Datasets:

haitengzhao
/

molecule_property_instruction

Dataset card Viewer Files Files and versions Community

Split (13)

bace · 1.51k rows

graph stringlengths 17 198	text sequencelengths 7 7	label stringclasses 2 values	dataset_name stringclasses 1 value	molecule_index stringlengths 1 4	split stringclasses 3 values
S1CC(=NC1(c1cc(ccc1)-c1cc(OC)ccc1)c1ccncc1)N	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	1000	train
s1nc(cc1)-c1cc2c(OC(CC23N=C(N)N(C)C3=O)(C)C)cc1	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	1001	train
Clc1cc2CC(N=C(NC(Cc3cscc3C#CC)C(=O)[O-])c2cc1)(C)C	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	1002	train
FC(F)(F)Oc1ccc(cc1)C1(N=C(N)N(C)C1=O)c1cc(ccc1)-c1cccnc1OC	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	1003	train
S1(=O)CC(Cc2cc(O)c(N)c(F)c2)C(O)C([NH2+]Cc2cc(ccc2)C(C)(C)C)C1	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	1004	train
FC(F)Oc1ccc(cc1)[C@@]1(N=C(N)N(C)C1=O)c1cc(ccc1)/C(/F)=C/C1CC1	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	1005	train
S1(=O)(=O)N(C2C=C(C=C3N(CC[NH+](C23)CC1)CC)C(=O)NC(Cc1ccccc1)C(O)C[NH2+]C1CC1)C	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	1006	train
Clc1ccccc1-c1n(Cc2nc(N)ccc2)c(cc1)-c1ccc(OCCCCC)cc1	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	1007	train
Clc1ccc(nc1)C(=O)Nc1cc(ccc1)C1(N=C(N)c2c1cccc2)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	1008	train
Fc1ccc(cc1-c1cccnc1F)C1(N=C(N)N(C)C1=O)c1cc(C)c(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	1009	train
Fc1cc(cc(F)c1)CC(NC(=O)C)C(O)C[NH2+]C1(CCCCC1)c1cc(ccc1)C1CCOCOC1	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	1010	train
S1(=O)(=O)CC(Cc2cc(F)c3NCC4(CCC4)c3c2)C(O)C([NH2+]Cc2cc(ccc2)C(C)(C)C)C1	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	1011	train
ClC1=CN=C(NC1=O)C(NC1=NC(Cc2c1ccc(Cl)c2)(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	1012	train
Clc1cc2CC(N=C(NC(Cc3cscc3CCC3CC3)C(=O)[O-])c2cc1)(C)C	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	1013	train
OC(C(NC(=O)C1CC(CCC1)C(NC(=O)CC)(C)C)Cc1ccccc1)C[NH2+]Cc1cc(ccc1)C(C)C	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	1014	train
Fc1cc(cc(F)c1)CC(NC(=O)C)C(O)C[NH2+]C1(CC1)c1cc(ccc1)C1OCCC1	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	1015	train
Fc1cc(cc(F)c1)CC(NC(=O)C)C(O)C[NH2+]C1(CC1)c1cc(ccc1)C1(OCCC1)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	1016	train
O=C(NCC=C)c1ccc(cc1)-c1n(Cc2nc(N)ccc2)c(cc1)-c1ccccc1	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	1017	train
Clc1ccccc1-c1n(Cc2nc(N)ccc2)c(cc1)-c1ccc(Oc2ccncc2)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	1018	train
IC1=CN=C(NC1=O)C(NC1=NC(Cc2c1ccc(Cl)c2)(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	1019	train
Fc1cc(cc(F)c1)CC(NC(=O)C(N1CCC(NC(=O)C)(C(CC)C)C1=O)CCc1ccccc1)[C@H](O)[C@H]1[NH2+]Cc2c(C1)cccc2	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	1020	train
Brc1ccccc1C1C[NH2+]CC1C(=O)N1CCC(CC1c1ccccc1)c1ccccc1	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	1021	train
Clc1cc(ccc1)-c1cc2c(OC(CC23N=C(N)N(CC(F)(F)F)C3=O)(C)C)cc1	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	1022	train
Fc1cc(cc(F)c1)C[C@H](NC(=O)C)[C@H](O)C[NH2+]C1(CCC1)c1cc(ccc1)C(C)(C)C	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	1023	train
Brc1cc(ccc1)CC1CS(=O)(=O)CC([NH2+]Cc2cc(ccc2)C(C)(C)C)C1O	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	1024	train
Clc1cc2CC(N=C(NC(Cc3cscc3CCC)C(=O)[O-])c2cc1)(C)C	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	1025	train
O(C)c1ccc(cc1C)C1(N=C(N)N(C)C1=O)c1cc(-c2cccnc2)c(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	1026	train
o1cc(cc1)-c1cc(ccc1)C1(N=C(N)N(C)C1=O)c1ccncc1	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	1027	train
Clc1cc2CC(N=C(NC(Cc3cscc3CC)C(=O)[O-])c2cc1)(C)C	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	1028	train
S1CCC(=NC1(C)c1cc(ccc1)-c1cc(OC)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	1029	train
s1c2c(nc1C)C(=NC2(c1cc(ccc1)-c1cncnc1)c1ccc(OC)cc1)N	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	1030	train
Fc1cc(cc(F)c1)CC(NC(=O)C)C(O)C[NH2+]C1(CC1)c1nccc(c1)C(C)(C)C	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	1031	train
O1CCCCNc2cc(cc(c2)C(=O)NC(Cc2cc1ccc2)C(O)C[NH2+]C(COC)c1cc(ccc1)C(C)(C)C)COC	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	1032	train
S1(=O)(=O)CC(Cc2cc(OCCC)ccc2)C(O)C([NH2+]Cc2cc(ccc2)C(C)(C)C)C1	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	1033	train
Fc1cc(cc(F)c1)CC(NC(=O)C)C(O)C[NH2+]C1(CCCCC1)c1cc(ccc1)CC	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	1034	train
Fc1cc(cc(F)c1)CC(NC(=O)C)C(O)C[NH2+]C1(CCCCC1)c1cc(N2CCCOCC2)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	1035	train
O=C1c2c(cc(cc2)-c2cncnc2)C2(N=C(N)N(C)C2=O)CC1(C)C	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	1036	train
Brc1ccsc1CC(NC1=NC(Cc2c1ccc(Cl)c2)(C)C)C(=O)[O-]	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	1037	train
S(=O)(=O)(C)c1cc(ccc1)C1([NH2+]CC(O)C(NC(=O)C)Cc2cc(F)cc(F)c2)CCCCC1	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	1038	train
Fc1cc(cc(F)c1)CC(NC(=O)C)C(O)C[NH2+]C1(CC1)c1cc(c[n+]([O-])c1)CC(C)(C)C	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	1039	train
Fc1ncccc1-c1cc(ccc1)[C@]1([NH+]=C(N2C1=NCCC2)N)c1cc2OC(F)(F)Oc2cc1	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	1040	train
Fc1ccc(OC)cc1-c1cc2c(Oc3c(cc(OC)cc3)C23N=C(OC3)N)cc1	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	1041	train
Fc1cc(cc(F)c1)CC(NC(=O)C)C(O)C[NH2+]C1(CCCCC1)c1cc(N2CCCOCC2=O)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	1042	train
Clc1cc2CC(N=C(NC(Cc3ccccc3)C=3NC(ON=3)=O)c2cc1)(C)C	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	1043	train
Fc1cc(cc(F)c1)C[C@H](NC(=O)C)[C@H](O)C[NH2+]C1(CC1)c1cc(ccc1)[C@H]1CCOC1	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	1044	train
Brc1cc(ccc1)CC1CS(=O)(=O)CC([NH2+]Cc2cc(ccc2)C(C)C)C1O	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	1045	train
Clc1cc2CC(N=C(NC(Cc3cscc3C#C)C(=O)[O-])c2cc1)(C)C	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	1046	train
Clc1ccc(nc1)C(=O)Nc1cc(ccc1)C12N=C(SCC1C2)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	1047	train
Fc1cc(cc(F)c1)CC(NC(=O)C)C(O)C[NH2+]C1(CC1)c1cc(cnc1)CC(C)(C)C	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	1048	train
Clc1cc(cnc1)-c1cc2c(CC(CC23N=C(OC3)N)(C)C)cc1	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	1049	train
FC(F)(F)Oc1ccc(cc1)[C@]1([NH+]=C(N2C1=NCCC2)N)c1cc(ccc1)-c1cncnc1	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	1050	train
S1CC(=NC1(c1cc(ccc1)-c1cccnc1)c1ccc(OC)cc1)N	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	1051	train
OC(C(NC(=O)C1CC(CCC1)C(NC(=O)C)C(C)C)Cc1ccccc1)CC(C(=O)NCCCC)C	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	1052	train
Fc1cc(cc(F)c1)CC(NC(=O)C)C(O)C[NH2+]C1(CCCCC1)c1cc(ccc1)C1CCCC1=O	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	1053	train
Fc1ncccc1-c1cc2c(Oc3c(cc(OC)cc3)C23N=C(OC3)N)cc1	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	1054	train
O(C)c1cc(ccc1)-c1cc(ccc1)C1(N=C(C)C(=N1)N)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	1055	train
Clc1ccccc1-c1n(Cc2nc(N)ccc2)c(cc1)-c1ccc(Oc2ncccc2)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	1056	train
Fc1cc(cc(F)c1)CC(NC(=O)C)C(O)C[NH2+]C1(CCCCC1)c1cc(ccc1)CC(C)C	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	1057	train
O=C1N(CC(=NC1(C)c1cc(NC(=O)c2ncc(cc2)C#N)ccc1)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	1058	train
Fc1cc(cc(F)c1)CC(NC(=O)C)C(O)C[NH2+]C1(CCCCC1)c1cc(N2CCCC2=O)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	1059	train
Clc1cc2CC(N=C(NC(Cc3cscc3-c3occn3)C(=O)[O-])c2cc1)(C)C	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	1060	train
S(=O)(=O)(N(C)c1cc(cc(c1)C(=O)NC(C)c1ccc(F)cc1)-c1nc([nH]n1)C([NH3+])(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	1061	train
Clc1cc(cc(Cl)c1NC(=O)C)CNC(=[NH2+])NC(=O)Cn1c2cc(ccc2cc1)CN(S(=O)(=O)C)C	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	1062	train
Clc1ccccc1-c1n(Cc2nc(N)ccc2)c(cc1)-c1ccc(Oc2ccccc2)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	1063	train
Fc1cc(cc(F)c1)CC(NC(=O)C)C(O)C[NH2+]C1(CCCN(C1)C(OCc1ccccc1)=O)c1cc(ccc1)C(C)(C)C	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	1064	train
O=C1N(C)C(=NC1(C1CCCCC1)c1cc(NC(=O)c2n(ccc2)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	1065	train
Fc1cc(cc(F)c1)CC(NC(=O)c1c2cc(ccc2n(c1)C(=O)N(CCCC)C)C(OCc1ccccc1)=O)C(O)C[NH2+]Cc1cc(OC)ccc1	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	1066	train
O(CCCC)c1ccc(cc1)C1(N=C(N)N(C)C1=O)C12CC3CC(C1)CC(C2)C3	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	1067	train
Fc1cc(cc(F)c1)CC(NC(=O)C)C(O)C[NH2+]C1(CC1)c1nn(cc1)CC(C)(C)C	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	1068	train
Fc1cc(cc(F)c1)CC(NC(=O)C(N1CCC(NC(=O)C)(C(CC)C)C1=O)CCc1ccccc1)C(O)C1[NH2+]Cc2c(C1)cccc2O	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	1069	train
S1(=O)(=O)CC(Cc2cc(CC)c(N)c(F)c2)C(O)C([NH2+]Cc2cc(ccc2)C(C)(C)C)C1	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	1070	train
FC(F)(F)Oc1ccc(cc1)C1(N=C(N)N(C)C1=O)c1cc(ccc1)-c1ccc(OC)nc1	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	1071	train
FC(F)Oc1ccc(cc1)[C@@]1(N=C(N)N(C)C1=O)c1cc(ccc1)CC	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	1072	train
Fc1c(cccc1OC)-c1cc2c(Oc3c(cc(OC)cc3)C23N=C(OC3)N)cc1	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	1073	train
Fc1ncc(cc1)-c1cc2c(Oc3c(cc(OC)cc3)C23N=C(OC3)N)cc1	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	1074	train
S1(Oc2c(N1c1cc(ccc1)C(=O)NC(Cc1ccccc1)C(O)C[NH2+]Cc1cc(ccc1)C(F)(F)F)cccc2)(=O)=O	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	1075	train
S(=O)(=O)(N(C)c1cc(cc(c1)COCC([NH3+])(Cc1ccccc1)C(F)F)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	1076	train
S(=O)(=O)(N(c1cc(ccc1C)C(=O)NC(Cc1ccccc1)C(O)C[NH2+]Cc1cc(ccc1)C(F)(F)F)c1ccccc1)C	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	1077	train
Fc1cc(cc(F)c1)CC(NC(=O)C)C(O)C[NH2+]C1(CCCCC1)c1cc(ccc1)C1CCCC1	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	1078	train
O=C1N(CCCCCC(=O)[O-])C(=NC1(C1CCCCC1)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	1079	train
Clc1cc2c(OC3(CC2[NH2+]CC(O)C(NC(=O)C)Cc2ccccc2)CCC3)nc1	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	1080	train
Clc1ccccc1-c1n(Cc2nc(N)ccc2)c(cc1)-c1ccc(Nc2cncnc2)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	1081	train
Fc1cc(cc(F)c1)C[C@H](NC(=O)C)[C@H](O)C[NH2+]C1(CC1)c1cc(-n2nccc2)ccc1	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	1082	train
O=C1N(C)C(=NC1(C1CCCCC1)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	1083	train
S1(=O)(=O)CC(Cc2cc(CCO)c(O)cc2)C(O)C([NH2+]Cc2cc(ccc2)C(C)C)C1	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	1084	train
S(=O)(=O)(N(C)c1cc(cc(c1)COCC([NH3+])(Cc1ccccc1)CF)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	1085	train
Fc1cc(cc(F)c1)CC(NC(=O)C)C(O)C[NH2+]C1(CCCCC1)c1cc(N2CCCNC2=O)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	1086	train
Fc1cc(cc(F)c1)CC(NC(=O)C(N1CCC(CCCC)C1=O)CCc1ccccc1)C(O)C1[NH2+]Cc2c(C1)cccc2	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	1087	train
S1CCC(=NC1(C)c1cc(ccc1)-c1cncnc1)N	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	1088	train
Clc1cc(cc(Cl)c1NC(=O)C)CNC(=[NH2+])NC(=O)Cn1c2c(cccc2)cc1	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	1089	train
Clc1ccc(nc1)C(=O)Nc1cc(ccc1)C1(N=C(N)N(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	1090	train
O1CCCC1CN1C(=O)C(N=C1N)(C1CCCCC1)c1ccccc1	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	1091	train
O=C1N(C)C(=NC1(C1CCCCC1)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	1092	train
Fc1cc(cc(F)c1)CN1C(=O)C(N=C1N)(C1CCCCC1)c1ccccc1	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	1093	train
Clc1cc2CC(N=C(NC(Cc3cscc3-c3cn(nc3)C)C(=O)[O-])c2cc1)(C)C	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	1094	train
s1cc(nc1N)C(Cc1cc([N+](=O)[O-])ccc1OC)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	1095	train
Fc1cc(cc(F)c1)CC(NC(=O)C)C(O)C[NH2+]C1(CCCCC1)c1cc(ccc1)-c1occc1	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	1096	train
Fc1cc(cc(F)c1)CC(NC(=O)c1c2c(n(c1)C(OCCCC)=O)cccc2)C(O)C[NH2+]Cc1cc(OC)ccc1	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	1097	train
S1(=O)(=O)CC(Cc2ccccc2)C(O)C([NH2+]Cc2cc(ccc2)C(C)C)C1	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	1098	train
S1(=O)(=O)CC(Cc2cc(ccc2)COCCC)C(O)C([NH2+]Cc2cc(ccc2)C(C)C)C1	[ "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Can this molecule bind to BACE1?", "The assay tests whether the molecule can bind to the BACE1 protein. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. BACE1 is a member of family of aspartic proteases. Same as other aspartic proteases, BACE1 is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The assay tests whether the molecule can bind to the BACE1 protein. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Is this molecule effective to the assay?", "BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths. Can this molecule bind to BACE1?" ]	No	bace	1099	train