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In previous works we decomposed the statistical potentials in different terms, named Split-Statistical Potentials, accounting for the type of amino acid pairs, their hydrophobicity, solvent accessibility and type of secondary structure. These potentials have been successfully used to identify near-native structures in protein structure prediction, rank protein docking poses, and predict PPI binding affinities.<\/jats:p><\/jats:sec><jats:sec><jats:title>Results<\/jats:title><jats:p>Here, we present the SPServer, a web server that applies the Split-Statistical Potentials to analyze protein folds and protein interfaces. SPServer provides global scores as well as residue\/residue-pair profiles presented as score plots and maps. This level of detail allows users to: (1) identify potentially problematic regions on protein structures; (2) identify disrupting amino acid pairs in protein interfaces; and (3) compare and analyze the quality of tertiary and quaternary structural models.<\/jats:p><\/jats:sec><jats:sec><jats:title>Conclusions<\/jats:title><jats:p>While there are many web servers that provide scoring functions to assess the quality of\u00a0either protein folds or PPI structures, SPServer integrates both aspects in a unique easy-to-use web server. Moreover, the server permits to locally assess the quality of the structures and interfaces at a residue level and provides tools to compare the local assessment between structures.<\/jats:p><\/jats:sec><jats:sec><jats:title>Server address<\/jats:title><jats:p><jats:ext-link xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" ext-link-type=\"uri\" xlink:href=\"https:\/\/sbi.upf.edu\/spserver\/\">https:\/\/sbi.upf.edu\/spserver\/<\/jats:ext-link>.<\/jats:p><\/jats:sec>","DOI":"10.1186\/s12859-020-03770-5","type":"journal-article","created":{"date-parts":[[2021,1,6]],"date-time":"2021-01-06T16:08:06Z","timestamp":1609949286000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":11,"title":["SPServer: split-statistical potentials for the analysis of protein structures and protein\u2013protein interactions"],"prefix":"10.1186","volume":"22","author":[{"given":"Joaquim","family":"Aguirre-Plans","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Alberto","family":"Meseguer","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ruben","family":"Molina-Fernandez","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Manuel Alejandro","family":"Mar\u00edn-L\u00f3pez","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Gaurav","family":"Jumde","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Kevin","family":"Casanova","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jaume","family":"Bonet","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Oriol","family":"Fornes","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Narcis","family":"Fernandez-Fuentes","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0702-0250","authenticated-orcid":false,"given":"Baldo","family":"Oliva","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"297","published-online":{"date-parts":[[2021,1,6]]},"reference":[{"key":"3770_CR1","doi-asserted-by":"publisher","first-page":"1011","DOI":"10.1002\/prot.25823","volume":"87","author":"A Kryshtafovych","year":"2019","unstructured":"Kryshtafovych A, Schwede T, Topf M, Fidelis K, Moult J. 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