DETERMINATION OF THE COMPLETE THREE-DIMENSIONAL STRUCTURE OF THE TRYPSIN INHIBITOR FROM SQUASH SEEDS IN AQUEOUS SOLUTION BY NUCLEAR MAGNETIC RESONANCE AND A COMBINATION OF DISTANCE GEOMETRY AND DYNAMICAL SIMULATED ANNEALING
Nuclear Magnetic Resonance Solution and X-Ray Structures of Squash Trypsin Inhibitor Exhibit the Same Conformation of the Proteinase Binding Loop