title: CheShift-2: graphic validation of protein structures.
abstract: The differences between observed and predicted (13)C(α) chemical shifts can be used as a sensitive probe with which to detect possible local flaws in protein structures. For this reason, we previously introduced CheShift, a Web server for protein structure validation. Now, we present CheShift-2 in which a graphical user interface is implemented to render such local flaws easily visible. A series of applications to 15 ensembles of conformations illustrate the ability of CheShift-2 to locate the main structural flaws rapidly and accurately on a per-residue basis. Since accuracy plays a central role in CheShift predictions, the treatment of histidine (His) is investigated here by exploring which form of His should be used in CheShift-2.
  
  
  BACKGROUND
  CheShift-2 is free of charge for academic use and can be accessed from www.cheshift.com
authors.affiliation: Universidad Nacional de San Luis, IMASL-CONICET, Ejército de Los Andes, San Luis, Argentina.
authors.forename: Osvaldo A
authors.initials: OA
authors.lastname: Martin
authors.forename: Jorge A
authors.initials: JA
authors.lastname: Vila
authors.forename: Harold A
authors.initials: HA
authors.lastname: Scheraga
mesh_terms: D000818:Animals; D002417:Cattle; D018360:Crystallography, X-Ray; D015786:Cytochromes b5 / Q000737:chemistry; D004398:Dyneins / Q000737:chemistry; D006639:Histidine / Q000032:analysis; D020407:Internet; D008958:Models, Molecular; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*; D011817:Rabbits; D051381:Rats; D012984:Software
chemical_list: D011506:Proteins; D006639:Histidine; D015786:Cytochromes b5; D004398:Dyneins