1N,6WOT,6WOU,6WOV,6X32,6X33,6X34,6X35,6X36,7CF9,7JMF,7JMG,7JMH,7JMI,7JMJ,7M6A,7M6L,7T64,7T65,7U9Q,7U9R,7U9T,7U9X,7U9Z,7UA1,7UA3,7UA4,7UA5,7UA9,7VML,7VMM,7VMN,7VMO,7VMP,7VMQ,7VMR,7VMS,8DUJ,8DVE,8SEN,8SEO,8SEP,8SEQ,8SER,8SES,8SET Peptidyl-prolyl cis-trans isomerase FKBP1B FKB1B_HUMAN P68106 Q13664 Q16645 Q53TM2 Q9BQ40 50043482 CCC1NC(=O)C(C(O)C(C)C\C=C\C)N(C)C(=O)[C@@H](C(C)C)N(C)[C@@H](O)[C@H](CC(C)C)N(C)[C@@H](O)[C@H](CC(C)C)N(C)C(=O)[C@@H](C)NC(=O)[C@H](C)N[C@@H](O)[C@@H](CC(C)C)N(C)C(=O)C(N[C@@H](O)[C@H](CC(C)C)N(C)[C@@H](O)CN(C)[C@@H]1O)C(C)C InChI=1S/C62H123N11O12/c1-25-27-28-40(15)52(75)51-56(79)65-43(26-2)58(81)67(18)33-48(74)68(19)44(29-34(3)4)55(78)66-49(38(11)12)61(84)69(20)45(30-35(5)6)54(77)63-41(16)53(76)64-42(17)57(80)70(21)46(31-36(7)8)59(82)71(22)47(32-37(9)10)60(83)72(23)50(39(13)14)62(85)73(51)24/h25,27,34-52,54-55,58-60,63,66,74-75,77-78,81-83H,26,28-33H2,1-24H3,(H,64,76)(H,65,79)/b27-25+/t40?,41-,42+,43?,44-,45+,46-,47-,48-,49?,50+,51?,52?,54-,55-,58+,59-,60-/m0/s1 RAPARJSMMZVCBG-ZEMLUYHMSA-N 50029191 15-Benzyl-30-ethyl-12-hydroxymethyl-33-(1-hydroxy-2-methyl-hex-4-enyl)-6,9,18,24-tetraisobutyl-3,21-diisopropyl-1,4,7,10,19,25,27,28-octamethyl-1,4,7,10,13,16,19,22,25,28,31undecaaza-cyclotritriacontan-2,5,8,11,14,17,20,23,26,29,32-undecaone::CHEMBL216520 Peptidyl-prolyl cis-trans isomerase FKBP1B Homo sapiens 3 ChEMBL 10.1021/jm00021a005 10.7270/Q2X34WGK 7473543 Hu, MK; Badger, A; Rich, DH University of Wisconsin-Madison http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50029191 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50000503&target=Peptidyl-prolyl+cis-trans+isomerase+FKBP1B&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50029191&enzyme=Peptidyl-prolyl+cis-trans+isomerase+FKBP1B&column=ki&startPg=0&Increment=50&submit=Search 44354786 103938262 CHEMBL216520 1 MGVEIETISPGDGRTFPKKGQTCVVHYTGMLQNGKKFDSSRDRNKPFKFRIGKQEVIKGFEEGAAQMSLGQRAKLTCTPDVAYGATGHPGVIPPNATLIFDVELLNLE 1C9H,1FKK,1FKL,4C02,5HKG,5T15,5T9M,5T9N,5T9R,5T9S,5T9V,5TA3,5TAL,5TAM,5TAN,5TAP,5TAQ,5TAS,5TAT,5TAU,5TAV,5TAW,5TAX,5TAY,5TAZ,5TB0,5TB1,5TB2,5TB3,5TB4,6JGZ,6JH6,6JHN,6JI0,6JI8,6JII,6JIU,6JIY,6JRR,6JRS,6M2W,6PV6,6W1N,6WOT,6WOU,6WOV,6X32,6X33,6X34,6X35,6X36,7CF9,7JMF,7JMG,7JMH,7JMI,7JMJ,7M6A,7M6L,7T64,7T65,7U9Q,7U9R,7U9T,7U9X,7U9Z,7UA1,7UA3,7UA4,7UA5,7UA9,7VML,7VMM,7VMN,7VMO,7VMP,7VMQ,7VMR,7VMS,8DUJ,8DVE,8SEN,8SEO,8SEP,8SEQ,8SER,8SES,8SET Peptidyl-prolyl cis-trans isomerase FKBP1B FKB1B_HUMAN P68106 Q13664 Q16645 Q53TM2 Q9BQ40 50043483 CC[C@@H]1NC(=O)[C@H]([C@H](O)C(C)C\C=C\C)N(C)C(=O)[C@@H](C(C)C)N(C)C(=O)[C@H](CC(C)C)N(C)C(=O)[C@@H](CC(C)C)N(C)C(=O)[C@@H](C)NC(=O)[C@@H](Cc2ccccc2)NC(=O)[C@@H](CC(C)C)N(C)C(=O)[C@@H](NC(=O)[C@H](CC(C)C)N(C)C(=O)CN(C)C1=O)C(C)C InChI=1S/C68H115N11O12/c1-24-26-30-45(15)58(81)57-62(85)70-48(25-2)64(87)73(17)38-54(80)74(18)50(33-39(3)4)61(84)72-55(43(11)12)67(90)75(19)51(34-40(5)6)60(83)71-49(37-47-31-28-27-29-32-47)59(82)69-46(16)63(86)76(20)52(35-41(7)8)65(88)77(21)53(36-42(9)10)66(89)78(22)56(44(13)14)68(91)79(57)23/h24,26-29,31-32,39-46,48-53,55-58,81H,25,30,33-38H2,1-23H3,(H,69,82)(H,70,85)(H,71,83)(H,72,84)/b26-24+/t45?,46-,48+,49-,50+,51-,52-,53+,55+,56-,57+,58-/m1/s1 GZKBBELRUUTXNY-VMLYWGILSA-N 50029194 15-Benzyl-30-ethyl-33-(1-hydroxy-2-methyl-hex-4-enyl)-6,9,18,24-tetraisobutyl-3,21-diisopropyl-1,4,7,10,12,19,25,28-octamethyl-1,4,7,10,13,16,19,22,25,28,31undecaaza-cyclotritriacontan-2,5,8,11,14,17,20,23,26,29,32-undecaone::CHEMBL2370711 Peptidyl-prolyl cis-trans isomerase FKBP1B Homo sapiens 33 ChEMBL 10.1021/jm00021a005 10.7270/Q2X34WGK 7473543 Hu, MK; Badger, A; Rich, DH University of Wisconsin-Madison http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50029194 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50000503&target=Peptidyl-prolyl+cis-trans+isomerase+FKBP1B&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50029194&enzyme=Peptidyl-prolyl+cis-trans+isomerase+FKBP1B&column=ki&startPg=0&Increment=50&submit=Search 73356151 103938265 CHEMBL2370711 1 MGVEIETISPGDGRTFPKKGQTCVVHYTGMLQNGKKFDSSRDRNKPFKFRIGKQEVIKGFEEGAAQMSLGQRAKLTCTPDVAYGATGHPGVIPPNATLIFDVELLNLE 1C9H,1FKK,1FKL,4C02,5HKG,5T15,5T9M,5T9N,5T9R,5T9S,5T9V,5TA3,5TAL,5TAM,5TAN,5TAP,5TAQ,5TAS,5TAT,5TAU,5TAV,5TAW,5TAX,5TAY,5TAZ,5TB0,5TB1,5TB2,5TB3,5TB4,6JGZ,6JH6,6JHN,6JI0,6JI8,6JII,6JIU,6JIY,6JRR,6JRS,6M2W,6PV6,6W1N,6WOT,6WOU,6WOV,6X32,6X33,6X34,6X35,6X36,7CF9,7JMF,7JMG,7JMH,7JMI,7JMJ,7M6A,7M6L,7T64,7T65,7U9Q,7U9R,7U9T,7U9X,7U9Z,7UA1,7UA3,7UA4,7UA5,7UA9,7VML,7VMM,7VMN,7VMO,7VMP,7VMQ,7VMR,7VMS,8DUJ,8DVE,8SEN,8SEO,8SEP,8SEQ,8SER,8SES,8SET Peptidyl-prolyl cis-trans isomerase FKBP1B FKB1B_HUMAN P68106 Q13664 Q16645 Q53TM2 Q9BQ40 50268437 CO[C@@H]1C[C@H](C[C@@H](C)[C@@H]2CC(=O)[C@H](C)\C=C(C)\[C@@H](O)[C@@H](OC)C(=O)[C@H](C)C[C@H](C)\C=C\C=C\C=C(C)\[C@H](C[C@@H]3CC[C@@H](C)[C@@](O)(O3)C(=O)C(=O)N3CCCC[C@H]3C(=O)O2)OC)CC[C@H]1O InChI=1S/C51H79NO13/c1-30-16-12-11-13-17-31(2)42(61-8)28-38-21-19-36(7)51(60,65-38)48(57)49(58)52-23-15-14-18-39(52)50(59)64-43(33(4)26-37-20-22-40(53)44(27-37)62-9)29-41(54)32(3)25-35(6)46(56)47(63-10)45(55)34(5)24-30/h11-13,16-17,25,30,32-34,36-40,42-44,46-47,53,56,60H,14-15,18-24,26-29H2,1-10H3/b13-11+,16-12+,31-17+,35-25+/t30-,32-,33-,34-,36-,37+,38+,39+,40-,42+,43+,44-,46-,47+,51-/m1/s1 QFJCIRLUMZQUOT-HPLJOQBZSA-N 36609 Rapamycin C-7, analog 4::SIROLIMUS::US11603377, Compound Ramycin Peptidyl-prolyl cis-trans isomerase FKBP1B Homo sapiens 0.200000 ChEMBL 10.1021/jm500325k 10.7270/Q2JW8GH3 24913411 Gibbs, AC Janssen Research and Development LLC http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=36609 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50000503&target=Peptidyl-prolyl+cis-trans+isomerase+FKBP1B&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=36609&enzyme=Peptidyl-prolyl+cis-trans+isomerase+FKBP1B&column=ki&startPg=0&Increment=50&submit=Search RAP 1Z58,5FLC,1C9H,4DRJ,4DRH,4DRI,5GPG,1PBK,7F2J,1FAP,4QT3,4QT2,2VCD,2DG4,2DG3,2DG9,5HKG,1FKL,1FKB,3KZ7,6M4W,6M4V,6M4U 5284616 118043176 9168 C07909 1 MGVEIETISPGDGRTFPKKGQTCVVHYTGMLQNGKKFDSSRDRNKPFKFRIGKQEVIKGFEEGAAQMSLGQRAKLTCTPDVAYGATGHPGVIPPNATLIFDVELLNLE 1C9H,1FKK,1FKL,4C02,5HKG,5T15,5T9M,5T9N,5T9R,5T9S,5T9V,5TA3,5TAL,5TAM,5TAN,5TAP,5TAQ,5TAS,5TAT,5TAU,5TAV,5TAW,5TAX,5TAY,5TAZ,5TB0,5TB1,5TB2,5TB3,5TB4,6JGZ,6JH6,6JHN,6JI0,6JI8,6JII,6JIU,6JIY,6JRR,6JRS,6M2W,6PV6,6W1N,6WOT,6WOU,6WOV,6X32,6X33,6X34,6X35,6X36,7CF9,7JMF,7JMG,7JMH,7JMI,7JMJ,7M6A,7M6L,7T64,7T65,7U9Q,7U9R,7U9T,7U9X,7U9Z,7UA1,7UA3,7UA4,7UA5,7UA9,7VML,7VMM,7VMN,7VMO,7VMP,7VMQ,7VMR,7VMS,8DUJ,8DVE,8SEN,8SEO,8SEP,8SEQ,8SER,8SES,8SET Peptidyl-prolyl cis-trans isomerase FKBP1B FKB1B_HUMAN P68106 Q13664 Q16645 Q53TM2 Q9BQ40 50268458 CO[C@@H]1C[C@@H](CC[C@H]1O)\C=C(/C)[C@H]1OC(=O)[C@@H]2CCCCN2C(=O)C(=O)[C@]2(O)O[C@@H]([C@H](C[C@H]2C)OC)[C@H](C[C@@H](C)C\C(C)=C\[C@@H](CC=C)C(=O)C[C@H](O)[C@H]1C)OC InChI=1S/C44H69NO12/c1-10-13-31-19-25(2)18-26(3)20-37(54-8)40-38(55-9)22-28(5)44(52,57-40)41(49)42(50)45-17-12-11-14-32(45)43(51)56-39(29(6)34(47)24-35(31)48)27(4)21-30-15-16-33(46)36(23-30)53-7/h10,19,21,26,28-34,36-40,46-47,52H,1,11-18,20,22-24H2,2-9H3/b25-19+,27-21+/t26-,28+,29+,30-,31+,32-,33+,34-,36+,37-,38-,39+,40+,44+/m0/s1 QJJXYPPXXYFBGM-LFZNUXCKSA-N 50030448 8-DEETHYL-8-[BUT-3-ENYL]-ASCOMYCIN::CHEMBL269732::TACROLIMUS Peptidyl-prolyl cis-trans isomerase FKBP1B Homo sapiens 0.400000 ChEMBL 10.1021/jm500325k 10.7270/Q2JW8GH3 24913411 Gibbs, AC Janssen Research and Development LLC http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50030448 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50000503&target=Peptidyl-prolyl+cis-trans+isomerase+FKBP1B&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50030448&enzyme=Peptidyl-prolyl+cis-trans+isomerase+FKBP1B&column=ki&startPg=0&Increment=50&submit=Search FK5 1BKF,3UQB,3UQA,3IHZ,4LAX,4NNR,3O5R,4ODR,4ODO,5HW8,5HWC,4DZ2,4DZ3,1Q6I,7U0U,2VN1,5D75,5HUA,3VAW,6VRX,1TCO,6TZ8,6TZ6,6TZ7,3UF8,1YAT,6MKE,1FKJ,1FKF,5B8I,6J2M,2FKE 445643 103939344 61049 CHEMBL269732 DB00864 6784 C01375 ZINC85537027 1 MGVEIETISPGDGRTFPKKGQTCVVHYTGMLQNGKKFDSSRDRNKPFKFRIGKQEVIKGFEEGAAQMSLGQRAKLTCTPDVAYGATGHPGVIPPNATLIFDVELLNLE 1C9H,1FKK,1FKL,4C02,5HKG,5T15,5T9M,5T9N,5T9R,5T9S,5T9V,5TA3,5TAL,5TAM,5TAN,5TAP,5TAQ,5TAS,5TAT,5TAU,5TAV,5TAW,5TAX,5TAY,5TAZ,5TB0,5TB1,5TB2,5TB3,5TB4,6JGZ,6JH6,6JHN,6JI0,6JI8,6JII,6JIU,6JIY,6JRR,6JRS,6M2W,6PV6,6W1N,6WOT,6WOU,6WOV,6X32,6X33,6X34,6X35,6X36,7CF9,7JMF,7JMG,7JMH,7JMI,7JMJ,7M6A,7M6L,7T64,7T65,7U9Q,7U9R,7U9T,7U9X,7U9Z,7UA1,7UA3,7UA4,7UA5,7UA9,7VML,7VMM,7VMN,7VMO,7VMP,7VMQ,7VMR,7VMS,8DUJ,8DVE,8SEN,8SEO,8SEP,8SEQ,8SER,8SES,8SET Peptidyl-prolyl cis-trans isomerase FKBP1B FKB1B_HUMAN P68106 Q13664 Q16645 Q53TM2 Q9BQ40 51031949 CC[C@@H]1NC(=O)[C@H]([C@H](O)[C@H](C)C\C=C\C)N(C)C(=O)[C@H](C(C)C)N(C)C(=O)[C@H](CC(C)C)N(C)C(=O)[C@H](CC(C)C)N(C)C(=O)[C@@H](C)NC(=O)[C@H](C)NC(=O)[C@H](CC(C)C)N(C)C(=O)[C@@H](NC(=O)[C@H](CC(C)C)N(C)C(=O)CN(C)C1=O)C(C)C InChI=1S/C62H111N11O12/c1-25-27-28-40(15)52(75)51-56(79)65-43(26-2)58(81)67(18)33-48(74)68(19)44(29-34(3)4)55(78)66-49(38(11)12)61(84)69(20)45(30-35(5)6)54(77)63-41(16)53(76)64-42(17)57(80)70(21)46(31-36(7)8)59(82)71(22)47(32-37(9)10)60(83)72(23)50(39(13)14)62(85)73(51)24/h25,27,34-47,49-52,75H,26,28-33H2,1-24H3,(H,63,77)(H,64,76)(H,65,79)(H,66,78)/b27-25+/t40-,41+,42-,43+,44+,45+,46+,47+,49+,50+,51+,52-/m1/s1 PMATZTZNYRCHOR-CGLBZJNRSA-N 50022815 (3S,6S,9S,12R,15S,18S,21S,24S,30S,33S)-30-ethyl-33-[(1R,2R,4E)-1-hydroxy-2-methylhex-4-en-1-yl]-1,4,7,10,12,15,19,25,28-nonamethyl-6,9,18,24-tetrakis(2-methylpropyl)-3,21-bis(propan-2-yl)-1,4,7,10,13,16,19,22,25,28,31-undecaazacyclotritriacontan-2,5,8,11,14,17,20,23,26,29,32-undecone::30-Ethyl-33-((E)-1-hydroxy-2-methyl-hex-4-enyl)-6,9,18,24-tetraisobutyl-3,21-diisopropyl-1,4,7,10,12,15,19,28-octamethyl-1,4,7,10,13,16,19,22,25,28,31undecaaza-cyclotritriacontan-2,5,8,11,14,17,20,23,26,29,32-undecaone::30-Ethyl-33-(1-hydroxy-2-methyl-hex-4-enyl)-6,9,18,24-tetraisobutyl-3,21-diisopropyl-1,4,7,10,12,15,19,25,28-nonamethyl-1,4,7,10,13,16,19,22,25,28,31undecaaza-cyclotritriacontan-2,5,8,11,14,17,20,23,26,29,32-undecaone::CYCLOSPORINE::Cyclosporin A::Cyclosporine A::Cyclosproine A::US10077289, Compound Cyclosporin A::US9138393, Cyclosporin A Peptidyl-prolyl cis-trans isomerase FKBP1B Homo sapiens 6.0 ChEMBL 10.1021/jm00021a005 10.7270/Q2X34WGK 7473543 Hu, MK; Badger, A; Rich, DH University of Wisconsin-Madison http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50022815 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50000503&target=Peptidyl-prolyl+cis-trans+isomerase+FKBP1B&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50022815&enzyme=Peptidyl-prolyl+cis-trans+isomerase+FKBP1B&column=ki&startPg=0&Increment=50&submit=Search 5284373 103933370 4031 C05086 1 MGVEIETISPGDGRTFPKKGQTCVVHYTGMLQNGKKFDSSRDRNKPFKFRIGKQEVIKGFEEGAAQMSLGQRAKLTCTPDVAYGATGHPGVIPPNATLIFDVELLNLE 1C9H,1FKK,1FKL,4C02,5HKG,5T15,5T9M,5T9N,5T9R,5T9S,5T9V,5TA3,5TAL,5TAM,5TAN,5TAP,5TAQ,5TAS,5TAT,5TAU,5TAV,5TAW,5TAX,5TAY,5TAZ,5TB0,5TB1,5TB2,5TB3,5TB4,6JGZ,6JH6,6JHN,6JI0,6JI8,6JII,6JIU,6JIY,6JRR,6JRS,6M2W,6PV6,6W1N,6WOT,6WOU,6WOV,6X32,6X33,6X34,6X35,6X36,7CF9,7JMF,7JMG,7JMH,7JMI,7JMJ,7M6A,7M6L,7T64,7T65,7U9Q,7U9R,7U9T,7U9X,7U9Z,7UA1,7UA3,7UA4,7UA5,7UA9,7VML,7VMM,7VMN,7VMO,7VMP,7VMQ,7VMR,7VMS,8DUJ,8DVE,8SEN,8SEO,8SEP,8SEQ,8SER,8SES,8SET Peptidyl-prolyl cis-trans isomerase FKBP1B FKB1B_HUMAN P68106 Q13664 Q16645 Q53TM2 Q9BQ40 51425108 COc1cccc(c1)[C@@H](CCc1ccc(OC)c(OC)c1)OC(=O)[C@@H]1CCCCN1C(=O)[C@@H](C1CCCCC1)c1cc(OC)c(OC)c(OC)c1 InChI=1S/C41H53NO9/c1-45-31-16-12-15-29(24-31)33(20-18-27-19-21-34(46-2)35(23-27)47-3)51-41(44)32-17-10-11-22-42(32)40(43)38(28-13-8-7-9-14-28)30-25-36(48-4)39(50-6)37(26-30)49-5/h12,15-16,19,21,23-26,28,32-33,38H,7-11,13-14,17-18,20,22H2,1-6H3/t32-,33+,38-/m0/s1 GKYACUAIJLXSDB-YGCWAPBFSA-N 50575646 CHEMBL4876664 Peptidyl-prolyl cis-trans isomerase FKBP1B Homo sapiens 203 ChEMBL 10.1021/acs.jmedchem.0c02195 10.7270/Q2988BT3 33666419 Bauder, M; Meyners, C; Purder, PL; Merz, S; Sugiarto, WO; Voll, AM; Heymann, T; Hausch, F Technical University Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50575646 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50000503&target=Peptidyl-prolyl+cis-trans+isomerase+FKBP1B&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50575646&enzyme=Peptidyl-prolyl+cis-trans+isomerase+FKBP1B&column=ki&startPg=0&Increment=50&submit=Search 164627258 471051769 1 MGVEIETISPGDGRTFPKKGQTCVVHYTGMLQNGKKFDSSRDRNKPFKFRIGKQEVIKGFEEGAAQMSLGQRAKLTCTPDVAYGATGHPGVIPPNATLIFDVELLNLE 1C9H,1FKK,1FKL,4C02,5HKG,5T15,5T9M,5T9N,5T9R,5T9S,5T9V,5TA3,5TAL,5TAM,5TAN,5TAP,5TAQ,5TAS,5TAT,5TAU,5TAV,5TAW,5TAX,5TAY,5TAZ,5TB0,5TB1,5TB2,5TB3,5TB4,6JGZ,6JH6,6JHN,6JI0,6JI8,6JII,6JIU,6JIY,6JRR,6JRS,6M2W,6PV6,6W1N,6WOT,6WOU,6WOV,6X32,6X33,6X34,6X35,6X36,7CF9,7JMF,7JMG,7JMH,7JMI,7JMJ,7M6A,7M6L,7T64,7T65,7U9Q,7U9R,7U9T,7U9X,7U9Z,7UA1,7UA3,7UA4,7UA5,7UA9,7VML,7VMM,7VMN,7VMO,7VMP,7VMQ,7VMR,7VMS,8DUJ,8DVE,8SEN,8SEO,8SEP,8SEQ,8SER,8SES,8SET Peptidyl-prolyl cis-trans isomerase FKBP1B FKB1B_HUMAN P68106 Q13664 Q16645 Q53TM2 Q9BQ40 51425109 COc1ccc(CC[C@H]2OC(=O)[C@@H]3CCCCN3C(=O)[C@@H](C3CCCCC3)c3cc(OC)c(OCCOc4cccc2c4)c(OC)c3)cc1OC InChI=1S/C41H51NO9/c1-45-34-19-17-27(23-35(34)46-2)16-18-33-29-13-10-14-31(24-29)49-21-22-50-39-36(47-3)25-30(26-37(39)48-4)38(28-11-6-5-7-12-28)40(43)42-20-9-8-15-32(42)41(44)51-33/h10,13-14,17,19,23-26,28,32-33,38H,5-9,11-12,15-16,18,20-22H2,1-4H3/t32-,33+,38-/m0/s1 HANZAPZKUAFCGC-YGCWAPBFSA-N 50575647 CHEMBL4856457 Peptidyl-prolyl cis-trans isomerase FKBP1B Homo sapiens 227 ChEMBL 10.1021/acs.jmedchem.0c02195 10.7270/Q2988BT3 33666419 Bauder, M; Meyners, C; Purder, PL; Merz, S; Sugiarto, WO; Voll, AM; Heymann, T; Hausch, F Technical University Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50575647 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50000503&target=Peptidyl-prolyl+cis-trans+isomerase+FKBP1B&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50575647&enzyme=Peptidyl-prolyl+cis-trans+isomerase+FKBP1B&column=ki&startPg=0&Increment=50&submit=Search S5W 7AWX 155817656 471051770 1 MGVEIETISPGDGRTFPKKGQTCVVHYTGMLQNGKKFDSSRDRNKPFKFRIGKQEVIKGFEEGAAQMSLGQRAKLTCTPDVAYGATGHPGVIPPNATLIFDVELLNLE 1C9H,1FKK,1FKL,4C02,5HKG,5T15,5T9M,5T9N,5T9R,5T9S,5T9V,5TA3,5TAL,5TAM,5TAN,5TAP,5TAQ,5TAS,5TAT,5TAU,5TAV,5TAW,5TAX,5TAY,5TAZ,5TB0,5TB1,5TB2,5TB3,5TB4,6JGZ,6JH6,6JHN,6JI0,6JI8,6JII,6JIU,6JIY,6JRR,6JRS,6M2W,6PV6,6W1N,6WOT,6WOU,6WOV,6X32,6X33,6X34,6X35,6X36,7CF9,7JMF,7JMG,7JMH,7JMI,7JMJ,7M6A,7M6L,7T64,7T65,7U9Q,7U9R,7U9T,7U9X,7U9Z,7UA1,7UA3,7UA4,7UA5,7UA9,7VML,7VMM,7VMN,7VMO,7VMP,7VMQ,7VMR,7VMS,8DUJ,8DVE,8SEN,8SEO,8SEP,8SEQ,8SER,8SES,8SET Peptidyl-prolyl cis-trans isomerase FKBP1B FKB1B_HUMAN P68106 Q13664 Q16645 Q53TM2 Q9BQ40 51425110 COc1ccc(CC[C@H]2OC(=O)[C@@H]3CCCCN3C(=O)[C@@H](C3CCCCC3)c3cc(OC)c(OCCCOc4cccc2c4)c(OC)c3)cc1OC InChI=1S/C42H53NO9/c1-46-35-20-18-28(24-36(35)47-2)17-19-34-30-14-10-15-32(25-30)50-22-11-23-51-40-37(48-3)26-31(27-38(40)49-4)39(29-12-6-5-7-13-29)41(44)43-21-9-8-16-33(43)42(45)52-34/h10,14-15,18,20,24-27,29,33-34,39H,5-9,11-13,16-17,19,21-23H2,1-4H3/t33-,34+,39-/m0/s1 YSZSLPRWNYBWRS-LSFNHRITSA-N 50575648 CHEMBL4848201 Peptidyl-prolyl cis-trans isomerase FKBP1B Homo sapiens 446 ChEMBL 10.1021/acs.jmedchem.0c02195 10.7270/Q2988BT3 33666419 Bauder, M; Meyners, C; Purder, PL; Merz, S; Sugiarto, WO; Voll, AM; Heymann, T; Hausch, F Technical University Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50575648 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50000503&target=Peptidyl-prolyl+cis-trans+isomerase+FKBP1B&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50575648&enzyme=Peptidyl-prolyl+cis-trans+isomerase+FKBP1B&column=ki&startPg=0&Increment=50&submit=Search R3B 7A6X 155817650 471051771 1 MGVEIETISPGDGRTFPKKGQTCVVHYTGMLQNGKKFDSSRDRNKPFKFRIGKQEVIKGFEEGAAQMSLGQRAKLTCTPDVAYGATGHPGVIPPNATLIFDVELLNLE 1C9H,1FKK,1FKL,4C02,5HKG,5T15,5T9M,5T9N,5T9R,5T9S,5T9V,5TA3,5TAL,5TAM,5TAN,5TAP,5TAQ,5TAS,5TAT,5TAU,5TAV,5TAW,5TAX,5TAY,5TAZ,5TB0,5TB1,5TB2,5TB3,5TB4,6JGZ,6JH6,6JHN,6JI0,6JI8,6JII,6JIU,6JIY,6JRR,6JRS,6M2W,6PV6,6W1N,6WOT,6WOU,6WOV,6X32,6X33,6X34,6X35,6X36,7CF9,7JMF,7JMG,7JMH,7JMI,7JMJ,7M6A,7M6L,7T64,7T65,7U9Q,7U9R,7U9T,7U9X,7U9Z,7UA1,7UA3,7UA4,7UA5,7UA9,7VML,7VMM,7VMN,7VMO,7VMP,7VMQ,7VMR,7VMS,8DUJ,8DVE,8SEN,8SEO,8SEP,8SEQ,8SER,8SES,8SET Peptidyl-prolyl cis-trans isomerase FKBP1B FKB1B_HUMAN P68106 Q13664 Q16645 Q53TM2 Q9BQ40 51425111 COc1ccc(CC[C@H]2OC(=O)[C@@H]3CCCCN3C(=O)[C@@H](C3CCCCC3)c3cc(OC)c(OC\C=C\COc4cccc2c4)c(OC)c3)cc1OC InChI=1S/C43H53NO9/c1-47-36-21-19-29(25-37(36)48-2)18-20-35-31-15-12-16-33(26-31)51-23-10-11-24-52-41-38(49-3)27-32(28-39(41)50-4)40(30-13-6-5-7-14-30)42(45)44-22-9-8-17-34(44)43(46)53-35/h10-12,15-16,19,21,25-28,30,34-35,40H,5-9,13-14,17-18,20,22-24H2,1-4H3/b11-10+/t34-,35+,40-/m0/s1 QGOZUOJTJYDDMS-YBMMQTEXSA-N 50575649 CHEMBL4875870 Peptidyl-prolyl cis-trans isomerase FKBP1B Homo sapiens 606 ChEMBL 10.1021/acs.jmedchem.0c02195 10.7270/Q2988BT3 33666419 Bauder, M; Meyners, C; Purder, PL; Merz, S; Sugiarto, WO; Voll, AM; Heymann, T; Hausch, F Technical University Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50575649 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50000503&target=Peptidyl-prolyl+cis-trans+isomerase+FKBP1B&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50575649&enzyme=Peptidyl-prolyl+cis-trans+isomerase+FKBP1B&column=ki&startPg=0&Increment=50&submit=Search 164627956 471051772 1 MGVEIETISPGDGRTFPKKGQTCVVHYTGMLQNGKKFDSSRDRNKPFKFRIGKQEVIKGFEEGAAQMSLGQRAKLTCTPDVAYGATGHPGVIPPNATLIFDVELLNLE 1C9H,1FKK,1FKL,4C02,5HKG,5T15,5T9M,5T9N,5T9R,5T9S,5T9V,5TA3,5TAL,5TAM,5TAN,5TAP,5TAQ,5TAS,5TAT,5TAU,5TAV,5TAW,5TAX,5TAY,5TAZ,5TB0,5TB1,5TB2,5TB3,5TB4,6JGZ,6JH6,6JHN,6JI0,6JI8,6JII,6JIU,6JIY,6JRR,6JRS,6M2W,6PV6,6W1N,6WOT,6WOU,6WOV,6X32,6X33,6X34,6X35,6X36,7CF9,7JMF,7JMG,7JMH,7JMI,7JMJ,7M6A,7M6L,7T64,7T65,7U9Q,7U9R,7U9T,7U9X,7U9Z,7UA1,7UA3,7UA4,7UA5,7UA9,7VML,7VMM,7VMN,7VMO,7VMP,7VMQ,7VMR,7VMS,8DUJ,8DVE,8SEN,8SEO,8SEP,8SEQ,8SER,8SES,8SET Peptidyl-prolyl cis-trans isomerase FKBP1B FKB1B_HUMAN P68106 Q13664 Q16645 Q53TM2 Q9BQ40 51425112 COc1ccc(CC[C@H]2OC(=O)[C@@H]3CCCCN3C(=O)[C@@H](C3CCCCC3)c3cc(OC)c(OC\C=C/COc4cccc2c4)c(OC)c3)cc1OC InChI=1S/C43H53NO9/c1-47-36-21-19-29(25-37(36)48-2)18-20-35-31-15-12-16-33(26-31)51-23-10-11-24-52-41-38(49-3)27-32(28-39(41)50-4)40(30-13-6-5-7-14-30)42(45)44-22-9-8-17-34(44)43(46)53-35/h10-12,15-16,19,21,25-28,30,34-35,40H,5-9,13-14,17-18,20,22-24H2,1-4H3/b11-10-/t34-,35+,40-/m0/s1 QGOZUOJTJYDDMS-LMRHAXCESA-N 50575650 CHEMBL4872122 Peptidyl-prolyl cis-trans isomerase FKBP1B Homo sapiens 658 ChEMBL 10.1021/acs.jmedchem.0c02195 10.7270/Q2988BT3 33666419 Bauder, M; Meyners, C; Purder, PL; Merz, S; Sugiarto, WO; Voll, AM; Heymann, T; Hausch, F Technical University Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50575650 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50000503&target=Peptidyl-prolyl+cis-trans+isomerase+FKBP1B&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50575650&enzyme=Peptidyl-prolyl+cis-trans+isomerase+FKBP1B&column=ki&startPg=0&Increment=50&submit=Search 164625262 471051773 1 MGVEIETISPGDGRTFPKKGQTCVVHYTGMLQNGKKFDSSRDRNKPFKFRIGKQEVIKGFEEGAAQMSLGQRAKLTCTPDVAYGATGHPGVIPPNATLIFDVELLNLE 1C9H,1FKK,1FKL,4C02,5HKG,5T15,5T9M,5T9N,5T9R,5T9S,5T9V,5TA3,5TAL,5TAM,5TAN,5TAP,5TAQ,5TAS,5TAT,5TAU,5TAV,5TAW,5TAX,5TAY,5TAZ,5TB0,5TB1,5TB2,5TB3,5TB4,6JGZ,6JH6,6JHN,6JI0,6JI8,6JII,6JIU,6JIY,6JRR,6JRS,6M2W,6PV6,6W1N,6WOT,6WOU,6WOV,6X32,6X33,6X34,6X35,6X36,7CF9,7JMF,7JMG,7JMH,7JMI,7JMJ,7M6A,7M6L,7T64,7T65,7U9Q,7U9R,7U9T,7U9X,7U9Z,7UA1,7UA3,7UA4,7UA5,7UA9,7VML,7VMM,7VMN,7VMO,7VMP,7VMQ,7VMR,7VMS,8DUJ,8DVE,8SEN,8SEO,8SEP,8SEQ,8SER,8SES,8SET Peptidyl-prolyl cis-trans isomerase FKBP1B FKB1B_HUMAN P68106 Q13664 Q16645 Q53TM2 Q9BQ40 51425113 COc1ccc(CC[C@H]2OC(=O)[C@@H]3CCCCN3C(=O)[C@@H](C3CCCCC3)c3cc(OC)c(OCCCCOc4cccc2c4)c(OC)c3)cc1OC InChI=1S/C43H55NO9/c1-47-36-21-19-29(25-37(36)48-2)18-20-35-31-15-12-16-33(26-31)51-23-10-11-24-52-41-38(49-3)27-32(28-39(41)50-4)40(30-13-6-5-7-14-30)42(45)44-22-9-8-17-34(44)43(46)53-35/h12,15-16,19,21,25-28,30,34-35,40H,5-11,13-14,17-18,20,22-24H2,1-4H3/t34-,35+,40-/m0/s1 RDJGELWAXUTIEU-TWBLSBBDSA-N 50575651 CHEMBL4863807 Peptidyl-prolyl cis-trans isomerase FKBP1B Homo sapiens 383 ChEMBL 10.1021/acs.jmedchem.0c02195 10.7270/Q2988BT3 33666419 Bauder, M; Meyners, C; Purder, PL; Merz, S; Sugiarto, WO; Voll, AM; Heymann, T; Hausch, F Technical University Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50575651 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50000503&target=Peptidyl-prolyl+cis-trans+isomerase+FKBP1B&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50575651&enzyme=Peptidyl-prolyl+cis-trans+isomerase+FKBP1B&column=ki&startPg=0&Increment=50&submit=Search 164624913 471051774 1 MGVEIETISPGDGRTFPKKGQTCVVHYTGMLQNGKKFDSSRDRNKPFKFRIGKQEVIKGFEEGAAQMSLGQRAKLTCTPDVAYGATGHPGVIPPNATLIFDVELLNLE 1C9H,1FKK,1FKL,4C02,5HKG,5T15,5T9M,5T9N,5T9R,5T9S,5T9V,5TA3,5TAL,5TAM,5TAN,5TAP,5TAQ,5TAS,5TAT,5TAU,5TAV,5TAW,5TAX,5TAY,5TAZ,5TB0,5TB1,5TB2,5TB3,5TB4,6JGZ,6JH6,6JHN,6JI0,6JI8,6JII,6JIU,6JIY,6JRR,6JRS,6M2W,6PV6,6W1N,6WOT,6WOU,6WOV,6X32,6X33,6X34,6X35,6X36,7CF9,7JMF,7JMG,7JMH,7JMI,7JMJ,7M6A,7M6L,7T64,7T65,7U9Q,7U9R,7U9T,7U9X,7U9Z,7UA1,7UA3,7UA4,7UA5,7UA9,7VML,7VMM,7VMN,7VMO,7VMP,7VMQ,7VMR,7VMS,8DUJ,8DVE,8SEN,8SEO,8SEP,8SEQ,8SER,8SES,8SET Peptidyl-prolyl cis-trans isomerase FKBP1B FKB1B_HUMAN P68106 Q13664 Q16645 Q53TM2 Q9BQ40 51425114 COc1ccc(CC[C@H]2OC(=O)[C@@H]3CCCCN3C(=O)[C@@H](C3CCCCC3)c3cc(OC)c(OCCC(=O)COc4cccc2c4)c(OC)c3)cc1OC InChI=1S/C43H53NO10/c1-48-36-19-17-28(23-37(36)49-2)16-18-35-30-13-10-14-33(24-30)53-27-32(45)20-22-52-41-38(50-3)25-31(26-39(41)51-4)40(29-11-6-5-7-12-29)42(46)44-21-9-8-15-34(44)43(47)54-35/h10,13-14,17,19,23-26,29,34-35,40H,5-9,11-12,15-16,18,20-22,27H2,1-4H3/t34-,35+,40-/m0/s1 CQYMGEZWICPCQG-TWBLSBBDSA-N 50575652 CHEMBL4878890 Peptidyl-prolyl cis-trans isomerase FKBP1B Homo sapiens 38 ChEMBL 10.1021/acs.jmedchem.0c02195 10.7270/Q2988BT3 33666419 Bauder, M; Meyners, C; Purder, PL; Merz, S; Sugiarto, WO; Voll, AM; Heymann, T; Hausch, F Technical University Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50575652 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50000503&target=Peptidyl-prolyl+cis-trans+isomerase+FKBP1B&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50575652&enzyme=Peptidyl-prolyl+cis-trans+isomerase+FKBP1B&column=ki&startPg=0&Increment=50&submit=Search 164627324 471051775 1 MGVEIETISPGDGRTFPKKGQTCVVHYTGMLQNGKKFDSSRDRNKPFKFRIGKQEVIKGFEEGAAQMSLGQRAKLTCTPDVAYGATGHPGVIPPNATLIFDVELLNLE 1C9H,1FKK,1FKL,4C02,5HKG,5T15,5T9M,5T9N,5T9R,5T9S,5T9V,5TA3,5TAL,5TAM,5TAN,5TAP,5TAQ,5TAS,5TAT,5TAU,5TAV,5TAW,5TAX,5TAY,5TAZ,5TB0,5TB1,5TB2,5TB3,5TB4,6JGZ,6JH6,6JHN,6JI0,6JI8,6JII,6JIU,6JIY,6JRR,6JRS,6M2W,6PV6,6W1N,6WOT,6WOU,6WOV,6X32,6X33,6X34,6X35,6X36,7CF9,7JMF,7JMG,7JMH,7JMI,7JMJ,7M6A,7M6L,7T64,7T65,7U9Q,7U9R,7U9T,7U9X,7U9Z,7UA1,7UA3,7UA4,7UA5,7UA9,7VML,7VMM,7VMN,7VMO,7VMP,7VMQ,7VMR,7VMS,8DUJ,8DVE,8SEN,8SEO,8SEP,8SEQ,8SER,8SES,8SET Peptidyl-prolyl cis-trans isomerase FKBP1B FKB1B_HUMAN P68106 Q13664 Q16645 Q53TM2 Q9BQ40 51425115 COc1ccc(CC[C@H]2OC(=O)[C@@H]3CCCCN3C(=O)[C@@H](C3CCCCC3)c3cc(OC)c(OCC(O)C(O)COc4cccc2c4)c(OC)c3)cc1OC InChI=1S/C43H55NO11/c1-49-36-19-17-27(21-37(36)50-2)16-18-35-29-13-10-14-31(22-29)53-25-33(45)34(46)26-54-41-38(51-3)23-30(24-39(41)52-4)40(28-11-6-5-7-12-28)42(47)44-20-9-8-15-32(44)43(48)55-35/h10,13-14,17,19,21-24,28,32-35,40,45-46H,5-9,11-12,15-16,18,20,25-26H2,1-4H3/t32-,33?,34?,35+,40-/m0/s1 PBDSFPLSNACCRE-QQIJZFFGSA-N 50575653 CHEMBL4856956 Peptidyl-prolyl cis-trans isomerase FKBP1B Homo sapiens 85 ChEMBL 10.1021/acs.jmedchem.0c02195 10.7270/Q2988BT3 33666419 Bauder, M; Meyners, C; Purder, PL; Merz, S; Sugiarto, WO; Voll, AM; Heymann, T; Hausch, F Technical University Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50575653 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50000503&target=Peptidyl-prolyl+cis-trans+isomerase+FKBP1B&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50575653&enzyme=Peptidyl-prolyl+cis-trans+isomerase+FKBP1B&column=ki&startPg=0&Increment=50&submit=Search 164613576 471051776 1 MGVEIETISPGDGRTFPKKGQTCVVHYTGMLQNGKKFDSSRDRNKPFKFRIGKQEVIKGFEEGAAQMSLGQRAKLTCTPDVAYGATGHPGVIPPNATLIFDVELLNLE 1C9H,1FKK,1FKL,4C02,5HKG,5T15,5T9M,5T9N,5T9R,5T9S,5T9V,5TA3,5TAL,5TAM,5TAN,5TAP,5TAQ,5TAS,5TAT,5TAU,5TAV,5TAW,5TAX,5TAY,5TAZ,5TB0,5TB1,5TB2,5TB3,5TB4,6JGZ,6JH6,6JHN,6JI0,6JI8,6JII,6JIU,6JIY,6JRR,6JRS,6M2W,6PV6,6W1N,6WOT,6WOU,6WOV,6X32,6X33,6X34,6X35,6X36,7CF9,7JMF,7JMG,7JMH,7JMI,7JMJ,7M6A,7M6L,7T64,7T65,7U9Q,7U9R,7U9T,7U9X,7U9Z,7UA1,7UA3,7UA4,7UA5,7UA9,7VML,7VMM,7VMN,7VMO,7VMP,7VMQ,7VMR,7VMS,8DUJ,8DVE,8SEN,8SEO,8SEP,8SEQ,8SER,8SES,8SET Peptidyl-prolyl cis-trans isomerase FKBP1B FKB1B_HUMAN P68106 Q13664 Q16645 Q53TM2 Q9BQ40 51425116 COc1ccc(CC[C@H]2OC(=O)[C@@H]3CCCCN3C(=O)[C@@H](C3CCCCC3)c3cc(OC)c(OCC\C=C\COc4cccc2c4)c(OC)c3)cc1OC InChI=1S/C44H55NO9/c1-48-37-22-20-30(26-38(37)49-2)19-21-36-32-16-13-17-34(27-32)52-24-11-6-12-25-53-42-39(50-3)28-33(29-40(42)51-4)41(31-14-7-5-8-15-31)43(46)45-23-10-9-18-35(45)44(47)54-36/h6,11,13,16-17,20,22,26-29,31,35-36,41H,5,7-10,12,14-15,18-19,21,23-25H2,1-4H3/b11-6+/t35-,36+,41-/m0/s1 CJICCQJQZUCWHW-LCWXHYGYSA-N 50575654 CHEMBL4867024 Peptidyl-prolyl cis-trans isomerase FKBP1B Homo sapiens 1075 ChEMBL 10.1021/acs.jmedchem.0c02195 10.7270/Q2988BT3 33666419 Bauder, M; Meyners, C; Purder, PL; Merz, S; Sugiarto, WO; Voll, AM; Heymann, T; Hausch, F Technical University Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50575654 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50000503&target=Peptidyl-prolyl+cis-trans+isomerase+FKBP1B&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50575654&enzyme=Peptidyl-prolyl+cis-trans+isomerase+FKBP1B&column=ki&startPg=0&Increment=50&submit=Search 164620950 471051777 1 MGVEIETISPGDGRTFPKKGQTCVVHYTGMLQNGKKFDSSRDRNKPFKFRIGKQEVIKGFEEGAAQMSLGQRAKLTCTPDVAYGATGHPGVIPPNATLIFDVELLNLE 1C9H,1FKK,1FKL,4C02,5HKG,5T15,5T9M,5T9N,5T9R,5T9S,5T9V,5TA3,5TAL,5TAM,5TAN,5TAP,5TAQ,5TAS,5TAT,5TAU,5TAV,5TAW,5TAX,5TAY,5TAZ,5TB0,5TB1,5TB2,5TB3,5TB4,6JGZ,6JH6,6JHN,6JI0,6JI8,6JII,6JIU,6JIY,6JRR,6JRS,6M2W,6PV6,6W1N,6WOT,6WOU,6WOV,6X32,6X33,6X34,6X35,6X36,7CF9,7JMF,7JMG,7JMH,7JMI,7JMJ,7M6A,7M6L,7T64,7T65,7U9Q,7U9R,7U9T,7U9X,7U9Z,7UA1,7UA3,7UA4,7UA5,7UA9,7VML,7VMM,7VMN,7VMO,7VMP,7VMQ,7VMR,7VMS,8DUJ,8DVE,8SEN,8SEO,8SEP,8SEQ,8SER,8SES,8SET Peptidyl-prolyl cis-trans isomerase FKBP1B FKB1B_HUMAN P68106 Q13664 Q16645 Q53TM2 Q9BQ40 51425117 COc1ccc(CC[C@H]2OC(=O)[C@@H]3CCCCN3C(=O)[C@@H](C3CCCCC3)c3cc(OC)c(OCC\C=C/COc4cccc2c4)c(OC)c3)cc1OC InChI=1S/C44H55NO9/c1-48-37-22-20-30(26-38(37)49-2)19-21-36-32-16-13-17-34(27-32)52-24-11-6-12-25-53-42-39(50-3)28-33(29-40(42)51-4)41(31-14-7-5-8-15-31)43(46)45-23-10-9-18-35(45)44(47)54-36/h6,11,13,16-17,20,22,26-29,31,35-36,41H,5,7-10,12,14-15,18-19,21,23-25H2,1-4H3/b11-6-/t35-,36+,41-/m0/s1 CJICCQJQZUCWHW-GTKPNJOPSA-N 50575655 CHEMBL4863883 Peptidyl-prolyl cis-trans isomerase FKBP1B Homo sapiens 495 ChEMBL 10.1021/acs.jmedchem.0c02195 10.7270/Q2988BT3 33666419 Bauder, M; Meyners, C; Purder, PL; Merz, S; Sugiarto, WO; Voll, AM; Heymann, T; Hausch, F Technical University Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50575655 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50000503&target=Peptidyl-prolyl+cis-trans+isomerase+FKBP1B&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50575655&enzyme=Peptidyl-prolyl+cis-trans+isomerase+FKBP1B&column=ki&startPg=0&Increment=50&submit=Search 164622640 471051778 1 MGVEIETISPGDGRTFPKKGQTCVVHYTGMLQNGKKFDSSRDRNKPFKFRIGKQEVIKGFEEGAAQMSLGQRAKLTCTPDVAYGATGHPGVIPPNATLIFDVELLNLE 1C9H,1FKK,1FKL,4C02,5HKG,5T15,5T9M,5T9N,5T9R,5T9S,5T9V,5TA3,5TAL,5TAM,5TAN,5TAP,5TAQ,5TAS,5TAT,5TAU,5TAV,5TAW,5TAX,5TAY,5TAZ,5TB0,5TB1,5TB2,5TB3,5TB4,6JGZ,6JH6,6JHN,6JI0,6JI8,6JII,6JIU,6JIY,6JRR,6JRS,6M2W,6PV6,6W1N,6WOT,6WOU,6WOV,6X32,6X33,6X34,6X35,6X36,7CF9,7JMF,7JMG,7JMH,7JMI,7JMJ,7M6A,7M6L,7T64,7T65,7U9Q,7U9R,7U9T,7U9X,7U9Z,7UA1,7UA3,7UA4,7UA5,7UA9,7VML,7VMM,7VMN,7VMO,7VMP,7VMQ,7VMR,7VMS,8DUJ,8DVE,8SEN,8SEO,8SEP,8SEQ,8SER,8SES,8SET Peptidyl-prolyl cis-trans isomerase FKBP1B FKB1B_HUMAN P68106 Q13664 Q16645 Q53TM2 Q9BQ40 51425118 COc1ccc(CC[C@H]2OC(=O)[C@@H]3CCCCN3C(=O)[C@@H](C3CCCCC3)c3cc(OC)c(OCCCCCOc4cccc2c4)c(OC)c3)cc1OC InChI=1S/C44H57NO9/c1-48-37-22-20-30(26-38(37)49-2)19-21-36-32-16-13-17-34(27-32)52-24-11-6-12-25-53-42-39(50-3)28-33(29-40(42)51-4)41(31-14-7-5-8-15-31)43(46)45-23-10-9-18-35(45)44(47)54-36/h13,16-17,20,22,26-29,31,35-36,41H,5-12,14-15,18-19,21,23-25H2,1-4H3/t35-,36+,41-/m0/s1 JOZMVUXPQMRQOL-KLBQNTFLSA-N 50575656 CHEMBL4863758 Peptidyl-prolyl cis-trans isomerase FKBP1B Homo sapiens 849 ChEMBL 10.1021/acs.jmedchem.0c02195 10.7270/Q2988BT3 33666419 Bauder, M; Meyners, C; Purder, PL; Merz, S; Sugiarto, WO; Voll, AM; Heymann, T; Hausch, F Technical University Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50575656 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50000503&target=Peptidyl-prolyl+cis-trans+isomerase+FKBP1B&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50575656&enzyme=Peptidyl-prolyl+cis-trans+isomerase+FKBP1B&column=ki&startPg=0&Increment=50&submit=Search 164622636 471051779 1 MGVEIETISPGDGRTFPKKGQTCVVHYTGMLQNGKKFDSSRDRNKPFKFRIGKQEVIKGFEEGAAQMSLGQRAKLTCTPDVAYGATGHPGVIPPNATLIFDVELLNLE 1C9H,1FKK,1FKL,4C02,5HKG,5T15,5T9M,5T9N,5T9R,5T9S,5T9V,5TA3,5TAL,5TAM,5TAN,5TAP,5TAQ,5TAS,5TAT,5TAU,5TAV,5TAW,5TAX,5TAY,5TAZ,5TB0,5TB1,5TB2,5TB3,5TB4,6JGZ,6JH6,6JHN,6JI0,6JI8,6JII,6JIU,6JIY,6JRR,6JRS,6M2W,6PV6,6W1N,6WOT,6WOU,6WOV,6X32,6X33,6X34,6X35,6X36,7CF9,7JMF,7JMG,7JMH,7JMI,7JMJ,7M6A,7M6L,7T64,7T65,7U9Q,7U9R,7U9T,7U9X,7U9Z,7UA1,7UA3,7UA4,7UA5,7UA9,7VML,7VMM,7VMN,7VMO,7VMP,7VMQ,7VMR,7VMS,8DUJ,8DVE,8SEN,8SEO,8SEP,8SEQ,8SER,8SES,8SET Peptidyl-prolyl cis-trans isomerase FKBP1B FKB1B_HUMAN P68106 Q13664 Q16645 Q53TM2 Q9BQ40 51425119 COc1ccc(CC[C@H]2OC(=O)[C@@H]3CCCCN3C(=O)[C@@H](C3CCCCC3)c3cc(OC)c(OCCOC\C=C\COc4cccc2c4)c(OC)c3)cc1OC InChI=1S/C45H57NO10/c1-49-38-21-19-31(27-39(38)50-2)18-20-37-33-15-12-16-35(28-33)54-24-11-10-23-53-25-26-55-43-40(51-3)29-34(30-41(43)52-4)42(32-13-6-5-7-14-32)44(47)46-22-9-8-17-36(46)45(48)56-37/h10-12,15-16,19,21,27-30,32,36-37,42H,5-9,13-14,17-18,20,22-26H2,1-4H3/b11-10+/t36-,37+,42-/m0/s1 MDPYBQRKSBXYSJ-SGYAFFFDSA-N 50575657 CHEMBL4866065 Peptidyl-prolyl cis-trans isomerase FKBP1B Homo sapiens 715 ChEMBL 10.1021/acs.jmedchem.0c02195 10.7270/Q2988BT3 33666419 Bauder, M; Meyners, C; Purder, PL; Merz, S; Sugiarto, WO; Voll, AM; Heymann, T; Hausch, F Technical University Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50575657 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50000503&target=Peptidyl-prolyl+cis-trans+isomerase+FKBP1B&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50575657&enzyme=Peptidyl-prolyl+cis-trans+isomerase+FKBP1B&column=ki&startPg=0&Increment=50&submit=Search 164621395 471051780 1 MGVEIETISPGDGRTFPKKGQTCVVHYTGMLQNGKKFDSSRDRNKPFKFRIGKQEVIKGFEEGAAQMSLGQRAKLTCTPDVAYGATGHPGVIPPNATLIFDVELLNLE 1C9H,1FKK,1FKL,4C02,5HKG,5T15,5T9M,5T9N,5T9R,5T9S,5T9V,5TA3,5TAL,5TAM,5TAN,5TAP,5TAQ,5TAS,5TAT,5TAU,5TAV,5TAW,5TAX,5TAY,5TAZ,5TB0,5TB1,5TB2,5TB3,5TB4,6JGZ,6JH6,6JHN,6JI0,6JI8,6JII,6JIU,6JIY,6JRR,6JRS,6M2W,6PV6,6W1N,6WOT,6WOU,6WOV,6X32,6X33,6X34,6X35,6X36,7CF9,7JMF,7JMG,7JMH,7JMI,7JMJ,7M6A,7M6L,7T64,7T65,7U9Q,7U9R,7U9T,7U9X,7U9Z,7UA1,7UA3,7UA4,7UA5,7UA9,7VML,7VMM,7VMN,7VMO,7VMP,7VMQ,7VMR,7VMS,8DUJ,8DVE,8SEN,8SEO,8SEP,8SEQ,8SER,8SES,8SET Peptidyl-prolyl cis-trans isomerase FKBP1B FKB1B_HUMAN P68106 Q13664 Q16645 Q53TM2 Q9BQ40 51425120 COc1ccc(CC[C@H]2OC(=O)[C@@H]3CCCCN3C(=O)[C@@H](C3CCCCC3)c3cc(OC)c(OCCOC\C=C/COc4cccc2c4)c(OC)c3)cc1OC InChI=1S/C45H57NO10/c1-49-38-21-19-31(27-39(38)50-2)18-20-37-33-15-12-16-35(28-33)54-24-11-10-23-53-25-26-55-43-40(51-3)29-34(30-41(43)52-4)42(32-13-6-5-7-14-32)44(47)46-22-9-8-17-36(46)45(48)56-37/h10-12,15-16,19,21,27-30,32,36-37,42H,5-9,13-14,17-18,20,22-26H2,1-4H3/b11-10-/t36-,37+,42-/m0/s1 MDPYBQRKSBXYSJ-QCXYFFPESA-N 50575658 CHEMBL4860544 Peptidyl-prolyl cis-trans isomerase FKBP1B Homo sapiens 344 ChEMBL 10.1021/acs.jmedchem.0c02195 10.7270/Q2988BT3 33666419 Bauder, M; Meyners, C; Purder, PL; Merz, S; Sugiarto, WO; Voll, AM; Heymann, T; Hausch, F Technical University Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50575658 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50000503&target=Peptidyl-prolyl+cis-trans+isomerase+FKBP1B&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50575658&enzyme=Peptidyl-prolyl+cis-trans+isomerase+FKBP1B&column=ki&startPg=0&Increment=50&submit=Search R3E 7A6W 155817649 471051781 1 MGVEIETISPGDGRTFPKKGQTCVVHYTGMLQNGKKFDSSRDRNKPFKFRIGKQEVIKGFEEGAAQMSLGQRAKLTCTPDVAYGATGHPGVIPPNATLIFDVELLNLE 1C9H,1FKK,1FKL,4C02,5HKG,5T15,5T9M,5T9N,5T9R,5T9S,5T9V,5TA3,5TAL,5TAM,5TAN,5TAP,5TAQ,5TAS,5TAT,5TAU,5TAV,5TAW,5TAX,5TAY,5TAZ,5TB0,5TB1,5TB2,5TB3,5TB4,6JGZ,6JH6,6JHN,6JI0,6JI8,6JII,6JIU,6JIY,6JRR,6JRS,6M2W,6PV6,6W1N,6WOT,6WOU,6WOV,6X32,6X33,6X34,6X35,6X36,7CF9,7JMF,7JMG,7JMH,7JMI,7JMJ,7M6A,7M6L,7T64,7T65,7U9Q,7U9R,7U9T,7U9X,7U9Z,7UA1,7UA3,7UA4,7UA5,7UA9,7VML,7VMM,7VMN,7VMO,7VMP,7VMQ,7VMR,7VMS,8DUJ,8DVE,8SEN,8SEO,8SEP,8SEQ,8SER,8SES,8SET Peptidyl-prolyl cis-trans isomerase FKBP1B FKB1B_HUMAN P68106 Q13664 Q16645 Q53TM2 Q9BQ40 51425121 COc1ccc(CC[C@H]2OC(=O)[C@@H]3CCCCN3C(=O)[C@@H](C3CCCCC3)c3cc(OC)c(OCCOCCCCOc4cccc2c4)c(OC)c3)cc1OC InChI=1S/C45H59NO10/c1-49-38-21-19-31(27-39(38)50-2)18-20-37-33-15-12-16-35(28-33)54-24-11-10-23-53-25-26-55-43-40(51-3)29-34(30-41(43)52-4)42(32-13-6-5-7-14-32)44(47)46-22-9-8-17-36(46)45(48)56-37/h12,15-16,19,21,27-30,32,36-37,42H,5-11,13-14,17-18,20,22-26H2,1-4H3/t36-,37+,42-/m0/s1 GWVGANOCGSMMAJ-FMXQOUBESA-N 50575659 CHEMBL4874574 Peptidyl-prolyl cis-trans isomerase FKBP1B Homo sapiens 429 ChEMBL 10.1021/acs.jmedchem.0c02195 10.7270/Q2988BT3 33666419 Bauder, M; Meyners, C; Purder, PL; Merz, S; Sugiarto, WO; Voll, AM; Heymann, T; Hausch, F Technical University Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50575659 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50000503&target=Peptidyl-prolyl+cis-trans+isomerase+FKBP1B&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50575659&enzyme=Peptidyl-prolyl+cis-trans+isomerase+FKBP1B&column=ki&startPg=0&Increment=50&submit=Search 164627601 471051782 1 MGVEIETISPGDGRTFPKKGQTCVVHYTGMLQNGKKFDSSRDRNKPFKFRIGKQEVIKGFEEGAAQMSLGQRAKLTCTPDVAYGATGHPGVIPPNATLIFDVELLNLE 1C9H,1FKK,1FKL,4C02,5HKG,5T15,5T9M,5T9N,5T9R,5T9S,5T9V,5TA3,5TAL,5TAM,5TAN,5TAP,5TAQ,5TAS,5TAT,5TAU,5TAV,5TAW,5TAX,5TAY,5TAZ,5TB0,5TB1,5TB2,5TB3,5TB4,6JGZ,6JH6,6JHN,6JI0,6JI8,6JII,6JIU,6JIY,6JRR,6JRS,6M2W,6PV6,6W1N,6WOT,6WOU,6WOV,6X32,6X33,6X34,6X35,6X36,7CF9,7JMF,7JMG,7JMH,7JMI,7JMJ,7M6A,7M6L,7T64,7T65,7U9Q,7U9R,7U9T,7U9X,7U9Z,7UA1,7UA3,7UA4,7UA5,7UA9,7VML,7VMM,7VMN,7VMO,7VMP,7VMQ,7VMR,7VMS,8DUJ,8DVE,8SEN,8SEO,8SEP,8SEQ,8SER,8SES,8SET Peptidyl-prolyl cis-trans isomerase FKBP1B FKB1B_HUMAN P68106 Q13664 Q16645 Q53TM2 Q9BQ40 51425122 COc1ccc(CC[C@H]2OC(=O)[C@@H]3CCCCN3C(=O)[C@@H](C3CCCCC3)c3cc(OC)c(OCCCOC\C=C\COc4cccc2c4)c(OC)c3)cc1OC InChI=1S/C46H59NO10/c1-50-39-22-20-32(28-40(39)51-2)19-21-38-34-16-12-17-36(29-34)55-26-11-10-24-54-25-13-27-56-44-41(52-3)30-35(31-42(44)53-4)43(33-14-6-5-7-15-33)45(48)47-23-9-8-18-37(47)46(49)57-38/h10-12,16-17,20,22,28-31,33,37-38,43H,5-9,13-15,18-19,21,23-27H2,1-4H3/b11-10+/t37-,38+,43-/m0/s1 WMULMJBGRBWPBD-HGTNHFRLSA-N 50575660 CHEMBL4855135 Peptidyl-prolyl cis-trans isomerase FKBP1B Homo sapiens 335 ChEMBL 10.1021/acs.jmedchem.0c02195 10.7270/Q2988BT3 33666419 Bauder, M; Meyners, C; Purder, PL; Merz, S; Sugiarto, WO; Voll, AM; Heymann, T; Hausch, F Technical University Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50575660 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50000503&target=Peptidyl-prolyl+cis-trans+isomerase+FKBP1B&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50575660&enzyme=Peptidyl-prolyl+cis-trans+isomerase+FKBP1B&column=ki&startPg=0&Increment=50&submit=Search 164612360 471051783 1 MGVEIETISPGDGRTFPKKGQTCVVHYTGMLQNGKKFDSSRDRNKPFKFRIGKQEVIKGFEEGAAQMSLGQRAKLTCTPDVAYGATGHPGVIPPNATLIFDVELLNLE 1C9H,1FKK,1FKL,4C02,5HKG,5T15,5T9M,5T9N,5T9R,5T9S,5T9V,5TA3,5TAL,5TAM,5TAN,5TAP,5TAQ,5TAS,5TAT,5TAU,5TAV,5TAW,5TAX,5TAY,5TAZ,5TB0,5TB1,5TB2,5TB3,5TB4,6JGZ,6JH6,6JHN,6JI0,6JI8,6JII,6JIU,6JIY,6JRR,6JRS,6M2W,6PV6,6W1N,6WOT,6WOU,6WOV,6X32,6X33,6X34,6X35,6X36,7CF9,7JMF,7JMG,7JMH,7JMI,7JMJ,7M6A,7M6L,7T64,7T65,7U9Q,7U9R,7U9T,7U9X,7U9Z,7UA1,7UA3,7UA4,7UA5,7UA9,7VML,7VMM,7VMN,7VMO,7VMP,7VMQ,7VMR,7VMS,8DUJ,8DVE,8SEN,8SEO,8SEP,8SEQ,8SER,8SES,8SET Peptidyl-prolyl cis-trans isomerase FKBP1B FKB1B_HUMAN P68106 Q13664 Q16645 Q53TM2 Q9BQ40 51425123 COc1ccc(CC[C@H]2OC(=O)[C@@H]3CCCCN3C(=O)[C@@H](C3CCCCC3)c3cc(OC)c(OCCCOCCCCOc4cccc2c4)c(OC)c3)cc1OC InChI=1S/C46H61NO10/c1-50-39-22-20-32(28-40(39)51-2)19-21-38-34-16-12-17-36(29-34)55-26-11-10-24-54-25-13-27-56-44-41(52-3)30-35(31-42(44)53-4)43(33-14-6-5-7-15-33)45(48)47-23-9-8-18-37(47)46(49)57-38/h12,16-17,20,22,28-31,33,37-38,43H,5-11,13-15,18-19,21,23-27H2,1-4H3/t37-,38+,43-/m0/s1 JLQNKNFGAZQZLQ-FDHYQTMZSA-N 50575661 CHEMBL4853042 Peptidyl-prolyl cis-trans isomerase FKBP1B Homo sapiens 277 ChEMBL 10.1021/acs.jmedchem.0c02195 10.7270/Q2988BT3 33666419 Bauder, M; Meyners, C; Purder, PL; Merz, S; Sugiarto, WO; Voll, AM; Heymann, T; Hausch, F Technical University Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50575661 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50000503&target=Peptidyl-prolyl+cis-trans+isomerase+FKBP1B&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50575661&enzyme=Peptidyl-prolyl+cis-trans+isomerase+FKBP1B&column=ki&startPg=0&Increment=50&submit=Search 164617421 471051784 1 MGVEIETISPGDGRTFPKKGQTCVVHYTGMLQNGKKFDSSRDRNKPFKFRIGKQEVIKGFEEGAAQMSLGQRAKLTCTPDVAYGATGHPGVIPPNATLIFDVELLNLE 1C9H,1FKK,1FKL,4C02,5HKG,5T15,5T9M,5T9N,5T9R,5T9S,5T9V,5TA3,5TAL,5TAM,5TAN,5TAP,5TAQ,5TAS,5TAT,5TAU,5TAV,5TAW,5TAX,5TAY,5TAZ,5TB0,5TB1,5TB2,5TB3,5TB4,6JGZ,6JH6,6JHN,6JI0,6JI8,6JII,6JIU,6JIY,6JRR,6JRS,6M2W,6PV6,6W1N,6WOT,6WOU,6WOV,6X32,6X33,6X34,6X35,6X36,7CF9,7JMF,7JMG,7JMH,7JMI,7JMJ,7M6A,7M6L,7T64,7T65,7U9Q,7U9R,7U9T,7U9X,7U9Z,7UA1,7UA3,7UA4,7UA5,7UA9,7VML,7VMM,7VMN,7VMO,7VMP,7VMQ,7VMR,7VMS,8DUJ,8DVE,8SEN,8SEO,8SEP,8SEQ,8SER,8SES,8SET Peptidyl-prolyl cis-trans isomerase FKBP1B FKB1B_HUMAN P68106 Q13664 Q16645 Q53TM2 Q9BQ40 51425124 COc1ccc(CC[C@H]2OC(=O)[C@@H]3CCCCN3C(=O)[C@@H](C3CCCCC3)c3cc(OC)c(OC)c(OCCOc4cccc2c4)c3)cc1OC InChI=1S/C41H51NO9/c1-45-34-19-17-27(23-35(34)46-2)16-18-33-29-13-10-14-31(24-29)49-21-22-50-37-26-30(25-36(47-3)39(37)48-4)38(28-11-6-5-7-12-28)40(43)42-20-9-8-15-32(42)41(44)51-33/h10,13-14,17,19,23-26,28,32-33,38H,5-9,11-12,15-16,18,20-22H2,1-4H3/t32-,33+,38-/m0/s1 CIIGIQJIDFAGKZ-YGCWAPBFSA-N 50575662 CHEMBL4859741 Peptidyl-prolyl cis-trans isomerase FKBP1B Homo sapiens 82 ChEMBL 10.1021/acs.jmedchem.0c02195 10.7270/Q2988BT3 33666419 Bauder, M; Meyners, C; Purder, PL; Merz, S; Sugiarto, WO; Voll, AM; Heymann, T; Hausch, F Technical University Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50575662 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50000503&target=Peptidyl-prolyl+cis-trans+isomerase+FKBP1B&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50575662&enzyme=Peptidyl-prolyl+cis-trans+isomerase+FKBP1B&column=ki&startPg=0&Increment=50&submit=Search 164614280 471051785 1 MGVEIETISPGDGRTFPKKGQTCVVHYTGMLQNGKKFDSSRDRNKPFKFRIGKQEVIKGFEEGAAQMSLGQRAKLTCTPDVAYGATGHPGVIPPNATLIFDVELLNLE 1C9H,1FKK,1FKL,4C02,5HKG,5T15,5T9M,5T9N,5T9R,5T9S,5T9V,5TA3,5TAL,5TAM,5TAN,5TAP,5TAQ,5TAS,5TAT,5TAU,5TAV,5TAW,5TAX,5TAY,5TAZ,5TB0,5TB1,5TB2,5TB3,5TB4,6JGZ,6JH6,6JHN,6JI0,6JI8,6JII,6JIU,6JIY,6JRR,6JRS,6M2W,6PV6,6W1N,6WOT,6WOU,6WOV,6X32,6X33,6X34,6X35,6X36,7CF9,7JMF,7JMG,7JMH,7JMI,7JMJ,7M6A,7M6L,7T64,7T65,7U9Q,7U9R,7U9T,7U9X,7U9Z,7UA1,7UA3,7UA4,7UA5,7UA9,7VML,7VMM,7VMN,7VMO,7VMP,7VMQ,7VMR,7VMS,8DUJ,8DVE,8SEN,8SEO,8SEP,8SEQ,8SER,8SES,8SET Peptidyl-prolyl cis-trans isomerase FKBP1B FKB1B_HUMAN P68106 Q13664 Q16645 Q53TM2 Q9BQ40 51425125 COc1ccc(CC[C@H]2OC(=O)[C@@H]3CCCCN3C(=O)[C@@H](C3CCCCC3)c3cc(OC)c(OC)c(OCCCOc4cccc2c4)c3)cc1OC InChI=1S/C42H53NO9/c1-46-35-20-18-28(24-36(35)47-2)17-19-34-30-14-10-15-32(25-30)50-22-11-23-51-38-27-31(26-37(48-3)40(38)49-4)39(29-12-6-5-7-13-29)41(44)43-21-9-8-16-33(43)42(45)52-34/h10,14-15,18,20,24-27,29,33-34,39H,5-9,11-13,16-17,19,21-23H2,1-4H3/t33-,34+,39-/m0/s1 GWXXZRRJFTVQCB-LSFNHRITSA-N 50575663 CHEMBL4879078 Peptidyl-prolyl cis-trans isomerase FKBP1B Homo sapiens 94 ChEMBL 10.1021/acs.jmedchem.0c02195 10.7270/Q2988BT3 33666419 Bauder, M; Meyners, C; Purder, PL; Merz, S; Sugiarto, WO; Voll, AM; Heymann, T; Hausch, F Technical University Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50575663 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50000503&target=Peptidyl-prolyl+cis-trans+isomerase+FKBP1B&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50575663&enzyme=Peptidyl-prolyl+cis-trans+isomerase+FKBP1B&column=ki&startPg=0&Increment=50&submit=Search 164626424 471051786 1 MGVEIETISPGDGRTFPKKGQTCVVHYTGMLQNGKKFDSSRDRNKPFKFRIGKQEVIKGFEEGAAQMSLGQRAKLTCTPDVAYGATGHPGVIPPNATLIFDVELLNLE 1C9H,1FKK,1FKL,4C02,5HKG,5T15,5T9M,5T9N,5T9R,5T9S,5T9V,5TA3,5TAL,5TAM,5TAN,5TAP,5TAQ,5TAS,5TAT,5TAU,5TAV,5TAW,5TAX,5TAY,5TAZ,5TB0,5TB1,5TB2,5TB3,5TB4,6JGZ,6JH6,6JHN,6JI0,6JI8,6JII,6JIU,6JIY,6JRR,6JRS,6M2W,6PV6,6W1N,6WOT,6WOU,6WOV,6X32,6X33,6X34,6X35,6X36,7CF9,7JMF,7JMG,7JMH,7JMI,7JMJ,7M6A,7M6L,7T64,7T65,7U9Q,7U9R,7U9T,7U9X,7U9Z,7UA1,7UA3,7UA4,7UA5,7UA9,7VML,7VMM,7VMN,7VMO,7VMP,7VMQ,7VMR,7VMS,8DUJ,8DVE,8SEN,8SEO,8SEP,8SEQ,8SER,8SES,8SET Peptidyl-prolyl cis-trans isomerase FKBP1B FKB1B_HUMAN P68106 Q13664 Q16645 Q53TM2 Q9BQ40 51425126 COc1ccc(CC[C@H]2OC(=O)[C@@H]3CCCCN3C(=O)[C@@H](C3CCCCC3)c3cc(OC)c(OC)c(OC\C=C\COc4cccc2c4)c3)cc1OC InChI=1S/C43H53NO9/c1-47-36-21-19-29(25-37(36)48-2)18-20-35-31-15-12-16-33(26-31)51-23-10-11-24-52-39-28-32(27-38(49-3)41(39)50-4)40(30-13-6-5-7-14-30)42(45)44-22-9-8-17-34(44)43(46)53-35/h10-12,15-16,19,21,25-28,30,34-35,40H,5-9,13-14,17-18,20,22-24H2,1-4H3/b11-10+/t34-,35+,40-/m0/s1 NDUCBUBAJQQVOX-YBMMQTEXSA-N 50575664 CHEMBL4868302 Peptidyl-prolyl cis-trans isomerase FKBP1B Homo sapiens 216 ChEMBL 10.1021/acs.jmedchem.0c02195 10.7270/Q2988BT3 33666419 Bauder, M; Meyners, C; Purder, PL; Merz, S; Sugiarto, WO; Voll, AM; Heymann, T; Hausch, F Technical University Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50575664 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50000503&target=Peptidyl-prolyl+cis-trans+isomerase+FKBP1B&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50575664&enzyme=Peptidyl-prolyl+cis-trans+isomerase+FKBP1B&column=ki&startPg=0&Increment=50&submit=Search T58 7B9Z 155817658 471051787 1 MGVEIETISPGDGRTFPKKGQTCVVHYTGMLQNGKKFDSSRDRNKPFKFRIGKQEVIKGFEEGAAQMSLGQRAKLTCTPDVAYGATGHPGVIPPNATLIFDVELLNLE 1C9H,1FKK,1FKL,4C02,5HKG,5T15,5T9M,5T9N,5T9R,5T9S,5T9V,5TA3,5TAL,5TAM,5TAN,5TAP,5TAQ,5TAS,5TAT,5TAU,5TAV,5TAW,5TAX,5TAY,5TAZ,5TB0,5TB1,5TB2,5TB3,5TB4,6JGZ,6JH6,6JHN,6JI0,6JI8,6JII,6JIU,6JIY,6JRR,6JRS,6M2W,6PV6,6W1N,6WOT,6WOU,6WOV,6X32,6X33,6X34,6X35,6X36,7CF9,7JMF,7JMG,7JMH,7JMI,7JMJ,7M6A,7M6L,7T64,7T65,7U9Q,7U9R,7U9T,7U9X,7U9Z,7UA1,7UA3,7UA4,7UA5,7UA9,7VML,7VMM,7VMN,7VMO,7VMP,7VMQ,7VMR,7VMS,8DUJ,8DVE,8SEN,8SEO,8SEP,8SEQ,8SER,8SES,8SET Peptidyl-prolyl cis-trans isomerase FKBP1B FKB1B_HUMAN P68106 Q13664 Q16645 Q53TM2 Q9BQ40 51425127 COc1ccc(CC[C@H]2OC(=O)[C@@H]3CCCCN3C(=O)[C@@H](C3CCCCC3)c3cc(OC)c(OC)c(OCCCCOc4cccc2c4)c3)cc1OC InChI=1S/C43H55NO9/c1-47-36-21-19-29(25-37(36)48-2)18-20-35-31-15-12-16-33(26-31)51-23-10-11-24-52-39-28-32(27-38(49-3)41(39)50-4)40(30-13-6-5-7-14-30)42(45)44-22-9-8-17-34(44)43(46)53-35/h12,15-16,19,21,25-28,30,34-35,40H,5-11,13-14,17-18,20,22-24H2,1-4H3/t34-,35+,40-/m0/s1 MXQVEDVUWHACDP-TWBLSBBDSA-N 50575665 CHEMBL4872580 Peptidyl-prolyl cis-trans isomerase FKBP1B Homo sapiens 62 ChEMBL 10.1021/acs.jmedchem.0c02195 10.7270/Q2988BT3 33666419 Bauder, M; Meyners, C; Purder, PL; Merz, S; Sugiarto, WO; Voll, AM; Heymann, T; Hausch, F Technical University Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50575665 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50000503&target=Peptidyl-prolyl+cis-trans+isomerase+FKBP1B&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50575665&enzyme=Peptidyl-prolyl+cis-trans+isomerase+FKBP1B&column=ki&startPg=0&Increment=50&submit=Search 164623065 471051788 1 MGVEIETISPGDGRTFPKKGQTCVVHYTGMLQNGKKFDSSRDRNKPFKFRIGKQEVIKGFEEGAAQMSLGQRAKLTCTPDVAYGATGHPGVIPPNATLIFDVELLNLE 1C9H,1FKK,1FKL,4C02,5HKG,5T15,5T9M,5T9N,5T9R,5T9S,5T9V,5TA3,5TAL,5TAM,5TAN,5TAP,5TAQ,5TAS,5TAT,5TAU,5TAV,5TAW,5TAX,5TAY,5TAZ,5TB0,5TB1,5TB2,5TB3,5TB4,6JGZ,6JH6,6JHN,6JI0,6JI8,6JII,6JIU,6JIY,6JRR,6JRS,6M2W,6PV6,6W1N,6WOT,6WOU,6WOV,6X32,6X33,6X34,6X35,6X36,7CF9,7JMF,7JMG,7JMH,7JMI,7JMJ,7M6A,7M6L,7T64,7T65,7U9Q,7U9R,7U9T,7U9X,7U9Z,7UA1,7UA3,7UA4,7UA5,7UA9,7VML,7VMM,7VMN,7VMO,7VMP,7VMQ,7VMR,7VMS,8DUJ,8DVE,8SEN,8SEO,8SEP,8SEQ,8SER,8SES,8SET Peptidyl-prolyl cis-trans isomerase FKBP1B FKB1B_HUMAN P68106 Q13664 Q16645 Q53TM2 Q9BQ40 51425128 COc1ccc(CC[C@H]2OC(=O)[C@@H]3CCCCN3C(=O)[C@@H](C3CCCCC3)c3cc(OC)c(OC)c(OCCC(=O)COc4cccc2c4)c3)cc1OC InChI=1S/C43H53NO10/c1-48-36-19-17-28(23-37(36)49-2)16-18-35-30-13-10-14-33(24-30)53-27-32(45)20-22-52-39-26-31(25-38(50-3)41(39)51-4)40(29-11-6-5-7-12-29)42(46)44-21-9-8-15-34(44)43(47)54-35/h10,13-14,17,19,23-26,29,34-35,40H,5-9,11-12,15-16,18,20-22,27H2,1-4H3/t34-,35+,40-/m0/s1 SZOGWFMMFBPZTI-TWBLSBBDSA-N 50575666 CHEMBL4863989 Peptidyl-prolyl cis-trans isomerase FKBP1B Homo sapiens 32 ChEMBL 10.1021/acs.jmedchem.0c02195 10.7270/Q2988BT3 33666419 Bauder, M; Meyners, C; Purder, PL; Merz, S; Sugiarto, WO; Voll, AM; Heymann, T; Hausch, F Technical University Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50575666 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50000503&target=Peptidyl-prolyl+cis-trans+isomerase+FKBP1B&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50575666&enzyme=Peptidyl-prolyl+cis-trans+isomerase+FKBP1B&column=ki&startPg=0&Increment=50&submit=Search 164619588 471051789 1 MGVEIETISPGDGRTFPKKGQTCVVHYTGMLQNGKKFDSSRDRNKPFKFRIGKQEVIKGFEEGAAQMSLGQRAKLTCTPDVAYGATGHPGVIPPNATLIFDVELLNLE 1C9H,1FKK,1FKL,4C02,5HKG,5T15,5T9M,5T9N,5T9R,5T9S,5T9V,5TA3,5TAL,5TAM,5TAN,5TAP,5TAQ,5TAS,5TAT,5TAU,5TAV,5TAW,5TAX,5TAY,5TAZ,5TB0,5TB1,5TB2,5TB3,5TB4,6JGZ,6JH6,6JHN,6JI0,6JI8,6JII,6JIU,6JIY,6JRR,6JRS,6M2W,6PV6,6W1N,6WOT,6WOU,6WOV,6X32,6X33,6X34,6X35,6X36,7CF9,7JMF,7JMG,7JMH,7JMI,7JMJ,7M6A,7M6L,7T64,7T65,7U9Q,7U9R,7U9T,7U9X,7U9Z,7UA1,7UA3,7UA4,7UA5,7UA9,7VML,7VMM,7VMN,7VMO,7VMP,7VMQ,7VMR,7VMS,8DUJ,8DVE,8SEN,8SEO,8SEP,8SEQ,8SER,8SES,8SET Peptidyl-prolyl cis-trans isomerase FKBP1B FKB1B_HUMAN P68106 Q13664 Q16645 Q53TM2 Q9BQ40 51425129 COc1ccc(CC[C@H]2OC(=O)[C@@H]3CCCCN3C(=O)[C@@H](C3CCCCC3)c3cc(OC)c(OC)c(OC[C@@H](O)[C@H](O)COc4cccc2c4)c3)cc1OC InChI=1S/C43H55NO11/c1-49-36-19-17-27(21-37(36)50-2)16-18-35-29-13-10-14-31(22-29)53-25-33(45)34(46)26-54-39-24-30(23-38(51-3)41(39)52-4)40(28-11-6-5-7-12-28)42(47)44-20-9-8-15-32(44)43(48)55-35/h10,13-14,17,19,21-24,28,32-35,40,45-46H,5-9,11-12,15-16,18,20,25-26H2,1-4H3/t32-,33+,34+,35+,40-/m0/s1 KMMZNLFAOHLXKG-NXKLTUDVSA-N 50575667 CHEMBL4871144 Peptidyl-prolyl cis-trans isomerase FKBP1B Homo sapiens 9.0 ChEMBL 10.1021/acs.jmedchem.0c02195 10.7270/Q2988BT3 33666419 Bauder, M; Meyners, C; Purder, PL; Merz, S; Sugiarto, WO; Voll, AM; Heymann, T; Hausch, F Technical University Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50575667 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50000503&target=Peptidyl-prolyl+cis-trans+isomerase+FKBP1B&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50575667&enzyme=Peptidyl-prolyl+cis-trans+isomerase+FKBP1B&column=ki&startPg=0&Increment=50&submit=Search T5B 7B9Y 155817657 471051790 1 MGVEIETISPGDGRTFPKKGQTCVVHYTGMLQNGKKFDSSRDRNKPFKFRIGKQEVIKGFEEGAAQMSLGQRAKLTCTPDVAYGATGHPGVIPPNATLIFDVELLNLE 1C9H,1FKK,1FKL,4C02,5HKG,5T15,5T9M,5T9N,5T9R,5T9S,5T9V,5TA3,5TAL,5TAM,5TAN,5TAP,5TAQ,5TAS,5TAT,5TAU,5TAV,5TAW,5TAX,5TAY,5TAZ,5TB0,5TB1,5TB2,5TB3,5TB4,6JGZ,6JH6,6JHN,6JI0,6JI8,6JII,6JIU,6JIY,6JRR,6JRS,6M2W,6PV6,6W1N,6WOT,6WOU,6WOV,6X32,6X33,6X34,6X35,6X36,7CF9,7JMF,7JMG,7JMH,7JMI,7JMJ,7M6A,7M6L,7T64,7T65,7U9Q,7U9R,7U9T,7U9X,7U9Z,7UA1,7UA3,7UA4,7UA5,7UA9,7VML,7VMM,7VMN,7VMO,7VMP,7VMQ,7VMR,7VMS,8DUJ,8DVE,8SEN,8SEO,8SEP,8SEQ,8SER,8SES,8SET Peptidyl-prolyl cis-trans isomerase FKBP1B FKB1B_HUMAN P68106 Q13664 Q16645 Q53TM2 Q9BQ40 51425130 COc1ccc(CC[C@H]2OC(=O)[C@@H]3CCCCN3C(=O)[C@@H](C3CCCCC3)c3cc(OC)c(OC)c(OC[C@H](O)[C@@H](O)COc4cccc2c4)c3)cc1OC InChI=1S/C43H55NO11/c1-49-36-19-17-27(21-37(36)50-2)16-18-35-29-13-10-14-31(22-29)53-25-33(45)34(46)26-54-39-24-30(23-38(51-3)41(39)52-4)40(28-11-6-5-7-12-28)42(47)44-20-9-8-15-32(44)43(48)55-35/h10,13-14,17,19,21-24,28,32-35,40,45-46H,5-9,11-12,15-16,18,20,25-26H2,1-4H3/t32-,33-,34-,35+,40-/m0/s1 KMMZNLFAOHLXKG-MVTSDCAPSA-N 50575668 CHEMBL4878667 Peptidyl-prolyl cis-trans isomerase FKBP1B Homo sapiens 19 ChEMBL 10.1021/acs.jmedchem.0c02195 10.7270/Q2988BT3 33666419 Bauder, M; Meyners, C; Purder, PL; Merz, S; Sugiarto, WO; Voll, AM; Heymann, T; Hausch, F Technical University Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50575668 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50000503&target=Peptidyl-prolyl+cis-trans+isomerase+FKBP1B&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50575668&enzyme=Peptidyl-prolyl+cis-trans+isomerase+FKBP1B&column=ki&startPg=0&Increment=50&submit=Search 164627517 471051791 1 MGVEIETISPGDGRTFPKKGQTCVVHYTGMLQNGKKFDSSRDRNKPFKFRIGKQEVIKGFEEGAAQMSLGQRAKLTCTPDVAYGATGHPGVIPPNATLIFDVELLNLE 1C9H,1FKK,1FKL,4C02,5HKG,5T15,5T9M,5T9N,5T9R,5T9S,5T9V,5TA3,5TAL,5TAM,5TAN,5TAP,5TAQ,5TAS,5TAT,5TAU,5TAV,5TAW,5TAX,5TAY,5TAZ,5TB0,5TB1,5TB2,5TB3,5TB4,6JGZ,6JH6,6JHN,6JI0,6JI8,6JII,6JIU,6JIY,6JRR,6JRS,6M2W,6PV6,6W1N,6WOT,6WOU,6WOV,6X32,6X33,6X34,6X35,6X36,7CF9,7JMF,7JMG,7JMH,7JMI,7JMJ,7M6A,7M6L,7T64,7T65,7U9Q,7U9R,7U9T,7U9X,7U9Z,7UA1,7UA3,7UA4,7UA5,7UA9,7VML,7VMM,7VMN,7VMO,7VMP,7VMQ,7VMR,7VMS,8DUJ,8DVE,8SEN,8SEO,8SEP,8SEQ,8SER,8SES,8SET Peptidyl-prolyl cis-trans isomerase FKBP1B FKB1B_HUMAN P68106 Q13664 Q16645 Q53TM2 Q9BQ40 51425131 COc1ccc(CC[C@H]2OC(=O)[C@@H]3CCCCN3C(=O)[C@@H](C3CCCCC3)c3cc(OC)c(OC)c(OCC\C=C\COc4cccc2c4)c3)cc1OC InChI=1S/C44H55NO9/c1-48-37-22-20-30(26-38(37)49-2)19-21-36-32-16-13-17-34(27-32)52-24-11-6-12-25-53-40-29-33(28-39(50-3)42(40)51-4)41(31-14-7-5-8-15-31)43(46)45-23-10-9-18-35(45)44(47)54-36/h6,11,13,16-17,20,22,26-29,31,35-36,41H,5,7-10,12,14-15,18-19,21,23-25H2,1-4H3/b11-6+/t35-,36+,41-/m0/s1 YBURQPQNUVSQHI-LCWXHYGYSA-N 50575669 CHEMBL4864747 Peptidyl-prolyl cis-trans isomerase FKBP1B Homo sapiens 709 ChEMBL 10.1021/acs.jmedchem.0c02195 10.7270/Q2988BT3 33666419 Bauder, M; Meyners, C; Purder, PL; Merz, S; Sugiarto, WO; Voll, AM; Heymann, T; Hausch, F Technical University Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50575669 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50000503&target=Peptidyl-prolyl+cis-trans+isomerase+FKBP1B&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50575669&enzyme=Peptidyl-prolyl+cis-trans+isomerase+FKBP1B&column=ki&startPg=0&Increment=50&submit=Search 164623202 471051792 1 MGVEIETISPGDGRTFPKKGQTCVVHYTGMLQNGKKFDSSRDRNKPFKFRIGKQEVIKGFEEGAAQMSLGQRAKLTCTPDVAYGATGHPGVIPPNATLIFDVELLNLE 1C9H,1FKK,1FKL,4C02,5HKG,5T15,5T9M,5T9N,5T9R,5T9S,5T9V,5TA3,5TAL,5TAM,5TAN,5TAP,5TAQ,5TAS,5TAT,5TAU,5TAV,5TAW,5TAX,5TAY,5TAZ,5TB0,5TB1,5TB2,5TB3,5TB4,6JGZ,6JH6,6JHN,6JI0,6JI8,6JII,6JIU,6JIY,6JRR,6JRS,6M2W,6PV6,6W1N,6WOT,6WOU,6WOV,6X32,6X33,6X34,6X35,6X36,7CF9,7JMF,7JMG,7JMH,7JMI,7JMJ,7M6A,7M6L,7T64,7T65,7U9Q,7U9R,7U9T,7U9X,7U9Z,7UA1,7UA3,7UA4,7UA5,7UA9,7VML,7VMM,7VMN,7VMO,7VMP,7VMQ,7VMR,7VMS,8DUJ,8DVE,8SEN,8SEO,8SEP,8SEQ,8SER,8SES,8SET Peptidyl-prolyl cis-trans isomerase FKBP1B FKB1B_HUMAN P68106 Q13664 Q16645 Q53TM2 Q9BQ40 51425132 COc1ccc(CC[C@H]2OC(=O)[C@@H]3CCCCN3C(=O)[C@@H](C3CCCCC3)c3cc(OC)c(OC)c(OCC\C=C/COc4cccc2c4)c3)cc1OC InChI=1S/C44H55NO9/c1-48-37-22-20-30(26-38(37)49-2)19-21-36-32-16-13-17-34(27-32)52-24-11-6-12-25-53-40-29-33(28-39(50-3)42(40)51-4)41(31-14-7-5-8-15-31)43(46)45-23-10-9-18-35(45)44(47)54-36/h6,11,13,16-17,20,22,26-29,31,35-36,41H,5,7-10,12,14-15,18-19,21,23-25H2,1-4H3/b11-6-/t35-,36+,41-/m0/s1 YBURQPQNUVSQHI-GTKPNJOPSA-N 50575670 CHEMBL4850434 Peptidyl-prolyl cis-trans isomerase FKBP1B Homo sapiens 116 ChEMBL 10.1021/acs.jmedchem.0c02195 10.7270/Q2988BT3 33666419 Bauder, M; Meyners, C; Purder, PL; Merz, S; Sugiarto, WO; Voll, AM; Heymann, T; Hausch, F Technical University Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50575670 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50000503&target=Peptidyl-prolyl+cis-trans+isomerase+FKBP1B&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50575670&enzyme=Peptidyl-prolyl+cis-trans+isomerase+FKBP1B&column=ki&startPg=0&Increment=50&submit=Search 164610590 471051793 1 MGVEIETISPGDGRTFPKKGQTCVVHYTGMLQNGKKFDSSRDRNKPFKFRIGKQEVIKGFEEGAAQMSLGQRAKLTCTPDVAYGATGHPGVIPPNATLIFDVELLNLE 1C9H,1FKK,1FKL,4C02,5HKG,5T15,5T9M,5T9N,5T9R,5T9S,5T9V,5TA3,5TAL,5TAM,5TAN,5TAP,5TAQ,5TAS,5TAT,5TAU,5TAV,5TAW,5TAX,5TAY,5TAZ,5TB0,5TB1,5TB2,5TB3,5TB4,6JGZ,6JH6,6JHN,6JI0,6JI8,6JII,6JIU,6JIY,6JRR,6JRS,6M2W,6PV6,6W1N,6WOT,6WOU,6WOV,6X32,6X33,6X34,6X35,6X36,7CF9,7JMF,7JMG,7JMH,7JMI,7JMJ,7M6A,7M6L,7T64,7T65,7U9Q,7U9R,7U9T,7U9X,7U9Z,7UA1,7UA3,7UA4,7UA5,7UA9,7VML,7VMM,7VMN,7VMO,7VMP,7VMQ,7VMR,7VMS,8DUJ,8DVE,8SEN,8SEO,8SEP,8SEQ,8SER,8SES,8SET Peptidyl-prolyl cis-trans isomerase FKBP1B FKB1B_HUMAN P68106 Q13664 Q16645 Q53TM2 Q9BQ40 51425133 COc1ccc(CC[C@H]2OC(=O)[C@@H]3CCCCN3C(=O)[C@@H](C3CCCCC3)c3cc(OC)c(OC)c(OCCCCCOc4cccc2c4)c3)cc1OC InChI=1S/C44H57NO9/c1-48-37-22-20-30(26-38(37)49-2)19-21-36-32-16-13-17-34(27-32)52-24-11-6-12-25-53-40-29-33(28-39(50-3)42(40)51-4)41(31-14-7-5-8-15-31)43(46)45-23-10-9-18-35(45)44(47)54-36/h13,16-17,20,22,26-29,31,35-36,41H,5-12,14-15,18-19,21,23-25H2,1-4H3/t35-,36+,41-/m0/s1 AFNJECWRDDBTHD-KLBQNTFLSA-N 50575671 CHEMBL4870008 Peptidyl-prolyl cis-trans isomerase FKBP1B Homo sapiens 100 ChEMBL 10.1021/acs.jmedchem.0c02195 10.7270/Q2988BT3 33666419 Bauder, M; Meyners, C; Purder, PL; Merz, S; Sugiarto, WO; Voll, AM; Heymann, T; Hausch, F Technical University Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50575671 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50000503&target=Peptidyl-prolyl+cis-trans+isomerase+FKBP1B&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50575671&enzyme=Peptidyl-prolyl+cis-trans+isomerase+FKBP1B&column=ki&startPg=0&Increment=50&submit=Search 164621520 471051794 1 MGVEIETISPGDGRTFPKKGQTCVVHYTGMLQNGKKFDSSRDRNKPFKFRIGKQEVIKGFEEGAAQMSLGQRAKLTCTPDVAYGATGHPGVIPPNATLIFDVELLNLE 1C9H,1FKK,1FKL,4C02,5HKG,5T15,5T9M,5T9N,5T9R,5T9S,5T9V,5TA3,5TAL,5TAM,5TAN,5TAP,5TAQ,5TAS,5TAT,5TAU,5TAV,5TAW,5TAX,5TAY,5TAZ,5TB0,5TB1,5TB2,5TB3,5TB4,6JGZ,6JH6,6JHN,6JI0,6JI8,6JII,6JIU,6JIY,6JRR,6JRS,6M2W,6PV6,6W1N,6WOT,6WOU,6WOV,6X32,6X33,6X34,6X35,6X36,7CF9,7JMF,7JMG,7JMH,7JMI,7JMJ,7M6A,7M6L,7T64,7T65,7U9Q,7U9R,7U9T,7U9X,7U9Z,7UA1,7UA3,7UA4,7UA5,7UA9,7VML,7VMM,7VMN,7VMO,7VMP,7VMQ,7VMR,7VMS,8DUJ,8DVE,8SEN,8SEO,8SEP,8SEQ,8SER,8SES,8SET Peptidyl-prolyl cis-trans isomerase FKBP1B FKB1B_HUMAN P68106 Q13664 Q16645 Q53TM2 Q9BQ40 51425134 COc1ccc(CC[C@H]2OC(=O)[C@@H]3CCCCN3C(=O)[C@@H](C3CCCCC3)c3cc(OC)c(OC)c(OCCC(=O)CCOc4cccc2c4)c3)cc1OC InChI=1S/C44H55NO10/c1-49-37-19-17-29(25-38(37)50-2)16-18-36-31-13-10-14-34(26-31)53-23-20-33(46)21-24-54-40-28-32(27-39(51-3)42(40)52-4)41(30-11-6-5-7-12-30)43(47)45-22-9-8-15-35(45)44(48)55-36/h10,13-14,17,19,25-28,30,35-36,41H,5-9,11-12,15-16,18,20-24H2,1-4H3/t35-,36+,41-/m0/s1 VHPLQZSHAKNOLI-KLBQNTFLSA-N 50575672 CHEMBL4858532 Peptidyl-prolyl cis-trans isomerase FKBP1B Homo sapiens 20 ChEMBL 10.1021/acs.jmedchem.0c02195 10.7270/Q2988BT3 33666419 Bauder, M; Meyners, C; Purder, PL; Merz, S; Sugiarto, WO; Voll, AM; Heymann, T; Hausch, F Technical University Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50575672 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50000503&target=Peptidyl-prolyl+cis-trans+isomerase+FKBP1B&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50575672&enzyme=Peptidyl-prolyl+cis-trans+isomerase+FKBP1B&column=ki&startPg=0&Increment=50&submit=Search 164609913 471051795 1 MGVEIETISPGDGRTFPKKGQTCVVHYTGMLQNGKKFDSSRDRNKPFKFRIGKQEVIKGFEEGAAQMSLGQRAKLTCTPDVAYGATGHPGVIPPNATLIFDVELLNLE 1C9H,1FKK,1FKL,4C02,5HKG,5T15,5T9M,5T9N,5T9R,5T9S,5T9V,5TA3,5TAL,5TAM,5TAN,5TAP,5TAQ,5TAS,5TAT,5TAU,5TAV,5TAW,5TAX,5TAY,5TAZ,5TB0,5TB1,5TB2,5TB3,5TB4,6JGZ,6JH6,6JHN,6JI0,6JI8,6JII,6JIU,6JIY,6JRR,6JRS,6M2W,6PV6,6W1N,6WOT,6WOU,6WOV,6X32,6X33,6X34,6X35,6X36,7CF9,7JMF,7JMG,7JMH,7JMI,7JMJ,7M6A,7M6L,7T64,7T65,7U9Q,7U9R,7U9T,7U9X,7U9Z,7UA1,7UA3,7UA4,7UA5,7UA9,7VML,7VMM,7VMN,7VMO,7VMP,7VMQ,7VMR,7VMS,8DUJ,8DVE,8SEN,8SEO,8SEP,8SEQ,8SER,8SES,8SET Peptidyl-prolyl cis-trans isomerase FKBP1B FKB1B_HUMAN P68106 Q13664 Q16645 Q53TM2 Q9BQ40 51425135 COc1ccc(CC[C@H]2OC(=O)[C@@H]3CCCCN3C(=O)[C@@H](C3CCCCC3)c3cc(OC)c(OC)c(OCCCC(=O)COc4cccc2c4)c3)cc1OC InChI=1S/C44H55NO10/c1-49-37-21-19-29(24-38(37)50-2)18-20-36-31-14-10-16-34(25-31)54-28-33(46)15-11-23-53-40-27-32(26-39(51-3)42(40)52-4)41(30-12-6-5-7-13-30)43(47)45-22-9-8-17-35(45)44(48)55-36/h10,14,16,19,21,24-27,30,35-36,41H,5-9,11-13,15,17-18,20,22-23,28H2,1-4H3/t35-,36+,41-/m0/s1 DOJMFMVTYZITGI-KLBQNTFLSA-N 50575673 CHEMBL4876415 Peptidyl-prolyl cis-trans isomerase FKBP1B Homo sapiens 43 ChEMBL 10.1021/acs.jmedchem.0c02195 10.7270/Q2988BT3 33666419 Bauder, M; Meyners, C; Purder, PL; Merz, S; Sugiarto, WO; Voll, AM; Heymann, T; Hausch, F Technical University Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50575673 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50000503&target=Peptidyl-prolyl+cis-trans+isomerase+FKBP1B&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50575673&enzyme=Peptidyl-prolyl+cis-trans+isomerase+FKBP1B&column=ki&startPg=0&Increment=50&submit=Search 164626542 471051796 1 MGVEIETISPGDGRTFPKKGQTCVVHYTGMLQNGKKFDSSRDRNKPFKFRIGKQEVIKGFEEGAAQMSLGQRAKLTCTPDVAYGATGHPGVIPPNATLIFDVELLNLE 1C9H,1FKK,1FKL,4C02,5HKG,5T15,5T9M,5T9N,5T9R,5T9S,5T9V,5TA3,5TAL,5TAM,5TAN,5TAP,5TAQ,5TAS,5TAT,5TAU,5TAV,5TAW,5TAX,5TAY,5TAZ,5TB0,5TB1,5TB2,5TB3,5TB4,6JGZ,6JH6,6JHN,6JI0,6JI8,6JII,6JIU,6JIY,6JRR,6JRS,6M2W,6PV6,6W1N,6WOT,6WOU,6WOV,6X32,6X33,6X34,6X35,6X36,7CF9,7JMF,7JMG,7JMH,7JMI,7JMJ,7M6A,7M6L,7T64,7T65,7U9Q,7U9R,7U9T,7U9X,7U9Z,7UA1,7UA3,7UA4,7UA5,7UA9,7VML,7VMM,7VMN,7VMO,7VMP,7VMQ,7VMR,7VMS,8DUJ,8DVE,8SEN,8SEO,8SEP,8SEQ,8SER,8SES,8SET Peptidyl-prolyl cis-trans isomerase FKBP1B FKB1B_HUMAN P68106 Q13664 Q16645 Q53TM2 Q9BQ40 51425136 COc1ccc(CC[C@H]2OC(=O)[C@@H]3CCCCN3C(=O)[C@@H](C3CCCCC3)c3cc(OC)c(OC)c(OCCOC\C=C\COc4cccc2c4)c3)cc1OC InChI=1S/C45H57NO10/c1-49-38-21-19-31(27-39(38)50-2)18-20-37-33-15-12-16-35(28-33)54-24-11-10-23-53-25-26-55-41-30-34(29-40(51-3)43(41)52-4)42(32-13-6-5-7-14-32)44(47)46-22-9-8-17-36(46)45(48)56-37/h10-12,15-16,19,21,27-30,32,36-37,42H,5-9,13-14,17-18,20,22-26H2,1-4H3/b11-10+/t36-,37+,42-/m0/s1 WAUBVJRWQJBYNY-SGYAFFFDSA-N 50575674 CHEMBL4862808 Peptidyl-prolyl cis-trans isomerase FKBP1B Homo sapiens 105 ChEMBL 10.1021/acs.jmedchem.0c02195 10.7270/Q2988BT3 33666419 Bauder, M; Meyners, C; Purder, PL; Merz, S; Sugiarto, WO; Voll, AM; Heymann, T; Hausch, F Technical University Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50575674 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50000503&target=Peptidyl-prolyl+cis-trans+isomerase+FKBP1B&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50575674&enzyme=Peptidyl-prolyl+cis-trans+isomerase+FKBP1B&column=ki&startPg=0&Increment=50&submit=Search 164621282 471051797 1 MGVEIETISPGDGRTFPKKGQTCVVHYTGMLQNGKKFDSSRDRNKPFKFRIGKQEVIKGFEEGAAQMSLGQRAKLTCTPDVAYGATGHPGVIPPNATLIFDVELLNLE 1C9H,1FKK,1FKL,4C02,5HKG,5T15,5T9M,5T9N,5T9R,5T9S,5T9V,5TA3,5TAL,5TAM,5TAN,5TAP,5TAQ,5TAS,5TAT,5TAU,5TAV,5TAW,5TAX,5TAY,5TAZ,5TB0,5TB1,5TB2,5TB3,5TB4,6JGZ,6JH6,6JHN,6JI0,6JI8,6JII,6JIU,6JIY,6JRR,6JRS,6M2W,6PV6,6W1N,6WOT,6WOU,6WOV,6X32,6X33,6X34,6X35,6X36,7CF9,7JMF,7JMG,7JMH,7JMI,7JMJ,7M6A,7M6L,7T64,7T65,7U9Q,7U9R,7U9T,7U9X,7U9Z,7UA1,7UA3,7UA4,7UA5,7UA9,7VML,7VMM,7VMN,7VMO,7VMP,7VMQ,7VMR,7VMS,8DUJ,8DVE,8SEN,8SEO,8SEP,8SEQ,8SER,8SES,8SET Peptidyl-prolyl cis-trans isomerase FKBP1B FKB1B_HUMAN P68106 Q13664 Q16645 Q53TM2 Q9BQ40 51425137 COc1ccc(CC[C@H]2OC(=O)[C@@H]3CCCCN3C(=O)[C@@H](C3CCCCC3)c3cc(OC)c(OC)c(OCCOC\C=C/COc4cccc2c4)c3)cc1OC InChI=1S/C45H57NO10/c1-49-38-21-19-31(27-39(38)50-2)18-20-37-33-15-12-16-35(28-33)54-24-11-10-23-53-25-26-55-41-30-34(29-40(51-3)43(41)52-4)42(32-13-6-5-7-14-32)44(47)46-22-9-8-17-36(46)45(48)56-37/h10-12,15-16,19,21,27-30,32,36-37,42H,5-9,13-14,17-18,20,22-26H2,1-4H3/b11-10-/t36-,37+,42-/m0/s1 WAUBVJRWQJBYNY-QCXYFFPESA-N 50575675 CHEMBL4856203 Peptidyl-prolyl cis-trans isomerase FKBP1B Homo sapiens 301 ChEMBL 10.1021/acs.jmedchem.0c02195 10.7270/Q2988BT3 33666419 Bauder, M; Meyners, C; Purder, PL; Merz, S; Sugiarto, WO; Voll, AM; Heymann, T; Hausch, F Technical University Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50575675 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50000503&target=Peptidyl-prolyl+cis-trans+isomerase+FKBP1B&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50575675&enzyme=Peptidyl-prolyl+cis-trans+isomerase+FKBP1B&column=ki&startPg=0&Increment=50&submit=Search 164610826 471051798 1 MGVEIETISPGDGRTFPKKGQTCVVHYTGMLQNGKKFDSSRDRNKPFKFRIGKQEVIKGFEEGAAQMSLGQRAKLTCTPDVAYGATGHPGVIPPNATLIFDVELLNLE 1C9H,1FKK,1FKL,4C02,5HKG,5T15,5T9M,5T9N,5T9R,5T9S,5T9V,5TA3,5TAL,5TAM,5TAN,5TAP,5TAQ,5TAS,5TAT,5TAU,5TAV,5TAW,5TAX,5TAY,5TAZ,5TB0,5TB1,5TB2,5TB3,5TB4,6JGZ,6JH6,6JHN,6JI0,6JI8,6JII,6JIU,6JIY,6JRR,6JRS,6M2W,6PV6,6W1N,6WOT,6WOU,6WOV,6X32,6X33,6X34,6X35,6X36,7CF9,7JMF,7JMG,7JMH,7JMI,7JMJ,7M6A,7M6L,7T64,7T65,7U9Q,7U9R,7U9T,7U9X,7U9Z,7UA1,7UA3,7UA4,7UA5,7UA9,7VML,7VMM,7VMN,7VMO,7VMP,7VMQ,7VMR,7VMS,8DUJ,8DVE,8SEN,8SEO,8SEP,8SEQ,8SER,8SES,8SET Peptidyl-prolyl cis-trans isomerase FKBP1B FKB1B_HUMAN P68106 Q13664 Q16645 Q53TM2 Q9BQ40 51425138 COc1ccc(CC[C@H]2OC(=O)[C@@H]3CCCCN3C(=O)[C@@H](C3CCCCC3)c3cc(OC)c(OC)c(OCCOCCCCOc4cccc2c4)c3)cc1OC InChI=1S/C45H59NO10/c1-49-38-21-19-31(27-39(38)50-2)18-20-37-33-15-12-16-35(28-33)54-24-11-10-23-53-25-26-55-41-30-34(29-40(51-3)43(41)52-4)42(32-13-6-5-7-14-32)44(47)46-22-9-8-17-36(46)45(48)56-37/h12,15-16,19,21,27-30,32,36-37,42H,5-11,13-14,17-18,20,22-26H2,1-4H3/t36-,37+,42-/m0/s1 OMGPIDRAHNFBAN-FMXQOUBESA-N 50575676 CHEMBL4862282 Peptidyl-prolyl cis-trans isomerase FKBP1B Homo sapiens 115 ChEMBL 10.1021/acs.jmedchem.0c02195 10.7270/Q2988BT3 33666419 Bauder, M; Meyners, C; Purder, PL; Merz, S; Sugiarto, WO; Voll, AM; Heymann, T; Hausch, F Technical University Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50575676 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50000503&target=Peptidyl-prolyl+cis-trans+isomerase+FKBP1B&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50575676&enzyme=Peptidyl-prolyl+cis-trans+isomerase+FKBP1B&column=ki&startPg=0&Increment=50&submit=Search 164623611 471051799 1 MGVEIETISPGDGRTFPKKGQTCVVHYTGMLQNGKKFDSSRDRNKPFKFRIGKQEVIKGFEEGAAQMSLGQRAKLTCTPDVAYGATGHPGVIPPNATLIFDVELLNLE 1C9H,1FKK,1FKL,4C02,5HKG,5T15,5T9M,5T9N,5T9R,5T9S,5T9V,5TA3,5TAL,5TAM,5TAN,5TAP,5TAQ,5TAS,5TAT,5TAU,5TAV,5TAW,5TAX,5TAY,5TAZ,5TB0,5TB1,5TB2,5TB3,5TB4,6JGZ,6JH6,6JHN,6JI0,6JI8,6JII,6JIU,6JIY,6JRR,6JRS,6M2W,6PV6,6W1N,6WOT,6WOU,6WOV,6X32,6X33,6X34,6X35,6X36,7CF9,7JMF,7JMG,7JMH,7JMI,7JMJ,7M6A,7M6L,7T64,7T65,7U9Q,7U9R,7U9T,7U9X,7U9Z,7UA1,7UA3,7UA4,7UA5,7UA9,7VML,7VMM,7VMN,7VMO,7VMP,7VMQ,7VMR,7VMS,8DUJ,8DVE,8SEN,8SEO,8SEP,8SEQ,8SER,8SES,8SET Peptidyl-prolyl cis-trans isomerase FKBP1B FKB1B_HUMAN P68106 Q13664 Q16645 Q53TM2 Q9BQ40 51425139 COc1ccc(CC[C@H]2OC(=O)[C@@H]3CCCCN3C(=O)[C@@H](C3CCCCC3)c3cc(OC)c(OC)c(OCCOCC(=O)CCOc4cccc2c4)c3)cc1OC InChI=1S/C45H57NO11/c1-50-38-19-17-30(25-39(38)51-2)16-18-37-32-13-10-14-35(26-32)55-22-20-34(47)29-54-23-24-56-41-28-33(27-40(52-3)43(41)53-4)42(31-11-6-5-7-12-31)44(48)46-21-9-8-15-36(46)45(49)57-37/h10,13-14,17,19,25-28,31,36-37,42H,5-9,11-12,15-16,18,20-24,29H2,1-4H3/t36-,37+,42-/m0/s1 NTCMRSFHPJYIPB-FMXQOUBESA-N 50575677 CHEMBL4866742 Peptidyl-prolyl cis-trans isomerase FKBP1B Homo sapiens 53 ChEMBL 10.1021/acs.jmedchem.0c02195 10.7270/Q2988BT3 33666419 Bauder, M; Meyners, C; Purder, PL; Merz, S; Sugiarto, WO; Voll, AM; Heymann, T; Hausch, F Technical University Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50575677 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50000503&target=Peptidyl-prolyl+cis-trans+isomerase+FKBP1B&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50575677&enzyme=Peptidyl-prolyl+cis-trans+isomerase+FKBP1B&column=ki&startPg=0&Increment=50&submit=Search 164620146 471051800 1 MGVEIETISPGDGRTFPKKGQTCVVHYTGMLQNGKKFDSSRDRNKPFKFRIGKQEVIKGFEEGAAQMSLGQRAKLTCTPDVAYGATGHPGVIPPNATLIFDVELLNLE 1C9H,1FKK,1FKL,4C02,5HKG,5T15,5T9M,5T9N,5T9R,5T9S,5T9V,5TA3,5TAL,5TAM,5TAN,5TAP,5TAQ,5TAS,5TAT,5TAU,5TAV,5TAW,5TAX,5TAY,5TAZ,5TB0,5TB1,5TB2,5TB3,5TB4,6JGZ,6JH6,6JHN,6JI0,6JI8,6JII,6JIU,6JIY,6JRR,6JRS,6M2W,6PV6,6W1N,6WOT,6WOU,6WOV,6X32,6X33,6X34,6X35,6X36,7CF9,7JMF,7JMG,7JMH,7JMI,7JMJ,7M6A,7M6L,7T64,7T65,7U9Q,7U9R,7U9T,7U9X,7U9Z,7UA1,7UA3,7UA4,7UA5,7UA9,7VML,7VMM,7VMN,7VMO,7VMP,7VMQ,7VMR,7VMS,8DUJ,8DVE,8SEN,8SEO,8SEP,8SEQ,8SER,8SES,8SET Peptidyl-prolyl cis-trans isomerase FKBP1B FKB1B_HUMAN P68106 Q13664 Q16645 Q53TM2 Q9BQ40 51425140 COc1ccc(CC[C@H]2OC(=O)[C@@H]3CCCCN3C(=O)[C@@H](C3CCCCC3)c3cc(OC)c(OC)c(OCCCOC\C=C/COc4cccc2c4)c3)cc1OC InChI=1S/C46H59NO10/c1-50-39-22-20-32(28-40(39)51-2)19-21-38-34-16-12-17-36(29-34)55-26-11-10-24-54-25-13-27-56-42-31-35(30-41(52-3)44(42)53-4)43(33-14-6-5-7-15-33)45(48)47-23-9-8-18-37(47)46(49)57-38/h10-12,16-17,20,22,28-31,33,37-38,43H,5-9,13-15,18-19,21,23-27H2,1-4H3/b11-10-/t37-,38+,43-/m0/s1 KSVMHCAVVOAVDP-ZCBFIPOHSA-N 50575678 CHEMBL4877731 Peptidyl-prolyl cis-trans isomerase FKBP1B Homo sapiens 352 ChEMBL 10.1021/acs.jmedchem.0c02195 10.7270/Q2988BT3 33666419 Bauder, M; Meyners, C; Purder, PL; Merz, S; Sugiarto, WO; Voll, AM; Heymann, T; Hausch, F Technical University Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50575678 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50000503&target=Peptidyl-prolyl+cis-trans+isomerase+FKBP1B&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50575678&enzyme=Peptidyl-prolyl+cis-trans+isomerase+FKBP1B&column=ki&startPg=0&Increment=50&submit=Search 164628280 471051801 1 MGVEIETISPGDGRTFPKKGQTCVVHYTGMLQNGKKFDSSRDRNKPFKFRIGKQEVIKGFEEGAAQMSLGQRAKLTCTPDVAYGATGHPGVIPPNATLIFDVELLNLE 1C9H,1FKK,1FKL,4C02,5HKG,5T15,5T9M,5T9N,5T9R,5T9S,5T9V,5TA3,5TAL,5TAM,5TAN,5TAP,5TAQ,5TAS,5TAT,5TAU,5TAV,5TAW,5TAX,5TAY,5TAZ,5TB0,5TB1,5TB2,5TB3,5TB4,6JGZ,6JH6,6JHN,6JI0,6JI8,6JII,6JIU,6JIY,6JRR,6JRS,6M2W,6PV6,6W1N,6WOT,6WOU,6WOV,6X32,6X33,6X34,6X35,6X36,7CF9,7JMF,7JMG,7JMH,7JMI,7JMJ,7M6A,7M6L,7T64,7T65,7U9Q,7U9R,7U9T,7U9X,7U9Z,7UA1,7UA3,7UA4,7UA5,7UA9,7VML,7VMM,7VMN,7VMO,7VMP,7VMQ,7VMR,7VMS,8DUJ,8DVE,8SEN,8SEO,8SEP,8SEQ,8SER,8SES,8SET Peptidyl-prolyl cis-trans isomerase FKBP1B FKB1B_HUMAN P68106 Q13664 Q16645 Q53TM2 Q9BQ40 51425141 COc1ccc(CC[C@H]2OC(=O)[C@@H]3CCCCN3C(=O)[C@@H](C3CCCCC3)c3cc(OC)c(OC)c(OCCCOCCCCOc4cccc2c4)c3)cc1OC InChI=1S/C46H61NO10/c1-50-39-22-20-32(28-40(39)51-2)19-21-38-34-16-12-17-36(29-34)55-26-11-10-24-54-25-13-27-56-42-31-35(30-41(52-3)44(42)53-4)43(33-14-6-5-7-15-33)45(48)47-23-9-8-18-37(47)46(49)57-38/h12,16-17,20,22,28-31,33,37-38,43H,5-11,13-15,18-19,21,23-27H2,1-4H3/t37-,38+,43-/m0/s1 PWZDMYVESVBPLA-FDHYQTMZSA-N 50575679 CHEMBL4850750 Peptidyl-prolyl cis-trans isomerase FKBP1B Homo sapiens 227 ChEMBL 10.1021/acs.jmedchem.0c02195 10.7270/Q2988BT3 33666419 Bauder, M; Meyners, C; Purder, PL; Merz, S; Sugiarto, WO; Voll, AM; Heymann, T; Hausch, F Technical University Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50575679 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50000503&target=Peptidyl-prolyl+cis-trans+isomerase+FKBP1B&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50575679&enzyme=Peptidyl-prolyl+cis-trans+isomerase+FKBP1B&column=ki&startPg=0&Increment=50&submit=Search 164612170 471051802 1 MGVEIETISPGDGRTFPKKGQTCVVHYTGMLQNGKKFDSSRDRNKPFKFRIGKQEVIKGFEEGAAQMSLGQRAKLTCTPDVAYGATGHPGVIPPNATLIFDVELLNLE 1C9H,1FKK,1FKL,4C02,5HKG,5T15,5T9M,5T9N,5T9R,5T9S,5T9V,5TA3,5TAL,5TAM,5TAN,5TAP,5TAQ,5TAS,5TAT,5TAU,5TAV,5TAW,5TAX,5TAY,5TAZ,5TB0,5TB1,5TB2,5TB3,5TB4,6JGZ,6JH6,6JHN,6JI0,6JI8,6JII,6JIU,6JIY,6JRR,6JRS,6M2W,6PV6,6W1N,6WOT,6WOU,6WOV,6X32,6X33,6X34,6X35,6X36,7CF9,7JMF,7JMG,7JMH,7JMI,7JMJ,7M6A,7M6L,7T64,7T65,7U9Q,7U9R,7U9T,7U9X,7U9Z,7UA1,7UA3,7UA4,7UA5,7UA9,7VML,7VMM,7VMN,7VMO,7VMP,7VMQ,7VMR,7VMS,8DUJ,8DVE,8SEN,8SEO,8SEP,8SEQ,8SER,8SES,8SET Peptidyl-prolyl cis-trans isomerase FKBP1B FKB1B_HUMAN P68106 Q13664 Q16645 Q53TM2 Q9BQ40