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haitengzhao
/
molecule_property_instruction

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Fc1cc(NC[C@@H](O)[C@@H](NC(=O)C=2[C@H](CCC)C(C(=O)C)=C(N(CC(OC(C)C)=O)C=2C)C)Cc2ccccc2)ccc1
[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]
No
bace
0
1400
train
O=C([O-])C(NC1=NC(Cc2c1cccc2)(C)C)Cc1ccccc1
[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]
No
bace
0
1401
train
Fc1ccc(nc1)C(=O)Nc1cc(ccc1)C12N=C(OC1COCC2)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
1402
train
O(C(=O)C=1[C@@H](C)C(C(=O)N[C@H]([C@H](O)C[NH2+]C2CC2)Cc2ccccc2)=C(N(CC(=O)N(C(C)C)C)C=1C)C)Cc1ccccc1
[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]
No
bace
0
1403
train
O1CCN(CC1)C(=O)CN1C(C)=C(C(=O)N[C@H]([C@H](O)C[NH2+]C2CC2)Cc2ccccc2)[C@H](C)C(C(OCc2ccccc2)=O)=C1C
[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an 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
1404
train
O(C(C)C)C(=O)CN1C(C)=C(C(=O)C)[C@@H](C)C(C(=O)N[C@H]([C@H](O)C[NH2+]C2CC2)Cc2ccccc2)=C1C
[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an 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
1405
train
Fc1cc(NC[C@@H](O)[C@@H](NC(=O)C2=CN(CC(OC(C)C)=O)C(C)=C(C(=O)C)[C@H]2C)Cc2ccccc2)ccc1
[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]
No
bace
0
1406
train
Brc1ccc(cc1)COC(=O)C1[NH2+]CC2(C1)c1c(NC2=O)cccc1
[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]
No
bace
0
1407
train
O(C(C)C)C(=O)CN1C=C(C(=O)N[C@H](C)c2ccccc2)[C@@H](CCC)C(=C1)C(=O)N[C@H]([C@H](O)C[NH2+]C1CC1)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
1408
train
s1c(nnc1C([NH3+])(Cc1ccccc1)C)-c1cc(cc(N(S(=O)(=O)C)C)c1)C(=O)NC(C)c1ccc(F)cc1
[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]
No
bace
0
1409
train
s1cccc1C1([NH2+]CC(O)C(NC(=O)C)Cc2cc(F)cc(F)c2)CCCCC1
[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]
No
bace
0
1410
train
Clc1ccc(nc1)C(=O)Nc1cc(ccc1)[C@@]1(N=C(N)CN(C)C1=O)C
[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]
No
bace
0
1411
train
Clc1ccc(nc1)C(=O)Nc1cc(ccc1)[C@@]1(N=C(N)C(=O)N(C1)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
1412
train
Clc1ccc(nc1)C(=O)Nc1cc([C@@]2(N=C(N)C(=O)N(C2)C)C)c(F)cc1
[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]
No
bace
0
1413
train
[NH+]=1[C@@](C=2N(CCCN=2)C=1N)(c1cc(ccc1)C(C)(C)C)c1ccccc1
[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]
No
bace
0
1414
train
O(C)c1cc(NC[C@@H](O)[C@@H](NC(=O)C2=CN(C=C(C(OC(C)(C)C)=O)[C@H]2CCC)CC(OC(C)C)=O)Cc2ccccc2)ccc1
[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]
No
bace
0
1415
train
O(C)c1cc(NC[C@@H](O)[C@@H](NC(=O)C2=CN(C=C(C(=O)N[C@H](C)c3ccccc3)[C@H]2CCC)CC(OC(C)C)=O)Cc2ccccc2)ccc1
[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]
No
bace
0
1416
train
O(C(=O)C1=CN(C=C(C(=O)N[C@H]([C@H](O)C[NH2+]C2CC2)Cc2ccccc2)[C@@H]1C)CC(OC(C)C)=O)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
1417
train
s1cc(nc1N)C(Cc1ccccc1)c1ccc(OC)cc1
[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]
No
bace
0
1418
train
O(C(C)C)C(=O)CN1C=C(C(=O)N[C@H](C)c2ccccc2)[C@@H](C)C(=C1)C(=O)N[C@H]([C@H](O)C[NH2+]C1CC1)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
1419
train
O(C(C)C)C(=O)CN1C(C)=C(C(=O)C)[C@@H](CCC)C(C(=O)N[C@H]([C@H](O)C[NH2+]C2CC2)Cc2ccccc2)=C1C
[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an 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
1420
train
O1C2CCCCC2(N=C1N)c1cc(ccc1)-c1cc(ccc1)C#N
[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]
No
bace
0
1421
train
O(CC1CC1)c1cc(ccc1)-c1ccc(cc1)C1CC1C=1N=C(N)N(C)C(=O)C=1
[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]
No
bace
0
1422
train
O(C)c1cc(ccc1)C([NH2+]CC(O)C(NC(=O)c1cc(N2CCCC2=O)c2c(n(cc2)CC)c1)Cc1ccccc1)(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
1423
train
O1C2CCCCC2(N=C1N)c1cc(ccc1)-c1cncnc1
[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]
No
bace
0
1424
train
O1C2COCCC2(N=C1N)c1cc(ccc1)-c1cc(OC)ccc1
[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]
No
bace
0
1425
train
Clc1ccc(cc1)C1(CCCC1)c1nc(sc1)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
1426
train
O(C)c1cc(ccc1)C[NH2+]CC(O)C(NC(=O)c1c2c(n(c1)CCCC)cccc2)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
1427
train
O1C2CCCCC2(N=C1N)c1cc(ccc1)-c1cc(OC)ccc1
[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]
No
bace
0
1428
train
O1C2COCCC2(N=C1N)c1cc(NC(=O)c2nc(oc2)C)ccc1
[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]
No
bace
0
1429
train
O(C(=O)C=1[C@H](C)C(C(=O)N[C@H]([C@H](O)C[NH2+]C2CC2)Cc2ccccc2)=C(N(CC(=O)N(C)C)C=1C)C)Cc1ccccc1
[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]
No
bace
0
1430
train
O=C1N(C)C(=NC(=C1)C1CC1c1ccc(cc1)-c1ccccc1C)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
1431
train
S(=O)(=O)(N(Cc1ccccc1)C)c1cc(ccc1)C(=O)NC(Cc1ccccc1)C(O)C[NH2+]C(C(=O)NC1CCCCC1)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
1432
train
Clc1ccc(nc1)C(=O)Nc1cc(ccc1)C12N=C(SCCC1C2)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
1433
train
Fc1cc(cc(F)c1)CC(NC(=O)C)C(O)C[NH2+]C1(CC1)c1occ(n1)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
1434
train
S(=O)(=O)(Cc1cc(ccc1)C(=O)NC(Cc1ccccc1)C(O)C[NH2+]C(C(=O)NC1CCCCC1)C)c1ccccc1
[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]
No
bace
0
1435
train
O(C)c1ccc(cc1C)[C@]1(N=C(N)N(C)C1=O)C12CC3CC(C1)CC(C2)C3
[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]
No
bace
0
1436
train
Clc1cc(cnc1)-c1cc(ccc1)C12N=C(OC1COCC2)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
1437
train
O1C2COCCC2(N=C1N)c1cc(ccc1)-c1cc(ccc1)C#N
[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]
No
bace
0
1438
train
s1cc(cc1)-c1ccc(cc1)C1CC1C=1N=C(N)N(C)C(=O)C=1
[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]
No
bace
0
1439
train
Fc1ncccc1-c1cc(ccc1)C12N=C(OC1CCCC2)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
1440
train
Brc1ccccc1C1C[NH2+]CC1C(=O)N1CCOCC1c1ccccc1
[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an 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
1441
train
O=C1N(Cc2ccc(cc2)CNC(=O)NCCCC)C(NC1(CCc1ccccc1)CC(C)C)=N
[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]
No
bace
0
1442
train
S(=O)(=O)(Cc1ccccc1)c1cc(ccc1)C(=O)NC(Cc1ccccc1)C(O)C[NH2+]C(C(=O)NC1CCCCC1)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
1443
train
s1cc(cc1-c1ccc(cc1)C1CC1C=1N=C(N)N(C)C(=O)C=1)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
1444
train
O(C)c1nc(ccc1)-c1ccc(cc1)C1CC1C=1N=C(N)N(C)C(=O)C=1
[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]
No
bace
0
1445
train
Clc1cc2nc(n(c2cc1)C(CC(C)C)CC(=O)NCc1cc(F)ccc1)N
[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]
No
bace
0
1446
train
O(C(C)C)c1cc(ccc1)-c1ccc(cc1)C1CC1C=1N=C(N)N(C)C(=O)C=1
[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]
No
bace
0
1447
train
Brc1ccccc1C1C[NH2+]CC1C(=O)N1CCCCC1c1ccccc1
[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an 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
1448
train
Clc1cc2nc(n(c2cc1)CCCC(=O)N(CC1CCCCC1)C)N
[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]
No
bace
0
1449
train
o1cccc1-c1ccc(cc1)C1CC1C=1N=C(N)N(C)C(=O)C=1
[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]
No
bace
0
1450
train
O=C1N(C)C(=NC(=C1)C1CC1c1ccc(cc1)-c1cc(ccc1)C(=O)N)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
1451
train
Brc1cc(ccc1O)CC1CS(=O)(=O)CC([NH2+]Cc2ccccc2)C1O
[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]
No
bace
0
1452
train
O=C1N(C)C(=NC(=C1)C1CC1c1ccc(cc1)-c1cc(NC(=O)C)ccc1)N
[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]
No
bace
0
1453
train
S(=O)(=O)(N(C)c1cc(cc(OCCC([NH3+])(Cc2ccccc2)CO)c1)C(=O)NC(C)c1ccc(F)cc1)C
[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]
No
bace
0
1454
train
Clc1cc2nc(n(c2cc1)C(CC(=O)NCc1ccccc1)CC)N
[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]
No
bace
0
1455
train
Clc1cc2CC(N=C(NC(Cc3ccccc3)c3nc4occc4cn3)c2cc1)(C)C
[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]
No
bace
0
1456
train
Clc1cc2nc(n(c2cc1)C(CC(=O)NC(C(OC)=O)COC(C)(C)C)CC)N
[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]
No
bace
0
1457
train
Clc1cc2nc(n(c2cc1)CCCC(=O)NCC1CCCCC1)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
1458
train
O(C(=O)C1[NH2+]CC2(C1)c1c(NC2=O)cccc1)C1CCN(CC1)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?" ]
No
bace
0
1459
train
Clc1cc2nc(n(c2cc1)C(CC(=O)NC(C(=O)[O-])COC(C)(C)C)CC)N
[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]
No
bace
0
1460
train
Clc1cc2nc(n(c2cc1)C(CC(=O)NCCC(C)(C)C)CC)N
[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]
No
bace
0
1461
train
S1(=O)(=O)NCC2(N1c1cc(F)ccc1)CC([NH+](CC2)Cc1cc(OC)ccc1)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
1462
train
S(=O)(=O)(N(C)c1cc(cc(c1)C(OCC([NH2+]C)(Cc1ccccc1)CO)=O)C(=O)NC(C)c1ccc(F)cc1)C
[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]
No
bace
0
1463
train
S(=O)(=O)(N(C)c1cc(cc(NCCC([NH3+])(Cc2ccccc2)CO)c1)C(=O)NC(C)c1ccc(F)cc1)C
[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]
No
bace
0
1464
train
S(CCC([NH3+])(Cc1ccccc1)CO)c1cc(cc(N(S(=O)(=O)C)C)c1)C(=O)NC(C)c1ccc(F)cc1
[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]
No
bace
0
1465
train
S(=O)(=O)(CCC([NH3+])(Cc1ccccc1)CO)c1cc(cc(N(S(=O)(=O)C)C)c1)C(=O)NC(C)c1ccc(F)cc1
[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]
No
bace
0
1466
train
S(=O)(=O)(N(C)c1cc(cc(c1)COCC([NH3+])(Cc1ccccc1)COC)C(=O)NC(C)c1ccc(F)cc1)C
[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]
No
bace
0
1467
train
O(C)c1cc(ccc1)C(=O)NCC(O)C(NC(=O)c1c2cccnc2n(c1)C(=O)N(CCCC)C)Cc1ccccc1
[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]
No
bace
0
1468
train
S(=O)(=O)(NCC(O)C(NC(=O)c1c2cccnc2n(c1)C(=O)N(CCCC)C)Cc1ccccc1)c1cc(OC)ccc1
[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]
No
bace
0
1469
train
OC(C(NC(=O)c1c2cccnc2n(c1)C(=O)N(CCCC)C)Cc1ccccc1)C[NH2+]C1CC1
[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]
No
bace
0
1470
train
Brc1cc(ccc1O)CC1CS(=O)(=O)CC([NH3+])C1O
[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]
No
bace
0
1471
train
n1cc(ccc1)-c1cc(ccc1)C1(N=C(C(C)C)C(=N1)N)C
[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]
No
bace
0
1472
train
O(C)c1nccc(c1)-c1ccc(cc1)C1CC1C=1N=C(N)N(C)C(=O)C=1
[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]
No
bace
0
1473
train
O=C1N(C)C(=NC(=C1)C1CC1c1ccc(cc1)-c1ccc(cc1)C)N
[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]
No
bace
0
1474
train
O=C1N(C)C(=NC(C1)(C)[C@H]1C[C@@H]1c1ccccc1)N
[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]
No
bace
0
1475
train
Clc1cc2CC(N=C(NC(Cc3ccccc3)c3ncccn3)c2cc1)(C)C
[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]
No
bace
0
1476
train
Fc1cc(cc(F)c1)CC(NC(=O)C)C(O)C[NH2+]C1(CCCCC1)c1occ(n1)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
1477
train
S1(=O)CC(Cc2cc(OC(COC)C(F)(F)F)c(N)c(F)c2)C(O)C([NH3+])C1
[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]
No
bace
0
1478
train
s1c(ccc1C)-c1ccc(cc1)C1CC1C=1N=C(N)N(C)C(=O)C=1
[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]
No
bace
0
1479
train
O=C1N(C)C(=NC(=C1)CCc1ccccc1)N
[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]
No
bace
0
1480
train
Clc1cc2CC(N=C(NC(Cc3ccccc3)c3ocnn3)c2cc1)(C)C
[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]
No
bace
0
1481
train
Clc1cc2nc(n(c2cc1)CCCC(=O)NC(C)C)N
[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]
No
bace
0
1482
train
Clc1cc2nc(n(c2cc1)CCCC(=O)N(Cc1cc(F)ccc1)C)N
[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]
No
bace
0
1483
train
O=C1N(C)C(=NC(=C1)CCc1ccc(cc1)-c1ccccc1)N
[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]
No
bace
0
1484
train
O1C2COCCC2(N=C1N)c1cc(NC(=O)c2ncccc2)ccc1
[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]
No
bace
0
1485
train
Brc1cc(ccc1)C12N=C(OC1CCCC2)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
1486
train
O1C2CCCCC2(N=C1N)c1cc(NC(=O)c2ncccc2)ccc1
[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]
No
bace
0
1487
train
O=C1N(C)C(=N[C@](C1)(CCc1ccccc1)C)N
[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]
No
bace
0
1488
train
s1cc(nc1N)C1(CCCC1)c1ccccc1
[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]
No
bace
0
1489
train
Clc1cc2nc(n(c2cc1)C(CC(C)C)CC(=O)NCc1ncccc1)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
1490
train
Clc1cc2nc(n(c2cc1)C(CC(=O)NCC1CC1)CC)N
[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]
No
bace
0
1491
train
Clc1cc2nc(n(c2cc1)C(CC(C)C)CC(=O)NC(C)C)N
[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]
No
bace
0
1492
train
Clc1cc2nc(n(c2cc1)CCCC(=O)NCc1cc(F)ccc1)N
[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]
No
bace
0
1493
train
Clc1cc2CC(N=C(NC(Cc3ccccc3)c3nc(ccn3)C)c2cc1)(C)C
[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]
No
bace
0
1494
train
Clc1cc2nc(n(c2cc1)C(CC(=O)NCc1ccc(F)cc1)CC)N
[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]
No
bace
0
1495
train
Clc1cc2nc(n(c2cc1)C(CC(=O)NCCC1CC[NH2+]C1)CC)N
[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]
No
bace
0
1496
train
Clc1cc2nc(n(c2cc1)CCCC(=O)NC1CC[NH+](CC1)C)N
[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]
No
bace
0
1497
train
Clc1cc2CC(N=C(NC(Cc3ccccc3)c3oc(nn3)C)c2cc1)(C)C
[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]
No
bace
0
1498
train
Clc1cc2nc(n(c2cc1)C(CC(=O)NCc1cc(F)ccc1)CC)N
[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]
No
bace
0
1499
train