{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Xlsx":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD050887/simple_mixtures_model_2.xlsx","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD050887/sample_file_model_2.xlsx"],"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD050887/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD050887/M31.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD050887/M33.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD050887/M14.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD050887/M11.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD050887/M24.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD050887/M35.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD050887/M22.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD050887/M21.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD050887/M13.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD050887/M32.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD050887/M25.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD050887/M12.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD050887/M15.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD050887/M34.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD050887/M23.raw"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["iatarasova@yandex.ru"],"submitter":["Tomiris Kusainova"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"software":["Not available"],"submitter_keywords":["Directms1","Metaproteomics","Microbiomes","Ms1-only"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD050887"],"sample_protocol":["Cells were cultivated for 72 hours in a shaking incubator (HZQ-111) at 27°С and 250 rpm in Erlenmeyer flasks with 100 mL of Evans medium. The composition of the medium was as follows (g/L or mL/L:): K2HPO4 8.71 g, 5 M NH4CI 1 mL, 0.1 M Na2SO4 1 mL, 62 mM MgCI2 1 mL, 1 mM CaCI2 1 mL, 0.005 mM (NH4)6Mo7O24 × 4H2O,  micronutrients solution 1 mL (as follows in g/L): ZnO 0.41 g, FeCI3 × 6H2O 5.4 g, MnCI2 × 4H2O 2 g, CuCI2 × 2H2O 0.17 g, CoCI2 × 6H2O 0.48 g, H3BO3 0.06 g, (pH 7.0) - with the addition of 200 uL 108 CFU inoculum and glucose (1%  v/v for R. opacus 1CP and 2% v/v for R. erythropolis X5, G. alkanivorans 135, G. amicalis, P. aryabhattai 25) as the sole source of carbon and energy. Model microbiomes were prepared by mixing tryptic peptide solutions. Composition of each sample is described in files simple_mixtures_model_2.xlsx.For mix model II  and characterization of metabolic activity changes, cell pellets were resuspended in a 150 µL lysis buffer (100 mM ABC, 4% SDS, 10 mM DTT)). Cells were boiled for 10 min at 95C and then cooled down on ice. To lyse cells, the samples were sonicated for 5 min (1 sec on 1 sec off) on 60 % amplitude (QSonica Q125, Newtown, Connecticut, USA). Samples were centrifuged for 10 min on 10 000 g, then the supernatant was taken. 100 uL of supernatant was purified and concentrated with chloroform-methanol precipitation. Dry pellets were resuspended with 50 uL 4M urea in 50 mM ABC and 150 uL 50 mM ABC. Protein concentration was measured by a BCA kit (Thermo Scientific, Germany). DTT 10mM was added for 20 min at 56 °C, followed by incubation with IAA for 30 min in the dark at room temperature. Trypsin was added in a 1:50 m/m ratio and samples were incubated overnight at 37 °C. Digest was stopped by adding 1 % TFA, then samples were desalted with OASIS HLB cartridges (Waters, USA) and dried in a vacuum concentrator.The experiments were performed using Orbitrap Q Exactive mass spectrometer (Thermo Scientific, San Jose, CA, USA) coupled to Dionex UltiMate 3000 LC system (Thermo Fisher Scientific, Germering, Germany. Trap column μ-Precolumn C18 PepMap100 (5 μm, 300 μm, i.d. 5 mm, 100 Å) (Thermo Fisher Scientific, USA) and self-packed analytical column (Reprosil-Pur 3 μm, 75 μm i.d., 15 cm length) were employed for separation. Mobile phases were as follows: (A) 0.1% formic acid (FA) in water; (B) 80% ACN, 0.1% FA in water. The gradient was from 5% to 35% phase B in 4.8 min at 1.5 μL/min. Total method time including column washing and equilibration was 7.5 min. Field asymmetric ion mobility spectrometry (FAIMS) separations were performed with the following compensation voltages (CV) -50 V, -65 V, and -80 V in a stepwise mode during LC-MS analysis. Data acquisition was performed in MS1-only mode. Full MS scans were acquired in a range from m/z 375 to 1500 at a resolution of 120,000 at m/z 200 with AGC target of 4e5, 1 microscan, and 50 ms maximum injection time. Samples were resuspended in phase A and quantities of 1 \uD835\uDF07g were loaded per injection."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["Thermo raw files were converted to mzML format using ThermoRawFileParser (https://github.com/compomics/ThermoRawFileParser). Peptide feature deteсtion was performed using the Biosaur2 software. The proteomic search engine ms1searchpy was used for protein identification. Search was performed against the SwissProt + TrEMBL database (accessed on 06 Dec 2020) of bacterial proteins and strain-specific databases based on annotations of bacterial genomes. Precursor tolerance was ±10 ppm. Carbamidomethylation of cysteine residues was fixed modification, no variable modifications and no missed cleavages were allowed in MS1 search. Protein identifications were filtered to 5% FDR using the target-decoy approach. Quantification was performed using DirectMS1Quant under default conditions."],"omics_type":["Proteomics"],"labhead":["Dr Irina A. Tarasova"],"instrument_platform":[""],"labhead_affiliation":["INEPCP FRCCP RAS, Moscow, Russia"],"submission_type":["PARTIAL"],"species":["Rhodococcus Qingshengii","Rhodococcus Opacus","Gordonia Polyisoprenivorans","Gordonia Alkanivorans","Rhodococcus Erythropolis"],"publication":["10.1093/FEMSML/UQAG027"],"submitter_mail":["kusainova7531@gmail.com"],"submitter_affiliation":["V. L. Talrose Institute for Energy Problems of Chemical Physics, N. N. Semenov Federal Research Center for Chemical Physics, Russian Academy of Sciences, 119334 Moscow, Russia\n\nMoscow Institute of Physics and Technology, 141701 Dolgoprudny, Russia"],"submitter_country":["Russia"],"additional_accession":[]},"is_claimable":false,"name":"Quantitative assessment of microbiomes using ultra-fast MS/MS-free metaproteomics: model 2","description":"This study presents an adaptation of the novel ultrafast MS1-based method called DirectMS1 to characterization of the single microorganisms and microbiomes. Using DirectMS1 we demonstrate the blind  identification (with no prior knowledge of the bacterias in the sample) of a single bacterial species and microbial compositions using two-step database search against the microbial part of SwissProt and TrEMBL (62Gb database size), the evaluation of fold changes in biomass of microorganisms between the metaproteomic samples, and the assessment of metabolic activity of Rhodococcus species responding to a change in growth conditions and cold 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