Cytochromes P450 are heme monooxygenases that play critical roles in the biosynthesis of lipids, steroids, antibiotics, and drugs metabolism. Understanding the active site structure and dynamics is important for drug discovery and providing insight on biological processes. Crystal structures of numerous P450 isoforms show the substrate positioned too far away from the heme to be the catalytically relevant binding mode. One proposed reason for the distant substrate is a temperature dependence on the ligand confirmation. This hypothesis is supported by molecular dynamic and deuterium NMR studies by Levy, Friesner, Jovanovic and coworkers. In this study we use solid state NMR to collect structural information at a variety of temperatures of N-palmitoylglycine (NPG) bound to cytochrome P450 BMP. Cytochrome P450 BMP is the heme domain of cytochrome P450 BM-3 from Bacillus megaterium, which is widely used as a model for human P450s. Since cytochrome P450 is paramagnetic it may be difficult to observe magnetization transfer from the ligand to the protein close to the heme. As a control we labeled an isoleucine and glycine pair approximately 5 � away from the heme in order to find the best methods of detection close to the paramagnetic center. In addition, we have assigned peaks for the methyl group of NPG, for the �gatekeeper � phenylalanine 87, and for alanine 82, which is close to the substrate in the low temperature form. Ongoing efforts focus on observing transfer of magnetization from the protein to substrate and identifying markers for the high temperature form.