Science Advances

Supplementary Materials

This PDF file includes:

  • Fig. S1. 1H, 15N-TROSY-HSQC spectra for PKA-CWT and PKA-CL205R in apo, ATPγN, and ATPγN/PKI-bound and ATPγN/VPS36-bound forms.
  • Fig. S2. CSPs observed upon ligand binding for PKA-CWT and PKA-CL205R.
  • Fig. S3. Intensity plot for the binding of VPS36 to ATPγN-saturated PKA-CL205R.
  • Fig. S4. PCA of the catalytic lobes in PKA-CWT and PKA-CL205R.
  • Fig. S5. Probability of the formation of inter-residue contact and ΔRMSF of PKA-C upon forming ternary complexes with PKI5–24 or VPS36.
  • Fig. S6. Allosteric changes upon peptide binding revealed by MD simulation and mutual information (MutInf) analysis.
  • Table S1. Changes in enthalpy, entropy, free energy, and dissociation constant of binding ATPγN, PKI5–24, and VPS36 for PKA-CWT and PKA-CL205R.
  • Table S2. Kinetic parameters of Kemptide and VPS36 phosphorylation by PKA-CWT and PKA-CL205R.
  • Table S3. PCA and SD of the CONCISE analysis of the structural states analyzed.
  • Table S4. Tm as determined using CD.

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