title: Peakr: simulating solid-state NMR spectra of proteins.
abstract: BACKGROUND
  When analyzing solid-state nuclear magnetic resonance (NMR) spectra of proteins, assignment of resonances to nuclei and derivation of restraints for 3D structure calculations are challenging and time-consuming processes. Simulated spectra that have been calculated based on, for example, chemical shift predictions and structural models can be of considerable help. Existing solutions are typically limited in the type of experiment they can consider and difficult to adapt to different settings.
  
  
  RESULTS
  Here, we present Peakr, a software to simulate solid-state NMR spectra of proteins. It can generate simulated spectra based on numerous common types of internuclear correlations relevant for assignment and structure elucidation, can compare simulated and experimental spectra and produces lists and visualizations useful for analyzing measured spectra. Compared with other solutions, it is fast, versatile and user friendly.
  
  
  METHODS
  Peakr is maintained under the GPL license and can be accessed at http://www.peakr.org. The source code can be obtained on request from the authors.
authors.affiliation: Department of NMR-based Structural Biology, Max-Planck-Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany. robert.schneider@ibs.fr
authors.forename: Robert
authors.initials: R
authors.lastname: Schneider
authors.forename: Florian
authors.initials: F
authors.lastname: Odronitz
authors.forename: Björn
authors.initials: B
authors.lastname: Hammesfahr
authors.forename: Marcel
authors.initials: M
authors.lastname: Hellkamp
authors.forename: Martin
authors.initials: M
authors.lastname: Kollmar
mesh_terms: D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*; D012984:Software
chemical_list: D011506:Proteins