Data Supplement

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  Figure 1.2. HPLC and LC-MS analysis of the reduction of GM by NQO1 to GMH2.

  Table 2.2. Total interaction energy, van der Waals, electrostatic energy, and hydrogen bonding interactions between yeast Hsp90 and GM/GMH2.

  Figure 3.2. HPLC analysis of GMH2 formation by MDA468 and MDA468/NQ16 cell sonicates.

  Figure 4.2. Effect of GM on growth inhibition and Hsp90 client proteins in human breast cancer cells.

  Figure 5.2. Molecular modeling of the N-terminal of the yeast Hsp90-GM/GMH2 complex.

  Figure 1.3. HPLC and LC-MS analysis of the reduction of 17AG by NQO1 to 17AGH2.

  Figure 3.3. HPLC analysis of 17AGH2 formation by MDA468 and MDA468/NQ16 cell sonicates.

  Figure 4.3. Effect of 17AG on growth inhibition and Hsp90 client proteins in human breast cancer cells.

  Figure 5.3. Molecular modeling of the N-terminal of the yeast Hsp90-17AG/17AGH2 complex.

  Table 2.3. Total interaction energy, van der Waals, electrostatic energy, and hydrogen bonding interactions between yeast Hsp90 and 17AG/17AGH2.

  Figure 1.4. HPLC and LC-MS analysis of the reduction of 17AEP-GA by NQO1 to 17AEP-GAH2.

  Figure 3.4. HPLC analysis of 17AEP-GAH2 formation by MDA468 and MDA468/NQ16 cell sonicates.

  Figure 4.4. Effect of 17AEP-GA on growth inhibition and Hsp90 client proteins in human breast cancer cells.

  Figure 5.4. Molecular modeling of the N-terminal of the yeast Hsp90-17AEP-GA/17AEP-GAH2 complex.

  Table 2.4. Total interaction energy, van der Waals, electrostatic energy, and hydrogen bonding interactions between yeast Hsp90 and 17AEP-GA/17AEP-GAH2.