ANTHEPROT 2.0: a three-dimensional module fully coupled with protein sequence analysis methods

J Mol Graph. 1995 Jun;13(3):209-12, 199-200. doi: 10.1016/0263-7855(95)00035-5.

Abstract

ANTHEPROT is a fully interactive graphics program devoted to the analysis of the sequences and structures of proteins. This program, originally developed to facilitate the protein sequence analysis coupled with multiple alignments and predicted secondary structures of proteins, now comprises a powerful 3D module to display and handle macromolecular structures. All the methods that were previously integrated into ANTHEPROT are now directly coupled with a 3D window that provides the user all the classic features of a molecular modeling package. Indeed, it allows real-time rotation and translation of 3D structures with many kinds of models in depth-cueing mode (space filling, backbone, wire models, main chain, and ribbons), selections (atom type, residue type, segments, and chain), color-coding systems (amino acid properties, predicted or observed secondary structures, temperature B factor, and subunits), geometric calculations (Ramachandran plot, distances, and angles), and fitting molecules. Stereo views are possible as well as HPGL standard files. A module specifically devoted to the determination of 3D structures using nuclear magnetic resonance is also available. This major release of our program for IBM rs6000 workstations is available by anonymous ftp to ibcp.fr for academic institutions.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Antigens / chemistry
  • Computer Graphics*
  • Magnetic Resonance Spectroscopy
  • Models, Molecular*
  • Molecular Structure
  • Protein Structure, Secondary*
  • Sequence Alignment

Substances

  • Antigens