The alignment of the antimicrobial peptide PGLa in a lipid bilayer was characterized by solid state IT NMR on selectively CF3-labeled peptides in oriented samples. Previous studies in liquid crystalline model membranes had shown that the amphiphilic alpha-helix of PGLa adopts a surface-aligned S-state or a tilted T-state, depending on the peptide/lipid ratio. Only in the presence of the synergistic partner peptide magainin 2 had PGLa been found insert into the bilayer in a transmembrane I-state orientation. Here, we have characterized the peptide alignment but as a function of temperature and lipid phase state. At temperatures below the lipid chain melting transition, PGLa is now seen to be able to insert on its own, with its helical axis nearly parallel to the bilayer normal (tilt angle of similar to 170 degrees), forming the I-state. Above the lipid phase transition, PGLa is aligned in the known T-state (tilt angle of similar to 130 degrees), but it is found flip into the S-state at more elevated temperatures (tilt angle of similar to 96 degrees). This way, three distinct alignment states were found, which also differ in their mobility. The complete membrane insertion of PGLa in the I-state, which could be trapped here in a get phase bilayer, supports mechanistic models that explain antimicrobial activity as a result of pore formation by some of the molecules.