Work has been carried out on a number of structural problems related to proteins derived from the HIV virus. These include the RNAse H domain of HIV-1 reverse transcriptase, the p7 nucleocapsid protein of HIV-1, and proteins of the immune system, in particular interleukin- 1beta and the double zinc finger domain of the human enhancer binding protein. The secondary structure of the RNaseH domain has been determined using double and triple resonance 3D NMR spectroscopy, and current work is being focused on studying its internal dynamics and obtaining a three-dimensional structure in solution. The solution structure of the zinc finger domains of the p7 nucleocapsid protein has been determined, and the two zinc binding domains shown to be identical within the errors of the coordinates. The high resolution structure of interleukin-1beta in solution has been determined using 3D and 4D heteronuclear NMR. In addition, structural studies have begun on the double zinc finger domain of the human enhancer protein which binds specifically to the regulatory region in the long terminal repeat of the HIV genome.