The VWF CTCK monomer crystal structure. Cysteines are colored consistently throughout the panels here and in other figures. (A) Ribbon diagram with cysteines shown in stick and the N-linked carbohydrate in thin stick. (B) β-Sheet diagram. Each backbone hydrogen bond is shown as a dashed line. Residues 2728 to 2812 are numbered as in pre-proVWF, except the first 2 digits are omitted for clarity. β4′ and β7′ from the other monomer are in gray. Residues in β-sheet framework and loops are shown in solid and open circles, respectively. Cysteines are surrounded with larger colored circles and those in inter-chain disulfides are also marked with small blue circles. The dyad axis at the β4 and β7 strands is marked with a lens. (C) Topology diagram. (D) Sequence, secondary structure, and disulfide connectivity. Cysteines are shown both in order C1 to C11 and with their residue numbers. (E-F) Experimental electron density after solvent flattening at disulfides. Density at 1σ around cysteine sidechains is shown as mesh in black around intra-chain disulfides and in purple around inter-chain disulfides. (E) The CKs in each monomer. (F) The C2-C8 disulfide.