our lab | web service | help | home DTA (Dihedral Transition Analysis) is the method for characterizing protein motion from one given 3D protein structure to another, based on large changes of main chain dihedral angles. The DTA server provides a database of 569 pairs of high resolution, comprehensive and non-redundant protein motions. Sorting and searching functions from different aspects are provided. The list of protein pairs given in the original paper (unpublished) is also provided here for reference. Description of DTA DATABASE Database search and Listing pdbid/keyword: proteins including TFs ranked by NLS from the largest proteins including TFs ranked by RMSD from the largest within the group of data having relatively small NLS values (<=1.0A) proteins including TFs ranked by RMSD from the smallest within the group of data having relatively small NLS values (<=1.0A) "domain" list "no domain" list from large proteins from large RMSD for whole protein same pdbID Link to the top 10 ranking table Table 1. Top10 TFs ranked by NLS from the largest Table 2. Top10 TFs ranked by RMSD from the largest in (NLS<=1.0Å) Table 3. Top10 TFs ranked by RMSD from the smallest in (NLS<=1.0Å) Copyright © 2008 | Dihedral Transition angle Analysis | created by walter mancini