--- OA_place: repository _id: '22687' abstract: - lang: eng text: "Understanding enzyme function requires characterizing not only static structure but also dynamics and ligand interactions. NMR spectroscopy provides this insight at atomic resolution, yet for large proteins the difficulty of resonance assignment has largely confined such studies to systems below ∼50 kDa, or to observing only methyl groups. Here we present an integrated magic-angle spinning (MAS) and solution NMR study of the 134 kDa tetrameric malate dehydrogenase from Ignicoccus islandicus (IiMDH), an enzyme of particular interest as an evolutionary intermediate between allosteric lactate\r\ndehydrogenases and non-allosteric malate dehydrogenases. By combining high-dimensional (up to 4D) MAS NMR experiments on sedimented protein with solution NMR, we achieved 92% backbone heavy- atom assignment and 91% assignment of all Ile-δ1, Leu-δ1/-δ2, Val-γ1/-γ2, Met-ε and Thr-γ methyl groups. Building on these assignments, we use various probes of backbone and sidechain dynamics: elevated MAS NMR 15N rotating-frame relaxation (R1ρ) points to microsecond motions in functionally critical regions, including the catalytic loop and the mobile surface loop. Complementary methyl-axis order parameters from solution NMR identified additional flexible sites in the hydrophobic core. Chemical shift perturbation experiments upon addition of the substrate analogue oxamate, monitored via backbone 1H-15N TROSY, revealed both active-site contacts and responses in helices α2F and α3G, regions implicated in allosteric signal transmission. The integrated approach demonstrated here exploits the distinct strengths of MAS and solution NMR, and provides a comprehensive view of structure, dynamics, and substrate interactions in a large oligomeric enzyme that would not be accessible by either technique alone." acknowledged_ssus: - _id: NMR - _id: LifeSc acknowledgement: This research was supported by the Scientific Service Units (SSU) of Institute of Science and Technology Austria (ISTA) through resources provided by the Nuclear Magnetic Resonance and the Lab Support Facilities. We thank Petra Rovó, Megha Mohan and Margarita Valhondo Falcón for excellent support of the NMR facility. article_processing_charge: No author: - first_name: Paul full_name: Schanda, Paul id: 7B541462-FAF6-11E9-A490-E8DFE5697425 last_name: Schanda orcid: 0000-0002-9350-7606 - first_name: Federico full_name: Napoli, Federico id: d42e08e7-f4fc-11eb-af0a-d71e26138f1b last_name: Napoli orcid: 0000-0002-9043-136X citation: ama: 'Schanda P, Napoli F. Data and scripts for: “Integrated solid/solution NMR assignment allows mapping dynamics and ligand binding in a 134 kDa enzyme.” 2026. doi:10.15479/AT-ISTA-22687' apa: 'Schanda, P., & Napoli, F. (2026). Data and scripts for: “Integrated solid/solution NMR assignment allows mapping dynamics and ligand binding in a 134 kDa enzyme.” Institute of Science and Technology Austria. https://doi.org/10.15479/AT-ISTA-22687' chicago: 'Schanda, Paul, and Federico Napoli. “Data and Scripts for: ‘Integrated Solid/Solution NMR Assignment Allows Mapping Dynamics and Ligand Binding in a 134 KDa Enzyme.’” Institute of Science and Technology Austria, 2026. https://doi.org/10.15479/AT-ISTA-22687.' ieee: 'P. Schanda and F. Napoli, “Data and scripts for: ‘Integrated solid/solution NMR assignment allows mapping dynamics and ligand binding in a 134 kDa enzyme.’” Institute of Science and Technology Austria, 2026.' ista: 'Schanda P, Napoli F. 2026. Data and scripts for: ‘Integrated solid/solution NMR assignment allows mapping dynamics and ligand binding in a 134 kDa enzyme’, Institute of Science and Technology Austria, 10.15479/AT-ISTA-22687.' mla: 'Schanda, Paul, and Federico Napoli. Data and Scripts for: “Integrated Solid/Solution NMR Assignment Allows Mapping Dynamics and Ligand Binding in a 134 KDa Enzyme.” Institute of Science and Technology Austria, 2026, doi:10.15479/AT-ISTA-22687.' short: P. Schanda, F. Napoli, (2026). contributor: - contributor_type: researcher first_name: Federico id: d42e08e7-f4fc-11eb-af0a-d71e26138f1b last_name: Napoli orcid: 0000-0002-9043-136X - contributor_type: project_leader first_name: Paul id: 7B541462-FAF6-11E9-A490-E8DFE5697425 last_name: Schanda orcid: 0000-0002-9350-7606 - contributor_type: project_member first_name: Rajkumar id: a3089acd-6806-11ee-bacc-f0c7d500ad20 last_name: Singh - contributor_type: project_member first_name: Anna id: 9fb2a840-89e1-11ee-a8b7-cc5c7ba62471 last_name: Kapitonova - contributor_type: project_member first_name: Virgil last_name: Aitenbichler - contributor_type: project_member first_name: Giorgia id: 334a5e40-8747-11f0-b671-ba1f5154b4b4 last_name: Toscano - contributor_type: data_collector first_name: Barbara last_name: Perrone corr_author: '1' date_created: 2026-08-12T16:12:19Z date_published: 2026-08-20T00:00:00Z date_updated: 2026-08-20T07:40:15Z day: '20' department: - _id: PaSc doi: 10.15479/AT-ISTA-22687 doi_confirm: '1' file: - access_level: open_access checksum: dd23db23f7e75bafad6c67381163c1e2 content_type: application/vnd.openxmlformats-officedocument.spreadsheetml.sheet creator: fnapoli date_created: 2026-08-18T07:13:26Z date_updated: 2026-08-18T07:13:26Z file_id: '22725' file_name: Pulse_parameters.xlsx file_size: 59096 relation: main_file success: 1 - access_level: open_access checksum: a7ad194d8d7f780725bc2c60c63d686d content_type: application/zip creator: fnapoli date_created: 2026-08-18T07:16:00Z date_updated: 2026-08-18T07:16:00Z file_id: '22726' file_name: Scripts_submission.zip file_size: 3591173 relation: main_file success: 1 - access_level: open_access checksum: dc099c298844973512ab224464964a1a content_type: application/zip creator: fnapoli date_created: 2026-08-18T07:15:59Z date_updated: 2026-08-18T07:15:59Z file_id: '22727' file_name: FLYA_runs.zip file_size: 28750919 relation: main_file success: 1 - access_level: open_access checksum: 04bcce8eb20c90089cbd2fb5e0c50a7f content_type: application/zip creator: fnapoli date_created: 2026-08-18T07:33:47Z date_updated: 2026-08-18T07:33:47Z file_id: '22728' file_name: spectra_Bruker.zip file_size: 3824856998 relation: main_file success: 1 - access_level: open_access checksum: 91c1161ca98632ed643d2b564395da5b content_type: application/zip creator: fnapoli date_created: 2026-08-18T08:03:33Z date_updated: 2026-08-18T08:03:33Z file_id: '22729' file_name: Titration_data.zip file_size: 17880653 relation: main_file success: 1 - access_level: open_access checksum: ca2cf03b82656ae2858931d4391a3158 content_type: text/plain creator: arashid date_created: 2026-08-20T07:35:05Z date_updated: 2026-08-20T07:35:05Z file_id: '22743' file_name: README.txt file_size: 868 relation: main_file success: 1 file_date_updated: 2026-08-20T07:35:05Z fulldoi: https://doi.org/10.15479/AT-ISTA-22687 has_accepted_license: '1' month: '08' oa: 1 oa_version: None project: - _id: eb9c82eb-77a9-11ec-83b8-aadd536561cf grant_number: I05812 name: AlloSpace. The emergence and mechanisms of allostery publisher: Institute of Science and Technology Austria status: public title: 'Data and scripts for: "Integrated solid/solution NMR assignment allows mapping dynamics and ligand binding in a 134 kDa enzyme"' tmp: image: /images/cc_by_nc.png legal_code_url: https://creativecommons.org/licenses/by-nc/4.0/legalcode name: Creative Commons Attribution-NonCommercial 4.0 International (CC BY-NC 4.0) short: CC BY-NC (4.0) type: research_data user_id: 68b8ca59-c5b3-11ee-8790-cd641c68093d year: '2026' ...