Complex with 1H histone chaperone Asf1, histones H3 (35-135aa) and H4; 70%-2H histone acetyltransferase Rtt109 and histone chaperone Vps75 (1-225aa) acquired in 100% v/v D2O

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    "title": "Histone chaperone exploits intrinsic disorder to switch acetylation specificity (Asf1-H3:H4-Rtt109-Vps75 protein complex, data for docking block selections)",
    "publication": {
      "title": "Histone chaperone exploits intrinsic disorder to switch acetylation specificity (Asf1-H3:H4-Rtt109-Vps75 protein complex, data for docking block selections)",
      "author_list": "Danilenko N, Lercher L, Kirkpatrick J, Gabel F, Codutti L, Carlomagno T",
      "journal": "Nat Commun",
      "doi": null,
      "pmid": null,
      "published_date": "2019 Aug 6"
    },
    "status": "released",
    "submitted_date": "2019-06-17",
    "released_date": "2019-07-10"
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        "affiliation": [
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            "short_name": null,
            "address": "Germany",
            "full_name": "Leibniz University of Hannover",
            "webpage": "https://www.uni-hannover.de"
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        "contributor_name": "Nataliya",
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