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AMP-PCP disodium is an ATP analogue and can bind to Hsp90 N-terminal domain with a K_d value of 3.8 μM. AMP-PCP disodium binding favors the formation of the active homodimer of Hsp90.

AMP-PCP binding favors the formation of the active homodimer of Hsp90 by enhancing the slow-motion featured conformational exchanges of those residues (A117-A141) within the lid segment (A111-G135) and around region. In total, 170 non-proline residues are identified for the triple-labeled Hsp90 bound with AMP-PCP.

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