The re-orientation of selected backbone N-H bond vectors from the previously reported HIV protease monomer simulation was studied and compared to NMR data for the dimer with a bound inhibitor. Reduction of the order parameter from the typical observed value of 0.8 for proteins was determined to occur from both larger than usual bacbone motions, and jump states indicating torsional transitions. The region around residue 40 showed particulalrly good agreement between the monomer simulation and the NMR measurements. Simulations more closely matching the experimental system may be performed.
