Three-Dimensional Structure of the Apo Form of the N-Terminal EGF-like Module of Blood Coagulation Factor X As Determined by NMR Spectroscopy and Simulated Folding
The three-dimensional structure of a 42-residue fragment containing the N-terminal EGF-like module of blood coagulation factor X was determined by means of 2D NMR spectroscopy and computer simulation. The spectroscopic data consisted of 370 NOE distances and 27 dihedral angle constraints. These were used to generate peptide conformations by molecular dynamics simulation. The simulations used a nov