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Beads were removed from the initial digest and 2nd digestion step took place using trypsin for 18h at 37 °C (0.5 µg; sequencing grade, Promega). Resulting peptides were extracted into LC-MS vials by 2.5% formic acid (FA) in 50% acetonitrile (ACN) and 100% ACN with addition of n-Dodecyl β-D-maltoside (DDM, final concentration 0.1%; Sigma-Aldrich) and concentrated in a SpeedVac concentrator (Thermo Fisher Scientific). LC-MS/MS analyses of peptides solutions were done using UltiMate 3000 RSLCnano system (Thermo Fisher Scientific) connected to timsTOF Ultra 2 spectrometer (Bruker). Prior to LC separation, tryptic digests were online concentrated and desalted using a trapping column (Acclaim™ PepMap™ 100 C18, dimensions 300 μm ID, 5 mm long, 5 μm particles, Thermo Fisher Scientific). After washing the trapping column with 0.1% trifluoroacetic acid, the peptides were eluted (flow rate - 150 nl/min) from the trapping column onto an analytical column (Aurora C18, 75μm ID, 250 mm long, 1.7 μm particles, heated to 50°C, PN AUR3-25075C18-CSI, Ion Opticks) by 60 min linear gradient program (3-42% of mobile phase B; mobile phase A: 0.1% FA in water; mobile phase B: 0.1% FA in 80% ACN). Equilibration of the trapping column and the analytical column was done prior to sample injection into the sample loop. The analytical column was placed inside Column Toaster heater (Bruker) and its emitter side was installed inside the CaptiveSpray ion source (Bruker) according to the manufacturer’s instructions with the column temperature set to 50 ºC and spray voltage 1.4kV was used. PASEF data denoising was switched off. MSn data were acquired in m/z range of 100-1700 and 1/k0 range of 0.6-1.4 V×s×cm-2 using DDA-PASEF method acquiring 10 PASEF scans with scheduled target intensity of 20,000 and intensity threshold of 500 and with measuring and switching times set to 2.75 and 1.65 ms, respectively. Active exclusion was set for 0.4min with precursor reconsideration for 4× more intense precursors."],"repository":["Pride"],"modification":[""],"quantification_method":["Not available"],"data_protocol":["Raw MS data were processed using DataAnalysis software (version 6.1) from which MS2 spectra were exported into the MGF spectra format. MS2 spectra in MGF format were database searched using Proteome Discoverer (version 1.4, Thermo Fisher Scientific) and in-house Mascot server (version 2.6.2)in the following two steps search. At first the data were searched against modified cRAP database based on https://www.thegpm.org/crap/ using the following search parameters: precursor and fragment tolerance of 10 ppm and 0.03 Da, respectively, full tryptic/P specificity with 2 allowed missed cleavage sites, Oxidation (M), Deamidated (NQ) and Acetyl (Protein N-term) set as variable and Carbamidomethyl (C) as fixed modification. Peptide cutoff score for the cRAP database search was set to 30. Following the cRAP database search, the MS2 spectra assigned to any protein in the cRAP database with Mascot ion score 30 and above were removed and the remaining spectra were searched against specific database containing proteins of interest. Search conditions were set identically to the cRAP database search with the following modifications: additional variable modification QTGG (K), maximum number of missed cleavages 5, peptide cut off score 20. Database search results were inspected manually in Proteome Discoverer and DataAnalysis (extracted ion chromatograms) considering all acquired data inspecting and especially the following characteristics: fragments assignment quality, reported fragments delta mass, Mascot ion score and extracted ion chromatograms of the identified QTGG (K) modified peptides."],"omics_type":["Proteomics"],"labhead":["Zbynek Zdrahal"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["Proteomics Core Facility and Research Group Proteomics, CEITEC-MU, Masaryk University, Brno, Czech Republic"],"species":["Arabidopsis Thaliana (mouse-ear Cress)"],"publication":["Not available"],"submitter_mail":["david.potesil@ceitec.muni.cz"],"submitter_affiliation":["Proteomics Core Facility and Research Group Proteomics\nCEITEC-MU\nMasaryk University\nBrno, Czech Republic"],"submitter_country":["Czech Republic"],"additional_accession":[]},"is_claimable":false,"name":"Structural Basis of βKNL2 Centromeric Targeting Mechanism and Its Role in Plant-Specific Kinetochore Assembly","description":"dodáme až bude připravený revidovaný manuscript dodáme až bude připravený revidovaný manuscript dodáme až bude připravený revidovaný manuscript dodáme až bude připravený revidovaný 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