{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2023,6,27]],"date-time":"2023-06-27T17:34:01Z","timestamp":1687887241915},"reference-count":48,"publisher":"Oxford University Press (OUP)","issue":"9","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2013,5,1]]},"abstract":"<jats:title>Abstract<\/jats:title>\n               <jats:p>Motivation: 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.<\/jats:p>\n               <jats:p>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.<\/jats:p>\n               <jats:p>Availability and implementation: 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.<\/jats:p>\n               <jats:p>Contact: \u00a0robert.schneider@ibs.fr or mako@nmr.mpibpc.mpg.de<\/jats:p>\n               <jats:p>Supplementary information: \u00a0Supplementary data are available at Bioinformatics online.<\/jats:p>","DOI":"10.1093\/bioinformatics\/btt125","type":"journal-article","created":{"date-parts":[[2013,3,15]],"date-time":"2013-03-15T11:03:31Z","timestamp":1363345411000},"page":"1134-1140","source":"Crossref","is-referenced-by-count":2,"title":["Peakr: simulating solid-state NMR spectra of proteins"],"prefix":"10.1093","volume":"29","author":[{"given":"Robert","family":"Schneider","sequence":"first","affiliation":[{"name":"1 Department of NMR-based Structural Biology, Max-Planck-Institute for Biophysical Chemistry, Am Fassberg 11, 37077 G\u00f6ttingen, Germany and 2Protein Dynamics and Flexibility by NMR Group, Institut de Biologie Structurale J.P. Ebel, 41 rue Jules Horowitz, F-38027 Grenoble Cedex 1, France"},{"name":"1 Department of NMR-based Structural Biology, Max-Planck-Institute for Biophysical Chemistry, Am Fassberg 11, 37077 G\u00f6ttingen, Germany and 2Protein Dynamics and Flexibility by NMR Group, Institut de Biologie Structurale J.P. Ebel, 41 rue Jules Horowitz, F-38027 Grenoble Cedex 1, France"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Florian","family":"Odronitz","sequence":"additional","affiliation":[{"name":"1 Department of NMR-based Structural Biology, Max-Planck-Institute for Biophysical Chemistry, Am Fassberg 11, 37077 G\u00f6ttingen, Germany and 2Protein Dynamics and Flexibility by NMR Group, Institut de Biologie Structurale J.P. Ebel, 41 rue Jules Horowitz, F-38027 Grenoble Cedex 1, France"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Bj\u00f6rn","family":"Hammesfahr","sequence":"additional","affiliation":[{"name":"1 Department of NMR-based Structural Biology, Max-Planck-Institute for Biophysical Chemistry, Am Fassberg 11, 37077 G\u00f6ttingen, Germany and 2Protein Dynamics and Flexibility by NMR Group, Institut de Biologie Structurale J.P. Ebel, 41 rue Jules Horowitz, F-38027 Grenoble Cedex 1, France"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Marcel","family":"Hellkamp","sequence":"additional","affiliation":[{"name":"1 Department of NMR-based Structural Biology, Max-Planck-Institute for Biophysical Chemistry, Am Fassberg 11, 37077 G\u00f6ttingen, Germany and 2Protein Dynamics and Flexibility by NMR Group, Institut de Biologie Structurale J.P. Ebel, 41 rue Jules Horowitz, F-38027 Grenoble Cedex 1, France"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Martin","family":"Kollmar","sequence":"additional","affiliation":[{"name":"1 Department of NMR-based Structural Biology, Max-Planck-Institute for Biophysical Chemistry, Am Fassberg 11, 37077 G\u00f6ttingen, Germany and 2Protein Dynamics and Flexibility by NMR Group, Institut de Biologie Structurale J.P. Ebel, 41 rue Jules Horowitz, F-38027 Grenoble Cedex 1, France"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"286","published-online":{"date-parts":[[2013,3,14]]},"reference":[{"key":"2023012810374073600_btt125-B1","volume-title":"ACD\/Labs NMR Predictors","author":"Advanced Chemistry Development","year":"2007"},{"key":"2023012810374073600_btt125-B2","doi-asserted-by":"crossref","first-page":"4849","DOI":"10.1021\/ja00534a056","article-title":"Natural abundance carbon-13-carbon-13 coupling observed via double-quantum coherence","volume":"102","author":"Bax","year":"1980","journal-title":"J. Am. Chem. 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