TitleIHMValidation: Assessment of Integrative Structure Models Deposited to the Protein Data Bank.
Publication TypeJournal Article
Year of Publication2025
AuthorsZalevsky AO, Vallat B, Webb BM, Tangmunarunkit H, Sekharan MR, Shafaeibejestan A, Ganesan S, Sagendorf J, Jeffries CM, Trewhella J, Graziadei A, Vizcaíno JAntonio, Leitner A, Rappsilber J, Peisach E, Flatt JW, Young JY, Majila K, Viswanath S, Kesselman C, Hoch JC, Kurisu G, Morris KL, Velankar S, Berman HM, Burley SK, Sali A
JournalJ Mol Biol
Pagination169598
Date Published2025 Dec 18
ISSN1089-8638
Abstract

PDB-IHM is a branch of the Protein Data Bank (PDB), a Worldwide Protein Data Bank (wwPDB) Core Archive, that expands its scope by allowing for additional biomolecular structure representations and types of experimental information (i.e., integrative/hybrid structure models). As of October 2025, PDB-IHM contained 374 entries, benefitting from multi-scale and multi-state representations and 17 types of experimental data. These structure models are assigned PDB accession codes and are archived alongside other experimental structures in the PDB. Rigorous interpretation of a structure model requires assessment of underlying data quality, consistency with the input data, and estimates of positional uncertainty of its components. Herein, we present the IHMValidation pipeline (https://validate.pdb-ihm.org; https://github.com/salilab/IHMValidation) based on recommendations from the wwPDB Integrative Methods Task Force plus the small-angle scattering (SAS), chemical crosslinking mass spectrometry (crosslinking-MS), and cryo-electron microscopy and tomography (3DEM) communities. The IHMValidation report (available in both PDF and HTML formats) comprises six sections: (i) overview; (ii) model details; (iii) data quality assessments; (iv) local geometry assessments (i.e., model quality); (v) fit of the model to the data used to generate it; and (vi) fit of the model to the data used for validation. Future expansions of the IHMValidation pipeline will: (i) reflect recommendations coming from additional experimental communities, including Förster resonance energy transfer (FRET) and hydrogen/deuterium exchange MS (HDX-MS); (ii) include other validation criteria, such as Bayesian likelihoods for the data; and (iii) represent estimates of structure model uncertainty based on the variation among alternative models satisfying input data.

DOI10.1016/j.jmb.2025.169598
Alternate JournalJ Mol Biol
PubMed ID41421450