Classifier Instance:

Anchor text: GFP
Target Entity: Green_fluorescent_protein
Preceding Context: Hsp60 (GroEL/GroES complex in E. coli) is the best characterized large (~ 1 MDa) chaperone complex. GroEL is a double-ring 14mer with a greasy hydrophobic patch at its opening; it is so large it can accommodate native folding of 54-kDa
Succeeding Context: in its lumen. GroES is a single-ring heptamer that binds to GroEL in the presence of ATP or ADP. GroEL/GroES may not be able to undo previous aggregation, but it does compete in the pathway of misfolding and aggregation. Also acts in mitochondrial matrix as molecular chaperone.
Paragraph Title: Hsp60
Source Page: Chaperone (protein)

Ground Truth Types:

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Predicted Types:

TypeConfidenceDecision
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wordnet_person_100007846-2.2783255496624633 0
yagoGeoEntity-1.5650426271342608 0
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