{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD075165/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD075165/02495_F1_R1_P0200208C08_TMT10.raw.rar","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD075165/02495_F1_R1_P0200208C09_TMT10.raw.rar","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD075165/02495_F1_R1_P0200208C01_TMT10.raw.rar","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD075165/02495_F1_R1_P0200208C07_TMT10.raw.rar","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD075165/02495_F1_R1_P0200208C06_TMT10.raw.rar","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD075165/02495_F1_R1_P0200208C05_TMT10.raw.rar","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD075165/02495_F1_R1_P0200208C04_TMT10.raw.rar","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD075165/02495_F1_R1_P0200208C10_TMT10.raw.rar","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD075165/02495_F1_R1_P0200208C02_TMT10.raw.rar","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD075165/02495_F1_R1_P0200208C03_TMT10.raw.rar"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD075165/F405161.dat","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD075165/F405165.dat","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD075165/IndexerVolumeGuid","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD075165/F405170.dat","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD075165/F405169.dat","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD075165/F405163.dat","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD075165/F405167.dat","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD075165/F405162.dat","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD075165/F405164.dat","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD075165/F405168.dat","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD075165/WPSettings.dat","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD075165/F405166.dat"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["thilo.x.werner@gsk.com"],"submitter":["Sascha  Knecht"],"technology_type":["Data-dependent acquisition","Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":[""],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD075165"],"sample_protocol":["37.5 µl of Mycobacterium tuberculosis protein extract were combined with SDS sample buffer and the proteins were digested according to a modified single pot solid-phase sample preparation (SP3) protocol (Ref. 2, 3). Briefly, proteins were bound to paramagnetic beads (SeraMag Speed beads, GE Healthcare, CAT#45152105050250, CAT#651521050502) in 50% Ethanol (final concentration). Beads were washed 4 times with 70 % Ethanol and proteins digested by resuspending in 0.1 mM HEPES (pH 8.5) containing TCEP, Chloroacetamide, Trypsin and LysC followed by o/n incubation. Peptides were labeled with isobaric mass tags (TMT10, Thermo FisherScientific, Waltham, MA using the 10-plex TMT reagents, enabling relative quantification of 10 conditions in a single experiment (Ref. 1, 4). The labeling reaction was performed in 40 mM triethylammoniumbicarbonate, pH 8.5 at 22°C and quenched with glycine. Labeled peptide extracts were combined into a single sample per experiment, lyophilized and subjected to LC-MS analysis.   Samples were pre-fractionated by reversed-phase chromatography at high pH to 16 samples of which 10 were measured (Ref. 5). After lyophilization, dried samples were resuspended in 0.05 % trifluoroacetic acid in water. Half of the sample was injected into an Ultimate3000 nanoRLSC (Dionex) coupled to a Q-Exactive (Thermo Fisher Scientific). Peptides were separated into custom-made 35 cm x 100 um (ID) reversed-phase columns (Reprosil) at 55°C, gradient elution was performed from 3.5 % acetonitrile to 29 % acetonitrile in 0.1 % formic acid and 3.5 % DMSO over 120 minutes.  The Q Exactive Plus operated with data-dependent top 10 method. MS spectra were acquired using 70.000 resolution and an ion target of 3E6. Higher energy collisional dissociation (HCD) scans were performed with 35 % NCE at 35.000 resolution (at m/z 200), and ion target settings   1. Werner, T., Sweetman, G., Savitski, M.F., Mathieson, T., Bantscheff, M., and Savitski, M.M. (2014). Ion Coalescence of Neutron Encoded TMT 10-Plex Reporter Ions. Anal. Chem. 86, 3594–3601  2. Hughes CS, Foehr S, Garfield DA, Furlong EE, Steinmetz LM, Krijgsveld J. Ultrasensitive proteome analysis using paramagnetic bead technology. Mol Syst Biol. 2014 Oct 30;10:757  3. Moggridge S, Sorensen PH, Morin GB, Hughes CS. Extending the Compatibility of the SP3 Paramagnetic Bead Processing Approach for Proteomics. J. Proteome Res. 17, 1730–1740 (2018).   4. Werner, T., Becher, I., Sweetman, G., Doce, C., Savitski, M.M., and Bantscheff, M. (2012). High-Resolution Enabled TMT 8-plexing. Anal. Chem. 84, 7188–7194"],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["Mascot 2.4 (Matrix Science, Boston, MA) was used for protein identification by using a 10 parts per million mass tolerance for peptide precursors and 20 mD (HCD) mass tolerance for fragment ions. To create the fasta file for mascot searching, all proteins corresponding to the taxonomy ‘Mycobacterium tuberculosis H37Rv’ were downloaded from Uniprot (release 20170621) and supplemented with common contaminant protein sequences of bovine serum albumin, porcine trypsin and mouse, rat, sheep and dog keratins. To assess the false discovery rate (FDR) “decoy” proteins (reverse of all protein sequences) were created and added to the database, resulting in a database containing a total of 7994 protein sequences, 50% forward, 50% reverse. Unless stated otherwise, we accepted protein identifications as follows: (i) For single spectrum to sequence assignments, we required this assignment to be the best match and a minimum Mascot score of 31 and a 10× difference of this assignment over the next best assignment. Based on these criteria, the decoy search results indicated <1% false discovery rate (FDR). (ii) For multiple spectra to sequence assignments and using the same parameters, the decoy search results indicated <0.1% FDR. Quantified proteins were required to contain at least 2 unique peptide matches. FDR for quantified proteins was < 0.1%. The raw data table for the Whole Proteome Profiling experiment can be found in Supplementary Table 1."],"omics_type":["Proteomics"],"labhead":["Thilo Werner"],"instrument_platform":[""],"labhead_affiliation":["Target Discovery, GSK / Cellzome"],"submission_type":["PARTIAL"],"species":["Mycobacterium Tuberculosis","Bacteria","Mycobacterium Tuberculosis H37rv"],"submitter_mail":["sascha.knecht@me.com"],"publication":["10.1038/S41467-026-71460-6"],"submitter_affiliation":["Target Discovery, GSK / Cellzome"],"submitter_country":["Germany"],"additional_accession":[]},"is_claimable":false,"name":"Alpibectir–Ethionamide combination (AlpE) for the treatment of tuberculosis","description":"MS/MS data for profiling of Mycobacterium tuberculosis treated with Compound 1, Compound 2, Alpibectir, Compound 3 and vehicle control: 10 samples were analyzed in parallel (TMT 10-plex) to generate whole proteome profiling data. Mycobacterium tuberculosis were treated for 72h with 1µM of the respective compound: Samples 1 and 2 treated with Compound 1, samples 3 and 4 with Compound 2, samples 5 and 6 with Alpibectir, samples 7 and 8 with Compound 3 and samples 9 and 10 with DMSO (vehicle control experiments n=1 and 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