Improved efficiency of protein structure calculations from NMR data using the program DIANA with redundant dihedral angle constraints.
A new strategy for NMR structure calculations of proteins with the variable target function method (Braun, W. and Go, N. (1985) J. Mol. Biol., 186, 611) is described, which makes use of redundant dihedral angle constraints (REDAC) derived from preliminary calculations of the complete structure. The REDAC approach reduces the computation time for obtaining a group of acceptable conformers with the program DIANA 5-100-fold, depending on the complexity of the protein structure, and retains good sampling of conformation space.
Güntert
P
P
Institut für Molekularbiologie und Biophysik, Eidgenössische Technische Hochschule-Hönggerberg, Zürich, Switzerland.
Wüthrich
K
K
D000595:Amino Acid Sequence; D051943:Antennapedia Homeodomain Protein; D043424:Carboxypeptidase B; D002268:Carboxypeptidases / Q000737:chemistry; D004268:DNA-Binding Proteins / Q000737:chemistry; D004792:Enzyme Precursors / Q000737:chemistry; D018398:Homeodomain Proteins; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D009687:Nuclear Proteins / Q000737:chemistry; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*; D012984:Software; D014157:Transcription Factors; D014359:Trypsin Inhibitor, Kazal Pancreatic / Q000737:chemistry
D051943:Antennapedia Homeodomain Protein; D004268:DNA-Binding Proteins; D004792:Enzyme Precursors; D018398:Homeodomain Proteins; D009687:Nuclear Proteins; D011506:Proteins; D014157:Transcription Factors; D014359:Trypsin Inhibitor, Kazal Pancreatic; D002268:Carboxypeptidases; D043424:Carboxypeptidase B