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stringclasses 1
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stringclasses 1
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FC(F)(F)c1cc(ccc1)C[NH2+]CC(O)C(NC(=O)c1cc(N2CCCC2=O)c(C)c(NCC)c1)Cc1ccccc1 | [
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?",
"The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?",
"The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?"
] | Yes | bace | 0 | 700 | train |
FC(F)(F)c1cc(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?"
] | Yes | bace | 0 | 701 | train |
O1c2ncc(cc2C([NH2+]CC(O)C(NC(=O)COC)Cc2cc(ccc2)-c2nccn2C)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?"
] | Yes | bace | 0 | 702 | valid |
Fc1cc(cc(F)c1)CC(NC(=O)c1c2c(n(c1)C(=O)N(CCCC)C)cc(F)cc2)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?"
] | Yes | bace | 0 | 703 | train |
FC1(F)COC(=NC1(C)c1cc(NC(=O)c2ncc(F)cc2)ccc1F)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?"
] | Yes | bace | 0 | 704 | train |
Fc1cc(cc(F)c1)CC(NC(=O)c1cc(cc(c1)/C(=N\OCc1ccccc1)/C)C(=O)N(CCC)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?"
] | Yes | bace | 0 | 705 | valid |
O1CCCCNc2cc(cc(c2)C(=O)NC(Cc2cc1ccc2)C(O)C[NH2+]C1(CCC1)c1cc(ccc1)C(C)(C)C)COC | [
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?",
"The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?",
"The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?"
] | Yes | bace | 0 | 706 | valid |
Clc1cnc(nc1)C(=O)Nc1cc(C2(N=C(OCC2(F)F)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?"
] | Yes | bace | 0 | 707 | valid |
Fc1cc(cc(F)c1)CC(NC(=O)C(N1CCC(C(O)CCC)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?"
] | Yes | bace | 0 | 708 | train |
S1(=O)(=O)CC(Cc2cc(OC(C(F)(F)F)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?"
] | Yes | bace | 0 | 709 | train |
O1c2c(cc(cc2)-c2cc(OC)ccc2)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?"
] | Yes | bace | 0 | 710 | train |
Fc1ncccc1-c1cc(ccc1)C1([NH+]=C(N2C1=NCCC2)N)c1ccc(OC)cc1 | [
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?",
"The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?",
"The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?"
] | Yes | bace | 0 | 711 | train |
O(C)c1ccc(cc1)C1(N=C(N)N(C)C1=O)C12CC3CC(C1)CC(C2)C3 | [
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?",
"The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?",
"The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?"
] | Yes | bace | 0 | 712 | train |
O(c1cc(ccc1OC)C1(N=C(N)N(C)C1=O)c1cc(ccc1)-c1cccnc1)C1CCCC1 | [
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?",
"The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?",
"The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?"
] | Yes | bace | 0 | 713 | valid |
O=C1N(C)C(=NC1(c1cc(ccc1)-c1cncnc1)c1cc(ncc1)C(C)C)N | [
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?",
"The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?",
"The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?"
] | Yes | bace | 0 | 714 | train |
O=C1N(C)C(=NC1(c1cc(ccc1)-c1nccnc1)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?"
] | Yes | bace | 0 | 715 | valid |
Clc1ccccc1-c1n(Cc2nc(N)c(NCCO)cc2)c(cc1)-c1ccc(Oc2cncnc2)cc1 | [
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?",
"The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?",
"The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?"
] | Yes | bace | 0 | 716 | train |
Fc1ccc(cc1OCC(F)F)[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?"
] | Yes | bace | 0 | 717 | train |
Fc1ccc(cc1OCC(F)F)[C@]1(N=C(N)N(C)C1=O)c1cc(C)c(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?"
] | Yes | bace | 0 | 718 | train |
Fc1cc(cc(F)c1)CC(NC(=O)c1c2cc(ccc2n(c1)C(=O)N(CCCC)C)C(=O)[O-])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?"
] | Yes | bace | 0 | 719 | train |
Fc1cc(cc(F)c1)CC(NC(=O)C(N1CCC(C(O)CCC)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?"
] | Yes | bace | 0 | 720 | train |
O=C1N(C)C(=NC1(c1cc(ccc1)-c1cncnc1)c1cn(nc1)C1CCCC1)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?"
] | Yes | bace | 0 | 721 | valid |
s1cc(cc1)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?"
] | Yes | bace | 0 | 722 | train |
Brc1cc2c(cc1)C1(CCC2)C[NH2+]CC1C(=O)N1CCC(CC1c1ccccc1)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?"
] | Yes | bace | 0 | 723 | valid |
O1c2c(cc(cc2)-c2cc(OCC)ccc2)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?"
] | Yes | bace | 0 | 724 | train |
s1ccnc1-c1cccc(CC(NC(=O)COC)C(O)C[NH2+]C2CC3(Oc4ncc(cc24)CC(C)(C)C)CCC3)c1F | [
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?",
"The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?",
"The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?"
] | Yes | bace | 0 | 725 | train |
S1(=O)(=O)N(c2cc(cc3c2n(cc3CC)CC1)C(=O)NC([C@H](O)C[NH2+]CC#C)Cc1ccccc1)C | [
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?",
"The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?",
"The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?"
] | Yes | bace | 0 | 726 | train |
Fc1cc(cc(F)c1)CC(NC(=O)C)C(O)C[NH2+]C1(CCC(Nc2ncccc2)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?"
] | Yes | bace | 0 | 727 | valid |
Fc1cc(cc(F)c1)CC(NC(=O)c1c2cccnc2n(c1)C(=O)N(CCOC)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?"
] | Yes | bace | 0 | 728 | train |
S1(=O)(=O)N(CCCC1)c1cc(ccc1)C(=O)NC(Cc1cc(F)cc(F)c1)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?"
] | Yes | bace | 0 | 729 | train |
FC(F)(F)c1cc(ccc1)-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?"
] | Yes | bace | 0 | 730 | train |
S(=O)(=O)(N(C)c1cc(ccc1)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?"
] | Yes | bace | 0 | 731 | train |
S1(=O)(=O)CC(Cc2cc(OCCC(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?"
] | Yes | bace | 0 | 732 | train |
Fc1cc(cc(F)c1)CC(NC(=O)C(N1CCC(C(C)C)C1=O)CCc1ccccc1)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?"
] | Yes | bace | 0 | 733 | train |
S(=O)(=O)(N(C)c1cc(cc(c1)/C(=N\O)/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?"
] | Yes | bace | 0 | 734 | train |
Fc1ccccc1C(=O)NC(Cc1cc2OCOc2cc1)C(O)C[NH2+]C1CC2(Oc3ncc(cc13)CC(C)(C)C)CCC2 | [
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?",
"The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?",
"The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?"
] | Yes | bace | 0 | 735 | valid |
Fc1cc(cc(F)c1)CC(NC(=O)C)C(O)C[NH2+]C1(CCCCC1)c1cc(cc(OC)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?"
] | Yes | bace | 0 | 736 | train |
S1(=O)(=O)CC(Cc2cc(CC(OC)C(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?"
] | Yes | bace | 0 | 737 | train |
Fc1c2c(ccc1)C(N=C2N)(c1cc(ccc1)-c1cncnc1)c1nc(C)c(OC)c(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?"
] | Yes | bace | 0 | 738 | valid |
S1(=O)(=O)N(c2cc(cc3n(cc(CC1)c23)CC)C(=O)NC([C@H](O)C[NH2+]CC(F)(F)F)Cc1ccccc1)C | [
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?",
"The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?",
"The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?"
] | Yes | bace | 0 | 739 | train |
S1(=O)(=O)CC(Cc2cc(-c3occc3)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?"
] | Yes | bace | 0 | 740 | valid |
Brc1cc2n(ccc2cc1)CC(=O)NC(=[NH2+])NCc1cc(Cl)c(NC(=O)C)c(Cl)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?"
] | Yes | bace | 0 | 741 | train |
Fc1ncccc1-c1cc(ccc1)C1([NH+]=C(N2C1=NCCC2)N)c1cc(OCC)c(OCC)cc1 | [
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?",
"The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?",
"The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?"
] | Yes | bace | 0 | 742 | train |
Fc1ncccc1-c1cc(ccc1)C1([NH+]=C(N2C1=NCC2)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?"
] | Yes | bace | 0 | 743 | valid |
Fc1ncccc1-c1cc(ccc1)C1([NH+]=C(N2C1=NCCCC2)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?"
] | Yes | bace | 0 | 744 | valid |
O=C1N(C)C(=N[C@@]1(c1cc(ccc1)-c1cncnc1)c1cc(ncc1)C)N | [
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?",
"The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?",
"The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?"
] | Yes | bace | 0 | 745 | train |
FCCCC(=O)c1cc(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?"
] | Yes | bace | 0 | 746 | train |
FCCC[C@@H](F)c1cc(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?"
] | Yes | bace | 0 | 747 | train |
FC(F)Oc1ccc(cc1C)[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?"
] | Yes | bace | 0 | 748 | train |
Fc1ccc(cc1-c1cncnc1)C1(N=C(N)N(C)C1=O)c1cn(nc1)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?"
] | Yes | bace | 0 | 749 | train |
s1cc(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?"
] | Yes | bace | 0 | 750 | train |
Clc1scc(c1)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?"
] | Yes | bace | 0 | 751 | train |
S1(=O)CC(Cc2cc(OC(COC)C(F)(F)F)c(N)c(F)c2)C(O)C([NH2+]Cc2cc(OC(C)C)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?"
] | Yes | bace | 0 | 752 | train |
Fc1cc(cc(F)c1)CC(NC(=O)c1c2cccnc2n(c1)C(=O)N(CCCC)C)C(O)C[NH2+]C1(CC1)c1cc(ccc1)CC | [
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?",
"The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?",
"The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?"
] | Yes | bace | 0 | 753 | valid |
O1CCCCOc2nc(cc(c2)C(=O)NC(Cc2cc1ccc2)C(O)C[NH2+]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?"
] | Yes | bace | 0 | 754 | train |
s1ccnc1NC1CCC([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?"
] | Yes | bace | 0 | 755 | valid |
S1(Oc2cc(cc3c2n(cc3CC)CC1)C(=O)NC([C@H](O)C[NH2+]CC1CCOCC1)Cc1ccccc1)(=O)=O | [
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?",
"The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?",
"The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?"
] | Yes | bace | 0 | 756 | valid |
Fc1c2c(ccc1)C(N=C2N)(c1cc(ccc1)-c1cncnc1)c1cc(ncc1)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?"
] | Yes | bace | 0 | 757 | valid |
FC(F)(F)c1cc(ccc1)C[NH2+]CC(O)C(NC(=O)c1cc(N2CCCC2=O)c2occ(c2c1)CC)Cc1ccccc1 | [
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?",
"The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?",
"The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?"
] | Yes | bace | 0 | 758 | valid |
Fc1cc(cc(F)c1)CC(NC(=O)C(N1CCC(CCCC)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?"
] | Yes | bace | 0 | 759 | train |
FC1(F)COC(=NC1(C)c1cc(NC(=O)c2ncc(cc2)C)ccc1F)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?"
] | Yes | bace | 0 | 760 | 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?"
] | Yes | bace | 0 | 761 | valid |
O=C(NCc1cccnc1)C(Cc1cc2cc(ccc2nc1N)-c1ccccc1C)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?"
] | Yes | bace | 0 | 762 | valid |
Fc1cc(cc(F)c1)CC(NC(=O)C(N1CCC(CC(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?"
] | Yes | bace | 0 | 763 | train |
Fc1c(cccc1OC)-c1cc(ccc1)C1(N=C(N2C1=NCCC2)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?"
] | Yes | bace | 0 | 764 | train |
S1(=O)(=O)N(CCCC1)c1cc(cc(c1)C(=O)N[C@H]([C@@H](O)C[NH2+]Cc1cc(OC)ccc1)Cc1cc(F)cc(F)c1)C(=O)C | [
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?",
"The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?",
"The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?"
] | Yes | bace | 0 | 765 | train |
O(C)c1cc(ccc1OC)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?"
] | Yes | bace | 0 | 766 | train |
O1CCOc2c1cc(cc2)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?"
] | Yes | bace | 0 | 767 | valid |
FC(F)Oc1ccc(cc1)[C@@]1(N=C(N)N(C)C1=O)c1cc(ccc1)CCC | [
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?",
"The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?",
"The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?"
] | Yes | bace | 0 | 768 | train |
FC(F)Oc1ccc(cc1)[C@@]1(N=C(N)N(C)C1=O)c1cc(ccc1)CCCCC | [
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?",
"The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?",
"The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?"
] | Yes | bace | 0 | 769 | train |
FC(F)Oc1ccc(cc1)[C@@]1(N=C(N)N(C)C1=O)c1cc(ccc1)\C=C\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?"
] | Yes | bace | 0 | 770 | train |
s1cc(cc1)C1(N=C(N)N(C)C1=O)c1cc(-c2cccnc2)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?"
] | Yes | bace | 0 | 771 | train |
s1cc(cc1)C1(N=C(N)N(C)C1=O)c1cc(ccc1)-c1nccnc1 | [
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?",
"The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?",
"The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?"
] | Yes | bace | 0 | 772 | valid |
S1(=O)(=O)N(CCCC1)c1cc(cc(NCC)c1)C(=O)NC(Cc1ccccc1)C(O)C[NH2+]C1CCOCC1 | [
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?",
"The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?",
"The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?"
] | Yes | bace | 0 | 773 | valid |
S1(=O)(=O)N(c2cc(cc3c2n(cc3CC)C1)C(=O)NC(Cc1ccccc1)C(O)C[NH2+]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?"
] | Yes | bace | 0 | 774 | train |
O1c2ncc(cc2C([NH2+]CC(O)C(NC(=O)C)Cc2ccccc2)CC12CCC2)CC | [
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?",
"The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?",
"The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?"
] | Yes | bace | 0 | 775 | train |
O(C)c1ccc(cc1)C1(N=C(N2C1=NCCC2)N)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?"
] | Yes | bace | 0 | 776 | train |
Fc1cc(cc(F)c1)CC(NC(=O)C)C(O)C[NH2+]C1(CCc2nc(ncc2C1)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?"
] | Yes | bace | 0 | 777 | train |
S(=O)(=O)(Nc1cc(cc(c1)C(C)(C)C)C1([NH2+]CC(O)C(NC(=O)C)Cc2cc(F)cc(F)c2)CCCCC1)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?"
] | Yes | bace | 0 | 778 | train |
S1(=O)(=O)CC(Cc2cc(C3CC3)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?"
] | Yes | bace | 0 | 779 | valid |
Fc1cc(cc(F)c1)CC(NC(=O)C(N1CCC(CCCC)C1=O)C)C(O)C1[NH2+]CC(O)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?"
] | Yes | bace | 0 | 780 | train |
Clc1ccc(nc1)C(=O)Nc1cc(C2(N=C(N)C3C(C2)C3)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?"
] | Yes | bace | 0 | 781 | valid |
O(C)c1cccnc1-c1cc2cc(CC(C(=O)NCCC(C)(C)C)C)c(nc2cc1)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?"
] | Yes | bace | 0 | 782 | train |
O(C)c1ccc(cc1C)C1(N=C(C)C(=N1)N)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?"
] | Yes | bace | 0 | 783 | train |
Fc1cc(ccc1)-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?"
] | Yes | bace | 0 | 784 | train |
O(C)c1ccc(cc1)[C@@]1([NH+]=C(N2C1=NCCC2)N)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?"
] | Yes | bace | 0 | 785 | valid |
Fc1cc(cc(F)c1)CC(NC(=O)C)C(O)C[NH2+]C1(CCC(NOC)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?"
] | Yes | bace | 0 | 786 | train |
o1cccc1C(=O)Nc1cc(ccc1)C1(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?"
] | Yes | bace | 0 | 787 | train |
O=C1N(C)C(=N[C@@]1(c1cc(ccc1)-c1cccnc1)c1cc(ncc1)C)N | [
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?",
"The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?",
"The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?"
] | Yes | bace | 0 | 788 | train |
Fc1cc(cc(F)c1)CC(NC(=O)C)C(O)C[NH2+]C1(CCCCC1)c1cc(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?"
] | Yes | bace | 0 | 789 | train |
Fc1ccc(cc1OCCCCF)[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?"
] | Yes | bace | 0 | 790 | train |
O=C1N(C)C(=NC1(c1cc(ccc1)-c1cncnc1)c1cn(nc1)C)N | [
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?",
"The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?",
"The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?"
] | Yes | bace | 0 | 791 | train |
FC1(F)CN2C(=NC1)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?"
] | Yes | bace | 0 | 792 | train |
S1(=O)(=O)CC(Cc2cc(OCCOC)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?"
] | Yes | bace | 0 | 793 | train |
s1cc(cc1C1([NH2+]CC(O)C(NC(=O)C)Cc2cc(F)cc(F)c2)CCCCC1)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 | 0 | 794 | train |
Brc1cc2c(n(cc2)CC(=O)NC(=[NH2+])NCc2cc(Cl)c(NC(=O)C)c(Cl)c2)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 | 0 | 795 | train |
O1CC2(N=C1N)c1cc(ccc1Oc1c2cc(OC)cc1)-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 | 0 | 796 | train |
FC1(F)CN2C(=NC1)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 | 0 | 797 | valid |
FC1(F)COC(=NC1(C)c1cc(NC(=O)c2ncc(OCC(F)(F)F)cc2)ccc1F)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 | 0 | 798 | train |
FC(F)(F)c1cc(ccc1)C[NH2+]CC(O)C(NC(=O)c1cc(N2CCCC2=O)c(OC)c(NCC)c1)Cc1ccccc1 | [
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?",
"The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?",
"The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?",
"BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?"
] | No | bace | 0 | 799 | train |