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haitengzhao
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molecule_property_instruction

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bace · 1.51k rows

graph stringlengths 17 198	text sequencelengths 7 7	label stringclasses 2 values	dataset_name stringclasses 1 value	molecule_index stringlengths 1 4	split stringclasses 3 values
Clc1ccccc1-c1n(Cc2nc(N)ccc2)c(cc1)-c1ccc(Oc2cncnc2)cc1	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	Yes	bace	100	train
S(=O)(=O)(C(CCC)CCC)C[C@@H](NC(OCc1ccccc1)=O)C(=O)N[C@H]([C@H](O)C[NH2+]Cc1cc(OC)ccc1)Cc1ccccc1	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	101	test
Fc1cc(cc(F)c1)C[C@H](NC(=O)c1cc(cc(c1)C)C(=O)N(CCC)CCC)[C@H](O)[C@@H]1[NH2+]CC[N@@H+](C1)Cc1ccccc1	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	102	test
S(=O)(=O)(N[C@@H]1C[C@H](C[C@@H](C1)C(=O)N[C@H]([C@@H](O)CC(=O)N[C@@H](CC(C)C)C(=O)N[C@H](C(=O)N([C@H](CC1CCCCC1)C(=O)N1CCC[C@H]1C(OC)=O)C)C)CC1CCCCC1)C(=O)N[C@H](C)C1CCCCC1)C	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	103	test
S1(=O)(=O)C[C@@H](Cc2cc(F)c3NCC4(CCC(F)(F)CC4)c3c2)[C@H](O)[C@@H]([NH2+]Cc2cc(ccc2)C(C)(C)C)C1	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	104	test
O=C(N1CC[C@H](C[C@H]1c1ccccc1)c1ccccc1)[C@@H]1C[NH2+]C[C@]12CCCc1c2cccc1	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	105	test
S1(=O)(=O)C[C@@H](Cc2cc(C[C@@H]3N(CCC)C(OC3)=O)c(O)cc2)[C@H](O)[C@@H]([NH2+]Cc2cc(ccc2)C(C)C)C1	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	106	test
S1C[C@H](NC(OC(C)(C)C)=O)C(=O)N[C@@H](C)C(=O)N[C@@H](CSC\C=C\C1)[C@@H](O)C[C@H](C(=O)N[C@@H](C(C)C)C(=O)NCCCC)C	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	107	test
O(C)c1ccc(cc1C)[C@@]1(N=C(N)N(C)C1=O)C12CC3CC(C1)CC(C2)C3	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	108	train
Clc1cc2CC([NH+]=C(N[C@@H](Cc3ccccc3)C=3NC(=O)c4c(N=3)ccnc4)c2cc1)(C)C	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	109	test
O=C1N(CCC1)c1cc(cc(NCC)c1)C(=O)N[C@H]([C@H](O)C[NH2+]C1CCCCC1)Cc1ccccc1	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	110	test
Fc1ccc(NC(=O)c2ncc(OCC)cc2)cc1[C@]1(N=C(OCC1(F)F)N)C	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	111	train
O(C(=O)[C@H]1N(CCC1)C(=O)[C@H](N(C(=O)[C@@H](NC(=O)[C@@H](NC(=O)C[C@H](O)[C@@H](NC(=O)[C@@H](N(C(=O)[C@@H](NC(=O)[C@@H](O)C)C(C)C)C)CCC(=O)N)CC1CCCCC1)CC(C)C)C)C)CC1CCCCC1)C	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	112	test
S1C[C@H](NC(=O)[C@@H](NC(=O)[C@@H]2[NH2+]CCC[C@@H]2SC\C=C\C1)C)[C@@H](O)C[C@H](C(=O)NCCCC)C	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	113	test
O(C)c1cc(ccc1)C[NH2+]C[C@@H](O)[C@@H](NC(=O)c1cc(ccc1)C(=O)N(CCC)CCC)Cc1ccccc1	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	114	train
O=C(NC[C@H]([NH3+])C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CC(C)C)C(=O)NC[C@](O)(CCc1ccccc1)C(=O)Nc1cc(ccc1)C(=O)[O-])c1nnn[n-]1	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	115	test
Fc1ccc(cc1-c1cncnc1)[C@]1([NH+]=C(N)c2c1cccc2F)c1cc(ncc1)C(F)(F)F	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	116	test
O(C)c1cc(ccc1)-c1cc(ccc1)CC[C@]1(N=C(N)N(C)C(=O)C1)C	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	117	train
S(=O)(=O)(N(C)c1cc(cc(c1)C(OC[C@]([NH3+])(Cc1ccccc1)CO)=O)C(=O)N[C@H](C)c1ccc(F)cc1)C	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	118	train
FC(F)(F)c1cc(ccc1)C[NH2+]C[C@@H](O)[C@@H](NC(=O)c1cc(N2CCCC2=O)c2nccc(c2c1)CC)Cc1ccccc1	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	119	test
Clc1cc(-c2cc3c(Oc4c(cc(OC)cc4)[C@@]34N=C(OC4)N)cc2)c(F)cc1	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	120	test
Brc1cscc1C[C@H](NC1=[NH+]C(Cc2c1ccc(Cl)c2)(C)C)C(=O)[O-]	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	121	train
Clc1ccc(nc1)C(=O)Nc1cc(ccc1)[C@]1([NH+]=C(N)CN(C)C1=O)C	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	122	test
O(C)c1cc(ccc1)-c1cc(ccc1)[C@]1(N=C(N)N(C)C(=O)C1)C	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	123	train
S(=O)(=O)(N(C)c1cc2cc(c1)C(=O)N[C@@H](COC\C=C\C[C@H](NC2=O)c1ccccc1)[C@H](O)C[NH2+]Cc1cc(ccc1)C(C)C)C	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	124	test
Clc1ccccc1-c1n(Cc2nc(N)ccc2)c(cc1)-c1ccc(OCCCC#N)cc1	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	125	train
Fc1ccc(NC(=O)c2ncc(cc2)C#N)cc1[C@]1(N=C(OC[C@H]1F)N)C	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	126	train
Clc1cc2CC([NH+]=C(N[C@@H](Cc3cscc3-c3cn[nH]c3)C(=O)[O-])c2cc1)(C)C	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	127	test
Clc1cc2CC([NH+]=C(N[C@@H](Cc3ccccc3)C=3NC(=O)C(=CN=3)C#N)c2cc1)(C)C	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	128	test
s1cc(cc1C1([NH2+]C[C@@H](O)[C@@H](NC(=O)C)Cc2cc(F)cc(F)c2)CC1)CC(C)(C)C	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	129	train
S(CC[C@H](NC(=O)CCC(C)C)C(=O)N[C@H]([C@@H](O)C[C@H](C(=O)NCCCC)C)CC(C)C)C	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	130	train
Clc1ccccc1-c1scc(-c2ccc(OCCC)cc2)c1CC(=O)NC(=[NH2+])N	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	131	test
O=C1N[C@@H](C[C@@H](CCCCCCCC(=O)N[C@H]1C)C)[C@@H](O)C[C@H](C(=O)NCCCC)C	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	132	test
Brc1cc(ccc1)C(=O)Nc1ccc(cc1)-c1n(CC(=O)NC(=[NH2+])N)c(cc1)-c1ccccc1	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	133	test
O(CCC)c1cc(cc(N2CCCC2=O)c1)C(=O)N[C@H]([C@H](O)C[NH2+][C@H](C(=O)NC1CCCCC1)C)Cc1ccccc1	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	134	train
O=C1N(C)C(N[C@@]1(CC1CCCCC1)CCC1CCCCC1)=N	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	135	test
Clc1cc2CC([NH+]=C(N[C@@H](Cc3cscc3CCC)C(=O)[O-])c2cc1)(C)C	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	136	train
s1c2c(nc1C)C(=[NH+][C@@]2(c1cc(ccc1)-c1cncnc1)c1ccc(OC)cc1)N	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	137	test
Clc1ccccc1-c1n(CC(=O)NC(=[NH2+])N)c(cc1)-c1ccc(Oc2ccc(cc2)C(=O)C)cc1	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	138	test
Clc1cc2CC([NH+]=C(N[C@@H](Cc3ccccc3)C3=NOC(=O)[N-]3)c2cc1)(C)C	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	139	test
Fc1ccc(NC(=O)c2ncc(cc2)C#N)cc1[C@]1(N=C(O[C@H](C1)C(F)(F)F)N)C	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	140	train
Brc1cc(ccc1O)C[C@@H]1CS(=O)(=O)C[C@H]([NH2+]Cc2cc(ccc2)C2CC2)[C@H]1O	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	141	test
Clc1cc(cc(Cl)c1NC(=O)C)C\N=C(\NC(=O)Cn1c2c(cccc2)cc1)/N	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	142	test
Fc1cc(cc(F)c1)C[C@H](NC(=O)c1cc(cc(c1)C)C(=O)N(CCC)CCC)[C@H](O)[C@@H]1[NH2+]CCN(C1)C(=O)c1ccccc1	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	143	test
Brc1cc(cc(F)c1N)C[C@@H]1CS(=O)(=O)C[C@H]([NH2+]Cc2cc(ccc2)C(F)(F)C)[C@H]1O	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	144	train
S(Oc1cc(cc(OCC(=O)NCCCCC[NH3+])c1)C(=O)N[C@H](C)c1ccc(F)cc1)(=O)(=O)Cc1ccccc1	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	145	test
O=C1N(C)C(=N[C@@]1(C12CC3CC(C1)CC(C2)C3)c1ccccc1)N	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	146	train
S(=O)(=O)(N(C)c1nc2CC[C@@H](CCc3cc(C[C@]([NH3+])(C)C(OCc(c1)c2)=O)ccc3)C)C	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	147	test
S(=O)(=O)(CCCCC)c1cc(ccc1)C(=O)N[C@H]([C@H](O)C[NH2+][C@H](C(=O)NC1CCCCC1)C)Cc1ccccc1	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	148	test
S1(=O)(=O)N([C@]2(C[C@@H]([N@H+](CC2)Cc2cc(OC(C)C)ccc2)C)CN1C)c1cc(F)ccc1	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	149	train
Fc1cc(N2C3(CC[NH+](CC3)Cc3ccc(NC(=O)C)cc3)C(=NC2=O)NC2CCCCC2)ccc1	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	150	test
Fc1ncccc1-c1cc(ccc1)[C@]1(N=C(OC1)N)c1ccc(OC)cc1	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	151	test
O(C)c1ccc(cc1)[C@@]1([NH+]=C(N)[C@H](OC)C1)c1cc(ccc1)-c1cccnc1	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	152	test
Fc1cc(ccc1OC)[C@H](Cc1cc([N+](=O)[O-])ccc1OC)c1nc([nH]c1)N	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	153	test
O=C(N[C@H]([C@@H](O)C[C@H](C(=O)NCCCC)C)Cc1ccccc1)[C@H]1C[C@H](CCC1)C(NC(=O)C)(C)C	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	154	train
O=C(NC(=[NH2+])N)Cn1c(ccc1-c1ccccc1)-c1ccccc1	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	155	test
Brc1cc2c(S(=O)(=O)CC[C@@H]2OC(=O)[C@@H]2[NH2+]C[C@]3(C2)c2c(NC3=O)cccc2)cc1	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	156	test
O(Cc1ncccc1)c1ccc(cc1CNc1cccnc1N)-c1cc2[nH]ccc2cc1	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	157	test
Fc1cc(cc(F)c1)C[C@H](NC(=O)c1cc(cc(c1)C)C(=O)N(CCC)CCC)[C@@H](O)C[NH2+]Cc1cc(OC)ccc1	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	158	train
O(C)c1cc(ccc1)-c1cc(ccc1)[C@@H]1C[C@@H]1C=1N=C(N)N(C)C(=O)C=1	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	159	test
Brc1cc(ccc1C#N)COC(=O)[C@@H]1[NH2+]C[C@]2(C1)c1c(NC2=O)cccc1	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	160	train
Clc1cc(ccc1)-c1cc(ccc1)[C@@]1(OCCC(=[NH+]1)N)C	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	161	test
O=C1N(Cc2ccc(cc2)CNC(=O)Nc2ccc(cc2)C#N)C(N[C@@]1(CC(C)C)C)=N	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	162	test
Clc1cc2nc(n(c2cc1)[C@H](CC(=O)NCC1CCCCC1)CC)N	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	163	train
O(C)c1ccc(cc1)[C@@]1([NH+]=C(N)CC1)c1cc(ccc1)-c1cncnc1	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	164	test
Clc1cc2nc(n(c2cc1)[C@H](CC(=O)NC1C2CC3CC1CC(C2)C3)CC)N	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	165	test
[nH]1c2cc(ccc2cc1)-c1cc(ccc1)CNc1cccnc1N	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	166	test
Clc1cc(cnc1)-c1cc(ccc1)[C@@]12N=C(O[C@@H]1CCCC2)N	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	167	test
O=C1Nc2c(cccc2)[C@]12C[C@@H]([NH2+]C2)C(OCc1ccc(cc1)C#N)=O	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	168	train
O=C1N(C)C(=NC(=C1)[C@H]1C[C@H]1c1ccc(cc1)-c1cc(ccc1)C)N	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	169	test
O=C1N(C)C(N[C@](C1)(C)[C@@H]1C[C@H]1c1ccccc1)=N	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	170	test
Brc1cc2c(SCC[C@@H]2OC(=O)[C@@H]2[NH2+]C[C@]3(C2)c2c(NC3=O)cccc2)cc1	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	171	test
S(=O)(=O)(Nc1cc(Nc2ncnc(c2)-c2ccccc2)ccc1C)C	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	172	test
O(C)c1cc(ccc1)-c1cc(ccc1)CCc1nc(N)ccc1	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	173	test
O(C(=O)[C@@H]1[NH2+]C[C@]2(C1)c1c(NC2=O)cccc1)C1(CCCCC1)C#N	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	174	test
Clc1cc2nc(n(c2cc1)CCCC(=O)N(C)C1CCCCC1)N	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	175	test
O=C([O-])[C@@H](\[NH+]=C\1/NC(Cc2c/1cccc2)(C)C)Cc1ccccc1	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	176	test
Brc1cc2c(OC(C[C@@]23N=C(N)N(C)C3=O)(C)C)cc1	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	177	test
[NH+]=1C(C=2N(CCCN=2)C=1N)(c1ccccc1)c1ccccc1	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	178	train
O(C)c1cc(cnc1)-c1cc(ccc1)CNc1cccnc1N	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	179	train
S1CC[C@@](N=C1N)(C)c1ccc(OC)cc1	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	180	test
O=C1N(C)C(=N[C@@](C1)(CCc1ccccc1)C)N	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	181	train
O=C1N(Cc2ccc(cc2)CNC(=O)NCCCC)C(N[C@@]1(CC(C)C)C)=N	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	182	train
O=C1Nc2c(cccc2)[C@]12C[C@@H]([NH2+]C2)C(OCc1ccccc1)=O	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	183	train
[nH]1c2cc(ccc2cc1)CCc1nc(N)ccc1	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	184	test
O1[C@@H]2COCC[C@@]2(N=C1N)c1cc(ccc1)-c1cncnc1	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	185	test
[NH+]=1[C@](N=C(c2ccccc2)C=1N)(C)c1cc(ccc1)-c1cccnc1	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	186	test
n1cccc(NCc2cc(ccc2)-c2cccnc2)c1N	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	187	train
O1CCC(OC(=O)[C@@H]2[NH2+]C[C@]3(C2)c2c(NC3=O)cccc2)CC1	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	188	test
O=C1NC(=NC(=C1)CCc1cc2[nH]ccc2cc1)N	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	189	test
Clc1cc(ccc1OCCCC)CSC(=[NH2+])N	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	190	train
o1cccc1C[N@H+](Cc1cc(ccc1)CCc1cccnc1N)C	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	191	test
n1cccc(NCc2ccccc2)c1N	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	192	test
Clc1cc(ccc1)CN1C(=O)[C@](NC1=N)(CC(C)C)C	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	193	train
Fc1ccc(cc1)CC1CC[NH2+]CC1	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	194	test
O=C1N(C)C(=NC(=C1)[C@H]1C[C@H]1c1ccccc1)N	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	195	test
Clc1cc(ccc1)CN1C(=O)C(NC1=N)(C)C	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	196	train
Clc1cc2nc(n(c2cc1)CCCO)N	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	197	train
n1c2c(nc(N)c1N1CCCC1)cccc2	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	198	test
Clc1cc(ccc1)CCc1cccnc1N	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	199	test