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Figure S1. Explicit presentation of the amino acid sequence of the RT RNH fragment used in this study, i.e. residues 427–560, with an additional N-terminal peptide, S–E–L (underlined).

Figure S2. Chemical shift perturbations induced by Mg2+ on (A) monomer and (B) dimer RNH fractions, and their highlight on the ribbon structure presentations (C and D, respectively).

Figure S3. (A) Overlaid 1H-15N HSQC spectra of the RNH monomer recorded in absence (black) or presence of 0.2, 0.4, 0.8 and 1.6× BHMP07 (orange, blue, pink, and magenta, respectively). (B) Normalized chemical shift changes as a function of BHMP07 concentration for some representative residues, E55 (filled circle), A79 (filled triangle), L80 (filled squares), A85 (filled diamond), S92 (open circle), and S76 (open triangle).

Figure S4. (A) Overlaid 1H-15N HSQC spectra of the RNH monomer after pre-addition of 20 mM MgCl2 recorded in absence (black) or presence of 0.25, 0.5 and 1.5× BHMP07 (orange, light blue and magenta, respectively). (B) Normalized chemical shift changes as a function of BHMP07 concentration (same residues and representation as in Figure S3B).

Figure S5. Histogram of backbone amide proton resonance shifts induced in RNH monomer by (A) BHMP07 in absence of Mg2+, (B) BHMP07 in 20 mM MgCl2 and (C) 20 mM MgCl2 only.

Figure S6. Histogram of backbone amide nitrogen resonance shifts induced in RNH monomer by (A) BHMP07 in absence of Mg2+, (B) BHMP07 in 20 mM MgCl2 and (C) 20 mM MgCl2 only.

Figure S7. Ligand interaction diagrams for BHMP07 docked into RNH shown for each predicted binding site.

Figure S8. Per-residue interaction scores for BHMP07 bound to Site II in its best pose (highest docking score).

Table S1. Individual KD for the interaction of monomeric RNH with BHMP07.

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CBDD_12010_sm_FigS1-S7-TableS1.pdf3134KSupporting info item

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