Figure 1.

Solution structure of PHD_VC5HCH_NSD1. (A) Superposition of the best 15 NMR structures PHD_V; the L3 loop and C5HCH are coloured in orange, gold and green, respectively. Zn²⁺ binding residues and Zn²⁺ ions are represented in sticks and spheres, respectively. (B) Cartoon representation of PHD_VC5HCH_NSD1 highlighting elements of secondary structure. Residues forming the domain hydrophobic core at the domains interface are shown in sticks and dotted space-filling representation. Zn²⁺ ions are represented in spheres. Amino acids in this and in the following Figures are numbered according to the human NSD1 sequence. (C) Electrostatic surface potential of PHD_VC5HCH_NSD1. The structures on the left and on the right are represented in the same orientation as in (A) and (B), respectively. (D) Backbone dynamics of PHD_VC5HCH_NSD1. Dotted line indicates the {¹H}–¹⁵N heteronuclear NOE value threshold of 0.65. Elements of secondary structure are indicated on the top.