File S1 - Dynamics of Linker Residues Modulate the Nucleic Acid Binding Properties of the HIV-1 Nucleocapsid Protein Zinc Fingers

This file contains Figures S1 - S3 and Table S1. Figure S1. Experimental 15N NMR relaxation data (Longitudinal (T1), transverse (T2) relaxation times and heteronuclear nOe) for backbone atoms obtained at 500 MHz for NC at 10°C. Figure S2. Order parameters determined from Model-Free analysis of 15N relaxation data obtained at 500 MHz for NC at 10°C. Figure S3. Structure of NC (pdb 1esk) showing the positioning of the N17 side chain (in red) relatively to the linker, the different residues R29 to K33 are shown with their side chain in blue, K34 in green, G35 in yellow. The side chains of the others residues are not shown, the zinc atoms are shown as spheres and the cysteines and histidines coordinating zinc atoms are shown in orange. Table S1. Results for the fits of the 15N NMR relaxation data obtained at 950, 600 ([52]) and 500 MHz using various models of motions with the model-free formalism described in Materials and Methods. (DOC)