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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)c(OCCO)cc2)c(cc1)-c1ccc(OCCCCC)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	800	train
s1cc(nc1)-c1cc(ccc1)C1([NH2+]CC(O)C(NC(=O)C)Cc2cc(F)cc(F)c2)CCCCC1	[ "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	801	valid
Fc1cc(cc(F)c1)C[C@H](NC(=O)C)[C@H](O)C[NH2+]C1(CCOCC1)c1cc(-n2nccc2)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	802	valid
FC(F)Oc1ccc(cc1)[C@@]1(N=C(N)N(C)C1=O)c1cc(ccc1)C[C@@H](CC)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	803	train
S1(=O)(=O)N(CCCC1)c1cc(cc(c1)/C(=N\OCC=C)/C)C(=O)N[C@H]([C@@H](O)C[NH2+]Cc1cc(OC)ccc1)Cc1cc(F)cc(F)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	804	train
O1c2c(cc(cc2)-c2cccnc2)C2(N=C(N)N(C)C2=O)CC1(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	805	train
S1(=O)(=O)N(CCCC1)c1cc(cc(NCC)c1)C(=O)NC(Cc1ccccc1)C(O)C[NH2+]C1CC1	[ "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	806	valid
Fc1cc(cc(F)c1)CC(NC(=O)C)C(O)C[NH2+]C1(CCC(=O)CC1)c1cc(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	807	valid
O(C)c1ccc(cc1C1CCCC1)C1(N=C(N)N(C)C1=O)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	808	valid
O1CCc2cc(ccc12)C1(N=C(N)N(C)C1=O)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	809	valid
OC(C(NC(=O)C(NC(=O)C(NC(=O)C)CC(C)C)C)CC(C)C)CC(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	810	train
Fc1cc(cc(F)c1)CC(NC(=O)C)C(O)C[NH2+]C1(CCCCC1)c1cc(ccc1)-c1ccoc1	[ "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	811	valid
Fc1ccc(cc1OCCF)[C@]1(N=C(N)N(C)C1=O)c1ccc(OC(F)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	812	train
Fc1cc(cc(F)c1)CC(NC(=O)c1c2c(n(c1)C(=O)N(CCCC)C)cc(cc2)C#N)C(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	813	train
Fc1ccc(cc1-c1cncnc1)C1(N=C(N)N(C)C1=O)c1cn(nc1)CC(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	814	train
S1(=O)(=O)CC(Cc2cc3c([nH]cc3CC(F)(F)F)cc2)C(O)C([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	815	train
S1(=O)(=O)CC(Cc2cc(O)c(N)c(F)c2)C(O)C([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	816	train
Clc1ccc(nc1)C(=O)Nc1cc(C2(Oc3c(cccc3)C(=N2)N)C)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	817	valid
Fc1cc(cc(F)c1)CC(NC(=O)c1cc(cc(c1)C(=O)N(CCC)CCC)C([NH3+])C)C(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	818	train
S(=O)(=O)(N(C)c1cc(cc(c1)C(=O)N[C@H]([C@@H](O)C[NH2+]Cc1cc(OC)ccc1)Cc1cc(F)cc(F)c1)C(=O)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	819	train
Fc1c2c(ccc1)C(N=C2N)(c1cc(ccc1)-c1cncnc1)c1ccncc1	[ "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	820	train
S(=O)(=O)(N(c1ccccc1OC)c1cc(ccc1)C(=O)NC(Cc1ccccc1)C(O)C[NH2+]C(C(=O)NC1CCCCC1)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	821	train
Oc1ccc(cc1-c1nccc(c1)C#CC)C1(N=C(C)C(=N1)N)C1CC1	[ "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	822	valid
Fc1ncccc1-c1cc2c(OC(CC23N=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	823	train
Fc1ncccc1-c1cc(ccc1)[C@]1([NH+]=C(N2C1=NCCCCC2)N)c1ccc(OC(F)(F)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	824	valid
O(C)c1ccc(cc1C)C1(N=C(N)N(C)C1=O)c1cc(-c2cccnc2)c(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	825	train
O=C1N(C)C(=NC1(c1cc(ccc1)-c1ccccc1)c1ccncc1)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	826	train
Fc1cc(cc(F)c1)CC(NC(=O)C)C(O)C[NH2+]C1(CCCCC1)c1cc(ccc1)C(CC)(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	827	train
S1(=O)(=O)CC(Cc2cc(OC(F)(F)F)c(N)cc2)C(O)C([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	828	train
S1(=O)(=O)CC(Cc2cc(CCC)c(N)c(F)c2)C(O)C([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	829	train
S1(=O)(=O)CC(Cc2cc(CCC(F)(F)F)c(N)c(F)c2)C(O)C([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	830	train
Clc1cc(ccc1)-c1cc2c(Oc3c(cc(OC)cc3)C23N=C(OC3)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	831	train
s1cc(cc1C1([NH2+]CC(O)C(NC(=O)C)Cc2cc(F)cc(F)c2)CCCCC1)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	832	train
FC(F)(F)c1nccc(c1)C1(N=C(N)c2c1cccc2)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	833	train
Fc1c2c(ccc1)C(N=C2N)(c1cc(ccc1)-c1cncnc1)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	834	train
Fc1c2c(ccc1)C(N=C2N)(c1cc(ccc1)-c1cc(F)cnc1)c1ccncc1	[ "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	835	train
Clc1ccc(nc1)C(=O)Nc1cc(C2(N=C(OCC2)N)C)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	836	train
Fc1cc(cc(F)c1)CC(NC(=O)C)C(O)C[NH2+]C1(CCCCC1)c1onc(c1)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	837	train
Fc1cc(cc(F)c1)CC(NC(=O)C)C(O)C[NH2+]C1(CCC(OC)CC1)c1cc(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	838	train
S(=O)(=O)(N(C)c1cc(cc(c1)C(=O)NC(C(O)CC(OC)COCc1ccc(OC)cc1)COc1cc(F)cc(F)c1)C(=O)NC(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	839	train
O=C1N(C)C(=N[C@]1(c1cc(nc(c1)C)C)c1cc(ccc1)-c1cncnc1)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	840	train
Fc1cc(cc(F)c1)CC(NC(=O)C)C(O)C[NH2+]C1(CC1)c1cc(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	841	train
s1cc(cc1C)C1(N=C(N)N(C)C1=O)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	842	train
Fc1cc(cc(F)c1)CC(NC(=O)C(N1CCC(NC(=O)C)(C(CC)C)C1=O)CCc1ccccc1)[C@H](O)[C@H]1[NH2+]Cc2c(C1)cccc2OC	[ "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	843	train
Brc1cc(ccc1N)CC1CS(=O)(=O)CC([NH2+]Cc2cc(ccc2)C(C)(C)C)C1O	[ "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	844	train
O1c2ncc(cc2C([NH2+]CC(O)C(NC(=O)C(C)C)Cc2cc3OCOc3cc2)CC12CCC2)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	845	train
Fc1cc(cnc1)-c1cc2c(OC(CC23N=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	846	train
S1(=O)(=O)N(c2c(CCC1)c(NCC)cc(c2)C(=O)NC(Cc1ccccc1)C(O)C[NH2+]C1CC1)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	847	valid
O(C)c1ccc(cc1C#N)C1(N=C(N)N(C)C1=O)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	848	train
O=C1N(C)C(=N[C@]1(c1cc(nc(c1)C)CC)c1cc(ccc1)-c1cncnc1)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	849	train
OC(C(NC(=O)C1CC(CCC1)C(N(C(=O)CC)C)(C)C)Cc1ccccc1)C[NH2+]Cc1cc(ccc1)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	850	train
S1(=O)(=O)CC(Cc2cc(CCCC)c(O)cc2)C(O)C([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	851	train
S1(=O)(=O)CC(Cc2cc(-c3ccoc3)c(N)c(F)c2)C(O)C([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	852	valid
S(=O)(=O)(N(C)c1cc(cc(c1)/C(=N\OCC=C)/C)C(=O)N[C@H]([C@@H](O)C[NH2+]Cc1cc(OC)ccc1)Cc1cc(F)cc(F)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	853	train
O1c2c(cc(cc2)-c2cncnc2)C2(N=C(N)N(C)C2=O)CC1(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	854	valid
Clc1cn(nc1C(=O)Nc1cc(C2(N=C(OCC2(F)F)N)C)c(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	855	train
Fc1ncccc1-c1cc(ccc1)C1([NH+]=C(N2C1=NCCC2)N)c1cc2OCOc2cc1	[ "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	856	valid
Fc1cc(cc(F)c1)CC(NC(=O)C)C(O)C[NH2+]C1(CCCCC1)c1cc(cc(c1)C(=O)C)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	857	train
Fc1cc(cc(F)c1)CC(NC(=O)c1c2cc(ccc2n(c1)C(=O)N(CCCC)C)C(F)(F)F)C(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	858	train
Fc1cc(cc(F)c1)CC(NC(=O)C(N1CCC(C(C)C)C1=O)C)C(O)C1[NH2+]CC(OCCC)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	859	train
Fc1cc(cc(F)c1)CC(NC(=O)C)C(O)C[NH2+]C1(CCCCC1)c1cc(ccc1)C(C#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	860	train
Clc1ccccc1-c1n(Cc2nc(N)c(NCCO)cc2)c(cc1)-c1ccc(OCCCCC)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	861	train
Fc1cc(cc(F)c1)CC(NC(=O)C)C(O)C[NH2+]C1(CCCCC1)c1cc(cc(O)c1)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	862	train
FC(F)Oc1ccc(cc1)[C@@]1(N=C(N)N(C)C1=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	863	train
Fc1cc(cc(F)c1)CC(NC(=O)C(N1CCC(C(C)C)C1=O)C)C(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	864	train
O(C)c1cc(ccc1)-c1cc(ccc1)C1(N=C(C)C(=N1)N)c1ccncc1	[ "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	865	valid
Clc1cc2CC(N=C(NC(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	866	valid
S(=O)(=O)(N(C)c1cc(cc(c1)/C(=N\OCC(C)C)/C)C(=O)N[C@H]([C@@H](O)C[NH2+]Cc1cc(OC)ccc1)Cc1cc(F)cc(F)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	867	train
Brc1cc(cc(c1)C(C)(C)C)C1([NH2+]CC(O)C(NC(=O)C)Cc2cc(F)cc(F)c2)CCCCC1	[ "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	868	train
FCC([NH2+]CC(O)C1NC(=O)c2cc(cc(NCCCCOc3cc(C1)ccc3)c2)COC)c1cc(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	869	train
S(=O)(=O)(N(Cc1ccccc1)c1cc(ccc1)C(=O)NC(Cc1ccccc1)C(O)C[NH2+]C(C(=O)NC1CCCCC1)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	870	valid
Fc1cc(cc(F)c1)CC(NC(=O)C)C(O)C[NH2+]C1(CCCCC1)c1cc(ccc1)C1OCCC1	[ "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	871	valid
Fc1cc(cc(F)c1)CC(NC(=O)C)C(O)C[NH2+]C1(CCCCC1)c1cc(cc(c1)C)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	872	train
s1c(C)c(cc1CC)C1(N=C(N)N(C)C1=O)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	873	train
S(=O)(=O)(N(C)c1cc2cc(c1)C(=O)NCCC\C=C\COCC(NC2=O)C(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	874	valid
S1(=O)(=O)N(c2c(CCC1)c(NCC)cc(c2)C(=O)NC(Cc1ccccc1)C(O)C[NH2+]C1CCOCC1)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	875	valid
Fc1ncccc1-c1cc(ccc1)[C@]1([NH+]=C(N2C1=NCCC2)N)c1cc2OCCOc2cc1	[ "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	876	train
Fc1ncccc1-c1cc(ccc1)[C@]1([NH+]=C(N2CC(N=C12)(C)C)N)c1ccc(OC(F)(F)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	877	train
S(=O)(=O)(N(c1cc(ccc1)C(=O)NC(Cc1ccccc1)C(O)C[NH2+]C(C(=O)NC1CCCCC1)C)c1ccc(cc1)C#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	878	train
Fc1cc(cc(F)c1)CC(NC(=O)c1c2c(n(c1)C(=O)NCCCC)cccc2)C(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	879	train
S1(=O)(=O)CC(Cc2cc(CCC)c(O)cc2)C(O)C([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	880	train
Fc1cc(cc(F)c1)C[C@H](NC(=O)C)[C@H](O)C[NH2+]C(C)(C)c1cc(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	881	train
FC(F)(F)CCOc1cc(ccc1)[C@]1(N=C(N)N(C)C1=O)c1ccc(OC(F)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	882	train
FC(F)Oc1cc(ccc1)[C@]1(N=C(N)N(C)C1=O)c1ccc(OC(F)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	883	train
S1(=O)(=O)CC(Cc2cc3c([nH]cc3CC)cc2)C(O)C([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	884	train
FC(F)(F)Oc1ccc(cc1)[C@@]1([NH+]=C(N2C1=NCCC2)N)c1cc(ccc1)CCC1CC1	[ "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	885	train
S(=O)(=O)(C)C1CCC([NH2+]CC(O)C(NC(=O)C)Cc2cc(F)cc(F)c2)(CC1)c1cc(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	886	train
Fc1cc(cc(F)c1)CC(NC(=O)C)C(O)C[NH2+]C1(CCC(NC=O)CC1)c1cc(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	887	train
O=C1N(C)C(=N[C@]1(C1CCCCC1)c1cc(NC(=O)COC)ccc1)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	888	train
S(=O)(=O)(N(c1cc(ccc1)C(=O)NC(Cc1ccccc1)C(O)C[NH2+]Cc1cc(ccc1)C(F)(F)F)c1ccncc1)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	889	train
Fc1cc(cc(F)c1)CC(NC(=O)C)C(O)C[NH2+]C1(CCCCC1)c1nn(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	890	train
Fc1cc(cc(F)c1)CC(NC(=O)c1c2cccnc2n(c1)C(=O)N(CC1CC1)CCC)C(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	891	train
S1(=O)CC(Cc2cc(OC(COC)C(F)(F)F)c(N)c(F)c2)C(O)C([NH2+]Cc2cc(OC(F)(F)F)ccc2)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	892	train
Fc1cc(cc(F)c1)CC(NC(=O)C)C(O)C[NH2+]C1(CCCC1)c1cc(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	893	train
Clc1ccccc1-c1n(Cc2nc(N)c(NCCCO)cc2)c(cc1)-c1ccc(OCCCCC)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	894	train
S1(=O)(=O)CC(Cc2cc3c([nH]nc3CCC)cc2)C(O)C([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	895	train
Ic1cc(cc(c1)C(C)(C)C)C1([NH2+]CC(O)C(NC(=O)C)Cc2cc(F)cc(F)c2)CCCCC1	[ "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	896	train
Clc1cc(cc(Cl)c1NC(=O)C)CNC(=[NH2+])NC(=O)Cn1c2cc(OC)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	897	train
S1(=O)CC(Cc2cc(OC(COC)C(F)(F)F)c(N)c(F)c2)C(O)C([NH2+]Cc2nccc(c2)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	898	train
Fc1cc(cc(F)c1)C[C@H](NC(=O)C)[C@H](O)C[NH2+]C1(CC1)c1cc(ccc1)C(C(F)F)(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	899	train