{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Xlsx":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD075095/MjGATase_K151L_13032021_15cutoff.xlsx","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD075095/MjGATase_D110V_240822_15relab.xlsx","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD075095/MjGATase_WT_170321_15relab.xlsx","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD075095/MjGATase_K113A_15RelAb.xlsx","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD075095/MjGATase_Y158F_K151L_180322_A_10RelAb.xlsx","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD075095/MjGATase_D110P_15.xlsx","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD075095/MjGATase_D110N_240822run_10cutoff.xlsx","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD075095/MjGATase_D110V_K151L_180322_A_10RelAb.xlsx","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD075095/MjGATase_K107L_070921_15RelAb.xlsx","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD075095/MjGATase_E108L_01_110321_15RelAb.xlsx","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD075095/MjGATase_E137L_13032021_15RelAb.xlsx","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD075095/MjGATase_Y158F_02_110221_15relabund.xlsx","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD075095/MjGATase_E108Q_DI_120K_131219_RelAb10.xlsx"],"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD075095/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD075095/MjGATase_E137L_01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD075095/MjGATase_D110V_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD075095/MjGATase_K151L_01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD075095/MjGATase_K113A_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD075095/MjGATase_D110P_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD075095/MjGATase_Y158F_K151L_A_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD075095/MjGATase_D110V_K151L_A_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD075095/MjGATase_Y158F_02.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD075095/MjGATase_E108L_01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD075095/MjGATase_WT_01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD075095/MjGAtase_E108Q_120K_DI_13122019.RAW","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD075095/MjGATase_K107L_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD075095/MjGATase_D110N_1.raw"]},"type":"primary"},"statusCodeValue":200,"statusCode":"OK"}],"scores":null,"additional":{"labhead_mail":["hb@jncasr.ac.in"],"submitter":["Hemalatha Balaram"],"technology_type":["Mass Spectrometry","Top-down proteomics"],"software":["Not available"],"submitter_keywords":["Lc-ms","Deamidation","Succinimide"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD075095"],"sample_protocol":["The MjGATase proteins were diluted to 1 mg ml-1 in water and dialyzed against water using a 10 kDa cut-off membrane. The protein was further diluted to 0.1-0.2 mg ml-1 in water with 0.1% formic acid. 10-30 pmol of the dialyzed protein sample was injected on to a C8 reverse phase column (Thermo Scientific, 2.1 mm diameter, length: 100 mm, 5 μm particle size, 175 Å pore size). Mass spectral analysis was carried out on a Q Exactive HF mass spectrometer (Thermo Scientific, USA) equipped with a Thermo Scientific Dionex Ultimate 3000 UHPLC system at the in-house Central Instrumentation Facility, Molecular Biology and Genetics Unit, JNCASR. The protein was eluted using water containing 0.1% formic acid (solvent A) and acetonitrile containing 0.1% formic acid (solvent B) as the solvent system at a flow rate of 0.3 ml min-1. The HPLC run conditions were as follows:  equilibration at 10% B for 1 min, gradient from 10% B to 80% B over 6 mins, isocratic at 80% B for 1 min, gradient of 80% B to 95% B in 1 min, isocratic at 95% B for 2 mins, back to 10% B in 1 min and finally equilibrate at 10% B for 3 mins. The column temperature was set to 40 ℃. Full MS scans were acquired at a resolution of 120,000 at m/z 200 Th, scan range of 500 - 2000 m/z, AGC target set to 1e6 with maximum ion injection time of 100 ms. The mass spectrometer was operated at a spray voltage of 3.8 kV, capillary temperature of 320 ℃, auxiliary gas heater temperature of 200 ℃, and S-lens RF level value set at 80. The flow rates of sheath gas and auxiliary gas were set to 20 and 10, respectively.   MjGATase_E108Q protein was diluted to 0.1 mg ml-1 in 50% methanol and MS-grade water with 0.1% formic acid. The mass spectrum was acquired by direct injection of the protein through a Hamilton syringe in the positive ion mode. The Q Exactive HF mass spectrometer was operated with a scan range of 400 – 2000 m/z, resolution of 120,000 at m/z 200 Th, spray voltage of 3.5 kV, capillary temperature of 275 °C, probe heater temperature of 200 °C, and S-lens RF level value at 80. The flow rates of sheath gas and auxiliary gas were set to 25 and 10, respectively. The ion injection time and ion target value were set at a threshold of 200 ms and 3e6, respectively."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["Data collection and visualization were carried out with Xcalibur v.4.1 software and Qual browser (Thermo Scientific). Deconvolution of the spectra was carried out using Biopharma finderTM v.3.2 software (Thermo Scientific). Xtract algorithm was used for deconvolution as our data were isotopically resolved. The source spectra were generated by using “Average over selected Retention time” method. A relative abundance threshold cut-off of 10-15% above the noise level of the spectrum was set during deconvolution."],"omics_type":["Proteomics"],"labhead":["Hemalatha Balaram"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["Molecular Biology and Genetics Unit, Jawaharlal Nehru Centre for Advanced Scientific research, Bengaluru, India"],"species":["Methanocaldococcus Jannaschii"],"submitter_mail":["hb@jncasr.ac.in"],"publication":["42055332 Chandrashekarmath A, Jash O, Singh K, Bellur A, Roy CS, Dongre A, Chathoth NE, Anjukandi P, Kumar S, Mukherjee S, Balaram P, Balasubramanian S, Balaram H. Insights into the role of internal catalysts in asparagine-to-succinimide conversion in a hyperthermophilic glutamine amidotransferase. J Biol Chem. 2026 302(6):113093 10.1016/j.jbc.2026.113093"],"submitter_affiliation":["Professor"],"submitter_country":["India"],"pubmed_abstract":["Succinimide (SNN), an intermediate spontaneously formed during asparaginyl deamidation or aspartyl dehydration in proteins, is generally hydrolysis-prone, leading to isomerization to an L/D α/β-aspartyl residue, with the latter being considered deleterious to protein structure and function. An unusually stable SNN-mediated conformational rigidity through restriction of the backbone dihedral angle, ψ, enhances the thermostability of glutamine amidotransferase (GATase) from Methanocaldococcus jannaschii (Mj). Although several structural features involved in maintaining a stable SNN and imparting SNN-mediated thermostability have been identified in MjGATase, the residues in the protein that catalyse the rapid and complete conversion of Asn109 to SNN remain unknown. Here, we investigated several mutants of MjGATase for their ability to retain the Asn109 side chain in the unmodified form. Mass spectrometric analysis of 10 single amino acid variants enabled the identification of residues that impacted the proportion of SNN and Asn population in the protein sample. This led to the generation of two double mutants of MjGATase that retained an intact Asn109 side chain, as confirmed by mass spectrometry and crystal structure analysis. These mutant proteins with intact Asn residue at position 109 displayed lower thermal stability than the protein with the SNN modification. Further understanding of the deprotonation mechanism was addressed using quantum mechanics/molecular mechanics molecular dynamics metadynamics simulations."],"pubmed_title":["Insights into the role of internal catalysts in asparagine-to-succinimide conversion in a hyperthermophilic glutamine amidotransferase."],"pubmed_authors":["Chandrashekarmath Anusha A, Jash Oishika O, Singh Karandeep K, Bellur Asutosh A, Roy Chitralekha Sen CS, Dongre Aparna A, Chathoth Nayana Edavan NE, Anjukandi Padmesh P, Kumar Sanjeev S, Mukherjee Souradip S, Balaram Padmanabhan P, Balasubramanian Sundaram S, Balaram Hemalatha H"],"additional_accession":[]},"is_claimable":false,"name":"Intact protein mass analysis of wild-type and mutants of glutamine amidotransferase from Methanocaldococcus jannaschii","description":"The glutamine amidotransferase (GATase) from Methanocaldococcus jannaschii (Mj) harbours a stable post-translational modification, succinimide (SNN). As shown from earlier studies, the spontaneous deamidation of Asn109 leading to the formation of stable SNN in MjGATase, imparts hyper-thermostability to the protein. To examine which of the residues in the environment of Asn109 catalyses the conversion of Asn to SNN, several mutants of MjGATase were generated. The intact protein masses of these mutants along with the wild-type enzyme were obtained through mass spectrometric analysis. The wild-type enzyme shows a mass difference of 17 Da due to the formation of SNN whereas, the MjGATase mutants harboring unmodified Asn109 would retain the mass corresponding to that obtained from the sequence. The mass analysis of 12 MjGATase mutant proteins showed varied levels retaining intact Asn109 residue. Two double mutants showed almost entire population with the expected mass, thus, highlighting the involvement of the neighbouring residues in formation of 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